ID  P61970;
PN  Nuclear transport factor 2;
GN  NUTF2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:7744965}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10679025}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000269|PubMed:10679025}.
DR  UNIPROT: P61970;
DR  UNIPROT: B2R4G7;
DR  UNIPROT: P13662;
DR  UNIPROT: Q6IB67;
DR  PDB: 1GY5;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DR  OMIM: 605813;
DR  DisGeNET: 10204;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:7744965}.
DE  Reference Proteome: Yes;
DE  Interaction: P37198; IntAct: EBI-591778,EBI-347978; Score: 0.78
DE  Interaction: Self; IntAct: EBI-591778,EBI-591778; Score: 0.67
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-591778; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-591778,EBI-286642; Score: 0.81
DE  Interaction: Q8WUF5; IntAct: EBI-5550163,EBI-591778; Score: 0.35
DE  Interaction: Q13625; IntAct: EBI-77642,EBI-591778; Score: 0.35
DE  Interaction: Q5T751; IntAct: EBI-12224199,EBI-591778; Score: 0.56
DE  Interaction: Q08117-2; IntAct: EBI-11741437,EBI-591778; Score: 0.56
DE  Interaction: Q5TCM9; IntAct: EBI-11955689,EBI-591778; Score: 0.56
DE  Interaction: Q9Y383; IntAct: EBI-352851,EBI-591778; Score: 0.37
DE  Interaction: P01889; IntAct: EBI-1046513,EBI-591778; Score: 0.40
DE  Interaction: Q9UET6; IntAct: EBI-591778,EBI-1055987; Score: 0.40
DE  Interaction: Q8WTR7; IntAct: EBI-751409,EBI-591778; Score: 0.37
DE  Interaction: P0DTD1; IntAct: EBI-25475891,EBI-591778; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-358311,EBI-591778; Score: 0.56
DE  Interaction: Q8NCX0-3; IntAct: EBI-12235840,EBI-591778; Score: 0.56
DE  Interaction: Q9NP66; IntAct: EBI-740641,EBI-591778; Score: 0.56
DE  Interaction: Q8WTV1; IntAct: EBI-17438286,EBI-591778; Score: 0.56
DE  Interaction: Q9BWC9; IntAct: EBI-711501,EBI-591778; Score: 0.56
DE  Interaction: Q14847-2; IntAct: EBI-9088686,EBI-591778; Score: 0.56
DE  Interaction: Q16740; IntAct: EBI-1056029,EBI-591778; Score: 0.56
DE  Interaction: Q9NSI6-4; IntAct: EBI-10693038,EBI-591778; Score: 0.56
DE  Interaction: Q9NQ35; IntAct: EBI-10311735,EBI-591778; Score: 0.56
DE  Interaction: Q9C004; IntAct: EBI-354861,EBI-591778; Score: 0.56
DE  Interaction: Q9BYU1; IntAct: EBI-10302990,EBI-591778; Score: 0.56
DE  Interaction: Q8IY57-5; IntAct: EBI-12111538,EBI-591778; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-710402,EBI-591778; Score: 0.56
DE  Interaction: Q8TDC0; IntAct: EBI-5662487,EBI-591778; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-742802,EBI-591778; Score: 0.56
DE  Interaction: Q5T0J7-2; IntAct: EBI-12833746,EBI-591778; Score: 0.56
DE  Interaction: Q96NC0; IntAct: EBI-2682299,EBI-591778; Score: 0.56
DE  Interaction: Q13555-5; IntAct: EBI-12020154,EBI-591778; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-744871,EBI-591778; Score: 0.56
DE  Interaction: Q5T6F2; IntAct: EBI-2514383,EBI-591778; Score: 0.56
DE  Interaction: Q96BZ8; IntAct: EBI-726510,EBI-591778; Score: 0.56
DE  Interaction: Q7Z7F0-4; IntAct: EBI-9089060,EBI-591778; Score: 0.56
DE  Interaction: Q9NX63; IntAct: EBI-743375,EBI-591778; Score: 0.56
DE  Interaction: Q9NQG5; IntAct: EBI-747925,EBI-591778; Score: 0.56
DE  Interaction: Q8N7W2-2; IntAct: EBI-10181188,EBI-591778; Score: 0.56
DE  Interaction: Q9BY43-2; IntAct: EBI-12178895,EBI-591778; Score: 0.56
DE  Interaction: O43790; IntAct: EBI-9996498,EBI-591778; Score: 0.56
DE  Interaction: Q6NTE8; IntAct: EBI-2857471,EBI-591778; Score: 0.56
DE  Interaction: P12532; IntAct: EBI-1050662,EBI-591778; Score: 0.56
DE  Interaction: P15531; IntAct: EBI-741141,EBI-591778; Score: 0.56
DE  Interaction: Q3KNR5; IntAct: EBI-10240813,EBI-591778; Score: 0.56
DE  Interaction: Q9H0A9-2; IntAct: EBI-11995806,EBI-591778; Score: 0.56
DE  Interaction: Q9UIL8; IntAct: EBI-2861403,EBI-591778; Score: 0.56
DE  Interaction: Q9BYQ0; IntAct: EBI-11958364,EBI-591778; Score: 0.56
DE  Interaction: Q01813; IntAct: EBI-359022,EBI-591778; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-591778; Score: 0.56
DE  Interaction: Q9P0W2; IntAct: EBI-713401,EBI-591778; Score: 0.56
DE  Interaction: P46527; IntAct: EBI-519280,EBI-591778; Score: 0.40
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0061608;
GO  GO:0008536;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:1904046;
GO  GO:0006913;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  A1Z8P9;
PN  Nucleoprotein TPR;
GN  Mtor;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. Nucleus matrix {ECO:0000269|PubMed:9152019}. Nucleus lamina {ECO:0000269|PubMed:15356261}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:22855526}; Peripheral membrane protein {ECO:0000305}; Nucleoplasmic side {ECO:0000269|PubMed:12027452}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:9152019}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:22855526}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19273613}. Midbody {ECO:0000269|PubMed:15356261}. Note=In interphase, localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:15356261). Enriched at the nuclear lamina and at intranuclear spaces surrounding the chromosomes and the nucleolus (PubMed:15356261, PubMed:15962301). Colocalized with hnRNPs and snRNPs at a single heat shock puff during heat shock (PubMed:12027452). Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner (PubMed:15356261). In prometaphase, localized at the spindle (PubMed:15356261). Localized to spindle midbody at telophase (PubMed:15356261). Recruited to the reforming nuclear envelope in early G1 (PubMed:15356261). Colocalized with Skeletor, Chro and east at the spindle matrix (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). Colocalized with Mad2 at the spindle matrix and kinetochore (PubMed:19273613). Associated with chromatin (PubMed:20174442). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}.
DR  UNIPROT: A1Z8P9;
DR  UNIPROT: O01385;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:12027452, PubMed:20174442). Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). During mitosis forms a gel-like spindle matrix complex together with Skeletor, Chro, east, and Asator embedding the microtubule spindle apparatus (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). Promotes assembly of the spindle-assembly checkpoint (SAC) ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad2 and Mps1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression (PubMed:19273613, PubMed:26714316). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex (PubMed:26714316). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:26714316, ECO:0000269|PubMed:9152019}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VG87; IntAct: EBI-127250,EBI-3406045; Score: 0.35
DE  Interaction: Q9VXU3; IntAct: EBI-127250,EBI-9942564; Score: 0.35
DE  Interaction: Q24238-1; IntAct: EBI-127250,EBI-3405995; Score: 0.35
DE  Interaction: Q9VDR4; IntAct: EBI-127250,EBI-177749; Score: 0.35
DE  Interaction: Q9W1X5; IntAct: EBI-127250,EBI-3406039; Score: 0.35
DE  Interaction: Q7JQU5; IntAct: EBI-127250,EBI-3433299; Score: 0.35
DE  Interaction: Q9VBD5; IntAct: EBI-127250,EBI-99036; Score: 0.35
DE  Interaction: C7LA76; IntAct: EBI-127250,EBI-3406035; Score: 0.35
DE  Interaction: Q9BIS2; IntAct: EBI-127250,EBI-422052; Score: 0.35
DE  Interaction: P54623-2; IntAct: EBI-127250,EBI-1448924; Score: 0.35
DE  Interaction: Q8IRG6; IntAct: EBI-127250,EBI-3405152; Score: 0.35
DE  Interaction: Q7KV88; IntAct: EBI-127250,EBI-868359; Score: 0.35
DE  Interaction: Q9VFA8; IntAct: EBI-127250,EBI-122584; Score: 0.35
DE  Interaction: Q9VWF7; IntAct: EBI-127250,EBI-3406011; Score: 0.35
DE  Interaction: Q9W1M6; IntAct: EBI-84282,EBI-127250; Score: 0.37
DE  Interaction: Q9VNZ7; IntAct: EBI-127250,EBI-141201; Score: 0.37
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0070090;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0005719;
GO  GO:0042405;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:1990047;
GO  GO:0051233;
GO  GO:0031490;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006325;
GO  GO:0006338;
GO  GO:0007549;
GO  GO:0060250;
GO  GO:0048133;
GO  GO:0007094;
GO  GO:0000022;
GO  GO:0006406;
GO  GO:0051781;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0045840;
GO  GO:0045944;
GO  GO:0006606;
GO  GO:0090235;
GO  GO:0007346;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0060236;
GO  GO:0006355;
GO  GO:0034976;
GO  GO:0009408;
GO  GO:0051225;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNE
SQ  LRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIA
SQ  RVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAV
SQ  KTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQL
SQ  TEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSE
SQ  ELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENK
SQ  KLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASE
SQ  KNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSE
SQ  QPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQK
SQ  EQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEK
SQ  ETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDE
SQ  EKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREH
SQ  GEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLK
SQ  SLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELL
SQ  RSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRN
SQ  NEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAI
SQ  TDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEE
SQ  FKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKN
SQ  RLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDE
SQ  HEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKD
SQ  INQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASI
SQ  RPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTS
SQ  SHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTAT
SQ  APSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKR
SQ  LRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDN
SQ  EGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWK
SQ  QAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSG
SQ  SDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVS
SQ  SEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNR
SQ  FAQRTRNRRPIRRPPPNNFNNGGRFP
//
ID  O55242;
PN  Sigma non-opioid intracellular receptor 1;
GN  Sigmar1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Cell junction, synapse, postsynaptic density membrane {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand- binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}.
DR  UNIPROT: O55242;
DR  UNIPROT: Q9JKU9;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, ECO:0000269|PubMed:9603192}.
DE  Reference Proteome: Yes;
DE  Interaction: G3I8R9; IntAct: EBI-988311,EBI-1557700; Score: 0.59
DE  Interaction: P61168; IntAct: EBI-8019871,EBI-1557700; Score: 0.52
DE  Interaction: P63141; IntAct: EBI-644033,EBI-1557700; Score: 0.56
GO  GO:0030054;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0042802;
GO  GO:0004985;
GO  GO:0038023;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0007399;
GO  GO:0070207;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEAT
SQ  ALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
//
ID  O02768;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: O02768;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R- lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:Q05769}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0043005;
GO  GO:0051213;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0050873;
GO  GO:0071498;
GO  GO:0071456;
GO  GO:0071471;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0006954;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0090336;
GO  GO:0031622;
GO  GO:0033138;
GO  GO:0031394;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0042127;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTH
SQ  FKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDS
SQ  KDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKY
SQ  QVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQQYNYQQFLYNNSIL
SQ  LEHGLTQFVESFTRQIAGRVAGGRNVPPAVQKVAKASIDQSRQMKYQSLNEYRKRFLLKPYESFEELTGEKEMAAELEAL
SQ  YGDIDAVELYPALLVERPRPDAIFGESMVEMGAPFSLKGLMGNPICSPNYWKPSTFGGEVGFKIVNTASIQSLICNNVKG
SQ  CPFTSFNVPDPQLTKTVTINASASHSRLEDINPTVLLKGRSTEL
//
ID  Q18508;
PN  Protein mel-28;
GN  mel;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27341616}. Nucleus envelope {ECO:0000269|PubMed:27341616}. Nucleus inner membrane {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:16950114}. Chromosome {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Note=Has a dynamic expression pattern during the cell cycle (PubMed:16950114, PubMed:27341616). During interphase, localizes to nuclear pore complexes and is also found in the nucleoplasm (PubMed:16950114, PubMed:27341616). During early mitosis, localizes to kinetochores in a hcp-3/CENP-A and hcp-4/CENP-C dependent manner (PubMed:16950114, PubMed:16950115, PubMed:27341616). At later stages of mitosis (anaphase), widely distributed on chromatin (PubMed:16950114, PubMed:27341616). During telophase, localizes again to the reforming nuclear envelope (PubMed:16950114, PubMed:27341616). {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}.
DR  UNIPROT: Q18508;
DE  Function: Nuclear envelope protein which has essential roles in assembly of nuclear pore complexes and in chromatin maintenance during the cell cycle (PubMed:16950114, PubMed:16950115, PubMed:26166571, PubMed:27341616). Appears to be a stable structural component of the nuclear envelope during interphase (PubMed:16950114, PubMed:16950115). In dividing cells, localizes to kinetochores during early stages of mitosis and then to chromatin during late mitosis (PubMed:16950114, PubMed:27341616). Important for several mitotic processes including chromosome condensation, kinetochore assembly, chromosome segregation and cell-cycle timing (PubMed:16950114, PubMed:16950115, PubMed:26166571, PubMed:27341616). In postmitotic cells, plays a role in the early steps of nuclear pore complex assembly by recruiting the nucleoporins npp-10 and npp-5 to chromatin (PubMed:16950114, PubMed:16950115). Also involved in meiotic chromosome segregation (PubMed:27341616). May function downstream of the Ran GTPase signaling pathway (PubMed:16950115). {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:26166571, ECO:0000269|PubMed:27341616}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EE71; IntAct: EBI-2002749,EBI-2002730; Score: 0.37
DE  Interaction: Q21443; IntAct: EBI-314110,EBI-2002730; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-313007,EBI-2002730; Score: 0.37
GO  GO:0000777;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0060090;
GO  GO:0051301;
GO  GO:0051321;
GO  GO:0000070;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDNENSSIFKSYQGYECWRGEKQIILKDSIGRQLPYIVNFKKNTCQIFDIEWERVTHSFVFPEGCALIDADYFPTEEGKL
SQ  GILVGVEDPRQSCGAEHFVLALAVDPDSPAMTITHSLEVPSKITVVKTLFSSADMADETQRTVLKLYHRLMTWQHIVAIG
SQ  CKETQCYLARLVAVETPSSPVITVHSEKKYLINLMNAYVSGSVLQYTLDDGAYREYPTAAVYISALSLMPRSRTLLVGLS
SQ  MGGILAASLNPSNQMMLLELRHERLVRKIAPLEPEDDPDKFEYFIATVDCSPRHPIMIQLWRGSFKTLEDVDGEEKYDRP
SQ  SFSVCLEHKILFGERWLAVNPIVTERDHMMLTRKRGTEDSMHNVSQTFGSTSNRNSVLLAYERKKMVIGTEDPNAEPEYI
SQ  VEAAIFDIDSWYYKRVPGRVSTDGTVLKQCAFLSTIKSNIRSEDVNDIGILTNEATDVSSFSSMVSDADQLFYPSALSFE
SQ  RVFVAKNTRIDWMKIQNIQDTILNKCAVKLPALIRNPEMISSVVMAAGLVRKNILSGSPNSSAAEINELQLSSDQKVLLN
SQ  VIVYYGKIEEFCQLASRPDISDTLKRELAEWALHEAVDYKRTISDKMVSLFQGRSLALSPLAEESIAQGIKLFRVVYEYL
SQ  KACSKALKDDRLRNLAHSVICMRNHTKLTSQFINFAIIPVDPIRQQRMKDLHSKRKNMARKNSSSLPVQSVVRKMNRQAP
SQ  NAQFWNDIPHDEWYPPTPLDLLECLLNVSISESIKRELVVQYVIDWISTSPEDSEHSEKQLALETIKIMTNQMLNVNLEK
SQ  IYYILDQGKKALTSSKTSDDMRALGEKVFSMKDDEISYEKLWGKDAPMTVTIGKHDLQRFEQRMKMQMEGGKVRLPVLDP
SQ  ESEILYQMFLFENEKFEAMSSEAISSNKLLSAFLPGMIKKDGRGRQKTAKEQEIEISVKKMFERKVQNDDEDMPEVFASV
SQ  NDKTERKRKSSQFGEDDESSVSSSQYVPPTAKRIQQWKSAVESVANNSSINSITSPDSHQNAEINMMIATPARYYKRHNE
SQ  EENVQDGFLSPAGNRPPPVSAHNSILKTAKGGQSASRGRIRFRADVPRGADESIEDNGRKGLALNFAILEDEEEETMTIR
SQ  KSRSMGKHDEEKDSEKNVVDEMEEVKDQEQENDECIESEKTFENQDDFEVLEDTSAPEAANTENGSETPPMEDTFEVRDD
SQ  DVMPPTDETYLSHLQTDKTGILEEEGEDEDIWDGVQRSFEVQMDEDCEAVPTIDVADDLESKSEEVNEEEVVESEEVQQD
SQ  AKEPEKTEKRQEEPEPEVMQPVIPEEPQNESLESSIKLQEELQEEPDIVPTGDEDTADKVQEQAVEEDRPPSRNTRSSSV
SQ  QKSTSQVEDRDPKELVEEERPPSRNTRSASVQKSSNQEKTSESGEVTEEDRPPSRNTRSASVQKSSSKVKDQKPEELIEE
SQ  DRPPSRNTRSASAQKTVAANKSVLESEIPSRSASRRTRSTSLRNDTVAEPDETSVAMTTRRRTRATSEVVSKQSSEDDGR
SQ  STPKTGRTPTKKAAASTSSSRAGSVTRGKKSIIQKMPSPLEVTMEVQEEEEEEAEEERPASRSTRSASVKNTTVDPSSSA
SQ  LASTKRTTSRKRGNSETIDFNQDDKSAPTTPKRGRPAKKDAGSPKVGSKARGTKPKSIFENQEDEEDRSSSPDIEQPATP
SQ  TRSSKRTARSRANSESIDDDSKQKTPKKKNAAVNEAGTSKQSRSVTRSRASSIDVQQEVEEPTTPKRGRGRPPKTVLENI
SQ  EEGEEERKETAATPLLRSARRAKQ
//
ID  P42704;
PN  Leucine-rich PPR motif-containing protein, mitochondrial;
GN  LRPPRC;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion. Nucleus, nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note=Seems to be predominantly mitochondrial.
DR  UNIPROT: P42704;
DR  UNIPROT: A0PJE3;
DR  UNIPROT: A8K1V1;
DR  UNIPROT: Q53PC0;
DR  UNIPROT: Q53QN7;
DR  UNIPROT: Q6ZUD8;
DR  UNIPROT: Q7Z7A6;
DR  UNIPROT: Q96D84;
DR  Pfam: PF01535;
DR  Pfam: PF13812;
DR  Pfam: PF17177;
DR  PROSITE: PS51375;
DR  OMIM: 220111;
DR  OMIM: 607544;
DR  DisGeNET: 10128;
DE  Function: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:12832482, ECO:0000269|PubMed:15081402, ECO:0000269|PubMed:15139850, ECO:0000269|PubMed:15272088, ECO:0000269|PubMed:17050673}.
DE  Disease: Leigh syndrome French-Canadian type (LSFC) [MIM:220111]: Severe neurological disorder characterized by bilaterally symmetrical necrotic lesions in subcortical brain regions that is commonly associated with systemic cytochrome c oxidase (COX) deficiency. In the Saguenay-Lac Saint Jean region of Quebec province in Canada, a biochemically distinct form of Leigh syndrome with COX deficiency has been described. Patients have been observed to have a developmental delay, hypotonia, mild facial dysmorphism, chronic well-compensated metabolic acidosis, and high mortality due to episodes of severe acidosis and coma. Enzyme activity was close to normal in kidney and heart, 50% of normal in fibroblasts and skeletal muscle, and nearly absent in brain and liver. LSFC patients show reduced (<30%) levels of LRPPRC in both fibroblast and liver mitochondria and a specifically reduced translation of COX subunits MT-CO1/COXI and MT-CO3 (COXIII). {ECO:0000269|PubMed:12529507, ECO:0000269|PubMed:26510951}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-641062,EBI-1050853; Score: 0.35
DE  Interaction: O14880; IntAct: EBI-724754,EBI-1050853; Score: 0.35
DE  Interaction: Q15118; IntAct: EBI-7016221,EBI-1050853; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-715747,EBI-1050853; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-1058922,EBI-1050853; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-352528,EBI-1050853; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-448665,EBI-1050853; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-1050853; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-10191195,EBI-1050853; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-720706,EBI-1050853; Score: 0.35
DE  Interaction: Q9BSB4; IntAct: EBI-2946739,EBI-1050853; Score: 0.40
DE  Interaction: O94966; IntAct: EBI-2511895,EBI-1050853; Score: 0.40
DE  Interaction: Q70CQ1; IntAct: EBI-2511022,EBI-1050853; Score: 0.40
DE  Interaction: Q9NXR7; IntAct: EBI-949389,EBI-1050853; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-447544,EBI-1050853; Score: 0.67
DE  Interaction: Q9Y6E7; IntAct: EBI-2606540,EBI-1050853; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-10973834,EBI-1050853; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-2551470,EBI-1050853; Score: 0.35
DE  Interaction: P09803; IntAct: EBI-984420,EBI-1050853; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-762451,EBI-1050853; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-1056089,EBI-1050853; Score: 0.35
DE  Interaction: Q9GZT3; IntAct: EBI-1050853,EBI-1050793; Score: 0.56
DE  Interaction: P42768; IntAct: EBI-1050853,EBI-346375; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-1050853,EBI-1802965; Score: 0.35
DE  Interaction: Q9HBM1; IntAct: EBI-1050853,EBI-999909; Score: 0.35
DE  Interaction: Q14573; IntAct: EBI-1050853,EBI-351055; Score: 0.35
DE  Interaction: P28715; IntAct: EBI-1050853,EBI-765885; Score: 0.35
DE  Interaction: Q9NPL8; IntAct: EBI-1050853,EBI-6268651; Score: 0.35
DE  Interaction: Q9BZQ6; IntAct: EBI-1050853,EBI-2556756; Score: 0.35
DE  Interaction: J3KS15; IntAct: EBI-1050853,EBI-11073518; Score: 0.35
DE  Interaction: A8K7Q2; IntAct: EBI-1050853,EBI-10971637; Score: 0.35
DE  Interaction: Q9P2K8-2; IntAct: EBI-1050853,EBI-10988447; Score: 0.35
DE  Interaction: J3QL56; IntAct: EBI-1050853,EBI-11137054; Score: 0.35
DE  Interaction: Q6UB35; IntAct: EBI-1050853,EBI-1046835; Score: 0.35
DE  Interaction: P38117; IntAct: EBI-1050853,EBI-1056543; Score: 0.35
DE  Interaction: Q6PJT7-9; IntAct: EBI-1050853,EBI-10963388; Score: 0.35
DE  Interaction: Q02224; IntAct: EBI-1050853,EBI-1375040; Score: 0.35
DE  Interaction: B4DR80; IntAct: EBI-1050853,EBI-11056323; Score: 0.35
DE  Interaction: P39748; IntAct: EBI-1050853,EBI-707816; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-1050853,EBI-357448; Score: 0.35
DE  Interaction: Q9H6K4; IntAct: EBI-8477908,EBI-1050853; Score: 0.35
DE  Interaction: Q9BVS5; IntAct: EBI-3197877,EBI-1050853; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-1050853,EBI-413628; Score: 0.51
DE  Interaction: O75381; IntAct: EBI-594898,EBI-1050853; Score: 0.35
DE  Interaction: Q6QDQ4; IntAct: EBI-5276623,EBI-1050853; Score: 0.35
DE  Interaction: Q15327; IntAct: EBI-5653378,EBI-1050853; Score: 0.37
DE  Interaction: P05919; IntAct: EBI-6248147,EBI-1050853; Score: 0.46
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-1050853; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-1050853; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-1050853; Score: 0.35
DE  Interaction: Q9Z381; IntAct: EBI-1050853,EBI-2865275; Score: 0.37
DE  Interaction: Q81ME0; IntAct: EBI-2813646,EBI-1050853; Score: 0.37
DE  Interaction: P11171; IntAct: EBI-1050853,EBI-1050906; Score: 0.40
DE  Interaction: Q9Y2Q3; IntAct: EBI-1050853,EBI-1053767; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-1050853,EBI-307369; Score: 0.40
DE  Interaction: Q9Y5V3; IntAct: EBI-1050853,EBI-716006; Score: 0.40
DE  Interaction: P01889; IntAct: EBI-1050853,EBI-1046513; Score: 0.40
DE  Interaction: P43360; IntAct: EBI-1050853,EBI-1045155; Score: 0.40
DE  Interaction: Q9UBN6; IntAct: EBI-1050853,EBI-1044859; Score: 0.40
DE  Interaction: P62330; IntAct: EBI-1050853,EBI-638181; Score: 0.40
DE  Interaction: P23508; IntAct: EBI-1050853,EBI-307531; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-1050853,EBI-359276; Score: 0.40
DE  Interaction: Q9HC98; IntAct: EBI-1050853,EBI-740364; Score: 0.40
DE  Interaction: P60520; IntAct: EBI-1050853,EBI-720116; Score: 0.40
DE  Interaction: P78396; IntAct: EBI-1050853,EBI-375065; Score: 0.40
DE  Interaction: P19532; IntAct: EBI-1050853,EBI-1048957; Score: 0.40
DE  Interaction: O75365; IntAct: EBI-1050853,EBI-1043866; Score: 0.40
DE  Interaction: Q9Y5J5; IntAct: EBI-1050853,EBI-1055859; Score: 0.40
DE  Interaction: Q9P2S5; IntAct: EBI-1050853,EBI-1054904; Score: 0.40
DE  Interaction: Q13480; IntAct: EBI-517684,EBI-1050853; Score: 0.35
DE  Interaction: Q15256; IntAct: EBI-2265659,EBI-1050853; Score: 0.35
DE  Interaction: P27361; IntAct: EBI-73995,EBI-1050853; Score: 0.35
DE  Interaction: Q16828; IntAct: EBI-746870,EBI-1050853; Score: 0.35
DE  Interaction: P28562; IntAct: EBI-975493,EBI-1050853; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-1783035,EBI-1050853; Score: 0.35
DE  Interaction: P08631; IntAct: EBI-346340,EBI-1050853; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-717097,EBI-1050853; Score: 0.35
DE  Interaction: Q14CZ7; IntAct: EBI-10234819,EBI-1050853; Score: 0.35
DE  Interaction: Q96KR7; IntAct: EBI-717068,EBI-1050853; Score: 0.35
DE  Interaction: Q9NZI8; IntAct: EBI-1053892,EBI-1050853; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-2931238,EBI-1050853; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-1050853; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-1050853; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-1050853,EBI-81279; Score: 0.40
DE  Interaction: Q15653; IntAct: EBI-1050853,EBI-352889; Score: 0.40
DE  Interaction: P60709; IntAct: EBI-353944,EBI-1050853; Score: 0.40
GO  GO:0000794;
GO  GO:0005856;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0042645;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0048487;
GO  GO:0008017;
GO  GO:0003723;
GO  GO:0003697;
GO  GO:0031625;
GO  GO:0047497;
GO  GO:0051028;
GO  GO:0000961;
GO  GO:0070129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALLRSARWLLRAGAAPRLPLSLRLLPGGPGRLHAASYLPAARAGPVAGGLLSPARLYAIAAKEKDIQEESTFSSRKIS
SQ  NQFDWALMRLDLSVRRTGRIPKKLLQKVFNDTCRSGGLGGSHALLLLRSCGSLLPELKLEERTEFAHRIWDTLQKLGAVY
SQ  DVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVT
SQ  GHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMDRDLLQIIFSFSKAGYPQY
SQ  VSEILEKVTCERRYIPDAMNLILLLVTEKLEDVALQILLACPVSKEDGPSVFGSFFLQHCVTMNTPVEKLTDYCKKLKEV
SQ  QMHSFPLQFTLHCALLANKTDLAKALMKAVKEEGFPIRPHYFWPLLVGRRKEKNVQGIIEILKGMQELGVHPDQETYTDY
SQ  VIPCFDSVNSARAILQENGCLSDSDMFSQAGLRSEAANGNLDFVLSFLKSNTLPISLQSIRSSLLLGFRRSMNINLWSEI
SQ  TELLYKDGRYCQEPRGPTEAVGYFLYNLIDSMSDSEVQAKEEHLRQYFHQLEKMNVKIPENIYRGIRNLLESYHVPELIK
SQ  DAHLLVESKNLDFQKTVQLTSSELESTLETLKAENQPIRDVLKQLILVLCSEENMQKALELKAKYESDMVTGGYAALINL
SQ  CCRHDKVEDALNLKEEFDRLDSSAVLDTGKYVGLVRVLAKHGKLQDAINILKEMKEKDVLIKDTTALSFFHMLNGAALRG
SQ  EIETVKQLHEAIVTLGLAEPSTNISFPLVTVHLEKGDLSTALEVAIDCYEKYKVLPRIHDVLCKLVEKGETDLIQKAMDF
SQ  VSQEQGEMVMLYDLFFAFLQTGNYKEAKKIIETPGIRARSARLQWFCDRCVANNQVETLEKLVELTQKLFECDRDQMYYN
SQ  LLKLYKINGDWQRADAVWNKIQEENVIPREKTLRLLAEILREGNQEVPFDVPELWYEDEKHSLNSSSASTTEPDFQKDIL
SQ  IACRLNQKKGAYDIFLNAKEQNIVFNAETYSNLIKLLMSEDYFTQAMEVKAFAETHIKGFTLNDAANSRLIITQVRRDYL
SQ  KEAVTTLKTVLDQQQTPSRLAVTRVIQALAMKGDVENIEVVQKMLNGLEDSIGLSKMVFINNIALAQIKNNNIDAAIENI
SQ  ENMLTSENKVIEPQYFGLAYLFRKVIEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLVDAGKVDDARALLQRCGAI
SQ  AEQTPILLLFLLRNSRKQGKASTVKSVLELIPELNEKEEAYNSLMKSYVSEKDVTSAKALYEHLTAKNTKLDDLFLKRYA
SQ  SLLKYAGEPVPFIEPPESFEFYAQQLRKLRENSS
//
ID  P08928;
PN  Lamin Dm0;
GN  Lam;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}. Nucleus inner membrane {ECO:0000269|PubMed:16439308}. Nucleus envelope {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}. Nucleus lamina {ECO:0000269|PubMed:18723885}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967}. Cytoplasm {ECO:0000269|PubMed:9199347}. Note=Nuclear periphery (PubMed:7593280). At metaphase and anaphase, weakly expressed in the nuclear envelope and spindle poles (PubMed:16439308). Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347). In spermatocytes detected at the spindle envelope, spindle poles and astral membrane throughout meiosis I, whereas mostly depleted in meiosis II (PubMed:27402967). Colocalizes with nuclear pore complex component Nup107 throughout meiosis I (PubMed:27402967). {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}.
DR  UNIPROT: P08928;
DR  UNIPROT: Q9VMQ0;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (PubMed:3126192, PubMed:15035436). May have a role in the localization of the LEM domain proteins Ote, bocks and MAN1 to the nuclear membrane (PubMed:15035436, PubMed:16439308). In spermatocytes, plays a role in maintaining type-A lamin LamC nuclear localization; regulates meiotic cytokinesis by maintaining the structure of the spindle envelope, and by contributing to the formation of the contractile ring and central spindle (PubMed:27402967). {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:3126192}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-188444,EBI-188444; Score: 0.27
DE  Interaction: Q9GQN4; IntAct: EBI-149669,EBI-188444; Score: 0.35
DE  Interaction: Q9VPX2; IntAct: EBI-3433683,EBI-188444; Score: 0.46
DE  Interaction: M9NFI9; IntAct: EBI-9933576,EBI-188444; Score: 0.35
DE  Interaction: Q8IPM8; IntAct: EBI-129885,EBI-188444; Score: 0.35
DE  Interaction: Q24247; IntAct: EBI-187829,EBI-188444; Score: 0.35
DE  Interaction: Q9V9S0; IntAct: EBI-117239,EBI-188444; Score: 0.35
DE  Interaction: Q9VMV9; IntAct: EBI-182234,EBI-188444; Score: 0.35
DE  Interaction: Q9VMT1; IntAct: EBI-3430567,EBI-188444; Score: 0.35
DE  Interaction: P23226; IntAct: EBI-239813,EBI-188444; Score: 0.35
DE  Interaction: Q8IQX8; IntAct: EBI-3432029,EBI-188444; Score: 0.35
DE  Interaction: Q9VT04; IntAct: EBI-125572,EBI-188444; Score: 0.35
DE  Interaction: Q8SXF0; IntAct: EBI-195791,EBI-188444; Score: 0.35
DE  Interaction: P34082; IntAct: EBI-868243,EBI-188444; Score: 0.53
DE  Interaction: P16568; IntAct: EBI-188444,EBI-112159; Score: 0.27
DE  Interaction: P25028; IntAct: EBI-188444,EBI-106103; Score: 0.27
DE  Interaction: O01382; IntAct: EBI-188444,EBI-91422; Score: 0.27
DE  Interaction: P20240; IntAct: EBI-115143,EBI-188444; Score: 0.50
DE  Interaction: Q9XTM1; IntAct: EBI-188444,EBI-96207; Score: 0.37
DE  Interaction: Q9VD23; IntAct: EBI-188444,EBI-187890; Score: 0.37
DE  Interaction: Q8T3J9; IntAct: EBI-188444,EBI-139759; Score: 0.37
DE  Interaction: Q9VAU6; IntAct: EBI-188444,EBI-184493; Score: 0.37
DE  Interaction: P52295; IntAct: EBI-145898,EBI-188444; Score: 0.37
DE  Interaction: Q9VR64; IntAct: EBI-146474,EBI-188444; Score: 0.37
GO  GO:0005737;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0005634;
GO  GO:0000922;
GO  GO:0003682;
GO  GO:0005102;
GO  GO:0005200;
GO  GO:0008344;
GO  GO:0007569;
GO  GO:0007417;
GO  GO:0040003;
GO  GO:0006342;
GO  GO:0001745;
GO  GO:0048546;
GO  GO:0035262;
GO  GO:0070870;
GO  GO:0007112;
GO  GO:0007110;
GO  GO:0007084;
GO  GO:0008285;
GO  GO:0050777;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0007097;
GO  GO:0031081;
GO  GO:0006997;
GO  GO:0030838;
GO  GO:2000433;
GO  GO:1900182;
GO  GO:1905832;
GO  GO:0090435;
GO  GO:0048137;
GO  GO:0007283;
GO  GO:0007430;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSKSRRAGTATPQPGNTSTPRPPSAGPQPPPPSTHSQTASSPLSPTRHSRVAEKVELQNLNDRLATYIDRVRNLETENS
SQ  RLTIEVQTTRDTVTRETTNIKNIFEAELLETRRLLDDTARDRARAEIDIKRLWEENEELKNKLDKKTKECTTAEGNVRMY
SQ  ESRANELNNKYNQANADRKKLNEDLNEALKELERLRKQFEETRKNLEQETLSRVDLENTIQSLREELSFKDQIHSQEINE
SQ  SRRIKQTEYSEIDGRLSSEYDAKLKQSLQELRAQYEEQMQINRDEIQSLYEDKIQRLQEAAARTSNSTHKSIEELRSTRV
SQ  RIDALNANINELEQANADLNARIRDLERQLDNDRERHGQEIDLLEKELIRLREEMTQQLKEYQDLMDIKVSLDLEIAAYD
SQ  KLLVGEEARLNITPATNTATVQSFSQSLRNSTRATPSRRTPSAAVKRKRAVVDESEDHSVADYYVSASAKGNVEIKEIDP
SQ  EGKFVRLFNKGSEEVAIGGWQLQRLINEKGPSTTYKFHRSVRIEPNGVITVWSADTKASHEPPSSLVMKSQKWVSADNTR
SQ  TILLNSEGEAVANLDRIKRIVSQHTSSSRLSRRRSVTAVDGNEQLYHQQGDPQQSNEKCAIM
//
ID  Q63190;
PN  Emerin;
GN  Emd;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane {ECO:0000250}. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle- attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q63190;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta- catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1- dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non- farnesylated prelamin-A/C (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0048487;
GO  GO:0071363;
GO  GO:0090090;
GO  GO:0048147;
GO  GO:0031468;
GO  GO:0046827;
GO  GO:0060828;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKK
SQ  EDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDS
SQ  AYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATF
SQ  LLFVYYSIQAQEGNPFWMDP
//
ID  P40318;
PN  ERAD-associated E3 ubiquitin-protein ligase DOA10;
GN  SSM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: P40318;
DR  UNIPROT: D6VVQ1;
DR  PDB: 2M6M;
DR  Pfam: PF12906;
DR  PROSITE: PS51292;
DE  Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. Also recognizes the N- terminally acetylated residue of proteins as degradation signal (degron). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8. {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:16179952, ECO:0000269|PubMed:16437165, ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:17051211, ECO:0000269|PubMed:18812321, ECO:0000269|PubMed:20110468}.
DE  Reference Proteome: Yes;
DE  Interaction: P39015; IntAct: EBI-11238,EBI-18208; Score: 0.44
DE  Interaction: P47137; IntAct: EBI-25572,EBI-18208; Score: 0.44
DE  Interaction: P40513; IntAct: EBI-10316,EBI-18208; Score: 0.44
DE  Interaction: P06738; IntAct: EBI-13389,EBI-18208; Score: 0.44
DE  Interaction: P38758; IntAct: EBI-24443,EBI-18208; Score: 0.44
DE  Interaction: P39683; IntAct: EBI-12218,EBI-18208; Score: 0.44
DE  Interaction: P16467; IntAct: EBI-5696,EBI-18208; Score: 0.44
DE  Interaction: P11154; IntAct: EBI-14358,EBI-18208; Score: 0.44
DE  Interaction: P33399; IntAct: EBI-10046,EBI-18208; Score: 0.44
DE  Interaction: P25617; IntAct: EBI-18208,EBI-375711; Score: 0.44
DE  Interaction: P32288; IntAct: EBI-7665,EBI-18208; Score: 0.44
DE  Interaction: P53982; IntAct: EBI-8892,EBI-18208; Score: 0.44
DE  Interaction: P10963; IntAct: EBI-18208,EBI-13770; Score: 0.44
DE  Interaction: P00925; IntAct: EBI-18208,EBI-6475; Score: 0.44
DE  Interaction: P40825; IntAct: EBI-18648,EBI-18208; Score: 0.44
DE  Interaction: P30952; IntAct: EBI-10428,EBI-18208; Score: 0.44
DE  Interaction: Q04697; IntAct: EBI-27807,EBI-18208; Score: 0.44
DE  Interaction: P32835; IntAct: EBI-7926,EBI-18208; Score: 0.44
DE  Interaction: P23542; IntAct: EBI-2002,EBI-18208; Score: 0.44
DE  Interaction: P38998; IntAct: EBI-10264,EBI-18208; Score: 0.44
DE  Interaction: P38720; IntAct: EBI-1965,EBI-18208; Score: 0.44
DE  Interaction: P35202; IntAct: EBI-19195,EBI-18208; Score: 0.44
DE  Interaction: P80210; IntAct: EBI-14267,EBI-18208; Score: 0.44
DE  Interaction: P40217; IntAct: EBI-8951,EBI-18208; Score: 0.44
DE  Interaction: P38009; IntAct: EBI-14223,EBI-18208; Score: 0.44
DE  Interaction: Q04458; IntAct: EBI-27205,EBI-18208; Score: 0.44
DE  Interaction: P40959; IntAct: EBI-11636,EBI-18208; Score: 0.44
DE  Interaction: Q05979; IntAct: EBI-10016,EBI-18208; Score: 0.44
DE  Interaction: P40892; IntAct: EBI-26263,EBI-18208; Score: 0.44
DE  Interaction: P08524; IntAct: EBI-7069,EBI-18208; Score: 0.44
DE  Interaction: P25561; IntAct: EBI-21696,EBI-18208; Score: 0.44
DE  Interaction: P38787; IntAct: EBI-12913,EBI-18208; Score: 0.44
DE  Interaction: P46655; IntAct: EBI-18665,EBI-18208; Score: 0.44
DE  Interaction: P38158; IntAct: EBI-10326,EBI-18208; Score: 0.44
DE  Interaction: P38081; IntAct: EBI-21453,EBI-18208; Score: 0.44
DE  Interaction: Q01454; IntAct: EBI-5209,EBI-18208; Score: 0.44
DE  Interaction: Q08968; IntAct: EBI-29375,EBI-18208; Score: 0.44
DE  Interaction: P41816; IntAct: EBI-12734,EBI-18208; Score: 0.44
DE  Interaction: P46151; IntAct: EBI-11567,EBI-18208; Score: 0.44
DE  Interaction: P54885; IntAct: EBI-13872,EBI-18208; Score: 0.44
DE  Interaction: Q08686; IntAct: EBI-19264,EBI-18208; Score: 0.44
DE  Interaction: Q08444; IntAct: EBI-29777,EBI-18208; Score: 0.44
DE  Interaction: P50278; IntAct: EBI-17675,EBI-18208; Score: 0.44
DE  Interaction: P37254; IntAct: EBI-12831,EBI-18208; Score: 0.44
DE  Interaction: Q10740; IntAct: EBI-10175,EBI-18208; Score: 0.44
DE  Interaction: P50101; IntAct: EBI-19898,EBI-18208; Score: 0.44
DE  Interaction: P00331; IntAct: EBI-2222,EBI-18208; Score: 0.44
DE  Interaction: P16862; IntAct: EBI-9435,EBI-18208; Score: 0.44
DE  Interaction: P46680; IntAct: EBI-2406,EBI-18208; Score: 0.44
DE  Interaction: Q04212; IntAct: EBI-28073,EBI-18208; Score: 0.44
DE  Interaction: P15274; IntAct: EBI-2548,EBI-18208; Score: 0.44
DE  Interaction: P54007; IntAct: EBI-18208,EBI-27168; Score: 0.44
DE  Interaction: Q99260; IntAct: EBI-29503,EBI-18208; Score: 0.44
DE  Interaction: Q04491; IntAct: EBI-16529,EBI-18208; Score: 0.44
DE  Interaction: P31539; IntAct: EBI-8050,EBI-18208; Score: 0.44
DE  Interaction: P10592; IntAct: EBI-8603,EBI-18208; Score: 0.44
DE  Interaction: P41903; IntAct: EBI-14154,EBI-18208; Score: 0.44
DE  Interaction: P38716; IntAct: EBI-24682,EBI-18208; Score: 0.44
DE  Interaction: P17076; IntAct: EBI-15431,EBI-18208; Score: 0.44
DE  Interaction: P53051; IntAct: EBI-10464,EBI-18208; Score: 0.44
DE  Interaction: P53265; IntAct: EBI-23264,EBI-18208; Score: 0.44
DE  Interaction: P53101; IntAct: EBI-24097,EBI-18208; Score: 0.44
DE  Interaction: P53183; IntAct: EBI-23747,EBI-18208; Score: 0.44
DE  Interaction: P10356; IntAct: EBI-22726,EBI-18208; Score: 0.44
DE  Interaction: P21524; IntAct: EBI-15234,EBI-18208; Score: 0.44
DE  Interaction: P25044; IntAct: EBI-14183,EBI-18208; Score: 0.44
DE  Interaction: Q07505; IntAct: EBI-5951,EBI-18208; Score: 0.44
DE  Interaction: P16120; IntAct: EBI-19259,EBI-18208; Score: 0.44
DE  Interaction: P25576; IntAct: EBI-21752,EBI-18208; Score: 0.44
DE  Interaction: P17967; IntAct: EBI-13012,EBI-18208; Score: 0.44
DE  Interaction: P00817; IntAct: EBI-9338,EBI-18208; Score: 0.44
DE  Interaction: P12866; IntAct: EBI-18383,EBI-18208; Score: 0.64
DE  Interaction: P32589; IntAct: EBI-8648,EBI-18208; Score: 0.35
DE  Interaction: Q04228; IntAct: EBI-27730,EBI-18208; Score: 0.71
DE  Interaction: P38428; IntAct: EBI-18208,EBI-27580; Score: 0.56
DE  Interaction: P38911; IntAct: EBI-18208,EBI-6951; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-18208,EBI-4308; Score: 0.71
GO  GO:0000837;
GO  GO:0005783;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNID
SQ  ISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMML
SQ  DGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPR
SQ  LSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLR
SQ  HVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQN
SQ  EFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAV
SQ  VFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNG
SQ  YTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPIL
SQ  AGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKIL
SQ  HDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESS
SQ  SYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVR
SQ  DVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPD
SQ  FRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCL
SQ  SKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAI
SQ  MIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSK
SQ  LNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESF
SQ  TFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES
//
ID  Q9UN42;
PN  Protein ATP1B4;
GN  ATP1B4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000269|PubMed:14656723, ECO:0000269|PubMed:17592128}.
DR  UNIPROT: Q9UN42;
DR  UNIPROT: Q17RR0;
DR  UNIPROT: Q9UN41;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DR  DisGeNET: 23439;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit. {ECO:0000269|PubMed:17592128}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07325; IntAct: EBI-12894731,EBI-3911467; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-12894731,EBI-3914288; Score: 0.56
DE  Interaction: Q8N6G5; IntAct: EBI-12894731,EBI-10267100; Score: 0.56
DE  Interaction: Q9BZL3; IntAct: EBI-12894731,EBI-741850; Score: 0.56
DE  Interaction: Q7Z2K6; IntAct: EBI-12894731,EBI-10976398; Score: 0.56
DE  Interaction: Q5BVD1; IntAct: EBI-12894731,EBI-10243654; Score: 0.56
DE  Interaction: P07306; IntAct: EBI-12894731,EBI-1172335; Score: 0.56
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0005890;
GO  GO:0015077;
GO  GO:0045944;
GO  GO:0006355;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGN
SQ  AWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFA
SQ  HSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGY
SQ  STGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVV
SQ  KNQAVPVQCQLKGKGVINDVINDRFVGRVIFTLNIET
//
ID  Q9N4M4;
PN  Nuclear anchorage protein 1;
GN  anc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:15773756, ECO:0000305|PubMed:12169658}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15773756}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, most probably the outer nuclear membrane, or with mitochondrial membrane. {ECO:0000305|PubMed:12169658}.
DR  UNIPROT: Q9N4M4;
DR  UNIPROT: O61841;
DR  UNIPROT: O61842;
DR  UNIPROT: Q6IMP3;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Plays a central role in nuclear and mitochondrial anchoring (PubMed:12169658, PubMed:6889924, PubMed:10375507, PubMed:22298703). Probably connects nuclei to the cytoskeleton by interacting with unc-84 at the nuclear envelope and with F-actin in the cytoplasm, creating a bridge across the nuclear envelope between the cytoskeleton and the nucleus (PubMed:15773756). Has a role in positioning of the cell body of the PVQ lumbar interneuron (PubMed:22298703). {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:22298703, ECO:0000269|PubMed:6889924, ECO:0000303|PubMed:15773756}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0051087;
GO  GO:0007010;
GO  GO:0051179;
GO  GO:0051647;
GO  GO:0006997;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MSSSPPARPCCVCFRFRPHEDEKAQKNTFTRWINFHLEEHSSSGRIEDLFEDIRDGVLLCHLIEVLTGEALAVHKGRVSK
SQ  RVHHIANLTTALTVLRRRGLELINNNAADIADGNPRIVLGLIWQIILHFQIETNMILLREWGWAATGTEEPTSSAQPEVV
SQ  VTAPSPTPSSKKSHSKVSSLSGSKTSLASGEKAPSSPLRQRIASFLTPTKKAPKLTAQPVKQSVEQVFLRWINAEIGDLV
SQ  GGRRVENMDKQWRDGILFCALVSRWRPDVISMREVTNANPRDNLELAFNLAHQHLGVRRLLAVEDMMIEKPDKRSVITYV
SQ  SQFVRMFGERSPMQGREQHEIFLAWLEATYLLCTRHELNSQECSRIRREFIEHRPLFNTIIVTKVNYDVEELVEIEKKWD
SQ  CIRETLEKYARRSERDLPEPFASIATWIAGAEHILSRPLDLDATDAKKTVTMLQKLISEHQKYMEDLPKRQEDFEEAVKH
SQ  GGLGGRPVAPEFSEPLRARFAQIEEENEPRISTLRILTTHYILLQYLQHIDEKIILWRTADSVTLLLRWIKEYTQLNAEN
SQ  PQAKCASYINKITLTMANDQNSKLDKEAILNTSNEKTAETLKRFESLWIELKLLKVEWVEWETHVSQLEEIIEERRRNGV
SQ  PPTPEDEQALAVITAGADQLAPKLGASARLSNNQRLDVLTHSFKKLTKTTIKIGGRLVVELEPSTSEQASKISYSWQASD
SQ  ELLKVEMQLRDRIQRDADSSDREQLEYRAETFRNIRDKLIELERLNEIYDNHSRDQVDTPNRNLIRHDMGTIIYGLQAGQ
SQ  YANFVDLSCYAFVYDEYNQVPVNLTENVLSEDYVREIVNRKKAILTRRENNEDEIRESIRDMEECDRIIEGWQSTEIEEL
SQ  RAEWNIKLSEFESWHEMMQQVEVLSQTIQTRLDVTVIQTIWILKERSYDIKHSELGGTLRESLEQLATTSETSVNRHLQN
SQ  LELSNEQDCPDAIEFLEEVGRESVSKLSAAVDDRYIYTLHVLRTKMELFRRLQNFCDAVKILRSQNTKWNGIKISQIDQV
SQ  QSEIDTLIVRLDEEWTQDANQLRAELASIHGSFFQLEFDRLNEKLNMLIHDKDKLRELMVHRRHYLTAANELITDSKTDL
SQ  AQRATSSDHPDDILRATDEVTKALDIKGEELRRLGELAEMNITDLVVVALILSFRRRQLGSEGEPEVEELRRALREIIAR
SQ  PITEPRDVSPDAIVADILRMKDEKKRDEKTIDEIQATTLTDEQRASFAPLIEDYRRRADRHRIVFEHLVMIYLDWLSRQF
SQ  DELEDEIGMTIQTSRADDLRRMNSTEWNKWKTDLANIERQVGPDTKKALSAELADLHRKRDSMEARINKYLTHSAKINAK
SQ  LTQFEKWLNAIEEDIEQTERQFEDPERSYRFGSLHEVALAKQRLVAKLERLNVANKEEVLRLCERYHTIMHKLTPFQTAV
SQ  GLPLHVSTNLDRNGPFQSQISVSSIASSELERPESVMSLTSSIGVIPADVAELSPFEAKINKLLQKLHIIEDSYLKGPKP
SQ  IDTVREDVKQLEKYRNRGAEILQQLSTSNIEDAEKEGLKHRFVLMLNNYDDILRSIENEIRDDNELTAKNQEILAELSNA
SQ  EQTLQNSPLEDLDISAELDRLQMQLDLVKVMCNKPRKYVECELIDSSREGSPQERRRRKKKVMVMVSNTITTIIHVVEER
SQ  LEASDISRNPDVQQKLVAVKENLRELDTTTVTPHPPSIMSPLGTENRNDLEEVKRLAAEIDRAIDTASSMYEDAPTDEDA
SQ  LKSAIHLLDDQKVTLNHLHVVLEGIPEKNEQDRTDAIDIASSVGEKLGNLKSAVEEVYEEVLASTNPVKEDQPLQHIQEV
SQ  QTTPAEQSNWDTDEFSRQPPVLSDERIELKTDPSAIDKFEVRSDEDPVPKIIDLFGQLQTAVNEASPLACEGTDDVDALQ
SQ  VASDKLTKQDRTIRKIHAILDTIDDPVQKPAIIESLDKIKDQINNARDNINRQIDNLNYNQTPVVVPKESTKTPLNEIED
SQ  AVRQASTVVSDELCNTEKLLSARQTLANVKPQVDSVEANVWSNPETIETVTPILEEYTTLVDNIEKKLANEIEVPTNDPS
SQ  RQDLVQQLQDVILECEEVVVNCDNIEKLEESKLKLEKARPLLDQIGDNVEKLSREQSPDTSDAIDALSNVHQQYNATIMS
SQ  IDDKIDELKNPEEDTSAADQLISELHVISEMPAVTIDLSMLNAIEEGLSTLPAHQAENVQAKIDELRQKKEVADQTEQIL
SQ  SDLNAFGDMPAITLDLDLLKSVEDGIAVLPVEDSERIKAKIVDLRKKKEDADQAEALLQELSVISDMPISTLDLNMLQGI
SQ  EDNLNSLPAEESDEIREKLNELRRRKQESDQAEALLQELSVISDMPISTLDLNMLQGVEDNLNSLPTEEADKIREKINDL
SQ  RRRKQESDLAEALLQELSVIYDMPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDLAEALLQELSVIYD
SQ  MPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDQAEALLQELSVVSDMPASTIDINMLQSIEDGLSTLL
SQ  SEDRSKIQQAIDSLRKKKSDSDLAQHALEALSVQSKLPSVSINLEELKKLEETLSTVPVEDSKVIRDKIAELKTEKALAD
SQ  HAENYLVELKKIEDMPISAVGSDVLATIEDQILQMPVQYQPSVKETLDKLKQAKEEDDKLAGVYDELEKIAKLPARDYDN
SQ  KLLAKIDEKLNSLPKDQIAETHRKVEDIKVTKADIVAQIDVLDKLPAKDIDEHLLNSIEEKLPTIPSDSSDQLQIAIGKL
SQ  RDRKQANIDEGKKILNELAEIQKMPADSLNEHALNLLATESDKFGSEISDKIMQEIDVLREKQNNHEVARLNAESVLQQL
SQ  DKISEEPHLSLTEERLAPFLQNIDTVPACFVDKIRNKINEVQKLHDEAVQDEKDELKEKLVAKVQNIGKTSIDDVNVSDF
SQ  EEIEREINGSLEAFEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSA
SQ  KVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVP
SQ  SSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDV
SQ  VSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDR
SQ  LNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNK
SQ  AAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQ
SQ  LGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYND
SQ  LLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKA
SQ  VIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRN
SQ  NSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKM
SQ  IDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLI
SQ  LSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAK
SQ  ESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKL
SQ  NNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTG
SQ  DDEKRADELKNDDGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELL
SQ  QALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLV
SQ  VGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPEND
SQ  PTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDRGRSTGSAVG
SQ  DKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLA
SQ  TAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAP
SQ  SSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLS
SQ  DLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDP
SQ  ERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLN
SQ  ISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKK
SQ  KKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDA
SQ  IKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRA
SQ  DELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKA
SQ  IPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEK
SQ  VFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADEL
SQ  RQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVS
SQ  GVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQ
SQ  YAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQ
SQ  PKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLL
SQ  KQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTE
SQ  LDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAA
SQ  HDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFV
SQ  KDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRD
SQ  RAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDP
SQ  QVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSN
SQ  NEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVE
SQ  NQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKS
SQ  PDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIV
SQ  SRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFL
SQ  AARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAE
SQ  QTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASR
SQ  KHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAE
SQ  PLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAK
SQ  NENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHL
SQ  ATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDD
SQ  ANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPE
SQ  DALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQ
SQ  LQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNA
SQ  ARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRA
SQ  ELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQ
SQ  AVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQR
SQ  ISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKS
SQ  DIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQ
SQ  LKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEM
SQ  IDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDA
SQ  EKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAV
SQ  KNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQ
SQ  AEINDRLNKLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDK
SQ  KQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRL
SQ  KDLLKQLGSAVGEKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKE
SQ  RAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKE
SQ  VEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERASIWERFVKAKDDLYDYLEKLENNVSDVLNRPRLPVSQAQQR
SQ  FNKLKEQSYLLDRIRDLKIDFDDLGEALLPLTVAEDELRFMHVHVESIERQYEDTMDKLNAEITAEVELLRTLDILSNEL
SQ  SQCKEDINNPSVDVDELSRATMLNDAIAHLENQKVVVARSEKDRKFVESSTSIDLDQLLAEAKRLLKEIEPRLQLAQPDH
SQ  DNEDDEDEEKGSDEKPYDVRAAAEVLSALYPDEHPHNVLRNIGFEELPSDSESRSEFDSLDSRSDGLLSPIPDDSTLSEE
SQ  QLRRQRSRWRRVLRTALPLQALLVLLMGAACLVPHCDDEYCCQLLNNFAKSFDPSLEFVNGPPPF
//
ID  O35425;
PN  Bcl-2-related ovarian killer protein;
GN  Bok;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000269|PubMed:23429263}. Recycling endosome membrane {ECO:0000269|PubMed:23429263}. Nucleus outer membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23429263}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor (PubMed:23429263, PubMed:26949185). Localizes in early and late endosome upon blocking of apoptosis (PubMed:23429263). Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}.
DR  UNIPROT: O35425;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DE  Function: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1- independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD- proteasome degradation system, resulting in cytochrome c release (PubMed:9535847, PubMed:26949185). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0033106;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0055038;
GO  GO:0032588;
GO  GO:0051400;
GO  GO:0046983;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0006919;
GO  GO:0008635;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0006921;
GO  GO:0097192;
GO  GO:0072332;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0051902;
GO  GO:1901029;
GO  GO:0060546;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:0048709;
GO  GO:0043065;
GO  GO:1902237;
GO  GO:1900119;
GO  GO:2001244;
GO  GO:1901030;
GO  GO:1903899;
GO  GO:0051259;
GO  GO:0010506;
GO  GO:1901382;
GO  GO:0051480;
GO  GO:1904708;
GO  GO:0001836;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQ
SQ  IRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRK
SQ  TLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
//
ID  Q9FLH0;
PN  Protein CROWDED NUCLEI 4;
GN  CRWN4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:23396599}; Peripheral membrane protein {ECO:0000269|PubMed:23396599}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:F4HRT5}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Localized frequently to the nuclear periphery as punctate structures of different sizes. During prometaphase to anaphase, localized diffusely in the cytoplasm. Later assembled into punctate structures in the cytoplasm and then to the chromatin surface. Relocalized in part to the nuclear periphery during late telophase, the other part is still localized on the punctate structures (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9FLH0;
DR  UNIPROT: F4JXK1;
DR  UNIPROT: O49539;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:24308514, PubMed:23396599). Involved in the maintenance of interphase chromocenter integrity and organization (PubMed:24308514). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
GO  GO:0010369;
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0006974;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23396599};
SQ  MATSSRSERFPITPSTAATNRLTITPNSRVLKSPLTEEIMWKRLKDAGFDEQSIKNRDKAALIAYIAKLESEVYDYQHNM
SQ  GLLLLEKNELSSQYEEIKASVDESDLTHMREKSAYVSALAEAKKREESLKKDVGIAKECISSLEKTLHEMRAECAETKVS
SQ  AGSTMSEAHVMIEDALKKLADAEAKMRAAEALQAEANRYHRIAERKLKEVESREDDLTRRLASFKSECETKENEMVIERQ
SQ  TLNERRKSLQQEHERLLDAQVSLNQREDHIFARSQELAELEKGLDTAKTTFEEERKAFEDKKSNLEIALALCAKREEAVS
SQ  ERESSLLKKEQELLVAEEKIASKESELIQNVLANQEVILRKRKSDVEAELECKSKSVEVEIESKRRAWELREVDIKQRED
SQ  LVGEKEHDLEVQSRALAEKEKDITEKSFNLDEKEKNLVATEEDINRKTTMLEDEKERLRKLDLELQQSLTSLEDKRKRVD
SQ  SATQKLEALKSETSELSTLEMKLKEELDDLRAQKLEMLAEADRLKVEKAKFEAEWEHIDVKREELRKEAEYITRQREAFS
SQ  MYLKDERDNIKEERDALRNQHKNDVESLNREREEFMNKMVEEHSEWLSKIQRERADFLLGIEMQKRELEYCIENKREELE
SQ  NSSRDREKAFEQEKKLEEERIQSLKEMAEKELEHVQVELKRLDAERLEIKLDRERREREWAELKDSVEELKVQREKLETQ
SQ  RHMLRAERDEIRHEIEELKKLENLKVALDDMSMAKMQLSNLERSWEKVSALKQKVVSRDDELDLQNGVSTVSNSEDGYNS
SQ  SMERQNGLTPSSATPFSWIKRCTNLIFKTSPEKSTLMHHYEEEGGVPSEKLKLESSRREEKAYTEGLSIAVERLEAGRKR
SQ  RGNTSGDETSEPSNNKKRKHDVTQKYSDEADTQSVISSPQNVPEDKHELPSSQTQTPSGMVVISETVKITRVTCETEVTN
SQ  KVTTLDCSESPSEAGRKMGEETEDGDCNQTGINASETVIHNEAATEDICT
//
ID  P54074;
PN  Protein ASI1;
GN  ASI1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P54074;
DR  UNIPROT: D6VZU2;
DE  Function: Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor- regulated genes in the absence of inducing signals. {ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
DE  Reference Proteome: Yes;
DE  Interaction: P53895; IntAct: EBI-27241,EBI-28975; Score: 0.46
DE  Interaction: P53983; IntAct: EBI-28603,EBI-27241; Score: 0.56
DE  Interaction: P02829; IntAct: EBI-27241,EBI-8659; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-27241,EBI-5127; Score: 0.40
DE  Interaction: Q969F0; IntAct: EBI-743099,EBI-27241; Score: 0.56
GO  GO:0097658;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0046872;
GO  GO:0004842;
GO  GO:0071230;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSSTSSENVFINSFSYLNQTSQAVISGNSTFANVINFPYRLGLSFIGAVNLQYEQTVKSEEIPPTLRSVFDTIGFFFSP
SQ  YAIFCFVIAIVLNRFVVFYAVLNNGSRRTLPLWLSNVFHVSAVVVLAMVSLGPLTLGKDFKILGDPAFAQEKFLLNIFYA
SQ  FAYSYCVETIFTIMRNSSPLEGTDYSLFELSIQFYTMTNNNTKFLDSPDYIIDCSMAILSRILIHLVEIFRLRNYRLLFS
SQ  TIMNLCHICYLGIRVKQGGWKSLPFSVKFRHFPKLFSVSIICLSLLIFKLSCLIRWDPFGKSRNSCELLQFYPLSRNWKK
SQ  YLNYTGEEDFSAMATKFALLLCSGTELMEKGIRREFPAINIPDNVNEKFFISGYLNELSKPYKENTSISFPKKNSSILKQ
SQ  RFFLMFPKSIIWIMKKLVGQVFFGFRDNKDEDIPDNDPSKMLKITKTNSLNNSAGHKEDIELELLNTSDDEYSEDYEPSE
SQ  VESLGDSDEENLEEDSLIFNETRDALLDLFSSEDNEVHTDYNWIMSTSRILQQKLLSDKTLTRASILDTKLSEVDETFGT
SQ  ESDFDLSCAVCKVNERNTVLWPCRCFAICEDCRISLGLRGFSTCVCCRSKVHGYCKVHPVSDSK
//
ID  Q9GYU8;
PN  Nuclear pore complex protein Nup88;
GN  mbo;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10921908}. Nucleus membrane {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:17032737}; Peripheral membrane protein {ECO:0000269|PubMed:10921908}; Cytoplasmic side {ECO:0000269|PubMed:10921908}. Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Note=Is recruited to non-active chromatin sites (PubMed:20144761). Localization to the nuclear rim is promoted by Nup214 (PubMed:17032737). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:20144761}.
DR  UNIPROT: Q9GYU8;
DR  UNIPROT: Q9VG41;
DR  Pfam: PF10168;
DE  Function: Essential component of nuclear pore complex (PubMed:10921908, PubMed:14638854, PubMed:17032737). Required for the anchoring of Nup214 and emb on the nuclear envelope and thereby attenuates nuclear export signal (NES)-mediated nuclear export (PubMed:14638854). Together with Nup214, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the activation of an immune response (PubMed:10921908, PubMed:17032737). {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7JXF5; IntAct: EBI-127204,EBI-161961; Score: 0.37
DE  Interaction: P98149; IntAct: EBI-161961,EBI-188843; Score: 0.27
DE  Interaction: P15330; IntAct: EBI-161961,EBI-198375; Score: 0.27
DE  Interaction: Q9VVK7; IntAct: EBI-98134,EBI-161961; Score: 0.37
DE  Interaction: Q9VSB2; IntAct: EBI-161961,EBI-111803; Score: 0.37
DE  Interaction: Q9Y091; IntAct: EBI-161961,EBI-101869; Score: 0.37
DE  Interaction: A1ZAW3; IntAct: EBI-161961,EBI-145169; Score: 0.37
DE  Interaction: Q9VC66; IntAct: EBI-166765,EBI-161961; Score: 0.37
DE  Interaction: Q9VT69; IntAct: EBI-132558,EBI-161961; Score: 0.37
DE  Interaction: Q9VVT5; IntAct: EBI-179987,EBI-161961; Score: 0.37
DE  Interaction: Q9VTP5; IntAct: EBI-161961,EBI-83709; Score: 0.37
DE  Interaction: Q9VS38; IntAct: EBI-161961,EBI-187169; Score: 0.37
DE  Interaction: Q9VS62; IntAct: EBI-161961,EBI-108483; Score: 0.37
DE  Interaction: Q9VVB4; IntAct: EBI-161961,EBI-94400; Score: 0.37
DE  Interaction: Q9XYW6; IntAct: EBI-135209,EBI-161961; Score: 0.37
DE  Interaction: Q8INY6; IntAct: EBI-161961,EBI-98027; Score: 0.37
DE  Interaction: Q9VND7; IntAct: EBI-161961,EBI-152722; Score: 0.37
DE  Interaction: Q9VNE1; IntAct: EBI-161961,EBI-157610; Score: 0.37
DE  Interaction: Q86B91; IntAct: EBI-188776,EBI-161961; Score: 0.37
DE  Interaction: Q9VF13; IntAct: EBI-161961,EBI-160031; Score: 0.37
DE  Interaction: Q9VUG5; IntAct: EBI-161961,EBI-185897; Score: 0.37
DE  Interaction: Q9VZ87; IntAct: EBI-161961,EBI-147544; Score: 0.37
DE  Interaction: Q9VFF6; IntAct: EBI-161961,EBI-147124; Score: 0.37
DE  Interaction: Q9VWQ6; IntAct: EBI-177552,EBI-161961; Score: 0.37
DE  Interaction: Q9VK23; IntAct: EBI-161961,EBI-192963; Score: 0.37
DE  Interaction: Q9W4L6; IntAct: EBI-161961,EBI-91499; Score: 0.37
DE  Interaction: A1Z6E8; IntAct: EBI-161961,EBI-130934; Score: 0.37
DE  Interaction: Q9W1A4; IntAct: EBI-161961,EBI-91385; Score: 0.40
DE  Interaction: Q7K0A0; IntAct: EBI-161961,EBI-184732; Score: 0.37
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0019730;
GO  GO:0006406;
GO  GO:0046826;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10921908};
SQ  MSLTDVLELNKTELFAKIRNGLPVVQRTQNLLDCKDDLLFAWHAKDSCLLVRNWRSSLAAKVNIQFQTLIPSSLVSLEVD
SQ  RVLASNEGSLVALSGPRGVVIMELPRRWGPDGYYKDGKPVITCRTFGLDTQLFLKNPHLEVRQVRWHPHSVSDSTLLVLL
SQ  NNNTIRVYNHSKLRHVWQVGPPVLRSGANNSLCDFGELAVDFDIAPAAKPRVTEPETAGNNETTLDKSNKTLVAAKSLPK
SQ  QERIEWPMVVLRENGNIYILMTGVDSENTRLQGPVTITPQAHDNYGLESCALMIIPSLPPTIVIAESNGKLHHALLMEAE
SQ  ATEHSFNEVDDSVLIEPAEYVVHVLETVELELGISAPATGKEGGNCPIYLKRDLINELRYFAYHNAGLHAVTVSFIAELQ
SQ  RYLESESDEDRLELAVSASAEYILCTKFDSSETVNAVFGLALLQIPAGIVLLLGSGQVISLKLVIDAQLLVTPNENKPVD
SQ  SEVSQQESGPPFVDTIKSLLQRSVNQPILADKLSSPSAQESFELLNQAIEVLREQYLKRHDLVRAAFTRHINQIQLKKEQ
SQ  QLQEIQDLEQERELISERAHKLAERFEEISYNQELLVRKCNALMQRANASLPNSVIAEREFSQEVIRLNKVTQSLAAGLE
SQ  TAKKTFNKQRYHIAQSQEDLKKNAYELPEKQHRTITEILTQLTGEIDRQITDVKRINKIVGI
//
ID  P32499;
PN  Nucleoporin NUP2;
GN  NUP2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
DR  UNIPROT: P32499;
DR  UNIPROT: D6VYX5;
DR  UNIPROT: Q06130;
DR  PDB: 1UN0;
DR  PDB: 2C1T;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading. {ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11425876, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631, ECO:0000269|PubMed:12062099, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:14514698, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-12401,EBI-12401; Score: 0.44
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-12401; Score: 0.78
DE  Interaction: P39705; IntAct: EBI-12401,EBI-20731; Score: 0.70
DE  Interaction: P46673; IntAct: EBI-12401,EBI-12345; Score: 0.44
DE  Interaction: P38181; IntAct: EBI-12401,EBI-11756; Score: 0.44
DE  Interaction: Q12306; IntAct: EBI-17490,EBI-12401; Score: 0.37
DE  Interaction: P16474; IntAct: EBI-7876,EBI-12401; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-8637,EBI-12401; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-12401; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12401,EBI-8627; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-8632,EBI-12401; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-12401; Score: 0.53
DE  Interaction: P33416; IntAct: EBI-8680,EBI-12401; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-12401,EBI-24570; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-12401,EBI-8611; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-12401; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-12401,EBI-8666; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-12401,EBI-25940; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-12401,EBI-3949; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-12401,EBI-8591; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-17751,EBI-12401; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-1797,EBI-12401; Score: 0.78
DE  Interaction: P50102; IntAct: EBI-19863,EBI-12401; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-18868,EBI-12401; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-12401,EBI-7926; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-12401,EBI-20254; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-12401,EBI-18981; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-12401,EBI-18986; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-12401,EBI-6314; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-12401,EBI-10789; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-12401,EBI-9166; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-12401,EBI-9890; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-12401,EBI-3242; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-12401,EBI-2218; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-13638,EBI-12401; Score: 0.35
DE  Interaction: P32799; IntAct: EBI-5070,EBI-12401; Score: 0.35
DE  Interaction: P19414; IntAct: EBI-2104,EBI-12401; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-12401; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-12401,EBI-19749; Score: 0.37
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0042564;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0061676;
GO  GO:0008536;
GO  GO:0017056;
GO  GO:0030466;
GO  GO:0035392;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0043547;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQ
SQ  VDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKS
SQ  SDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKT
SQ  ETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTF
SQ  GSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQ
SQ  EDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINT
SQ  NTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKG
SQ  SQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKK
SQ  DDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK
//
ID  Q80VJ8;
PN  Protein KASH5;
GN  Ccdc155;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22826121}. Chromosome, telomere {ECO:0000269|PubMed:22826121}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000269|PubMed:24586178, ECO:0000269|PubMed:26842404}.
DR  UNIPROT: Q80VJ8;
DR  UNIPROT: E9QNS3;
DR  UNIPROT: E9QQ69;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homologue pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0000781;
GO  GO:0016021;
GO  GO:0000800;
GO  GO:0034993;
GO  GO:0090619;
GO  GO:0005640;
GO  GO:0070840;
GO  GO:0042802;
GO  GO:0007015;
GO  GO:0090220;
GO  GO:0000724;
GO  GO:0090172;
GO  GO:0048477;
GO  GO:0007283;
GO  GO:0051225;
GO  GO:0051653;
GO  GO:0007129;
GO  GO:0034397;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHSILRSSLSSREALRMRQLKGLRKERPGRHPLGVRLRAIWTSFLFPNPPHSGGKLRASTAAVEEHQEWSMDLPEGQAGG
SQ  PTAQMYLWEQPEEASSRPLLSLEEQILNSTFEACDPHKTGTVTVAHLLAYLEAVTGQGPQDVRLQTLARSLDPYGEGAGA
SQ  TVELDTFLVVMRDWIAACQLQGGLERAEETAYEGALASPHLPSVCPEAEESANLESFGGEDPRPEGPATAELLSNLEDLE
SQ  LSNRRLAGENAKLQRSVETAEEGSARLGEEITALRKQLRSTQQALQVAKALDEELEDLKTLAKSLEEQNRSLMAQARHTE
SQ  KEQQHLAAEVETLQEENEKLLAERDGVKRRSEELATEKDALKRQLCECERLICQREAVLSERTRHAESLARTLEEYRTTT
SQ  QELRQEISNLEEQLSQSQEGPEELLEGAEAGRVGWIMALPPSLDLEIQAIRQEQDVASAGLSSPLYGVWQWEEVEPEPEP
SQ  EPEPEPEPEPQEVEFPSEDPARQQTDLQREPVRALEGSRAPCLRLSRSQEEEEEEEESWVLADPSSPLGTYHHKLAPGSS
SQ  RESCHIVPEMHQALMPVVRDLVPVERSRTQHCLHPQHSPGIRISQHPLVPTPVLGLLLLLLLSILLFSQSPPPTWPHLQL
SQ  YYLQPPPV
//
ID  Q7JRE4;
PN  Inner nuclear membrane protein Man1;
GN  MAN1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16439308}; Multi-pass membrane protein {ECO:0000269|PubMed:16439308}. Cytoplasm {ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308}. Note=During anaphase and metaphase, detected in the nuclear envelope and spindle poles. {ECO:0000269|PubMed:16439308}.
DR  UNIPROT: Q7JRE4;
DR  UNIPROT: Q961B2;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:16439308). Acts as a negative regulator of the BMP (Dpp) signaling cascade during crossvein development in pupal wings and possibly during synaptic transmission at the neuromuscular junction (NMJ) (PubMed:18723885, PubMed:20036230). Appears to be required for pupal development and consequently transition to the adult stage (PubMed:18723885, PubMed:20036230). During pupal development, plays essential and redundant functions with the other LEM domain proteins; bocks and Ote (PubMed:24700158). {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:20036230, ECO:0000269|PubMed:24700158}.
DE  Reference Proteome: Yes;
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-3415366; Score: 0.35
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0003676;
GO  GO:0001525;
GO  GO:0030514;
GO  GO:0006997;
GO  GO:1902531;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTESLNSLSDKELHRKLIQSGFPSTPVTETTRAVLIEKLRKHTRADKLKKRSNKYVLYSKEQQESPPFPQYHQYHAPQP
SQ  PQNYANGLDNNNDLDQTGGSSAYNRSLDESDSSPLQLSASKMYAPPPVVASNYDGDCSPHSLGLNGKYLQPCSMPYAIDT
SQ  SNNYGKPSGKAKLSDGGVVNRLLSFRDTTIQRKFNYPTGQASRIPLRKERLTRFALSDLKSFIRNPDIRPYVIPRVLISL
SQ  FLIFLTIITVLYVGKRFEQSPIDKAALKYTLCNPNDMQMISEKVNCIEKDSLRGALDMSEELFRHLNERARLHHCKDANL
SQ  SPALEIGEFVREMVSNPKTHRGNLHSNLMAAKYLITENPQWSIQVVDSTKHLGQTSHFELSEPNLPLKCIVLKKVTRFFT
SQ  VIGALLLIVAGFLIVYVAVVIYRVKQKEALLAVDQFQKDIINELIYLSSQSESPEVVINQLQEKFLPAKKRSKLLSSWNK
SQ  ALKQLEKNDSRVLFGMVNRDGKAMRTIAWNRNVDKKDVGLVKKWQSPAFDNSNKIANPPTPCLKIRHMFDSSEVDQANLK
SQ  QSIVESIIEKVGTRCKICDVQLDVQSCCVYIRCASEEDAGTIHKEINGWWFDKRLISIKFLRLERYLSRFPKPSAEPLYF
SQ  HTNEAANTHS
//
ID  Q14764;
PN  Major vault protein;
GN  MVP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16441665}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:16441665}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16441665}. Note=5% found in the nuclear pore complex (PubMed:15133037). Translocates from the nucleus to the cytoplasm upon EGF treatment (PubMed:16441665).
DR  UNIPROT: Q14764;
DR  UNIPROT: Q96BG4;
DR  UNIPROT: Q9BPW6;
DR  UNIPROT: Q9BQT1;
DR  UNIPROT: Q9UBD1;
DR  PDB: 1Y7X;
DR  Pfam: PF11978;
DR  Pfam: PF01505;
DR  Pfam: PF17794;
DR  Pfam: PF17795;
DR  Pfam: PF17796;
DR  PROSITE: PS51224;
DR  OMIM: 605088;
DR  DisGeNET: 9961;
DE  Function: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217, ECO:0000269|PubMed:16441665}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-740019,EBI-2816254; Score: 0.44
DE  Interaction: Q07065; IntAct: EBI-2816254,EBI-702400; Score: 0.37
DE  Interaction: Self; IntAct: EBI-2816254,EBI-2816254; Score: 0.80
DE  Interaction: P13569; IntAct: EBI-349854,EBI-2816254; Score: 0.35
DE  Interaction: Q8NHY2-1; IntAct: EBI-9698228,EBI-2816254; Score: 0.35
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-2816254; Score: 0.37
DE  Interaction: P60710; IntAct: EBI-353957,EBI-2816254; Score: 0.35
DE  Interaction: Q9QWF0; IntAct: EBI-639217,EBI-2816254; Score: 0.35
DE  Interaction: Q9D6T1; IntAct: EBI-10990005,EBI-2816254; Score: 0.35
DE  Interaction: P51692; IntAct: EBI-1186119,EBI-2816254; Score: 0.35
DE  Interaction: Q6IRU7; IntAct: EBI-2553851,EBI-2816254; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-354956,EBI-2816254; Score: 0.35
DE  Interaction: Q07797; IntAct: EBI-8399565,EBI-2816254; Score: 0.35
DE  Interaction: Q06180; IntAct: EBI-8471238,EBI-2816254; Score: 0.35
DE  Interaction: P21980; IntAct: EBI-727668,EBI-2816254; Score: 0.35
DE  Interaction: Q5SRY7; IntAct: EBI-11073522,EBI-2816254; Score: 0.35
DE  Interaction: Q3TRR0; IntAct: EBI-8328917,EBI-2816254; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-2816254; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-354967,EBI-2816254; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-8322817,EBI-2816254; Score: 0.35
DE  Interaction: P18031; IntAct: EBI-968788,EBI-2816254; Score: 0.35
DE  Interaction: Q9UMR2-2; IntAct: EBI-21500353,EBI-2816254; Score: 0.35
DE  Interaction: Q9UKK3; IntAct: EBI-2816254,EBI-2623021; Score: 0.35
DE  Interaction: Q9P2K3-3; IntAct: EBI-2816254,EBI-11087909; Score: 0.35
DE  Interaction: Q9HD26-2; IntAct: EBI-2816254,EBI-11102276; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-2816254,EBI-351896; Score: 0.35
DE  Interaction: Q9H0E2; IntAct: EBI-74615,EBI-2816254; Score: 0.56
DE  Interaction: Q53EP0-3; IntAct: EBI-10242151,EBI-2816254; Score: 0.56
DE  Interaction: P52292; IntAct: EBI-349938,EBI-2816254; Score: 0.37
DE  Interaction: P00156; IntAct: EBI-1224441,EBI-2816254; Score: 0.37
DE  Interaction: Q14161; IntAct: EBI-1046878,EBI-2816254; Score: 0.37
DE  Interaction: Q13423; IntAct: EBI-1391318,EBI-2816254; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-2816254,EBI-752420; Score: 0.37
DE  Interaction: P34913; IntAct: EBI-2816254,EBI-724704; Score: 0.37
DE  Interaction: P00738; IntAct: EBI-2816254,EBI-1220767; Score: 0.37
DE  Interaction: A0A384KY07; IntAct: EBI-2816254,EBI-2843582; Score: 0.37
DE  Interaction: Q81ME0; IntAct: EBI-2816254,EBI-2813646; Score: 0.37
DE  Interaction: Q81ZA2; IntAct: EBI-2816254,EBI-2811440; Score: 0.37
DE  Interaction: Q81TT4; IntAct: EBI-2810319,EBI-2816254; Score: 0.37
DE  Interaction: A0A0F7RF31; IntAct: EBI-2810739,EBI-2816254; Score: 0.37
DE  Interaction: P20339; IntAct: EBI-399437,EBI-2816254; Score: 0.35
DE  Interaction: O60496; IntAct: EBI-1046024,EBI-2816254; Score: 0.35
DE  Interaction: Q14254; IntAct: EBI-348613,EBI-2816254; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-1056125,EBI-2816254; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-2816254; Score: 0.40
DE  Interaction: P57053; IntAct: EBI-2880265,EBI-2816254; Score: 0.40
DE  Interaction: P58876; IntAct: EBI-4409942,EBI-2816254; Score: 0.40
DE  Interaction: Q5QNW6-2; IntAct: EBI-20847120,EBI-2816254; Score: 0.40
DE  Interaction: Q8WUN7; IntAct: EBI-2816254,EBI-12867288; Score: 0.56
DE  Interaction: Q16656-4; IntAct: EBI-2816254,EBI-11742836; Score: 0.56
DE  Interaction: Q86UW9; IntAct: EBI-2816254,EBI-740376; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-2816254,EBI-741158; Score: 0.56
DE  Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-2816254; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-2547514,EBI-2816254; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-2816254; Score: 0.35
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0016020;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034774;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0038127;
GO  GO:0051028;
GO  GO:0031953;
GO  GO:0061099;
GO  GO:0023057;
GO  GO:0043312;
GO  GO:0015031;
GO  GO:0023051;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQ
SQ  VRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVV
SQ  EIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRG
SQ  VSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGI
SQ  QDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRA
SQ  VIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARV
SQ  VFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAK
SQ  LFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDV
SQ  QSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTG
SQ  TAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTE
SQ  AIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAP
SQ  QAPGDNHVVPVLR
//
ID  O75694;
PN  Nuclear pore complex protein Nup155;
GN  NUP155;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.
DR  UNIPROT: O75694;
DR  UNIPROT: Q9UBE9;
DR  UNIPROT: Q9UFL5;
DR  PDB: 5A9Q;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DR  OMIM: 606694;
DR  OMIM: 615770;
DR  DisGeNET: 9631;
DE  Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
DE  Disease: Atrial fibrillation, familial, 15 (ATFB15) [MIM:615770]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:19070573}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1050769; Score: 0.35
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-1050769; Score: 0.35
DE  Interaction: Q96I36; IntAct: EBI-6570698,EBI-1050769; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-1050769,EBI-374880; Score: 0.55
DE  Interaction: Q9Y275; IntAct: EBI-519169,EBI-1050769; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-1050769; Score: 0.35
DE  Interaction: P51159; IntAct: EBI-716881,EBI-1050769; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-2807346,EBI-1050769; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-6659161,EBI-1050769; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-1050769; Score: 0.40
DE  Interaction: Q53GS7; IntAct: EBI-1955541,EBI-1050769; Score: 0.37
DE  Interaction: O43281; IntAct: EBI-1050769,EBI-718488; Score: 0.56
DE  Interaction: Q8WVZ9; IntAct: EBI-473695,EBI-1050769; Score: 0.40
DE  Interaction: Q8IY92; IntAct: EBI-2370740,EBI-1050769; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-2551981,EBI-1050769; Score: 0.40
DE  Interaction: Q09019; IntAct: EBI-724564,EBI-1050769; Score: 0.40
DE  Interaction: Q6GQQ9; IntAct: EBI-527784,EBI-1050769; Score: 0.40
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-1050769; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-1050769; Score: 0.35
DE  Interaction: Q86VQ0; IntAct: EBI-6658186,EBI-1050769; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-1046993,EBI-1050769; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-1050769; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-1050769; Score: 0.35
DE  Interaction: Q15637; IntAct: EBI-1050769,EBI-744603; Score: 0.37
DE  Interaction: P02545; IntAct: EBI-351935,EBI-1050769; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-1050769; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-1050769; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1050769; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-1050769; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-716247,EBI-1050769; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-1050769; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-1050769; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-1050769; Score: 0.35
DE  Interaction: A0A384KHV9; IntAct: EBI-2862405,EBI-1050769; Score: 0.37
DE  Interaction: P01889; IntAct: EBI-1050769,EBI-1046513; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-1050769,EBI-359276; Score: 0.40
DE  Interaction: P11171; IntAct: EBI-1050769,EBI-1050906; Score: 0.40
DE  Interaction: P11802; IntAct: EBI-1050769,EBI-295644; Score: 0.40
DE  Interaction: P19532; IntAct: EBI-1050769,EBI-1048957; Score: 0.40
DE  Interaction: P23508; IntAct: EBI-1050769,EBI-307531; Score: 0.40
DE  Interaction: P40337; IntAct: EBI-1050769,EBI-301246; Score: 0.40
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-1050769; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-1050769; Score: 0.35
GO  GO:0043657;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0086014;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0006998;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006405;
GO  GO:0000972;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P37199};
SQ  MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPE
SQ  ISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPH
SQ  VRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAY
SQ  QAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQ
SQ  NAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASS
SQ  TVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDH
SQ  IPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAA
SQ  CDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALG
SQ  NPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEF
SQ  LDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCE
SQ  HQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANEL
SQ  LQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIV
SQ  GLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALY
SQ  NWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIAR
SQ  AILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAE
SQ  CKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNW
SQ  DVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGY
SQ  LVELQSMSSSVAVQAITGNFKSLQAKLERLH
//
ID  P20676;
PN  Nucleoporin NUP1;
GN  NUP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
DR  UNIPROT: P20676;
DR  UNIPROT: D6W2F9;
DR  PDB: 4C31;
DR  PDB: 4MBE;
DR  PDB: 5OWU;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1- KAP95-cargo complex. {ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-12392; Score: 0.77
DE  Interaction: P16474; IntAct: EBI-12392,EBI-7876; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-12392,EBI-10154; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-12392,EBI-8571; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12392,EBI-8627; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-12392,EBI-8632; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-12392,EBI-8591; Score: 0.35
DE  Interaction: P52297; IntAct: EBI-618940,EBI-12392; Score: 0.44
DE  Interaction: P35177; IntAct: EBI-17958,EBI-12392; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-19863,EBI-12392; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-12392,EBI-740459; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-12392; Score: 0.56
DE  Interaction: P10592; IntAct: EBI-12392,EBI-8603; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-12392,EBI-1797; Score: 0.69
DE  Interaction: P10081; IntAct: EBI-12392,EBI-9017; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-12392,EBI-7218; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-12392,EBI-13275; Score: 0.35
DE  Interaction: P06168; IntAct: EBI-12392,EBI-9082; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-12392,EBI-13517; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-12392,EBI-2447; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-12392,EBI-6475; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-12392,EBI-6333; Score: 0.35
DE  Interaction: P41832; IntAct: EBI-12392,EBI-3692; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-12392,EBI-2218; Score: 0.35
DE  Interaction: Q03771; IntAct: EBI-36525,EBI-12392; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-12392; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12392; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12392; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTLHVNKRKRVSGTSQHSDSLTQ
SQ  NNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRNMRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTP
SQ  SPIKNGSCTRQLAGKSGEDTNVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKT
SQ  SENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPIQESFVPNSERSGTPTLKKNI
SQ  EPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAVFKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTV
SQ  PSTTLFNFGGKSDTVTSASQPFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNT
SQ  KPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSSAQFTFGKAATAKETHTKPSE
SQ  TPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEERKSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTE
SQ  PAQKDSSVVSEPKKPSFTFASSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTT
SQ  TSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTPIPVLGKPTDATGNTTSKSAF
SQ  SFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTNIAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAAS
SQ  NQSSFNFGNNGAGGLNPFTSATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSN
SQ  NQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNVTNPSSIFGGAGGVPTTSFGQ
SQ  PQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR
//
ID  Q9UKX7;
PN  Nuclear pore complex protein Nup50;
GN  NUP50;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065}. Nucleus membrane {ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Localizes to the nucleoplasmic fibrils of the nuclear pore complex (By similarity). Dissociates from the NPC structure early during prophase of mitosis (PubMed:12802065). Associates with the newly formed nuclear membrane during telophase (PubMed:12802065). In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa (By similarity). {ECO:0000250|UniProtKB:O08587, ECO:0000269|PubMed:12802065}.
DR  UNIPROT: Q9UKX7;
DR  UNIPROT: B1AHA4;
DR  UNIPROT: B2RB15;
DR  UNIPROT: O75644;
DR  UNIPROT: Q8N6V5;
DR  UNIPROT: Q9NPM9;
DR  UNIPROT: Q9NPR6;
DR  UNIPROT: Q9P1K5;
DR  PDB: 2EC1;
DR  PDB: 3TJ3;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DR  OMIM: 604646;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:20016008). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin- alpha:beta-cargo complex and importin recycling (PubMed:20016008). Interacts with regulatory proteins of cell cycle progression including CDKN1B (By similarity). This interaction is required for correct intracellular transport and degradation of CDKN1B (By similarity). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000269|PubMed:20016008}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-351935,EBI-2371082; Score: 0.46
DE  Interaction: P49790; IntAct: EBI-286779,EBI-2371082; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-2371082; Score: 0.35
DE  Interaction: P29991; IntAct: EBI-8826488,EBI-2371082; Score: 0.37
DE  Interaction: Q9UBN7; IntAct: EBI-301697,EBI-2371082; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-2371082; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-396343,EBI-2371082; Score: 0.72
DE  Interaction: O15131; IntAct: EBI-2371082,EBI-540602; Score: 0.67
DE  Interaction: O60684; IntAct: EBI-359923,EBI-2371082; Score: 0.72
DE  Interaction: P52292; IntAct: EBI-349938,EBI-2371082; Score: 0.72
DE  Interaction: P52294; IntAct: EBI-2371082,EBI-358383; Score: 0.83
DE  Interaction: Q7Z726; IntAct: EBI-2371082,EBI-10323362; Score: 0.56
DE  Interaction: O00505; IntAct: EBI-358297,EBI-2371082; Score: 0.72
DE  Interaction: Q8IY92; IntAct: EBI-2370740,EBI-2371082; Score: 0.35
DE  Interaction: Q9QWT9; IntAct: EBI-2552204,EBI-2371082; Score: 0.40
DE  Interaction: E9PVX6; IntAct: EBI-2553009,EBI-2371082; Score: 0.40
DE  Interaction: E9PUA5; IntAct: EBI-10972016,EBI-2371082; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11335160,EBI-2371082; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-2371082; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-2371082; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-2371082; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-1058976,EBI-2371082; Score: 0.27
DE  Interaction: P42694; IntAct: EBI-1210654,EBI-2371082; Score: 0.27
DE  Interaction: Q14145; IntAct: EBI-2371082,EBI-751001; Score: 0.56
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-2371082; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-593303,EBI-2371082; Score: 0.44
DE  Interaction: P16403; IntAct: EBI-358372,EBI-2371082; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-358900,EBI-2371082; Score: 0.40
DE  Interaction: P58876; IntAct: EBI-4409942,EBI-2371082; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-1056125,EBI-2371082; Score: 0.40
DE  Interaction: Q99880; IntAct: EBI-1237119,EBI-2371082; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-2371082; Score: 0.40
DE  Interaction: Q13547; IntAct: EBI-301834,EBI-2371082; Score: 0.40
DE  Interaction: Q8IW93-1; IntAct: EBI-25410216,EBI-2371082; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-356283,EBI-2371082; Score: 0.60
DE  Interaction: Q9NRA8; IntAct: EBI-2371082,EBI-301024; Score: 0.27
DE  Interaction: Q2M3V2; IntAct: EBI-2371082,EBI-8832444; Score: 0.27
DE  Interaction: Q9Y2I1; IntAct: EBI-2688731,EBI-2371082; Score: 0.27
DE  Interaction: Q9Y4F3; IntAct: EBI-5235902,EBI-2371082; Score: 0.27
GO  GO:0043657;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O08587};
SQ  MAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTGGAFKGFKGLVVPSGGGRFSGFGSGA
SQ  GGKPLEGLSNGNNITSAPPFASAKAAADPKVAFGSLAANGPTTLVDKVSNPKTNGDSQQPSSSGLASSKACVGNAYHKQL
SQ  AALNCSVRDWIVKHVNTNPLCDLTPIFKDYEKYLANIEQQHGNSGRNSESESNKVAAETQSPSLFGSTKLQQESTFLFHG
SQ  NKTEDTPDKKMEVASEKKTDPSSLGATSASFNFGKKVDSSVLGSLSSVPLTGFSFSPGNSSLFGKDTTQSKPVSSPFPTK
SQ  PLEGQAEGDSGECKGGDEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGIGTLHLKPTANQKTQLLVRADTN
SQ  LGNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPIDEKNATMPVTMLIRVKTSEDADELHKILLEKKDA
//
ID  P14907;
PN  Nucleoporin NSP1;
GN  NSP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P14907;
DR  UNIPROT: D6VWE3;
DR  PDB: 1O6O;
DR  Pfam: PF05064;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport. {ECO:0000269|PubMed:10889207, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11352936, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9461539, ECO:0000269|PubMed:9774653, ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-12265; Score: 0.72
DE  Interaction: P40368; IntAct: EBI-12331,EBI-12265; Score: 0.87
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12265; Score: 0.35
DE  Interaction: Q02796; IntAct: EBI-30514,EBI-12265; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-12265,EBI-8555; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12265,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12265,EBI-8603; Score: 0.53
DE  Interaction: P40005; IntAct: EBI-2342435,EBI-12265; Score: 0.56
DE  Interaction: P48363; IntAct: EBI-12265,EBI-13239; Score: 0.56
DE  Interaction: P52553; IntAct: EBI-12265,EBI-13260; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-13246,EBI-12265; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-12265,EBI-8680; Score: 0.35
DE  Interaction: P48353; IntAct: EBI-8369,EBI-12265; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-12265,EBI-8591; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-3824,EBI-12265; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-17964,EBI-12265; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-17751,EBI-12265; Score: 0.35
DE  Interaction: Q02199; IntAct: EBI-12315,EBI-12265; Score: 0.68
DE  Interaction: P39723; IntAct: EBI-20675,EBI-12265; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12265; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-12265,EBI-286758; Score: 0.62
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-12265; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-2186,EBI-12265; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-19863,EBI-12265; Score: 0.35
DE  Interaction: P48837; IntAct: EBI-12265,EBI-12324; Score: 0.81
DE  Interaction: Q05166; IntAct: EBI-12265,EBI-3035; Score: 0.37
DE  Interaction: Q8IYF3-3; IntAct: EBI-12265,EBI-11523345; Score: 0.56
DE  Interaction: P40066; IntAct: EBI-22648,EBI-12265; Score: 0.44
DE  Interaction: P34077; IntAct: EBI-12056,EBI-12265; Score: 0.35
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-12265; Score: 0.35
DE  Interaction: P51998; IntAct: EBI-12265,EBI-450; Score: 0.35
DE  Interaction: P40477; IntAct: EBI-12265,EBI-11747; Score: 0.59
DE  Interaction: P22353; IntAct: EBI-12265,EBI-407; Score: 0.35
DE  Interaction: Q06678; IntAct: EBI-12265,EBI-392; Score: 0.35
DE  Interaction: P36516; IntAct: EBI-12265,EBI-387; Score: 0.35
DE  Interaction: P36525; IntAct: EBI-12265,EBI-15545; Score: 0.35
DE  Interaction: P36523; IntAct: EBI-12265,EBI-15518; Score: 0.35
DE  Interaction: Q04599; IntAct: EBI-12265,EBI-38719; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-12265,EBI-8659; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12265; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12265; Score: 0.32
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0097064;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0006405;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPT
SQ  SNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGN
SQ  ANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFG
SQ  SGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKP
SQ  AFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKPDENKASATSKPAFSF
SQ  GAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKS
SQ  DEKKDSDSSKPAFSFGTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSFGSKPTGKE
SQ  EGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSTADVKSSDSLKLNSKPVELKPVSLDNKTLDDL
SQ  VTKWTNQLTESASHFEQYTKKINSWDQVLVKGGEQISQLYSDAVMAEHSQNKIDQSLQYIERQQDELENFLDNFETKTEA
SQ  LLSDVVSTSSGAAANNNDQKRQQAYKTAQTLDENLNSLSSNLSSLIVEINNVSNTFNKTTNIDINNEDENIQLIKILNSH
SQ  FDALRSLDDNSTSLEKQINSIKK
//
ID  P40477;
PN  Nucleoporin NUP159;
GN  NUP159;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P40477;
DR  UNIPROT: D6VVH2;
DR  PDB: 1XIP;
DR  PDB: 3PBP;
DR  PDB: 3RRM;
DR  PDB: 3TKN;
DR  PDB: 4DS1;
DR  Pfam: PF16755;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre- ribosome, and protein export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:9736720, ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12265,EBI-11747; Score: 0.59
DE  Interaction: P40066; IntAct: EBI-22648,EBI-11747; Score: 0.44
DE  Interaction: P40368; IntAct: EBI-12331,EBI-11747; Score: 0.81
DE  Interaction: Q06142; IntAct: EBI-11747,EBI-9145; Score: 0.61
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11747; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-11747,EBI-8591; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-11747; Score: 0.35
DE  Interaction: P47138; IntAct: EBI-25576,EBI-11747; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-11747,EBI-19049; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-11747,EBI-22339; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-11747; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-11747,EBI-8627; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-11747,EBI-8632; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-11747; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-11747,EBI-8659; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-11747,EBI-8603; Score: 0.35
DE  Interaction: Q12046; IntAct: EBI-11747,EBI-553; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11747; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11747; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0000774;
GO  GO:0017056;
GO  GO:0003714;
GO  GO:0097064;
GO  GO:0006607;
GO  GO:0031081;
GO  GO:0016973;
GO  GO:0006611;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKAVVGELQLLRDHITSDSTPLTF
SQ  KWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFRTVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQL
SQ  AQNVTSFDVTNSQLAVLLKDRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDDE
SQ  VSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASSCSSEVSIWDSKQVIEPSQDSE
SQ  RAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTIERLPLVYILNNEGSLQIVGLFHVAAIKSGHYSINLESLEHE
SQ  KSLSPTSEKIPIAGQEQEEKKKNNESSKALSENPFTSANTSGFTFLKTQPAAANSLQSQSSSTFGAPSFGSSAFKIDLPS
SQ  VSSTSTGVASSEQDATDPASAKPVFGKPAFGAIAKEPSTSEYAFGKPSFGAPSFGSGKSSVESPASGSAFGKPSFGTPSF
SQ  GSGNSSVEPPASGSAFGKPSFGTPSFGSGNSSAEPPASGSAFGKPSFGTSAFGTASSNETNSGSIFGKAAFGSSSFAPAN
SQ  NELFGSNFTISKPTVDSPKEVDSTSPFPSSGDQSEDESKSDVDSSSTPFGTKPNTSTKPKTNAFDFGSSSFGSGFSKALE
SQ  SVGSDTTFKFGTQASPFSSQLGNKSPFSSFTKDDTENGSLSKGSTSEINDDNEEHESNGPNVSGNDLTDSTVEQTSSTRL
SQ  PETPSDEDGEVVEEEAQKSPIGKLTETIKKSANIDMAGLKNPVFGNHVKAKSESPFSAFATNITKPSSTTPAFSFGNSTM
SQ  NKSNTSTVSPMEEADTKETSEKGPITLKSVENPFLPAKEERTGESSKKDHNDDPKDGYVSGSEISVRTSESAFDTTANEE
SQ  IPKSQDVNNHEKSETDPKYSQHAVVDHDNKSKEMNETSKNNERSGQPNHGVQGDGIALKKDNEKENFDSNMAIKQFEDHQ
SQ  SSEEDASEKDSRQSSEVKESDDNMSLNSDRDESISESYDKLEDINTDELPHGGEAFKAREVSASADFDVQTSLEDNYAES
SQ  GIQTDLSESSKENEVQTDAIPVKHNSTQTVKKEAVDNGLQTEPVETCNFSVQTFEGDENYLAEQCKPKQLKEYYTSAKVS
SQ  NIPFVSQNSTLRLIESTFQTVEAEFTVLMENIRNMDTFFTDQSSIPLVKRTVRSINNLYTWRIPEAEILLNIQNNIKCEQ
SQ  MQITNANIQDLKEKVTDYVRKDIAQITEDVANAKEEYLFLMHFDDASSGYVKDLSTHQFRMQKTLRQKLFDVSAKINHTE
SQ  ELLNILKLFTVKNKRLDDNPLVAKLAKESLARDGLLKEIKLLREQVSRLQLEEKGKKASSFDASSSITKDMKGFKVVEVG
SQ  LAMNTKKQIGDFFKNLNMAK
//
ID  P40368;
PN  Nucleoporin NUP82;
GN  NUP82;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P40368;
DR  UNIPROT: D6VWC1;
DR  PDB: 3PBP;
DR  PDB: 3TKN;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain. {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:7559750, ECO:0000269|PubMed:9843582}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12331,EBI-12265; Score: 0.87
DE  Interaction: P37198; IntAct: EBI-12331,EBI-347978; Score: 0.56
DE  Interaction: P40066; IntAct: EBI-22648,EBI-12331; Score: 0.44
DE  Interaction: Q06410; IntAct: EBI-30856,EBI-12331; Score: 0.37
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12331; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12331,EBI-8627; Score: 0.53
DE  Interaction: P48363; IntAct: EBI-13239,EBI-12331; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12331; Score: 0.35
DE  Interaction: Q02199; IntAct: EBI-12331,EBI-12315; Score: 0.37
DE  Interaction: P40477; IntAct: EBI-12331,EBI-11747; Score: 0.81
DE  Interaction: P46673; IntAct: EBI-12331,EBI-12345; Score: 0.55
DE  Interaction: Q03790; IntAct: EBI-12331,EBI-27321; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-12331,EBI-11730; Score: 0.37
DE  Interaction: Q02630; IntAct: EBI-12331,EBI-11703; Score: 0.67
DE  Interaction: Q02629; IntAct: EBI-12331,EBI-11698; Score: 0.55
DE  Interaction: Q9BQD3; IntAct: EBI-739657,EBI-12331; Score: 0.56
DE  Interaction: Q9HCM9-2; IntAct: EBI-12331,EBI-11523450; Score: 0.56
DE  Interaction: Q9Y3C0; IntAct: EBI-12331,EBI-712969; Score: 0.56
DE  Interaction: Q12443; IntAct: EBI-12331,EBI-32591; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-12331,EBI-8591; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-12331,EBI-8632; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12331; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12331; Score: 0.32
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044612;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSQSSRLSALPIFQASLSASQSPRYIFSSQNGTRIVFIQDNIIRWYNVLTDSLYHSLNFSRHLVLDDTFHVISSTSGDLL
SQ  CLFNDNEIFVMEVPWGYSNVEDVSIQDAFQIFHYSIDEEEVGPKSSIKKVLFHPKSYRDSCIVVLKEDDTITMFDILNSQ
SQ  EKPIVLNKPNNSFGLDARVNDITDLEFSKDGLTLYCLNTTEGGDIFAFYPFLPSVLLLNEKDLNLILNKSLVMYESLDST
SQ  TDVIVKRNVIKQLQFVSKLHENWNSRFGKVDIQKEYRLAKVQGPFTINPFPGELYDYTATNIATILIDNGQNEIVCVSFD
SQ  DGSLILLFKDLEMSMSWDVDNYVYNNSLVLIERVKLQREIKSLITLPEQLGKLYVISDNIIQQVNFMSWASTLSKCINES
SQ  DLNPLAGLKFESKLEDIATIERIPNLAYINWNDQSNLALMSNKTLTFQNISSDMKPQSTAAETSISTEKSDTVGDGFKMS
SQ  FTQPINEILILNDNFQKACISPCERIIPSADRQIPLKNEASENQLEIFTDISKEFLQRIVKAQTLGVSIHNRIHEQQFEL
SQ  TRQLQSTCKIISKDDDLRRKFEAQNKKWDAQLSRQSELMERFSKLSKKLSQIAESNKFKEKKISHGEMKWFKEIRNQILQ
SQ  FNSFVHSQKSLQQDLSYLKSELTRIEAETIKVDKKSQNEWDELRKMLEIDSKIIKECNEELLQVSQEFTTKTQ
//
ID  P49687;
PN  Nucleoporin NUP145C;
GN  NUP145;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. [Nucleoporin NUP145N]: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards the nucleoplasmic side, nuclear pore complex.
DR  UNIPROT: P49687;
DR  UNIPROT: D6VU53;
DR  PDB: 3BG0;
DR  PDB: 3BG1;
DR  PDB: 3IKO;
DR  PDB: 3JRO;
DR  PDB: 3JRP;
DR  PDB: 3KEP;
DR  PDB: 3KES;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization. {ECO:0000269|PubMed:10542288, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8195299, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9305650}.
DE  Reference Proteome: Yes;
DE  Interaction: P32500; IntAct: EBI-11730,EBI-11950; Score: 0.37
DE  Interaction: P35729; IntAct: EBI-11713,EBI-11730; Score: 0.95
DE  Interaction: P38181; IntAct: EBI-11756,EBI-11730; Score: 0.59
DE  Interaction: P40368; IntAct: EBI-12331,EBI-11730; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-11730,EBI-12345; Score: 0.92
DE  Interaction: P47054; IntAct: EBI-25846,EBI-11730; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-12324,EBI-11730; Score: 0.44
DE  Interaction: P49686; IntAct: EBI-11730,EBI-12310; Score: 0.44
DE  Interaction: Self; IntAct: EBI-11730,EBI-11730; Score: 0.37
DE  Interaction: Q04491; IntAct: EBI-11730,EBI-16529; Score: 0.97
DE  Interaction: P55735; IntAct: EBI-1046596,EBI-11730; Score: 0.70
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-11730; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-11730; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-11730; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11730; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11730; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-17244,EBI-11730; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-11730,EBI-8591; Score: 0.35
DE  Interaction: P52891; IntAct: EBI-12337,EBI-11730; Score: 0.95
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11730; Score: 0.35
DE  Interaction: Q02199; IntAct: EBI-11730,EBI-12315; Score: 0.37
DE  Interaction: P10592; IntAct: EBI-11730,EBI-8603; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-11730,EBI-16940; Score: 0.81
DE  Interaction: P32582; IntAct: EBI-4167,EBI-11730; Score: 0.27
DE  Interaction: Q03718; IntAct: EBI-27756,EBI-11730; Score: 0.35
DE  Interaction: P53230; IntAct: EBI-23156,EBI-11730; Score: 0.35
DE  Interaction: Q06411; IntAct: EBI-576,EBI-11730; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-25778,EBI-11730; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11730; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11730; Score: 0.32
GO  GO:0000781;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0031080;
GO  GO:0016787;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0035392;
GO  GO:0006607;
GO  GO:0031081;
GO  GO:0016973;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0046822;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFNKSVNSGFTFGNQNTSTPTSTPAQPSSSLQFPQKSTGLFGNVNVNANTSTPSPSGGLFNANSNANSISQQPANNSLFG
SQ  NKPAQPSGGLFGATNNTTSKSAGSLFGNNNATANSTGSTGLFSGSNNIASSTQNGGLFGNSNNNNITSTTQNGGLFGKPT
SQ  TTPAGAGGLFGNSSSTNSTTGLFGSNNTQSSTGIFGQKPGASTTGGLFGNNGASFPRSGETTGTMSTNPYGINISNVPMA
SQ  VADMPRSITSSLSDVNGKSDAEPKPIENRRTYSFSSSVSGNAPLPLASQSSLVSRLSTRLKATQKSTSPNEIFSPSYSKP
SQ  WLNGAGSAPLVDDFFSSKMTSLAPNENSIFPQNGFNFLSSQRADLTELRKLKIDSNRSAAKKLKLLSGTPAITKKHMQDE
SQ  QDSSENEPIANADSVTNIDRKENRDNNLDNTYLNGKEQSNNLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAA
SQ  VSNFVIGRRGYGCITFQHDVDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKKT
SQ  KKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFSIWGLVNEEDAEIDEDDLSKQEDGGEQPLRKVRTL
SQ  AQSKPSDKEVILKTDGTFGTLSGKDDSIVEEKAYEPDLSDADFEGIEASPKLDVSKDWVEQLILAGSSLRSVFATSKEFD
SQ  GPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEI
SQ  EKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVS
SQ  QIGPEIEEKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSIDKNI
SQ  SKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKFSLPYDDPIGVIFQLYAANENTEKL
SQ  YKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMRE
SQ  ITLLRASTNDHILNRLKIPSQLIFNAQALKDRYEGNYLSEVQNLLLGSSYDLAEMAIVTSLGPRLLLSNNPVQNNELKTL
SQ  REILNEFPDSERDKWSVSINVFEVYLKLVLDNVETQETIDSLISGMKIFYDQYKHCREVAACCNVMSQEIVSKILEKNNP
SQ  SIGDSKAKLLELPLGQPEKAYLRGEFAQDLMKCTYKI
//
ID  P54265;
PN  Myotonin-protein kinase;
GN  Dmpk;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Sarcoplasmic reticulum membrane. Cell membrane. Note=Localizes to sarcoplasmic reticulum membranes of cardiomyocytes. [Isoform 1]: Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. [Isoform 8]: Mitochondrion outer membrane; Single-pass type IV membrane protein. [Isoform 5]: Cytoplasm, cytosol.
DR  UNIPROT: P54265;
DR  Pfam: PF08826;
DR  Pfam: PF00069;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. {ECO:0000269|PubMed:12612014, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:18729234, ECO:0000269|PubMed:21949239, ECO:0000269|PubMed:9294109}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0031307;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0033017;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0017020;
GO  GO:0004674;
GO  GO:0006874;
GO  GO:0035556;
GO  GO:0010657;
GO  GO:0006998;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0014853;
GO  GO:0008016;
GO  GO:0010830;
GO  GO:0014722;
GO  GO:0002028;
GO  GO:0051823;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAEVRLRQLQQLVLDPGFLGLEPLLDLLLGVHQELGASHLAQDKYVADFLQWVEPIAARLKEVRLQRDDFEILKVIGRG
SQ  AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVKGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLL
SQ  SKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLQPDGMVRSLVAVGTPDYLSP
SQ  EILQAVGGGPGAGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYAKIVHYREHLSLPLADTVVPEEAQDLIRGLLCP
SQ  AEIRLGRGGAGDFQKHPFFFGLDWEGLRDSVPPFTPDFEGATDTCNFDVVEDRLTAMVSGGGETLSDMQEDMPLGVRLPF
SQ  VGYSYCCMAFRDNQVPDPTPMELEALQLPVSDLQGLDLQPPVSPPDQVAEEADLVAVPAPVAEAETTVTLQQLQEALEEE
SQ  VLTRQSLSRELEAIRTANQNFSSQLQEAEVRNRDLEAHVRQLQERMEMLQAPGAAAITGVPSPRATDPPSHLDGPPAVAV
SQ  GQCPLVGPGPMHRRHLLLPARIPRPGLSEARCLLLFAAALAAAATLGCTGLVAYTGGLTPVWCFPGATFAP
//
ID  Q05166;
PN  Nucleoporin ASM4;
GN  ASM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q05166;
DR  UNIPROT: D6VRR0;
DR  UNIPROT: E9P903;
DR  UNIPROT: Q12456;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). May have a mitosis control function (By similarity). {ECO:0000250, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12265,EBI-3035; Score: 0.37
DE  Interaction: P32500; IntAct: EBI-11950,EBI-3035; Score: 0.67
DE  Interaction: P34077; IntAct: EBI-3035,EBI-12056; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-12345,EBI-3035; Score: 0.37
DE  Interaction: P47054; IntAct: EBI-25846,EBI-3035; Score: 0.55
DE  Interaction: P49686; IntAct: EBI-12310,EBI-3035; Score: 0.44
DE  Interaction: P52891; IntAct: EBI-12337,EBI-3035; Score: 0.37
DE  Interaction: Q02199; IntAct: EBI-12315,EBI-3035; Score: 0.37
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-3035; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-3035; Score: 0.44
DE  Interaction: Q03790; IntAct: EBI-27321,EBI-3035; Score: 0.37
DE  Interaction: Self; IntAct: EBI-3035,EBI-3035; Score: 0.37
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-3035; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-6679,EBI-3035; Score: 0.35
DE  Interaction: Q04947; IntAct: EBI-38020,EBI-3035; Score: 0.37
DE  Interaction: Q03718; IntAct: EBI-3035,EBI-27756; Score: 0.37
DE  Interaction: Q06344; IntAct: EBI-34121,EBI-3035; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-3035; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-3035; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGIRSGNNNGGFTNLTSQAPQTTQMFQSQSQLQPQPQPQPQQQQQHLQFNGSSDASSLRFGNSLSNTVNANNYSSNIGN
SQ  NSINNNNIKNGTNNISQHGQGNNPSWVNNPKKRFTPHTVIRRKTTKQNSSSDINQNDDSSSMNATMRNFSKQNQDSKHNE
SQ  RNKSAANNDINSLLSNFNDIPPSVTLQDWQREDEFGSIPSLTTQFVTDKYTAKKTNRSAYDSKNTPNVFDKDSYVRIANI
SQ  EQNHLDNNYNTAETNNKVHETSSKSSSLSAIIVFGYPESISNELIEHFSHFGHIMEDFQVLRLGRGINPNTFRIFHNHDT
SQ  GCDENDSTVNKSITLKGRNNESNNKKYPIFTGESWVKLTYNSPSSALRALQENGTIFRGSLIGCIPYSKNAVEQLAGCKI
SQ  DNVDDIGEFNVSMYQNSSTSSTSNTPSPPNVIITDGTLLREDDNTPAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQ
SQ  NAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL
//
ID  P36161;
PN  Nucleoporin NUP133;
GN  NUP133;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P36161;
DR  UNIPROT: D6VXE2;
DR  PDB: 3KFO;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre- ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:7862658, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9049242}.
DE  Reference Proteome: Yes;
DE  Interaction: P39523; IntAct: EBI-27256,EBI-11722; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11722; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-11722,EBI-8571; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11722; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-11722; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-11722; Score: 0.35
DE  Interaction: P48363; IntAct: EBI-13239,EBI-11722; Score: 0.35
DE  Interaction: P47079; IntAct: EBI-11722,EBI-19072; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-11722,EBI-8632; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-11722; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-11722; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-11722,EBI-8666; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-11722,EBI-8050; Score: 0.35
DE  Interaction: Q04432; IntAct: EBI-11722,EBI-35591; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-11722,EBI-11756; Score: 0.37
DE  Interaction: P52891; IntAct: EBI-12337,EBI-11722; Score: 0.55
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11722; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-11722,EBI-20254; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-11722,EBI-8637; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-11722,EBI-8591; Score: 0.35
DE  Interaction: P46673; IntAct: EBI-11722,EBI-12345; Score: 0.55
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11722; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11722; Score: 0.32
GO  GO:0000781;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0030466;
GO  GO:0006302;
GO  GO:0035392;
GO  GO:0031990;
GO  GO:0000122;
GO  GO:0031081;
GO  GO:0016973;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0000972;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSEKKVHLRLRKELSVPIAVVENESLAQLSYEEESQASLMDISMEQQQLRLHSHFDNSKVFTENNRYIVKTLQTDYSSGF
SQ  SNDDELNGYIDMQIGYGLVNDHKKVYIWNIHSTQKDTPYITVPFRSDDNDEIAVAPRCILTFPATMDESPLALNPNDQDE
SQ  TGGLIIIKGSKAIYYEDINSINNLNFKLSEKFSHELELPINSSGGEKCDLMLNCEPAGIVLSTNMGRIFFITIRNSMGKP
SQ  QLKLGKLLNKPFKLGIWSKIFNTNSSVVSLRNGPILGKGTRLVYITTNKGIFQTWQLSATNSHPTKLIDVNIYEAILESL
SQ  QDLYPFAHGTLKIWDSHPLQDESSQLFLSSIYDSSCNETYYILSTIIFDSSSNSFTIFSTYRLNTFMESITDTKFKPKIF
SQ  IPQMENANDTNEVTSILVMFPNAVVITQVNSKLDSSYSMRRKWEDIVSLRNDIDIIGSGYDSKSLYVLTKQMGVLQFFVK
SQ  ENEETNSKPEVGFVKSHVDQAVYFSKINANPIDFNLPPEISLDQESIEHDLKLTSEEIFHSNGKYIPPMLNTLGQHLSVR
SQ  KEFFQNFLTFVAKNFNYKISPELKLDLIEKFEILNCCIKFNSIIRQSDVLNDIWEKTLSNYNLTQNEHLTTKTVVINSPD
SQ  VFPVIFKQFLNHVVFVLFPSQNQNFKLNVTNLINLCFYDGILEEGEKTIRYELLELDPMEVDTSKLPWFINFDYLNCINQ
SQ  CFFDFTFACEEEGSLDSYKEGLLKIVKILYYQFNQFKIWINTQPVKSVNANDNFININNLYDDNHLDWNHVLCKVNLKEQ
SQ  CIQIAEFYKDLSGLVQTLQTLDQNDSTTVSLYETFFNEFPKEFSFTLFEYLIKHKKLNDLIFRFPQQHDVLIQFFQESAP
SQ  KYGHVAWIQQILDGSYADAMNTLKNITVDDSKKGESLSECELHLNVAKLSSLLVEKDNLDINTLRKIQYNLDTIDAEKNI
SQ  SNKLKKGEVQICKRFKNGSIREVFNILVEELKSTTVVNLSDLVELYSMLDDEESLFIPLRLLSVDGNLLNFEVKKFLNAL
SQ  VWRRIVLLNASNEGDKLLQHIVKRVFDEELPKNNDFPLPSVDLLCDKSLLTPEYISETYGRFPIDQNAIREEIYEEISQV
SQ  ETLNSDNSLEIKLHSTIGSVAKEKNYTINYETNTVEY
//
ID  F6ZDS4;
PN  Nucleoprotein TPR;
GN  Tpr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear- derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
DR  UNIPROT: F6ZDS4;
DR  UNIPROT: Q8R4A0;
DR  UNIPROT: Q921B9;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress- induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC- associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TPH6; IntAct: EBI-1811542,EBI-8317182; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-7280013,EBI-8317182; Score: 0.35
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0017056;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0035457;
GO  GO:0007094;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0006999;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0032880;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270};
SQ  MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQ
SQ  QVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLN
SQ  NQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKL
SQ  DELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTS
SQ  NEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQD
SQ  HLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQ
SQ  DQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDN
SQ  QRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETRER
SQ  EEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSS
SQ  TSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYE
SQ  MLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLL
SQ  AEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINL
SQ  HLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYR
SQ  AMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNE
SQ  VQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLE
SQ  CKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRRE
SQ  KEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERL
SQ  EQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTK
SQ  RIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFE
SQ  ELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELS
SQ  RLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRI
SQ  SRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNK
SQ  STPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQT
SQ  QATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDT
SQ  VEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTT
SQ  SSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGT
SQ  DPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQ
SQ  ELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDM
SQ  PQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLS
SQ  TTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTL
SQ  RQGVRGRQFNRQRGISHAMGGRGGINRGNIN
//
ID  Q9VCH5;
PN  Nuclear pore complex protein Nup96;
GN  Nup98;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus membrane {ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25197089}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. Nucleus {ECO:0000269|PubMed:28366641}. Note=Associates with transcriptionally active chromatin. {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:28366641}. [Nuclear pore complex protein Nup98]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}.
DR  UNIPROT: Q9VCH5;
DR  UNIPROT: B8A421;
DR  UNIPROT: Q6NP55;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Part of the nuclear pore complex (NPC) (PubMed:25197089). Required for MAD import as part of the Nup107-160 complex and required for nuclear export of Moe probably via its association with Rae1 (PubMed:20547758, PubMed:28554770). Plays a role in nuclear mRNA export (PubMed:28554770). Promotes cell antiviral response by upregulating FoxK-dependent antiviral gene transcription (PubMed:25197089, PubMed:25852164). In germline stem cells, involved in their maintenance and division together with the TGF-Beta and EGFR signaling pathways (PubMed:21949861). In larval lymph glands, has a role in the maintenance of hematopoiesis by regulating Pvr expression (PubMed:25201876). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089, ECO:0000269|PubMed:25201876, ECO:0000269|PubMed:25852164, ECO:0000269|PubMed:28554770}. [Nuclear pore complex protein Nup98]: Part of the nuclear pore complex (NPC) (PubMed:25310983). In the nucleoplasm, binds to transcriptionally active chromatin with a preference for regulatory regions; co-localizes with RNA polymerase II in a RNA-independent manner and before transition into transcription elongation (PubMed:20144760, PubMed:20144761, PubMed:28366641). Plays a role in the transcriptional memory process by stabilizing enhancer-promoter loops and by mediating anchoring of chromatin to the nuclear pore complex region (PubMed:28366641). During larval development, interacts with trx and MBD-R2 and regulates transcription of developmental genes including ecdysone-responsive genes such as Eip74 and E23 (PubMed:20144761, PubMed:25310983, PubMed:28366641). {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641}. [Nuclear pore complex protein Nup96]: Part of the nuclear pore complex (NPC). {ECO:0000269|PubMed:25310983}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-139789; Score: 0.35
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-139789; Score: 0.35
DE  Interaction: Q9VRM7; IntAct: EBI-154881,EBI-139789; Score: 0.37
DE  Interaction: Q9VYG2; IntAct: EBI-139789,EBI-75169; Score: 0.37
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005700;
GO  GO:0005704;
GO  GO:0005703;
GO  GO:0031490;
GO  GO:0008139;
GO  GO:1990841;
GO  GO:0003723;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0071390;
GO  GO:0034605;
GO  GO:0030718;
GO  GO:0035080;
GO  GO:0035167;
GO  GO:0036098;
GO  GO:0051028;
GO  GO:0043922;
GO  GO:0030838;
GO  GO:0002230;
GO  GO:0010628;
GO  GO:0045944;
GO  GO:0060261;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0046822;
GO  GO:0035075;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0071733;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52948};
SQ  MFGGAKPSFGATPAATSFGGFSGTTTTTPFGQSAFGKPAAPAFGNTSTFAAQPAQQSLFGAAATPAQPAGGLFGANTSTG
SQ  FGSTATAQPTAFGAFSQPQQTSNIFGSTQTAASTSLFGQSTLPAFGAAKPTMTAFGQTAAAQPTGSLFGQPAAATSTTGF
SQ  GGFGTSAPTTTNVFGSGTASAFAQPQATAVGASGVNTGTAVAKYQPTIGTDTLMKSGQANSVNTKQHCITAMKEFEGKSL
SQ  EELRLEDYMCGRKGPQAGNAPGAFGFGAQVTQPAQPASGGLFGSTAQPSTGLFGQTVTENKSMFGTTAFGQQPATNNAFG
SQ  AATQQNNFLQKPFGATTTTPFAAPAADASNPFGAKPAFGQGGSLFGQAPATSAAPAFGQTNTGFGGFGTTAGATQQSTLF
SQ  GATPAADPNKSAFGLGTAASAATTGFGFGAPATSTAGGGLFGNKPATSFAAPTFGATSTASTPFSNFGLNTSTAATGGGL
SQ  FNSGLNKPATSGFGGFGATSAAPLNFNAGNTGGSLFGNTAKPGGGLFGGGTTTLGGTGAAPTGGLFGGGTTSFGGVGGSL
SQ  GGGGFGMGTNNSLTGGIMGAQPTLGIMTPSHQPIHQQILARVTSPYGDSPIFKDLKLSSEADATRATNPAAQQAVLDLTS
SQ  NQYKISTSNNPAPMKVKALGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRP
SQ  KGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRK
SQ  PLDTYRPSSTVRLSVSTIPENPFEDQSSTIARRETFTSQQANESVLSNRSNEAEDSAANQSRLAIEAAAAEAADDESHPT
SQ  GIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIG
SQ  QGLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHFSKYGLGDSDEED
SQ  ELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGN
SQ  SDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASES
SQ  SSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPR
SQ  SIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVK
SQ  GNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLVSKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELV
SQ  DLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAV
SQ  FRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYND
SQ  AFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCS
SQ  PLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKA
SQ  VKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDIS
SQ  AKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALER
SQ  LPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
//
ID  P46673;
PN  Nucleoporin NUP85;
GN  NUP85;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P46673;
DR  UNIPROT: D6VWL3;
DR  PDB: 3EWE;
DR  PDB: 3F3F;
DR  PDB: 3F3G;
DR  PDB: 3F3P;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8816998, ECO:0000269|PubMed:9774696}.
DE  Reference Proteome: Yes;
DE  Interaction: P32499; IntAct: EBI-12401,EBI-12345; Score: 0.44
DE  Interaction: P35729; IntAct: EBI-12345,EBI-11713; Score: 0.95
DE  Interaction: P36161; IntAct: EBI-11722,EBI-12345; Score: 0.55
DE  Interaction: P40368; IntAct: EBI-12331,EBI-12345; Score: 0.55
DE  Interaction: P53011; IntAct: EBI-12345,EBI-16940; Score: 0.92
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-12345; Score: 0.59
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-12345; Score: 0.59
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12345; Score: 0.35
DE  Interaction: Q03790; IntAct: EBI-12345,EBI-27321; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-12345,EBI-3035; Score: 0.37
DE  Interaction: Q8WUM0; IntAct: EBI-295695,EBI-12345; Score: 0.51
DE  Interaction: P49687; IntAct: EBI-11730,EBI-12345; Score: 0.92
DE  Interaction: P52891; IntAct: EBI-12337,EBI-12345; Score: 0.73
DE  Interaction: P51862; IntAct: EBI-15702,EBI-12345; Score: 0.35
DE  Interaction: Q04491; IntAct: EBI-16529,EBI-12345; Score: 0.53
DE  Interaction: Q07622; IntAct: EBI-38674,EBI-12345; Score: 0.27
DE  Interaction: P32582; IntAct: EBI-4167,EBI-12345; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12345; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12345; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0031081;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0000055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MTIDDSNRLLMDVDQFDFLDDGTAQLSNNKTDEEEQLYKRDPVSGAILVPMTVNDQPIEKNGDKMPLKFKLGPLSYQNMA
SQ  FITAKDKYKLYPVRIPRLDTSKEFSAYVSGLFEIYRDLGDDRVFNVPTIGVVNSNFAKEHNATVNLAMEAILNELEVFIG
SQ  RVKDQDGRVNRFYELEESLTVLNCLRTMYFILDGQDVEENRSEFIESLLNWINRSDGEPDEEYIEQVFSVKDSTAGKKVF
SQ  ETQYFWKLLNQLVLRGLLSQAIGCIERSDLLPYLSDTCAVSFDAVSDSIELLKQYPKDSSSTFREWKNLVLKLSQAFGSS
SQ  ATDISGELRDYIEDFLLVIGGNQRKILQYSRTWYESFCGFLLYYIPSLELSAEYLQMSLEANVVDITNDWEQPCVDIISG
SQ  KIHSILPVMESLDSCTAAFTAMICEAKGLIENIFEGEKNSDDYSNEDNEMLEDLFSYRNGMASYMLNSFAFELCSLGDKE
SQ  LWPVAIGLIALSATGTRSAKKMVIAELLPHYPFVTNDDIEWMLSICVEWRLPEIAKEIYTTLGNQMLSAHNIIESIANFS
SQ  RAGKYELVKSYSWLLFEASCMEGQKLDDPVLNAIVSKNSPAEDDVIIPQDILDCVVTNSMRQTLAPYAVLSQFYELRDRE
SQ  DWGQALRLLLLLIEFPYLPKHYLVLLVAKFLYPIFLLDDKKLMDEDSVATVIEVIETKWDDADEKSSNLYETIIEADKSL
SQ  PSSMATLLKNLRKKLNFKLCQAFM
//
ID  Q8LLD0;
PN  Nuclear pore complex protein NUP96;
GN  NUP96;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16751346}; Peripheral membrane protein {ECO:0000269|PubMed:16751346}; Nucleoplasmic side {ECO:0000269|PubMed:16751346}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:21203492}.
DR  UNIPROT: Q8LLD0;
DR  UNIPROT: Q38941;
DR  UNIPROT: Q8LLD1;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Contributes to the transfer of mature mRNA from the nucleus to the cytosol. Required for both R gene-mediated and basal disease resistance. RNA export seems to play a critical role in stress responses and regulation of plant growth and development. {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:21203492, ECO:0000269|PubMed:22288649}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0015288;
GO  GO:0017056;
GO  GO:0006952;
GO  GO:0009870;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0009733;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16751346};
SQ  MTSLSIQPFPEISRMARDLDSRKKRRISLDGIAALCEHSKEIIDSLPMLNSPDYFLKPCINELVEREIESPDYCSRVPDF
SQ  TIGRIGYGYIRFLGNTDVRRLDLDHIVKFHRHEVIVYDDESSKPVVGEGLNKAAEVTLVVNIPDLTWGKQQVNHIAYKLK
SQ  QSTERQGATFISFDPDNGLWKFFVPHFSRFGLSDDEAEDIAMDDAPGLGDPVGLDGKKVADIDEEDQMETSELELSHSLP
SQ  AHLGLDPEKMKEMRMLMFPNEDEDESEDFREQTSHLMTSLTKRNVRPSQKIAQRNSHQDPPPVVRKTPLALLEYNPGNDK
SQ  SSPGSILMVQQNKNLAVRKSKTGGFELDISHVTPLTDNYSRNVVDAALFMGRSFRAGWGPNGVLFHTGKPICSSSSQMVL
SQ  SSVINKEKIAIDKVVWDRKGKVQKELIDSAFEAPLSLHKELNHVEEEVRFGSFSLKLQNVVTDRVVLSDICRSYIGIIEK
SQ  QLEVAGLSTSAKLFLMHQVMVWELIKVLFSERQSTERLMYAASDNEEDVMQDVKEDSAKIDTEALPLIRRAEFSCWLQES
SQ  VSHRVQEDVSDLNGSSYLEHLFFLLTGRELDSAVELAISKGDVRLACLLSQAGGSTVNRNDILQQLHLWRRNGLDFNFIE
SQ  KERIKLYELLAGNIHDALQDFTIDWKRFLGLLMWHHLPPDSSLPIIFRSYQLLLNQAKAPWPVPIYIDEGPADGFVSDNK
SQ  HSDILYYLMLLHSKEEEEFGFLQTMFSAFSSTDDPLDYHMIWHHRGILEAVGAFTSDDLHTLDMGFVAQLLSQGLCHWAI
SQ  YVVLHIPFREDHPYLHVTVIREILFQYCETWSSMESQRQFIKDLGIPSEWMHEALAVYYNYHGDFVKALDQFIECANWQR
SQ  AHSIFMTSVAHSLFLSANHSEIWRIATSMDDRKSEIENWDLGAGIYMSFYLLKSSLQEDADTMVELEPLDSTNESCRNFV
SQ  GRLNESLAVWGDRLPVEARVAYSKMAEEICDLLLSDLSKNPSRETQLTCFETAFDAPLPEDVRSTHLQDAVSLFSLYLSE
SQ  TGQISA
//
ID  Q5SNT2;
PN  Transmembrane protein 201;
GN  TMEM201;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 2]: Nucleus inner membrane {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}; Multi-pass membrane protein {ECO:0000269|PubMed:19494128}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19494128}. Note=The C- terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane in distinct micro-domains and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle. {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}.
DR  UNIPROT: Q5SNT2;
DR  UNIPROT: B9EH90;
DR  UNIPROT: Q5SNT3;
DR  Pfam: PF10476;
DR  Pfam: PF09779;
DR  DisGeNET: 199953;
DE  Function: Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery (PubMed:27541860). {ECO:0000250|UniProtKB:A2A8U2, ECO:0000305|PubMed:27541860}. [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle (PubMed:19494128). Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina (PubMed:21610090). {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}.
DE  Reference Proteome: Yes;
DE  Interaction: P57078; IntAct: EBI-4422308,EBI-10986145; Score: 0.35
DE  Interaction: P61021; IntAct: EBI-8320093,EBI-10986145; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-352936,EBI-10986145; Score: 0.35
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0000922;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0051642;
GO  GO:0010761;
GO  GO:0006998;
GO  GO:0030473;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTMVNCWFCNQDTLVPYGNRNCWDCPHCEQYNGFQENG
SQ  DYNKPIPAQYLEHLNHVVSSAPSLRDPSQPQQWVSSQVLLCKRCNHHQTTKIKQLAAFAPREEGRYDEEVEVYRHHLEQM
SQ  YKLCRPCQAAVEYYIKHQNRQLRALLLSHQFKRREADQTHAQNFSSAVKSPVQVILLRALAFLACAFLLTTALYGASGHF
SQ  APGTTVPLALPPGGNGSATPDNGTTPGAEGWRQLLGLLPEHMAEKLCEAWAFGQSHQTGVVALGLLTCLLAMLLAGRIRL
SQ  RRIDAFCTCLWALLLGLHLAEQHLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRFFPGDSAGLFPTS
SQ  PSLAIPHPSVGGSPASLFIPSPPSFLPLANQQLFRSPRRTSPSSLPGRLSRALSLGTIPSLTRADSGYLFSGSRPPSQVS
SQ  RSGEFPVSDYFSLLSGSCPSSPLPSPAPSVAGSVASSSGSLRHRRPLISPARLNLKGQKLLLFPSPPGEAPTTPSSSDEH
SQ  SPHNGSLFTMEPPHVPRKPPLQDVKHALDLRSKLERGSACSNRSIKKEDDSSQSSTCVVDTTTRGCSEEAATWRGRFGPS
SQ  LVRGLLAVSLAANALFTSVFLYQSLR
//
ID  O43567;
PN  E3 ubiquitin-protein ligase RNF13;
GN  RNF13;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23378536}. Golgi apparatus membrane. Late endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Lysosome membrane. Nucleus inner membrane {ECO:0000250}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250}.
DR  UNIPROT: O43567;
DR  UNIPROT: A6NC87;
DR  UNIPROT: B3KR12;
DR  UNIPROT: Q05D66;
DR  UNIPROT: Q6IBJ9;
DR  PDB: 5ZBU;
DR  PDB: 5ZC4;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DR  OMIM: 609247;
DR  OMIM: 618379;
DR  DisGeNET: 11342;
DE  Function: E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. Involved in apoptosis regulation. Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (PubMed:23378536, PubMed:30595371). {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:30595371}.
DE  Disease: Epileptic encephalopathy, early infantile, 73 (EIEE73) [MIM:618379]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE73 is an autosomal dominant form with onset at birth. {ECO:0000269|PubMed:30595371}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P51668; IntAct: EBI-743540,EBI-2129183; Score: 0.37
DE  Interaction: P62837; IntAct: EBI-347677,EBI-2129183; Score: 0.37
DE  Interaction: P61077; IntAct: EBI-348268,EBI-2129183; Score: 0.37
DE  Interaction: Q9Y2X8; IntAct: EBI-745527,EBI-2129183; Score: 0.37
DE  Interaction: P51965; IntAct: EBI-2129183,EBI-348546; Score: 0.37
DE  Interaction: Q969T4; IntAct: EBI-2129183,EBI-348496; Score: 0.37
DE  Interaction: P61088; IntAct: EBI-2129183,EBI-1052908; Score: 0.59
DE  Interaction: Q13404; IntAct: EBI-2129183,EBI-1050671; Score: 0.44
DE  Interaction: P22314; IntAct: EBI-2129183,EBI-709688; Score: 0.44
DE  Interaction: P42229; IntAct: EBI-749537,EBI-2129183; Score: 0.35
DE  Interaction: P48681; IntAct: EBI-10966836,EBI-2129183; Score: 0.35
DE  Interaction: P32241; IntAct: EBI-3917984,EBI-2129183; Score: 0.35
DE  Interaction: O00214; IntAct: EBI-740058,EBI-2129183; Score: 0.35
DE  Interaction: O00182-2; IntAct: EBI-12130578,EBI-2129183; Score: 0.35
DE  Interaction: Q86Y82; IntAct: EBI-2691717,EBI-2129183; Score: 0.35
DE  Interaction: Q9UEU0; IntAct: EBI-723716,EBI-2129183; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-7810230,EBI-2129183; Score: 0.35
DE  Interaction: Q9Y240; IntAct: EBI-3957044,EBI-2129183; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-2830042,EBI-2129183; Score: 0.35
DE  Interaction: Q9Y3E1; IntAct: EBI-2129183,EBI-2847459; Score: 0.35
DE  Interaction: Q9H6Y7; IntAct: EBI-2129183,EBI-1055214; Score: 0.35
DE  Interaction: Q92572; IntAct: EBI-2129183,EBI-4289921; Score: 0.35
DE  Interaction: P59780; IntAct: EBI-2129183,EBI-3914571; Score: 0.35
DE  Interaction: P56377; IntAct: EBI-2129183,EBI-1054374; Score: 0.35
DE  Interaction: P51798; IntAct: EBI-2129183,EBI-4402346; Score: 0.35
DE  Interaction: P29597; IntAct: EBI-2129183,EBI-1383454; Score: 0.35
DE  Interaction: P24468; IntAct: EBI-2129183,EBI-2795198; Score: 0.35
DE  Interaction: O60637; IntAct: EBI-2129183,EBI-750541; Score: 0.35
DE  Interaction: O43602-2; IntAct: EBI-2129183,EBI-14148644; Score: 0.35
DE  Interaction: O14617-2; IntAct: EBI-2129183,EBI-21566092; Score: 0.35
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSA
SQ  QSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
//
ID  P52948;
PN  Nuclear pore complex protein Nup96;
GN  NUP98;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:28221134}; Peripheral membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:28221134}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket (PubMed:11839768). Dissociates from the dissasembled NPC structure early during prophase of mitosis (PubMed:12802065). Colocalized with NUP153 and TPR to the nuclear basket of NPC (PubMed:11839768). Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body) (PubMed:11839768, PubMed:28221134). Remains localized to the nuclear membrane after poliovirus (PV) infection (PubMed:11106761). {ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:28221134}.
DR  UNIPROT: P52948;
DR  UNIPROT: Q8IUT2;
DR  UNIPROT: Q8WYB0;
DR  UNIPROT: Q96E54;
DR  UNIPROT: Q9H3Q4;
DR  UNIPROT: Q9NT02;
DR  UNIPROT: Q9UF57;
DR  UNIPROT: Q9UHX0;
DR  UNIPROT: Q9Y6J4;
DR  UNIPROT: Q9Y6J5;
DR  PDB: 1KO6;
DR  PDB: 2Q5X;
DR  PDB: 2Q5Y;
DR  PDB: 3MMY;
DR  PDB: 4OWR;
DR  PDB: 5A9Q;
DR  PDB: 6BZM;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DR  OMIM: 601021;
DR  DisGeNET: 4928;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283}.
DE  Disease: Note=A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro- megakaryocytic lineage. {ECO:0000269|PubMed:16028218}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-295727; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-295727; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-295727; Score: 0.35
DE  Interaction: Q9UKE5; IntAct: EBI-295727,EBI-1051794; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-395506,EBI-295727; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-295634,EBI-295727; Score: 0.35
DE  Interaction: Q9BY41; IntAct: EBI-6598095,EBI-295727; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-295727; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-295727,EBI-727707; Score: 0.37
DE  Interaction: Q93009; IntAct: EBI-302474,EBI-295727; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-295727; Score: 0.40
DE  Interaction: P24386; IntAct: EBI-2515129,EBI-295727; Score: 0.40
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-295727; Score: 0.56
DE  Interaction: Q6ZQH8; IntAct: EBI-2554037,EBI-295727; Score: 0.40
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-295727; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-447544,EBI-295727; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-2551981,EBI-295727; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-295727; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-295727; Score: 0.35
DE  Interaction: P45983; IntAct: EBI-286483,EBI-295727; Score: 0.35
DE  Interaction: Q6ZYL4; IntAct: EBI-6380438,EBI-295727; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-749627,EBI-295727; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-295727; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-295727; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-295727; Score: 0.35
DE  Interaction: P21698; IntAct: EBI-6148916,EBI-295727; Score: 0.35
DE  Interaction: Q8ZIC6; IntAct: EBI-2860508,EBI-295727; Score: 0.37
DE  Interaction: Q9H0J4; IntAct: EBI-1053637,EBI-295727; Score: 0.40
DE  Interaction: Q9H8S9; IntAct: EBI-748229,EBI-295727; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-295727; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-358900,EBI-295727; Score: 0.40
DE  Interaction: Q92623; IntAct: EBI-295727,EBI-20865549; Score: 0.40
DE  Interaction: P0DTC6; IntAct: EBI-25475897,EBI-295727; Score: 0.35
DE  Interaction: B2RTY4; IntAct: EBI-355398,EBI-295727; Score: 0.35
DE  Interaction: Q8IW93-1; IntAct: EBI-25410216,EBI-295727; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-295727; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-295695,EBI-295727; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-9032368; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-716392,EBI-9032368; Score: 0.40
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0043231;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044615;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:1990904;
GO  GO:0003729;
GO  GO:0008139;
GO  GO:1990841;
GO  GO:0003723;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0003713;
GO  GO:0005215;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0051292;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0048026;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFG
SQ  FGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGT
SQ  TIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGL
SQ  FSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFG
SQ  VTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLG
SQ  TNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFG
SQ  APQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRV
SQ  RPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKP
SQ  VDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDRE
SQ  EIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVV
SQ  VYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHF
SQ  SKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLD
SQ  TMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSK
SQ  TRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPR
SQ  EKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEK
SQ  LSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALW
SQ  GHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLAL
SQ  LLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTA
SQ  SISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPL
SQ  DYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWA
SQ  KETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERS
SQ  SLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLS
SQ  LHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL
//
ID  P46892;
PN  Cyclin-dependent kinase 11B;
GN  Cdk11b;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cytoplasm, perinuclear region.
DR  UNIPROT: P46892;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity- dependent manner. May act as a negative regulator of normal cell cycle progression. {ECO:0000250|UniProtKB:P21127}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0004674;
GO  GO:0001824;
GO  GO:0007049;
GO  GO:2001234;
GO  GO:0006468;
GO  GO:0001558;
GO  GO:0010468;
GO  GO:0007346;
GO  GO:0007088;
GO  GO:0050684;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MKSEKSRTTSWLFQSHEVTEILGRVKKNRKKLVKGLHRAGPPPEKNYLPDSPALSPIELKQELPKYLPALQGCRSVEEFQ
SQ  CLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPLTSIREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYV
SQ  EHDLKSLMETMKQPFLPGEVKTLMIQLLSGVKHLHDNWILHRDLKTSNLLLTHAGILKVGDFGLAREYGSPLKAYTPVVV
SQ  TLWYRAPELLLGAKEYSTACDMWSVGCIFGELLTQKPLFPGKSDIDQINKIFKDIGTPSEKIWPGYSELPAVKKMTFSEL
SQ  PYNNLRKRFGALLSDQGFDLMNKFLTYYPGRRINAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQCVKRGTSPKPPEGG
SQ  LGYSQLGDDDLKETGFHLTTTNDGAVSCRPWCSLLF
//
ID  Q6DVA0;
PN  LEM domain-containing protein 2;
GN  Lemd2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM). Localized exclusively to the nuclear envelope, giving rise to a typical rim-like staining of the nuclear periphery.
DR  UNIPROT: Q6DVA0;
DR  UNIPROT: Q8C4H8;
DR  UNIPROT: Q8R0N2;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Involved in nuclear structure organization (PubMed:16339967). Required for maintaining the integrity of the nuclear envelope (By similarity). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967}. Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT (PubMed:25790465). Required for myoblast differentiation involving regulation of ERK signaling (PubMed:17062158, PubMed:19720741). {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19720741, ECO:0000269|PubMed:25790465}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005783;
GO  GO:0005639;
GO  GO:0031965;
GO  GO:0060914;
GO  GO:0030514;
GO  GO:0043409;
GO  GO:0051898;
GO  GO:0022008;
GO  GO:0006998;
GO  GO:0071168;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPL
SQ  RARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPD
SQ  RHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVK
SQ  MGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANV
SQ  TSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWG
SQ  LLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNE
SQ  SRIQTESHRVAGEDMLVWRWTKPSSFSDSER
//
ID  O15504;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}. Nucleus membrane {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12228227}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:10358091}.
DR  UNIPROT: O15504;
DR  UNIPROT: A4D143;
DR  UNIPROT: B4DP42;
DR  UNIPROT: Q49AE7;
DR  UNIPROT: Q9BS49;
DR  PDB: 6B4F;
DR  PDB: 6B4I;
DR  PDB: 6B4J;
DR  PROSITE: PS50103;
DR  DisGeNET: 11097;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:16000379}. (Microbial infection) In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. {ECO:0000269|PubMed:12228227}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13158; IntAct: EBI-494804,EBI-2515057; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-2515057; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-727707,EBI-2515057; Score: 0.37
DE  Interaction: P24386; IntAct: EBI-2515129,EBI-2515057; Score: 0.40
DE  Interaction: Q7KZI7; IntAct: EBI-516560,EBI-2515057; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-2515057; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-2515057; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-2515057; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-2515057; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-2515057; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-2515057; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-286779,EBI-2515057; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-2811583,EBI-2515057; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-464743,EBI-2515057; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-11963218,EBI-2515057; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-2515057; Score: 0.35
DE  Interaction: A0A0F7RN56; IntAct: EBI-2821677,EBI-2515057; Score: 0.37
DE  Interaction: Q81KT8; IntAct: EBI-2515057,EBI-2809955; Score: 0.37
DE  Interaction: Q8IW93-1; IntAct: EBI-25410216,EBI-2515057; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-2515057,EBI-1046596; Score: 0.37
DE  Interaction: A5YKK6; IntAct: EBI-1222758,EBI-2515057; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-444173,EBI-2515057; Score: 0.35
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0003723;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYF
SQ  SSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRL
SQ  EYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSS
SQ  DNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLP
SQ  ASLATGPVRAPVAPAFGGGSSVAGFGSPGSHSHTAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQ
SQ  FQSKKFTLGKIPLKPPPLELLNV
//
ID  G5EEH9;
PN  Nuclear pore complex protein Nup96;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nuclear pore complex protein Nup98]: Cytoplasmic granule {ECO:0000269|PubMed:20335358}. Nucleus membrane {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:28122936}; Peripheral membrane protein {ECO:0000269|PubMed:20335358}; Nucleoplasmic side {ECO:0000269|PubMed:20335358}. Note=P granule localization dependent on nucleoporins npp-7, npp-8 and npp-9 which are involved in P granule integrity. {ECO:0000269|PubMed:20335358}. [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:20335358}. Nucleus envelope {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360}. Chromosome {ECO:0000269|PubMed:16950114}. Note=Requires mel-28 for chromatin association during early steps of nuclear pore complex assembly. {ECO:0000269|PubMed:16950114}.
DR  UNIPROT: G5EEH9;
DR  UNIPROT: D1MN48;
DR  UNIPROT: H2L014;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC) (PubMed:20335358, PubMed:28122936). Required for the nuclear import of hcp-4 during mitotic prophase, this step is essential for centrosome assembly and resolution (PubMed:28122936). Regulates nucleoporin npp-5 localization to the nuclear membrane during interphase and to kinetochores during metaphase (PubMed:22238360). Has a role in P granule integrity; may promote the 'liquid phase' of P granules by increasing the number of interacting RNA-protein complexes (PubMed:20335358). Binds nos-2 mRNA, probably indirectly, and promotes its accumulation in P granules (PubMed:20335358). {ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360, ECO:0000269|PubMed:28122936}.
DE  Reference Proteome: Yes;
DE  Interaction: O02333; IntAct: EBI-6455549,EBI-328275; Score: 0.37
DE  Interaction: G5ECG0; IntAct: EBI-6455549,EBI-320612; Score: 0.37
DE  Interaction: Q21443; IntAct: EBI-6455549,EBI-314110; Score: 0.37
DE  Interaction: P91457; IntAct: EBI-6455549,EBI-2004585; Score: 0.37
DE  Interaction: Q8TA83; IntAct: EBI-331999,EBI-6455549; Score: 0.37
DE  Interaction: P91400; IntAct: EBI-6455549,EBI-325226; Score: 0.37
DE  Interaction: P34402; IntAct: EBI-1570073,EBI-6455549; Score: 0.37
DE  Interaction: P90900; IntAct: EBI-6455549,EBI-322249; Score: 0.37
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0043186;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0051301;
GO  GO:0009792;
GO  GO:1990893;
GO  GO:0051028;
GO  GO:0031081;
GO  GO:0006997;
GO  GO:0030719;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0034501;
GO  GO:0090435;
GO  GO:0015031;
GO  GO:0006405;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:20335358};
SQ  MFGQNKSFGSSSFGGGSSGSGLFGQNNQNNQNKGLFGQPANNSGTTGLFGAAQNKPAGSIFGAASNTSSIFGSPQQPQNN
SQ  QSSLFGGGQNNANRSIFGSTSSAAPASSSLFGNNANNTGTSSIFGSNNNAPSGGGLFGASTVSGTTVKFEPPISSDTMMR
SQ  NGTTQTISTKHMCISAMSKYDGKSIEELRVEDYIANRKAPGTGTTSTGGGLFGASNTTNQAGSSGLFGSSNAQQKTSLFG
SQ  GASTSSPFGGNTSTANTGSSLFGNNNANTSAASGSLFGAKPAGSSLFGSTATTGASTFGQTTGSSLFGNQQPQTNTGGSL
SQ  FGNTQNQNQSGSLFGNTGTTGTGLFGQAQQQPQQQSSGFSFGGAPAATNAFGQPAAANTGGSLFGNTSTANTGSSLFGAK
SQ  PATSTGFTFGATQPTTTNAFGSTNTGGGLFGNNAAKPGGLFGNTTNTGTGGGLFGSQPQASSGGLFGSNTQATQPLNTGF
SQ  GNLAQPQIVMQQQVAPVPVIGVTADVLQMQANMKSLKSQLTNAPYGDSPLLKYNANPEIDGKSSPASTQRQLRFLAAKKG
SQ  ALSSSSDAQDSSFIIPPISKVMSDLSPAVTRSADVTKDLNYTSKEAPPSLARGLRNSTFNPNMSLTNRSVHESSALDKTI
SQ  DSALDASMNGTSNRLGVRGSVRRSNLKQLDMSLLADSSRVGRESRVADPDALPRISESERRQDVVTSTPAVDPVQAVIQR
SQ  HNDRNRDPPSLNLDTTCDEHTGLEPVSAATSSAASVVSTPSEETVNVNSAAGVKLTKPDYFSLPTINEMKNMIKNGRVVL
SQ  EDGLTVGRSSYGSVYWPGRVELKDVALDEIVVFRHREVTVYPNEEEKAPEGQELNRPAEVTLERVWYTDKKTKKEVRDVV
SQ  KLSEIGWREHLERQTIRMGAAFKDFRAETGSWVFRVDHFSKYGLADDDEPMDGSPPQQALQASSPLQVIDMNTSARDVNN
SQ  QVQRKKVHKATDAHHQEIILERVPAPAALGDVVPIIRRVNRKGLGGGTLDDSREESCIGNMTTEFNESGHDSIIEEGQQP
SQ  EKKPKLELLADLEYESSRFIRNLQELKVMPKANDPAHRFHGGGHSAKMIGYGKSKLIDIGIVKGRSSHVGWSETGCLVWS
SQ  AQPRHNQVLFGTIDRTSDVNENTLISMLDVNVHVSETSRKGPSSQSNSVKSSLTSNFVTYSDSYSSMFAKYIDVAQAGGY
SQ  DGHVSVWKLISALFPYERREGWSFERGEEIGEWLRTEAVKSVPDDRSADTSSNGVWNQLCLGDIDKAFQIAIDNNQPQLA
SQ  TMLQTSAVCPEATVHCFKAQLDNWKKCETLHLIPKETLKCYVLMSGLSHYEWDQDGKNHSINCLDGLNWIQALGLHVWYL
SQ  RAWTGLEESYDAYQKDVNAGRAASNRGDLPGELIKLACESQHSVEVVLDCAAGENPNDYFLQWHVWSLLYSVGYRTMSKT
SQ  SETRLHRNYSSQLEASSLSKYALFVLQHIDDDEERSTAVRSLLDRIARFTDNDMFDSISEQFDIPSEWIADAQFSIAKSV
SQ  DDSTQLFELAVAAKNYLEICRLFVDDIAPTAVVAGDHDALKAACAMVRPFENQIPEWGATGMVYTDYCRLINLIENDAEE
SQ  ELLQDVLESLETRLHAPTISKNSLQKLSLQTIGRVLFEYRADKNTLPEWTKLLGHRQMFKIFRDRSSWGIERFTIEFD
//
ID  P39685;
PN  Nucleoporin POM152;
GN  POM152;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: P39685;
DR  UNIPROT: D6VZV2;
DR  PDB: 5TVZ;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs. {ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9988776}.
DE  Reference Proteome: Yes;
DE  Interaction: P11484; IntAct: EBI-12739,EBI-8627; Score: 0.35
DE  Interaction: P39102; IntAct: EBI-12739,EBI-20578; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-19054,EBI-12739; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-12739; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-8666,EBI-12739; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-12739; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-25940,EBI-12739; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-12739,EBI-8591; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-6314,EBI-12739; Score: 0.40
DE  Interaction: Q12158; IntAct: EBI-16655,EBI-12739; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12739; Score: 0.40
GO  GO:0071944;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005641;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0043495;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEHRYNVFNDTPRGNHWMGSSVSGSPRPSYSSRPNVNTTRRFQYSDDEPAEKIRPLRSRSFKSTESNISDEKSRISERDS
SQ  KDRYINGDKKVDIYSLPLISTDVLEISKQRTFAVILFLIIQCYKIYDLVILKSGLPLSGLLFKNYRFNFISKYFIIDSFF
SQ  LYVLPSFNIPRLTFKPWVVYLQILAMLLLNIFISSDHEFVLISLIMTTWRKLYTKELSVTGSAINHHRIFDSSAHFKGAL
SQ  TIKILPENTAMFNPLHESYCLPMDTNLFKINSIDVPIRINSTEEIEYIELEYRDLYTNSVELRSLSKKDFKIIDNPKSFL
SQ  KKDQSVLKSHSNDFEEGSTIRYLAVTLQDIGFYQIKKIVDSKKLNLKIHQSHLVVPYCPIASITGTGSNDRCIGDSDNVS
SQ  FEIQGVPPMKLAYSKIVNGQTFSYVDSSLQPEYFESPLQSSKSKQSFTQGELNDLKWGRNQPVNINLDSSITQDGKFAYK
SQ  IDKITDGLGNVVDFTSLPEELKKRYDLSYNFNVHEVPRAALEERFDPKSPTKRSIAIVFEEIKNWISDIPYVISLSYTDA
SQ  QDKSKKIMNVTTDSLTKVLQADLPGSYNLEYIESKFCPGEIVGKSNVLVTMPVAPTMEVKSFPILDQCVGQVGLNFELSF
SQ  TGAPPYYYNTKIYKLENGERKLYDAKRYTSEGTRNRFSYSPPKEGNYEIVFDTVSNKLFTEPIKLEPVKEYTFKTSMRVK
SQ  PSASLKLHHDLKLCLGDHSSVPVALKGQGPFTLTYDIIETFSSKRKTFEIKEIKTNEYVIKTPVFTTGGDYILSLVSIKD
SQ  STGCVVGLSQPDAKIQVRRDIPSAAFNFFEPIKEAKIKHGSVTEIPLKLSGEGPFTVKFKHMDYDGNIVKEFENKFQNSY
SQ  KPALKVSKEGLYQLVDIRDSSCQGNVIYRNSLYKVSFLEKPKFAIQDNHHITKVTENLFSKEEVCQGMEGTVDLALFGSP
SQ  PFILEYDLMAPNGHISTKKIQVATKYASLKLPNQIPGEYITTIKAIFDGNYGESDIHFREHQSELIIKQTVHPIPDVAFA
SQ  DGGKTLRACAANVDQISFLEPINLKFLQGESPFSITFSVYHESTSRTDQYTIDNIDSENFSFEKLYEGMKLGNHAITIDS
SQ  VVDANGCVNSLISGPRNQILVSITDAPKIHILDPSTEYCVGDYVAYQLNGVAPFMIKYEFNGIPLKSKERSSQFVRLASE
SQ  PGIISITSLQDSSSQCIVDFTNPKLKSEFDDLSLNIHPIPSVTVSQGNYVTEDIREGDQAEVIFSFEGTPPFSLTYVRTE
SQ  ETDGKHGKRRSQVVETHKVTDIYSHEYKVITSLQGTYEAIEITDAYCFAKNDLFFNN
//
ID  F4HRT5;
PN  Protein CROWDED NUCLEI 1;
GN  CRWN1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}; Peripheral membrane protein {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:24667841}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (PubMed:24667841). Mostly localized at the nuclear periphery and, to a lesser extent, in the nucleoplasm (PubMed:17873096). Localized on the condensing chromatin during prometaphase to anaphase, but transferred from the decondensing chromatin to the reassembling nuclear envelope during early telophase. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}.
DR  UNIPROT: F4HRT5;
DR  UNIPROT: Q0WKV7;
DR  UNIPROT: Q8GZ88;
DR  UNIPROT: Q9FYH0;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:17873096, PubMed:24308514, PubMed:23396599, PubMed:24824484). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514, ECO:0000269|PubMed:24824484}.
DE  Reference Proteome: Yes;
GO  GO:0000789;
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEW
SQ  SSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANA
SQ  LVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQ
SQ  EGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKA
SQ  RELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALD
SQ  RKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTE
SQ  EERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERL
SQ  KKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLF
SQ  EEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSR
SQ  FLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKML
SQ  KLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVA
SQ  ADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRK
SQ  RGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEE
SQ  GIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKV
SQ  SIGKKLWTFLTT
//
ID  P42167;
PN  Thymopentin;
GN  TMPO;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Single-pass type II membrane protein. Note=Tightly associated with the nuclear lamina. [Isoform Zeta]: Cytoplasm {ECO:0000269|PubMed:18403046}.
DR  UNIPROT: P42167;
DR  UNIPROT: A2T926;
DR  UNIPROT: Q14861;
DR  Pfam: PF03020;
DR  Pfam: PF08198;
DR  PROSITE: PS50954;
DR  PROSITE: PS50955;
DR  OMIM: 188380;
DR  DisGeNET: 7112;
DE  Function: May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95. Thymopoietin (TP) and Thymopentin (TP5) may play a role in T- cell development and function. TP5 is an immunomodulating pentapeptide.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-2849976,EBI-455283; Score: 0.35
DE  Interaction: P00519; IntAct: EBI-375543,EBI-455283; Score: 0.40
DE  Interaction: P02545; IntAct: EBI-455283,EBI-351935; Score: 0.60
DE  Interaction: P20700; IntAct: EBI-455283,EBI-968218; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-455283,EBI-515315; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-455283,EBI-401755; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-455283,EBI-389883; Score: 0.40
DE  Interaction: Q00005; IntAct: EBI-1052159,EBI-455283; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-924724,EBI-455283; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-1001132,EBI-455283; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-6253193,EBI-455283; Score: 0.35
DE  Interaction: O14646-2; IntAct: EBI-455283,EBI-10961487; Score: 0.35
DE  Interaction: Q6IE81-2; IntAct: EBI-455283,EBI-10986812; Score: 0.35
DE  Interaction: Q7KZ85; IntAct: EBI-455283,EBI-2515547; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-455283,EBI-354213; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-455283,EBI-358348; Score: 0.35
DE  Interaction: Q9BXS6-2; IntAct: EBI-455283,EBI-10969852; Score: 0.35
DE  Interaction: P98160; IntAct: EBI-455283,EBI-947664; Score: 0.35
DE  Interaction: P62807; IntAct: EBI-455283,EBI-354552; Score: 0.35
DE  Interaction: O95696-2; IntAct: EBI-455283,EBI-11017508; Score: 0.35
DE  Interaction: P26640; IntAct: EBI-455283,EBI-355765; Score: 0.35
DE  Interaction: P49916; IntAct: EBI-455283,EBI-1753381; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-455283,EBI-954063; Score: 0.35
DE  Interaction: P17480; IntAct: EBI-455283,EBI-396235; Score: 0.35
DE  Interaction: Q10589; IntAct: EBI-455283,EBI-2476339; Score: 0.35
DE  Interaction: Q14978-2; IntAct: EBI-455283,EBI-396172; Score: 0.35
DE  Interaction: P46100; IntAct: EBI-455283,EBI-396461; Score: 0.35
DE  Interaction: P55197; IntAct: EBI-455283,EBI-1104952; Score: 0.35
DE  Interaction: B4E2V5; IntAct: EBI-455283,EBI-10977770; Score: 0.35
DE  Interaction: Q9P2E9; IntAct: EBI-455283,EBI-2371806; Score: 0.35
DE  Interaction: Q8WWQ0; IntAct: EBI-455283,EBI-722984; Score: 0.35
DE  Interaction: E7ESK6; IntAct: EBI-455283,EBI-10986808; Score: 0.35
DE  Interaction: Q9BW71; IntAct: EBI-455283,EBI-723624; Score: 0.35
DE  Interaction: P42766; IntAct: EBI-455283,EBI-356819; Score: 0.35
DE  Interaction: O95251; IntAct: EBI-455283,EBI-473199; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-455283,EBI-302589; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-455283,EBI-371922; Score: 0.35
DE  Interaction: Q8NHU3; IntAct: EBI-455283,EBI-10977284; Score: 0.35
DE  Interaction: Q969G5; IntAct: EBI-455283,EBI-3893101; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-2553509,EBI-455283; Score: 0.35
DE  Interaction: Q9Y587; IntAct: EBI-2115780,EBI-455283; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-455283; Score: 0.46
DE  Interaction: P68431; IntAct: EBI-79722,EBI-455283; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-455283; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-455283; Score: 0.35
DE  Interaction: P06821; IntAct: EBI-2547404,EBI-455283; Score: 0.35
DE  Interaction: P27105; IntAct: EBI-1211440,EBI-455283; Score: 0.56
DE  Interaction: Q8WZ60; IntAct: EBI-6426464,EBI-455283; Score: 0.56
DE  Interaction: Q8NBJ4; IntAct: EBI-712073,EBI-455283; Score: 0.56
DE  Interaction: Q99JP4; IntAct: EBI-2554171,EBI-455283; Score: 0.35
DE  Interaction: C5E524; IntAct: EBI-12561527,EBI-455283; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12562139,EBI-455283; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-2547442,EBI-455283; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0005521;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSG
SQ  AAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSST
SQ  PLPTISSSAENTRQNGSNDSDRYSDNEEDSKIELKLEKREPLKGRAKTPVTLKQRRVEHNQSYSQAGITETEWTSGSSKG
SQ  GPLQALTRESTRGSRRTPRKRVETSEHFRIDGPVISESTPIAETIMASSNESLVVNRVTGNFKHASPILPITEFSDIPRR
SQ  APKKPLTRAEVGEKTEERRVERDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYVPLADV
SQ  KSEKTKKGRSIPVWIKILLFVVVAVFLFLVYQAMETNQVNPFSNFLHVDPRKSN
//
ID  P35729;
PN  Nucleoporin NUP120;
GN  NUP120;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P35729;
DR  UNIPROT: D6VXN0;
DR  UNIPROT: P35730;
DR  PDB: 3F7F;
DR  PDB: 3H7N;
DR  PDB: 3HXR;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8557737, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-11713,EBI-11713; Score: 0.53
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-11713; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-11713; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11713; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-11713; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-11713,EBI-8627; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-13246,EBI-11713; Score: 0.35
DE  Interaction: P46673; IntAct: EBI-12345,EBI-11713; Score: 0.95
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11713; Score: 0.35
DE  Interaction: P49687; IntAct: EBI-11713,EBI-11730; Score: 0.95
DE  Interaction: P55735; IntAct: EBI-11713,EBI-1046596; Score: 0.40
DE  Interaction: P53011; IntAct: EBI-11713,EBI-16940; Score: 0.91
DE  Interaction: Q8WUM0; IntAct: EBI-11713,EBI-295695; Score: 0.40
DE  Interaction: P52891; IntAct: EBI-11713,EBI-12337; Score: 0.91
DE  Interaction: P47054; IntAct: EBI-25846,EBI-11713; Score: 0.37
DE  Interaction: Q04439; IntAct: EBI-11687,EBI-11713; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-11713,EBI-8603; Score: 0.35
DE  Interaction: Q06488; IntAct: EBI-11713,EBI-16198; Score: 0.35
DE  Interaction: Q04491; IntAct: EBI-16529,EBI-11713; Score: 0.88
DE  Interaction: P32582; IntAct: EBI-4167,EBI-11713; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11713; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11713; Score: 0.32
GO  GO:0000781;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0035392;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0000122;
GO  GO:0031081;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MACLSRIDANLLQYYEKPEPNNTVDLYVSNNSNNNGLKEGDKSISTPVPQPYGSEYSNCLLLSNSEYICYHFSSRSTLLT
SQ  FYPLSDAYHGKTINIHLPNASMNQRYTLTIQEVEQQLLVNVILKDGSFLTLQLPLSFLFSSANTLNGEWFHLQNPYDFTV
SQ  RVPHFLFYVSPQFSVVFLEDGGLLGLKKVDGVHYEPLLFNDNSYLKSLTRFFSRSSKSDYDSVISCKLFHERYLIVLTQN
SQ  CHLKIWDLTSFTLIQDYDMVSQSDSDPSHFRKVEAVGEYLSLYNNTLVTLLPLENGLFQMGTLLVDSSGILTYTFQNNIP
SQ  TNLSASAIWSIVDLVLTRPLELNVEASYLNLIVLWKSGTASKLQILNVNDESFKNYEWIESVNKSLVDLQSEHDLDIVTK
SQ  TGDVERGFCNLKSRYGTQIFERAQQILSENKIIMAHNEDEEYLANLETILRDVKTAFNEASSITLYGDEIILVNCFQPYN
SQ  HSLYKLNTTVENWFYNMHSETDGSELFKYLRTLNGFASTLSNDVLRSISKKFLDIITGELPDSMTTVEKFTDIFKNCLEN
SQ  QFEITNLKILFDELNSFDIPVVLNDLINNQMKPGIFWKKDFISAIKFDGFTSIISLESLHQLLSIHYRITLQVLLTFVLF
SQ  DLDTEIFGQHISTLLDLHYKQFLLLNLYRQDKCLLAEVLLKDSSEFSFGVKFFNYGQLIAYIDSLNSNVYNASITENSFF
SQ  MTFFRSYIIENTSHKNIRFFLENVECPFYLRHNEVQEFMFAMTLFSCGNFDQSYEIFQLHDYPEAINDKLPTFLEDLKSE
SQ  NYHGDSIWKDLLCTFTVPYRHSAFYYQLSLLFDRNNSQEFALKCISKSAEYSLKEIQIEELQDFKEKQHIHYLNLLIHFR
SQ  MFEEVLDVLRLGHECLSDTVRTNFLQLLLQEDIYSRDFFSTLLRLCNAHSDNGELYLRTVDIKIVDSILSQNLRSGDWEC
SQ  FKKLYCFRMLNKSERAAAEVLYQYILMQADLDVIRKRKCYLMVINVLSSFDSAYDQWILNGSKVVTLTDLRDELRGL
//
ID  Q8TEM1;
PN  Nuclear pore membrane glycoprotein 210;
GN  NUP210;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:2195063}. Nucleus membrane {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein {ECO:0000269|PubMed:2195063}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein {ECO:0000269|PubMed:2195063}.
DR  UNIPROT: Q8TEM1;
DR  UNIPROT: A6NN56;
DR  UNIPROT: O94980;
DR  UNIPROT: Q6NXG6;
DR  UNIPROT: Q8NBJ1;
DR  UNIPROT: Q9H6C8;
DR  UNIPROT: Q9UFP3;
DR  Pfam: PF02368;
DR  OMIM: 607703;
DR  DisGeNET: 23225;
DE  Function: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. {ECO:0000269|PubMed:14517331}.
DE  Reference Proteome: Yes;
DE  Interaction: P49790; IntAct: EBI-286779,EBI-372826; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-372826; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-372826; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-372826; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-372826; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-372826; Score: 0.35
DE  Interaction: J3KSN0; IntAct: EBI-21259955,EBI-372826; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21259559,EBI-372826; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-372826; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-372826; Score: 0.35
DE  Interaction: Q9NRD1; IntAct: EBI-3938499,EBI-372826; Score: 0.35
DE  Interaction: Q96JQ5; IntAct: EBI-12820341,EBI-372826; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-372826; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-712001,EBI-372826; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-372826; Score: 0.35
DE  Interaction: P02866; IntAct: EBI-2905940,EBI-372826; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-372826; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11333674,EBI-372826; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-1059012,EBI-372826; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-372826; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-372826; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-80168,EBI-372826; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-372826; Score: 0.35
DE  Interaction: O94955; IntAct: EBI-2367123,EBI-372826; Score: 0.35
DE  Interaction: Q9UK39; IntAct: EBI-5655962,EBI-372826; Score: 0.40
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-372826; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-372826; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-372826; Score: 0.35
DE  Interaction: Q81S14; IntAct: EBI-2811794,EBI-372826; Score: 0.37
DE  Interaction: Q81X77; IntAct: EBI-372826,EBI-2810439; Score: 0.37
DE  Interaction: Q9NR11; IntAct: EBI-372826,EBI-3916142; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475862,EBI-372826; Score: 0.35
DE  Interaction: Q9NQT4; IntAct: EBI-372826,EBI-371876; Score: 0.37
GO  GO:0005789;
GO  GO:0043657;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0016925;
GO  GO:0065003;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARGRGLLLLTLSVLLAAGPSAAAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWLSTRPEVASIEPLGLDEQQCSQKA
SQ  VVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHDIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFEWT
SQ  IVKDSEADRFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLIL
SQ  ENILLNPAYDVYLMVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPGPEGDPARPVAVLAQDTSMVTALQLGQSSL
SQ  VLGHRSIRMQGASRLPNSTIYVVEPGYLGFTVHPGDRWVLETGRLYEITIEVFDKFSNKVYVSDNIRIETVLPAEFFEVL
SQ  SSSQNGSYHRIRALKRGQTAIDAALTSVVDQDGGVHILQVPVWNQQEVEIHIPITLYPSILTFPWQPKTGAYQYTIRAHG
SQ  GSGNFSWSSSSHLVATVTVKGVMTTGSDIGFSVIQAHDVQNPLHFGEMKVYVIEPHSMEFAPCQVEARVGQALELPLRIS
SQ  GLMPGGASEVVTLSDCSHFDLAVEVENQGVFQPLPGRLPPGSEHCSGIRVKAEAQGSTTLLVSYRHGHVHLSAKITIAAY
SQ  LPLKAVDPSSVALVTLGSSKEMLFEGGPRPWILEPSKFFQNVTAEDTDSIGLALFAPHSSRNYQQHWILVTCQALGEQVI
SQ  ALSVGNKPSLTNPFPAVEPAVVKFVCAPPSRLTLAPVYTSPQLDMSCPLLQQNKQVVPVSSHRNPRLDLAAYDQEGRRFD
SQ  NFSSLSIQWESTRPVLASIEPELPMQLVSQDDESGQKKLHGLQAILVHEASGTTAITATATGYQESHLSSARTKQPHDPL
SQ  VPLSASIELILVEDVRVSPEEVTIYNHPGIQAELRIREGSGYFFLNTSTADVVKVAYQEARGVAMVHPLLPGSSTIMIHD
SQ  LCLVFPAPAKAVVYVSDIQELYIRVVDKVEIGKTVKAYVRVLDLHKKPFLAKYFPFMDLKLRAASPIITLVALDEALDNY
SQ  TITFLIRGVAIGQTSLTASVTNKAGQRINSAPQQIEVFPPFRLMPRKVTLLIGATMQVTSEGGPQPQSNILFSISNESVA
SQ  LVSAAGLVQGLAIGNGTVSGLVQAVDAETGKVVIISQDLVQVEVLLLRAVRIRAPIMRMRTGTQMPIYVTGITNHQNPFS
SQ  FGNAVPGLTFHWSVTKRDVLDLRGRHHEASIRLPSQYNFAMNVLGRVKGRTGLRVVVKAVDPTSGQLYGLARELSDEIQV
SQ  QVFEKLQLLNPEIEAEQILMSPNSYIKLQTNRDGAASLSYRVLDGPEKVPVVHVDEKGFLASGSMIGTSTIEVIAQEPFG
SQ  ANQTIIVAVKVSPVSYLRVSMSPVLHTQNKEALVAVPLGMTVTFTVHFHDNSGDVFHAHSSVLNFATNRDDFVQIGKGPT
SQ  NNTCVVRTVSVGLTLLRVWDAEHPGLSDFMPLPVLQAISPELSGAMVVGDVLCLATVLTSLEGLSGTWSSSANSILHIDP
SQ  KTGVAVARAVGSVTVYYEVAGHLRTYKEVVVSVPQRIMARHLHPIQTSFQEATASKVIVAVGDRSSNLRGECTPTQREVI
SQ  QALHPETLISCQSQFKPAVFDFPSQDVFTVEPQFDTALGQYFCSITMHRLTDKQRKHLSMKKTALVVSASLSSSHFSTEQ
SQ  VGAEVPFSPGLFADQAEILLSNHYTSSEIRVFGAPEVLENLEVKSGSPAVLAFAKEKSFGWPSFITYTVGVLDPAAGSQG
SQ  PLSTTLTFSSPVTNQAIAIPVTVAFVVDRRGPGPYGASLFQHFLDSYQVMFFTLFALLAGTAVMIIAYHTVCTPRDLAVP
SQ  AALTPRASPGHSPHYFAASSPTSPNALPPARKASPPSGLWSPAYASH
//
ID  P70582;
PN  Nuclear pore complex protein Nup54;
GN  Nup54;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Cytoplasmic side {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Nucleoplasmic side {ECO:0000269|PubMed:8707840}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter.
DR  UNIPROT: P70582;
DR  PDB: 3T97;
DR  PDB: 3T98;
DR  PDB: 4J3H;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000269|PubMed:8707840}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0036228;
GO  GO:0006605;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8707840};
SQ  MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTSTGTGTGLGTG
SQ  LGTGLGFGGFNTQQQQQQQQTSLGGLFSQPAQAPAQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNN
SQ  NIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQ
SQ  TEVVIYIVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNP
SQ  DSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMDLSHRTLQVLIKQEIQR
SQ  KSGYAIQAEEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHL
SQ  ISIIKDDLEDIKLVEHGLNETIHSRGGVFS
//
ID  Q02630;
PN  Nucleoporin NUP116/NSP116;
GN  NUP116;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q02630;
DR  UNIPROT: D6VZM2;
DR  PDB: 1O6P;
DR  PDB: 2AIV;
DR  PDB: 3PBP;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. By binding ATPase AFG2, promotes AFG2-mediated release of shuttling protein RLP24 from pre-60S ribosomal particles (PubMed:23185031). {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9463388, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-11703,EBI-12265; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-11703,EBI-20589; Score: 0.37
DE  Interaction: P34077; IntAct: EBI-11703,EBI-12056; Score: 0.44
DE  Interaction: P35729; IntAct: EBI-11703,EBI-11713; Score: 0.44
DE  Interaction: P38181; IntAct: EBI-11703,EBI-11756; Score: 0.44
DE  Interaction: P40066; IntAct: EBI-22648,EBI-11703; Score: 0.61
DE  Interaction: P40368; IntAct: EBI-12331,EBI-11703; Score: 0.67
DE  Interaction: P46673; IntAct: EBI-11703,EBI-12345; Score: 0.59
DE  Interaction: P47054; IntAct: EBI-11703,EBI-25846; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-12324,EBI-11703; Score: 0.53
DE  Interaction: P49686; IntAct: EBI-12310,EBI-11703; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-11703,EBI-11730; Score: 0.44
DE  Interaction: P52593; IntAct: EBI-11763,EBI-11703; Score: 0.37
DE  Interaction: P52891; IntAct: EBI-11703,EBI-12337; Score: 0.44
DE  Interaction: P53011; IntAct: EBI-11703,EBI-16940; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-11703,EBI-12315; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-11703; Score: 0.65
DE  Interaction: Self; IntAct: EBI-11703,EBI-11703; Score: 0.53
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-11703; Score: 0.67
DE  Interaction: Q05166; IntAct: EBI-11703,EBI-3035; Score: 0.44
DE  Interaction: Q04934; IntAct: EBI-35255,EBI-11703; Score: 0.37
DE  Interaction: P53038; IntAct: EBI-19106,EBI-11703; Score: 0.37
DE  Interaction: P40054; IntAct: EBI-16961,EBI-11703; Score: 0.37
DE  Interaction: P45819; IntAct: EBI-24068,EBI-11703; Score: 0.37
DE  Interaction: P39723; IntAct: EBI-20675,EBI-11703; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-11703; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-11703; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-19863,EBI-11703; Score: 0.35
DE  Interaction: Q12443; IntAct: EBI-11703,EBI-32591; Score: 0.37
DE  Interaction: P32589; IntAct: EBI-11703,EBI-8648; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-11703,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-11703,EBI-8603; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11703; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11703; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0051117;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006999;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGVSRGAFPSATTQPFGSTGSTFGGQQQQQQPVANTSAFGLSQQTNTTQAPAFGNFGNQTSNSPFGMSGSTTANGTPFG
SQ  QSQLTNNNASGSIFGGMGNNTALSAGSASVVPNSTAGTSIKPFTTFEEKDPTTGVINVFQSITCMPEYRNFSFEELRFQD
SQ  YQAGRKFGTSQNGTGTTFNNPQGTTNTGFGIMGNNNSTTSATTGGLFGQKPATGMFGTGTGSGGGFGSGATNSTGLFGSS
SQ  TNLSGNSAFGANKPATSGGLFGNTTNNPTNGTNNTGLFGQQNSNTNGGLFGQQQNSFGANNVSNGGAFGQVNRGAFPQQQ
SQ  TQQGSGGIFGQSNANANGGAFGQQQGTGALFGAKPASGGLFGQSAGSKAFGMNTNPTGTTGGLFGQTNQQQSGGGLFGQQ
SQ  QNSNAGGLFGQNNQSQNQSGLFGQQNSSNAFGQPQQQGGLFGSKPAGGLFGQQQGASTFASGNAQNNSIFGQNNQQQQST
SQ  GGLFGQQNNQSQSQPGGLFGQTNQNNNQPFGQNGLQQPQQNNSLFGAKPTGFGNTSLFSNSTTNQSNGISGNNLQQQSGG
SQ  LFQNKQQPASGGLFGSKPSNTVGGGLFGNNQVANQNNPASTSGGLFGSKPATGSLFGGTNSTAPNASSGGIFGSNNASNT
SQ  AATTNSTGLFGNKPVGAGASTSAGGLFGNNNNSSLNNSNGSTGLFGSNNTSQSTNAGGLFQNNTSTNTSGGGLFSQPSQS
SQ  MAQSQNALQQQQQQQRLQIQNNNPYGTNELFSKATVTNTVSYPIQPSATKIKADERKKASLTNAYKMIPKTLFTAKLKTN
SQ  NSVMDKAQIKVDPKLSISIDKKNNQIAISNQQEENLDESILKASELLFNPDKRSFKNLINNRKMLIASEEKNNGSQNNDM
SQ  NFKSKSEEQETILGKPKMDEKETANGGERMVLSSKNDGEDSATKHHSRNMDEENKENVADLQKQEYSEDDKKAVFADVAE
SQ  KDASFINENYYISPSLDTLSSYSLLQLRKVPHLVVGHKSYGKIEFLEPVDLAGIPLTSLGGVIITFEPKTCIIYANLPNR
SQ  PKRGEGINVRARITCFNCYPVDKSTRKPIKDPNHQLVKRHIERLKKNPNSKFESYDADSGTYVFIVNHAAEQT
//
ID  Q8IVL0;
PN  Neuron navigator 3;
GN  NAV3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}.
DR  UNIPROT: Q8IVL0;
DR  UNIPROT: Q8NFW7;
DR  UNIPROT: Q9Y2E7;
DR  Pfam: PF00004;
DR  Pfam: PF00307;
DR  PROSITE: PS50021;
DR  OMIM: 611629;
DR  DisGeNET: 89795;
DE  Function: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:16166283}.
DE  Disease: Note=A chromosomal aberration disrupting NAV3 has been found in patients with Sezary syndrome (PubMed:16166283). Translocation t(12;18)(q21;q21.2) (PubMed:16166283). {ECO:0000269|PubMed:16166283}.
DE  Reference Proteome: Yes;
DE  Interaction: P25054; IntAct: EBI-727707,EBI-2795733; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-447544,EBI-2795733; Score: 0.35
DE  Interaction: P84101; IntAct: EBI-720132,EBI-2795733; Score: 0.40
GO  GO:0005640;
GO  GO:0005524;
GO  GO:0008017;
GO  GO:0030336;
GO  GO:0032703;
GO  GO:0007026;
GO  GO:0007399;
GO  GO:0022008;
GO  GO:1905929;
GO  GO:0031116;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPVLGVASKLRQPAVGSKPVHTALPIPNLGTTGSQHCSSRPLELTETESSMLSCQLALKSTCEFGEKKPLQGKAKEKEDS
SQ  KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS
SQ  AEEIRNGNLKAILGLFFSLSRYKQQQHHQQQYYQSLVELQQRVTHASPPSEASQAKTQQDMQSSLAARYATQSNHSGIAT
SQ  SQKKPTRLPGPSRVPAAGSSSKVQGASNLNRRSQSFNSIDKNKPPNYANGNEKDSSKGPQSSSGVNGNVQPPSTAGQPPA
SQ  SAIPSPSASKPWRSKSMNVKHSATSTMLTVKQSSTATSPTPSSDRLKPPVSEGVKTAPSGQKSMLEKFKLVNARTALRPP
SQ  QPPSSGPSDGGKDDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKLAPPKAGSKNLSNKKSLLQPKEKEEKNRDKNKVCT
SQ  EKPVKEEKDQVTEMAPKKTSKIASLIPKGSKTTAAKKESLIPSSSGIPKPGSKVPTVKQTISPGSTASKESEKFRTTKGS
SQ  PSQSLSKPITMEKASASSCPAPLEGREAGQASPSGSCTMTVAQSSGQSTGNGAVQLPQQQQHSHPNTATVAPFIYRAHSE
SQ  NEGTALPSADSCTSPTKMDLSYSKTAKQCLEEISGEDPETRRMRTVKNIADLRQNLEETMSSLRGTQISHSTLETTFDST
SQ  VTTEVNGRTIPNLTSRPTPMTWRLGQACPRLQAGDAPSLGAGYPRSGTSRFIHTDPSRFMYTTPLRRAAVSRLGNMSQID
SQ  MSEKASSDLDMSSEVDVGGYMSDGDILGKSLRTDDINSGYMTDGGLNLYTRSLNRIPDTATSRDIIQRGVHDVTVDADSW
SQ  DDSSSVSSGLSDTLDNISTDDLNTTSSVSSYSNITVPSRKNTQLRTDSEKRSTTDETWDSPEELKKPEEDFDSHGDAGGK
SQ  WKTVSSGLPEDPEKAGQKASLSVSQTGSWRRGMSAQGGAPSRQKAGTSALKTPGKTDDAKASEKGKAPLKGSSLQRSPSD
SQ  AGKSSGDEGKKPPSGIGRSTATSSFGFKKPSGVGSSAMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQ
SQ  DDVVLHVSSKTTLQYRSLPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKE
SQ  KEKVAVSDSESVSLSGSPKSSPTSASACGAQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGVKSSSVMPSPST
SQ  TLARQGSLESPSSGTGSMGSAGGLSGSSSPLFNKPSDLTTDVISLSHSLASSPASVHSFTSGGLVWAANMSSSSAGSKDT
SQ  PSYQSMTSLHTSSESIDLPLSHHGSLSGLTTGTHEVQSLLMRTGSVRSTLSESMQLDRNTLPKKGLRYTPSSRQANQEEG
SQ  KEWLRSHSTGGLQDTGNQSPLVSPSAMSSSAAGKYHFSNLVSPTNLSQFNLPGPSMMRSNSIPAQDSSFDLYDDSQLCGS
SQ  ATSLEERPRAISHSGSFRDSMEEVHGSSLSLVSSTSSLYSTAEEKAHSEQIHKLRRELVASQEKVATLTSQLSANAHLVA
SQ  AFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAIQGALNGPDHPPKDLRIRRQHSSESVSSINSAT
SQ  SHSSIGSGNDADSKKKKKKNWVNSRGSELRSSFKQAFGKKKSTKPPSSHSDIEELTDSSLPASPKLPHNAGDCGSASMKP
SQ  SQSASASPLVWPPKKRQNGPVIYKHRSRICECTEAEAEIILQLKSELREKELKLTDIRLEALSSAHHLDQIREAMNRMQN
SQ  EIEILKAENDRLKAETGNTAKPTRPPSESSSSTSSSSSRQSLGLSLNNLNITEAVSSDILLDDAGDATGHKDGRSVKIIV
SQ  SISKGYGRAKDQKSQAYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRIDTSTSLGLSSDCIASYCIGDLIRSHNLEVPEL
SQ  LPCGYLVGDNNIITVNLKGVEENSLDSFVFDTLIPKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVITKSGRK
SQ  KTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGVELPVVIILDNLHHVGSLSDIFNGFLNCKYNKCPYIIGTMNQGV
SQ  SSSPNLELHHNFRWVLCANHTEPVKGFLGRYLRRKLIEIEIERNIRNNDLVKIIDWIPKTWHHLNSFLETHSSSDVTIGP
SQ  RLFLPCPMDVEGSRVWFMDLWNYSLVPYILEAVREGLQMYGKRTPWEDPSKWVLDTYPWSSATLPQESPALLQLRPEDVG
SQ  YESCTSTKEATTSKHIPQTDTEGDPLMNMLMKLQEAANYSSTQSCDSESTSHHEDILDSSLESTL
//
ID  P48837;
PN  Nucleoporin NUP57;
GN  NUP57;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P48837;
DR  UNIPROT: D6VUQ0;
DR  Pfam: PF13634;
DR  Pfam: PF13874;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9725905}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12265,EBI-12324; Score: 0.81
DE  Interaction: P34077; IntAct: EBI-12056,EBI-12324; Score: 0.84
DE  Interaction: P37198; IntAct: EBI-347978,EBI-12324; Score: 0.56
DE  Interaction: P38181; IntAct: EBI-11756,EBI-12324; Score: 0.44
DE  Interaction: P40066; IntAct: EBI-22648,EBI-12324; Score: 0.27
DE  Interaction: Self; IntAct: EBI-12324,EBI-12324; Score: 0.65
DE  Interaction: Q02630; IntAct: EBI-12324,EBI-11703; Score: 0.53
DE  Interaction: Q02629; IntAct: EBI-12324,EBI-11698; Score: 0.53
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-12324; Score: 0.44
DE  Interaction: P49686; IntAct: EBI-12310,EBI-12324; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-12324,EBI-11730; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-12324,EBI-12315; Score: 0.90
DE  Interaction: P52891; IntAct: EBI-12324,EBI-12337; Score: 0.44
DE  Interaction: Q06410; IntAct: EBI-30856,EBI-12324; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-8591,EBI-12324; Score: 0.53
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12324; Score: 0.35
DE  Interaction: Q02959; IntAct: EBI-8484,EBI-12324; Score: 0.35
DE  Interaction: P38265; IntAct: EBI-21579,EBI-12324; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-8611,EBI-12324; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12324,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12324,EBI-8603; Score: 0.53
DE  Interaction: P32589; IntAct: EBI-12324,EBI-8648; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-12324; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12324; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-12324; Score: 0.35
DE  Interaction: Q6WNK7; IntAct: EBI-1251050,EBI-12324; Score: 0.35
DE  Interaction: P53165; IntAct: EBI-23812,EBI-12324; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-12324,EBI-394607; Score: 0.56
DE  Interaction: P19012; IntAct: EBI-12324,EBI-739566; Score: 0.56
DE  Interaction: P43365; IntAct: EBI-12324,EBI-749530; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-12324; Score: 0.56
DE  Interaction: Q7Z6G3-2; IntAct: EBI-12324,EBI-10172876; Score: 0.56
DE  Interaction: P13196; IntAct: EBI-12324,EBI-3905054; Score: 0.56
DE  Interaction: Q5JR59-3; IntAct: EBI-12324,EBI-11522433; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-739895,EBI-12324; Score: 0.56
DE  Interaction: P02829; IntAct: EBI-12324,EBI-8659; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12324; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12324; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006606;
GO  GO:0036228;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGFSGSNNGFGNKPAGSTGFSFGQNNNNTNTQPSASGFGFGGSQPNSGTATTGGFGANQATNTFGSNQQSSTGGGLFGN
SQ  KPALGSLGSSSTTASGTTATGTGLFGQQTAQPQQSTIGGGLFGNKPTTTTGGLFGNSAQNNSTTSGGLFGNKVGSTGSLM
SQ  GGNSTQNTSNMNAGGLFGAKPQNTTATTGGLFGSKPQGSTTNGGLFGSGTQNNNTLGGGGLFGQSQQPQTNTAPGLGNTV
SQ  STQPSFAWSKPSTGSNLQQQQQQQIQVPLQQTQAIAQQQQLSNYPQQIQEQVLKCKESWDPNTTKTKLRAFVYNKVNETE
SQ  AILYTKPGHVLQEEWDQAMEKKPSPQTIPIQIYGFEGLNQRNQVQTENVAQARIILNHILEKSTQLQQKHELDTASRILK
SQ  AQSRNVEIEKRILKLGTQLATLKNRGLPLGIAEEKMWSQFQTLLQRSEDPAGLGKTNELWARLAILKERAKNISSQLDSK
SQ  LMVFNDDTKNQDSMSKGTGEESNDRINKIVEILTNQQRGITYLNEVLEKDAAIVKKYKNKT
//
ID  P40064;
PN  Nucleoporin NUP157;
GN  NUP157;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P40064;
DR  UNIPROT: D3DM12;
DR  PDB: 4MHC;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000269|PubMed:12473689}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-11740,EBI-10420; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-11740,EBI-11756; Score: 0.37
DE  Interaction: P11978; IntAct: EBI-11740,EBI-17237; Score: 0.40
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11740; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-11740,EBI-8648; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-11740; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-11740,EBI-8591; Score: 0.35
DE  Interaction: Q03790; IntAct: EBI-27321,EBI-11740; Score: 0.55
DE  Interaction: P39081; IntAct: EBI-11740,EBI-12980; Score: 0.37
DE  Interaction: P47007; IntAct: EBI-11740,EBI-26105; Score: 0.37
DE  Interaction: Q08817; IntAct: EBI-11740,EBI-30849; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11740; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11740; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0003677;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHV
SQ  KISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIK
SQ  SDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDR
SQ  THELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPS
SQ  IPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLS
SQ  NRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDT
SQ  GPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTAL
SQ  LDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEA
SQ  CSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLF
SQ  SQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALIL
SQ  LINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTS
SQ  ADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQ
SQ  PKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLK
SQ  KRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALAS
SQ  SDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVL
SQ  PLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTD
SQ  VVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGS
SQ  IAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK
//
ID  Q8TC36;
PN  SUN domain-containing protein 5;
GN  SUN5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000305|PubMed:27640305}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9DA32}. Golgi apparatus {ECO:0000250|UniProtKB:Q9DA32}. Note=During spermiogenesis, traffics through the Golgi apparatus before reaching the round spermatid inner membrane of the nuclear envelope and later migrates to the coupling apparatus of the sperm during sperm head elongation and differentiation. In mature spermatozoa, is localized to the coupling apparatus of the sperm head and tail in the implementation fossa. {ECO:0000305|PubMed:27640305}.
DR  UNIPROT: Q8TC36;
DR  UNIPROT: A6NJ82;
DR  UNIPROT: Q5T9R0;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 613942;
DR  OMIM: 617187;
DR  DisGeNET: 140732;
DE  Function: Plays an essential role in anchoring sperm head to the tail. Is responsible for the attachment of the coupling apparatus to the sperm nuclear envelope. {ECO:0000305|PubMed:28541472, ECO:0000305|PubMed:28945193}.
DE  Disease: Spermatogenic failure 16 (SPGF16) [MIM:617187]: An infertility disorder caused by spermatogenesis defects and characterized by abnormally shaped spermatozoa in the semen of affected individuals. Most spermatozoa are made up of headless tails, while a small proportion has an abnormal head-tail junction. A few spermatozoa are made up of tailless heads. {ECO:0000269|PubMed:27640305, ECO:0000269|PubMed:28541472, ECO:0000269|PubMed:28945193, ECO:0000269|PubMed:29298896}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NPE6; IntAct: EBI-10819434,EBI-13068796; Score: 0.56
GO  GO:0005623;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0097224;
GO  GO:0043495;
GO  GO:0090286;
GO  GO:0006998;
GO  GO:0007286;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPRSSRSPGDPGALLEDVAHNPRPRRIAQRGRNTSRMAEDTSPNMNDNILLPVRNNDQALGLTQCMLGCVSWFTCFACSL
SQ  RTQAQQVLFNTCRCKLLCQKLMEKTGILLLCAFGFWMFSIHLPSKMKVWQDDSINGPLQSLRLYQEKVRHHSGEIQDLRG
SQ  SMNQLIAKLQEMEAMSDEQKMAQKIMKMIHGDYIEKPDFALKSIGASIDFEHTSVTYNHEKAHSYWNWIQLWNYAQPPDV
SQ  ILEPNVTPGNCWAFEGDRGQVTIQLAQKVYLSNLTLQHIPKTISLSGSLDTAPKDFVIYGMEGSPKEEVFLGAFQFQPEN
SQ  IIQMFPLQNQPARAFSAVKVKISSNWGNPGFTCLYRVRVHGSVAPPREQPHQNPYPKRD
//
ID  P38181;
PN  Nucleoporin NUP170;
GN  NUP170;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: P38181;
DR  UNIPROT: D6VPS4;
DR  PDB: 3I5P;
DR  PDB: 3I5Q;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity. {ECO:0000269|PubMed:11290711, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12473689, ECO:0000269|PubMed:14697200, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-10420,EBI-11756; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-12401,EBI-11756; Score: 0.44
DE  Interaction: P36161; IntAct: EBI-11722,EBI-11756; Score: 0.37
DE  Interaction: Self; IntAct: EBI-11756,EBI-11756; Score: 0.37
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-11756; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-11756; Score: 0.44
DE  Interaction: P48837; IntAct: EBI-11756,EBI-12324; Score: 0.44
DE  Interaction: P32597; IntAct: EBI-18410,EBI-11756; Score: 0.50
DE  Interaction: Q03790; IntAct: EBI-27321,EBI-11756; Score: 0.72
DE  Interaction: P11938; IntAct: EBI-14821,EBI-11756; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-11756,EBI-17237; Score: 0.50
DE  Interaction: Q00684; IntAct: EBI-4192,EBI-11756; Score: 0.35
DE  Interaction: P14832; IntAct: EBI-5463,EBI-11756; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11756; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-11756; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11756; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-11756,EBI-25940; Score: 0.35
DE  Interaction: P39929; IntAct: EBI-11756,EBI-17554; Score: 0.44
DE  Interaction: Q03281; IntAct: EBI-22131,EBI-11756; Score: 0.44
DE  Interaction: Q03707; IntAct: EBI-11756,EBI-18064; Score: 0.37
DE  Interaction: P40064; IntAct: EBI-11740,EBI-11756; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-11756,EBI-11730; Score: 0.59
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11756; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11756; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11756; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0003682;
GO  GO:1990841;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0006342;
GO  GO:0007059;
GO  GO:0016458;
GO  GO:0070869;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0016584;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFQSFFHNNGPAAAGETFSDSRSYPLTNHQEVPRNGLNELASSATKAQQQPTHILNSYPITGSNPLMRASAMGATSGSIN
SQ  PNMSNMNEHIRVSGMGTSKPLDLAGKYIDHLQHKDSNTPVLDERSYYNSGVDYNFSREKNGLGAFTPFEKQDVFNIPDEI
SQ  LHEFSTSQTKTDMGIFPELNRCWITIDNKLILWNINNDNEYQVVDDMKHTIQKVALVRPKPNTFVPAVKHLLLISTTMEL
SQ  FMFAISLDKATNELSVFNTHLSVPVQGIDVIDIVSHERSGRIFFAGQASGLNIWELHYSGSDDWFNSKCSKVCLTKSALL
SQ  SLLPTNMLSQIPGVDFIQALFEDNSNGNGGFSQETITQLTIDQQRGIIYSLSSKSTIRAYVITEKSLEGPMSIEPAYISR
SQ  IIGTTTARAAPILGPKYLKIVKISSVAPEENNNLFLVALTVGGVRLYFNGSMGRFNIEALRLESIKFPPSSVTPEVIQQE
SQ  LLHQQQEQAKRSFPFFSNLMSSEPVLLKFQKKSSVLLETTKASTIISPGIFFSAVIKSSQQTHQQEKKENSSVTGTTATA
SQ  GSKTVKQQPVTLQHKLFVSVPDYGILKTHGKYVENATFLETAGPVQQIIPLSGLFNATTKPQGFANEFATQYTSETLRVA
SQ  VLTSTSIEIYKYRTPDEIFEDLIDNPLPFVLNYGAAEACSTALFVTCKSNKSEKLRSNALTFLTMGIPGVVDIKPVYNRY
SQ  SVSTVSSLLSKPTLSTATTNLQQSITGFSKPSPANKEDFDLDDVILSPRFYGIALLITRLLRDIWGRHVFMTFTDNRVTS
SQ  HAFISSSDPITPSINNLKSDEISQNRNIISKVSISKDCIEYYLSSINILNEFFITYGDSISQISAPYVLANNSNGRVIDK
SQ  TEEVANQAESIAINAMIKMVQSIKEGLSFLNVLYEESEVEGFDNQYLGFKDIISFVSLDVQKDLVKLDFKDLFAPNDKTK
SQ  SLIREILLSIINRNITKGASIEYTATALQERCGSFCSASDILGFRAIEHLRRAKEIGLRNYDSLNYHLKNATALLEQIVD
SQ  DLSIEKLKEAVSMMLSVNYYPKSIEFLLNIANSMDKGKLACQYVANGFLENDDRKQYYDKRILVYDLVFDTLIKVDELAE
SQ  KKQSSKTQNQISISNDDEVKLRQKSYEAALKYNDRLFHYHMYDWLVSQNREEKLLDIETPFILPYLMEKAGSSLKISNIL
SQ  WVYYSRRSKFFESAEILYRLATSNFDITLFERIEFLSRANGFCNSVSPLSQKQRIVQLASRIQDACEVAGIQGDILSLVY
SQ  TDARIDSAIKDELIKTLDGKILSTSELFNDFAVPLSYHEIALFIFKIADFRDHEVIMAKWDELFQSLRMEFNNTGKKEDS
SQ  MNFINLLSNVLIKIGKNVQDSEFIFPIFELFPIVCNFFYETLPKEHIVSGSIVSIFITAGVSFNKMYYILKELIETSDSD
SQ  NSVFNKEMTWLIHEWYKSDRKFRDIISYNDIIHLKEYKIDNDPIEKYVKNSGNNLGICFYKE
//
ID  Q02629;
PN  Nucleoporin NUP100/NSP100;
GN  NUP100;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q02629;
DR  UNIPROT: D6VXL9;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP100 plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport. {ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8557738}.
DE  Reference Proteome: Yes;
DE  Interaction: P34077; IntAct: EBI-11698,EBI-12056; Score: 0.44
DE  Interaction: P35729; IntAct: EBI-11698,EBI-11713; Score: 0.44
DE  Interaction: P38181; IntAct: EBI-11698,EBI-11756; Score: 0.44
DE  Interaction: P40368; IntAct: EBI-12331,EBI-11698; Score: 0.55
DE  Interaction: P46673; IntAct: EBI-11698,EBI-12345; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-12324,EBI-11698; Score: 0.53
DE  Interaction: P49686; IntAct: EBI-12310,EBI-11698; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-11698,EBI-11730; Score: 0.44
DE  Interaction: P52593; IntAct: EBI-11763,EBI-11698; Score: 0.37
DE  Interaction: P52891; IntAct: EBI-11698,EBI-12337; Score: 0.59
DE  Interaction: Q02199; IntAct: EBI-12315,EBI-11698; Score: 0.44
DE  Interaction: Self; IntAct: EBI-11698,EBI-11698; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-11698,EBI-11703; Score: 0.65
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-11698; Score: 0.82
DE  Interaction: Q05166; IntAct: EBI-11698,EBI-3035; Score: 0.44
DE  Interaction: P40482; IntAct: EBI-16592,EBI-11698; Score: 0.37
DE  Interaction: P53038; IntAct: EBI-11698,EBI-19106; Score: 0.37
DE  Interaction: P43603; IntAct: EBI-22980,EBI-11698; Score: 0.37
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11698; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11698; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-11698,EBI-8632; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-11698,EBI-19749; Score: 0.37
DE  Interaction: P53035; IntAct: EBI-11698,EBI-10919; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11698; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11698; Score: 0.53
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFG
SQ  QSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFG
SQ  GQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLG
SQ  GSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLF
SQ  GKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPA
SQ  GTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNT
SQ  ASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSS
SQ  AVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKR
SQ  NSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLN
SQ  VINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISS
SQ  KVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSI
SQ  YENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT
//
ID  P35845;
PN  Oxysterol-binding protein homolog 1;
GN  SWH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm. Golgi apparatus membrane. Nucleus outer membrane. Note=Soluble protein that accumulates on the surface of late Golgi membranes and at nucleus-vacuole (NV) junctions, interorganelle interfaces between the nuclear envelope and the vacuole membrane formed during piecemeal microautophagy of the nucleus (PMN). Targeted exclusively to NV junctions in stationary phase.
DR  UNIPROT: P35845;
DR  UNIPROT: D6VPN6;
DR  UNIPROT: P39555;
DR  UNIPROT: P80234;
DR  UNIPROT: Q86ZC4;
DR  UNIPROT: Q86ZS1;
DR  PDB: 5H28;
DR  PDB: 5H2C;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition. {ECO:0000269|PubMed:15173322}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-12611,EBI-12611; Score: 0.62
DE  Interaction: P10591; IntAct: EBI-12611,EBI-8591; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-12611; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-12611,EBI-8680; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-12611; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-8603,EBI-12611; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-12611,EBI-8632; Score: 0.53
DE  Interaction: P32589; IntAct: EBI-12611,EBI-8648; Score: 0.35
DE  Interaction: P43613; IntAct: EBI-23020,EBI-12611; Score: 0.35
DE  Interaction: P40564; IntAct: EBI-12611,EBI-25380; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-12611; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-12611; Score: 0.35
DE  Interaction: P40075; IntAct: EBI-16735,EBI-12611; Score: 0.55
DE  Interaction: P29056; IntAct: EBI-19142,EBI-12611; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-12611,EBI-7218; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-12611,EBI-6333; Score: 0.35
DE  Interaction: P32794; IntAct: EBI-12611,EBI-2310; Score: 0.35
DE  Interaction: P38881; IntAct: EBI-24885,EBI-12611; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-6533,EBI-12611; Score: 0.44
DE  Interaction: P40510; IntAct: EBI-12611,EBI-16821; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-12611,EBI-14372; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-12611,EBI-6314; Score: 0.56
DE  Interaction: P26786; IntAct: EBI-12611,EBI-16161; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-12611,EBI-16136; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-12611,EBI-15270; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-12611,EBI-11191; Score: 0.35
DE  Interaction: P32317; IntAct: EBI-12611,EBI-2306; Score: 0.35
DE  Interaction: P53919; IntAct: EBI-12611,EBI-28887; Score: 0.37
DE  Interaction: P38829; IntAct: EBI-12611,EBI-24704; Score: 0.37
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0000139;
GO  GO:0000138;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0071561;
GO  GO:0005545;
GO  GO:0008289;
GO  GO:0008142;
GO  GO:0032934;
GO  GO:0120015;
GO  GO:0015248;
GO  GO:0006897;
GO  GO:0006887;
GO  GO:0030011;
GO  GO:0034727;
GO  GO:0015918;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEQPDLSSVAISKPLLKLKLLDALRQGSFPNLQDLLKKQFQPLDDPNVQQVLHLMLHYAVQVAPMAVIKEIVHHWVSTTN
SQ  TTFLNIHLDLNERDSNGNTPLHIAAYQSRGDIVAFLLDQPTINDCVLNNSHLQAIEMCKNLNIAQMMQVKRSTYVAETAQ
SQ  EFRTAFNNRDFGHLESILSSPRNAELLDINGMDPETGDTVLHEFVKKRDVIMCRWLLEHGADPFKRDRKGKLPIELVRKV
SQ  NENDTATNTKIAIDIELKKLLERATREQSVIDVTNNNLHEAPTYKGYLKKWTNFAQGYKLRWFILSSDGKLSYYIDQADT
SQ  KNACRGSLNMSSCSLHLDSSEKLKFEIIGGNNGVIRWHLKGNHPIETNRWVWAIQGAIRYAKDREILLHNGPYSPSLALS
SQ  HGLSSKVSNKENLHATSKRLTKSPHLSKSTLTQNDHDNDDDSTNNNNNKSNNDYDDNNNNNNNDDDDYDDDDESRPLIEP
SQ  LPLISSRSQSLSEITPGPHSRKSTVSSTRAADIPSDDEGYSEDDSDDDGNSSYTMENGGENDGDEDLNAIYGPYIQKLHM
SQ  LQRSISIELASLNELLQDKQQHDEYWNTVNTSIETVSEFFDKLNRLTSQREKRMIAQMTKQRDVNNVWIQSVKDLEMELV
SQ  DKDEKLVALDKERKNLKKMLQKKLNNQPQVETEANEESDDANSMIKGSQESTNTLEEIVKFIEATKESDEDSDADEFFDA
SQ  EEAASDKKANDSEDLTTNKETPANAKPQEEAPEDESLIVISSPQVEKKNQLLKEGSFVGYEDPVRTKLALDEDNRPKIGL
SQ  WSVLKSMVGQDLTKLTLPVSFNEPTSLLQRVSEDIEYSHILDQAATFEDSSLRMLYVAAFTASMYASTTNRVSKPFNPLL
SQ  GETFEYARTDGQYRFFTEQVSHHPPISATWTESPKWDFYGECNVDSSFNGRTFAVQHLGLWYITIRPDHNISVPEETYSW
SQ  KKPNNTVIGILMGKPQVDNSGDVKVTNHTTGDYCMLHYKAHGWTSAGAYEVRGEVFNKDDKKLWVLGGHWNDSIYGKKVT
SQ  ARGGELTLDRIKTANSATGGPKLDGSKFLIWKANERPSVPFNLTSFALTLNALPPHLIPYLAPTDSRLRPDQRAMENGEY
SQ  DKAAAEKHRVEVKQRAAKKEREQKGEEYRPKWFVQEEHPVTKSLYWKFNGEYWNKRKNHDFKDCADIF
//
ID  Q08931;
PN  Pheromone-regulated membrane protein 3;
GN  PRM3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane; Single-pass membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
DR  UNIPROT: Q08931;
DR  UNIPROT: D6W3H6;
DE  Function: Required for the fusion of nuclear envelopes during mating, ensuring proper karyogamy. Plays a role in the initiation of outer nuclear envelope fusion. {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:19297527, ECO:0000269|PubMed:19570912}.
DE  Reference Proteome: Yes;
DE  Interaction: P40857; IntAct: EBI-36479,EBI-26003; Score: 0.37
DE  Interaction: P47088; IntAct: EBI-36479,EBI-26307; Score: 0.37
DE  Interaction: P38074; IntAct: EBI-36479,EBI-8394; Score: 0.37
GO  GO:0005737;
GO  GO:0031316;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005816;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAMKEDNAALITLKKNNDQEKLRVHKLTDASSNSADGFVINKAKNGGPLNKKSLVNNEQHIKKAVSPGRVRKHKTTTSS
SQ  TKSRTKSKKKDASESKVQRENKGSFYQGAIFGSFLGAAVTTVLSNLAVKALQN
//
ID  P14906;
PN  Protein translocation protein SEC63;
GN  SEC63;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein.
DR  UNIPROT: P14906;
DR  UNIPROT: D6W2V5;
DR  UNIPROT: Q08690;
DR  PDB: 6N3Q;
DR  PDB: 6ND1;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination. {ECO:0000269|PubMed:11226176}.
DE  Reference Proteome: Yes;
DE  Interaction: P32915; IntAct: EBI-16400,EBI-16636; Score: 0.79
DE  Interaction: P33754; IntAct: EBI-16636,EBI-16647; Score: 0.83
DE  Interaction: P39742; IntAct: EBI-16636,EBI-16651; Score: 0.83
DE  Interaction: P21825; IntAct: EBI-16632,EBI-16636; Score: 0.75
DE  Interaction: P37898; IntAct: EBI-1998,EBI-16636; Score: 0.35
DE  Interaction: Q12168; IntAct: EBI-32973,EBI-16636; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-2169,EBI-16636; Score: 0.35
DE  Interaction: P22108; IntAct: EBI-2635,EBI-16636; Score: 0.35
DE  Interaction: P08566; IntAct: EBI-2883,EBI-16636; Score: 0.35
DE  Interaction: Q06834; IntAct: EBI-16636,EBI-33224; Score: 0.35
DE  Interaction: Q08347; IntAct: EBI-16636,EBI-3763789; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-16636,EBI-31563; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-16636,EBI-9890; Score: 0.35
DE  Interaction: Q12018; IntAct: EBI-16636,EBI-4321; Score: 0.35
DE  Interaction: Q06697; IntAct: EBI-16636,EBI-29913; Score: 0.35
DE  Interaction: P53197; IntAct: EBI-23684,EBI-16636; Score: 0.35
DE  Interaction: P40094; IntAct: EBI-16605,EBI-16636; Score: 0.35
DE  Interaction: Q01454; IntAct: EBI-16636,EBI-5209; Score: 0.35
DE  Interaction: P38865; IntAct: EBI-16636,EBI-5268; Score: 0.35
DE  Interaction: P31373; IntAct: EBI-5473,EBI-16636; Score: 0.35
DE  Interaction: P32582; IntAct: EBI-4167,EBI-16636; Score: 0.35
DE  Interaction: Q08496; IntAct: EBI-16636,EBI-31943; Score: 0.35
DE  Interaction: P53759; IntAct: EBI-16636,EBI-27885; Score: 0.35
DE  Interaction: Q06053; IntAct: EBI-16636,EBI-27095; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-24359,EBI-16636; Score: 0.35
DE  Interaction: P36053; IntAct: EBI-16636,EBI-26919; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-16636,EBI-6468; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-16636,EBI-6475; Score: 0.35
DE  Interaction: P45976; IntAct: EBI-6940,EBI-16636; Score: 0.35
DE  Interaction: P15442; IntAct: EBI-16636,EBI-330; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-7727,EBI-16636; Score: 0.35
DE  Interaction: P32347; IntAct: EBI-16636,EBI-5711; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-16636,EBI-8883; Score: 0.35
DE  Interaction: P53982; IntAct: EBI-16636,EBI-8892; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-16636,EBI-25710; Score: 0.35
DE  Interaction: P32361; IntAct: EBI-9364,EBI-16636; Score: 0.35
DE  Interaction: P48526; IntAct: EBI-18725,EBI-16636; Score: 0.35
DE  Interaction: P38144; IntAct: EBI-16636,EBI-21087; Score: 0.35
DE  Interaction: Q12494; IntAct: EBI-16636,EBI-37528; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-16636,EBI-9619; Score: 0.35
DE  Interaction: Q02574; IntAct: EBI-16636,EBI-10658; Score: 0.35
DE  Interaction: P00958; IntAct: EBI-18762,EBI-16636; Score: 0.35
DE  Interaction: Q07980; IntAct: EBI-33369,EBI-16636; Score: 0.35
DE  Interaction: Q02455; IntAct: EBI-11009,EBI-16636; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-16636,EBI-25261; Score: 0.35
DE  Interaction: P48563; IntAct: EBI-28333,EBI-16636; Score: 0.35
DE  Interaction: P30775; IntAct: EBI-14964,EBI-16636; Score: 0.35
DE  Interaction: P53166; IntAct: EBI-16636,EBI-23808; Score: 0.35
DE  Interaction: Q02950; IntAct: EBI-16636,EBI-37241; Score: 0.35
DE  Interaction: P47047; IntAct: EBI-16636,EBI-11592; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-16636,EBI-11659; Score: 0.35
DE  Interaction: P33420; IntAct: EBI-16636,EBI-12049; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-12114,EBI-16636; Score: 0.35
DE  Interaction: P38271; IntAct: EBI-16636,EBI-12563; Score: 0.35
DE  Interaction: Q12451; IntAct: EBI-16636,EBI-12621; Score: 0.35
DE  Interaction: P40960; IntAct: EBI-16636,EBI-30551; Score: 0.35
DE  Interaction: P17558; IntAct: EBI-16341,EBI-16636; Score: 0.35
DE  Interaction: P40433; IntAct: EBI-16636,EBI-1956; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-16636,EBI-13275; Score: 0.35
DE  Interaction: P36093; IntAct: EBI-16636,EBI-13366; Score: 0.35
DE  Interaction: P07271; IntAct: EBI-16636,EBI-13404; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-465,EBI-16636; Score: 0.35
DE  Interaction: P52489; IntAct: EBI-16636,EBI-9895; Score: 0.35
DE  Interaction: P38344; IntAct: EBI-21136,EBI-16636; Score: 0.35
DE  Interaction: P29539; IntAct: EBI-2083307,EBI-16636; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-16636,EBI-15475; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-14480,EBI-16636; Score: 0.35
DE  Interaction: P54780; IntAct: EBI-14485,EBI-16636; Score: 0.35
DE  Interaction: P05749; IntAct: EBI-16636,EBI-14552; Score: 0.35
DE  Interaction: Q12149; IntAct: EBI-16636,EBI-1782; Score: 0.35
DE  Interaction: Q02206; IntAct: EBI-16636,EBI-16204; Score: 0.35
DE  Interaction: P40482; IntAct: EBI-16592,EBI-16636; Score: 0.35
DE  Interaction: P11075; IntAct: EBI-16636,EBI-16882; Score: 0.35
DE  Interaction: P34223; IntAct: EBI-16636,EBI-17093; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-16636,EBI-34508; Score: 0.35
DE  Interaction: P39928; IntAct: EBI-17357,EBI-16636; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-16636,EBI-17402; Score: 0.35
DE  Interaction: P25357; IntAct: EBI-16636,EBI-17596; Score: 0.35
DE  Interaction: P36126; IntAct: EBI-17726,EBI-16636; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-16636,EBI-18084; Score: 0.35
DE  Interaction: P36085; IntAct: EBI-18340,EBI-16636; Score: 0.35
DE  Interaction: P08153; IntAct: EBI-16636,EBI-18633; Score: 0.35
DE  Interaction: Q06510; IntAct: EBI-2094606,EBI-16636; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-16636,EBI-7218; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-6314,EBI-16636; Score: 0.35
DE  Interaction: P32367; IntAct: EBI-19150,EBI-16636; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-16636,EBI-8951; Score: 0.56
DE  Interaction: P35169; IntAct: EBI-19374,EBI-16636; Score: 0.35
DE  Interaction: P40061; IntAct: EBI-22621,EBI-16636; Score: 0.35
DE  Interaction: P53874; IntAct: EBI-19873,EBI-16636; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-14372,EBI-16636; Score: 0.35
DE  Interaction: P34241; IntAct: EBI-26595,EBI-16636; Score: 0.35
DE  Interaction: Q12339; IntAct: EBI-16636,EBI-30231; Score: 0.35
DE  Interaction: Q06685; IntAct: EBI-16636,EBI-35034; Score: 0.35
DE  Interaction: P22203; IntAct: EBI-16636,EBI-20268; Score: 0.35
DE  Interaction: O13584; IntAct: EBI-32314,EBI-16636; Score: 0.35
DE  Interaction: P33301; IntAct: EBI-16636,EBI-20599; Score: 0.35
DE  Interaction: P19880; IntAct: EBI-16636,EBI-31265; Score: 0.35
DE  Interaction: O13527; IntAct: EBI-16636,EBI-33845; Score: 0.35
DE  Interaction: P87264; IntAct: EBI-16636,EBI-3770432; Score: 0.35
DE  Interaction: P39991; IntAct: EBI-3665883,EBI-16636; Score: 0.35
DE  Interaction: P38854; IntAct: EBI-24799,EBI-16636; Score: 0.35
DE  Interaction: P34246; IntAct: EBI-16636,EBI-26803; Score: 0.35
DE  Interaction: Q05948; IntAct: EBI-16636,EBI-36984; Score: 0.35
DE  Interaction: Q06567; IntAct: EBI-16636,EBI-27160; Score: 0.35
DE  Interaction: Q03153; IntAct: EBI-28199,EBI-16636; Score: 0.35
DE  Interaction: Q12751; IntAct: EBI-16636,EBI-27406; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-16636,EBI-28374; Score: 0.35
DE  Interaction: Q12697; IntAct: EBI-16636,EBI-3770507; Score: 0.35
DE  Interaction: Q08748; IntAct: EBI-16636,EBI-2050125; Score: 0.35
DE  Interaction: Q06813; IntAct: EBI-16636,EBI-38252; Score: 0.35
DE  Interaction: P36019; IntAct: EBI-16636,EBI-29415; Score: 0.35
DE  Interaction: P31111; IntAct: EBI-29645,EBI-16636; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-16636; Score: 0.35
DE  Interaction: P39079; IntAct: EBI-19077,EBI-16636; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-16636,EBI-8648; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-3003,EBI-16636; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-16636,EBI-20589; Score: 0.35
DE  Interaction: P14922; IntAct: EBI-16636,EBI-18215; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-6587,EBI-16636; Score: 0.35
DE  Interaction: P21268; IntAct: EBI-16636,EBI-6780; Score: 0.35
DE  Interaction: P00927; IntAct: EBI-16636,EBI-19200; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-28814,EBI-16636; Score: 0.35
DE  Interaction: Q12524; IntAct: EBI-16636,EBI-27150; Score: 0.35
DE  Interaction: P54885; IntAct: EBI-16636,EBI-13872; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-8973,EBI-16636; Score: 0.35
DE  Interaction: P40016; IntAct: EBI-16636,EBI-15927; Score: 0.35
DE  Interaction: Q12250; IntAct: EBI-15935,EBI-16636; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-35018,EBI-16636; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-16636,EBI-31337; Score: 0.35
DE  Interaction: P31376; IntAct: EBI-16636,EBI-20613; Score: 0.35
DE  Interaction: P38326; IntAct: EBI-21031,EBI-16636; Score: 0.35
DE  Interaction: P38123; IntAct: EBI-20881,EBI-16636; Score: 0.35
DE  Interaction: Q05471; IntAct: EBI-22102,EBI-16636; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-8958,EBI-16636; Score: 0.35
DE  Interaction: Q05946; IntAct: EBI-34702,EBI-16636; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-16636,EBI-20415; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-6338,EBI-16636; Score: 0.35
DE  Interaction: P53719; IntAct: EBI-28456,EBI-16636; Score: 0.35
DE  Interaction: P53740; IntAct: EBI-28524,EBI-16636; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-16636,EBI-8591; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-16636; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-16636,EBI-20254; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-16636,EBI-8603; Score: 0.35
DE  Interaction: P32629; IntAct: EBI-2595,EBI-16636; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-16636,EBI-19749; Score: 0.37
DE  Interaction: P47026; IntAct: EBI-25989,EBI-16636; Score: 0.35
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0031207;
GO  GO:0008320;
GO  GO:0003723;
GO  GO:0046967;
GO  GO:0006620;
GO  GO:0031204;
GO  GO:0006614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDK
SQ  NSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKG
SQ  LTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVS
SQ  RWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNN
SQ  AKFRIVAKCHSLLHGLLDIACGFRNLDIALGAINTFKCIVQAVPLTPNCQILQLPNVDKEHFITKTGDIHTLGKLFTLED
SQ  AKIGEVLGIKDQAKLNETLRVASHIPNLKIIKADFLVPGENQVTPSSTPYISLKVLVRSAKQPLIPTSLIPEENLTEPQD
SQ  FESQRDPFAMMSKQPLVPYSFAPFFPTKRRGSWCCLVSSQKDGKILQTPIIIEKLSYKNLNDDKDFFDKRIKMDLTKHEK
SQ  FDINDWEIGTIKIPLGQPAPETVGDFFFRVIVKSTDYFTTDLDITMNMKVRDSPAVEQVEVYSEEDDEYSTDDDETESDD
SQ  ESDASDYTDIDTDTEAEDDESPE
//
ID  Q03790;
PN  Nucleoporin NUP53;
GN  NUP53;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q03790;
DR  UNIPROT: D6VZX4;
DR  PDB: 3W3Y;
DR  PDB: 5UAZ;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation. {ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12473689, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:14697200, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P32500; IntAct: EBI-11950,EBI-27321; Score: 0.55
DE  Interaction: P34077; IntAct: EBI-12056,EBI-27321; Score: 0.67
DE  Interaction: P38181; IntAct: EBI-27321,EBI-11756; Score: 0.72
DE  Interaction: P40064; IntAct: EBI-27321,EBI-11740; Score: 0.55
DE  Interaction: P40368; IntAct: EBI-12331,EBI-27321; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-12345,EBI-27321; Score: 0.37
DE  Interaction: P47054; IntAct: EBI-27321,EBI-25846; Score: 0.37
DE  Interaction: Self; IntAct: EBI-27321,EBI-27321; Score: 0.67
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-27321; Score: 0.44
DE  Interaction: Q05166; IntAct: EBI-27321,EBI-3035; Score: 0.37
DE  Interaction: P32597; IntAct: EBI-18410,EBI-27321; Score: 0.35
DE  Interaction: P11938; IntAct: EBI-14821,EBI-27321; Score: 0.35
DE  Interaction: P38265; IntAct: EBI-21579,EBI-27321; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-27321,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-27321; Score: 0.53
DE  Interaction: P32589; IntAct: EBI-27321,EBI-8648; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-27321,EBI-8591; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-27321; Score: 0.35
DE  Interaction: Q05359; IntAct: EBI-6581,EBI-27321; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-27321,EBI-20254; Score: 0.35
DE  Interaction: Q12398; IntAct: EBI-27321,EBI-32583; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-27321,EBI-6475; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-27321; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-27321; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0042802;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0034501;
GO  GO:0007088;
GO  GO:0060188;
GO  GO:0006355;
GO  GO:0072417;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFN
SQ  NPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDS
SQ  NEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGS
SQ  KEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKS
SQ  ELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKV
SQ  RNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL
//
ID  A4GSN8;
PN  Nuclear-pore anchor;
GN  NUA;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000269|PubMed:19704557}; Peripheral membrane protein {ECO:0000269|PubMed:19704557}; Nucleoplasmic side {ECO:0000269|PubMed:19704557}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:19704557}. Note=Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557}.
DR  UNIPROT: A4GSN8;
DR  UNIPROT: F4IDK8;
DR  UNIPROT: F4IDK9;
DR  UNIPROT: O64521;
DR  UNIPROT: O64522;
DR  UNIPROT: O64524;
DR  UNIPROT: O64525;
DR  UNIPROT: Q8H7F1;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:17535820, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:19704774, ECO:0000303|PubMed:20872268}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-1545660,EBI-1545660; Score: 0.37
DE  Interaction: Q94F30; IntAct: EBI-1545660,EBI-1545674; Score: 0.37
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0009910;
GO  GO:0033234;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0060968;
GO  GO:0048443;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:19704557};
SQ  MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQS
SQ  DFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSS
SQ  EKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSL
SQ  NWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESS
SQ  YKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGT
SQ  ALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSV
SQ  SEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKI
SQ  ISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVA
SQ  MYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLA
SQ  MEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAE
SQ  KRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNN
SQ  AVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGE
SQ  VESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALL
SQ  SASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELR
SQ  KLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSG
SQ  LQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRES
SQ  NMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYN
SQ  RLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNK
SQ  KIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKT
SQ  EDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLS
SQ  GSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASD
SQ  NKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQAD
SQ  SLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVE
SQ  AQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPE
SQ  TLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSS
SQ  TLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGR
SQ  APRGGRGQSPSPP
//
ID  Q21443;
PN  Lamin-1;
GN  lmn;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12490171, ECO:0000269|PubMed:25057012}; Lipid-anchor {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}. Note=Remains in the nuclear envelope until late anaphase in early embryos. Depends on mel-28 for nuclear envelope localization after mitosis. {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114}.
DR  UNIPROT: Q21443;
DR  UNIPROT: O62127;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:11071918, PubMed:25057012). Provides a framework for the nuclear envelope and probably also interacts with chromatin (PubMed:11071918, PubMed:25057012). Essential to maintain the shape and integrity of the nucleus, and for DNA replication (PubMed:11071918). Involved in spatial organization of nuclear pore complexes (PubMed:11071918). It is not a target for ced-3 during apoptosis, suggesting that lamin cleavage is not essential for apoptosis in C.elegans (PubMed:12064941). {ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12064941, ECO:0000269|PubMed:25057012}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EEH9; IntAct: EBI-6455549,EBI-314110; Score: 0.37
DE  Interaction: Q18508; IntAct: EBI-314110,EBI-2002730; Score: 0.37
DE  Interaction: Self; IntAct: EBI-314110,EBI-314110; Score: 0.64
DE  Interaction: G5EDM4; IntAct: EBI-314110,EBI-313674; Score: 0.37
DE  Interaction: Q09284; IntAct: EBI-314110,EBI-2915600; Score: 0.37
DE  Interaction: G5ECZ8; IntAct: EBI-2915667,EBI-314110; Score: 0.37
DE  Interaction: C1P635; IntAct: EBI-2917046,EBI-314110; Score: 0.37
DE  Interaction: Q7JLR4; IntAct: EBI-2415541,EBI-314110; Score: 0.49
DE  Interaction: Q9XTB5; IntAct: EBI-314110,EBI-2535391; Score: 0.53
DE  Interaction: O44548; IntAct: EBI-2002279,EBI-314110; Score: 0.37
DE  Interaction: G5ECR7; IntAct: EBI-330567,EBI-314110; Score: 0.37
DE  Interaction: P34402; IntAct: EBI-1570073,EBI-314110; Score: 0.37
DE  Interaction: Q19749; IntAct: EBI-320763,EBI-314110; Score: 0.37
DE  Interaction: Q9U3C1; IntAct: EBI-314110,EBI-2004353; Score: 0.37
DE  Interaction: Q21295; IntAct: EBI-314110,EBI-2004307; Score: 0.37
DE  Interaction: O01585; IntAct: EBI-2004403,EBI-314110; Score: 0.37
DE  Interaction: P30642; IntAct: EBI-314110,EBI-311981; Score: 0.37
DE  Interaction: P91457; IntAct: EBI-2004585,EBI-314110; Score: 0.37
DE  Interaction: Q86S68; IntAct: EBI-3902879,EBI-314110; Score: 0.37
DE  Interaction: Q95XY1; IntAct: EBI-331661,EBI-314110; Score: 0.37
DE  Interaction: Q65XX1; IntAct: EBI-2004375,EBI-314110; Score: 0.37
DE  Interaction: G5ECG0; IntAct: EBI-314110,EBI-320612; Score: 0.37
DE  Interaction: Q95QC4; IntAct: EBI-314110,EBI-331795; Score: 0.37
DE  Interaction: O02217; IntAct: EBI-1187455,EBI-314110; Score: 0.37
DE  Interaction: Q8WQC0-3; IntAct: EBI-6459543,EBI-314110; Score: 0.37
DE  Interaction: P39745-1; IntAct: EBI-6455829,EBI-314110; Score: 0.37
DE  Interaction: Q9N583; IntAct: EBI-6460139,EBI-314110; Score: 0.37
DE  Interaction: Q09601-1; IntAct: EBI-314110,EBI-6455756; Score: 0.37
DE  Interaction: P12114; IntAct: EBI-2001946,EBI-314110; Score: 0.37
DE  Interaction: Q8MPS6; IntAct: EBI-314110,EBI-6457529; Score: 0.37
DE  Interaction: Q23593; IntAct: EBI-6460566,EBI-314110; Score: 0.37
DE  Interaction: Q09583; IntAct: EBI-314110,EBI-315406; Score: 0.37
DE  Interaction: Q17391; IntAct: EBI-593075,EBI-314110; Score: 0.37
DE  Interaction: P91505; IntAct: EBI-314110,EBI-326040; Score: 0.37
DE  Interaction: Q9XXH8; IntAct: EBI-314110,EBI-312159; Score: 0.37
DE  Interaction: O01527; IntAct: EBI-314110,EBI-6726969; Score: 0.37
DE  Interaction: Q9GYG1; IntAct: EBI-314846,EBI-314110; Score: 0.37
DE  Interaction: O62090; IntAct: EBI-314110,EBI-2917690; Score: 0.37
DE  Interaction: P34288-2; IntAct: EBI-314110,EBI-11465290; Score: 0.37
DE  Interaction: Q8WQC0; IntAct: EBI-6499941,EBI-314110; Score: 0.37
DE  Interaction: Q95ZY7; IntAct: EBI-11468703,EBI-314110; Score: 0.37
DE  Interaction: Q965F9; IntAct: EBI-314110,EBI-11465387; Score: 0.37
DE  Interaction: O44452; IntAct: EBI-314110,EBI-314097; Score: 0.37
DE  Interaction: Q19633; IntAct: EBI-314110,EBI-320052; Score: 0.37
DE  Interaction: Q19969; IntAct: EBI-314110,EBI-317340; Score: 0.37
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0042393;
GO  GO:0042802;
GO  GO:0005198;
GO  GO:0008340;
GO  GO:0009792;
GO  GO:0007281;
GO  GO:0030473;
GO  GO:0031081;
GO  GO:0006997;
GO  GO:0008284;
GO  GO:0008104;
GO  GO:0051983;
GO  GO:0007346;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDI
SQ  EVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQA
SQ  KQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDM
SQ  TTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLI
SQ  ERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVH
SQ  HVSFSSGGASAQRGVKRRRVVDVNGEDQDIDYLNRRSKLNKETVGPVGIDEVDEEGKWVRVANNSEEEQSIGGYKLVVKA
SQ  GNKEASFQFSSRMKLAPHASATVWSADAGAVHHPPEVYVMKKQQWPIGDNPSARLEDSEGDTVSSITVEFSESSDPSDPA
SQ  DRCSIM
//
ID  Q19131;
PN  Nuclear pore complex protein 5;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22238360}. Nucleus membrane {ECO:0000269|PubMed:22238360}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to nuclear membrane periphery during interphase and to kinetochore during mitosis. {ECO:0000269|PubMed:22238360}.
DR  UNIPROT: Q19131;
DR  Pfam: PF04121;
DE  Function: Involved in kinetochore assembly and chromosome segregation during embryonic mitosis. Required for the localization of the NDC80 complex member him-10, the chromosomal passenger complex component air- 2 and nuclear pore complex proteins npp-23 and npp-15 to kinetochores during metaphase. Required for npp-23 localization to the nuclear envelope during interphase. Recruits mdf-1, a component of the spindle assembly checkpoint, to the nuclear envelope. Appears dispensable for the assembly of the nuclear pore complex and for nuclear protein import. {ECO:0000269|PubMed:22238360}.
DE  Reference Proteome: Yes;
DE  Interaction: O17982; IntAct: EBI-325671,EBI-318528; Score: 0.37
GO  GO:0000777;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0034613;
GO  GO:0007059;
GO  GO:0051382;
GO  GO:0006406;
GO  GO:0002119;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0034501;
GO  GO:1900037;
GO  GO:0010965;
GO  GO:0097298;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MTDLFASGDNSSNSFDDSNDEIARKNETAFKYTTIFHTNLSEKLYHELCALAFGEFDIPQGQISPLMWTRLHEIYSEVEM
SQ  QTRKLPAGSNYSASSQKYANEAVQIASVLSIYTALAHEYDETVEVSLLSKLVVEDVEFRRIYALLLWSEKAISEQQYEKG
SQ  LGDKVRKLEGIKSSRINSMMALKRPTFGAANAPKDASLDPDAPGTKEDQALEQMAMNVFFQLIRSGETSKAANLAIDLGM
SQ  GAIGAQLQLHSMLRNPLDIPLEASKQNFGEYKRSRRAKYYQMTQKLIEQSQGSEDDAYWMLISAIRGNIQPMLKAGKSVI
SQ  EKVWAYANSAVLARILAAEGAMTQETISTLFNVPLTSKSILDELRSEADRTKEVYILLRVIDDMLNDDIEDLYKFANETV
SQ  GEFVPNDKNCQVNMLALDIFFHLVAVSYASGFEPNDDGNAVIILGFDDLRARSGTSSHKKMAAFYSRFLPEDMKLPEIVE
SQ  TMKAVDSDEEREILAESLKQSDIDFGRCACTLIEQIRKDDKTKVVTLEEQIDHWHWLLIGGEETALAALEECNRLVRKVM
SQ  LSTPIDESVIRQIIRKALHFEVPKLLSQAVENEATVLSLITDGTLFEQKPGSQLAINKIEHAALEFYGLCSFVDVNNFMI
SQ  TIALKLGLMFKYTPITDDELSMIGGVKRLDNTTAADWEASLRVRARAEQTLREEVLKKRAAEHNTRVGMVQQHLDTVLPM
SQ  LRGLVNNIGVRPEYFLSPRANGDPMRVHRKEIQEIRNLFLPQFFILLAQAAVRLDDTTNFNDFFTSFNNDLGLDQEWMVF
SQ  IKAFYAELNLKVE
//
ID  P52891;
PN  Nucleoporin NUP84;
GN  NUP84;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P52891;
DR  UNIPROT: D6VRN4;
DR  PDB: 3IKO;
DR  PDB: 3JRO;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: P35729; IntAct: EBI-11713,EBI-12337; Score: 0.91
DE  Interaction: P36161; IntAct: EBI-12337,EBI-11722; Score: 0.55
DE  Interaction: P46673; IntAct: EBI-12337,EBI-12345; Score: 0.73
DE  Interaction: P48837; IntAct: EBI-12324,EBI-12337; Score: 0.44
DE  Interaction: P49686; IntAct: EBI-12310,EBI-12337; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-12337,EBI-11730; Score: 0.95
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-12337; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-12337; Score: 0.59
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12337; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-12337,EBI-8680; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-12337; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-12337,EBI-8591; Score: 0.35
DE  Interaction: Q05166; IntAct: EBI-12337,EBI-3035; Score: 0.37
DE  Interaction: Q8WUM0; IntAct: EBI-295695,EBI-12337; Score: 0.40
DE  Interaction: P16140; IntAct: EBI-12337,EBI-20254; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-12337,EBI-6314; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12337,EBI-8603; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-12337,EBI-16940; Score: 0.64
DE  Interaction: Q04491; IntAct: EBI-12337,EBI-16529; Score: 0.53
DE  Interaction: P34232; IntAct: EBI-12337,EBI-11585; Score: 0.53
DE  Interaction: Q99257; IntAct: EBI-12337,EBI-11642; Score: 0.61
DE  Interaction: P32582; IntAct: EBI-4167,EBI-12337; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12337; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12337; Score: 0.32
GO  GO:0000781;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006974;
GO  GO:0030466;
GO  GO:0006302;
GO  GO:0035392;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0031081;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDESNVISSKDWELEARFWHLVEL
SQ  LLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDF
SQ  PLRENTNVLDVKDKEEDHIFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKH
SQ  SLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIENYLLENNQVGTDELILPLPSH
SQ  ALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIIN
SQ  PGSVEEVDKSKLITTYISLLKLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTT
SQ  QRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLNGRVKALEQFMERNNIGEICK
SQ  NYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEWQKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTS
SQ  SNFADSADYEILYEIRALYTPFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVAR
SQ  TATLSN
//
ID  P53011;
PN  Nucleoporin SEH1;
GN  SEH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Cytoplasmic side {ECO:0000269|PubMed:10684247}. Vacuole membrane {ECO:0000269|PubMed:21454883}; Peripheral membrane protein {ECO:0000269|PubMed:21454883}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Nucleoplasmic side {ECO:0000269|PubMed:10684247}. Note=Symmetric distribution. {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: P53011;
DR  UNIPROT: D6VU45;
DR  PDB: 3EWE;
DR  PDB: 3F3F;
DR  PDB: 3F3G;
DR  PDB: 3F3P;
DR  PDB: 4XMM;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. {ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:21454883, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: P35729; IntAct: EBI-11713,EBI-16940; Score: 0.91
DE  Interaction: P46673; IntAct: EBI-12345,EBI-16940; Score: 0.92
DE  Interaction: P49687; IntAct: EBI-11730,EBI-16940; Score: 0.81
DE  Interaction: P52891; IntAct: EBI-12337,EBI-16940; Score: 0.64
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-16940; Score: 0.44
DE  Interaction: P47170; IntAct: EBI-25710,EBI-16940; Score: 0.58
DE  Interaction: P39923; IntAct: EBI-12212,EBI-16940; Score: 0.35
DE  Interaction: P38742; IntAct: EBI-24336,EBI-16940; Score: 0.35
DE  Interaction: Q08281; IntAct: EBI-2047093,EBI-16940; Score: 0.35
DE  Interaction: Q03897; IntAct: EBI-32422,EBI-16940; Score: 0.53
DE  Interaction: P38164; IntAct: EBI-21365,EBI-16940; Score: 0.50
DE  Interaction: P32472; IntAct: EBI-2883297,EBI-16940; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-30084,EBI-16940; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-16940; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-16940,EBI-19054; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-16940,EBI-8050; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-16940; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-295695,EBI-16940; Score: 0.40
DE  Interaction: P18888; IntAct: EBI-17550,EBI-16940; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-3903,EBI-16940; Score: 0.35
DE  Interaction: P41543; IntAct: EBI-12651,EBI-16940; Score: 0.35
DE  Interaction: P41811; IntAct: EBI-4898,EBI-16940; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-861,EBI-16940; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-340,EBI-16940; Score: 0.27
DE  Interaction: Q04491; IntAct: EBI-16529,EBI-16940; Score: 0.53
DE  Interaction: P32582; IntAct: EBI-4167,EBI-16940; Score: 0.27
DE  Interaction: P40018; IntAct: EBI-432,EBI-16940; Score: 0.35
DE  Interaction: P53919; IntAct: EBI-16940,EBI-28887; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-16940; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-16940; Score: 0.32
GO  GO:0097042;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0017056;
GO  GO:0034629;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10684247};
SQ  MQPFDSGHDDLVHDVVYDFYGRHVATCSSDQHIKVFKLDKDTSNWELSDSWRAHDSSIVAIDWASPEYGRIIASASYDKT
SQ  VKLWEEDPDQEECSGRRWNKLCTLNDSKGSLYSVKFAPAHLGLKLACLGNDGILRLYDALEPSDLRSWTLTSEMKVLSIP
SQ  PANHLQSDFCLSWCPSRFSPEKLAVSALEQAIIYQRGKDGKLHVAAKLPGHKSLIRSISWAPSIGRWYQLIATGCKDGRI
SQ  RIFKITEKLSPLASEESLTNSNMFDNSADVDMDAQGRSDSNTEEKAELQSNLQVELLSEHDDHNGEVWSVSWNLTGTILS
SQ  SAGDDGKVRLWKATYSNEFKCMSVITAQQ
//
ID  Q9V466;
PN  Nuclear pore complex protein Nup107;
GN  Nup107;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:31784359}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:27402967}. Nucleus membrane {ECO:0000269|PubMed:26485283}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18562695}. Chromosome {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:31784359}. Nucleus matrix {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure (By similarity). During syncytial embryo and larval neuroblast mitosis localizes to the nuclear envelope in interphase, accumulates in the nucleus in prometaphase, localizes to the spindle envelope in metaphase and then to condensing chromatin in telophase (PubMed:18562695). In spermatocytes, detected in the nuclear matrix by the nuclear envelope in metaphase I, and in the spindle envelope in premeiotic nuclei and during anaphase I (PubMed:27402967). Colocalizes with type-B lamin Lam throughout meiosis I (PubMed:27402967). Unlike in mammals, does not localize to kinetochore (PubMed:18562695, PubMed:27402967). Can localize to the nuclear lumen proximal to the inner nuclear membrane (PubMed:31784359). {ECO:0000250|UniProtKB:P57740, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9V466;
DR  Pfam: PF04121;
DE  Function: Plays a role in nuclear pore complex (NPC) assembly and maintenance (PubMed:20547758). Required for nuclear import of Mad (PubMed:20547758). Mediates the association between the nuclear pore complex and a subset of active chromatin regions adjacent to lamin- associated domains (PubMed:31784359). Plays a role in double strand break repair by relocalizing the heterochromatic double strain breaks (DSBs) to the nuclear periphery as part of the homologous recombination (HR) repair process (PubMed:26502056). Regulates cytokinesis during spermatocyte meiosis by maintaining type-B lamin Lam localization to the spindle envelope (PubMed:27402967). Regulates female gonad development and oogenesis (PubMed:26485283). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26485283, ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-89961; Score: 0.35
DE  Interaction: Q95TK5; IntAct: EBI-89961,EBI-189908; Score: 0.37
DE  Interaction: Q9W2N5; IntAct: EBI-89961,EBI-114432; Score: 0.37
DE  Interaction: P02844; IntAct: EBI-89961,EBI-192398; Score: 0.37
DE  Interaction: Q9VWG6; IntAct: EBI-89961,EBI-148155; Score: 0.37
DE  Interaction: O44424; IntAct: EBI-89961,EBI-99053; Score: 0.37
DE  Interaction: P18459-2; IntAct: EBI-89961,EBI-198251; Score: 0.37
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0000724;
GO  GO:0030703;
GO  GO:0008585;
GO  GO:0007112;
GO  GO:0007110;
GO  GO:0006406;
GO  GO:1900182;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0046822;
GO  GO:0006355;
GO  GO:0048137;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADSPFPRSSRSGLLRTTLNSSMPPQNLSHSLLILEKSNAEQNELSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQ
SQ  EAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARQRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTL
SQ  GGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAP
SQ  VREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRR
SQ  DIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNG
SQ  RMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQ
SQ  ERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRL
SQ  AHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYG
SQ  SVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVK
SQ  EQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLSWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADE
SQ  ISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
//
ID  O95259;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  KCNH1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:21559285, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Nucleus inner membrane {ECO:0000269|PubMed:21559285}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Cell junction, synapse, postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000269|PubMed:22841712}. Note=Perinuclear KCNH1 is located to NPC-free islands.
DR  UNIPROT: O95259;
DR  UNIPROT: B1AQ26;
DR  UNIPROT: O76035;
DR  UNIPROT: Q14CL3;
DR  PDB: 5J7E;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DR  OMIM: 135500;
DR  OMIM: 603305;
DR  OMIM: 611816;
DR  DisGeNET: 3756;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9738473, PubMed:11943152, PubMed:10880439, PubMed:22732247, PubMed:25556795, PubMed:27325704, PubMed:27005320, PubMed:27618660). Channel properties are modulated by subunit assembly (PubMed:11943152). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}.
DE  Disease: Temple-Baraitser syndrome (TMBTS) [MIM:611816]: A developmental disorder characterized by intellectual disability, epilepsy, hypoplasia or aplasia of the thumb and great toe nails, and broadening and/or elongation of the thumbs and halluces, which have a tubular aspect. Some patients show facial dysmorphism. {ECO:0000269|PubMed:25420144}. Note=The disease is caused by mutations affecting the gene represented in this entry. Zimmermann-Laband syndrome 1 (ZLS1) [MIM:135500]: A form of Zimmermann-Laband syndrome, a rare developmental disorder characterized by facial dysmorphism with bulbous nose and thick floppy ears, gingival enlargement, hypoplasia or aplasia of terminal phalanges and nails, hypertrichosis, joint hyperextensibility, and hepatosplenomegaly. Some patients manifest intellectual disability with or without epilepsy. ZLS1 inheritance is autosomal dominant. {ECO:0000269|PubMed:25915598}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00560; IntAct: EBI-727004,EBI-2909270; Score: 0.56
DE  Interaction: Q7L8L6; IntAct: EBI-747570,EBI-2909270; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-741158,EBI-2909270; Score: 0.56
GO  GO:0030673;
GO  GO:0030054;
GO  GO:0009986;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0005637;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0008076;
GO  GO:0071889;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:0042802;
GO  GO:0044325;
GO  GO:1902936;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0007520;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0006813;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
GO  GO:0001964;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q63472};
SQ  MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTI
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA
SQ  FMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSI
SQ  GDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFA
SQ  VAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICP
SQ  KDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGK
SQ  GDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEER
SQ  MKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSF
SQ  QAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSC
SQ  DSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTS
SQ  RRSSQSPQELFEISRPQSPESERDIFGAS
//
ID  P32500;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex. Spindle pole body, central plaque.
DR  UNIPROT: P32500;
DR  UNIPROT: D6VZE3;
DR  Pfam: PF09531;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envelope, thus allowing for the assembly of the nucleoplasmic SPB side. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:15075274, ECO:0000269|PubMed:9864355}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07457; IntAct: EBI-31563,EBI-11950; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11950; Score: 0.35
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11950; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-11730,EBI-11950; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-11950,EBI-3035; Score: 0.67
DE  Interaction: Q03790; IntAct: EBI-11950,EBI-27321; Score: 0.55
DE  Interaction: P16521; IntAct: EBI-11950,EBI-6338; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-11950,EBI-21409; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-11950,EBI-20254; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-11950,EBI-6314; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-11950,EBI-7218; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-11950,EBI-16037; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-11950,EBI-5687; Score: 0.35
DE  Interaction: P14742; IntAct: EBI-11950,EBI-7557; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-11950,EBI-2218; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11950; Score: 0.40
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005816;
GO  GO:0017056;
GO  GO:0071790;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVT
SQ  RKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVT
SQ  DADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFI
SQ  TFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGN
SQ  TWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDE
SQ  SPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSD
SQ  ESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSIC
SQ  ALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLA
SQ  NWFLEVYASGNPNAT
//
ID  Q9VXE6;
PN  Nuclear pore complex protein Nup153;
GN  Nup153;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:17682050}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:18562695}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Chromosome {ECO:0000269|PubMed:20174442}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18562695}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:17682050). Localized at the spindle in mitotic syncytial embryos (PubMed:18562695). Associates with chromatin (PubMed:20174442). {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:20174442, ECO:0000303|PubMed:17682050}.
DR  UNIPROT: Q9VXE6;
DR  UNIPROT: Q1LZ48;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:17682050). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:17682050). Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in a Importin alpha/Importin beta receptor-dependent manner (PubMed:17682050). Required for nuclear import of Mad (PubMed:20547758). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:20174442). Binds chromatin to nucleoporin- associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Mtor, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). May play a role in double strand break DNA repair (PubMed:26502056). {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26502056}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-178209; Score: 0.35
DE  Interaction: P07207; IntAct: EBI-103438,EBI-178209; Score: 0.46
DE  Interaction: M9NFI9; IntAct: EBI-9933576,EBI-178209; Score: 0.46
DE  Interaction: Q9GQR5; IntAct: EBI-133338,EBI-178209; Score: 0.35
DE  Interaction: Q9VXY7; IntAct: EBI-126312,EBI-178209; Score: 0.35
DE  Interaction: Q9VDW6; IntAct: EBI-110986,EBI-178209; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-3411876,EBI-178209; Score: 0.35
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-178209; Score: 0.35
DE  Interaction: Q9VJ30; IntAct: EBI-154050,EBI-178209; Score: 0.35
DE  Interaction: Q9W258; IntAct: EBI-3417884,EBI-178209; Score: 0.35
DE  Interaction: P40798; IntAct: EBI-178209,EBI-88209; Score: 0.37
DE  Interaction: Q9VPG5; IntAct: EBI-178209,EBI-180337; Score: 0.37
DE  Interaction: Q9VVQ1; IntAct: EBI-178209,EBI-173837; Score: 0.37
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005719;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0031490;
GO  GO:0046872;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0006974;
GO  GO:0006325;
GO  GO:0006338;
GO  GO:0007549;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0045944;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDAQEQRESSQAELAKKHPLTPLKELPEESEEEEEEEDESSAGALRESDSNNSIMGKMKMRVSSILPASLSGWFSPSSK
SQ  DGNDALSSPANLRQSQPRQSNGRLTTKRKRGRRRIMLAEVDADAADDLDDGSDAKGLNYEEVALADNIAEHDLAAEDEQT
SQ  RRSEYNVFLLRKRAGAVAAAGGDEDEAEEDELEEDDEDGDEEDDDEEQENLQQSAAVQTKRRRLELETPVNLPNMRRLPL
SQ  LSSTPAAPLAAATSSSSSQMYKGVSHIAPHRRNHLNLYGSQRQREPAYNFFTGNEAAEGSTGDLPHSIRRSLNIPFGGSS
SQ  TATSYNNSLSSLPNHKRPSLIGKQTHRRDLTMDETGTGPAMSSEEHLNHLLRISRTNNNTSNNNNNNNNNNNVIETKTRR
SQ  SELSAAAGGCGDSQSESDMNEYHDNGEGHDGLRPSHYNSNSNLEFYGNLQSSKSIFNRSNTAAQQSHRNSTWSLNSLTQR
SQ  RRFNASIYGSTSALSDSRLLSGSASNSGSASASSSPFYQGRTTFGGNSGNNRLFSRSNLSSSAASSMLGLNSAGSSPAHQ
SQ  LHASMTGGIGYGMKAVDMRPSDSGSLAETSVGQGGSKKPGTGLSNTTMRILNLLESYSTPLIDAKRMGSSIKEHQSSRQQ
SQ  RQGTPATPYLRSTSASRNVSVPNHINELAELRSNKLLVPTMQQLLERRRLHRVTQNSRDVVHSQNVRAGGENNQEKPKPT
SQ  APYVAPIDQSANHTQHTNKMRSRLSHQTRNKETRTAEEEAPPPLDLPQISFPDMASAPKFDLIIKPTVPVVSKPSTTDPI
SQ  QSSKSSNTNLSTTNSKQMPNFLANPQPAAPIVNFAANGNVSAISKPSKRTFTFSEPTPLSNFQENCIPKPKINRKYTFSA
SQ  PAPLDDLRITNKQSQPTINGTPSSKEWECDTCMVRNKPEINKCVACETAKPVASAAPVQAPLPPSTAAIDTQSFVGFGDR
SQ  FKKSTTAWECDACMLSNKAEASKCIACETPRKTVAPKVNNFSPLITNAKSNEWECSVCLVRNKVEVSKCVACESAKPGAT
SQ  MALPATSNIAVATPSIITDGFGDRFKKSATAWECDACMLSNKAEASKCIACETPRKSSTPIANSSYPSINNNLPAGSGFD
SQ  ISFTRKANMWECQTCLVMNKSSDEECIACQTPNSQARNSNSESALISSISSSSASFSGSLSRPSSRSSSGSTSTCGSVCS
SQ  GSIVSISSTTESAKALSAKKVPPKPDAGFQQLVAAQKTSTWECEACLAKNDMSRKTCICCEQMMPEAFNPAATTANSAAS
SQ  SVPKFRFGFSHVKEVVKPSVETTTTPAPTSAQFSFGFGQSNQGKDVADSKKTEAPKTFMFGVSKVEEPKTVSFGTGIKET
SQ  TATSSTEATAPTPAAAAPAPVQFVFKAPTTATTASSLTTTISTTSNAPALGGFSFGAPSSSSTVSSSTTSTSANPAAVKP
SQ  MFSWSGAGSAVSSTSSSQQPVAKAPTLGFGVSSSTVTTTTTSTKVFAFTPASGLDPAAATSAPAAGAGFSFGSQSKPATT
SQ  QNTGTFFFGQPTAVAPATPTNPSVSSIFGAPATSTTASTSVSATTSTSTANAIASSFAPTSTPQLFGNWGEKKTDLTTFG
SQ  ASSGSGTTTTPSFGWSSNGDAAKSNSAAVGSAAVPSSSASTMATPIFGSSSMFGPSSSSNNTTSTSTTSLPFGSAATTAA
SQ  TTPAGGNAALTGLFGNVGNSLAGVGAPVATTPAATAAAPLTNIFGNPTPVAAAAPVFGSGSTIPSAGFGAPAAAAPLAAP
SQ  ALPGAFNFGGATAATPAASSAPFVFGSSTNEPLAKPSFNFTGSAASSTAPAPAFNFTANTAATNNPSGGDSTPNANALFQ
SQ  FSATSTAPANIFAFNPPAAGNSAQSSQTARRKIRAPVRRLPPR
//
ID  H2QII6;
PN  E3 SUMO-protein ligase RanBP2;
GN  RANBP2;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:22959972}. Nucleus membrane {ECO:0000269|PubMed:22959972}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22959972}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}.
DR  UNIPROT: H2QII6;
DR  PDB: 4GA1;
DR  PDB: 4GA2;
DR  Pfam: PF12185;
DR  Pfam: PF00160;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS00170;
DR  PROSITE: PS50072;
DR  PROSITE: PS50196;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (By similarity). Binds single- stranded RNA (in vitro) (PubMed:22959972). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:22959972}.
DE  Reference Proteome: Yes;
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0003755;
GO  GO:0008536;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0043547;
GO  GO:0006457;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRSKADVERYIASVQGSTPSPRQKSIKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAV
SQ  ECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAVYKLKEQLLDCEGEDGWNKLFDLIQSELYV
SQ  RPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYA
SQ  NLMLLTLSTRDVQESRELLESFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCY
SQ  LIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLREIVETFANKSGQSALYDALFSSQSPKDTSF
SQ  LGSDDIGNIDVREPELEDLARYDVGAIRAHDGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPQETSRLETNAPESIC
SQ  ILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNAAKLRLLVQHEIN
SQ  TLRAQEKHGLQPALLVHWAKCLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQA
SQ  SEIVEYEEDAHITFAILDVVNGNIEDAMTAFESIQSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIK
SQ  IIDDSDSNLSVVKKLPVPLESVKEMLKSVMQELEAYSEGGPLYTNGSLRNADSEIKHSTPSHTRYSLSPSKSYKYSPKTP
SQ  PRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQS
SQ  PAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDD
SQ  YFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSN
SQ  DGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQ
SQ  KNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAK
SQ  LFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQ
SQ  LAIRFKTPEEAALFKCKFEEAQSILKAPGTNVATASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQFAKKEGSWWHCNS
SQ  CSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQN
SQ  TKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPAS
SQ  FKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFE
SQ  GMFTKKEGQWDCSVCLVRNEASATKCVACQNPGKQNQTTSAVSTPASSETSRAPKSGFEGMFTKKEGQWDCSVCLVRNEA
SQ  SATKCIACQSPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAIS
SQ  TPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSPGSQVGTG
SQ  FKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENDT
SQ  GFQAQDISGQKNGSGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDD
SQ  DAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQV
SQ  LKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDT
SQ  GRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSS
SQ  SSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLV
SQ  EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER
SQ  VWLWTAYDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERT
SQ  DVTQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNTSATGSLFGFSFNAPLKSNNSET
SQ  SSVAQSGSESKVEPNKCELSKNSDIEQSSDSKVKNLSASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTP
SQ  TAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLEGSEKCRPLEENTADNEKECIIVWEKKPTV
SQ  EEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSIT
SQ  KSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVF
SQ  GTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKI
SQ  LWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC
SQ  QQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDF
SQ  VCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFFITLKKAELLDFKHVVFGFVKDGMDTVK
SQ  KIESFGSPKGSVCRRITITECGQI
//
ID  Q9V463;
PN  Nuclear pore complex protein Nup154;
GN  Nup154;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17410542}. Chromosome {ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}. Nucleus {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:9732281}. Nucleus membrane {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral membrane protein {ECO:0000269|PubMed:17410542}; Cytoplasmic side {ECO:0000269|PubMed:17410542}. Nucleus membrane {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral membrane protein {ECO:0000269|PubMed:17410542}; Nucleoplasmic side {ECO:0000269|PubMed:17410542}. Cytoplasm {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353}. Note=Increased localization to chromatin before interphase (PubMed:22718353). Distributed along filamentous structures that extend radially on the nuclear side of the pore complex (PubMed:17410542). {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353}.
DR  UNIPROT: Q9V463;
DR  UNIPROT: O62536;
DR  UNIPROT: O62610;
DR  UNIPROT: O62613;
DR  UNIPROT: Q9VKL5;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Component of the nuclear pore complex (PubMed:17410542). Has a role in the organization of the inner nuclear membrane proteins at the nuclear envelope (PubMed:22718353). In germ cells, plays a role in the nuclear localization of components of the dpp signaling pathways, such as Medea and phosphorylated Mad (PubMed:21696798). Binds to chromatin, and together with Nup62 and Nup93-1, contributes to karyosome morphology and chromatin organization including attachment to the nuclear envelope in oocytes and nurse cells (PubMed:22718353, PubMed:26341556). Has a role in female fertility including egg chamber development; in nurse cells, has a role in the organization of F-actin in subcortical and cytoplasmic actin filaments important for the transfer of cytoplasm from nurse cells to the growing oocytes (PubMed:9732281, PubMed:10511559, PubMed:17410542, PubMed:17277377). Has a role in male spermatogenesis and fertility (PubMed:9732281, PubMed:10511559). Has a role in germ line cell proliferation (PubMed:21696798). {ECO:0000269|PubMed:10511559, ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:21696798, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:9732281, ECO:0000303|PubMed:17410542}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-118619; Score: 0.35
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-118619; Score: 0.35
DE  Interaction: Q9VTU4; IntAct: EBI-118619,EBI-178321; Score: 0.37
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0007015;
GO  GO:0055050;
GO  GO:0007303;
GO  GO:0001654;
GO  GO:0007281;
GO  GO:0007295;
GO  GO:0007140;
GO  GO:0051028;
GO  GO:0001555;
GO  GO:0030715;
GO  GO:0030717;
GO  GO:0048477;
GO  GO:1905938;
GO  GO:0042307;
GO  GO:1900182;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0045477;
GO  GO:1905879;
GO  GO:1905475;
GO  GO:0006405;
GO  GO:0007283;
GO  GO:0000972;
GO  GO:0035220;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17410542};
SQ  MTLPQAQLDFFTTATSMLEWHYNLERNKPGLLELTGVSQHGRATMSGLNDYDYQSLSFLKSDRTHNLQQMRTVTKSAIPN
SQ  EILEHFKHIKCHCTMGLFPEIGRAWLTIDSEIYIWTFNQTRDVAYYDGLSHLIVSVGLVKPKPGVFVQDVKYLLVLTTPI
SQ  EVIVLGVTFGESSYNEMQLMNRPVFVIGTDNVSISVIKGTDDGRIFLGGRDGCLYEIYYQAESSWFGKRCKKINLSQGLV
SQ  SYMVPSFLKVFSEVDPIEHIEIDNSRKLLYVLTEKGVIEAWDISTSYTTARRLGRITQNDITNQAVSLITTVDPSIFKSV
SQ  KAICPLSADDADKLHLVAVTQCGVRLFFSTTSLNVKQQFGPAVPCSPGENTGFGQPAVQPPLSPNAEAPKGLYLLHVRLP
SQ  PGYTPNATTNKPKQVHAAHYTEGTMLMITTQQHEQDLLWSLSSAPSVNFTYLVESTALESLDGVVWGLAEVHEPSTPQRK
SQ  SPLNSARHARKVALLTNQGTHIIEVLKMVDVLRQILLSCNGPHHEEVKMFFQSQNQREACVTALLLATSDTYRGSDVALW
SQ  AAQAFMLYGGEPCYQHQKFLNASNRNMANQTLGPNTTNVRERQSMFMSTPMPNSVANSPVGFPGSQFNQPISPIGNMQPP
SQ  QVAVSNENSPIVFSAKHDGLYMYVSRMLHSVWQMRCVNEQFCSNLSQSECALLLSDLRSLRSFLEVHSVHDISSTTRVSF
SQ  DNHLDRTNSYNTIMMGNTLLPIPEQRVLSEQAQVEETRSLSALNLFVKHACEVISLWNILNSHSFQLICVQLSPEHQKLL
SQ  TCSTFRDLLITRSEVCAFLIISLINLYLKDAAGVSEVSKNLRENCPNLYRHEDDVTYKATELLMNAKNCTSATEKEHMLR
SQ  TTLHMCKEAAPTLPLHSICMQFISADFFEGVIELSAVCASKSDPEEVGVHFYNNGEPADDREGYTCFATRMAYYKEVQLM
SQ  LDHIYQRVCNKTHVQDKSINPLKGTAKASDAKNGATQTIPKIVAHTLKVKDPLIHITLYEWLLAHDMLKELLDVVEPSLG
SQ  EFLRRSVSQNVDNVVLIDLLWKYYEKNSHHSQAAHILDNLAMTRSENINLEQRIEYLVRAVMCMRNGNVGSSLSNGIFLK
SQ  ELEDKLDIARVQKSVLAAMTELASDKLEAATAVKELNYALYDITQLYQHFAEPFDLWECQLSILNCSHHNDPLLIESVWG
SQ  QIINSVVDKPGTTSERCNRLFTKIEILVREYGESGVCFPFAFLIRELEVKACQLRFPEGIVPEKLVSMNLDIELLLEYYS
SQ  RMISMNERVWANEGNEWHLIQSVIRVVSLLADNAQSIWYRSKRRIVGKAQDIVAGCLNICYQKPDTNRLQHSLKELQSQL
SQ  QRLLI
//
ID  Q02199;
PN  Nucleoporin NUP49/NSP49;
GN  NUP49;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q02199;
DR  UNIPROT: D6VTY0;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9971735}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12315,EBI-12265; Score: 0.68
DE  Interaction: P34077; IntAct: EBI-12315,EBI-12056; Score: 0.62
DE  Interaction: P40368; IntAct: EBI-12331,EBI-12315; Score: 0.37
DE  Interaction: P48837; IntAct: EBI-12324,EBI-12315; Score: 0.90
DE  Interaction: P49686; IntAct: EBI-12310,EBI-12315; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-11730,EBI-12315; Score: 0.37
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-12315; Score: 0.59
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-12315; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-12315,EBI-11698; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12315; Score: 0.35
DE  Interaction: P38265; IntAct: EBI-21579,EBI-12315; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-12315,EBI-14372; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12315,EBI-8603; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-12315,EBI-9428; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12315; Score: 0.35
DE  Interaction: Q05166; IntAct: EBI-12315,EBI-3035; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-12315,EBI-741048; Score: 0.37
DE  Interaction: Q06411; IntAct: EBI-12315,EBI-576; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12315; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12315; Score: 0.32
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0000055;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGS
SQ  ATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSL
SQ  FGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQ
SQ  QLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSES
SQ  ATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNG
SQ  IDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI
//
ID  Q9BVL2;
PN  Nucleoporin p58/p45;
GN  NUP58;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}.
DR  UNIPROT: Q9BVL2;
DR  UNIPROT: A6NI12;
DR  UNIPROT: B4DZJ1;
DR  UNIPROT: O43160;
DR  UNIPROT: Q5JRG2;
DR  UNIPROT: Q5JRG5;
DR  PDB: 4JO7;
DR  PDB: 4JO9;
DR  PDB: 4JQ5;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  OMIM: 607615;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70581}.
DE  Reference Proteome: Yes;
DE  Interaction: O15504; IntAct: EBI-2811583,EBI-2515057; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-2811583,EBI-347978; Score: 0.80
DE  Interaction: P49792; IntAct: EBI-2811583,EBI-973138; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-2811583,EBI-295687; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-2811583,EBI-1049404; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-2811583; Score: 0.87
DE  Interaction: Q8N1F7; IntAct: EBI-2811583,EBI-1042703; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-2811583,EBI-9050429; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-2811583,EBI-1045046; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-2811583,EBI-466029; Score: 0.55
DE  Interaction: Q13077; IntAct: EBI-2811583,EBI-359224; Score: 0.84
DE  Interaction: Q9P2A4; IntAct: EBI-2811583,EBI-742038; Score: 0.78
DE  Interaction: Q9UMX0-2; IntAct: EBI-2811583,EBI-10173939; Score: 0.56
DE  Interaction: P25054; IntAct: EBI-727707,EBI-2811583; Score: 0.37
DE  Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-2811583; Score: 0.35
DE  Interaction: Q99988; IntAct: EBI-2811583,EBI-2116863; Score: 0.35
DE  Interaction: Q969P6-2; IntAct: EBI-2811583,EBI-10988354; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-2811583,EBI-2689235; Score: 0.35
DE  Interaction: Q9BTX1-2; IntAct: EBI-2811583,EBI-10966386; Score: 0.35
DE  Interaction: P11532; IntAct: EBI-2811583,EBI-295827; Score: 0.35
DE  Interaction: O15440; IntAct: EBI-2811583,EBI-2880066; Score: 0.35
DE  Interaction: Q96A73-3; IntAct: EBI-2811583,EBI-11040309; Score: 0.35
DE  Interaction: P52948-5; IntAct: EBI-2811583,EBI-5280407; Score: 0.35
DE  Interaction: Q96BD5-2; IntAct: EBI-2811583,EBI-10981746; Score: 0.35
DE  Interaction: P35658-2; IntAct: EBI-2811583,EBI-10969485; Score: 0.35
DE  Interaction: Q14746-2; IntAct: EBI-2811583,EBI-10233912; Score: 0.35
DE  Interaction: Q81XC3; IntAct: EBI-2809705,EBI-2811583; Score: 0.37
DE  Interaction: Q9BYV2; IntAct: EBI-2811583,EBI-2130429; Score: 0.37
DE  Interaction: Q7Z3B4-1; IntAct: EBI-22121524,EBI-2811583; Score: 0.37
DE  Interaction: O75830; IntAct: EBI-2811583,EBI-750144; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475877,EBI-2811583; Score: 0.35
DE  Interaction: Q96KN3; IntAct: EBI-2692890,EBI-2811583; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-712648,EBI-2811583; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-1049638,EBI-2811583; Score: 0.56
DE  Interaction: P55347; IntAct: EBI-1373569,EBI-2811583; Score: 0.56
DE  Interaction: O14770-4; IntAct: EBI-8025850,EBI-2811583; Score: 0.56
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-2811583; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-3044087,EBI-2811583; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-947187,EBI-2811583; Score: 0.56
DE  Interaction: Q96JB2-2; IntAct: EBI-9091495,EBI-2811583; Score: 0.56
DE  Interaction: Q96NL6; IntAct: EBI-2514016,EBI-2811583; Score: 0.35
DE  Interaction: Q9NYP9; IntAct: EBI-1104552,EBI-2811583; Score: 0.56
DE  Interaction: Q7Z3Y7; IntAct: EBI-11980489,EBI-2811583; Score: 0.56
GO  GO:0043657;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0042306;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P70581};
SQ  MSTGFSFGSGTLGSTTVAAGGTSTGGVFSFGTGASSNPSVGLNFGNLGSTSTPATTSAPSSGFGTGLFGSKPATGFTLGG
SQ  TNTGIATTITTGLTLGTPATTSAATTGFSLGFNKPAASATPFALPITSTSASGLTLSSALTSTPAASTGFTLNNLGGTTA
SQ  TTTTASTGLSLGGALAGLGGSLFQSTNTGTSGLGQNALGLTLGTTAATSTAGNEGLGGIDFSSSSDKKSDKTGTRPEDSK
SQ  ALKDENLPPVICQDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAANGIQRNTLNIDKLKIETAQELK
SQ  NAEIALRTQKTPPGLQHEYAAPADYFRILVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALA
SQ  AQLQSIHENVKVLKEQYLGYRKMFLGDAVDVFETRRAEAKKWQNTPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGP
SQ  QPSLGVSFGTPFGSGIGTGLQSSGLGSSNLGGFGTSSGFGCSTTGASTFGFGTTNKPSGSLSAGFGSSSTSGFNFSNPGI
SQ  TASAGLTFGVSNPASAGFGTGGQLLQLKKPPAGNKRGKR
//
ID  Q96HA1;
PN  Nuclear envelope pore membrane protein POM 121;
GN  POM121;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
DR  UNIPROT: Q96HA1;
DR  UNIPROT: A6NFS9;
DR  UNIPROT: A8CDT4;
DR  UNIPROT: A8K933;
DR  UNIPROT: A8MXF9;
DR  UNIPROT: O75115;
DR  UNIPROT: Q96DI0;
DR  UNIPROT: Q9H9X1;
DR  UNIPROT: Q9Y2N3;
DR  UNIPROT: Q9Y4S7;
DR  PDB: 5T6W;
DR  OMIM: 615753;
DR  DisGeNET: 9883;
DE  Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.
DE  Reference Proteome: Yes;
DE  Interaction: O60711; IntAct: EBI-739990,EBI-744222; Score: 0.37
DE  Interaction: P02545; IntAct: EBI-351935,EBI-739990; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-286779,EBI-739990; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-739990,EBI-1046596; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-739990; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-739990; Score: 0.40
DE  Interaction: P54253; IntAct: EBI-739990,EBI-930964; Score: 0.49
DE  Interaction: Q9NSC5; IntAct: EBI-748420,EBI-739990; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-739990,EBI-712648; Score: 0.67
DE  Interaction: P51116; IntAct: EBI-739990,EBI-740459; Score: 0.67
DE  Interaction: Q6ZW49-2; IntAct: EBI-10236271,EBI-739990; Score: 0.56
DE  Interaction: Q8IYF3; IntAct: EBI-739990,EBI-742397; Score: 0.67
DE  Interaction: Q8TAP6; IntAct: EBI-739990,EBI-742887; Score: 0.56
DE  Interaction: Q93062; IntAct: EBI-739990,EBI-740322; Score: 0.67
DE  Interaction: P25054; IntAct: EBI-739990,EBI-727707; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-739990; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-739990; Score: 0.35
DE  Interaction: P42262; IntAct: EBI-3909876,EBI-739990; Score: 0.35
DE  Interaction: Q8CI51; IntAct: EBI-299301,EBI-739990; Score: 0.35
DE  Interaction: P55345; IntAct: EBI-78458,EBI-739990; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-2903122,EBI-739990; Score: 0.35
DE  Interaction: O14595; IntAct: EBI-2802973,EBI-739990; Score: 0.35
DE  Interaction: Q9UN86-2; IntAct: EBI-11035716,EBI-739990; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-6153153,EBI-739990; Score: 0.35
DE  Interaction: P69961; IntAct: EBI-2847280,EBI-739990; Score: 0.37
DE  Interaction: Q8D014; IntAct: EBI-2840312,EBI-739990; Score: 0.37
DE  Interaction: Q15654; IntAct: EBI-739990,EBI-742327; Score: 0.37
DE  Interaction: P46976; IntAct: EBI-739990,EBI-740533; Score: 0.37
DE  Interaction: P25963; IntAct: EBI-739990,EBI-307386; Score: 0.37
DE  Interaction: Q08379; IntAct: EBI-739990,EBI-618309; Score: 0.37
DE  Interaction: P63010; IntAct: EBI-739990,EBI-432924; Score: 0.37
DE  Interaction: P14136; IntAct: EBI-739990,EBI-744302; Score: 0.37
DE  Interaction: P36406; IntAct: EBI-739990,EBI-740098; Score: 0.37
DE  Interaction: Q53EZ4; IntAct: EBI-739990,EBI-747776; Score: 0.37
DE  Interaction: Q9Y4F3; IntAct: EBI-739990,EBI-5235902; Score: 0.27
DE  Interaction: Q504Q3; IntAct: EBI-739990,EBI-1058976; Score: 0.27
DE  Interaction: Q2M3V2; IntAct: EBI-739990,EBI-8832444; Score: 0.27
DE  Interaction: P42694; IntAct: EBI-739990,EBI-1210654; Score: 0.27
DE  Interaction: Q6UXL0; IntAct: EBI-14022792,EBI-739990; Score: 0.35
DE  Interaction: A4D1S0; IntAct: EBI-21511322,EBI-739990; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-2802853,EBI-739990; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-9008641,EBI-739990; Score: 0.35
DE  Interaction: O15482; IntAct: EBI-751954,EBI-739990; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-7810230,EBI-739990; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-2129267,EBI-739990; Score: 0.35
DE  Interaction: Q9NRJ7; IntAct: EBI-21584519,EBI-739990; Score: 0.35
DE  Interaction: P36941; IntAct: EBI-3509981,EBI-739990; Score: 0.35
DE  Interaction: Q96JJ6; IntAct: EBI-2847044,EBI-739990; Score: 0.35
DE  Interaction: Q504Y0-3; IntAct: EBI-21572145,EBI-739990; Score: 0.35
DE  Interaction: Q96G97-3; IntAct: EBI-21504572,EBI-739990; Score: 0.35
DE  Interaction: Q8IV45; IntAct: EBI-12238241,EBI-739990; Score: 0.35
DE  Interaction: Q9Y5P4; IntAct: EBI-739994,EBI-739990; Score: 0.37
GO  GO:0005789;
GO  GO:0043657;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006405;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPAAAAAGAGERRRPIASVRDGRGRGCGGPARAVLLGLSLVGLLLYLVPAAAALAWLTVGATAAWWGLSREPRGSRPLS
SQ  SFVRKARHRRPLSSFVRKARHRRTLFASPLAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAAAPEGQDLRD
SQ  RPGRRPPARPAPRSPPPRSPPPRSPPPSPPTHRAHHVYPSLPTPLLRPSRRPSPRDCGTLPNRFVITPRRRYPIHQAQYS
SQ  CLGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKE
SQ  KKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVANGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGA
SQ  YASGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADRESQGEK
SQ  AADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASN
SQ  SVTETPPITQPSFTFTLPAAAPASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLS
SQ  QSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPA
SQ  ASSAPPMFKPIFTAPPKSEKEGPTPPGPSVTATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATA
SQ  PTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGS
SQ  IFQFGKPPALPTTTTVTTFSQSLHTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPL
SQ  PSYPGANPQPAFGAAEGQPPGAAKPALAPSFGSSFTFGNSAAPAAAPTPAPPSMIKVVPAYVPTPIHPIFGGATHSAFGL
SQ  KATASAFGAPASSQPAFGGSTAVFFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGS
SQ  STTTGAFSFGAGQSGSTATSTPFAGGLGQNALGTTGQSTPFAFNVSSTTESKPVFGGTATPTFGLNTPAPGVGTSGSSLS
SQ  FGASSAPAQGFVGVAPFGSAALSFSIGAGSKTPGARQRLQARRQHTRKK
//
ID  P20240;
PN  Otefin;
GN  Ote;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:27174470, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}; Peripheral membrane protein {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347}; Nucleoplasmic side {ECO:0000269|PubMed:2517292}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8999964}. Cytoplasm {ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:9199347}. Chromosome {ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22751930}. Note=Component of the spindle envelope during early mitotic cycles (PubMed:2186029, PubMed:2517292). Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles (PubMed:22751930, PubMed:2517292). At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes (PubMed:22751930, PubMed:2517292). At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area (PubMed:22751930). During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body (PubMed:22751930). At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope (PubMed:9199347). Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347). {ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:9199347}.
DR  UNIPROT: P20240;
DR  UNIPROT: Q9V8E5;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:2186029, PubMed:9199347, PubMed:18410727, PubMed:22751930). Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis (PubMed:9199347, PubMed:22751930). Essential for differentiation of certain tissues and the maintenance of progenitor cell populations (PubMed:18410727, PubMed:24700158, PubMed:23806619, PubMed:27174470). Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche (PubMed:18410727, PubMed:23806619, PubMed:27174470). This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation (PubMed:18410727, PubMed:23806619). During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1 (PubMed:24700158). Also has a redundant but important role with bocks during larval development (PubMed:24700158). {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:23806619, ECO:0000269|PubMed:24700158, ECO:0000269|PubMed:27174470, ECO:0000269|PubMed:9199347}.
DE  Reference Proteome: Yes;
DE  Interaction: P08928; IntAct: EBI-115143,EBI-188444; Score: 0.50
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-115143; Score: 0.35
DE  Interaction: P23572; IntAct: EBI-108689,EBI-115143; Score: 0.27
DE  Interaction: Q94524; IntAct: EBI-115143,EBI-158251; Score: 0.37
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0005815;
GO  GO:0005641;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0003714;
GO  GO:0008134;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0030718;
GO  GO:0060250;
GO  GO:0045892;
GO  GO:0031468;
GO  GO:0048477;
GO  GO:0030513;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTP
SQ  VDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERK
SQ  VVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKV
SQ  VEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANEL
SQ  SDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQK
SQ  YHIKSKLFIVLLVLLLIGVYYIFY
//
ID  Q09601;
PN  Nucleoporin NUP35;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000269|PubMed:12937276}.
DR  UNIPROT: Q09601;
DR  UNIPROT: O62340;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (By similarity). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). Required for the proper organization of chromosomes on the mitotic spindle during anaphase (PubMed:28122936). {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:28122936}.
DE  Reference Proteome: Yes;
DE  Interaction: Q09601-1; IntAct: EBI-6455756,EBI-2004755; Score: 0.37
DE  Interaction: Q9BKT9; IntAct: EBI-2004755,EBI-2005827; Score: 0.37
DE  Interaction: Q95Y13; IntAct: EBI-6456240,EBI-2004755; Score: 0.37
DE  Interaction: H2KYA1; IntAct: EBI-11466183,EBI-2004755; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0009792;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006997;
GO  GO:0007096;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSHLNQNTSGRHNSMDLNNSSISNFGTPVEQSTPALLFGKRKATVPSSYTASPLNTASAPCSDIFAVSAPAVPQHLKDT
SQ  PGSKSVHWSPSLVQSGEKSAAQTQNTPANLSFGGNSSFSAPTKPAPQSIQTSSFGGQAMHAPPLRSLRDKVEPAKKISRR
SQ  NTFTARSTPLSTPITQRVTSRLAEAEEQPMEEEADAADTWVTVFGFQPSQVSILLNLFSRHGEVVSHQTPSKGNFIHMRY
SQ  SCVTHAQQAISRNGTLLDQDTFIGVVQCTNKDVINGSASGIVARSSNIAAAANRSASMYNSFVENDMADQSVNHNENSVL
SQ  NSSNVFDANNSLNSSRISVRSGVGMRPLAADQRTNILQGTPSVRKAPDGLLNKFWNTIGLN
//
ID  Q9XTB5;
PN  LEM protein 2;
GN  lem;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}; Multi-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}. Chromosome {ECO:0000269|PubMed:16950114}. Note=Remains in the nuclear envelope until mid-late anaphase (PubMed:10982402). Requires mel-28 for chromatin reassociation after mitosis and for nuclear envelope localization (PubMed:16950114). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114}.
DR  UNIPROT: Q9XTB5;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Essential protein involved in chromosome segregation and cell division, probably via its interaction with lmn-1, the main component of nuclear lamina. Has some overlapping function with emr-1 (PubMed:12684533). May play a role in radiation-induced DNA damage repair response (PubMed:22383942). {ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:22383942}.
DE  Reference Proteome: Yes;
DE  Interaction: O01971; IntAct: EBI-2535391,EBI-6260308; Score: 0.27
DE  Interaction: Q21443; IntAct: EBI-314110,EBI-2535391; Score: 0.53
DE  Interaction: Q03565; IntAct: EBI-2535603,EBI-2535391; Score: 0.44
GO  GO:0005694;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031490;
GO  GO:0005521;
GO  GO:0001525;
GO  GO:0007059;
GO  GO:0000281;
GO  GO:0030514;
GO  GO:0006997;
GO  GO:1902531;
GO  GO:0010165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVDVEKMSDAELRAELNVRGANVGPVTGTTRSLYEKKLKKLLSGGAKTPARPTVAKPAPKPTPKSAPAPKSPKSPPARRS
SQ  IPRAAATAANSTINSTFNRSEIEEMSDSDDDMRDDDDDDEEILSPKSKQSSFRSANSTASSVGRGRPVSSTPNKRLSPVY
SQ  KPSPVPKNTPRTTSSSSKTTINTTTTRIPSTPRRITSVPGLITDFTPSFSTFGSDRPGATPPRKSIYTSKVSKVLHDLGN
SQ  TTGEEDDDDEFEGQETSRIIYKTEEPSRRGIVKNAWNKVLGYGFDASKNPGDSYDLRAGASRIRVQKNPRTGKVTVKQTN
SQ  IFNEAIYFALYVILILFVVLGIAYALTTTHRPKTADFSGYWGVLKAAGRDSLNFFYNYAILPVVSLGIFVVLGAGIYFGH
SQ  RKYKEAKEQEEAKLYELIERITELIRESSIDGDPYVSQPHVRDVLFPPAKRRSAELARWEQAVKFIDTNESRVATDVLVL
SQ  PSGNECAVWKWIGNQSQKRW
//
ID  P34077;
PN  Nucleoporin NIC96;
GN  NIC96;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P34077;
DR  UNIPROT: D6VTN2;
DR  PDB: 2QX5;
DR  PDB: 2RFO;
DR  Pfam: PF04097;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import. {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624, ECO:0000269|PubMed:10806080, ECO:0000269|PubMed:11121302, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12496130, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:7828598, ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9017593}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-12056,EBI-12265; Score: 0.35
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-12056; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-11698,EBI-12056; Score: 0.44
DE  Interaction: P48837; IntAct: EBI-12056,EBI-12324; Score: 0.84
DE  Interaction: P51998; IntAct: EBI-12056,EBI-450; Score: 0.37
DE  Interaction: Q00684; IntAct: EBI-4192,EBI-12056; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-12056; Score: 0.35
DE  Interaction: P02293; IntAct: EBI-8088,EBI-12056; Score: 0.35
DE  Interaction: P38265; IntAct: EBI-21579,EBI-12056; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-3824,EBI-12056; Score: 0.35
DE  Interaction: P47054; IntAct: EBI-12056,EBI-25846; Score: 0.55
DE  Interaction: Q03790; IntAct: EBI-12056,EBI-27321; Score: 0.67
DE  Interaction: P52593; IntAct: EBI-11763,EBI-12056; Score: 0.37
DE  Interaction: Q02199; IntAct: EBI-12315,EBI-12056; Score: 0.62
DE  Interaction: P39723; IntAct: EBI-20675,EBI-12056; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12056; Score: 0.35
DE  Interaction: P46675; IntAct: EBI-18471,EBI-12056; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-12056; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-3035,EBI-12056; Score: 0.37
DE  Interaction: P53863; IntAct: EBI-29183,EBI-12056; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-12056,EBI-14372; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12056,EBI-8603; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-12056,EBI-9166; Score: 0.35
DE  Interaction: P40066; IntAct: EBI-22648,EBI-12056; Score: 0.27
DE  Interaction: Q07953; IntAct: EBI-27124,EBI-12056; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12056; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12056; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044612;
GO  GO:0044615;
GO  GO:0017056;
GO  GO:0006999;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLETLRGNKLHSGTSKGANKKLNELLESSDNLPSASSELGSIQVSINELRRRVFQLRSKNKASKDYTKAHYLLANSGLSF
SQ  EDVDAFIKDLQTNQFLEPNPPKIIESEELEFYIRTKKEENILMSIEQLLNGATKDFDNFINHNLNLDWAQHKNEVMKNFG
SQ  ILIQDKKTVDHKKSISSLDPKLPSWGNKGNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEFIS
SQ  ILSSANGTRNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGLATNVNKIKSFIDTKLKKADKSW
SQ  KISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKANIKKVEQSFLTYFKAYASSKDHGLPVEYSTKLHTEYNQHIKS
SQ  SLDGDPYRLAVYKLIGRCDLSRKNIPAVTLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYYLQ
SQ  TLLLSGLYGLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANILANYTKSFRYSDPRVAVEYLVLI
SQ  TLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGARIPGVIEERQPLLHVRDEKEFLHTITEQAARRADEDGRIYDS
SQ  ILLYQLAEEYDIVITLVNSLLSDTLSASDLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLLNI
SQ  SSIRELYFNKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIITLSCISNMIHILNESKYQSSTKG
SQ  QQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVSL
//
ID  P49686;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P49686;
DR  UNIPROT: D6VSH5;
DR  PDB: 6B4E;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP42 is specifically important for nuclear protein and mRNA export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:10805742, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: P48837; IntAct: EBI-12310,EBI-12324; Score: 0.44
DE  Interaction: Self; IntAct: EBI-12310,EBI-12310; Score: 0.44
DE  Interaction: Q06142; IntAct: EBI-12310,EBI-9145; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-12310,EBI-11703; Score: 0.44
DE  Interaction: Q02629; IntAct: EBI-12310,EBI-11698; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-11730,EBI-12310; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-12310,EBI-12315; Score: 0.44
DE  Interaction: Q05166; IntAct: EBI-12310,EBI-3035; Score: 0.44
DE  Interaction: P52891; IntAct: EBI-12310,EBI-12337; Score: 0.44
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-12310; Score: 0.74
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-12310; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-12310; Score: 0.40
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0003714;
GO  GO:0071472;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSAFGNPFTSGAKPNLSNTSGINPFTNNAASTNNMGGSAFGRPSFGTANTMTGGTTTSAFGMPQFGTNTGNTGNTSISAF
SQ  GNTSNAAKPSAFGAPAFGSSAPINVNPPSTTSAFGAPSFGSTGFGAMAATSNPFGKSPGSMGSAFGQPAFGANKTAIPSS
SQ  SVSNSNNSAFGAASNTPLTTTSPFGSLQQNASQNASSTSSAFGKPTFGAATNTQSPFGTIQNTSTSSGTGVSPFGTFGTN
SQ  SNNKSPFSNLQSGAGAGSSPFGTTTSKANNNNNVGSSAFGTTNNQSPFSGGSGGTFGSASNLNKNTNGNFQSSFGNKGFS
SQ  FGITPQNDANKVSQSNPSFGQTMPNTDPNISLKSNGNATSFGFGQQQMNATNVNANTATGKIRFVQGLSSEKDGILELAD
SQ  LAEETLKIFRANKFELGLVPDIPPPPALVA
//
ID  P39705;
PN  Nucleoporin NUP60;
GN  NUP60;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Nuclear basket.
DR  UNIPROT: P39705;
DR  UNIPROT: D6VPL6;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-20731,EBI-10420; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-12401,EBI-20731; Score: 0.70
DE  Interaction: Q06142; IntAct: EBI-9145,EBI-20731; Score: 0.77
DE  Interaction: P36016; IntAct: EBI-20731,EBI-10154; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-20731,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-20731; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-20731; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-20731,EBI-25940; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-20731,EBI-8591; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-2186,EBI-20731; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-19863,EBI-20731; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-20731,EBI-1797; Score: 0.69
DE  Interaction: P40069; IntAct: EBI-9166,EBI-20731; Score: 0.67
DE  Interaction: Q12449; IntAct: EBI-37072,EBI-20731; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-20731; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-20731; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-20731; Score: 0.32
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0030466;
GO  GO:0051276;
GO  GO:0006302;
GO  GO:0008298;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0060188;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MHRKSLRRASATVPSAPYRKQIISNAHNKPSLFSKIKTFFTQKDSARVSPRNNVANKQPRNESFNRRISSMPGGYFHSEI
SQ  SPDSTVNRSVVVSAVGEARNDIENKEEEYDETHETNISNAKLANFFSKKGNEPLSEIEIEGVMSLLQKSSKSMITSEGEQ
SQ  KSAEGNNIDQSLILKESGSTPISISNAPTFNPKYDTSNASMNTTLGSIGSRKYSFNYSSLPSPYKTTVYRYSAAKKIPDT
SQ  YTANTSAQSIASAKSVRSGVSKSAPSKKISNTAAALVSLLDENDSKKNNAASELANPYSSYVSQIRKHKRVSPNAAPRQE
SQ  ISEEETTVKPLFQNVPEQGEEPMKQLNATKISPSAPSKDSFTKYKPARSSSLRSNVVVAETSPEKKDGGDKPPSSAFNFS
SQ  FNTSRNVEPTENAYKSENAPSASSKEFNFTNLQAKPLVGKPKTELTKGDSTPVQPDLSVTPQKSSSKGFVFNSVQKKSRS
SQ  NLSQENDNEGKHISASIDNDFSEEKAEEFDFNVPVVSKQLGNGLVDENKVEAFKSLYTF
//
ID  A1Z6H7;
PN  Nuclear pore membrane glycoprotein 210;
GN  Gp210;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:3919018}; Single-pass type I membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Cytoplasm {ECO:0000269|PubMed:2517292}. Note=During mitosis diffusively localized throughout the cytoplasm. {ECO:0000269|PubMed:2517292}.
DR  UNIPROT: A1Z6H7;
DR  UNIPROT: Q6NP18;
DR  UNIPROT: Q9GPI0;
DE  Function: Component of the nuclear pore complex. {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}.
DE  Reference Proteome: Yes;
DE  Interaction: P34082; IntAct: EBI-868243,EBI-82439; Score: 0.35
DE  Interaction: Q9VLS7; IntAct: EBI-190906,EBI-82439; Score: 0.35
DE  Interaction: Q9VQA2; IntAct: EBI-198744,EBI-82439; Score: 0.37
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0044615;
GO  GO:0070762;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTV
SQ  RTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEP
SQ  GSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPS
SQ  EVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTV
SQ  AYPNRLSISLLPHLNWVTVQGEHHAIALDLFAADGQKITMGTKYSINSEVDESFFAIVDRTRNGSRLFGQAKKEGITQVY
SQ  GSYKDLSVQAELQIFEELQLAPTKVVLPYDPNSLKPLKLQFHASGGDNNYAWFSGNPQVIQIDTQGQATTEIRDVKSAYV
SQ  NQEVLKDGGKLTAHTTVKVALSKNQKISRVAHIYFLPPERLQITRSNFETALKDFVHVHVGVYARINNSEVPYTSCDNLH
SQ  FQLDFSQPILQLEGNEGAEAAHEACHVLRLRATAVGTTSLRVSYMYMDKVLYDIIDLYVFEPLVVLNPIENEVVLPVGSS
SQ  RNIIYANGPQRSFTVAAEIIQSTAFDEKILKVSKLEFDTQNLITAFTVLCRELGETQFTYRVHNSLPTSSFALYQSEVTT
SQ  KVHCVRPRFLKLYARHNLRDSCPLEKRTSLLFLKDPENKIEIEIEVHDSNNRRLMNISSLGLDWEFSAGEERYQKNIIPH
SQ  RQISELEFNHGVTLPSRDLLVLTLSEVATNFRIKGTVSQYNDKLLAQHGIHAERPPFGIKNPQTGLIYTPLIENEIRLHA
SQ  VNSTLLPKDYMSIFLASGYSERIPIAQGSGYLQLELSEAGIVQVEYNENTRILVLTPLRLGHVRLELTDRCLMNEPSHLS
SQ  ISVVGIGAIEVVSMDRLERTTRIEAIVRLFDTNDNLLLVDQSKLSAYDLSEVVADQSILSVRLGEQENVGPGEIRYTITG
SQ  NQVGETKILFQSGKGIYKVASDPLNIQVFAPIRLFPRDSTLVVGSSIQVYFHGGPHPNTNMIISVEKEQVATISSTVVTA
SQ  HKLGTTKIVGKCLLKNPVTGKDEVVSQDSVEVHVVALKGVQIRTPLVRIHSGAVMPATLWGLSDLSPMILGTLQNTKISW
SQ  KVSQPQVVEIFNVFTTAGIEYQSGDLISVRVRALNPGKATITASVTLADGTILPPATVDLQVFKTLELVTPNAIKMDSIL
SQ  AAPRSILQLKSNMDNVVYKLDDRSNGIVSVTPDGLVHTKDSLGRDLIIATTADQSLPIGIEVKNVQYILVTLMPILKLRE
SQ  LEHKIPRGMNFVFKVSLHDNLGNELSHNIEDFNGLRYELGNKDDVDVQIDNNLTFALNLMRETNNVIGISLKDSTGVKHS
SQ  MDFIKLSVVESDNLFPTKTIFSVGDIICFDSPLTLSSTWRSSNEQIVYINKHTGIAQVLSHRLKPGEKIEITNGDETKRG
SQ  GFLKYDLEVRESDTILFVKSVDTFSGPEYRGQLVIRNHLQSEKYSNLIAQNVSKCARELGSVPVNFFTCRLAAKDALGRN
SQ  LLKMYKVDALFEPSIGQYSCRLQLLTGFIELLSIVKTHDVYLELEAVVAKGVSDKMSLKLVPGIKVFPESVRVTDLKPHE
SQ  IHISGLDKALLKVQVKPSDSKYFAVDFIEHGHGLSKYRLELFDDLPLDENFYILVVSPDTKQSIEVPIIGNTMLAPKCTD
SQ  RRYGGPLVYRILENLGFVLTTTVIVIISIWVYMSCFQTQGVTQVNFEAFKKGKSRTELMQQSGRSSQDDTFGDSFNVRNF
SQ  SPDRRRPPSNALSESYIYGHPRLNSSNRSENSTSFS
//
ID  Q86UE4;
PN  Protein LYRIC;
GN  MTDH;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain (By similarity). TNF-alpha causes translocation from the cytoplasm to the nucleus. {ECO:0000250}.
DR  UNIPROT: Q86UE4;
DR  UNIPROT: Q05DH2;
DR  UNIPROT: Q52QU9;
DR  UNIPROT: Q6PK07;
DR  UNIPROT: Q8TCX3;
DR  PDB: 4QMG;
DR  Pfam: PF15686;
DR  OMIM: 610323;
DR  DisGeNET: 92140;
DE  Function: Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-1046588; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-1046588; Score: 0.35
DE  Interaction: P08473; IntAct: EBI-353759,EBI-1046588; Score: 0.35
DE  Interaction: Q04206; IntAct: EBI-1046588,EBI-73886; Score: 0.40
DE  Interaction: Q92793; IntAct: EBI-1046588,EBI-81215; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1046588; Score: 0.35
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-1046588; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-745632,EBI-1046588; Score: 0.35
DE  Interaction: P14316; IntAct: EBI-2866589,EBI-1046588; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-358011,EBI-1046588; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-528269,EBI-1046588; Score: 0.50
DE  Interaction: Q7KZF4; IntAct: EBI-1046588,EBI-1044112; Score: 0.71
DE  Interaction: O95166; IntAct: EBI-712001,EBI-1046588; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1046588; Score: 0.35
DE  Interaction: Q8N6M0; IntAct: EBI-2510892,EBI-1046588; Score: 0.40
DE  Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-1046588; Score: 0.35
DE  Interaction: Q96Q45; IntAct: EBI-2602465,EBI-1046588; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-1046588; Score: 0.35
DE  Interaction: Q9NPD3; IntAct: EBI-371823,EBI-1046588; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1046588; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1046588; Score: 0.35
DE  Interaction: Q9Y466; IntAct: EBI-11792373,EBI-1046588; Score: 0.35
DE  Interaction: Q9C0D3; IntAct: EBI-1046588,EBI-1811414; Score: 0.35
DE  Interaction: O75324; IntAct: EBI-21894129,EBI-1046588; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-347804,EBI-1046588; Score: 0.44
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-1046588; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-1046588; Score: 0.35
DE  Interaction: O60739; IntAct: EBI-1046588,EBI-1043343; Score: 0.40
DE  Interaction: Q9NX58; IntAct: EBI-1046588,EBI-713507; Score: 0.40
DE  Interaction: P28562; IntAct: EBI-975493,EBI-1046588; Score: 0.35
DE  Interaction: Q8NEH6; IntAct: EBI-1046588,EBI-743811; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475891,EBI-1046588; Score: 0.35
DE  Interaction: Q5JR59-3; IntAct: EBI-11522433,EBI-1046588; Score: 0.35
DE  Interaction: Q8IXJ6-2; IntAct: EBI-5240785,EBI-1046588; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0001650;
GO  GO:0016021;
GO  GO:0046581;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0051059;
GO  GO:0003723;
GO  GO:0001085;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0070830;
GO  GO:0031663;
GO  GO:0043066;
GO  GO:0000122;
GO  GO:0045766;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051897;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARK
SQ  KRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNE
SQ  KSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASF
SQ  PVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPS
SQ  AWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEE
SQ  WGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKT
SQ  RPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQT
SQ  KSETSWESPKQIKKKKKARRET
//
ID  P40305;
PN  Interferon alpha-inducible protein 27, mitochondrial;
GN  IFI27;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion membrane {ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:27673746}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:11722583, ECO:0000269|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. Note=Exclusive localizations in either the nucleus or the mitochondrion have been reported. {ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:27673746}.
DR  UNIPROT: P40305;
DR  UNIPROT: A0A087WZF8;
DR  UNIPROT: A8K0H0;
DR  UNIPROT: Q53YA6;
DR  UNIPROT: Q6IEC1;
DR  UNIPROT: Q7Z5R0;
DR  UNIPROT: Q7Z5R1;
DR  UNIPROT: Q7Z5R2;
DR  UNIPROT: Q96BK3;
DR  UNIPROT: Q9H4B1;
DR  Pfam: PF06140;
DR  OMIM: 600009;
DR  DisGeNET: 3429;
DE  Function: Probable adapter protein involved in different biological processes (PubMed:22427340, PubMed:27194766). Part of the signaling pathways that lead to apoptosis (PubMed:18330707, PubMed:27673746, PubMed:24970806). Involved in type-I interferon-induced apoptosis characterized by a rapid and robust release of cytochrome C from the mitochondria and activation of BAX and caspases 2, 3, 6, 8 and 9 (PubMed:18330707, PubMed:27673746). Also functions in TNFSF10-induced apoptosis (PubMed:24970806). May also have a function in the nucleus, where it may be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors (PubMed:22427340). May thereby play a role in the vascular response to injury (By similarity). In the innate immune response, has an antiviral activity towards hepatitis C virus/HCV (PubMed:27194766, PubMed:27777077). May prevent the replication of the virus by recruiting both the hepatitis C virus non-structural protein 5A/NS5A and the ubiquitination machinery via SKP2, promoting the ubiquitin- mediated proteasomal degradation of NS5A (PubMed:27194766, PubMed:27777077). {ECO:0000250|UniProtKB:Q8R412, ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:24970806, ECO:0000269|PubMed:27194766, ECO:0000269|PubMed:27673746, ECO:0000269|PubMed:27777077}.
DE  Reference Proteome: Yes;
DE  Interaction: P05549-1; IntAct: EBI-2805952,EBI-9678982; Score: 0.37
DE  Interaction: Q92754; IntAct: EBI-2805952,EBI-937309; Score: 0.37
DE  Interaction: A0A384KLT9; IntAct: EBI-2805952,EBI-2853974; Score: 0.37
DE  Interaction: Q0WHE4; IntAct: EBI-2840791,EBI-2805952; Score: 0.37
DE  Interaction: P17778; IntAct: EBI-2805952,EBI-2842665; Score: 0.37
DE  Interaction: A0A384KST0; IntAct: EBI-2845592,EBI-2805952; Score: 0.37
DE  Interaction: Q8ZG09; IntAct: EBI-2842762,EBI-2805952; Score: 0.37
DE  Interaction: Q8ZHF1; IntAct: EBI-2805952,EBI-2849437; Score: 0.37
DE  Interaction: Q81KT8; IntAct: EBI-2805952,EBI-2809955; Score: 0.37
DE  Interaction: A0A1Q4LWR1; IntAct: EBI-2831752,EBI-2805952; Score: 0.37
DE  Interaction: A0A0F7RKM4; IntAct: EBI-2812285,EBI-2805952; Score: 0.37
DE  Interaction: Q81VA8; IntAct: EBI-2812761,EBI-2805952; Score: 0.37
DE  Interaction: Q5NGF6; IntAct: EBI-2805952,EBI-2798182; Score: 0.37
DE  Interaction: Q8ZCW0; IntAct: EBI-2842923,EBI-2805952; Score: 0.37
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0001102;
GO  GO:0006915;
GO  GO:0097190;
GO  GO:0051607;
GO  GO:0097191;
GO  GO:0045087;
GO  GO:0044827;
GO  GO:0000122;
GO  GO:0043161;
GO  GO:0070936;
GO  GO:0046825;
GO  GO:0060337;
GO  GO:0016032;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGG
SQ  GVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY
//
ID  Q12315;
PN  Nucleoporin GLE1;
GN  GLE1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Cytoplasmic side {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Nucleoplasmic side {ECO:0000269|PubMed:10523319}. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q12315;
DR  UNIPROT: D6VRE7;
DR  PDB: 3PEU;
DR  PDB: 3PEV;
DR  PDB: 3RRM;
DR  PDB: 3RRN;
DR  PDB: 6B4E;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonucleoprotein (hnRNP) NAB2 from exported mRNA. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11336711, ECO:0000269|PubMed:15208322}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-7635,EBI-12265; Score: 0.32
DE  Interaction: P20676; IntAct: EBI-7635,EBI-12392; Score: 0.32
DE  Interaction: P32500; IntAct: EBI-7635,EBI-11950; Score: 0.37
DE  Interaction: P34077; IntAct: EBI-7635,EBI-12056; Score: 0.32
DE  Interaction: P35729; IntAct: EBI-7635,EBI-11713; Score: 0.32
DE  Interaction: P36161; IntAct: EBI-7635,EBI-11722; Score: 0.32
DE  Interaction: P38181; IntAct: EBI-7635,EBI-11756; Score: 0.32
DE  Interaction: P39705; IntAct: EBI-7635,EBI-20731; Score: 0.32
DE  Interaction: P40064; IntAct: EBI-7635,EBI-11740; Score: 0.32
DE  Interaction: P40066; IntAct: EBI-7635,EBI-22648; Score: 0.32
DE  Interaction: P40368; IntAct: EBI-7635,EBI-12331; Score: 0.32
DE  Interaction: P40477; IntAct: EBI-7635,EBI-11747; Score: 0.32
DE  Interaction: P46673; IntAct: EBI-7635,EBI-12345; Score: 0.32
DE  Interaction: P47054; IntAct: EBI-7635,EBI-25846; Score: 0.32
DE  Interaction: P48837; IntAct: EBI-7635,EBI-12324; Score: 0.32
DE  Interaction: P49686; IntAct: EBI-7635,EBI-12310; Score: 0.74
DE  Interaction: P49687; IntAct: EBI-7635,EBI-11730; Score: 0.32
DE  Interaction: P52593; IntAct: EBI-7635,EBI-11763; Score: 0.32
DE  Interaction: P52891; IntAct: EBI-7635,EBI-12337; Score: 0.32
DE  Interaction: P53011; IntAct: EBI-7635,EBI-16940; Score: 0.32
DE  Interaction: Q02199; IntAct: EBI-7635,EBI-12315; Score: 0.32
DE  Interaction: Q02629; IntAct: EBI-7635,EBI-11698; Score: 0.53
DE  Interaction: Q02630; IntAct: EBI-7635,EBI-11703; Score: 0.32
DE  Interaction: Q03790; IntAct: EBI-7635,EBI-27321; Score: 0.32
DE  Interaction: Q04839; IntAct: EBI-27549,EBI-7635; Score: 0.44
DE  Interaction: Q05166; IntAct: EBI-7635,EBI-3035; Score: 0.32
DE  Interaction: Self; IntAct: EBI-7635,EBI-7635; Score: 0.53
DE  Interaction: P12385; IntAct: EBI-7635,EBI-6533; Score: 0.40
DE  Interaction: P05453; IntAct: EBI-7635,EBI-6540; Score: 0.52
DE  Interaction: P06103; IntAct: EBI-8973,EBI-7635; Score: 0.40
DE  Interaction: Q04067; IntAct: EBI-8958,EBI-7635; Score: 0.40
DE  Interaction: P38074; IntAct: EBI-7635,EBI-8394; Score: 0.37
DE  Interaction: Q02159; IntAct: EBI-7635,EBI-19749; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-20939,EBI-7635; Score: 0.40
DE  Interaction: Q12445; IntAct: EBI-7635,EBI-34287; Score: 0.32
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0008047;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10523319};
SQ  MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLI
SQ  PINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQR
SQ  KRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLG
SQ  KAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGD
SQ  SLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGW
SQ  KRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAA
SQ  AVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP
//
ID  Q10109;
PN  Lap-Emerin-Man domain protein 2;
GN  lem2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}.
DR  UNIPROT: Q10109;
DR  PDB: 5YCA;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Nucleus inner membrane protein involved in meiosis. {ECO:0000269|PubMed:20404563}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0061638;
GO  GO:0034506;
GO  GO:0034507;
GO  GO:0099115;
GO  GO:0005639;
GO  GO:0044732;
GO  GO:1904834;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0031618;
GO  GO:1902377;
GO  GO:0005724;
GO  GO:0097038;
GO  GO:1990578;
GO  GO:0003682;
GO  GO:0072766;
GO  GO:0030702;
GO  GO:1990141;
GO  GO:0000183;
GO  GO:0030466;
GO  GO:0099114;
GO  GO:0097240;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0071765;
GO  GO:0031937;
GO  GO:0097355;
GO  GO:0034398;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDNWEDPNFELRNLRVIDLKKILHESGVSFPVNARKIEYIRMVDRIRKNKLSSGPQHLLSHLQKEENSNTSKASSSEDEI
SQ  APKYLYPSSPSKSTKKPHNETEPLLSPQFIDKPSNIETPVKIESPHVSQNNTFQSYSELSPNVETSLTMKTPPAHASTPK
SQ  FRSHKSHRVAVPMSFMDSSALHTSPAFSERLKLLSSSNNFSPQLRSPKISHRLQTSATSSPLQHKRPFTNVPERVSRDIE
SQ  FAPLDSARPSESSSPYSEVDSAEEDDELFQNYVLQQTRKESKLWSFIKKVFHDIKYANYRLLHNLRAFPGISAISSSYLV
SQ  HIFMILLGVVAAIFLALLREKMFTAGFCDSGASGSSASILGISFPSLCRTCPPNAICPSPNYVECKPGYVLYEPWYSSLG
SQ  FWPSKYCVSDTSREESVNIFREECLSVLRSWNAILHCSNNSSDLLERNMSYNAHPYVADNLNISSDHISFPSKPFALGLL
SQ  HDTLLERKSPTLGLEMFEDLFKASLAVLSETNEVVMDSKLICYDSWAGIPLRCRLKQQLIKFVWRNKVFLFGILALSGVI
SQ  FKLINFFRTRSIVAKYLPSASRFCVESLKRQKANYQMSRSQEPVIPLIEMHDILFHGNGPLEQIHMTKATARTLWEAIVE
SQ  RVEQVGSVRTRESEVDGEWTRVWEWVGTNTLDFQTDRSFINTTSPLRE
//
ID  P45436;
PN  Cell death protein 3 subunit p13;
GN  ced;
OS  31234;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P42573}. Perikaryon {ECO:0000250|UniProtKB:P42573}. Cell junction, synapse {ECO:0000250|UniProtKB:P42573}. Mitochondrion {ECO:0000250|UniProtKB:P42573}. Cytoplasm {ECO:0000250|UniProtKB:P42573}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P42573}. Note=Colocalizes with nucleoporin npp- 14 to the perinuclear region in germ cells. Becomes diffused in the cytoplasm in apoptotic germ cells. Localizes to axonal mitochondria and synapses of DD motor neurons. Synaptic localization is dependent on axonal mitochondria. {ECO:0000250|UniProtKB:P42573}.
DR  UNIPROT: P45436;
DR  UNIPROT: E3M6B9;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  PROSITE: PS01122;
DR  PROSITE: PS01121;
DR  PROSITE: PS50207;
DR  PROSITE: PS50208;
DE  Function: Acts as a cysteine protease in controlling programmed cell death (apoptosis) by proteolytically activating or inactivating a wide range of substrates. Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development. During oogenesis, required for germline apoptosis downstream of ced-9 and ced-4 but independently of egl-1. By cleaving and activating ced-8, promotes phosphatidylserine exposure on the surface of apoptotic cells; phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation. By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis. During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap-independent translation. During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9. By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis. Downstream of ced-4, may play a role in sex- specific cell apoptosis by cleaving sex-determining protein fem-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Cleaves ced-9 in vitro. Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro. Independently of its apoptotic role has additional functions. Probably by cleaving and thereby activating actin-severing protein gsnl-1, required for the elimination of transient presynaptic components during larval development downstream of egl-1, ced-9 and ced-4 pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development. Acts in cell fate patterning by cleaving heterochronic protein lin-28, likely promoting its degradation. Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro. Downstream of calreticulin crt- 1 and ced-4 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy. Cleaves 14-3-3-like protein ftt-2, tubulin tbb-2 and calreticulin crt-1 in vitro. Plays also a role in resistance to S.typhimurium-mediated infection. {ECO:0000250|UniProtKB:P42573}.
DE  Reference Proteome: Yes;
GO  GO:0008303;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0008656;
GO  GO:0097200;
GO  GO:0042802;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0046716;
GO  GO:1905803;
GO  GO:1904747;
GO  GO:1905845;
GO  GO:0043525;
GO  GO:1901046;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0016540;
GO  GO:0030163;
GO  GO:0030155;
GO  GO:0042659;
GO  GO:0040034;
GO  GO:0040012;
GO  GO:0031647;
GO  GO:0040028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMRQDRRNLLERNILVFSNKLQSEQILEVLIAKQILNADNGDVINSCRTERDKRKEIVKAVQRRGDVAFDAFYDALRDTG
SQ  HHELAAVLEPLARTIDFITPRDLECPMSPASHRRSRALSPSTFSSPTRVHRDSVSSVSSFTSTYQDVYTRARSTSRSSRP
SQ  LHASDRHNYVSPSNSFQSQPSSANSSFTGCSSLGYSSSRTRSYSKASAHSQYIFHEEDMNYVDAPTIHRVFDEKTMYRNF
SQ  STPRGLCLIINNEHFEQMPTRNGTKADKDNISNLFRCMGYIVHCKDNLTGRAMMLTIRDFAKNETHGDSAILVILSHGEE
SQ  NVIIGVDDVSVNVHEIYDLLNAANAPRLANKPKLVFVQACRGERRDNGFPVLDSVDGVPALIRPRGWDKGDGPLFNFLGC
SQ  VRPQAQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSLHAKDMDVVELLTEVNKKVACGFQTSQGANI
SQ  LKQMPELTSRLLKKFYFWPEDRNRSSAV
//
ID  O75844;
PN  CAAX prenyl protease 1 homolog;
GN  ZMPSTE24;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}.
DR  UNIPROT: O75844;
DR  UNIPROT: B3KQI7;
DR  UNIPROT: D3DPU7;
DR  UNIPROT: Q8NDZ8;
DR  UNIPROT: Q9UBQ2;
DR  PDB: 2YPT;
DR  PDB: 4AW6;
DR  PDB: 5SYT;
DR  PDB: 6BH8;
DR  Pfam: PF01435;
DR  Pfam: PF16491;
DR  OMIM: 275210;
DR  OMIM: 606480;
DR  OMIM: 608612;
DR  DisGeNET: 10269;
DE  Function: Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C.
DE  Disease: Mandibuloacral dysplasia with type B lipodystrophy (MADB) [MIM:608612]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and generalized lipodystrophy with loss of subcutaneous fat from the extremities, face, neck and trunk. {ECO:0000269|PubMed:12913070, ECO:0000269|PubMed:17152860, ECO:0000269|PubMed:18435794, ECO:0000269|PubMed:20814950}. Note=The disease is caused by mutations affecting the gene represented in this entry. Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P08473; IntAct: EBI-353759,EBI-1056377; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1056377; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-1056377; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-1056377; Score: 0.35
DE  Interaction: Q16666-2; IntAct: EBI-6273540,EBI-1056377; Score: 0.35
DE  Interaction: Q08AM6; IntAct: EBI-2107455,EBI-1056377; Score: 0.35
DE  Interaction: P54219; IntAct: EBI-21493000,EBI-1056377; Score: 0.35
DE  Interaction: O15263; IntAct: EBI-1056377,EBI-21800352; Score: 0.40
DE  Interaction: P14324; IntAct: EBI-948245,EBI-1056377; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-10194262,EBI-1056377; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-1056377; Score: 0.35
DE  Interaction: Q9UET6; IntAct: EBI-1056377,EBI-1055987; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-1056377,EBI-5327611; Score: 0.40
DE  Interaction: A4D263; IntAct: EBI-1056377,EBI-20831539; Score: 0.40
DE  Interaction: P47902; IntAct: EBI-8514176,EBI-1056377; Score: 0.40
DE  Interaction: P06821; IntAct: EBI-2547404,EBI-1056377; Score: 0.50
DE  Interaction: O00624-2; IntAct: EBI-21654602,EBI-1056377; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-1056377; Score: 0.50
DE  Interaction: C5E519; IntAct: EBI-12562139,EBI-1056377; Score: 0.50
DE  Interaction: Q6DPW5; IntAct: EBI-1056377,EBI-12562156; Score: 0.40
DE  Interaction: Q99679; IntAct: EBI-6309069,EBI-1056377; Score: 0.35
DE  Interaction: P29084; IntAct: EBI-2853321,EBI-1056377; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-394678,EBI-1056377; Score: 0.35
DE  Interaction: Q6PEY0; IntAct: EBI-21551278,EBI-1056377; Score: 0.35
DE  Interaction: P22732; IntAct: EBI-2825135,EBI-1056377; Score: 0.35
DE  Interaction: Q8WTR4; IntAct: EBI-2833203,EBI-1056377; Score: 0.35
DE  Interaction: Q86WS5; IntAct: EBI-21771370,EBI-1056377; Score: 0.35
DE  Interaction: Q9BY78; IntAct: EBI-2129375,EBI-1056377; Score: 0.35
DE  Interaction: Q02223; IntAct: EBI-519945,EBI-1056377; Score: 0.35
DE  Interaction: Q9BVJ7; IntAct: EBI-724940,EBI-1056377; Score: 0.35
GO  GO:0070062;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0032991;
GO  GO:0003690;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0008235;
GO  GO:0007628;
GO  GO:0030282;
GO  GO:0071586;
GO  GO:1990036;
GO  GO:0061762;
GO  GO:0061337;
GO  GO:0048739;
GO  GO:0003231;
GO  GO:0044255;
GO  GO:0071480;
GO  GO:0008340;
GO  GO:0006281;
GO  GO:0003417;
GO  GO:0001942;
GO  GO:0003007;
GO  GO:1990164;
GO  GO:0043979;
GO  GO:0044029;
GO  GO:0006925;
GO  GO:0060993;
GO  GO:0001889;
GO  GO:0043007;
GO  GO:0035264;
GO  GO:1903799;
GO  GO:0050905;
GO  GO:0006998;
GO  GO:0030327;
GO  GO:0006508;
GO  GO:0010506;
GO  GO:0030500;
GO  GO:0008360;
GO  GO:2000772;
GO  GO:0050688;
GO  GO:0043516;
GO  GO:0048145;
GO  GO:0010906;
GO  GO:2000618;
GO  GO:0032350;
GO  GO:0019216;
GO  GO:1903463;
GO  GO:0040014;
GO  GO:1903025;
GO  GO:0070302;
GO  GO:2000730;
GO  GO:0032006;
GO  GO:0060307;
GO  GO:0072423;
GO  GO:0048538;
GO  GO:0003229;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFW
SQ  SGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTL
SQ  GFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEV
SQ  MAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNK
SQ  KQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYN
SQ  EVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH
//
ID  Q9N0Z4;
PN  Probable phospholipid-transporting ATPase IF;
GN  ATP11B;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Recycling endosome membrane {ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y2G3}. Early endosome {ECO:0000250|UniProtKB:Q9Y2G3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, mainly located in recycling endosomes. {ECO:0000250|UniProtKB:Q9Y2G3}. [Isoform 2]: Nucleus inner membrane {ECO:0000269|PubMed:11058586}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9N0Z4;
DR  UNIPROT: Q8WMR2;
DR  Pfam: PF16212;
DR  Pfam: PF16209;
DR  PROSITE: PS00154;
DE  Function: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). Isoform 2/RFBP appears to play a role in the subnuclear trafficking of transcription factors with RING motifs. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0055038;
GO  GO:0005524;
GO  GO:0140326;
GO  GO:0000287;
GO  GO:0015914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  LGFDPPHQSDTRTIYIANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLFEQFRRVANFYFLIIFLVQLMIDTPTSPI
SQ  TSGLPLFFVITVTAIKQGYEDWLRHNSDNEVNGAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDG
SQ  SCHVTTASLDGETNLKTHVAVPETAVLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPESLLLRGAR
SQ  LKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLIILISEAIISTILKYTWQAEEKWDEPWYNQKTEH
SQ  QRNSSKILRFISDFLAFLVLYNFIIPISLYVTVEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDK
SQ  TGTLTENEMQFRECSIHGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHVNSLSHLTSSSSFRTSPENDTELIKEHDLF
SQ  FKAVSLCHTVQISSVQTDGIGDGPWQSSLAPSQLEYYASSPDEKALVEAAARIGIVFVGNTEETMEVKILGKLERYKLLH
SQ  VLEFDSDRRRMSVIVQAPSGERFLFAKGAESSILPKCIGGEIEKTRIHVDEFALKGLRTLCVAYRQFTSKEYEVIDRRLF
SQ  EARTALQQREEKLADVFHYIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSCGHFHRTMN
SQ  ILELTNQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLFMEVCRNCSAVLCCRMAPLQKAKVIRLIK
SQ  ISPEKPITIGCWDGANDVSMIQEAHVGIGIMGKERRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVC
SQ  FITPQFLYQFYCLFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHIDPHILQNKPTLYRDISKNRLLSIKTFLYWTILG
SQ  FSRSFIFLFGSYFLIGKDASLLGNGQMFGNWTFGTLVFTVMVITVTVKMALETHFWTWINHLVTWGSIIFYFVFSLFYGG
SQ  ILWPFLGSQNMYFVFIQLVSSGSAWFAIILMVVTCLFLDVMKKVFDRQLHPTSTEKAQLTETNSSIKCVDSLCCFPEGET
SQ  TCTSVRRMLERVIGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
//
ID  Q9TXI7;
PN  Phosphatidylinositol 3-kinase catalytic subunit type 3;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:11927551}; Peripheral membrane protein {ECO:0000269|PubMed:11927551}. Cytoplasm {ECO:0000269|PubMed:11927551}. Cytoplasmic granule {ECO:0000269|PubMed:11927551}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Note=Colocalizes with rab-5 and dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
DR  UNIPROT: Q9TXI7;
DR  UNIPROT: Q5TYK9;
DR  UNIPROT: Q9TXI6;
DR  UNIPROT: Q9XZR0;
DR  Pfam: PF00454;
DR  Pfam: PF00792;
DR  Pfam: PF00613;
DR  PROSITE: PS51547;
DR  PROSITE: PS00915;
DR  PROSITE: PS00916;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DE  Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate (PubMed:11927551). Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking (PubMed:11927551, PubMed:16111945). Plays a role in endosome-to-Golgi retrograde transport of mig-14 (PubMed:21183797). Involved in clearance of apoptotic cell corpses by phagosomes (PubMed:22272187). Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab- 5, rab-2 and rab-7, downstream of dynamin dyn-1 (PubMed:22272187, PubMed:18425118). The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse (PubMed:22272187). Required for embryonic development (PubMed:22272187). Together with bec-1, involved in L3/L4 larval molting stage probably by regulating cuticle shedding (PubMed:11927551). Regulates the expansion of the nucleus outer membrane (PubMed:11927551). Involved in the secretion and localization of lrp-1 at the apical surface of hyp7 syncytium (PubMed:16111945). May regulate endocytosis in hypodermal cells (PubMed:11927551). May play a role in the formation of gut granules (a lysosome-related organelle) (PubMed:15843430). Plays a role in germ stem cell proliferation during larval development (PubMed:28285998). {ECO:0000269|PubMed:11927551, ECO:0000269|PubMed:15843430, ECO:0000269|PubMed:16111945, ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:21183797, ECO:0000269|PubMed:22272187, ECO:0000269|PubMed:28285998}.
DE  Reference Proteome: Yes;
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005730;
GO  GO:0005777;
GO  GO:0001891;
GO  GO:0000407;
GO  GO:0034271;
GO  GO:0034272;
GO  GO:0016303;
GO  GO:0005524;
GO  GO:0052742;
GO  GO:0000045;
GO  GO:0030242;
GO  GO:0008340;
GO  GO:0042395;
GO  GO:0006897;
GO  GO:0002119;
GO  GO:0006998;
GO  GO:0090386;
GO  GO:0046854;
GO  GO:0036092;
GO  GO:0048015;
GO  GO:1901076;
GO  GO:0061365;
GO  GO:0030100;
GO  GO:0051036;
GO  GO:0050708;
GO  GO:0000003;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11927551};
SQ  MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLA
SQ  RQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPD
SQ  PFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFY
SQ  KVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIV
SQ  NLPSSQVLTREQRDLVWKFRHYLRQFPKALNKYLRSVNWVHPQEVKTALALMNDWELIEAEDALELLSSAFTHPAVRAYS
SQ  VSRLLEAASPEQVLLYLPQLVQALKYEQGQQLPEEGNPVPVVSEEEGKIPSVATTPTEELEGRDMTVVTKKEARKAASGD
SQ  LATFLIDYALASPKVSNYLYWHLKTEIESTKESKEEHSKMYQNIQDRLMEALVKRPDTRAQVDSLHQQQIFVEDLIILMN
SQ  EAKARGGRLNESKSAEFRTMLSRAKHMLDLKGVHLPLDPSFRLSSVIPDTASFFKSEMMPAKISFKVLQPNGKADRNIPE
SQ  EYTVIFKTGDDLRQDQLIQQMVRLIDIILKKGQLDLKLTPYLVLSTGVGQGFVQCIKSKPLRAIQEQYKAHKMDCIREAM
SQ  KELRPGDGPFGIEPNVIDNYVRSLAGYSVIMYILGLGDRHLDNLLLCENGKLFHVDFGFILGRDPKPMPPPMKLTSEMVQ
SQ  VMGGVKSKQFLEFVQHVDSAYRILRRHSNVLLNLFSLMLDAGIPDIAAEPDKAIFKIEQRLRLDLSDEAATKHIFTQIES
SQ  SLNAKMAMISDIIHAYKQNLM
//
ID  Q23064;
PN  Nuclear migration protein unc-83;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906, ECO:0000305|PubMed:21411627}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus outer membrane {ECO:0000269|PubMed:16481402}; Single-pass type IV membrane protein {ECO:0000305}. Note=The transmembrane domain associates with the nuclear envelope (PubMed:11748140). Co-localizes with unc-84 and lmn-1 at the nuclear envelope (PubMed:11748140). {ECO:0000269|PubMed:11748140}.
DR  UNIPROT: Q23064;
DR  UNIPROT: Q95WB6;
DE  Function: Cargo-specific adapter that is involved in nuclear migration during development and thereafter (PubMed:11748140, PubMed:19605495, PubMed:20005871, PubMed:20921138, PubMed:27697906). Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it interacts with unc-84 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules (PubMed:11748140, PubMed:16481402, PubMed:25023515). Within the complex, connects the nuclear envelope to the microtubule cytoskeleton through the kinesin-1 light chain protein klc-2 (most likely within the Kinesin 1 motor complex) to regulate nuclear migrations (PubMed:19605495, PubMed:20921138). Moreover, within the complex, also recruits the large microtubule-associated bicd-1-dlc-1- egal-1 and lis-1-nud-2 complexes to the nuclear envelope to regulate both the bidirectional migration of nuclei and the extent of nuclear migrations (PubMed:20005871). Not required for centrosome attachment to the nucleus (PubMed:11748140). {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:20921138, ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: Q20745; IntAct: EBI-2902228,EBI-313630; Score: 0.37
DE  Interaction: Q22799; IntAct: EBI-2902228,EBI-328324; Score: 0.37
DE  Interaction: V6CJ04; IntAct: EBI-2006416,EBI-2902228; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0045503;
GO  GO:0040011;
GO  GO:0007399;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0018991;
GO  GO:0009791;
GO  GO:0090435;
GO  GO:0030334;
GO  GO:0040025;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVMDSFSEVEMPNDISSEDHLLKVIESSAEEVDIFLENCSSLYNLILDSLHNLTSKTISCECLDEMTSTLEKSAKKILA
SQ  ERPEAENSVLLRLNTICCAMDQLRVQHNSRMMSGADSDTASSARSSTSSSTGEMRLWLHEVERRLEINEKRIRVEPNLQL
SQ  LLSDQQALQLEIQHEGQLLVNRLNKQIKDDHDSDSSEEEKRKTCVDAIRKRWHTIYLNSLSLVCRIEELINHQQASEDSE
SQ  SDPDLVGPPIKRARIRTVGHLTASDTEESEADEEDRHSQTETVVTEDDNVLPFAENEYESIMDGRVTVDSCTSSSEDQMV
SQ  EQSTNKKWESVLQDVGYSSGENSIHEALNTCADHLVPETSDMRRKRIECSPVKAFYRTVQLEDMSDLEVTKAINHDVEEE
SQ  PNLSDSMYVNHDSTFLATQNLPEYDEVMALMDDDDLPMDMSMTESFNTKWREIHGQKKPLRRASRPSREQMNLIAKSSCD
SQ  ASSEDSSEGENQTNLEDDPEMMSVSFNSAQFDTSSPLKRQRSARGLKNASFLYDSLEMDGSFCSTRSEMLPPCKTRSLAR
SQ  RKLRVRRMPRSMSDGEQLGVVSSKPEGMMTPMIRVSPPSTPVRRLLRKLDEQIRNRDSDTAPEHSDAAQAYEWDEYNPPQ
SQ  KDDSISDRHIQTMTDISDQLMNIDDDFAEHFGTSSAIRLIEESKSHLRVVLKALEESDSNIPQLSNFELIARSNLRQVDE
SQ  ALKIQSGNQPSFLETSTLQDLRSEWANLYESIRSPFARIMHQVKKFAATLQEVSSMASLGDVDIRSKEDVAKTLDAVTAI
SQ  ERRLSSERQELRDLLASSSFRDVAKDLSCEFESVSEGYDDAVDKIGKMAHSLSQVKGEWDAWNSRQNDIRNAMVRIESHL
SQ  KEGQMDNKMIADEMELCQERMNSLETMCNYLTASLGSIQNESNSKNLPDFKAELSIYSNALARLKDRFNDMIRVPTPPTV
SQ  QFHPPEPLPSLARSMTTQTAEMESETENEPLTIAEAISSSRLIKFTFALSLLAALAAIFYYHVFGKPFGPHVTYVNGPPP
SQ  V
//
ID  Q8N205;
PN  Nesprin-4;
GN  SYNE4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:23348741}; Single-pass type IV membrane protein {ECO:0000269|PubMed:23348741}. Note=Localization at the nucleus outer membrane requires the presence of SUN1. {ECO:0000250}.
DR  UNIPROT: Q8N205;
DR  UNIPROT: A8MRS0;
DR  UNIPROT: A8MYE3;
DR  UNIPROT: Q7Z7L3;
DR  Pfam: PF10541;
DR  PROSITE: PS51049;
DR  OMIM: 615535;
DR  OMIM: 615540;
DR  DisGeNET: 163183;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity). {ECO:0000250}.
DE  Disease: Deafness, autosomal recessive, 76 (DFNB76) [MIM:615540]: A form of non-syndromic sensorineural deafness, a disorder resulting from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB76 affected individuals have onset of progressive high frequency hearing impairment between birth and 6 years of age. The hearing loss is severe at high frequencies by adulthood. {ECO:0000269|PubMed:23348741}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A8K660; IntAct: EBI-7131783,EBI-10174479; Score: 0.56
DE  Interaction: P54849; IntAct: EBI-7131783,EBI-4319440; Score: 0.56
DE  Interaction: P56748; IntAct: EBI-7131783,EBI-10215641; Score: 0.56
DE  Interaction: P56851; IntAct: EBI-7131783,EBI-10215665; Score: 0.56
DE  Interaction: O00631; IntAct: EBI-7131783,EBI-10180786; Score: 0.56
DE  Interaction: Q6PL45; IntAct: EBI-7131783,EBI-10254180; Score: 0.56
DE  Interaction: Q6UX06; IntAct: EBI-7131783,EBI-2804156; Score: 0.56
DE  Interaction: Q6ZP80; IntAct: EBI-7131783,EBI-10255122; Score: 0.56
DE  Interaction: Q86UP2; IntAct: EBI-7131783,EBI-359761; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-7131783,EBI-749955; Score: 0.56
DE  Interaction: Q9BXN2; IntAct: EBI-7131783,EBI-3939278; Score: 0.67
DE  Interaction: Q9HC62; IntAct: EBI-7131783,EBI-714881; Score: 0.56
DE  Interaction: Q8TBU1; IntAct: EBI-7131783,EBI-10273677; Score: 0.56
DE  Interaction: Q96LK0; IntAct: EBI-7131783,EBI-741885; Score: 0.56
DE  Interaction: Q9BVK8; IntAct: EBI-7131783,EBI-348587; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-8640191,EBI-7131783; Score: 0.56
DE  Interaction: Q9NRS4-3; IntAct: EBI-7131783,EBI-10312990; Score: 0.56
DE  Interaction: Q9NSK0; IntAct: EBI-7131783,EBI-949319; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-7131783,EBI-2844246; Score: 0.56
DE  Interaction: Q9NWD8; IntAct: EBI-7131783,EBI-10314986; Score: 0.56
DE  Interaction: Q9NXK6; IntAct: EBI-7131783,EBI-10316423; Score: 0.56
DE  Interaction: Q9P0N8; IntAct: EBI-7131783,EBI-10317612; Score: 0.56
DE  Interaction: Q9UEU0; IntAct: EBI-7131783,EBI-723716; Score: 0.67
DE  Interaction: Q969F0; IntAct: EBI-7131783,EBI-743099; Score: 0.56
DE  Interaction: Q96D05; IntAct: EBI-7131783,EBI-2548784; Score: 0.56
DE  Interaction: Q96DZ9; IntAct: EBI-7131783,EBI-2548702; Score: 0.56
DE  Interaction: Q96E93; IntAct: EBI-7131783,EBI-750770; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-8652744,EBI-7131783; Score: 0.56
DE  Interaction: Q15437; IntAct: EBI-7131783,EBI-742673; Score: 0.56
DE  Interaction: O75355; IntAct: EBI-7131783,EBI-10187968; Score: 0.56
DE  Interaction: O95471; IntAct: EBI-7131783,EBI-740744; Score: 0.56
DE  Interaction: O95858; IntAct: EBI-7361096,EBI-7131783; Score: 0.56
DE  Interaction: P11686; IntAct: EBI-7131783,EBI-10197617; Score: 0.56
DE  Interaction: P15622-3; IntAct: EBI-7131783,EBI-10177272; Score: 0.56
DE  Interaction: Q16625; IntAct: EBI-7131783,EBI-2903088; Score: 0.56
DE  Interaction: Q53G59; IntAct: EBI-7131783,EBI-740929; Score: 0.56
DE  Interaction: Q5BVD1; IntAct: EBI-7131783,EBI-10243654; Score: 0.56
DE  Interaction: Q5J5C9; IntAct: EBI-7131783,EBI-10244198; Score: 0.56
DE  Interaction: Q5TAB7; IntAct: EBI-7131783,EBI-10246897; Score: 0.56
DE  Interaction: Q9ULW3; IntAct: EBI-7131783,EBI-2602396; Score: 0.56
DE  Interaction: Q9Y287; IntAct: EBI-7131783,EBI-2866431; Score: 0.56
DE  Interaction: Q07325; IntAct: EBI-7131783,EBI-3911467; Score: 0.56
DE  Interaction: Q08722; IntAct: EBI-7131783,EBI-1268321; Score: 0.56
DE  Interaction: Q12893; IntAct: EBI-7131783,EBI-8633987; Score: 0.56
DE  Interaction: Q13021; IntAct: EBI-7131783,EBI-750078; Score: 0.56
DE  Interaction: Q8N6G5; IntAct: EBI-7131783,EBI-10267100; Score: 0.56
GO  GO:0031309;
GO  GO:0034993;
GO  GO:0045198;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MALSLPLGPRLGSEPLNHPPGAPREADIVGCTVCPASGEESTSPEQAQTLGQDSLGPPEHFQGGPRGNEPAAHPPRWSTP
SQ  SSYEDPAGGKHCEHPISGLEVLEAEQNSLHLCLLGLGRRLQDLEQGLGHWALAQSGMVQLQALQVDLRGAAERVEALLAF
SQ  GEGLAQRSEPRAWAALEQILRALGAYRDSIFRRLWQLQAQLVSYSLVFEEANTLDQDLEVEGDSDWPGPGGVWGPWAPSS
SQ  LPTSTELEWDPAGDIGGLGPLGQKTARTLGVPCELCGQRGPQGRGQGLEEADTSHSRQDMLESGLGHQKRLARHQRHSLL
SQ  RKPQDKKRQASPHLQDVRLEGNPGAPDPASRQPLTFLLILFLLFLLLVGAMFLLPASGGPCCSHARIPRTPYLVLSYVNG
SQ  LPPV
//
ID  Q9FF75;
PN  SUN domain-containing protein 1;
GN  SUN1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}. Note=Dynamic localization during mitosis and meosis, tightly coupled with nuclear envelope (NE) dynamics. Localized with the nuclear envelope during meiotic prophase I. NE re-formation during metaphase is temporally and spatially coordinated with plant-specific microtubule structures such as phragmoplasts. During anaphase, after NE breakdown (NEBD), predominantly localized with the endoplasmic reticulum, in the outside of the segregated chromosomes and not in between segregated chromosomes. {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
DR  UNIPROT: Q9FF75;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (PubMed:24667841, PubMed:25759303). Required for the maintenance and/or formation of polarized nuclear shape in root hairs (PubMed:21294795, PubMed:25759303). Modulates the anchoring and mobility of WIP proteins and RANGAP1 in the nuclear envelope (NE) (PubMed:22270916). In association with SUN2, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis (PubMed:25412930). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:22270916, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8RWU6; IntAct: EBI-4425800,EBI-4460545; Score: 0.37
DE  Interaction: Q9FG89; IntAct: EBI-4425800,EBI-4425805; Score: 0.37
GO  GO:0005623;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0009524;
GO  GO:0043495;
GO  GO:0043621;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0006997;
GO  GO:0051291;
GO  GO:0051260;
GO  GO:0090435;
GO  GO:2000769;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSASTVSITANTAAATRRTPILAGEKKSNFDYPQSESLANGGVGEAGGTSRDLSRGEATLDRSQGQDLGPVTRRSVSAAT
SQ  GTNTTATQRRTRKVATPKSEKARWKTVVRIFAKQLGALLIIVGLIQLTRKMILKASSPSSPISSYETEMAFSGLESRIAE
SQ  VDGLVKATTNSMQVQVELLDKKMEREAKVLRQEIERKASAFQSELKKIESRTESLEKSVDEVNAKPWVTKDELERIYEEL
SQ  KKGNVDDSAFSEISIDELRAYARDIMEKEIEKHAADGLGRVDYALASGGAFVMEHSDPYLVGKGSSWFATTMRRAHTNAV
SQ  KMLSPSFGEPGQCFPLKGSEGYVQIRLRGPIIPEAFTLEHVAKSVAYDRSSAPKDCRVSGSLQGPESSAETENMQLLTEF
SQ  TYDLDRSNAQTFNILESSSSGLIDTVRLDFTSNHGSDSHTCIYRFRVHGRAPDPVPVVGTNLDQDSSPESE
//
ID  Q8WXH0;
PN  Nesprin-2;
GN  SYNE2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:15671068}; Single- pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton. Mitochondrion. Nucleus, nucleoplasm. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000305|PubMed:15671068}. Note=Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter soluble isoforms can be found in the cytoplasm and within the nucleus. [Isoform 8]: Cell junction, focal adhesion {ECO:0000269|PubMed:22768332}. Note=In U2OS cells. {ECO:0000269|PubMed:22768332}.
DR  UNIPROT: Q8WXH0;
DR  UNIPROT: B4DND7;
DR  UNIPROT: B4DPR6;
DR  UNIPROT: I6XXQ5;
DR  UNIPROT: Q540G1;
DR  UNIPROT: Q86YP9;
DR  UNIPROT: Q8N1S3;
DR  UNIPROT: Q8NF49;
DR  UNIPROT: Q8TER7;
DR  UNIPROT: Q8WWW3;
DR  UNIPROT: Q8WWW4;
DR  UNIPROT: Q8WWW5;
DR  UNIPROT: Q8WXH1;
DR  UNIPROT: Q9NU50;
DR  UNIPROT: Q9UFQ4;
DR  UNIPROT: Q9Y2L4;
DR  UNIPROT: Q9Y4R1;
DR  PDB: 4DXS;
DR  PDB: 4FI9;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DR  OMIM: 608442;
DR  OMIM: 612999;
DR  DisGeNET: 23224;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 may act redundantly. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000250|UniProtKB:Q6ZWQ0, ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:22945352}.
DE  Disease: Emery-Dreifuss muscular dystrophy 5, autosomal dominant (EDMD5) [MIM:612999]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O94901; IntAct: EBI-2372294,EBI-2796904; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-2372294,EBI-529989; Score: 0.37
DE  Interaction: Q8TDR0-2; IntAct: EBI-2372294,EBI-11946508; Score: 0.37
DE  Interaction: Q9UKE5; IntAct: EBI-2372294,EBI-1051794; Score: 0.37
DE  Interaction: Q96MT8-2; IntAct: EBI-2372294,EBI-21369329; Score: 0.37
DE  Interaction: Q9NV70; IntAct: EBI-2372294,EBI-1045313; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-2372294,EBI-366182; Score: 0.37
DE  Interaction: Q99459; IntAct: EBI-2372294,EBI-374880; Score: 0.37
DE  Interaction: O60239; IntAct: EBI-2372294,EBI-624860; Score: 0.37
DE  Interaction: Q9GZM8; IntAct: EBI-2372294,EBI-928842; Score: 0.37
DE  Interaction: Q9UH99; IntAct: EBI-1044964,EBI-2372294; Score: 0.77
DE  Interaction: Q16543; IntAct: EBI-295634,EBI-2372294; Score: 0.35
DE  Interaction: P29991; IntAct: EBI-8826656,EBI-2372294; Score: 0.37
DE  Interaction: Q9NWT6; IntAct: EBI-745632,EBI-2372294; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-2372294; Score: 0.35
DE  Interaction: Q5VYV7; IntAct: EBI-2370881,EBI-2372294; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-2551470,EBI-2372294; Score: 0.35
DE  Interaction: Q7Z569; IntAct: EBI-2372294,EBI-349900; Score: 0.37
DE  Interaction: P26447; IntAct: EBI-717058,EBI-2372294; Score: 0.35
DE  Interaction: O43172; IntAct: EBI-718395,EBI-2372294; Score: 0.35
DE  Interaction: Q9WTX6; IntAct: EBI-1551052,EBI-2372294; Score: 0.35
DE  Interaction: Q5TBB1; IntAct: EBI-9027329,EBI-2372294; Score: 0.35
DE  Interaction: Q9D7F7; IntAct: EBI-11116446,EBI-2372294; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-990792,EBI-2372294; Score: 0.35
DE  Interaction: Q14149; IntAct: EBI-2556145,EBI-2372294; Score: 0.35
DE  Interaction: O00267; IntAct: EBI-710464,EBI-2372294; Score: 0.35
DE  Interaction: Q8TBP0; IntAct: EBI-11116618,EBI-2372294; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-714559,EBI-2372294; Score: 0.35
DE  Interaction: Q9UKG1; IntAct: EBI-741243,EBI-2372294; Score: 0.51
DE  Interaction: Q8IZP0; IntAct: EBI-375446,EBI-2372294; Score: 0.37
DE  Interaction: Q86Y22; IntAct: EBI-2372294,EBI-373279; Score: 0.40
DE  Interaction: O00186; IntAct: EBI-2372294,EBI-2803005; Score: 0.40
DE  Interaction: P78527; IntAct: EBI-352053,EBI-2372294; Score: 0.40
DE  Interaction: P11021; IntAct: EBI-354921,EBI-2372294; Score: 0.40
DE  Interaction: P62424; IntAct: EBI-354172,EBI-2372294; Score: 0.40
DE  Interaction: P06748; IntAct: EBI-78579,EBI-2372294; Score: 0.40
DE  Interaction: Q14696; IntAct: EBI-6165891,EBI-2372294; Score: 0.40
DE  Interaction: P49286; IntAct: EBI-1188341,EBI-2372294; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0031527;
GO  GO:0005925;
GO  GO:0016021;
GO  GO:0045111;
GO  GO:0031258;
GO  GO:0034993;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0051642;
GO  GO:0090286;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0021817;
GO  GO:0030335;
GO  GO:1902017;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MASSPELPTEDEQGSWGIDDLHISLQAEQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLP
SQ  RDKGSNTFQCRINIEHALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTIILHFHIEKLAQTLSCNYNQPSLDDVSVVD
SQ  SSPASSPPAKKCSKVQARWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKD
SQ  NLREAFRIAEQELKIPRLLEPEDVDVVDPDEKSIMTYVAQFLQYSKDAPGTGEEAQGKVKDAMGWLTLQKEKLQKLLKDS
SQ  ENDTYFKKYNSLLSFMESFNEEKKSFLDVLSIKRDLDELDKDHLQLREAWDGLDHQINAWKIKLNYALPPPLHQTEAWLQ
SQ  EVEELMDEDLSASQDHSQAVTLIQEKMTLFKSLMDRFEHHSNILLTFENKDENHLPLVPPNKLEEMKRRINNILEKKFIL
SQ  LLEFHYYKCLVLGLVDEVKSKLDIWNIKYGSRESVELLLEDWHKFIEEKEFLARLDTSFQKCGEIYKNLAGECQNINKQY
SQ  MMVKSDVCMYRKNIYNVKSTLQKVLACWATYVENLRLLRACFEETKKEEIKEVPFETLAQWNLEHATLNEAGNFLVEVSN
SQ  DVVGSSISKELRRLNKRWRKLVSKTQLEMNLPLMIKKQDQPTFDNSGNILSKEEKATVEFSTDMSVELPENYNQNIKAGE
SQ  KHEKENEEFTGQLKVAKDVEKLIGQVEIWEAEAKSVLDQDDVDTSMEESLKHLIAKGSMFDELMARSEDMLQMDIQNISS
SQ  QESFQHVLTTGLQAKIQEAKEKVQINVVKLIAALKNLTDVSPDLDIRLKMEESQKELESYMMRAQQLLGQRESPGELISK
SQ  HKEALIISNTKSLAKYLKAVEELKNNVTEDIKMSLEEKSRDVCAKWESLHHELSLYVQQLKIDIEKGKLSDNILKLEKQI
SQ  NKEKKLIRRGRTKGLIKEHEACFSEEGCLYQLNHHMEVLRELCEELPSQKSQQEVKRLLKDYEQKIERLLKCASEIHMTL
SQ  QPTAGGTSKNEGTITTSENRGGDPHSEAPFAKSDNQPSTEKAMEPTMKFSLASVLRPLQEESIMEKDYSASINSLLERYD
SQ  TYRDILEHHLQNNKFRITSDFSSEEDRSSSCLQAKLTDLQVIKNETDARWKEFEIISLKLENHVNDIKKPFVIKERDTLK
SQ  ERERELQMTLNTRMESLETALRLVLPVEKASLLLCGSDLPLHKMAIQGFHLIDADRIYQHLRNIQDSIAKQIEICNRLEE
SQ  PGNFVLKELHPFDLHAMQNIILKYKTQFEGMNHRVQRSEDTLKALEDFLASLRTAKLSAEPVTDLSASDTQVAQENTLTV
SQ  KNKEGEIHLMKDKAKHLDKCLKMLDMSFKDAERGDDTSCENLLDAFSIKLSETHGYGVQEEFTEENKLLEACIFKNNELL
SQ  KNIQDVQSQISKIGLKDPTVPAVKHRKKSLIRLDKVLDEYEEEKRHLQEMANSLPHFKDGREKTVNQQCQNTVVLWENTK
SQ  ALVTECLEQCGRVLELLKQYQNFKSILTTLIQKEESVISLQASYMGKENLKKRIAEIEIVKEEFNEHLEVVDKINQVCKN
SQ  LQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRALALWDKLFNLKNVIDEWTEKALQKMELHQLTEEDRE
SQ  RLKEELQVHEQKTSEFSRRVAEIQFLLQSSEIPLELQVMESSILNKMEHVQKCLTGESNCHALSGSTAELREDLDQAKTQ
SQ  IGMTESLLKALSPSDSLEIFTKLEEIQQQILQQKHSMILLENQIGCLTPELSELKKQYESVSDLFNTKKSVLQDHFSKLL
SQ  NDQCKNFNDWFSNIKVNLKECFESSETKKSVEQKLQKLSDFLTLEGRNSKIKQVDSVLKHVKKHLPKAHVKELISWLVGQ
SQ  EFELEKMESICQARAKELEDSLQQLLRLQDDHRNLRKWLTNQEEKWKGMEEPGEKTELFCQALARKREQFESVAQLNNSL
SQ  KEYGFTEEEEIIMEATCLMDRYQTLLRQLSEIEEEDKLLPTEDQSFNDLAHDVIHWIKEIKESLMVLNSSEGKMPLEERI
SQ  QKIKEIILLKPEGDARIETIMKQAESSEAPLVQKTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIE
SQ  LKKKQEAGFALQHGLQEKKAQLKIYKKFLKKAQDLTSLLKELKSQGNYLLECTKNPSFSEEPWLEIKHLHESLLQQLQDS
SQ  VQNLDGHVREHDSYQVCVTDLNTTLDNFSKEFVSFSDKPVDQIAVEEKLQKLQELENRLSLQDGTLKKILALAKSVKQNT
SQ  SSVGQKIIKDDIKSLQCKQKDLENRLASAKQEMECCLNSILKSKRSTEKKGKFTLPGREKQATSDVQESTQESAAVEKLE
SQ  EDWEINKDSAVEMAMSKQLSLNAQESMKNTEDERKVNELQNQPLELDTMLRNEQLEEIEKLYTQLEAKKAAIKPLEQTEC
SQ  LNKTETGALVLHNIGYSAQHLDNLLQALITLKKNKESQYCVLRDFQEYLAAVESSMKALLTDKESLKVGPLDSVTYLDKI
SQ  KKFIASIEKEKDSLGNLKIKWENLSNHVTDMDKKLLESQIKQLEHGWEQVEQQIQKKYSQQVVEYDEFTTLMNKVQDTEI
SQ  SLQQQQQHLQLRLKSPEERAGNQSMIALTTDLQATKHGFSVLKGQAELQMKRIWGEKEKKNLEDGINNLKKQWETLEPLH
SQ  LEAENQIKKCDIRNKMKETILWAKNLLGELNPSIPLLPDDILSQIRKCKVTHDGILARQQSVESLAEEVKDKVPSLTTYE
SQ  GSDLNNTLEDLRNQYQMLVLKSTQRSQQLEFKLEERSNFFAIIRKFQLMVQESETLIIPRVETAATEAELKHHHVTLEAS
SQ  QKELQEIDSGISTHLQELTNIYEELNVFERLFLEDQLKNLKIRTNRIQRFIQNTCNEVEHKIKFCRQFHEKTSALQEEAD
SQ  SIQRNELLLNQEVNKGVKEEIYNLKDRLTAIKCCILQVLKLKKVFDYIGLNWDFSQLDQLQTQVFEKEKELEEKIKQLDT
SQ  FEEEHGKYQALLSKMRAIDLQIKKMTEVVLKAPDSSPESRRLNAQILSQRIEKAKCLCDEIIKKLNENKTFDDSFKEKEI
SQ  LQIKLNAEENDKLYKVLQNMVLELSPKELDEKNCQDKLETSLHVLNQIKSQLQQPLLINLEIKHIQNEKDNCEAFQEQVW
SQ  AEMCSIKAVTAIEKQREENSSEASDVETKLREFEDLQMQLNTSIDLRTNVLNDAYENLTRYKEAVTRAVESITSLEAIII
SQ  PYRVDVGNPEESLEMPLRKQEELESTVAHIQDLTEKLGMISSPEAKLQLQYTLQELVSKNSAMKEAFKAQETEAERYLEN
SQ  YKCYRKMEEDIYTNLSKMETVLGQSMSSLPLSYREALERLEQSKALVSNLISTKEELMKLRQILRLLRLRCTENDGICLL
SQ  KIVSALWEKWLSLLEAAKEWEMWCEELKQEWKFVSEEIEREAIILDNLQEELPEISKTKEAATTEELSELLDCLCQYGEN
SQ  VEKQQLLLTLLLQRIRSIQNVPESSGAVETVPAFQEITSMKERCNKLLQKVQKNKELVQTEIQERHSFTKEIIALKNFFQ
SQ  QTTTSFQNMAFQDHPEKSEQFEELQSILKKGKLTFENIMEKLRIKYSEMYTIVPAEIESQVEECRKALEDIDEKISNEVL
SQ  KSSPSYAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLNELDSEVQDIVEQDPGQAQEWMDNLM
SQ  IPFQQYQQVSQRAECRTSQLNKATVKMEEYSDLLKSTEAWIENTSHLLANPADYDSLRTLSHHASTVQMALEDSEQKHNL
SQ  LHSIFMDLEDLSIIFETDELTQSIQELSNQVTALQQKIMESLPQIQRMADDVVAIESEVKSMEKRVSKIKTILLSKEIFD
SQ  FSPEEHLKHGEVILENIRPMKKTIAEIVSYQVELRLPQTGMKPLPVFQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNE
SQ  WDEEIENLKQILNNYSAQFSLEHMSPDQADKLPQLQGEIERMEKQILSLNQRKEDLLVDLKATVLNLHQHLKQEQEGVER
SQ  DRLPAVTSEEGGVAERDASERKLNRRGSMSYLAAVEEEVEESSVKSDNGDEKAEPSPQSWSSLWKHDKDMEEDRASSSSG
SQ  TIVQEAYGKISTSDNSMAQILTPDSLNTEQGPECSLRPNQTEEGTTPPIEADTLDSSDAQGGLEPRVEKTRPEPTEVLHA
SQ  CKTQVAELELWLQQANVAVEPETLNADMQQVLEQQLVGCQAMLTEIEHKVAFLLETCKDQGLGDNGATQHEAEALSLKLK
SQ  TVKCNLEKVQMMLQEKHSEDQHPTILKKSSEPEHQEALQPVNLSELESIVTERPQFSRQKDFQQQQVLELKPMEQKDFIK
SQ  FIEFNAKKMWPQYCQHDNDTTQESSASNQASSPENDVPDSILSPQGQNGDKWQYLHHELSSKIKLPLPQLVEPQVSTNMG
SQ  ILPSVTMYNFRYPTTEELKTYTTQLEDLRQEASNLQTQENMTEEAYINLDKKLFELFLTLSQCLSSVEEMLEMPRLYRED
SQ  GSGQQVHYETLALELKKLYLALSDKKGDLLKAMTWPGENTNLLLECFDNLQVCLEHTQAAAVCRSKSLKAGLDYNRSYQN
SQ  EIKRLYHQLIKSKTSLQQSLNEISGQSVAEQLQKADAYTVELENAESRVAKLRDEGERLHLPYALLQEVYKLEDVLDSMW
SQ  GMLRARYTELSSPFVTESQQDALLQGMVELVKIGKEKLAHGHLKQTKSKVALQAQIENHKVFFQKLVADMLLIQAYSAKI
SQ  LPSLLQNRETFWAEQVTEVKILEEKSRQCGMKLQSLLQKWEEFDENYASLEKDLEILISTLPSVSLVEETEERLVERISF
SQ  YQQIKRNIGGKHARLYQTLNEGKQLVASVSCPELEGQIAKLEEQWLSLNKKIDHELHRLQALLKHLLSYNRDSDQLTKWL
SQ  ESSQHTLNYWKEQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTATLRASLAQFEQKWTML
SQ  ITQLPDIQEKLHQLQMEKLPSRKAITEMISWMNNVEHQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDYKQWIVDFVNQ
SQ  SLLQLSTCDVESKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLKTLQKPE
SQ  SVISVQKLLLDCQDIENQLAIKSKALDELKQSYLTLESGAVPLLEDTASRIDELFQKRSSVLTQVNQLKTSMQSVLQEWK
SQ  IYDQLYDEVNMMTIRFWYCMEHSKPVVLSLETLRCQVENLQSLQDEAESSEGSWEKLQEVIGKLKGLCPSVAEIIEEKCQ
SQ  NTHKRWTQVNQAIADQLQKAQSLLQLWKAYSNAHGEAAARLKQQEAKFQQLANISMSGNNLAEILPPALQDIKELQHDVQ
SQ  KTKEAFLQNSSVLDRLPQPAESSTHMLLPGPLHSLQRAAYLEKMLLVKANEFEFVLSQFKDFGVRLESLKGLIMHEEENL
SQ  DRLHQQEKENPDSFLNHVLALTAQSPDIEHLNEVSLKLPLSDVAVKTLQNMNRQWIRATATALERCSELQGIGLNEKFLY
SQ  CCEKWIQLLEKIEEALKVDVANSLPELLEQQKTYKMLEAEVSINQTIADSYVTQSLQLLDTTEIENRPEFITEFSKLTDR
SQ  WQNAVQGVRQRKGDVDGLVRQWQDFTTSVENLFRFLTDTSHLLSAVKGQERFSLYQTRSLIHELKNKEIHFQRRRTTCAL
SQ  TLEAGEKLLLTTDLKTKESVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETWDQCEKKIKELKSRLQVLKAQSEDPLPEL
SQ  HEDLHNEKELIKELEQSLASWTQNLKELQTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRLNTWV
SQ  VFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDCMEEINLFSENKLQLKQMGDQLIKASNKSRAAEIDDKLNKIN
SQ  DRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPVVYDVCDDQEIQKRLAEQQDLQRDIEQHSAGV
SQ  ESVFNICDVLLHDSDACANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQKFLDDYSRFEDWLKSAERTAA
SQ  CPNSSEVLYTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDTASRLKQMVHEGNQRWDNLQRRVTAVLRRL
SQ  RHFTNQREEFEGTRESILVWLTEMDLQLTNVEHFSESDADDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPLDAV
SQ  LIEDELEELHRYCQEVFGRVSRFHRRLTSCTPGLEDEKEASENETDMEDPREIQTDSWRKRGESEEPSSPQSLCHLVAPG
SQ  HERSGCETPVSVDSIPLEWDHTGDVGGSSSHEEDEEGPYYSALSGKSISDGHSWHVPDSPSCPEHHYKQMEGDRNVPPVP
SQ  PASSTPYKPPYGKLLLPPGTDGGKEGPRVLNGNPQQEDGGLAGITEQQSGAFDRWEMIQAQELHNKLKIKQNLQQLNSDI
SQ  SAITTWLKKTEAELEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQSRLRQLSL
SQ  LWEAAQGAVDSWRGGLRQSLMQCQDFHQLSQNLLLWLASAKNRRQKAHVTDPKADPRALLECRRELMQLEKELVERQPQV
SQ  DMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQDLMALQGTQNPASPLPSFDEVDSGDQPPATSVPAPRAK
SQ  QFRAVRTTEGEEETESRVPGSTRPQRSFLSRVVRAALPLQLLLLLLLLLACLLPSSEEDYSCTQANNFARSFYPMLRYTN
SQ  GPPPT
//
ID  Q20745;
PN  Nuclear migration and anchoring protein unc-84;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:27956467, ECO:0000305|PubMed:21411627}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=Associated with nuclei during interphase, prophase, prometaphase, metaphase and early anaphase (PubMed:11907270). Released from nuclear membrane in the same time that the nuclear envelope disassembly, during late anaphase, and begins to reaccumulate in early telophase (PubMed:11907270). Localization at the nuclear envelope depends on lmn-1 (PubMed:11748140, PubMed:11907270). Co-localizes with unc-83 at the nuclear envelope, but its localization at the nuclear envelope does not depend on unc-83 (PubMed:11748140, PubMed:11907270). {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270}.
DR  UNIPROT: Q20745;
DR  UNIPROT: Q9U475;
DR  UNIPROT: Q9U476;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in nuclear migration and anchoring in hypodermal precursor cells (PubMed:10375507, PubMed:11748140, PubMed:12169658, PubMed:11907270, PubMed:16481402, PubMed:20921138, PubMed:21411627, PubMed:23150597, PubMed:25023515, PubMed:25057012). Most likely recruits anc-1 to the nuclear envelope where anc-1 functions to tether the nucleus to the actin cytoskeleton (PubMed:12169658). Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it recruits and interacts with unc-83 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules (PubMed:11748140, PubMed:16481402). Its role in nuclear migration may be in association with lamin, lmn-1 (PubMed:25057012). Regulates nuclear migrations in one-cell embryos, controlling the posterior migration of the male pronucleus following fertilization (PubMed:21798253). Not required for centrosome attachment to the nucleus (PubMed:10375507, PubMed:11907270). Plays a role in the maintenance of the nuclear envelope architecture in body wall muscle cells (PubMed:25023515). May be involved in DNA damage repair through an association with zyg-12 (PubMed:27956467). Potentially has roles in homologous recombination, double strand break repair and meiotic recombination (PubMed:27956467). Specifically, may in part inhibit non-homologous end joining repair, most likely through recruiting fan-1 to the nucleoplasm, to facilitate the repair of DNA cross-links (PubMed:27956467). {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:20921138, ECO:0000269|PubMed:21411627, ECO:0000269|PubMed:21798253, ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:25057012, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: P34258; IntAct: EBI-322705,EBI-313630; Score: 0.37
DE  Interaction: Q23064; IntAct: EBI-2902228,EBI-313630; Score: 0.37
DE  Interaction: O45904; IntAct: EBI-313630,EBI-316320; Score: 0.37
DE  Interaction: G5EFL5; IntAct: EBI-313630,EBI-316352; Score: 0.37
DE  Interaction: P90740; IntAct: EBI-313630,EBI-313626; Score: 0.37
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0040011;
GO  GO:0007399;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0018991;
GO  GO:0009791;
GO  GO:0030334;
GO  GO:0040025;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:21411627};
SQ  MAPATEADNNFDTHEWKSEFASTRSGRNSPNIFAKVRRKLLLTPPVRNARSPRLTEEELDALTGDLPYATNYTYAYSKIY
SQ  DPSLPDHWEVPNLGGTTSGSLSEQEHWSAASLSRQLLYILRFPVYLVLHVITYILEAFYHVIKITSFTIWDYLLYLVKLA
SQ  KTRYYAYQDHRRRTALIRNRQEPFSTKAARSIRRFFEILVYVVLTPYRMLTRSNNGVEQYQYRSIKDQLENERASRMTTR
SQ  SQTLERSRKFDGLSKSPARRAAPAFVKTSTITRITAKVFSSSPFGEGTSENITPTVVTTRTVKQRSVTPRFRQTRATREA
SQ  ITRALDTPELEIDTPLSTYGLRSRGLSHLNTPEPTFDIGHAAATSTPLFPQETYNYQYEEATGNKIKTAFTWLGYLILFP
SQ  FFAARHVWYTFYDYGKSAYMKLTNYQQAPMETIHVRDINEPAPSSSDVHDAVGVSWRIRIADFLSSFVATIVEAHQVVFA
SQ  MFKGGIVETVSYFGGLFAGLTDKKSSKFSWCQILGLLLALLFAIFLLGFLTSDNTAIRVKEITKDKNASKKSEGSLPAVP
SQ  IWISAANHVKHYTWMVKEFVVDIAFDTYNYGKSTIGRLGTTPRYAWDLIASGCGAVGNGLKSVLSSSFRFIDFCAGKLFY
SQ  YGSDGFLSANKSIGTFFNGCYETLYNGCTAIVGHTKSFIYNASNAVYNFFSTIFAGLLNFSTSSQNSILSLLKSFGTGIT
SQ  NIFYNFIYAPIAGVFNFAGDNYMYFFNEVAAVFGKVYNSVVSVLKTVINWILFLIAYPFSLCTRAWIRISQYAPEDVVQV
SQ  IPIPQAITPTPDVERIVEEPLRKVTDVEDEELVIIPAPAPKPIPVPAPTPAPVIIHQTNVVETVDKDAIIKEVTEKLRAE
SQ  LSAQFQQELSAKFEQNYNTIIEQLKMENTNIQYDKNHLEAIIRQMIYEYDTDKTGKVDYALESSGGAVVSTRCSETYKSY
SQ  TRLEKFWDIPIYYFHYSPRVVIQRNSKSLFPGECWCFKESRGYIAVELSHFIDVSSISYEHIGSEVAPEGNRSSAPKGVL
SQ  VWAYKQIDDLNSRVLIGDYTYDLDGPPLQFFLAKHKPDFPVKFVELEVTSNYGAPFTCLYRLRVHGKVVQV
//
ID  Q6ZWR6;
PN  Nesprin-1;
GN  Syne1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6ZWR6;
DR  UNIPROT: Q8K3T7;
DR  UNIPROT: Q9ERT7;
DR  UNIPROT: Q9ERT8;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus- centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenenis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9D415; IntAct: EBI-400152,EBI-10760754; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-7280013,EBI-10760754; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-300895,EBI-10760754; Score: 0.35
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0044327;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0030017;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0005102;
GO  GO:0051642;
GO  GO:0090286;
GO  GO:0007030;
GO  GO:0042692;
GO  GO:2001054;
GO  GO:0061886;
GO  GO:0090292;
GO  GO:0007097;
GO  GO:0002053;
GO  GO:0048260;
GO  GO:1902017;
GO  GO:0048814;
GO  GO:1903353;
GO  GO:0099149;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MATSRASSRSHRDITNVMQRLQDEQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQG
SQ  HRVKRIHAVANIGTALKFLEGRKIKLVNINATDIADGRPSIVLGLMWTIILYFQIEELTSNLPQLQSLSSSASSVDSMVS
SQ  TETASPPSKRKVAAKIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLE
SQ  DAFTIAETQLGIPRLLDPEDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDGQEDDVVFVGFTNNIALLLGFQRDDRLIL
SQ  KETKVWIEQFERDFTRAQMTESSLQDKYQAFKHFRVQYEMKRKQVEHIIQPLQRDGKLTLDQALVKQCWERVSSRLFDWH
SQ  IQLDKSLPAPLGTIGAWLYRAEVALREEITIQQVHEETANTIQRKLEQHKDLLQNTDAHKRAFHEIYQTRSVNGIPMPPD
SQ  QLEDMAERFHFVSSTSELHLMKMEFLELKYRLLSLLVLAESKLKSWIIKYGRRESVELLLQSYISFIENSKFFEQYEVTY
SQ  QILKQTADIYVKAEGSVEEAENVMKFMSEATAQWRNLSVEVRSVRSMLEEVISNWDRYGDTVASLQAWLEDAEKMLSQSE
SQ  HAKKDFFRNLPHWIQQHTAMNDAGNFLIETCDEIVSRDLKQQLLLLNGRWRELFMEVKQYARADEMDRMKKEYIDVTTTL
SQ  FGFATEAHRKLSEPLEVSFINVKLLIQDLEDLEKRVPVMDAQYKMIAKKAHLFAKESPQEEANEMLTTMSKLKEQLSKVK
SQ  ECCSPLLYEAQQLTVPLEELETQITSFYDSLGKINEILSVLEQEAQSSTLFKQKHQELLASQENCKKSLTLIEKGSQSVQ
SQ  KLVTSSQARKPWDHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAQEGLEEKGDPEELL
SQ  RRHTEFFSQLDQRVLNAFLKACDELTDILPEQEQQGLQEAVRKLHKQWKDLQGEAPYHLLHLKIAVEKDRFSAAVEECRA
SQ  ELEQETKLAPQEGSEKIIKEHRVFFSDKGPHHLCEKRLQLIEELCGKLPVQDPVRDTCGACHTALKELKASIDNTYTMLV
SQ  DDPDKWKDYTSRFSEFSSWVSAKKACLKKIKDEPIDTGNHDEVKHMVDEIRNDITKKGESLSWLKSRLKYLIDISSENEA
SQ  QKRGDELAELSSSFKALVALLSEVEKLLSNFGECVQYKEIVKSSLEGLISGPQESKEEAEMILDSKNLLEAQQLLLHHQQ
SQ  KTKMISAKKRDLQEQMEQAQQGGQAGPGQEELRKLESTLTGLEQSRERQERRIQVSLRKWERFETNKETVVRYLFQTGSS
SQ  HERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKEAAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTME
SQ  MVKSKWDHFGSNFETLSIWILEKENELSSLEASASAADVQISQIKVTIQEIESKIDSIVGLEEEAQSFAQFVTTGESARI
SQ  KAKLTQIRRYWEELQEHARGLEGTILGHLSQQQKFEENLRKIRQSVSEFAERLADPIKICSSAAETYKVLQEHMDLCQAV
SQ  ESLSSTVTMFSASAQKAVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPE
SQ  KDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALFSVASKEDVAVMKLQLEQLDERWGDLPQIISKRMHFLQS
SQ  VLAEHKQFDELLFSFSVWIKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAQDLHPL
SQ  QSKVDDCFQLFEEASQVVERRKLALAQLAEFLQSHACMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESS
SQ  AISLDGTLTKAQCHLKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMD
SQ  RERLKVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRRQIHENQGQCC
SQ  GLIDLVREYQSLKSTVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSKQKELDSFTSKGKHLLSELKKIHSG
SQ  DFSLVKTDMESTLDKWLDVSERIEENMDMLRVSLSIWDDVLSRKDEIEGWSNSSLPKLAENISNLNNSLRAEELLKELES
SQ  EVKIKALKLEDLHSKINNLKELTKNPETPTELQFIEADLRQKLEHAKEITEEARGTLKDFTAQRTQVERFVKDITAWLIN
SQ  VEESLTRCAQTETCEGLKKAKDIRKELQSQQNSITSTQEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQAR
SQ  IQDSLEKHFSGSMKEFQEWFLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQSKLDVVTQEGQTLYAHLPKQIV
SQ  SSIQEQITKANEEFQAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTENLGESKHHISEKKNEVRKVEM
SQ  FLGELLAARESLDKLSQRGQLLSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKD
SQ  VQDRLACAESTLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLEMLKKAWAEAMNSAV
SQ  HAQSTLESVIDQWNDYLEKKSQLEQWMESVDQRLEHPLQLQPGLKEKFSLLDHFQSIVSEAEDHTGALQQLAAKSRELYQ
SQ  KTQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKDHLMYLDAVQEFADWLHSAKEELHRWSDTSGDPSATQKKLLK
SQ  IKELIDSREIGAGRLSRVESLAPAVKQNTAASGCELLNSEMQALRADWRQWEDCLFQTQSSLESLVSEMALSEQEFFGQV
SQ  TQLEQALEQFCTLLKTWAQQLTLLEGKNSDEEILECWHKGREILDALQKAEPMTEDLKSQLNELCRFSRDLSPYSEKVSG
SQ  LIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKITTAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLN
SQ  TMLFKGELLSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKESALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNR
SQ  LYDLPAKRREQQKLQSVLEEIQCYEPQLHRLKEKARQLWEGQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEH
SQ  NRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLKLEALLSVRQEKEIQMKMVVTRGEYVLQSTSLEGSAAVQQQ
SQ  LQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALGKAKLLNEEVLSH
SQ  SSLLETIEVKRAAMTEHYVTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSVHE
SQ  GDTNAHETMLRDLQELQVRCAEGQALLNSVLHTREDVIPSGLPQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRL
SQ  MEQKFQQADEWLKRMEEKINFRSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEEVGTRAQGILDETHISSRMGCQATQL
SQ  TSRYQALLLQVLEQIKFFEEELQCLEETESSLSSYSDWYGSTHKNFKNVATKIDKVDESMMGKKLKTLEVLLKDMEKGHS
SQ  LLKSAREKGERAMKFLAEHEAEALRKEIHTYMEQLKNLTSTVRKECMSLEKGLHLAKEFSDKYKVLAQWMAEYQEILCTP
SQ  EEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQSLKDKIQKLQSDFQDLCSRAKERVFSLEAKVK
SQ  DHEDYNTELQEVEKWLLQMSGRLVAPDLLEMSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHLQAKQ
SQ  KQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDTLQQCQAWISAVQPDLKPSPQPPLSRAEAVKQVKHFRAL
SQ  QEQARTYLDLLCSMCDLSNSSVKNTAKDIQQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDADQQLQNMKRRHTE
SQ  LEINIAQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKNQESPEHKEITHLNDQWQDLCLQSDKLCAQREQDLQRTSSY
SQ  HDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYAIDDLKDCKQKLIEQLGLDDRELVREQTSHLE
SQ  QRWFQLQDLVKRKIQVSVTNLEELNVIQSRFQELMEWAEEQQPNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLK
SQ  SLMKDADRVMADLGLNERKVIQKALSEAQKHVSCLSDLVGQRRKYLNKALSEKTQFLMAVFQATSQIQQHERKIVFREYI
SQ  CLLPDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLV
SQ  SRKHFKEDFDKACHWLKQADIVTFPEINLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLS
SQ  EKLSALPQQFNVIVALAKDKFYKTQEAILARKEYTSLIELTTQSLGDLEDQFLKMRKMPSDLIVEESVSLQQSCSALLGE
SQ  VVALGEAVNELNQKKESFRSTGQPWQPEKMLQLATLYHRLKRQAEQRVSFLEDTTSVYKEHAQMCRQLESQLEVVKREQA
SQ  KVNEETLPAEEKLKVYHSLAGSLQDSGILLKRVATHLEDLSPHLDPTAYEKAKSQVQSWQEELKQMTSDVGELVTECESR
SQ  MVQSIDFQTEMSRSLDWLRRVKAELSGPVCLDLSLQDIQEEIRKIQIHQEEVLSSLRIMSALSHKEQEKFTKAKELISAD
SQ  LEHTLAELQELDGDVQEALRTRQATLTEIYSRCQRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTE
SQ  GQFHSNMEELRGLVARLDPLIKATGKEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVIELMNDAEK
SQ  KLSEFAVLKTSSIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQ
SQ  EKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLLESHDTYLMDLESQQLTLGVLQQRALSMLQDR
SQ  AFPGTEEEVPILRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYLGNPTIEIDTQLEELKR
SQ  LLAEATSHQESIEKIAEEQKNKYLGLYTVLPSEISLQLAEVALDLKIHDQIQEKVQEIEEGKAMSQEFSCKIQKVTKDLT
SQ  TILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELHQQTIRQAENRLSKL
SQ  NQALSHMEEYNEMLETVRKWIEKAKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQHLANVYCTGKL
SQ  SQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLCHRQHLLSEMESL
SQ  KPKMQAVQLCQSALRIPEDVVASLPLCHAALRLQEEASQLQHTAIQQCNIMQAKKHSLIFPPKEAVVQYEQYKQEMKHLQ
SQ  QLIEEAHREIEDKPVATSNIQELQAQISLHEELAQKIKGYQEQIDSLNSKCKMLTMKAKHATMLLTVTEVEGLAEGTEDL
SQ  DRELHPTPSAHPSVVMMTAGRCHTLLSPVTEESGEEGTNSEISSPPACRSPSPVANTEAAVNQDIAYYQALSAEGLQTDA
SQ  ARIPPSAAVSQELYEPGLEPSATAKLGDLQRSWETLKNVISEKQRTLYEVLERQQKYQDSLQSISTKMEAMEMKLGESLE
SQ  PSRSPESQMAEHQALMDEVQMLQDEINGLQVSLAEELVAESQESDPAEQLALQSTLTVLAERMSTIRMKAAGKRQLLEEK
SQ  LSDQLEEQRQEQALQRYRCEADELDHWLLNTKATLDVALGTSQEPMDMDAQLVDCQNMLVEIEQKVVALSQLSVHNENLL
SQ  LEGKAHTKEEAEQLAVKLRLLKGSLGELQRALHDRQLDMQGVTQEKEENDVDFTDTQSPGVQEWLAQARTTRTHQRQSSL
SQ  QQQKEFEQELAEQKSLLRSVASRGEEILTQHSTAEGSGGLGEKPDVLSQELGIAEDQMRVKWESLHQEFSAKQKLLQNIL
SQ  EQEQEQVLYSSPNRLLSGVLPFRGEAQTQDKTSVTSLLDGLSQAFGEASSQSGGTDRQSIHLEQKLYDGVSATSTWLNDV
SQ  EERLFVATAPLPEETEACLFNQEALAKDIKEMSEEMDKNKNLFSQAFPEDSDNRDVIEDTLGCLLGRLSLLDSVVDQRCH
SQ  QMKERLQQILRFQNDLKVLFTSLADSKYIILQKLANVFEQPIVEQMQAIQQAEEGLRDLEGGISELKRWADKLQVEQSAV
SQ  QELSKLQDMYDELLMTVSSRRSSLHQNLALKSQYDKALQDLVDLLDTGQEKMTGDQKIIVCSKEEIQQLLGKHKEYFQGL
SQ  ESHMILTEILFRKIVGFAAVKETQFHTDCMAQASAVLKQAHKRGVELEYILEMWSHLDENRQELSRQLEVIENSIPSVGL
SQ  VEESEDRLVERTNLYQHLKSSLNEYQPKLYQALDDGKRLLMSVSCSELESQLNQLGEHWLSNTNKVSKELHRLETILKHW
SQ  TRYQSEAAALNHWLQCAKDRLAFWTQQSVTVPQELEMVRDHLSAFLEFSKEVDAKSALKSSVTSTGNQLLRLKKVDTAAL
SQ  RAELSRMDSQWTDLLTGIPVVQEKLHQLQMDKLPSRHAISEVMSWISLMESVILKDEEDIRNAIGYKAIHEYLQKYKGFK
SQ  IDLNCKQLTADFVNQSVLQISSQDVESKRSDKTDFAEQLGAMNKSWQLLQGRVGEKIQMLEGLLESWSEYENSVQSLKAW
SQ  FANQERKLKEQHLLGDRNSVENALKDCQELEDLIKAKEKEVEKIEQNGLALIQNKREEVSGSVMSTLQELRQTWISLDRT
SQ  VEQLKIQLTSALGQWSNHKAACDEINGHLMEARYSLSRFRLLTGSSEAVQVQVDNLQNLHDELEKQEGGLQKFGSITNQL
SQ  LKECHPPVAETLSSTLQEVNMRWNNLLEEIAEQLHSSKALLQLWQRYKDYSKQCASAIQRQEEQTSVLLKAATNKDIADD
SQ  EVTKWIQDCNDLLKGLETVKDSLFILRELGEQLGQQVDVSAAAAIQCEQLCFSQRLGALEQALCKQQAVLQAGVVDYETF
SQ  AKSLEALEVWMVEAEGILQGQDPTHSSDLSTIQERMEELKGQMLKFSSLAPDLDRLNELGYRLPLNDKEIKRMQNLNRHW
SQ  SLTSSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEHKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIVD
SQ  GQNLLEQGQVDDREEFSLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLAEVSHLPLSGLGNIPVPL
SQ  QQVRMLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELTDIQEKWKAASMHLEEQKKKLAFLLKDWEK
SQ  CERGIANSLEKLRMFKKRLSQPLPDHHEELHAEQMRCKELENAVGRWTDDLTELMLVRDALAVYLSAEDISMLKERVELL
SQ  QRQWEELCHQVSLRRQQVSERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAVAQENKIQLQ
SQ  EMGERLAKASHESKASEIQYKLSRVKDRWQHLLDLMAARVKKLKETLVAVQQLDKNMGSLRTWLAHMESELAKPIVYDSC
SQ  NSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEET
SQ  WRLWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSACS
SQ  LRQMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEIS
SQ  LNHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKLIRLPVRLPDDHDLSDRELDLEDSTALS
SQ  DLRWQDPSADGMPSPQPSSNPSLSLPQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESASRTLPSEDEEGEEDKEFY
SQ  LRGAVGLSGDPSSLESQMRQLDKALDDSRFQIQQTANILRSKTPTGPDLDTSYKGYMKLLGECSGSIDSVRRLEHKLAEE
SQ  ESFPGFVNLNSTETQTAGVIDRWELLQAQAMSKELRMKQNLQKWQQFNSDLNNIWAWLGETEEELDRLQHLALSTDIHTI
SQ  ESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDLQDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEM
SQ  SHALLLMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVI
SQ  GNRLKLLLKEVSHHIKDLEKLLDMSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKSPRGKCSLSQPGPSVSSPKSR
SQ  STRDGSDSSRSDPRPERVGRAFLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPPL
//
ID  Q4FZC9;
PN  Nesprin-3;
GN  Syne3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum.
DR  UNIPROT: Q4FZC9;
DR  UNIPROT: Q8BMM1;
DR  UNIPROT: Q8C117;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS51049;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:16330710}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005791;
GO  GO:0051015;
GO  GO:0090286;
GO  GO:0007010;
GO  GO:0090150;
GO  GO:0007097;
GO  GO:0051647;
GO  GO:0008360;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MTQQPQEDFERSVEDAQAWMKVIQEQLQVNDNTKGPRAALEARLRETEKICQLESEGMVKVELVLRAAEALLATCQEGQK
SQ  PEILARLRDIKSQWEETVTYMTHCHSRIEWVWLHWSEYLLAQDEFYRWFQKMVVALEPPVELQLGLKEKQWQLSHAQVLL
SQ  HNVDNQAVLLDRLLEEAGSLFSRIGDPSVDEDAQKRMKAEYDAVKARAQRRVDLLAQVAQDHEQYREDVNEFQLWLKAVV
SQ  EKVHSCLGRNCKLATELRLSTLQDIAKDFPRGEESLKRLEEQAVGVIQNTSPLGAEKISGELEEMRGVLEKLRVLWKEEE
SQ  GRLRGLLQSRGDCEQQIQQLEAELGDFKKSLQRLAQEGLEPTVKTATEDELVAQWRLFSGTRAALASEEPRVDRLQTQLK
SQ  KLVTFPDLQSLSDSVVATIQEYQSMKGKNTRLHNATRAELWQRFQRPLNDLQLWKALAQRLLDITASLPDLASIHTFLPQ
SQ  IEAALTESSRLKEQLAMLQLKTDLLGSIFGQERAATLLEQVTSSVRDRDLLHNSLLQRKSKLQSLLVQHKDFGVAFDPLN
SQ  RKLLDLQARIQAEKGLPRDLPGKQVQLLRLQGLQEEGLDLGTQIEAVRPLAHGNSKHQQKVDQISCDQQALQRSLEDLVD
SQ  RCQQNVREHCTFSHRLSELQLWITMATQTLESHQGDVRLWDAESQEAGLETLLSEIPEKEVQVSLLQALGQLVMKKSSPE
SQ  GATMVQEELRKLMESWQALRLLEENMLSLMRNQQLQRTEVDTGKKQVFTNNIPKAGFLINPQDPIPRRQHGANPLEGHDL
SQ  PEDHPQLLRDFEQWLQAENSKLRRIITMRVATAKDLRTREVKLQELEARIPEGQHLFENLLRLRPARDPSNELEDLRYRW
SQ  MLYKSKLKDSGHLLTESSPGELTAFQKSRRQKRWSPCSLLQKACRVALPLQLLLLLFLLLLFLLPAGEEERSCALANNFA
SQ  RSFALMLRYNGPPPT
//
ID  Q92621;
PN  Nuclear pore complex protein Nup205;
GN  NUP205;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}; Peripheral membrane protein {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}. Note=Localized near the center, on both the cytoplasmic and nuclear side, of the NPC core structure. {ECO:0000269|PubMed:15229283}.
DR  UNIPROT: Q92621;
DR  UNIPROT: A6H8X3;
DR  UNIPROT: Q86YC1;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  Pfam: PF11894;
DR  OMIM: 614352;
DR  OMIM: 616893;
DR  DisGeNET: 23165;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC (PubMed:15229283). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}.
DE  Disease: Nephrotic syndrome 13 (NPHS13) [MIM:616893]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. {ECO:0000269|PubMed:26878725}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-1045046; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-286779,EBI-1045046; Score: 0.35
DE  Interaction: P50613; IntAct: EBI-1245958,EBI-1045046; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-1045046; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-1045046; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-1045046; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-1045046; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-1045046; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-1045046; Score: 0.40
DE  Interaction: P62491; IntAct: EBI-745098,EBI-1045046; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-399437,EBI-1045046; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-1045046; Score: 0.35
DE  Interaction: P49336; IntAct: EBI-394377,EBI-1045046; Score: 0.35
DE  Interaction: Q96I36; IntAct: EBI-6570698,EBI-1045046; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-448665,EBI-1045046; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1045046; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-1045046; Score: 0.35
DE  Interaction: Q13286; IntAct: EBI-3248760,EBI-1045046; Score: 0.40
DE  Interaction: Q70EL3; IntAct: EBI-2512953,EBI-1045046; Score: 0.40
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-1045046; Score: 0.53
DE  Interaction: Q9NYD6; IntAct: EBI-1188075,EBI-1045046; Score: 0.37
DE  Interaction: Q99P88; IntAct: EBI-2551981,EBI-1045046; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-1045046; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11333674,EBI-1045046; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-1045046; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-2873150,EBI-1045046; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-2563266,EBI-1045046; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-1045046; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-1045046; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-1045046; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-80168,EBI-1045046; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-2811583,EBI-1045046; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-1045046; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-1045046; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-1047508,EBI-1045046; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-356625,EBI-1045046; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-1045046; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-358318,EBI-1045046; Score: 0.35
DE  Interaction: P49841; IntAct: EBI-373586,EBI-1045046; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-624291,EBI-1045046; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-1045046; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-1045046; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1045046; Score: 0.35
DE  Interaction: P27105; IntAct: EBI-1211440,EBI-1045046; Score: 0.51
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-1045046; Score: 0.53
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-1045046; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-1045046; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-1045046; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-1045046; Score: 0.35
DE  Interaction: Q9Y5J5; IntAct: EBI-1045046,EBI-1055859; Score: 0.40
DE  Interaction: Q13418; IntAct: EBI-1045046,EBI-747644; Score: 0.40
DE  Interaction: Q9Y5V3; IntAct: EBI-1045046,EBI-716006; Score: 0.40
DE  Interaction: Q99623; IntAct: EBI-1045046,EBI-358348; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-1045046,EBI-447544; Score: 0.40
DE  Interaction: P37268; IntAct: EBI-1045046,EBI-714550; Score: 0.40
DE  Interaction: Q14CB8-1; IntAct: EBI-25409092,EBI-1045046; Score: 0.35
DE  Interaction: Q86YR7-3; IntAct: EBI-25410117,EBI-1045046; Score: 0.35
DE  Interaction: Q6ZRI8-2; IntAct: EBI-25410664,EBI-1045046; Score: 0.35
DE  Interaction: P06821; IntAct: EBI-2547404,EBI-1045046; Score: 0.35
DE  Interaction: Q9UPV0; IntAct: EBI-3937015,EBI-1045046; Score: 0.35
DE  Interaction: P56180-2; IntAct: EBI-11960323,EBI-1045046; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12577179,EBI-1045046; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585275,EBI-1045046; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-1045046; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-1045046; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-6050648,EBI-1045046; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12561553,EBI-1045046; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12562139,EBI-1045046; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579807,EBI-1045046; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-2547514,EBI-1045046; Score: 0.35
GO  GO:0043657;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATPLAVNSAASLWGPYKDIWHKVGNALWRRQPEAVHLLDKILKKHKPDFISLFKNPPKNVQQHEKVQKASTEGVAIQGQ
SQ  QGTRLLPEQLIKEAFILSDLFDIGELAAVELLLAGEHQQPHFPGLTRGLVAVLLYWDGKRCIANSLKALIQSRRGKTWTL
SQ  ELSPELASMTTRFTDELMEQGLTYKVLTLVSQIDVNNEFEKLQRERGLGSEKHRKEVSDLIKECRQSLAESLFAWACQSP
SQ  LGKEDTLLLIGHLERVTVEANGSLDAVNLALLMALLYCFDISFIEQSTEERDDMIHQLPLLTEKQYIATIHSRLQDSQLW
SQ  KLPGLQATVRLAWALALRGISQLPDVTALAEFTEADEAMAELAIADNVFLFLMESVVVSEYFYQEEFYIRRVHNLITDFL
SQ  ALMPMKVKQLRNRADEDARMIHMSMQMGNEPPISLRRDLEHLMLLIGELYKKNPFHLELALEYWCPTEPLQTPTIMGSYL
SQ  GVAHQRPPQRQVVLSKFVRQMGDLLPPTIYIPYLKMLQGLANGPQCAHYCFSLLKVNGSSHVENIQGAGGSPVSWEHFFH
SQ  SLMLYHEHLRKDLPSADSVQYRHLPSRGITQKEQDGLIAFLQLTSTIITWSENARLALCEHPQWTPVVVILGLLQCSIPP
SQ  VLKAELLKTLAAFGKSPEIAASLWQSLEYTQILQTVRIPSQRQAIGIEVELNEIESRCEEYPLTRAFCQLISTLVESSFP
SQ  SNLGAGLRPPGFDPYLQFLRDSVFLRFRTRAYRRAAEKWEVAEVVLEVFYKLLRDYEPQLEDFVDQFVELQGEEIIAYKP
SQ  PGFSLMYHLLNESPMLELALSLLEEGVKQLDTYAPFPGKKHLEKAVQHCLALLNLTLQKENLFMDLLRESQLALIVCPLE
SQ  QLLQGINPRTKKADNVVNIARYLYHGNTNPELAFESAKILCCISCNSNIQIKLVGDFTHDQSISQKLMAGFVECLDCEDA
SQ  EEFVRLEEGSELEKKLVAIRHETRIHILNLLITSLECNPPNLALYLLGFELKKPVSTTNLQDPGVLGCPRTCLHAILNIL
SQ  EKGTEGRTGPVAVRESPQLAELCYQVIYQLCACSDTSGPTMRYLRTSQDFLFSQLQYLPFSNKEYEISMLNQMSWLMKTA
SQ  SIELRVTSLNRQRSHTQRLLHLLLDDMPVKPYSDGEGGIEDENRSVSGFLHFDTATKVRRKILNILDSIDFSQEIPEPLQ
SQ  LDFFDRAQIEQVIANCEHKNLRGQTVCNVKLLHRVLVAEVNALQGMAAIGQRPLLMEEISTVLQYVVGRNKLLQCLHAKR
SQ  HALESWRQLVEIILTACPQDLIQAEDRQLIIRDILQDVHDKILDDEAAQELMPVVAGAVFTLTAHLSQAVLTEQKETSVL
SQ  GPAEAHYAFMLDSCFTSPPPEENPLVGFASIGDSSLYIILKKLLDFILKTGGGFQRVRTHLYGSLLYYLQIAQRPDEPDT
SQ  LEAAKKTMWERLTAPEDVFSKLQRENIAIIESYGAALMEVVCRDACDGHEIGRMLALALLDRIVSVDKQQQWLLYLSNSG
SQ  YLKVLVDSLVEDDRTLQSLLTPQPPLLKALYTYESKMAFLTRVAKIQQGALELLRSGVIVRLAQCQVYDMRPETDPQSMF
SQ  GMRDPPMFIPTPVDRYRQILLPALQLCQVILTSSMAQHLQAAGQVLQFLISHSDTIQAILRCQDVSAGSLQELALLTGII
SQ  SKAALPGILSELDVDVNEGSLMELQGHIGRFQRQCLGLLSRFGGSDRLRQFKFQDDNVEGDKVSKKDEIELAMQQICANV
SQ  MEYCQSLMLQSSPTFQHAVCLFTPSLSETVNRDGPRQDTQAPVVPYWRLPGLGIIIYLLKQSANDFFSYYDSHRQSVSKL
SQ  QNVEQLPPDEIKELCQSVMPAGVDKISTAQKYVLARRRLVKVINNRAKLLSLCSFIIETCLFILWRHLEYYLLHCMPTDS
SQ  QDSLFASRTLFKSRRLQDSFASETNLDFRSGLAIVSQHDLDQLQADAINAFGESLQKKLLDIEGLYSKVRSRYSFIQALV
SQ  RRIRGLLRISRN
//
ID  Q9XZ06;
PN  Nuclear pore complex protein Nup93-1;
GN  Nup93;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:31784359}. Nucleus, nucleoplasm {ECO:0000269|PubMed:31784359}. Note=When not in the nuclear pore complex, can localize to the nuclear lumen proximal to the inner nuclear membrane. {ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9XZ06;
DR  Pfam: PF04097;
DE  Function: Required for nuclear pore complex assembly, maintenance and function (PubMed:20547758, PubMed:22718353). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). Mediates the association between the nuclear pore complex and a subclass of silenced regions bound by Polycomb group (PcG) proteins, enables long-range interactions between Polycomb loci and contributes to repression of polycomb targets (PubMed:31784359). Together with Nup62 and Nup154, contributes to karyosome morphology and chromatin organization including attachment to the nuclear envelope in oocytes and nurse cells (PubMed:26341556). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-179313; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-3411876,EBI-179313; Score: 0.46
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-179313; Score: 0.35
DE  Interaction: P53034; IntAct: EBI-179313,EBI-184606; Score: 0.49
DE  Interaction: P19538; IntAct: EBI-179313,EBI-94976; Score: 0.37
DE  Interaction: Q9VYS8; IntAct: EBI-182389,EBI-179313; Score: 0.37
DE  Interaction: P54360; IntAct: EBI-499647,EBI-179313; Score: 0.37
DE  Interaction: Q9W215; IntAct: EBI-93587,EBI-179313; Score: 0.37
DE  Interaction: Q9VH87; IntAct: EBI-178603,EBI-179313; Score: 0.37
DE  Interaction: P84029; IntAct: EBI-85896,EBI-179313; Score: 0.37
DE  Interaction: A1Z6Z9; IntAct: EBI-116955,EBI-179313; Score: 0.37
DE  Interaction: Q9VHK1; IntAct: EBI-84639,EBI-179313; Score: 0.37
DE  Interaction: Q9VQE0; IntAct: EBI-179313,EBI-169823; Score: 0.37
DE  Interaction: Q9VRS2; IntAct: EBI-97739,EBI-179313; Score: 0.37
DE  Interaction: P35381; IntAct: EBI-129010,EBI-179313; Score: 0.37
DE  Interaction: Q9Y119; IntAct: EBI-157989,EBI-179313; Score: 0.37
DE  Interaction: Q9VQ61; IntAct: EBI-129434,EBI-179313; Score: 0.37
DE  Interaction: P07909-2; IntAct: EBI-209354,EBI-179313; Score: 0.37
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0003682;
GO  GO:0031490;
GO  GO:0017056;
GO  GO:0006325;
GO  GO:0097240;
GO  GO:0006999;
GO  GO:0030717;
GO  GO:0016973;
GO  GO:0031937;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0097298;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLMELLKQAQRLTNETNTDTEVPGVERTMSQVLQATKEFHSRVTQMGTNDLQAHILLGSKGVDLPKLTQKLESLSARQT
SQ  FEPIDPVTETNVQAYLKNERENAILSVIDETNRSIFKSVERQKWRCIYSEWGEEKEALLNALVGPNQQDFPDVQFQIVPT
SQ  AMADEPTPYSQLNGHEQMYAEQIAIHNQSIILGRRPNLLSTLAHVVQDSFNDESVAEMWNVLQFMTALPPVSSTIDPIKN
SQ  RQTSPQFVEQARTYLERRYRTYMRKFIVANLAKARRGGIPSVYHMVRSYVGVTLQGQRALYGLHDVNNGQPLWPHVYYSL
SQ  RSGDMDAAALYLKESGTCPDLLTLLTLRKNGDRDNLMVKLEGQLKLEYNSRLRACTDPYKKAVYVVLLACDPHFTHVELM
SQ  RSIDDFLWMQLSILRRSDQSDSNTEQLTFSGLQSLILEKYGENYFNAREKAALYFQVLTLTGQFEAAIEFLARTEKNRTH
SQ  AIHMAIALNEISMLGTPRSVEQSLLSSDPDDPKPMKRLNLVRLIVMYTKCFERTDTTQALHYYYLLRNFKSENGRGNVML
SQ  TCVCDLLVEKCDDEMLELIFGTEDKKNGLRYGGIYAEFQIHECDKYSLAEMVGDELSKRGDYELAIELYFIGGQLDKALR
SQ  LVNSLLAQVVHQPTQNGSVRNRLGDIINRLDAALVVRKSDVEVQVVVTYTVLTKVMKFFDHYHEGALRSALEILTNNHLI
SQ  PASSLEVDECVTNIKRMGPEVIKVLPDILLASMDIVYQEYVKLMDSNETASGFFDESKCVNKEPAVKHLRDRAKAFTNMA
SQ  ASVPYRMPSTTNQRLVQLEILMH
//
ID  Q9D666;
PN  SUN domain-containing protein 1;
GN  Sun1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}; Single-pass type II membrane protein {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. In round spermatids mainly localizes to the posterior pole of the nucleus. This localization is gradually disappearing during spermiogenesis. In elongated spermatids localizes to anterior regions outside the nucleus indicative for isoform 5. {ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:26842404}. [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000305|PubMed:20711465}. Note=Localized to the anterior pole of spermatids. {ECO:0000305|PubMed:20711465}.
DR  UNIPROT: Q9D666;
DR  UNIPROT: D3Z0V9;
DR  UNIPROT: Q3TIW3;
DR  UNIPROT: Q3TV96;
DR  UNIPROT: Q6B4H0;
DR  UNIPROT: Q80SU8;
DR  UNIPROT: Q8BZ99;
DR  UNIPROT: Q99P23;
DR  PDB: 5YWZ;
DR  Pfam: PF09387;
DR  Pfam: PF07738;
DR  Pfam: PF18580;
DR  PROSITE: PS51469;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:20711465, PubMed:16380439, PubMed:24062341, PubMed:25892231, PubMed:26842404). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (PubMed:19874786). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (PubMed:19874786). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (PubMed:17543860, PubMed:19211677, PubMed:19509342, PubMed:24062341, PubMed:25892231, PubMed:26842404). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (PubMed:17543860). Helps to define the distribution of nuclear pore complexes (NPCs) (PubMed:17724119). Required for efficient localization of SYNE4 in the nuclear envelope (PubMed:23348741). May be involved in nuclear remodeling during sperm head formation in spermatogenenis (PubMed:20711465). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (By similarity). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:17543860, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:19211677, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:23348741, ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}. Isoform 5 may be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN1 isoform 5:SYNE3 LINC complex may tether spermatid nuclei to anterior cytoskeletal structures such as actin filaments present at membraneous junctions of spermatids and Sertoli cells. {ECO:0000305|PubMed:20711465}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8CAM5; IntAct: EBI-11568902,EBI-6752574; Score: 0.35
GO  GO:0002080;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0043231;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0002081;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0090286;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0021817;
GO  GO:0001503;
GO  GO:0009612;
GO  GO:0007283;
GO  GO:0007129;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHKLEPVFDSPRMSRRSLRLVTTASYSSGDSQAIDSHISTSR
SQ  ATPAKGRETRTVKQRRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLK
SQ  GGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAIHGTTSRVYSRDRTLKPRGVSFYLDRTLWLAKSTSSS
SQ  FASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLEIHT
SQ  ATHSQLPQPHRVAGAMGRLCIYTGDLLVQALRRTRAAGWSVAEAVWSVLWLAVSAPGKAASGTFWWLGSGWYQFVTLISW
SQ  LNVFLLTRCLRNICKVFVLLLPLLLLLGAGVSLWGQGNFFSLLPVLNWTAMQPTQRVDDSKGMHRPGPLPPSPPPKVDHK
SQ  ASQWPQESDMGQKVASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKNVVGQHLQEMGTIEPPDAKTDFM
SQ  TFHHDHEVRLSNLEDVLRKLTEKSEAIQKELEETKLKAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLKTSCEQAGA
SQ  RIQETVQLMFSEDQQGGSLEWLLEKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAVNQAGISGIT
SQ  EAQAHIIVNNALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAF
SQ  KGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPKDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPD
SQ  QAFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
//
ID  Q8BJS4;
PN  SUN domain-containing protein 2;
GN  Sun2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}. Endosome membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes. {ECO:0000269|PubMed:24586178}.
DR  UNIPROT: Q8BJS4;
DR  UNIPROT: Q3TBU0;
DR  UNIPROT: Q3U160;
DR  UNIPROT: Q6B4H2;
DR  PDB: 5ED8;
DR  PDB: 5ED9;
DR  Pfam: PF07738;
DR  Pfam: PF18580;
DR  PROSITE: PS51469;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. {ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752, ECO:0000269|PubMed:24586178, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3U1F9; IntAct: EBI-8468834,EBI-646914; Score: 0.40
DE  Interaction: P39428; IntAct: EBI-646914,EBI-520123; Score: 0.37
GO  GO:0005623;
GO  GO:0000794;
GO  GO:0010008;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0000784;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0090286;
GO  GO:0051321;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0031022;
GO  GO:0021817;
GO  GO:0030335;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESY
SQ  IGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQH
SQ  SSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGL
SQ  TYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLE
SQ  RLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEA
SQ  RVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLL
SQ  GDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGM
SQ  VDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTL
SQ  EHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCI
SQ  YRFRVHGEPAH
//
ID  Q8C0V1;
PN  Telomere repeats-binding bouquet formation protein 1;
GN  Terb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres during meiotic prophase (PubMed:24413433). In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane (PubMed:26548954). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}.
DR  UNIPROT: Q8C0V1;
DR  UNIPROT: A1L2Z9;
DR  UNIPROT: E9QPF2;
DR  UNIPROT: Q14CI1;
DR  UNIPROT: Q8C0N5;
DR  PDB: 1X58;
DR  PROSITE: PS50176;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis (PubMed:24885367, PubMed:24413433, PubMed:26548954). Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN- TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA (PubMed:26548954). In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment' (PubMed:26548954). Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex (PubMed:24885367, PubMed:24413433). Also recruits cohesin to telomeres to develop structural rigidity (PubMed:24413433). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954, ECO:0000305|PubMed:24885367}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0000781;
GO  GO:0000784;
GO  GO:0005637;
GO  GO:0003677;
GO  GO:0070197;
GO  GO:0045141;
GO  GO:0007129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESEKPKKTQEMKTDLKLLLECLKYHMGNPLSQKEVLITIHSVCKQNSDAGIYFREIGGLMFIINLAKSSEQSLVKEAAL
SQ  YTLGSIAEENVYCQQSLCTSELFQDLTGLLTNDDSNTNLKRMSVYVLLVLVSNNRNGQTLVREVGCIEVLSQMFRTVLSN
SQ  YELNLSDNSVFQSYLLWSSVCSTLCVCVNNPQNDENQMLCCSLFPCVNEWLMNCMRPEVIRPICSFIGLTLANNTHAQNC
SQ  FVSSGGLDVLCQVLVQLESDSHNTLSSAKLAVIVTKTMDACITDNSAAFTVVLSKYHIVSTLLALLLHESLDSREKFSII
SQ  LAIGHCTEDCEKNQYELLKNNGLPLMIQALTEFKNEDLSKAATYVLHNCKKITGKLSLSLGQNSFGENEIELKDISEKET
SQ  LREHWKAAKEILCRIKQFEKGGKEEKQQNRSGHYKDNTPSMKVNIQTNLKRLCADSTGGTRAEDKDINQSRELRSYKPSE
SQ  IMSKACANENQLTTRKKNTNPVHPFCKEKGQSKIVHETTPSCAQNLDKEKTFDQKDSVSQSSDQVLKHLPHTVKNRKQVP
SQ  ETDPFTLCLDIIDREVGIQATDSCSRMLKYTCSGCIVARKLLNSRNFSKFLHSCAYQCVHHKVIMEAEDKYKNELRKTFI
SQ  CAKKILLTPCRRRQLCKESTASEELKIVHQKPDSKKLPGLEAQALNTSIPEAMERRSPVPGQSGLHKKRRIRKDFTKEEV
SQ  NYLFHGVKTMGNHWNSILWSFPFQKGRRAVDLAHKYHRLIKGPSCAAL
//
ID  P15565;
PN  tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial;
GN  TRM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Mitochondrion. [Isoform 2]: Mitochondrion. Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Predominantly targeted to the nucleus.
DR  UNIPROT: P15565;
DR  UNIPROT: D6VSA6;
DR  UNIPROT: Q9URQ7;
DR  UNIPROT: Q9URQ8;
DR  Pfam: PF02005;
DR  PROSITE: PS51626;
DE  Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs.
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-19543,EBI-8591; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-19543; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-19543; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-19543; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-19543,EBI-8648; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-19543,EBI-3949; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-29684,EBI-19543; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-19543; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-17964,EBI-19543; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-17751,EBI-19543; Score: 0.35
DE  Interaction: Q12060; IntAct: EBI-8287,EBI-19543; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-2186,EBI-19543; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-19863,EBI-19543; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-27500,EBI-19543; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-19543; Score: 0.35
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0004809;
GO  GO:0000049;
GO  GO:0030488;
GO  GO:0002940;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAW
SQ  DNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREV
SQ  IANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCT
SQ  DLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNV
SQ  MSSTMTTYHCSRCGSYHNQPLGRISQREGRNNKTFTKYSVAQGPPVDTKCKFCEGTYHLAGPMYAGPLHNKEFIEEVLRI
SQ  NKEEHRDQDDTYGTRKRIEGMLSLAKNELSDSPFYFSPNHIASVIKLQVPPLKKVVAGLGSLGFECSLTHAQPSSLKTNA
SQ  PWDAIWYVMQKCDDEKKDLSKMNPNTTGYKILSAMPGWLSGTVKSEYDSKLSFAPNEQSGNIEKLRKLKIVRYQENPTKN
SQ  WGPKARPNTS
//
ID  P40066;
PN  Nucleoporin GLE2;
GN  GLE2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P40066;
DR  UNIPROT: D3DM14;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically important for nuclear mRNA export. {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:8970155, ECO:0000269|PubMed:9463388}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-22648,EBI-12265; Score: 0.44
DE  Interaction: P34077; IntAct: EBI-22648,EBI-12056; Score: 0.27
DE  Interaction: P22696; IntAct: EBI-6679,EBI-22648; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-17964,EBI-22648; Score: 0.35
DE  Interaction: P53040; IntAct: EBI-18876,EBI-22648; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-18868,EBI-22648; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-22648; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-22648; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-22648,EBI-8627; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-22648,EBI-8591; Score: 0.35
DE  Interaction: P40368; IntAct: EBI-22648,EBI-12331; Score: 0.44
DE  Interaction: P40477; IntAct: EBI-22648,EBI-11747; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-22648,EBI-11703; Score: 0.61
DE  Interaction: P10592; IntAct: EBI-22648,EBI-8603; Score: 0.27
DE  Interaction: P47054; IntAct: EBI-22648,EBI-25846; Score: 0.27
DE  Interaction: P48837; IntAct: EBI-22648,EBI-12324; Score: 0.27
DE  Interaction: Q04599; IntAct: EBI-22648,EBI-38719; Score: 0.27
DE  Interaction: P36516; IntAct: EBI-22648,EBI-387; Score: 0.27
DE  Interaction: P22353; IntAct: EBI-22648,EBI-407; Score: 0.27
DE  Interaction: P36523; IntAct: EBI-22648,EBI-15518; Score: 0.27
DE  Interaction: P36525; IntAct: EBI-22648,EBI-15545; Score: 0.27
DE  Interaction: Q06678; IntAct: EBI-22648,EBI-392; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-20939,EBI-22648; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-22648; Score: 0.32
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0031081;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:2000728;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSFFNRSNTTSALGTSTAMANEKDLANDIVINSPAEDSISDIAFSPQQDFMFSASSWDGKVRIWDVQNGVPQGRAQHESS
SQ  SPVLCTRWSNDGTKVASGGCDNALKLYDIASGQTQQIGMHSAPIKVLRFVQCGPSNTECIVTGSWDKTIKYWDMRQPQPV
SQ  STVMMPERVYSMDNKQSLLVVATAERHIAIINLANPTTIFKATTSPLKWQTRCVACYNEADGYAIGSVEGRCSIRYIDDG
SQ  MQKKSGFSFKCHRQTNPNRAPGSNGQSLVYPVNSIAFHPLYGTFVTAGGDGTFNFWDKNQRHRLKGYPTLQASIPVCSFN
SQ  RNGSVFAYALSYDWHQGHMGNRPDYPNVIRLHATTDEEVKEKKKR
//
ID  Q9WU40;
PN  Inner nuclear membrane protein Man1;
GN  Lemd3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Multi-pass membrane protein.
DR  UNIPROT: Q9WU40;
DR  UNIPROT: Q0VGU6;
DR  UNIPROT: Q3USB5;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0003677;
GO  GO:0001525;
GO  GO:0002044;
GO  GO:0032926;
GO  GO:0030514;
GO  GO:0030512;
GO  GO:0006997;
GO  GO:0051726;
GO  GO:1903053;
GO  GO:1902531;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAATAAAAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQQQQQQQQQHRAGGRGNKTRNSNNNNT
SQ  ATAMGGRPGSGDLAYLRSPAGLGRLSASAAESPVAGGSGGAAAVPAAGSKVLLGFSSDESDVEASPREQAGGGGGGGARR
SQ  DRAALQYRGLRAPPAPPAAGEVTGGHPGERRKPHSWWGARRPAGPEPQPPAAGSDGAAEDADEELADGEDRDPEAEEPLW
SQ  ASRAVNGSRLLPYSSCREHYSDSEEEEEEGEEDGDVAPARQVLKDDSLARHRPRRSHSKPFSALTAKSGGSRQETSVQGG
SQ  GALAMNDRAAAAGSLDRSRNLEEAAAEPGGGGGGGCGCDPVDSIPRYRAGAKKLAPLLSPPSPDGDSTLESPTGPLLKTN
SQ  NHIGGGAFGVDSPGLYANSLPPGATAAAAPGTLRINHANHTGSNHTYLKTAYGKPKLCEPEEELLQQFKREEVSPTGSFS
SQ  AHYLSMFLLTAACLFFLILGLTYLGMRGTGVPEDGGLIKNPFDETFGKIQESEKNLLMSTLYKLHDRLAQIAGDHECGSS
SQ  SQRMLSVQEAAAYLKNLGPEYEDVFNTSLLWIFKNGKDVGIRCVGYGPEEDLTNITDVQFLQSTRPQMPFWCRFRRAFIT
SQ  VTHRLLLLCLGVVLVCVALRYMRYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQETKDLQPYMPLPHVRDSLIQPQDRK
SQ  KMKKVWDRAVDFLAANESRVRTETRRVGGADFLVWRWIQPSASCDKTLVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRN
SQ  MFDPVMEIGDHWHLAIQEAILEKCSDNDGIVHIAVDRNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDR
SQ  YHHRFPQALTCNTPLKPANKHMNSLSHLRLRTGLANSQGSS
//
ID  Q8MLV1;
PN  Lamin-B receptor;
GN  LBR;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15054108}; Multi-pass membrane protein {ECO:0000269|PubMed:15054108}; Nucleoplasmic side {ECO:0000269|PubMed:15054108}.
DR  UNIPROT: Q8MLV1;
DR  UNIPROT: Q0E8Z1;
DR  UNIPROT: Q709R7;
DR  UNIPROT: Q9W2D2;
DR  Pfam: PF01222;
DE  Function: Anchors the lamina and the heterochromatin to the inner nuclear membrane. {ECO:0000269|PubMed:15054108}.
DE  Reference Proteome: Yes;
DE  Interaction: P13607-1; IntAct: EBI-124823,EBI-213208; Score: 0.37
GO  GO:0030176;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0005521;
GO  GO:0016627;
GO  GO:0016628;
GO  GO:0006997;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPAT
SQ  RTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTT
SQ  NTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTE
SQ  EGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLL
SQ  LPTAVYYLTWSCTARNACQFKHLNLGILLDVNYLTRQVFQPRVVGAFAAYQVVVFLLVALLPGRRVHLTRETYKFNCLAV
SQ  SLTLLIASGVAEYLKYPVVTFVLRHYLRFCIFGLVGAFVAAAWSYWLVDTAKYNVLRQTLTNDYGRTGSFVVDFALGRQL
SQ  NPKWLGRVDWKQFQYRLSLVTTLIYATCYIYQTLVWPQKPQLGEQEGYLYQAKYYWNNVNYDPATLFSASCLLFYVLDAI
SQ  IFEHHLSSSFELQHEGYGCLLLLRYAATPYLLTAVTKYFYEQRVPISCWYAPLAVAALLSLGLLVKRFSCAYKYKYRLNS
SQ  QSPIFANIETIHTYQGSRLLLSGMWGWVRQPNYLGDIVALLALAAPMALRPAWPPVLGLSLIILLLLHRATRANARNQAR
SQ  YHSSWQRYSTQVRSYILPRVY
//
ID  Q9SAF6;
PN  Protein CROWDED NUCLEI 2;
GN  CRWN2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17873096}; Peripheral membrane protein {ECO:0000269|PubMed:17873096}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Nucleus lamina {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Mostly localized in the nucleoplasm and, to a lesser extent, at the nuclear periphery (PubMed:17873096). During prometaphase to anaphase, localized diffusely in the cytoplasm. A small population is later transferred from the cytoplasm to the chromatin surface. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9SAF6;
DR  UNIPROT: F4HP35;
DR  UNIPROT: Q0WQM6;
DR  UNIPROT: Q94AW6;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:17873096, PubMed:24308514, PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17873096};
SQ  MTPRSETHKIGGVTNPRNADRKGKAVAFSDDLVIPTLPPPPIGTLTGQGVSRGHTDDMDMGDWRRFREVGLLNEASMEKK
SQ  DQEALLEKISTLEKELYGYQHNMGLLLMENKELVSKHEQLNQAFQEAQEILKREQSSHLYALTTVEQREENLRKALGLEK
SQ  QCVQELEKALREIQEENSKIRLSSEAKLVEANALVASVNGRSSDVENKIYSAESKLAEATRKSSELKLRLKEVETRESVL
SQ  QQERLSFTKERESYEGTFQKQREYLNEWEKKLQGKEESITEQKRNLNQREEKVNEIEKKLKLKEKELEEWNRKVDLSMSK
SQ  SKETEEDITKRLEELTTKEKEAHTLQITLLAKENELRAFEEKLIAREGTEIQKLIDDQKEVLGSKMLEFELECEEIRKSL
SQ  DKELQRKIEELERQKVEIDHSEEKLEKRNQAMNKKFDRVNEKEMDLEAKLKTIKEREKIIQAEEKRLSLEKQQLLSDKES
SQ  LEDLQQEIEKIRAEMTKKEEMIEEECKSLEIKKEEREEYLRLQSELKSQIEKSRVHEEFLSKEVENLKQEKERFEKEWEI
SQ  LDEKQAVYNKERIRISEEKEKFERFQLLEGERLKKEESALRVQIMQELDDIRLQRESFEANMEHERSALQEKVKLEQSKV
SQ  IDDLEMMRRNLEIELQERKEQDEKDLLDRMAQFEDKRMAELSDINHQKQALNREMEEMMSKRSALQKESEEIAKHKDKLK
SQ  EQQVEMHNDISELSTLSINLKKRREVFGRERSRFLAFVQKLKDCGSCGQLVNDFVLSDLQLPSNDEVAILPPIGVLNDLP
SQ  GSSNASDSCNIKKSLDGDASGSGGSRRPSMSILQKCTSIIFSPSKRVEHGIDTGKPEQRLSSSVAVGMETKGEKPLPVDL
SQ  RLRPSSSSIPEEDEEYTDSRVQETSEGSQLSEFQSSRRGRGRPRKAKPALNPTSSVKHASLEESSKDELSGHVSVTSKKT
SQ  TGGGGRKRQHIDDTATGGKRRRQQTVAVLPQTPGQRHYNLRRKKTVDQVPADVEDNAAAGEDDADIAASAPSKDTVEETV
SQ  VETLRARRIETNADVVSAENNGDVPVANVEPTVNEDTNEDGDEEEDEAQDDDNEENQDDDDDDDGDDDGSPRPGEGSIRK
SQ  KLWTFLTT
//
ID  Q9D992;
PN  Membrane-anchored junction protein;
GN  Majin;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:26548954}; Single-pass membrane protein {ECO:0000305|PubMed:26548954}. Chromosome, telomere {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout meiotic prophase I and disapears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000269|PubMed:26548954}.
DR  UNIPROT: Q9D992;
DR  UNIPROT: E9Q4N4;
DR  Pfam: PF15077;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000269|PubMed:26548954}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005639;
GO  GO:0000784;
GO  GO:0003677;
GO  GO:0070197;
GO  GO:0045141;
GO  GO:0007129;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLKPFTYPFPETRFLHAGPNVYKFKIRYGNSIRGEEIEDKEVIVQELEDSIRAVLANMDSLQPFVTEHFIVFPYKSKWE
SQ  RVSHLKFKHGESILTPYPFVFTLYIEMKWFAEDLPSGKPADDIPLELVLAETEAEEATMRKWKRKLMEEPSSPSRQGPHR
SQ  AKMETSSEASSNKKPLKESKRSTDEEAQQEYQDTPASNAIAVKEQDAALGHGLQGLVVPPLQHSSPPPPKEPGARGFLGF
SQ  LSALFPFRYFFKKSGQ
//
ID  O55034;
PN  Sperm-associated antigen 4 protein;
GN  Spag4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm. {ECO:0000269|PubMed:10373309}.
DR  UNIPROT: O55034;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity (By similarity). May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail (PubMed:10373309). {ECO:0000250|UniProtKB:Q9JJF2, ECO:0000305|PubMed:10373309}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005874;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0043495;
GO  GO:0030154;
GO  GO:0090286;
GO  GO:0006998;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRP
SQ  KLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVY
SQ  REICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHS
SQ  ERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQ
SQ  GQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFP
SQ  KVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH
//
ID  P52593;
PN  Nucleoporin NUP188;
GN  NUP188;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P52593;
DR  UNIPROT: D6W0I1;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-11763,EBI-20589; Score: 0.35
DE  Interaction: P34077; IntAct: EBI-11763,EBI-12056; Score: 0.37
DE  Interaction: P40069; IntAct: EBI-11763,EBI-9166; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-11763; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-11763,EBI-8571; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-30084,EBI-11763; Score: 0.35
DE  Interaction: P46988; IntAct: EBI-13224,EBI-11763; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-11763; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-8632,EBI-11763; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-11763,EBI-8591; Score: 0.53
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-11763; Score: 0.35
DE  Interaction: Q02629; IntAct: EBI-11763,EBI-11698; Score: 0.37
DE  Interaction: Q02630; IntAct: EBI-11763,EBI-11703; Score: 0.37
DE  Interaction: Q08959; IntAct: EBI-11763,EBI-38526; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-11763,EBI-24471; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-11763,EBI-20254; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-11763,EBI-14372; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-11763,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-11763,EBI-18976; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-11763,EBI-6314; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-11763,EBI-7218; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-11763,EBI-8603; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-11763,EBI-16032; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-11763,EBI-15447; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-11763,EBI-15394; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-11763,EBI-11191; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-11763,EBI-11178; Score: 0.35
DE  Interaction: Q12134; IntAct: EBI-11763,EBI-37262; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-11763,EBI-9890; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-11763,EBI-2218; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-23061,EBI-11763; Score: 0.35
DE  Interaction: P53877; IntAct: EBI-29063,EBI-11763; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-11763; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-11763; Score: 0.32
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0031990;
GO  GO:0006999;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATPSFGNSSPQLTFTHVANFMNDAAADVSAVDAKQLAQIRQFLKANKTNLIESLNTIRQNVTSSGDHNKLRSTIANLLQ
SQ  INVDNDPFFAQSEDLSHAVEFFMSERSSRLHIVYSLLVNPDIDLETYSFIDNDRFNVVGKLISIISSVIQNYDIITASSL
SQ  AHDYNNDQDMFTIVSLVQLKKFSDLKFILQILQILNLMILNTKVPVDIVNQWFLQYQNQFVEFCRNINSTDKSIDTSSLQ
SQ  LYKFQNFQDLSYLSETLISRISSLFTITTILILGLNTSIAQFDIQSPLYMDTETFDTVNSALENDVATNIVNEDPIFHPM
SQ  IHYSWSFILYYRRALQSSESFDDSDITKFALFAESHDVLQKLNTLSEILSFDPVYTTVITVFLEFSLNFIPITASTSRVF
SQ  AKIISKAPEQFIENFLTNDTFEKKLSIIKAKLPLLNESLIPLINLALIDTEFANFELKDICSFAVTKSSLNDLDYDLIAD
SQ  TITNSSSSSDIIVPDLIELKSDLLVAPPLENENSNCLLSIPKSTKGKILTIKQQQQQQQQQNGQQPPTTSNLIIFLYKFN
SQ  GWSLVGRILQNLLHSYMEKGTQLDDLQHELMISIIKLVTNVVDPKTSIEKSSEILSYLSNSLDTSASTINGASIIQVIFE
SQ  IFEISLQRKDYTSIVQCCEFMTMLTPNYLHLVSSYLNKSDLLDKYGKTGLSNMILGSVELSTGDYTFTIQLLKLTKVFIR
SQ  ESLSLKNIHISKRSKIDIINKLILHAIHIFESYYNWKYNNFLQKFEIAFHLTLIFYDVLHDVFTINPHQKDQLIISSSAN
SQ  KLLQLFLTPMDSIDLAPNTLTNILISPLNTTTKILGDKILGNLYSKVMNNSFKLCTLLIAIRGSNRDLKPSNLEKLLFIN
SQ  SSKLVDVYTLPSYVHFKVQIIELLSYLVEAPWNDDYPFLLSFLGEAKSMAFLKEVLSDLSSPVQDWNLLRSLYIFFTTLL
SQ  ESKQDGLSILFLTGQFASNKKINDESSIDKKSSILTVLQKNSLLLDSTPEEVSCKLLETITYVLNTWTNSKIFIKDPKFV
SQ  NSLLAKLKDSKKLFQKKENLTRDETVSLIKKYKLISRIVEIFALCIYNSTDSNSEILNFLNQEDLFELVHHFFQIDGFNK
SQ  TFHDELNLKFKEKWPSLELQSFQKIPLSRINENENFGYDIPLLDIVLKADRSWNEPSKSQTNFKEEITDASLNLQYVNYE
SQ  ISTAKAWGALITTFVKRSTVPLNDGFVDLVEHFLKLNIDFGSDKQMFTQIYLERIELSFYILYSFKLSGKLLKEEKIIEL
SQ  MNKIFTIFKSGEIDFIKNIGKSLKNNFYRPLLRSVLVLLELVSSGDRFIELISDQLLEFFELVFSKGVYLILSEILCQIN
SQ  KCSTRGLSTDHTTQIVNLEDNTQDLLLLLSLFKKITNVNPSKNFNVILASSLNEVGTLKVILNLYSSAHLIRINDEPILG
SQ  QITLTFISELCSIEPIAAKLINSGLYSVLLESPLSVAIQQGDIKPEFSPRLHNIWSNGLLSIVLLLLSQFGIKVLPETCL
SQ  FVSYFGKQIKSTIYNWGDNKLAVSSSLIKETNQLVLLQKMLNLLNYQELFIQPKNSDDQQEAVELVIGLDSEHDKKRLSA
SQ  ALSKFLTHPKYLNSRIIPTTLEEQQQLEDESSRLEFVKGISRDIKALQDSLFKDV
//
ID  O13838;
PN  Nucleoporin nup40;
GN  nup40;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: O13838;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
GO  GO:0006407;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSS
SQ  SFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFT
SQ  MSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGML
SQ  INDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQP
SQ  RNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF
//
ID  Q9W1X4;
PN  Nuclear pore complex protein Nup214;
GN  Nup214;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:20547758}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:20547758}. Note=Localization to the nucleus membrane depends on mbo/Nup88. {ECO:0000269|PubMed:17032737}.
DR  UNIPROT: Q9W1X4;
DR  UNIPROT: Q8T3K4;
DE  Function: Serves as a docking site in the receptor-mediated import of substrates across the nuclear pore complex including emb, RanGAP and phosphorylated Mad (PubMed:17682050, PubMed:20547758, PubMed:17032737). Protects mbo/Nup88 from proteasomal degradation at the nuclear pore (PubMed:17032737). Together with mbo/Nup88, sequesters emb in the cytoplasm and thereby attenuates nuclear export signal (NES)-mediated nuclear export (PubMed:17032737). Together with mbo/Nup88, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the activation of an immune response (PubMed:17032737). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XTM1; IntAct: EBI-102000,EBI-96207; Score: 0.37
DE  Interaction: P19339-3; IntAct: EBI-199603,EBI-102000; Score: 0.37
DE  Interaction: P40798; IntAct: EBI-102000,EBI-88209; Score: 0.37
DE  Interaction: Q9VT59; IntAct: EBI-102000,EBI-163656; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0046826;
GO  GO:0046833;
GO  GO:0006606;
GO  GO:0090204;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAQNAPDCEDTQDFQFKLHHKIVAFKKCGEPRSNVNLLAVSSSRGLLFAGSPTQPELKVIIVKDLVNAKSTAQQPQARLV
SQ  PLPSIPNYIACSSDGNLLAVNHTQNGTSLLSIYAVLSFMTPDVRPVYNIRLAAEDHVHGVQLLWNPVLPNSLAVVLSNGA
SQ  LAMYALKEGGNFEMHSLDKNQQVKCGCWSPKGKQIVLGFPGGTVKQFKPDLTLAKTLLCPPNIHDAPFDTIAIQWLSTFQ
SQ  FAVIFLQHGEDCSPSLYILNAPKAGAPSYINYYDICYSMNGPRNHQFVFSHVPQWNLLLVVSANGVEVGIMRSTEAGDTP
SQ  AWQQLTLLDEARIEMPLSEDKDETFPLGFAFDTSTTHQLTINEKKLQTMPMVHVLSSDGELLSFNFLNVLPTAVSVCSPP
SQ  PPVADTSGQFKPLNMLLASEEEEQPAWAASPSKAPAATPAASSDISFAFTPNTVTSTPAPSKDKQPSLFSGFGAAAAKAP
SQ  APQLSFGTAPTSSPVSFGAPTTNAAKPTTPFGGFGTQATTTAMGSMFSASGANAFGGMALNKPAIASVTPRTAAPGSTVP
SQ  ATPASAPANKPLYTVPLTFTPVDTKPATSAPPQIADESLKPDDTEPIIKDMIALQIEAFSKDIQKQKEQTKELLKGIAAP
SQ  SALRAYAKRLDDLQELNEQAKDVEFELDVQGLRQGLNEAYAIVAECRGKLEIYRKPEITRLMNSSSCDPSGRRMLARLQS
SQ  YVAANEAQLRLAQQHVDLQWEQFQDVVRRNSKSRMHMPCLEGIYQRLTRLQNLTSNQRIVQNNIKSKLKERGLLQAALLD
SQ  QEKSRTRTNEAVDTLTDSILTMSLSQVVDSNAAKLTRERLQKIRNIVQLQKINVICPQRPDRVGLKSEVILETKRRAEQI
SQ  KRAAAKPATANKYTQAAVAPPSPPDVAPTPAVAPMPQATVTVAPPLPKPMPSIPSVVEKPGVPTHPTTPVATPFSFSQSI
SQ  PFVKTSTVTPTTNTVTPGEAAKPGLSIFGGSTISSFSFGGGAAKSALSFGTGSPAVAAPTPKPNPLSAVEKPTPEPTKPK
SQ  EQKAAESKEFKAVQPETEESKVPQKPKAETENKSFGFGGFTGTGGTVGNTSSSPFSFGGLGSSLGFGGTAAAVPKSEPSS
SQ  TATTSVATSASTAPFGIFSAALAKPSNSEPITTVTSNTTTITSKPTNVIASSSVTDAPSVTTTNAVTSSTDPIGGLFSSV
SQ  TICKPNTPADTTKPANIFGGGLSAGSFSFGGTIDASKGLFGSTKPVATAPTSVTEANNKTDPISTTPSAISTTTATTTVS
SQ  SPAVVPAAVTAAVPATSSTTVTSSTAVPGSAFSFSNAFSTLSAGGAAAPTTSASAPLAAKSPTATSTGNNSSNSVFGGGF
SQ  AVATSTAAPVASPFQSAAKSPVSSANIFGSIPKAETSVFGGATTAPSNTTAAATPDAPPAGLFASAAISNPSPFGSPTTR
SQ  APASGGNIFGQAVKPSVFGQPAQAGDSGGSIFGGGSASTPFGSSSIFGGGNTQGAVGAPAAGSTSIFGQKVFGQSSAAAP
SQ  AAGGNIFSNPVGSPQASPFGGGGNSIFGSPATAPPASGGSIFGGGSSSGGFGSFTQTTPAQGGFGGGFGQGGGGSVAQTG
SQ  FGSPQAPQQQTTTPGGFGAKPVFGGSPAFGASPTFGGGATFGSPKGFGGFGGASPVASPPPFGAAAKPAQGNIFETLGGQ
SQ  ESGLSFGNLAQTGNSNAQKPAFGGSSFMNYR
//
ID  Q709R6;
PN  LEM domain-containing protein Bocksbeutel;
GN  bocks;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:24700158}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Note=Detected in the nucleus envelope and cytoplasm. In the cytoplasm, it appears to localize to discrete foci. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}. [Isoform A]: Nucleus, nucleoplasm {ECO:0000269|PubMed:15035436}. Cytoplasm {ECO:0000269|PubMed:15035436}. Note=Predominantly expressed in the nucleoplasm with very low expression levels in the cytoplasm. {ECO:0000269|PubMed:15035436}. [Isoform B]: Nucleus inner membrane {ECO:0000269|PubMed:15035436}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:15035436}. Note=Appears to be predominantly expressed in the nucleus envelope but expression is not uniform. Outside of the nucleus it is located to discrete foci which may be the endoplasmic reticulum. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}.
DR  UNIPROT: Q709R6;
DR  UNIPROT: Q8SZZ5;
DR  UNIPROT: Q9VHA7;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:15035436, PubMed:24700158). May have a role in maintaining the structural integrity of the nuclear lamina (PubMed:24700158). During pupal development, plays essential and redundant functions with the other LEM domain proteins; MAN1 and Ote (PubMed:24700158). Also has a redundant but important role with Ote in larval development (PubMed:24700158). {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:24700158}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7JR34; IntAct: EBI-182405,EBI-93986; Score: 0.37
DE  Interaction: Q06559; IntAct: EBI-114639,EBI-93986; Score: 0.37
DE  Interaction: Q9VVQ1; IntAct: EBI-93986,EBI-173837; Score: 0.37
DE  Interaction: Q9VLU0; IntAct: EBI-105147,EBI-93986; Score: 0.37
DE  Interaction: O01666; IntAct: EBI-159423,EBI-93986; Score: 0.37
DE  Interaction: Q9VC86; IntAct: EBI-174235,EBI-93986; Score: 0.37
DE  Interaction: O76454; IntAct: EBI-87224,EBI-93986; Score: 0.37
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0007049;
GO  GO:0051301;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDLSYLDTLGNKELLAKCLEHGLPGVPVTDSTRSVIIRRLKAKITGVPLNKSKSASKKAIPRRETVHGSQVTTPTSEPV
SQ  RRTPGKSAGRTSSNNNKISEQSRRTIAYGLDNTSISGRSVQTTTTVSDMSSQSEDDDSYMVDSPVPNYSKDQQPRRYVSL
SQ  AKSGVLTTSYTREVDQPLYEQEDIPRSYTYERPHVPAATLHALPTYEPRIEPSTYRPTDLGFSRPLLTQTNLNSTSYEES
SQ  STYNPKLSPISPRNTFSGSARPFGGPAPAPAPIRQRQSVPVSGSNLARGRLLQPTTAVNTLYPQLNEFYDQPNDAGEPME
SQ  TESESEVEEVPINSHFQKNRFSPLARKPLVRHHDQVSPMAQFRALAVSLDQKYNLKFYLILVVSVMLATMVYVVLTPNA
//
ID  O01971;
PN  Emerin homolog 1;
GN  emr;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Single-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}. Note=Lmn-1 and mel-28 are required for its localization to the nuclear envelope (PubMed:11870211, PubMed:16950114). Remains in the nuclear envelope until mid-late anaphase (PubMed:10982402). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:16950114}.
DR  UNIPROT: O01971;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Involved in chromosome segregation and cell division, probably via its interaction with lmn-1, the main component of nuclear lamina (PubMed:11870211, PubMed:12684533). Has some overlapping function with lem-2 (PubMed:12684533). May play a role in radiation- induced DNA damage repair response (PubMed:22383942). {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12684533}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XTB5; IntAct: EBI-2535391,EBI-6260308; Score: 0.27
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005521;
GO  GO:0007059;
GO  GO:0000281;
GO  GO:0010165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVS
SQ  AATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAET
SQ  NPEDTI
//
ID  P23913;
PN  Delta(14)-sterol reductase LBR;
GN  LBR;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:2170422}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
DR  UNIPROT: P23913;
DR  PDB: 2L8D;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0070402;
GO  GO:0016627;
GO  GO:0006695;
GO  GO:0030223;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPNRKYADGEVVMGRWPGSVLYYEVQVTSYDDASHLYTVKYKDGTELALKESDIRLQSSFKQRKSQSSSSSPSRRSRSRS
SQ  RSRSPGRPAKGRRRSSSHSREHKEDKKKIIQETSLAPPKPSENNTRRYNGEPDSTERNDTSSKLLEQQKLKPDVEMERVL
SQ  DQYSLRSRREEKKKEEIYAEKKIFEAIKTPEKPSSKTKELEFGGRFGTFMLMFFLPATVLYLVLMCKQDDPSLMNFPPLP
SQ  ALESLWETKVFGVFLLWFFFQALFYLLPIGKVVEGLPLSNPRKLQYRINGFYAFLLTAAAIGTLLYFQFELHYLYDHFVQ
SQ  FAVSAAAFSMALSIYLYIRSLKAPEEDLAPGGNSGYLVYDFFTGHELNPRIGSFDLKYFCELRPGLIGWVVINLAMLLAE
SQ  MKIHNQSMPSLSMILVNSFQLLYVVDALWNEEAVLTTMDITHDGFGFMLAFGDLVWVPFVYSLQAFYLVGHPIAISWPVA
SQ  AAITILNCIGYYIFRSANSQKNNFRRNPADPKLSYLKVIPTATGKGLLVTGWWGFVRHPNYLGDIIMALAWSLPCGFNHI
SQ  LPYFYVIYFICLLVHREARDEHHCKKKYGLAWERYCQRVPYTHISLHLLEHSTYLICKLKYTSHLCTWSVCYLGFKH
//
ID  Q9CA42;
PN  Protein CROWDED NUCLEI 3;
GN  CRWN3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:F4HRT5}; Peripheral membrane protein {ECO:0000250|UniProtKB:F4HRT5}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Nucleus lamina {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Punctate or bundle-like structures are detected, especially in trichomes where bundle-shape localization pattern along the long axis of the nucleus is observed. During prometaphase to anaphase, localized diffusely in the cytoplasm. Later transferred from the cytoplasm to the chromatin surface, preferentially assembling to the distal surface of the chromatin. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9CA42;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:24308514, PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9SB04; IntAct: EBI-1997616,EBI-1100883; Score: 0.37
DE  Interaction: Q9ZWS7; IntAct: EBI-1100917,EBI-1997616; Score: 0.37
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0009506;
GO  GO:0006997;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:F4HRT5};
SQ  MFTPQRNRWPETDRKGKAIAFSDEIITPPPQRVLLREDDDWQKFKEVGLLDEASLERKDRDALIEKILKLEKELFDYQHN
SQ  MGLLLIEKKQWTSTNNELQQAYDEAMEMLKREKTSNAITLNEADKREENLRKALIDEKQFVAELENDLKYWQREHSVVKS
SQ  TSEAKLEEANALVIGMKEKALEVDRERAIAEEKFSVMNRKSSELERKLKEVETREKVHQREHLSLVTEREAHEAVFYKQR
SQ  EDLQEWEKKLTLEEDRLSEVKRSINHREERVMENERTIEKKEKILENLQQKISVAKSELTEKEESIKIKLNDISLKEKDF
SQ  EAMKAKVDIKEKELHEFEENLIEREQMEIGKLLDDQKAVLDSRRREFEMELEQMRRSLDEELEGKKAEIEQLQVEISHKE
SQ  EKLAKREAALEKKEEGVKKKEKDLDARLKTVKEKEKALKAEEKKLHMENERLLEDKECLRKLKDEIEEIGTETTKQESRI
SQ  REEHESLRITKEERVEFLRLQSELKQQIDKVKQEEELLLKEREELKQDKERFEKEWEALDKKRANITREQNEVAEENEKL
SQ  RNLQISEKHRLKREEMTSRDNLKRELDGVKMQKESFEADMEDLEMQKRNLDMEFQRQEEAGERDFNERARTYEKRSQEEL
SQ  DNINYTKKLAQREMEEMQYEKLALEREREQISVRKKLLKEQEAEMHKDITELDVLRSSLKEKRKEFICERERFLVFLEKL
SQ  KSCSSCGEITENFVLSDLRLPDVEDGDKRFGKQKLKAEEALNISPSAENSKRTSLLGKIASKLLSISPIGKTDKVTDLGI
SQ  TVKLPESSQPDDSLDRVSGEDHEPSATEQSFTDSRIQEGPEGSLQSEMKSDKPRRGRGRGRGRGKSVRGRSQATKAVSRD
SQ  SKPSDGETPRKRQREQTSRITESEQAAGDSDEGVDSITTGGRRKKRQIAVPVSQTPGQTRYQLRRHRNVGTEEDKAQASK
SQ  GATEKQERVNDDIRKVPSPKETRTPPEGENRENGKAEVLVETVTHEEIVTVETETVFKVNNTGKNPVEDPQLEVGGSGEI
SQ  REHGEEDDENISMIEEENEGEEEEETERQGNDASIGKKIWVFFTT
//
ID  Q12445;
PN  Nucleoporin POM34;
GN  POM34;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: Q12445;
DR  UNIPROT: D6VY20;
DR  UNIPROT: E9P8U3;
DR  UNIPROT: Q7LGY6;
DR  Pfam: PF08058;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
DE  Reference Proteome: Yes;
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-34287; Score: 0.32
DE  Interaction: P11484; IntAct: EBI-34287,EBI-8627; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-34287; Score: 0.40
GO  GO:0031309;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKIQAGQLGLDDNDVPGPLPDTDSKPSSQSQNDTPMFKLGNFESPVLKELSRRTVNKEMETQRIMTNVIAFAFWNLLVKF
SQ  IKFFWNNTHVGRQFCNRLSRIHLYMLTFHTLKKANIIYHTTFSWLNAELLDYLFHLLISLNILFSLWKLLSTVKVSDLNL
SQ  TDRQKKLLGVDMQSSVDTGLQPQHPHYVSTSKISQMAQNKTHIPQTNLKNHPAYLFKGLETPLKARQREMAEEQTKLQSQ
SQ  SLHTKNVFGTLQRHSGISSTLVSANNDNNSPHTPVTRKGYIPSSKYAYMMNSQSPRGKI
//
ID  Q54HI5;
PN  Lamin-like protein;
GN  lmnB;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19466752}. Nucleus inner membrane {ECO:0000269|PubMed:22090348}.
DR  UNIPROT: Q54HI5;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane. Helps to maintain integrity of nuclear structures in response to mechanical stress. {ECO:0000269|PubMed:22090348}.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0030527;
GO  GO:0007098;
GO  GO:0051642;
GO  GO:0010847;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMSKKKSKRASPIESSQEEIAISTSKTATTEKPKKTKTTTKKKASQPSQEVVMETESEVEITTTTTSTSTTNNNNITTT
SQ  STSSQQSNGTLSSSSSPTIQSIPTTPISKYIPSLSQIGTPLSPNRAAQRLREKDELSLIHNRLKSALKKLESAETELEKK
SQ  NQEYEELDQKHTATIKQLKQRSDQVEKQLIEEQNQNSDLTSNRNILENELKSKESVWKKEKDEILLKFQESINKLNQENS
SQ  LAQSQLKSEIVSKEYEIDGLKSEINRLKDDLQYRIREGEEKSRKLLENEYNRFKGKEEEYNQLIVSKDEEIKKYKFELKE
SQ  KEKSSNAMNKKENELNNLIQAHERQIEDMRDSINREWELKAAQMMEEHHARTIHLQQAVDSFNEEKERIKSQMETLNGQI
SQ  EDINIKNNEYEDRIKEMNVLLSQKDNSIGELGVEIEESKKKMRKQMADLKSKDGQIALLQIEINTKDNKCNTLQTETNRL
SQ  KSELYSITNQIDPEIPLDPEINSLKELVKGFEKTVDDRKRKRSKLQHEFNAAANQDQNGMTIEEQSSTSTTTTTSATGSS
SQ  SSTSHLDNIDSSKLPTGPEQSELFNPDTVSFSLVDSNQEFIKLSVHGDMDNGLSISKWRLIVVKPDGSKSGFSFPDGIQP
SQ  FKGIKSVTVWTGRPRPQGTPTENEFYWARTELWTSPVEGTIVKLVSPSEETTTVTLPADGIYQKPSSAGKSNCLIM
//
ID  Q10331;
PN  Nucleoporin nup107;
GN  nup107;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:15226438}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11309419, ECO:0000269|PubMed:15226438}.
DR  UNIPROT: Q10331;
DR  UNIPROT: O94351;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:12618370}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P797; IntAct: EBI-295788,EBI-295769; Score: 0.57
DE  Interaction: Q9UTH0; IntAct: EBI-295788,EBI-295780; Score: 0.57
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006407;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACCCYSTILTHTRLDFKTMHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEK
SQ  FNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAV
SQ  LEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRL
SQ  DERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTK
SQ  NKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSN
SQ  SSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSD
SQ  SIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSV
SQ  SPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDG
SQ  EPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHP
SQ  STLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAG
SQ  ECSLSTPNGLFSL
//
ID  Q9NZP6;
PN  Nuclear pore-associated protein 1;
GN  NPAP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:22694955}. Nucleus inner membrane {ECO:0000269|PubMed:22694955}. Note=Colocalizes with the NPC and nuclear lamins at the nuclear periphery.
DR  UNIPROT: Q9NZP6;
DR  OMIM: 610922;
DR  DisGeNET: 23742;
DE  Function: May be involved in spermatogenesis.
DE  Reference Proteome: Yes;
GO  GO:0005637;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0030154;
GO  GO:0007275;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNLLSKFRPGCRRRPLPGPGRGAPAPLSRDASPPGRAHSVPTPRPFRGLFRRNARRRPSAASIFVAPKRPCPLPRAAAA
SQ  PLGVLPAVGWGLAIRKTPMLPARNPPRFGHPSSVRIPPPSRMFTLLLPSPREPAVKARKPIPATLLEETEVWAQEGPRRV
SQ  KKDEDPVQIEGEDDEKRTPLSSGEASSTSRSQGTQGDVASFRCSPGPLEGNVYHKFSENSMSEKAQASPASSCLEGPAMP
SQ  STHSQAGCARHLGKPDPDATAPPEPAVGCSLLQQKLAAEVLNEEPPPSSLGLPIPLMSGKRMPDEKPFCIPPRSAAPPRA
SQ  ARNRPCKRKMSIPLLLPLPPSLPLLWDRGELPPPAKLPCLSVEGDLHTLEKSPEYKRNSRILEDKTETMTNSSITQPAPS
SQ  FSQPVQTTDSLPLTTYTSQVSAPLPIPDLADLATGPLILPIPPLSTTPKMDEKIAFTIPNSPLALPADLVPILGDQSNEK
SQ  GGSYNSVVGAAPLTSDPPTPPSSTPSFKPPVTRESPISMCVDSPPPLSFLTLLPVPSTGTSVITSKPMNSTSVISTVTTN
SQ  ASAHLTSQTAVDPEVVNMDTTAPSQVVIFTSSLSSRVSSLPNSQIHCSAEQRHPGKTSVYTSPLPFIFHNTTPSFNQLFG
SQ  KEATPQPKFEAPDGQPQKASLPSACVFLSLPIIPPPDTSTLVNSASTASSSKPPIETNAMHTTPPSKAVILQSASVSKKY
SQ  LPFYLGLPGSGNTQPSGNTASVQGSTSLPAQSVRAPATASNHPLNPGATPQPKFGAPDGPQQKTSLPSAHDFLSLPIMVP
SQ  PDTSTLVSSASAASLSKPAIDTSDMNTTPPSKTVILQSTFVSRKEEYIRFYMGLPGSGNTLHSDSIASAQVSTSFPAQAD
SQ  RRPTTTSSHPLNTGSISHSTLGATDGQQKSDSSFILGNPATPAPVIGLTSPSVQPLSGSIIPPGFAELTSPYTALGTPVN
SQ  AEPVEGHNASAFPNGTAKTSGFRIATGMPGTGDSTLLVGNTIPGPQVIMGPGTPMDGGSIGFSMSAPGPSSTSGELNIGQ
SQ  GQSGTPSTTSVFPFGQAAWDPTGHSMAAAPQGASNIPVFGYTSAAAYIPGLDPPTQNSCSGMGGDGTRSIVGGPCVPAFQ
SQ  QCILQHTWTERKFYTSSTHYYGQETYVRRHVCFQLP
//
ID  Q9C811;
PN  Nuclear pore complex protein NUP160;
GN  NUP160;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17030626, ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:22902705}; Peripheral membrane protein {ECO:0000269|PubMed:17030626}; Nucleoplasmic side {ECO:0000269|PubMed:17030626}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:17030626}.
DR  UNIPROT: Q9C811;
DR  UNIPROT: F4HR72;
DR  UNIPROT: F4HR73;
DR  Pfam: PF17238;
DE  Function: Contributes to the transfer of mature mRNA from the nucleus to the cytosol. Required for both R gene-mediated and basal disease resistance. RNA export seems to play a critical role in stress responses and regulation of plant growth and development. Required for proper expression of factors associated with auxin signaling. {ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:17030626, ECO:0000269|PubMed:20872268, ECO:0000269|PubMed:22238449, ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006952;
GO  GO:0016973;
GO  GO:0009733;
GO  GO:0009409;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17030626};
SQ  MEENRRNPSAGMEVPVAGGGNVVKWIEISVPSPSVSSSSIGANSSEDNECVQLPLSEDYASSSVIGEPSISFVWRINKTS
SQ  PNALELLQLSAKSGFPITGLRFVFAQTLSPFAFVYADEGGDSGRLVYFLYSLTPSGVVYVLKLSNTLAYKSGSVFPLDHL
SQ  IHLDVRPYLNESRVTSVAASPGFIFLGRSDGCVSCFQPIVYFQKSSGFHQELRDDTGFGRLGTVVAAVQDLFISEVHGRN
SQ  YLCVLHADGALRVWDILTYSRVLCQSIAAKNLEGVMCVRLWLGKADYDSGIIPLAVLYRKSMNDSMDVITVYGLHFSSAE
SQ  GIALSLDSGLQNIPLEEGELRDVRFTSDKIWTLKANELTSYMLCQKSSTMEAQSYTLQEDYISEQLFLSSRSSSHDLLLT
SQ  THSLFSSAKDQIMGFISSIFLRRLLCPGIFHNVALRLTLLDHNKNWTDSEFQSLSLDELTSEILLLVEHEVTAETSISVF
SQ  HWWKNFCTSYLHHWCSNNEPRTLLVQSDVIGLVRNNSVSLFFRLENAEHSLGGSSSEHSNLTSLDLGVSHSDHEILAEVL
SQ  RCTSKISKQWGGAPYAMYYESITGRPIISSDEIVPRLVNILESGYSTTIGQRTWSDLGADRAWEKELEAHKNLRTFSIDM
SQ  LLSLSALCQRAGSWEKVFTIMEHYLQYLVPKKSMQKNDGEALSDICSSILVQATSQFVKVMFESAFDIFLLISYLLNIAG
SQ  QVNMSQQDICKLRLELLPMIQDIVSEWLIILFFVTTPAESTSMEDFSLKLSSLQIDSSIDKRSWNAMLGKCGFSLAFILL
SQ  FSDRSCIVDGRFNLRYLPSSQIITSLVQNFISWIRYSKTGDDSSSLLRRSTELSLRLIRNGQSDAVERILVVVEASLRGE
SQ  KTFGCSQDTSGDWCLLQHLRGCCLLDQVQRGASGILRERKIIDAIRCFFRASSGEGSWKALHSLSKEAGFSPATTGPSIL
SQ  DGSTSSAAWKLHYYEWAMQIFERYNISEGACQFAYAALEQVDDAYNFIEMTEEFDPTKAATYTRGRLWANVFKFTLDLNL
SQ  LNDAYCAIISNPDEEIKRICLRRFIIVLFECGKTKILSDGHLPFIGLTEKITQELFWKAGRSDIMMKPNPYKLLYAYEMR
SQ  RHNWRMAASYMYQFSARLRSEGACKDYKHMSLVLQERLNGLSAAMNALALVHPGYAWIDPVPEETTRYPVKKARRAEEEQ
SQ  LRSNDQPKGEKSCIDIEKLQNEFVFTTAEYMLSLKNFGWTYSGLEKPPSDLVDLLVQANLYDMAFTVVLKFWRGSALKRE
SQ  LEKIFENMAIKCCPAKGTLWSSPNLMLTSNDEEVTHSPDRSPADQGSKLAGDWEILEVYLKRYIDIHARLPVSVASTLLQ
SQ  ADSCIELPLWLIQMFKDGQKEKALGMAGQEASPASLFQLYVDYGRLTEATNLLLEYMESFASSKPAEVLKRKKVSGVWFP
SQ  YTTVERLWWELEKTMNSGRMVEQCHKLKEQLHHALLNHLKLLKVDSNDAVSSATG
//
ID  O13961;
PN  Nuclear envelope protein ndc1;
GN  cut11;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: O13961;
DR  UNIPROT: Q9UTH4;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC) and the spindle pole body (SPB), which plays a key role in de novo assembly and insertion of both structures in the nuclear envelope. Involved in the formation of the bipolar mitotic spindle. Anchors the spindle pole body in the nuclear envelope. {ECO:0000269|PubMed:9763447}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005816;
GO  GO:0106166;
GO  GO:0017056;
GO  GO:0071790;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVM
SQ  LKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYF
SQ  SHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRI
SQ  AYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIAT
SQ  EELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHE
SQ  EINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQN
SQ  EALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAAN
SQ  ALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS
//
ID  P53983;
PN  Protein ASI3;
GN  ASI3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P53983;
DR  UNIPROT: D6W1G9;
DE  Function: Negative regulator of SPS-sensor signaling. Together with ASI1 and ASI2, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor- regulated genes in the absence of inducing signals. {ECO:0000269|PubMed:17085444}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-10420,EBI-28603; Score: 0.35
DE  Interaction: P53895; IntAct: EBI-28603,EBI-28975; Score: 0.46
DE  Interaction: P11484; IntAct: EBI-28603,EBI-8627; Score: 0.35
DE  Interaction: P39077; IntAct: EBI-28603,EBI-19063; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-28603,EBI-8591; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-28603,EBI-17244; Score: 0.35
DE  Interaction: P54074; IntAct: EBI-28603,EBI-27241; Score: 0.56
DE  Interaction: P10614; IntAct: EBI-5127,EBI-28603; Score: 0.40
DE  Interaction: P49626; IntAct: EBI-28603,EBI-15394; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-28603,EBI-19749; Score: 0.37
GO  GO:0097658;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0046872;
GO  GO:0004842;
GO  GO:0071230;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTNILQHVKQLLHNRDVFSFFHNKTGNLNYLDNTTQKPEVFVSPNSTIVSAPTLDSFQALMEKGNFTTLQLAKVGIRMF
SQ  FSYSVSKYAVLCFSTAIILNRLTVMSSLRSNSTNIRLPLWSKTLLHLVATLSLVKALLQILSQFGLMHELHVSDTDFYAL
SQ  SVYLFVALSDCIEIFISSTTNVPSLICSDFSIWGLSLNLYIISKMPAGQQHIGDNVELLGAVFHRLVIHLVELFHIRAYR
SQ  LCGEVILNAGFFTAFVTRTYLNGLDFINICLIHNYFPGFFYISTILLASIGIFLKALFTSNPFRSLYSRYKNLEKWWRSN
SQ  NYNGEEEFNEIALSLCLLLTSNDYKIFKKSDNVKSVDEVAAFSNSYVVSGHLNQLQSTPEDLLSRKEMTTDSQLPGFART
SQ  YLGLFELVRTIILTYSRLLKNLLWSKNFESSIDKKPRVGKRKKRDLNKYVTEKNYKKFLYKPDVKELNIESDLRSLELLL
SQ  PEDDSSKDYFPPRKIDESVSDEEFDSDMESQLIIDEEKELTHLSSNAVDSDDLEEIAWNISMWSILNYEMDVHNKVNGPL
SQ  TRSQYGKRNPQGVLVDVVIERLLHHTNSRYMYKRLNMKDDDKLEFKFDFAFDSCDEVEEMDLSCLICKVNKRNIVTWPCR
SQ  CLALCDDCRISLGYKGFATCVSCDSEVKGYSKLNIV
//
ID  Q949W6;
PN  Protein KAKU4;
GN  KAKU4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:24824484}.
DR  UNIPROT: Q949W6;
DR  UNIPROT: F4JS05;
DR  UNIPROT: O49592;
DE  Function: Required for nucleus structure organization (e.g. size and shape). {ECO:0000269|PubMed:24824484}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8LBH4; IntAct: EBI-4459053,EBI-4425603; Score: 0.37
DE  Interaction: Q9LPU9; IntAct: EBI-4425603,EBI-4473600; Score: 0.37
DE  Interaction: Q9LZM7; IntAct: EBI-4425603,EBI-4435277; Score: 0.37
DE  Interaction: Q9FFS8; IntAct: EBI-4449747,EBI-4425603; Score: 0.37
DE  Interaction: O49653; IntAct: EBI-4458381,EBI-4425603; Score: 0.37
DE  Interaction: Q9SZB2; IntAct: EBI-4425606,EBI-4425603; Score: 0.37
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005802;
GO  GO:0071763;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSVSGYAAGAGQPRVGGKIVRPRRTAVVRTPCERPVQRSRDPPQQNPSWISRLVYKPASVIASGAGKFISSVVFSDSSS
SQ  SSEEDEDSSSDIDGDEDVEKNNPDFTEEDLLSAQQPSIQRLSSKRVIEQLLLQETFAREEGDRLIDIIKARVVDHPSVPS
SQ  AIETSHDDYGLTSDVNVGEMSNTAVMEARKWLEEKKSGSSSKYKATEDGAGSPVDVAKSYMRARLPWGSPAANNLDFRSP
SQ  SSARVQGTPLPYSAGNFSSSKLKRKSGSNQSWNIQDEIRKVRAKATEEMLKSPSSVASLEPKYSPYVLATDMLKGNASSL
SQ  NADGAVRNEQSRALPNSAIPTSEHNQTTEANQAVKETGVLHTRSRGVGLEETFISTQGVKPSEDTNTAPQSGTAVDDFND
SQ  QDGDFIQPTSTIGNTTNAVLALGATLDPTGNSCIPKDVFETSKEADEIGASRHTSNGFPSSSPSGYGRSTKTHTTRRNQG
SQ  FSAYS
//
ID  O94652;
PN  Nucleoporin gle1;
GN  gle1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94652;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q09847; IntAct: EBI-21243842,EBI-21243819; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16823372};
SQ  MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWA
SQ  KKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKH
SQ  KENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQ
SQ  ITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFAR
SQ  LQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQ
SQ  LMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP
//
ID  Q10168;
PN  Nucleoporin nsp1;
GN  nsp1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15116432}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000250|UniProtKB:P14907}.
DR  UNIPROT: Q10168;
DR  Pfam: PF05064;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Appears to have a role in the formation of the septum. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0000917;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0010389;
GO  GO:0000054;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16823372};
SQ  MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNST
SQ  NASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTN
SQ  TTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSN
SQ  TTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFT
SQ  KPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPS
SQ  AKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRI
SQ  DDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISE
SQ  IVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF
//
ID  Q7K0D8;
PN  Nuclear pore complex protein Nup50;
GN  Nup50;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:20144760}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O08587}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Associates with chromatin (PubMed:20144760).
DR  UNIPROT: Q7K0D8;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta- cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation (PubMed:20144760). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000250|UniProtKB:Q9UKX7, ECO:0000269|PubMed:20144760}.
DE  Reference Proteome: Yes;
DE  Interaction: Q4V5M2; IntAct: EBI-193476,EBI-194571; Score: 0.49
DE  Interaction: Q9VWE4; IntAct: EBI-194571,EBI-122539; Score: 0.37
DE  Interaction: Q9VD47; IntAct: EBI-194571,EBI-144988; Score: 0.37
DE  Interaction: Q9VSK1; IntAct: EBI-194571,EBI-148683; Score: 0.37
DE  Interaction: P40798; IntAct: EBI-194571,EBI-88209; Score: 0.37
DE  Interaction: P52295; IntAct: EBI-145898,EBI-194571; Score: 0.37
DE  Interaction: Q9W0Y8; IntAct: EBI-194571,EBI-105939; Score: 0.37
DE  Interaction: Q9VJ53; IntAct: EBI-194571,EBI-122209; Score: 0.37
GO  GO:0000785;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005704;
GO  GO:0031490;
GO  GO:0035080;
GO  GO:0051028;
GO  GO:0045944;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKP
SQ  AASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPT
SQ  TSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEE
SQ  SARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTA
SQ  SFTAPVPSSSSIFSLTAKPTGEAKSDDTPKSSIFSFGAKDTTTKKDEPNFSAPKTNGFSFGLKSNNDDKPSTSLFAGFGK
SQ  APGGAGDGAKGFSFTNSATPFSLGNIHPPAAAAAPAEEEKEEDTPPKVEFKQVVEDDAIYSKRCKVFIKKDKDFGDRGVG
SQ  TLYLKPVKDSEKIQLLVRADTNLGNILVNLILSKGIPCQRMGKNNVLMVCVPTPEDSKATSLLLRVKTGDEADDLLEKIK
SQ  EHIK
//
ID  Q19972;
PN  Chromo domain-containing protein cec-4;
GN  cec;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792}; Peripheral membrane protein {ECO:0000305|PubMed:26607792}.
DR  UNIPROT: Q19972;
DR  Pfam: PF00385;
DR  PROSITE: PS50013;
DE  Function: Chromatin anchor protein which binds to methylated lysine residues on histone H3, thereby recruiting heterochromatin to the nuclear periphery. May be required for the correct positioning of chromatin and nucleoli in embryos. {ECO:0000269|PubMed:26607792}.
DE  Reference Proteome: Yes;
GO  GO:0000793;
GO  GO:0005637;
GO  GO:0003682;
GO  GO:0035064;
GO  GO:0097240;
GO  GO:0045595;
GO  GO:0010468;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:26607792};
SQ  MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQS
SQ  DDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTP
SQ  KSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDE
SQ  DDDDEQREEVVTTAPVETKSRWGFGSWKWF
//
ID  Q04839;
PN  mRNA transport factor GFD1;
GN  GFD1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10523319}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Cytoplasmic side {ECO:0000269|PubMed:10523319}.
DR  UNIPROT: Q04839;
DR  UNIPROT: D6W081;
DR  PDB: 3LCN;
DR  Pfam: PF17331;
DE  Function: High-copy suppressor of mutant alleles of ATP-dependent RNA helicase DBP5, which is involved in mRNA export from the nucleus. It may also play an important role in a late stage of NAB2-mRNA export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:15208322}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-20589,EBI-27549; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-27549,EBI-8627; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-27549,EBI-8591; Score: 0.35
DE  Interaction: Q12315; IntAct: EBI-27549,EBI-7635; Score: 0.44
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044877;
GO  GO:0006406;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10523319};
SQ  MPLESIWADAPDEEPIKKQKPSHKRSNNNKKNNNSRWSNESSSNNKKKDSVNKVKNNKGNHESKTKNKIKETLPREKKPP
SQ  HSQGKISPVSESLAINPFSQKATEISPPPVSPSKMKTTKTQSKQDTASKMKLLKKKIEEQREILQKTHHKNQQQQVLMDF
SQ  LNDEGSSNWVDDDEEELILQRLKTSLKI
//
ID  O77751;
PN  Transmembrane protein 109;
GN  TMEM109;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000269|PubMed:21381722}.
DR  UNIPROT: O77751;
DE  Function: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (By similarity). Can form voltage-gated calcium and potassium channels in vitro (PubMed:21381722). {ECO:0000250|UniProtKB:Q3UBX0, ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:21381722}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0033017;
GO  GO:0005244;
GO  GO:0071480;
GO  GO:0060548;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGSGSSAPWGKHLLHAVLMVLVALVLLHSALAQSHRDFAPPGQQRREAPVDLLTQIGRSVRETLDTWIGPETMHLISET
SQ  LSQVMWAISSAISVAFFALSGIAAQLLTALGLDGDHLTQGLKLSPSQVQTFLLWGAGALVVYWLLSLLLGLVLAVLGRIL
SQ  GGLKLVIFLAGFVALVRSVPDPSTRALLLLALLTLYALLSRLTGSRASGAQLEAKVRGLERQVDELRWRQRRAAKGARSV
SQ  EEE
//
ID  O97921;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250}. Nucleus membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Secreted {ECO:0000250}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted (By similarity). {ECO:0000250}.
DR  UNIPROT: O97921;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLT
SQ  STFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRP
SQ  EVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN
//
ID  Q17602;
PN  Nuclear pore complex protein 14;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35658}. Nucleus membrane {ECO:0000269|PubMed:27723735}; Peripheral membrane protein {ECO:0000305|PubMed:27723735}. Note=Cytoplasmic side of the nuclear pore complex (By similarity). Co-localizes with caspase ced-3 to the perinuclear region in germ cells. {ECO:0000250|UniProtKB:P35658, ECO:0000269|PubMed:27723735}.
DR  UNIPROT: Q17602;
DE  Function: May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (By similarity). Plays a role in apoptosis by tethering caspase ced-3 to the nuclear membrane preventing its autoprocessing in absence of ced-4. {ECO:0000250|UniProtKB:P35658, ECO:0000269|PubMed:27723735}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0089720;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:1990001;
GO  GO:0051028;
GO  GO:1900118;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:27723735};
SQ  MSNEDVAEDVSQVTDFHFHTCRKFRLFSSKSDGYSQNEINIRNRVATSSQLGVTFVTVNSNQLSCFHTKSLLGYKITREN
SQ  MNVEVTDLPIKTIRLHGVVLINDMGVNSDGTVLGVLHTKNNDVSVDVFDIKKICTSSSIEPFKPLCTTRVGTEQINQGSC
SQ  LEWNPAFPDTFAASSTDRSILVAKINVQSPANQKLVGIGKFGAVTTAISWSPKGKQLTIGDSLGKIVQLKPELEVVRSQH
SQ  GPENKPNYGRITGLCWLATTEWLVSLENGTDQDAYLMRCKKDKPTEWIQFHELSYSSSKWPLPPQLFPATQLLVDWNVVI
SQ  VGNSKTSEISTVGKRDDWQTWVPVEGESIYLPTTSSGKDTVPIGVAVDRSMTDEVLLNPDGSQRHRPSPLVLCLTNDGIL
SQ  TAHHIISTFAAHIPCQMSSQNLAINDLKKLQFDSQKPISAPPSDQTPVTKPSTVFGQKPEAETLKSSLVGSPSSVQTPKP
SQ  SSSLFNPKSIASNIETSQLTESKPSTPAAPSSQPKIASTPKSEAIPKISDKTLEHKKAELIATKKQVLIERMDKINDSMA
SQ  GAKDATMKLSFAVGKVKTTIMECADVVRASLGDSKEVMDELKNLILSIERMSDRTQHTVKEMDFEIDEKMELVAGVEDGN
SQ  QVLEKLRNMSETEKLMRFNKLETAADLLNGKYEECSDLIKKLRMSLSEKESLRKQAILSPLRLSSNLNQLRSGSETELAL
SQ  KVMRNVSKIIMDTREQIQRTELEFVRFQRDVKFQNFKKGKENLNFTQPLEMSSLDGDAPQGKSLTDAESIKVRQALVNQI
SQ  QKRGIVKTRNVIVESYKKSENSAAMKNDLLDTSNLSNAILKLSMTPRRVMPSSSLFSASPSTPSTKSDAATQADEPPIVK
SQ  TVVVTVESPAKPIASAPAVSSPLIKLNTTTATTTMTTPKVTVPKEEANKTQDQKPIISTPASSSIFSSGSLFGTKTQTPL
SQ  VSKEESTLTTGVPSLINSSLSISPQEIEKASSKVETLNKTEEVKDEKSENEVTPDLKSEEPKSLETKVKEEPKPAVQTPV
SQ  KEEETGSNIQKTPSFSFNSTTTPKSTSSTSSIFGGGLKTQTPSSSNSTNIFGARTTTTATPTPASNTSSIFGGGSKAASS
SQ  PFGSFGQAGCQPAKTSNPATSTASVTFSFNTGATSASAKPAGFGSFGAGASAKPSSVFGGSVTAPTVPNVDDGMEDDSMA
SQ  NGGGSGGFMSGLGNARTSNTSGGNNPFAPKTSTGTSASSSSWLFGGGGNQQQQQQQKPSFSFNTAGSSAQQASAPATGTS
SQ  SVFGGAPKFGSQPAFGAKPFGGGANAGLSKNASIFGGATSSTTNNPATGGFAQFASGQKTSSLFGGGATPQTNTSIFGGG
SQ  ANTTPAPTSSVFGGGASANANKPTSFTSWR
//
ID  O60158;
PN  Bouquet formation protein 4;
GN  bqt4;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: O60158;
DR  UNIPROT: Q9USF5;
DR  PDB: 5YBX;
DR  PDB: 5YC2;
DR  PDB: 5YCA;
DR  PDB: 6A6W;
DR  PROSITE: PS51299;
DE  Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. {ECO:0000269|PubMed:19948484}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005639;
GO  GO:1990862;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0051301;
GO  GO:0070197;
GO  GO:0044820;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSA
SQ  FPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEG
SQ  EPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPS
SQ  SSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVN
SQ  KGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITK
SQ  LESEVYYEKRKVRALGGIAIGLGVGAILPFLF
//
ID  P04288;
PN  Envelope glycoprotein M;
GN  gM;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:26999189}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:17079321}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:17079321}.
DR  UNIPROT: P04288;
DR  UNIPROT: B9VQD7;
DR  UNIPROT: Q09IC3;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:26999189}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGRPAPRGSPDSAPPTKGMTGARTAWWVWCVQVATFVVSAVCVTGLLVLASVFRARFPCFYATASSYAGVNSTAEVRGGV
SQ  AVPLRLDTQSLVGTYVITAVLLLAVAVYAVVGAVTSRYDRALDAGRRLAAARMAMPHATLIAGNVCSWLLQITVLLLAHR
SQ  ISQLAHLVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLMELAPTHHRVVGPARAVLTNALLLGVFLCTADAAVSLNTI
SQ  AAFNFNFSAPGMLICLTVLFAILVVSLLLVVEGVLCHYVRVLVGPHLGAVAATGIVGLACEHYYTNGYYVVETQWPGAQT
SQ  GVRVALALVAAFALGMAVLRCTRAYLYHRRHHTKFFMRMRDTRHRAHSALKRVRSSMRGSRDGRHRPAPGSPPGIPEYAE
SQ  DPYAISYGGQLDRYGDSDGEPIYDEVADDQTDVLYAKIQHPRHLPDDDPIYDTVGGYDPEPAEDPVYSTVRRW
//
ID  O55227;
PN  Protein unc-50 homolog;
GN  Unc50;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus membrane {ECO:0000250}; Multi- pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000269|PubMed:10980252}; Multi-pass membrane protein {ECO:0000269|PubMed:10980252}.
DR  UNIPROT: O55227;
DR  Pfam: PF05216;
DE  Function: May be involved in cell surface expression of neuronal nicotinic receptors. Binds RNA. {ECO:0000269|PubMed:10980252}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0007166;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPSTSLNSSMYGNGALNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFISNKYLVKRQSRDYDVEWGYAFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVVLLYPFAPLIVLYGLSL
SQ  ALGWNFTHTLCSFYKYRVK
//
ID  G0SAK3;
PN  Nucleoporin NUP145C;
GN  NUP145;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Cytoplasmic side {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. {ECO:0000250|UniProtKB:P49687}. [Nucleoporin NUP145N]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Biased towards the nucleoplasmic side, nuclear pore complex. {ECO:0000250|UniProtKB:P49687}.
DR  UNIPROT: G0SAK3;
DR  UNIPROT: G3EQ75;
DR  UNIPROT: G3EQ76;
DR  PDB: 5CWW;
DR  PDB: 5HB0;
DR  PDB: 5HB5;
DR  PDB: 5HB6;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. {ECO:0000250|UniProtKB:P49687}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016787;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P49687};
SQ  MSFGFGSGGFGQNNNSSTFGGFGSTPTTNTGFGSTGTTAFGSTSNTTGGGLFGGGGGGFGSGNTFGSGFGSKPAFGTPAT
SQ  TSSTSLFGSTTTTAGGTGFGSGGFGSTNTSSPFGGGGTSLFGNKTTTGFGSGTSTFGSNTGGGLFGGGSTTTGFGATNNP
SQ  GIGTNVGDPPGTAVVPFSPTVEKEVNNPSQSNSYQNILFMDAYKKWSAEELRLADYNQGRKTAAPGGTGAFGSSGFGGFG
SQ  TTSNTGGFGSNTGGGLFGNTQQNTGGFGTTNTTGSAFGSGGGLFGNKPATGGLFGTSSSQPAQSGGLFGSGTASTFGSSN
SQ  TGTTSTFGSNNNTGGGLFGSNNTSSKPAFSFGTSNTSTPGFGTATTGSGFGTGTTTNTGGGLFGNTAQNTNTGGGLFGNQ
SQ  QQSGSAFGSGTGFGQQNQSTGTSLFGNTQQKPGGLFGSTTTNTSGGLFGSTNTGTSTFGQTPATQNTGGGLFGSKPAGTG
SQ  GLFGSTATNQPASTGGLFGNLNTNAQTQQPATGGLFGNLGQNNQAKPSLFGTSTTTGGGLFGNTNAQQQTGSLFGTSTAQ
SQ  QQPQTGLGASLFGSSQQQQQQPQTFSTSITDISAYGATTLFSGLPDDKIQNPGPLATPLSGKAKVKSRSILPMYKLSPAN
SQ  ASRLVTTPQKRAYGFSFSAYGSPTSPSSSASSTPGAFGQSILSSSINRGLNKSISASNLRRSLNVEDSILQPGAFSANSS
SQ  MRLLGGPGSHKKLVINKDMRTDLFSPPNKDKQPQEDGTAARKTVTKRVSFDTSNVETPEKTIESSIPATDDSGYLKPDAR
SQ  STANGTNGANGAKSSPVAAASPPEMEQVKGKELAVVHEEESPAPAQTDKPRGSQIEPGAYWMSPTADDIRAMNRMQRQRV
SQ  VGFTVGRENVGSVQFKVPVDLSNINLDDLFGTIVILEPRSATVYPNAAKKPPMGKGLNVPALISLEHSWPRGGPTIKGRR
SQ  LERHIERLKSIPDTTFESYDPETGVWAFSVEHFTTYGLGDDDDYDDDDYETEPESAVKSTPRPVTSPSISKSSTSPIDPD
SQ  DTFEFRRSRRALPGAFDDAALSDTDEVANHAQRQGTLSPEPQDADTPLPSREWPEDESMADGLDEYQLEAYEEASQQGSV
SQ  DEQEDFLPSRFAADNDAPQVPAGIMRARMRAVKKLNAPTKIEVAGGDDWTQILQASVKAPRTMDRATLRALNESGAVWEM
SQ  KDRGSPPPQATATVSDGMGFATSIDLMKSLFEQAKAPTQPALTTSGKGFVKWPYEQRSKTDTEENLAVPRTNWGPNELLI
SQ  STQHNEPNLLPVDAADDSATSPSTLARLQQYINLVSSKKQLQRVAGPEFRELAQGDSVWELAALLFDDNGEGVSQFWQQL
SQ  VSEATDRALSFTAGLEEKAIICLAGNRVDEACRHLLAAGNFRLATLVSTIGKVDNKDIRAQLKDWRESNVLAEFSEPIRA
SQ  IYELLAGNASVCAGVKNVPIENRVNSFTISQRFGLDWMRSFGLRLWYTSGVIPDVAAAVRSFQEDIEQDREPEPDSALWT
SQ  LLKAFASREYDWSDTRLGWLLTKAIYTTGKVSFGEDALQKLDKASVTFASALTAASHWVPATFVLLQLSDPASREAAVRD
SQ  HLGRHAHRIGSPRNLMSPFFTLQKFGVPEAWIWEAKALDYRSRQDSQQEFLALIWAQNYAEANRTFVTRVGPDLVIERNL
SQ  PRLFAFAQLLFKVKKHLPNWERSAAVYLLYPMAVMQNQGSGKLDRFDNQLIDGLVALHSQTHGDIRQEAAIADMAEELIK
SQ  CKGAAAASDPRLLQLLPQDVRGKYLRAQVLEAF
//
ID  Q86HW7;
PN  Nuclear transport factor 2;
GN  nutf2;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: Q86HW7;
DR  UNIPROT: Q551K9;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}.
DE  Reference Proteome: Yes;
DE  Interaction: O76329; IntAct: EBI-922673,EBI-922768; Score: 0.40
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0008536;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQSVDPQVVGVGKQFVEHYYGIFDSNRAGLTQIYQQQTTLTWEGKFLSGADAIVKHIVELPFQQTNRKINSIDCQQTYQP
SQ  GIMITVTGTLIIDGEAKNQLKFVQVFNLASNNGSFLLINDFFRLVLD
//
ID  Q03281;
PN  Inner nuclear membrane protein HEH2;
GN  HEH2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16929305}; Single-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
DR  UNIPROT: Q03281;
DR  UNIPROT: D6VT82;
DR  PDB: 4PVZ;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P38181; IntAct: EBI-22131,EBI-11756; Score: 0.44
DE  Interaction: P39929; IntAct: EBI-22131,EBI-17554; Score: 0.58
DE  Interaction: P11484; IntAct: EBI-22131,EBI-8627; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-22131; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-22131; Score: 0.35
DE  Interaction: P52917; IntAct: EBI-20475,EBI-22131; Score: 0.40
DE  Interaction: P32462; IntAct: EBI-6502,EBI-22131; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-22131,EBI-26307; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0034399;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKS
SQ  KKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSEL
SQ  ETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETR
SQ  NESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIW
SQ  LWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEP
SQ  GYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWES
SQ  QREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLG
SQ  VLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQ
SQ  SENIELYLLEENGEIMTCWEWKE
//
ID  P52370;
PN  Envelope glycoprotein M;
GN  gM;
OS  10323;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52370;
DR  UNIPROT: O39493;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044177;
GO  GO:0044178;
GO  GO:0033644;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0019012;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAGSAQPAAVHWRLWLAQVGVFAGLALLLLITLIGAASPGAGLPCFYAAIVNYNARNLSADGGAWAQRELGARHPALFLE
SQ  TPTTAAFSAYTAVVLLAVAAFDVAAAIIIRRENSGGFAAAYHMNALATLATPPGALLLGALAAWTLQAAVLLLSHKIMVL
SQ  AAATYLAHLAPPAAFVGLFCTAGLPGAEYAQAVHALRERSPRAHRLLGPGRAVMINLAGGLLALIIGTAPLMLGQLLGAG
SQ  LGLSLAQTVVAGVTVFCLAAVLFLVLTELVLSRYTQVLPGPAFGTLVAASCIAVASHDYFHQLRGVVRTQAPRAAARVKL
SQ  ALAGVALLAVAMLVLRLVRACLHHRRKGSAFYGHVSAARQQAARYIARARSSRGMAPLEGDAAALLDRGVASDDEEAVYE
SQ  AHAPPRPPTIPLRRPEVPHSRASHPRPPPRSPPPAHVK
//
ID  Q03707;
PN  Inner nuclear membrane protein SRC1;
GN  SRC1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16929305}; Multi-pass membrane protein {ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
DR  UNIPROT: Q03707;
DR  UNIPROT: D6VZE1;
DR  UNIPROT: Q03712;
DR  PDB: 4XZR;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Plays a role in sister chromatid separation. {ECO:0000269|PubMed:11754482}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-18064,EBI-10420; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-11756,EBI-18064; Score: 0.37
DE  Interaction: P39929; IntAct: EBI-17554,EBI-18064; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-8591,EBI-18064; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-18064; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-18064,EBI-24570; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-18064,EBI-8632; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-18064; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-18064; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-18064; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-18064; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-18064,EBI-29516; Score: 0.35
DE  Interaction: Q12066; IntAct: EBI-18064,EBI-35877; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-18064,EBI-15427; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-18064,EBI-5687; Score: 0.35
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0034087;
GO  GO:0043007;
GO  GO:0000070;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSS
SQ  PSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNK
SQ  SDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVK
SQ  TPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEV
SQ  EQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTE
SQ  KDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRL
SQ  LIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDD
SQ  KKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQ
SQ  LSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKV
SQ  IEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNI
SQ  KSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI
//
ID  Q9HGN7;
PN  Translocation protein sec63;
GN  sec63;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9HGN7;
DR  Pfam: PF00226;
DR  Pfam: PF02889;
DR  PROSITE: PS50076;
DE  Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec63 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031207;
GO  GO:0030544;
GO  GO:0008320;
GO  GO:0003723;
GO  GO:0006620;
GO  GO:0031204;
GO  GO:0006614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAI
SQ  GFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKT
SQ  RENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMET
SQ  SLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVL
SQ  KLWQHIVQAIPLDAPFPLLQLPHLLMEDVKNLSIRNISSIPQFLSLSEEQTKDYLPNYSKNQLKEMREIANGIPRISVVA
SQ  AKVLVDDDEYITVGAIANLILDLKCSYGTEVVPEVSTDGTETATKKDEEDAEKYHQSKDVVLGDVETLPYAWAPYFTQHH
SQ  KTAWWIYVVDPRQNRVIVPPFSITDIPKTLRTFRIPFQVPPVAGTFSFQLHIMSNSYVGEDVISNLTMIVKDTSVLQEQL
SQ  QEEAVSDLEDNSDIDESANAGKDFSDDENIGSDEEDESEYDPMDTDTSDGE
//
ID  P52590;
PN  Nuclear pore complex protein Nup107;
GN  Nup107;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P57740}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. {ECO:0000250|UniProtKB:P57740}.
DR  UNIPROT: P52590;
DR  Pfam: PF04121;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis. {ECO:0000250|UniProtKB:P57740}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0008585;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0051292;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRSGFGGMSSPVIRDPEVTRTARKHSAHKRVLIQANQDENFGTTTPRSQIIPRTPSSFRQPFTPPSRSLLRHPDISYIF
SQ  GTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGFYTNTEHHSMTEDINLSTVMLREDDPGEAASMSMFSDFLQ
SQ  SFLKHSSTTVFDLVEEYENICASQVNILSKIVSRATRWDWQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENM
SQ  FAIAGINASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGDFSDNIEFYAKSVYWENTLHSLKQRQLLSYIGSTRPL
SQ  VTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLHHDPNVNGGTELEPVE
SQ  GNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTLDETEELP
SQ  REYMEANWTLEKVFEELQATDKKRVLEENQEHYHVVQKFLILGDIDGLMDEFSKWLSKSRSSLPGHLLRFMTHLILFFRT
SQ  LGLQTKEEVSIEVLKTYIQLLINEKHTNLIAFYTCHLPQDLAVAQYALFLEGVTECEQRHQCLELAKEADLDVATITKTV
SQ  VENIRKKDNGEFSHHDLAPSLDTATTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDS
SQ  IAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNERFKHMNSAPQKPTLLSQATFTEKVAHEHKEKKYEMDH
SQ  NIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEEDPERAHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLAD
SQ  MVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS
//
ID  Q640Z6;
PN  Nuclear pore complex protein Nup153;
GN  nup153;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:9531546}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9531546}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Colocalizes with tpr at the nuclear pore complex.
DR  UNIPROT: Q640Z6;
DR  Pfam: PF08604;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. May be involved in the retention of unspliced mRNAs in the nucleus. Probably mediates tpr anchoring to the nuclear membrane at NPC. Possible DNA- binding subunit of the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0003677;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAGGGGPGGPGTGGKIRSRRYHLSSGRTPYSKSRQQQQGIISRVTDTVKSIVPGWLQKYFNKQEEEHDRVHSASEVIV
SQ  NDTEARENNAEHHIYVVDDDDDEEGNSPTDGRVTPEPIINVDEEVPSTSQSAINNTDALTRPSLHRASLNFNIFDSPALN
SQ  CQPSTSSAFPIGTSGFSLIKEIKDSTSQHDDDNISTTSGFSSRASDKDLAVSKNVSVPPLWSPEVDRSQSLSHNSSMTSK
SQ  KPTFNLSAFGSLSPSLGNASILNRQLGDSPFYPGKTTYQGAAAVRSSRVRATPYQAPLRRQVKAKPAAHSQQCGVTSSAA
SQ  RRILQSLEKMSSPLADAKRIPSNSSLSHTPEKNVMDIPENPSKRKKVESPFPPVQRLVTPKSISVSANRSLYIKPSLTPS
SQ  AVSNTNSRRIQPDKHNESRKNNLQTTSQSHSFSYPKFSTPASNGLSSGTGGGKMMREKGSHYSTKPANEELDGPVLPEIP
SQ  LPLSTAALPSFQFSTLSGSATSPISVTKPANSTTCRLTSSSPSFTFSSPIVKSTESNAQSPGSSVDFTFSVPAAKASSAT
SQ  SDESKVSAVSRAAKTHAAVSSAKNTDDEQLGFCKPAKTLKEGSVLDMLRSPGFSSSPSLLTSASSLNRSTPTLSKTVGNT
SQ  FSPANVSLGVGSKQAFGLWQCSACFHENMSSDSNCISCSALKPRPTETSKKLPASPPSSNTKSTVPLSSTPGLGDIFKKP
SQ  AGMWDCDTCLVQNKAEVTKCVACETPKPGTGMKATLLIPSTTKSTNPATNTLAFASCSASIPNEEMFKKPMGSWECTVCH
SQ  MQNKTEDNTCVGCKAEKPGTVKSVPTAAPSGLLGLLDQFKKPTGSWDCDVCLIQNKPEANKCIACESAKPGTKAELKGTF
SQ  DTVKNSVSVAPLSSGQLGLLDQFKKSAGSWDCDVCLVENKPEATKCVACETSKPGTKAELKGFGTSTFSSGTAAPTFKFG
SQ  VQSSDSTAELKSGASTSGFAKSIGNFKFGLASASTTTEETGKKSFTFGSSTTNEVSAGFKFGIAGSAQTKPDTLSQSTTS
SQ  GFTFGSVSNTVSLAPTATSSGSTGLQVAAVIADSNLATTATLKSAEEKKAEAPTITPFSFGKTDQNKETASTSFVFGKKD
SQ  EKTDSAPTGSSFAFGLKKDGEESKQFLFGKPEPTKVDGSAASAGFAFGVTNPTEKKDIEQPGKSVFAFGAQTSITDAGAS
SQ  KQPFSFLTNVSSTAASSSTCGVSSSVFGSVTQSSTPATPSNVFGSAISANAPAPSSGVFGNLTPSNAPAASSTLFGNVAP
SQ  SSTPSGSSGLFGTAAASSTPATSTSLFGSAAKLSAPASSGGVFNSAAPAAPASTASSVFGSVASSTNTSANSANIFGSSG
SQ  GAATAPGAFVFGQPASTASTVFGNSSESKSTFVFSGQENKPVTSASTSVTPFLFGAVSASTTPAAPGFNFGRTITSNTTG
SQ  TSSSPFIFGAGASGSASSSITAQANPVPAFGQSSNPSTAPAFGSSTSVPVFPAGNSQQVPAFGSSSAQPPVFGQQATQPS
SQ  FGSPAAPSAGSGFPFGNNANFNFNSTNSSGGVFTFNANSGSTTQPPPPGYMFNAAAPGFNMGTNGRTTPASTISTRKIKT
SQ  ARRRK
//
ID  Q22747;
PN  Transmembrane protein 201 homolog;
GN  samp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:25057012}; Multi-pass membrane protein {ECO:0000255}. Note=Localization at the nuclear envelope does not require lmn-1. {ECO:0000269|PubMed:25057012}.
DR  UNIPROT: Q22747;
DR  Pfam: PF09779;
DE  Function: Plays a role in nuclear migration in hypodermal cells. {ECO:0000269|PubMed:25057012}.
DE  Reference Proteome: Yes;
DE  Interaction: Q94420; IntAct: EBI-320790,EBI-324189; Score: 0.49
DE  Interaction: Q21021; IntAct: EBI-2003933,EBI-324189; Score: 0.37
DE  Interaction: Q9N5U1; IntAct: EBI-2005375,EBI-324189; Score: 0.37
DE  Interaction: Q9U2Z1; IntAct: EBI-324189,EBI-2006699; Score: 0.37
DE  Interaction: H2L0Q6; IntAct: EBI-324189,EBI-11466777; Score: 0.37
DE  Interaction: O17915; IntAct: EBI-324189,EBI-324099; Score: 0.37
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0009792;
GO  GO:0030473;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVAAAVGVIASVPILYKAIRPRIKTSVECWFCRKSTKVEYQQRNSFTCPSCEQYNGFTEDGDYNRRIPGQAWTTPKRYC
SQ  EPGKMQSEKPSTFLDRFGGVNMSPKASNGLCSECNLGQEIIMNKVAEFEPIDEDRWNEELEDYRYKLERMYQLCPRCTIQ
SQ  VHGKLEEDKKKYSYLLKVKYKLKHAIGSTLREVMNNQKRSRRFFFAGGSTCEALHFGCLISSIILFLANIDFLQQDAGAS
SQ  LINLPKALQDILPEVYKYSFVINFLIFTTHLIAAFNNKCRVTLPDLLLPILLILAMLTVLTSSDNLSQDVALVRGACASF
SQ  STILSMAVTLLPRKKLHKKRPNKIVSSAFSVASTPISQCSSQNSRNASLLDHDHTILRRSPHTPSASPPAMNSSPPLLRE
SQ  ITNGPVWSAMRSRENKENMQSYQTKPNNHVESMDWDDSESMAAQSVAQSTRSSHFKPGLLSRNINERMTAQQLTPSVANL
SQ  NLDTRSVDSPSIFSRQHRQMAQQQNHTPTRSLFGPPRSMVASQYDRSHYMAPEAHTRPGSVFTSVSQQDGHSTVSGAWQC
SQ  RVIGILFALVFIVLIMQIGLFYVLFTRN
//
ID  Q9NZJ0;
PN  Denticleless protein homolog;
GN  DTL;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:26431207}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome. Note=Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis.
DR  UNIPROT: Q9NZJ0;
DR  UNIPROT: A8K8H8;
DR  UNIPROT: D3DT98;
DR  UNIPROT: Q5VT77;
DR  UNIPROT: Q96SN0;
DR  UNIPROT: Q9NW03;
DR  UNIPROT: Q9NW34;
DR  UNIPROT: Q9NWM5;
DR  PDB: 6QC0;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 610617;
DR  DisGeNET: 51514;
DE  Function: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA- dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). {ECO:0000269|PubMed:16861906, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17085480, ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:18794348, ECO:0000269|PubMed:19332548, ECO:0000269|PubMed:20129063, ECO:0000269|PubMed:23478441, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:23677613, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:27906959}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TLR7; IntAct: EBI-2553626,EBI-1176075; Score: 0.40
DE  Interaction: Q7L5N1; IntAct: EBI-486838,EBI-1176075; Score: 0.56
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-1176075; Score: 0.35
DE  Interaction: Q3U1J4; IntAct: EBI-2552275,EBI-1176075; Score: 0.40
DE  Interaction: O60232; IntAct: EBI-741415,EBI-1176075; Score: 0.35
DE  Interaction: Q9UHV9; IntAct: EBI-359873,EBI-1176075; Score: 0.35
DE  Interaction: Q8NB37-2; IntAct: EBI-21529247,EBI-1176075; Score: 0.35
DE  Interaction: Q99627; IntAct: EBI-2510102,EBI-1176075; Score: 0.35
DE  Interaction: Q92990; IntAct: EBI-726150,EBI-1176075; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-11963218,EBI-1176075; Score: 0.35
DE  Interaction: Q13619; IntAct: EBI-456106,EBI-1176075; Score: 0.53
DE  Interaction: Q13620; IntAct: EBI-456067,EBI-1176075; Score: 0.53
DE  Interaction: P61964; IntAct: EBI-1176075,EBI-540834; Score: 0.40
DE  Interaction: Q16531; IntAct: EBI-1176075,EBI-350322; Score: 0.56
DE  Interaction: Q9BQ67; IntAct: EBI-1176075,EBI-351000; Score: 0.35
DE  Interaction: P97784; IntAct: EBI-1176075,EBI-1266607; Score: 0.40
DE  Interaction: Q99832; IntAct: EBI-357046,EBI-1176075; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-356673,EBI-1176075; Score: 0.35
DE  Interaction: Q13557-10; IntAct: EBI-16813278,EBI-1176075; Score: 0.35
DE  Interaction: Q6ZN54-2; IntAct: EBI-12346463,EBI-1176075; Score: 0.35
DE  Interaction: Q15170-2; IntAct: EBI-11156070,EBI-1176075; Score: 0.35
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0080008;
GO  GO:0031464;
GO  GO:0031465;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0006974;
GO  GO:0042769;
GO  GO:0006260;
GO  GO:0010971;
GO  GO:0045732;
GO  GO:0043687;
GO  GO:0006513;
GO  GO:0000209;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0048511;
GO  GO:0072425;
GO  GO:0019985;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYN
SQ  TESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGG
SQ  RDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGII
SQ  KVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFY
SQ  VKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGG
SQ  DKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPI
SQ  NRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCL
SQ  ESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPL
SQ  RPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQED
SQ  FCGPEHSTEL
//
ID  Q9LV85;
PN  Protein CPR-5;
GN  CPR5;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:21875893, ECO:0000269|PubMed:25455564}.
DR  UNIPROT: Q9LV85;
DR  UNIPROT: Q8W3U8;
DE  Function: May play a role in transcriptional processes (PubMed:21875893). Regulates negatively the senescence and chlorotic lesions induced by biotic (e.g. pathogens) and abiotic (e.g. sugars, darkness) agents, probably by controlling programmed cell death (pcd) (PubMed:11846876,PubMed:9338960, Ref.6, PubMed:11728314). Negative regulator of plant programmed cell death (PCD) and effector-triggered immunity (ETI) (PubMed:25455564). Promotes cell division and endoreduplication (e.g. in trichomes) (PubMed:11728314). {ECO:0000269|PubMed:11728314, ECO:0000269|PubMed:11846876, ECO:0000269|PubMed:25455564, ECO:0000269|PubMed:9338960, ECO:0000269|Ref.6, ECO:0000305|PubMed:21875893}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0006952;
GO  GO:0010150;
GO  GO:0048573;
GO  GO:0010182;
GO  GO:0009627;
GO  GO:0010090;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEALLLPPSPEPQNQITNPANSKPNHQSGDVHKDETMMMKKKKDTNPSNLEKRKLKGKKKEIMDNDEASSSYCSTSSTSN
SQ  SNSTKRVTRVVHRLRNPMRLGMARRSVGERQAEKLAKPLGFSLAAFANMVIARKNAAGQNVYVDDLVEIFATLVEESLAN
SQ  VYGNKLGSFATNFEQTFSSTLKILKLTNECANPHQSNNNDGGSCNLDRSTIDGCSDTELFERETSSATSAYEVMQGSATA
SQ  TSLMNELALFEETLQLSCVPPRSSAMALTTDERFLKEQTRANDLKTVEIGLQIRELRCKETALGLKFESNNLGKAALELD
SQ  VSKAAFRAEKFKTELEDTRKEEMVTRIMDWLLVSVFSMLASMVLGVYNFSIKRIEDATSVCDQSEEKSSSWWVPKQVSSI
SQ  NSGFNTFICRVRVWVQIFFGVLMIIVFTYFLNKRSSGTKQTMPISFIVLFLGIFCGVSGKLCVDTLGGDGKLWLIVWEVF
SQ  CLLQFVANVFTLALYGLMFGPINVTQETRSNRCNSMFPYWARRSVVYVVILFVLPVINGLLPFATFGEWRDFAMYHLHGG
SQ  SDYA
//
ID  Q13023;
PN  A-kinase anchor protein 6;
GN  AKAP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum. Nucleus membrane. Note=In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences.
DR  UNIPROT: Q13023;
DR  UNIPROT: A7E242;
DR  UNIPROT: A7E2D4;
DR  UNIPROT: O15028;
DR  OMIM: 604691;
DR  DisGeNET: 9472;
DE  Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes.
DE  Reference Proteome: Yes;
DE  Interaction: P00519; IntAct: EBI-375543,EBI-1056102; Score: 0.40
DE  Interaction: P12931; IntAct: EBI-621482,EBI-1056102; Score: 0.40
DE  Interaction: Q06787; IntAct: EBI-1056102,EBI-366305; Score: 0.37
DE  Interaction: P06241; IntAct: EBI-515315,EBI-1056102; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-1056102,EBI-401755; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-389883,EBI-1056102; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-79464,EBI-1056102; Score: 0.40
DE  Interaction: P46108; IntAct: EBI-886,EBI-1056102; Score: 0.40
DE  Interaction: Q99459; IntAct: EBI-1056102,EBI-374880; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-1056102,EBI-529989; Score: 0.37
DE  Interaction: Q8TDR0-2; IntAct: EBI-1056102,EBI-11946508; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-748974,EBI-1056102; Score: 0.51
DE  Interaction: A0A2B6C7C6; IntAct: EBI-2816451,EBI-1056102; Score: 0.37
DE  Interaction: Q96EV8; IntAct: EBI-465804,EBI-1056102; Score: 0.37
GO  GO:0034704;
GO  GO:0005901;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0014704;
GO  GO:0014701;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0008179;
GO  GO:0044325;
GO  GO:0060090;
GO  GO:0051018;
GO  GO:0034237;
GO  GO:0043495;
GO  GO:0001508;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071345;
GO  GO:0070886;
GO  GO:0030307;
GO  GO:0061051;
GO  GO:1902261;
GO  GO:1901381;
GO  GO:0051281;
GO  GO:0060316;
GO  GO:0006605;
GO  GO:0060306;
GO  GO:0010738;
GO  GO:0010880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMT
SQ  SERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLV
SQ  LRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGL
SQ  GDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPG
SQ  LTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEET
SQ  FKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISS
SQ  SLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQR
SQ  SWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQT
SQ  EVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDI
SQ  LSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAME
SQ  TTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHS
SQ  WILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNG
SQ  LLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDS
SQ  INEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQL
SQ  QYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLN
SQ  VIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAP
SQ  SSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNS
SQ  GSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKV
SQ  GDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQP
SQ  DVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWL
SQ  TSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSI
SQ  NEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSST
SQ  LTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPS
SQ  DTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENL
SQ  GSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSD
SQ  ALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENE
SQ  VAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACV
SQ  EGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAE
SQ  NLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR
//
ID  Q9HD36;
PN  Bcl-2-like protein 10;
GN  BCL2L10;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:11593390}. Nucleus membrane {ECO:0000269|PubMed:11593390}.
DR  UNIPROT: Q9HD36;
DR  UNIPROT: Q3SX80;
DR  UNIPROT: Q52LQ9;
DR  UNIPROT: Q8TCS9;
DR  PDB: 4B4S;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  OMIM: 606910;
DR  DisGeNET: 10017;
DE  Function: Promotes cell survival. Suppresses apoptosis induced by BAX but not BAK. {ECO:0000269|PubMed:11278245}.
DE  Reference Proteome: Yes;
DE  Interaction: P22736; IntAct: EBI-721550,EBI-2126349; Score: 0.40
DE  Interaction: Q13323; IntAct: EBI-2126349,EBI-700794; Score: 0.70
DE  Interaction: Q86VY9; IntAct: EBI-11732844,EBI-2126349; Score: 0.56
DE  Interaction: Q99735; IntAct: EBI-11324706,EBI-2126349; Score: 0.56
DE  Interaction: O43521; IntAct: EBI-526406,EBI-2126349; Score: 0.78
DE  Interaction: Q07812; IntAct: EBI-516580,EBI-2126349; Score: 0.40
DE  Interaction: O43521-1; IntAct: EBI-526416,EBI-2126349; Score: 0.40
DE  Interaction: Q5PRF9; IntAct: EBI-1047489,EBI-2126349; Score: 0.56
DE  Interaction: Q96LC9; IntAct: EBI-3919268,EBI-2126349; Score: 0.56
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0089720;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006919;
GO  GO:0097192;
GO  GO:0007292;
GO  GO:0008630;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVDQLRERTTMADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFELVAL
SQ  MADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQ
SQ  GGWDGFCHFFRTPFPLAFWRKQLVQAFLSCLLTTAFIYLWTRLL
//
ID  O00299;
PN  Chloride intracellular channel protein 1;
GN  CLIC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710}. Nucleus membrane {ECO:0000269|PubMed:9139710}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710, ECO:0000305|PubMed:11978800, ECO:0000305|PubMed:14613939}. Cell membrane {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:14613939, ECO:0000305|PubMed:11978800}; Single-pass membrane protein {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:14613939}. Note=Mostly in the nucleus including in the nuclear membrane (PubMed:9139710, PubMed:12681486). Small amount in the cytoplasm and the plasma membrane (PubMed:9139710). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (PubMed:11940526, PubMed:11551966, PubMed:14613939). {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
DR  UNIPROT: O00299;
DR  UNIPROT: Q15089;
DR  UNIPROT: Q502X1;
DR  PDB: 1K0M;
DR  PDB: 1K0N;
DR  PDB: 1K0O;
DR  PDB: 1RK4;
DR  PDB: 3O3T;
DR  PDB: 3P8W;
DR  PDB: 3P90;
DR  PDB: 3QR6;
DR  PDB: 3SWL;
DR  PDB: 3TGZ;
DR  PDB: 3UVH;
DR  PDB: 4IQA;
DR  PDB: 4JZQ;
DR  PDB: 4K0G;
DR  PDB: 4K0N;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DR  OMIM: 602872;
DR  DisGeNET: 1192;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
DE  Reference Proteome: Yes;
DE  Interaction: P32121; IntAct: EBI-714559,EBI-347404; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-347404; Score: 0.35
DE  Interaction: O75832; IntAct: EBI-752185,EBI-347404; Score: 0.65
DE  Interaction: Q9Y2H1; IntAct: EBI-991501,EBI-347404; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-347404; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-347404; Score: 0.35
DE  Interaction: Q9Y251; IntAct: EBI-5453868,EBI-347404; Score: 0.35
DE  Interaction: P40692; IntAct: EBI-744248,EBI-347404; Score: 0.37
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-347404; Score: 0.35
DE  Interaction: Q5NID2; IntAct: EBI-2796292,EBI-347404; Score: 0.37
DE  Interaction: A0A384KST0; IntAct: EBI-2845592,EBI-347404; Score: 0.37
DE  Interaction: P20292; IntAct: EBI-3904621,EBI-347404; Score: 0.37
DE  Interaction: P24539; IntAct: EBI-1044810,EBI-347404; Score: 0.37
DE  Interaction: P27449; IntAct: EBI-347404,EBI-721179; Score: 0.37
DE  Interaction: Q93050; IntAct: EBI-347404,EBI-2891238; Score: 0.37
DE  Interaction: P34130; IntAct: EBI-347404,EBI-3907456; Score: 0.37
DE  Interaction: P50416; IntAct: EBI-347404,EBI-2817330; Score: 0.37
DE  Interaction: Q99676; IntAct: EBI-347404,EBI-3907489; Score: 0.37
DE  Interaction: P05386; IntAct: EBI-354582,EBI-347404; Score: 0.37
DE  Interaction: P10827; IntAct: EBI-286285,EBI-347404; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-81279,EBI-347404; Score: 0.37
DE  Interaction: P37198; IntAct: EBI-347978,EBI-347404; Score: 0.37
DE  Interaction: Q9NR11; IntAct: EBI-3916142,EBI-347404; Score: 0.37
DE  Interaction: P60710; IntAct: EBI-353957,EBI-347404; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-400918,EBI-347404; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-2553589,EBI-347404; Score: 0.35
DE  Interaction: Q9NQX4; IntAct: EBI-1237297,EBI-347404; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-352936,EBI-347404; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-762451,EBI-347404; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-347404; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-8316222,EBI-347404; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-347404; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-356283,EBI-347404; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-297509,EBI-347404; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135403,EBI-347404; Score: 0.35
DE  Interaction: Q86WR7; IntAct: EBI-347404,EBI-2880603; Score: 0.35
DE  Interaction: Q4KMQ1-2; IntAct: EBI-347404,EBI-11978969; Score: 0.67
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-347404; Score: 0.56
DE  Interaction: P15336; IntAct: EBI-1170906,EBI-347404; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-347404; Score: 0.35
DE  Interaction: Q13162; IntAct: EBI-2211957,EBI-347404; Score: 0.37
DE  Interaction: Q81Z98; IntAct: EBI-2809746,EBI-347404; Score: 0.37
DE  Interaction: A0A0F7REA8; IntAct: EBI-347404,EBI-2830099; Score: 0.37
DE  Interaction: Q8CZM8; IntAct: EBI-347404,EBI-2848309; Score: 0.37
DE  Interaction: Q81XG9; IntAct: EBI-347404,EBI-2811950; Score: 0.37
DE  Interaction: P01889; IntAct: EBI-1046513,EBI-347404; Score: 0.40
DE  Interaction: P11171; IntAct: EBI-347404,EBI-1050906; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-347404,EBI-307369; Score: 0.40
DE  Interaction: P62330; IntAct: EBI-347404,EBI-638181; Score: 0.40
DE  Interaction: P23508; IntAct: EBI-347404,EBI-307531; Score: 0.40
DE  Interaction: Q8N5H7; IntAct: EBI-745980,EBI-347404; Score: 0.35
DE  Interaction: Q15139; IntAct: EBI-1181072,EBI-347404; Score: 0.35
DE  Interaction: O15116; IntAct: EBI-347619,EBI-347404; Score: 0.67
DE  Interaction: Q5HYW2; IntAct: EBI-347404,EBI-2859639; Score: 0.56
DE  Interaction: Q81U22; IntAct: EBI-2814904,EBI-347404; Score: 0.37
DE  Interaction: Q9HCN8; IntAct: EBI-2339921,EBI-347404; Score: 0.35
GO  GO:0072562;
GO  GO:0005903;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005615;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0045296;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0006821;
GO  GO:0070527;
GO  GO:0045669;
GO  GO:0051726;
GO  GO:0034765;
GO  GO:0051881;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDE
SQ  GVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKAL
SQ  K
//
ID  Q8TD16;
PN  Protein bicaudal D homolog 2;
GN  BICD2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11864968}. Cytoplasm {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664120}. Nucleus envelope {ECO:0000269|PubMed:20386726}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20386726}. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (PubMed:20386726). {ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:20386726}.
DR  UNIPROT: Q8TD16;
DR  UNIPROT: O75181;
DR  UNIPROT: Q5TBQ2;
DR  UNIPROT: Q5TBQ3;
DR  UNIPROT: Q96LH2;
DR  UNIPROT: Q9BT84;
DR  UNIPROT: Q9H561;
DR  PDB: 6OFP;
DR  Pfam: PF09730;
DR  OMIM: 609797;
DR  OMIM: 615290;
DR  OMIM: 618291;
DR  DisGeNET: 23299;
DE  Function: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi- endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:25962623). Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (By similarity). {ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:25962623}.
DE  Disease: Spinal muscular atrophy, lower extremity-predominant 2A, childhood onset, autosomal dominant (SMALED2A) [MIM:615290]: An autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life. {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:23664120, ECO:0000269|PubMed:28635954}. Note=The disease is caused by mutations affecting the gene represented in this entry. Spinal muscular atrophy, lower extremity-predominant, 2B, prenatal onset, autosomal dominant (SMALED2B) [MIM:618291]: An autosomal dominant neuromuscular disorder characterized by decreased fetal movements, fractures in utero, severe congenital joint contractures, arthrogryposis multiplex congenita, severe hypotonia, muscle atrophy, and respiratory insufficiency and failure due to muscle weakness. Some patients may have dysmorphic facial features and/or abnormalities on brain imaging. Death in early childhood may occur. {ECO:0000269|PubMed:27751653, ECO:0000269|PubMed:28635954, ECO:0000269|PubMed:30054298}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-2372628; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-476768,EBI-2372628; Score: 0.35
DE  Interaction: Q0WH91; IntAct: EBI-2372628,EBI-2874902; Score: 0.37
DE  Interaction: Q9D0F1; IntAct: EBI-309872,EBI-2372628; Score: 0.40
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-2372628; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2552999,EBI-2372628; Score: 0.40
DE  Interaction: Q9UGI0; IntAct: EBI-527853,EBI-2372628; Score: 0.40
DE  Interaction: Q15154; IntAct: EBI-741421,EBI-2372628; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-2873150,EBI-2372628; Score: 0.35
DE  Interaction: Q9Q2G4; IntAct: EBI-6248094,EBI-2372628; Score: 0.35
DE  Interaction: A0A0H2W0T4; IntAct: EBI-2372628,EBI-2841918; Score: 0.37
DE  Interaction: Q14204; IntAct: EBI-356015,EBI-2372628; Score: 0.40
DE  Interaction: O14576; IntAct: EBI-2372628,EBI-366267; Score: 0.52
DE  Interaction: P20340; IntAct: EBI-1052826,EBI-2372628; Score: 0.46
DE  Interaction: Q8N4N8; IntAct: EBI-2372628,EBI-443523; Score: 0.40
DE  Interaction: P55081; IntAct: EBI-2372628,EBI-1048159; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-2372628,EBI-358900; Score: 0.40
DE  Interaction: Q8TE73; IntAct: EBI-1057712,EBI-2372628; Score: 0.40
DE  Interaction: Q71DI3; IntAct: EBI-750650,EBI-2372628; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-1056125,EBI-2372628; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-2372628; Score: 0.40
DE  Interaction: O94989; IntAct: EBI-740691,EBI-2372628; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-2372628,EBI-358372; Score: 0.40
DE  Interaction: P10412; IntAct: EBI-2372628,EBI-358163; Score: 0.40
DE  Interaction: P61163; IntAct: EBI-2372628,EBI-774234; Score: 0.40
DE  Interaction: O95858; IntAct: EBI-7361096,EBI-2372628; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-2372628; Score: 0.40
DE  Interaction: O15021; IntAct: EBI-2372628,EBI-3956957; Score: 0.40
DE  Interaction: Q8TD19; IntAct: EBI-2372628,EBI-1044009; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-5327611,EBI-2372628; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-2372628; Score: 0.35
GO  GO:0005642;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005886;
GO  GO:0008093;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0051959;
GO  GO:0017137;
GO  GO:0051642;
GO  GO:0072393;
GO  GO:0007018;
GO  GO:0072385;
GO  GO:0051028;
GO  GO:0034067;
GO  GO:0015031;
GO  GO:0070507;
GO  GO:0006890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKE
SQ  AFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQR
SQ  GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL
SQ  EEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTP
SQ  KKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRL
SQ  QASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQA
SQ  LTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREG
SQ  QGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKH
SQ  LQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKA
SQ  MVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLE
SQ  LDHEQTRRGRAKAAPKTKPATPSL
//
ID  Q93084;
PN  Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
GN  ATP2A3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}.
DR  UNIPROT: Q93084;
DR  UNIPROT: A8MZG0;
DR  UNIPROT: D3DTJ8;
DR  UNIPROT: O60900;
DR  UNIPROT: O60901;
DR  UNIPROT: O75501;
DR  UNIPROT: O75502;
DR  UNIPROT: Q16115;
DR  UNIPROT: Q6JHX1;
DR  UNIPROT: Q8TEX5;
DR  UNIPROT: Q8TEX6;
DR  Pfam: PF00689;
DR  Pfam: PF00690;
DR  PROSITE: PS00154;
DR  OMIM: 601929;
DR  DisGeNET: 489;
DE  Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction. {ECO:0000269|PubMed:11956212, ECO:0000269|PubMed:15028735}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-641062,EBI-1046185; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-1046185; Score: 0.35
DE  Interaction: P16333; IntAct: EBI-389883,EBI-1046185; Score: 0.40
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-1046185; Score: 0.35
DE  Interaction: P15336; IntAct: EBI-1170906,EBI-1046185; Score: 0.35
DE  Interaction: P04578; IntAct: EBI-6163496,EBI-1046185; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-1046185,EBI-1054904; Score: 0.40
DE  Interaction: P04439; IntAct: EBI-1046185,EBI-1042870; Score: 0.40
DE  Interaction: Q9HAW0; IntAct: EBI-1046185,EBI-1055224; Score: 0.40
DE  Interaction: P22626; IntAct: EBI-299649,EBI-1046185; Score: 0.40
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-1046185; Score: 0.35
GO  GO:0005623;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0031090;
GO  GO:0031095;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0005524;
GO  GO:0015085;
GO  GO:0005388;
GO  GO:0030899;
GO  GO:0008656;
GO  GO:0044325;
GO  GO:0046872;
GO  GO:0008553;
GO  GO:0006919;
GO  GO:0070588;
GO  GO:0006816;
GO  GO:1903515;
GO  GO:0006874;
GO  GO:0070059;
GO  GO:0034220;
GO  GO:1900121;
GO  GO:1903779;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEE
SQ  GEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVP
SQ  ADLRLIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA
SQ  AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLA
SQ  LGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQ
SQ  PVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMR
SQ  KEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPTSREQILAKIRDWGSGSDTLR
SQ  CLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGMLDPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLG
SQ  IFGDTEDVAGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAM
SQ  GSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTD
SQ  GLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAIGVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDN
SQ  PLFAGIDCEVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVT
SQ  PLSGRQWVVVLQISLPVILLDEALKYLSRNHMHACLYPGLLRTVSQAWSRQPLTTSWTPDHTGRNEPEVSAGNRVESPVC
SQ  TSD
//
ID  P00519;
PN  Tyrosine-protein kinase ABL1;
GN  ABL1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity). {ECO:0000250}. [Isoform IB]: Nucleus membrane; Lipid-anchor. Note=The myristoylated c-ABL protein is reported to be nuclear.
DR  UNIPROT: P00519;
DR  UNIPROT: A3KFJ3;
DR  UNIPROT: Q13869;
DR  UNIPROT: Q13870;
DR  UNIPROT: Q16133;
DR  UNIPROT: Q17R61;
DR  UNIPROT: Q45F09;
DR  PDB: 1AB2;
DR  PDB: 1ABL;
DR  PDB: 1AWO;
DR  PDB: 1BBZ;
DR  PDB: 1JU5;
DR  PDB: 1OPL;
DR  PDB: 1ZZP;
DR  PDB: 2ABL;
DR  PDB: 2E2B;
DR  PDB: 2F4J;
DR  PDB: 2FO0;
DR  PDB: 2G1T;
DR  PDB: 2G2F;
DR  PDB: 2G2H;
DR  PDB: 2G2I;
DR  PDB: 2GQG;
DR  PDB: 2HIW;
DR  PDB: 2HYY;
DR  PDB: 2HZ0;
DR  PDB: 2HZ4;
DR  PDB: 2HZI;
DR  PDB: 2O88;
DR  PDB: 2V7A;
DR  PDB: 3CS9;
DR  PDB: 3EG0;
DR  PDB: 3EG1;
DR  PDB: 3EG2;
DR  PDB: 3EG3;
DR  PDB: 3EGU;
DR  PDB: 3K2M;
DR  PDB: 3PYY;
DR  PDB: 3QRI;
DR  PDB: 3QRJ;
DR  PDB: 3QRK;
DR  PDB: 3T04;
DR  PDB: 3UE4;
DR  PDB: 3UYO;
DR  PDB: 4J9B;
DR  PDB: 4J9C;
DR  PDB: 4J9D;
DR  PDB: 4J9E;
DR  PDB: 4J9F;
DR  PDB: 4J9G;
DR  PDB: 4J9H;
DR  PDB: 4J9I;
DR  PDB: 4JJB;
DR  PDB: 4JJC;
DR  PDB: 4JJD;
DR  PDB: 4TWP;
DR  PDB: 4WA9;
DR  PDB: 4XEY;
DR  PDB: 4YC8;
DR  PDB: 4ZOG;
DR  PDB: 5DC0;
DR  PDB: 5DC4;
DR  PDB: 5DC9;
DR  PDB: 5HU9;
DR  PDB: 5MO4;
DR  PDB: 5NP2;
DR  PDB: 5OAZ;
DR  PDB: 6AMV;
DR  PDB: 6AMW;
DR  PDB: 6BL8;
DR  PDB: 6NPE;
DR  PDB: 6NPU;
DR  PDB: 6NPV;
DR  Pfam: PF08919;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DR  OMIM: 189980;
DR  OMIM: 608232;
DR  OMIM: 617602;
DR  DisGeNET: 25;
DE  Function: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250|UniProtKB:P00520, ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.
DE  Disease: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T- lymphoid cells, but not marrow fibroblasts. Note=The gene represented in this entry is involved in disease pathogenesis. Note=A chromosomal aberration involving ABL1 has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). Congenital heart defects and skeletal malformations syndrome (CHDSKM) [MIM:617602]: An autosomal dominant disorder characterized by congenital heart disease with atrial and ventricular septal defects, variable skeletal abnormalities, and failure to thrive. Skeletal defects include pectus excavatum, scoliosis, and finger contractures. Some patient exhibit joint laxity. {ECO:0000269|PubMed:28288113}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P06241; IntAct: EBI-375543,EBI-515315; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-375543,EBI-401755; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-375543,EBI-389883; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-375543,EBI-79464; Score: 0.40
DE  Interaction: P19174; IntAct: EBI-375543,EBI-79387; Score: 0.40
DE  Interaction: O43900; IntAct: EBI-375543,EBI-1751761; Score: 0.40
DE  Interaction: Q9HCM9; IntAct: EBI-375543,EBI-739510; Score: 0.40
DE  Interaction: Q9Y697; IntAct: EBI-375543,EBI-1751791; Score: 0.40
DE  Interaction: Q92918; IntAct: EBI-375543,EBI-881; Score: 0.57
DE  Interaction: P78345; IntAct: EBI-375543,EBI-366493; Score: 0.40
DE  Interaction: Q8NFP9; IntAct: EBI-375543,EBI-723014; Score: 0.40
DE  Interaction: O43390; IntAct: EBI-375543,EBI-713419; Score: 0.40
DE  Interaction: O00254; IntAct: EBI-375543,EBI-1751853; Score: 0.40
DE  Interaction: Q9Y5Y3; IntAct: EBI-375543,EBI-1751869; Score: 0.40
DE  Interaction: Q9UL51; IntAct: EBI-375543,EBI-1751885; Score: 0.40
DE  Interaction: P78357; IntAct: EBI-375543,EBI-1751903; Score: 0.40
DE  Interaction: Q96NS5; IntAct: EBI-375543,EBI-1751918; Score: 0.40
DE  Interaction: Q07890; IntAct: EBI-375543,EBI-298181; Score: 0.40
DE  Interaction: O94856; IntAct: EBI-375543,EBI-1751948; Score: 0.40
DE  Interaction: Q9NZV5; IntAct: EBI-375543,EBI-1751965; Score: 0.40
DE  Interaction: P49450; IntAct: EBI-375543,EBI-1751979; Score: 0.40
DE  Interaction: Q92874; IntAct: EBI-375543,EBI-1751995; Score: 0.40
DE  Interaction: Q7Z408; IntAct: EBI-375543,EBI-1957312; Score: 0.40
DE  Interaction: P98161; IntAct: EBI-375543,EBI-1752013; Score: 0.40
DE  Interaction: P43699; IntAct: EBI-1391923,EBI-375543; Score: 0.40
DE  Interaction: P50570; IntAct: EBI-375543,EBI-346547; Score: 0.40
DE  Interaction: Q96GP6; IntAct: EBI-375543,EBI-1752088; Score: 0.40
DE  Interaction: Q14315; IntAct: EBI-375543,EBI-489954; Score: 0.40
DE  Interaction: P31273; IntAct: EBI-375543,EBI-1752118; Score: 0.40
DE  Interaction: Q92664; IntAct: EBI-375543,EBI-1752104; Score: 0.40
DE  Interaction: Q9UJV9; IntAct: EBI-375543,EBI-1046350; Score: 0.40
DE  Interaction: O43493; IntAct: EBI-375543,EBI-1752146; Score: 0.40
DE  Interaction: Q15427; IntAct: EBI-375543,EBI-348469; Score: 0.40
DE  Interaction: Q12979; IntAct: EBI-375543,EBI-489922; Score: 0.40
DE  Interaction: Q13023; IntAct: EBI-375543,EBI-1056102; Score: 0.40
DE  Interaction: P15586; IntAct: EBI-375543,EBI-1752200; Score: 0.40
DE  Interaction: P23760; IntAct: EBI-375543,EBI-1167564; Score: 0.40
DE  Interaction: Q9UIF9; IntAct: EBI-375543,EBI-934890; Score: 0.40
DE  Interaction: Q9UM47; IntAct: EBI-375543,EBI-1236377; Score: 0.40
DE  Interaction: Q13415; IntAct: EBI-375543,EBI-374847; Score: 0.40
DE  Interaction: P06865; IntAct: EBI-375543,EBI-723519; Score: 0.40
DE  Interaction: Q9H2X0; IntAct: EBI-375543,EBI-947551; Score: 0.40
DE  Interaction: P51587; IntAct: EBI-375543,EBI-79792; Score: 0.40
DE  Interaction: Q9UMN6; IntAct: EBI-375543,EBI-765774; Score: 0.40
DE  Interaction: Q12947; IntAct: EBI-375543,EBI-1752316; Score: 0.40
DE  Interaction: Q9BYB0; IntAct: EBI-375543,EBI-1752330; Score: 0.40
DE  Interaction: Q9UBS5; IntAct: EBI-375543,EBI-724156; Score: 0.40
DE  Interaction: Q8IZD9; IntAct: EBI-375543,EBI-1752361; Score: 0.40
DE  Interaction: P28340; IntAct: EBI-375543,EBI-716569; Score: 0.40
DE  Interaction: Q9NYQ7; IntAct: EBI-375543,EBI-308417; Score: 0.40
DE  Interaction: P78329; IntAct: EBI-375543,EBI-1752413; Score: 0.40
DE  Interaction: O43708; IntAct: EBI-375543,EBI-748043; Score: 0.40
DE  Interaction: Q9H5I1; IntAct: EBI-375543,EBI-723127; Score: 0.40
DE  Interaction: P46013; IntAct: EBI-375543,EBI-876367; Score: 0.40
DE  Interaction: O76039; IntAct: EBI-375543,EBI-1752465; Score: 0.40
DE  Interaction: Q14008; IntAct: EBI-375543,EBI-310585; Score: 0.40
DE  Interaction: Q13087; IntAct: EBI-375543,EBI-1752525; Score: 0.40
DE  Interaction: O14513; IntAct: EBI-375543,EBI-1752508; Score: 0.40
DE  Interaction: O95886; IntAct: EBI-375543,EBI-1752541; Score: 0.40
DE  Interaction: Q9Y5X2; IntAct: EBI-375543,EBI-1752557; Score: 0.40
DE  Interaction: P42566; IntAct: EBI-375543,EBI-396684; Score: 0.40
DE  Interaction: Q96RL7; IntAct: EBI-375543,EBI-1752583; Score: 0.40
DE  Interaction: Q9UMY4; IntAct: EBI-375543,EBI-1752602; Score: 0.40
DE  Interaction: Q9C0E4; IntAct: EBI-375543,EBI-949557; Score: 0.40
DE  Interaction: Q15036; IntAct: EBI-375543,EBI-1752620; Score: 0.40
DE  Interaction: P34820; IntAct: EBI-375543,EBI-1752660; Score: 0.40
DE  Interaction: P30260; IntAct: EBI-375543,EBI-994813; Score: 0.40
DE  Interaction: O75751; IntAct: EBI-375543,EBI-1752674; Score: 0.40
DE  Interaction: Q86UR5; IntAct: EBI-375543,EBI-1043236; Score: 0.40
DE  Interaction: Q9NZQ3; IntAct: EBI-375543,EBI-745080; Score: 0.40
DE  Interaction: P26992; IntAct: EBI-375543,EBI-743758; Score: 0.40
DE  Interaction: P50851; IntAct: EBI-375543,EBI-1052167; Score: 0.40
DE  Interaction: O76081; IntAct: EBI-375543,EBI-1052678; Score: 0.40
DE  Interaction: Q92988; IntAct: EBI-375543,EBI-1752755; Score: 0.40
DE  Interaction: Q96PC5; IntAct: EBI-375543,EBI-1050253; Score: 0.40
DE  Interaction: Q9BQ89; IntAct: EBI-375543,EBI-1752811; Score: 0.40
DE  Interaction: P20810; IntAct: EBI-375543,EBI-1268770; Score: 0.40
DE  Interaction: Q9H1R2; IntAct: EBI-375543,EBI-1752795; Score: 0.40
DE  Interaction: P02765; IntAct: EBI-375543,EBI-1223374; Score: 0.40
DE  Interaction: Q9Y3S1; IntAct: EBI-375543,EBI-948521; Score: 0.40
DE  Interaction: Q13905; IntAct: EBI-375543,EBI-976876; Score: 0.66
DE  Interaction: Q9UQ16; IntAct: EBI-375543,EBI-1111783; Score: 0.40
DE  Interaction: Q9Y5K6; IntAct: EBI-375543,EBI-298152; Score: 0.40
DE  Interaction: O15255; IntAct: EBI-375543,EBI-954396; Score: 0.40
DE  Interaction: Q8TB24; IntAct: EBI-375543,EBI-1570523; Score: 0.40
DE  Interaction: O95157; IntAct: EBI-375543,EBI-1752913; Score: 0.40
DE  Interaction: O43281; IntAct: EBI-375543,EBI-718488; Score: 0.40
DE  Interaction: O15085; IntAct: EBI-375543,EBI-311099; Score: 0.40
DE  Interaction: P08047; IntAct: EBI-375543,EBI-298336; Score: 0.40
DE  Interaction: P98164; IntAct: EBI-375543,EBI-947916; Score: 0.40
DE  Interaction: Q86SG6; IntAct: EBI-375543,EBI-1752987; Score: 0.40
DE  Interaction: Q9H0X9; IntAct: EBI-375543,EBI-1753005; Score: 0.40
DE  Interaction: Q9NQC3; IntAct: EBI-375543,EBI-715945; Score: 0.40
DE  Interaction: O60244; IntAct: EBI-375543,EBI-394489; Score: 0.40
DE  Interaction: Q9UK85; IntAct: EBI-375543,EBI-1753048; Score: 0.40
DE  Interaction: Q9BXM0; IntAct: EBI-375543,EBI-1753064; Score: 0.40
DE  Interaction: O43918; IntAct: EBI-375543,EBI-1753081; Score: 0.40
DE  Interaction: Q96AC6; IntAct: EBI-375543,EBI-724040; Score: 0.40
DE  Interaction: Q9HCQ7; IntAct: EBI-375543,EBI-1753111; Score: 0.40
DE  Interaction: O15056; IntAct: EBI-375543,EBI-310513; Score: 0.40
DE  Interaction: P32239; IntAct: EBI-375543,EBI-1753137; Score: 0.40
DE  Interaction: Q15027; IntAct: EBI-375543,EBI-751746; Score: 0.40
DE  Interaction: O14490; IntAct: EBI-375543,EBI-1753207; Score: 0.40
DE  Interaction: Q8WX92; IntAct: EBI-375543,EBI-347721; Score: 0.40
DE  Interaction: Q9NUR3; IntAct: EBI-375543,EBI-1753189; Score: 0.40
DE  Interaction: P13671; IntAct: EBI-375543,EBI-1753221; Score: 0.40
DE  Interaction: P42167; IntAct: EBI-375543,EBI-455283; Score: 0.40
DE  Interaction: Q99572; IntAct: EBI-375543,EBI-1753251; Score: 0.40
DE  Interaction: O15117; IntAct: EBI-375543,EBI-1753267; Score: 0.40
DE  Interaction: Q14767; IntAct: EBI-375543,EBI-1546118; Score: 0.40
DE  Interaction: Q9NQ76; IntAct: EBI-375543,EBI-1753293; Score: 0.40
DE  Interaction: Q9Y2J2; IntAct: EBI-375543,EBI-310986; Score: 0.40
DE  Interaction: O60493; IntAct: EBI-375543,EBI-727209; Score: 0.40
DE  Interaction: Q9UHL9; IntAct: EBI-375543,EBI-372530; Score: 0.40
DE  Interaction: Q05193; IntAct: EBI-375543,EBI-713135; Score: 0.40
DE  Interaction: Q9ULH1; IntAct: EBI-375543,EBI-346622; Score: 0.40
DE  Interaction: Q9UN86; IntAct: EBI-375543,EBI-1044298; Score: 0.40
DE  Interaction: P49916; IntAct: EBI-375543,EBI-1753381; Score: 0.40
DE  Interaction: Q9P1A6; IntAct: EBI-375543,EBI-1753397; Score: 0.40
DE  Interaction: Q9Y2H0; IntAct: EBI-375543,EBI-722139; Score: 0.40
DE  Interaction: Q9BZM3; IntAct: EBI-375543,EBI-1753426; Score: 0.40
DE  Interaction: Q9UJT2; IntAct: EBI-375543,EBI-852101; Score: 0.40
DE  Interaction: P12018; IntAct: EBI-375543,EBI-1753454; Score: 0.40
DE  Interaction: Q9ULD4; IntAct: EBI-375543,EBI-1753470; Score: 0.40
DE  Interaction: Q9Y3Q4; IntAct: EBI-375543,EBI-1753521; Score: 0.40
DE  Interaction: Q9NRJ4; IntAct: EBI-375543,EBI-1753487; Score: 0.40
DE  Interaction: O60721; IntAct: EBI-375543,EBI-1753504; Score: 0.40
DE  Interaction: O75326; IntAct: EBI-375543,EBI-1753538; Score: 0.40
DE  Interaction: Q08209; IntAct: EBI-375543,EBI-352922; Score: 0.40
DE  Interaction: Q14999; IntAct: EBI-375543,EBI-308606; Score: 0.40
DE  Interaction: Q9BWW9; IntAct: EBI-375543,EBI-1753592; Score: 0.40
DE  Interaction: Q8TAS1; IntAct: EBI-375543,EBI-1753608; Score: 0.40
DE  Interaction: P21333; IntAct: EBI-375543,EBI-350432; Score: 0.40
DE  Interaction: P29074; IntAct: EBI-375543,EBI-710431; Score: 0.40
DE  Interaction: Q9UN72; IntAct: EBI-375543,EBI-1753660; Score: 0.40
DE  Interaction: P52803; IntAct: EBI-375543,EBI-1753674; Score: 0.40
DE  Interaction: P20774; IntAct: EBI-375543,EBI-1753690; Score: 0.40
DE  Interaction: Q99259; IntAct: EBI-375543,EBI-743184; Score: 0.40
DE  Interaction: P46108; IntAct: EBI-375543,EBI-886; Score: 0.67
DE  Interaction: P12931; IntAct: EBI-375543,EBI-621482; Score: 0.59
DE  Interaction: P31946-2; IntAct: EBI-10770173,EBI-375543; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-359832,EBI-375543; Score: 0.74
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-375543; Score: 0.64
DE  Interaction: Q9BY11; IntAct: EBI-375543,EBI-721769; Score: 0.37
DE  Interaction: Q03468; IntAct: EBI-375543,EBI-295284; Score: 0.66
DE  Interaction: P10275; IntAct: EBI-375543,EBI-608057; Score: 0.44
DE  Interaction: P10721; IntAct: EBI-375543,EBI-1379503; Score: 0.44
DE  Interaction: P14618-1; IntAct: EBI-375543,EBI-4304679; Score: 0.44
DE  Interaction: Q38SD2; IntAct: EBI-375543,EBI-1050422; Score: 0.59
DE  Interaction: Q5S007; IntAct: EBI-375543,EBI-5323863; Score: 0.44
DE  Interaction: P00533; IntAct: EBI-375543,EBI-297353; Score: 0.69
DE  Interaction: Q64010-2; IntAct: EBI-2642543,EBI-375543; Score: 0.35
DE  Interaction: P97465; IntAct: EBI-914917,EBI-375543; Score: 0.35
DE  Interaction: Q8BTZ4; IntAct: EBI-10976824,EBI-375543; Score: 0.35
DE  Interaction: Q8BL66; IntAct: EBI-647872,EBI-375543; Score: 0.35
DE  Interaction: Q1H9T6; IntAct: EBI-11104272,EBI-375543; Score: 0.35
DE  Interaction: Q15637; IntAct: EBI-375543,EBI-744603; Score: 0.37
DE  Interaction: P53999; IntAct: EBI-375543,EBI-998260; Score: 0.35
DE  Interaction: P61604; IntAct: EBI-375543,EBI-711483; Score: 0.35
DE  Interaction: P26641; IntAct: EBI-375543,EBI-351467; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-375543,EBI-356498; Score: 0.53
DE  Interaction: Q9Y295; IntAct: EBI-375543,EBI-719554; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-375543,EBI-739737; Score: 0.35
DE  Interaction: P63220; IntAct: EBI-375543,EBI-714051; Score: 0.35
DE  Interaction: Q12906; IntAct: EBI-375543,EBI-78756; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-375543,EBI-359815; Score: 0.53
DE  Interaction: P52272; IntAct: EBI-375543,EBI-486809; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-375543,EBI-400434; Score: 0.35
DE  Interaction: Q9BY44; IntAct: EBI-375543,EBI-1776615; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-375543,EBI-359854; Score: 0.35
DE  Interaction: P05386; IntAct: EBI-375543,EBI-354582; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-375543,EBI-351962; Score: 0.35
DE  Interaction: P12956; IntAct: EBI-375543,EBI-353208; Score: 0.35
DE  Interaction: Q96AG4; IntAct: EBI-375543,EBI-358888; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-375543,EBI-702400; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-375543,EBI-347088; Score: 0.62
DE  Interaction: P53355; IntAct: EBI-375543,EBI-358616; Score: 0.44
DE  Interaction: P08238; IntAct: EBI-375543,EBI-352572; Score: 0.40
DE  Interaction: P78362; IntAct: EBI-375543,EBI-593303; Score: 0.44
DE  Interaction: Q63767; IntAct: EBI-375543,EBI-1176801; Score: 0.44
DE  Interaction: Q13671; IntAct: EBI-375543,EBI-366017; Score: 0.61
DE  Interaction: Q13315; IntAct: EBI-495465,EBI-375543; Score: 0.70
DE  Interaction: P54274-2; IntAct: EBI-375543,EBI-711018; Score: 0.40
DE  Interaction: Q9BX66; IntAct: EBI-375543,EBI-433642; Score: 0.52
DE  Interaction: P31947; IntAct: EBI-375543,EBI-476295; Score: 0.50
DE  Interaction: Q8CBW3; IntAct: EBI-375543,EBI-375511; Score: 0.40
DE  Interaction: Q8IZP0; IntAct: EBI-375543,EBI-375446; Score: 0.90
GO  GO:0015629;
GO  GO:0005623;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0000405;
GO  GO:0003677;
GO  GO:0046875;
GO  GO:0000400;
GO  GO:0016301;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0051019;
GO  GO:0038191;
GO  GO:0004515;
GO  GO:0004715;
GO  GO:0001784;
GO  GO:0070064;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0005080;
GO  GO:0004713;
GO  GO:1990837;
GO  GO:0042169;
GO  GO:0017124;
GO  GO:0019905;
GO  GO:0003713;
GO  GO:0030036;
GO  GO:0090135;
GO  GO:0050798;
GO  GO:1990051;
GO  GO:0046632;
GO  GO:0006914;
GO  GO:0002322;
GO  GO:0050853;
GO  GO:0001922;
GO  GO:0060020;
GO  GO:0072358;
GO  GO:0007050;
GO  GO:0006464;
GO  GO:0006974;
GO  GO:1903351;
GO  GO:0070301;
GO  GO:0071222;
GO  GO:0034599;
GO  GO:0021587;
GO  GO:0048668;
GO  GO:0071103;
GO  GO:0006975;
GO  GO:0006897;
GO  GO:0043542;
GO  GO:0007173;
GO  GO:0045184;
GO  GO:0038096;
GO  GO:0007229;
GO  GO:0008630;
GO  GO:0030035;
GO  GO:0006298;
GO  GO:0051882;
GO  GO:0000278;
GO  GO:0030514;
GO  GO:0022408;
GO  GO:2000773;
GO  GO:2000352;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:1900272;
GO  GO:0045930;
GO  GO:1900275;
GO  GO:0071901;
GO  GO:0051444;
GO  GO:0001843;
GO  GO:0060563;
GO  GO:0050885;
GO  GO:0038189;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0035791;
GO  GO:1905555;
GO  GO:2000251;
GO  GO:1904531;
GO  GO:0043065;
GO  GO:0090050;
GO  GO:0007204;
GO  GO:0010595;
GO  GO:0070374;
GO  GO:0051894;
GO  GO:0043123;
GO  GO:1902715;
GO  GO:1900042;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:0051149;
GO  GO:1901216;
GO  GO:0033690;
GO  GO:0051353;
GO  GO:0050731;
GO  GO:0001934;
GO  GO:0051281;
GO  GO:0051496;
GO  GO:1900026;
GO  GO:0045944;
GO  GO:2000096;
GO  GO:0009791;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0032956;
GO  GO:2000249;
GO  GO:0042981;
GO  GO:0010506;
GO  GO:0030516;
GO  GO:0032489;
GO  GO:0030155;
GO  GO:2000145;
GO  GO:0030100;
GO  GO:1903053;
GO  GO:1902036;
GO  GO:0031113;
GO  GO:1905244;
GO  GO:2001020;
GO  GO:0045580;
GO  GO:0006355;
GO  GO:0006979;
GO  GO:0042770;
GO  GO:0048536;
GO  GO:0034446;
GO  GO:0050852;
GO  GO:0048538;
GO  GO:0002333;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTL
SQ  SITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQ
SQ  RSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERT
SQ  DITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY
SQ  GNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAK
SQ  FPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNP
SQ  SDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESD
SQ  PLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRD
SQ  ISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSAS
SQ  CVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKD
SQ  IMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKH
SQ  SSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVL
SQ  PATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALC
SQ  LAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSS
SQ  VKEISDIVQR
//
ID  P20291;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  Alox5ap;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P20291;
DR  UNIPROT: Q5RJL3;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0071277;
GO  GO:0019370;
GO  GO:0002540;
GO  GO:0019372;
GO  GO:0002675;
GO  GO:0070207;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAVGNVVLLAIVTLISVVQNAFFAHKVELESKAQSGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNHYLIFFFGSDFENYIRTITTTISPLLLI
SQ  P
//
ID  Q63850;
PN  Nuclear pore glycoprotein p62;
GN  Nup62;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle. {ECO:0000250|UniProtKB:P37198}.
DR  UNIPROT: Q63850;
DR  UNIPROT: Q99JN7;
DR  Pfam: PF05064;
DE  Function: Essential component of the nuclear pore complex. The N- terminal is probably involved in nucleocytoplasmic transport. The C- terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown. {ECO:0000250|UniProtKB:P37198}.
DE  Reference Proteome: Yes;
GO  GO:0005642;
GO  GO:0005623;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0090543;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0032991;
GO  GO:1990904;
GO  GO:0000922;
GO  GO:0030544;
GO  GO:0051879;
GO  GO:0019894;
GO  GO:0005543;
GO  GO:0044877;
GO  GO:0051425;
GO  GO:0030159;
GO  GO:0042169;
GO  GO:0017056;
GO  GO:0046966;
GO  GO:0043130;
GO  GO:0007569;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007166;
GO  GO:0098534;
GO  GO:0007098;
GO  GO:0000278;
GO  GO:0007100;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0042059;
GO  GO:0043407;
GO  GO:0043069;
GO  GO:0046580;
GO  GO:0046601;
GO  GO:0043123;
GO  GO:1903438;
GO  GO:0045840;
GO  GO:1904781;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0060236;
GO  GO:0042306;
GO  GO:0006405;
GO  GO:0007283;
GO  GO:0006351;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGT
SQ  TPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSF
SQ  TSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLS
SQ  LPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPAS
SQ  STAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFI
SQ  LSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICK
SQ  ILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD
//
ID  Q9NR21;
PN  Protein mono-ADP-ribosyltransferase PARP11;
GN  PARP11;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25673562}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000269|PubMed:25673562}.
DR  UNIPROT: Q9NR21;
DR  UNIPROT: B4DRQ0;
DR  UNIPROT: F8WBZ7;
DR  UNIPROT: Q68DS1;
DR  UNIPROT: Q8N5Y9;
DR  PDB: 2DK6;
DR  Pfam: PF00644;
DR  Pfam: PF02825;
DR  PROSITE: PS51059;
DR  PROSITE: PS50918;
DR  OMIM: 616706;
DE  Function: Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins (PubMed:25043379, PubMed:25673562). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q8CFF0, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25673562}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15645; IntAct: EBI-358993,EBI-748917; Score: 0.49
DE  Interaction: Q8TEB1; IntAct: EBI-748917,EBI-2213388; Score: 0.40
DE  Interaction: Q9Y508; IntAct: EBI-748917,EBI-723587; Score: 0.40
DE  Interaction: P61626; IntAct: EBI-748917,EBI-355360; Score: 0.40
DE  Interaction: Q99750; IntAct: EBI-724076,EBI-748917; Score: 0.37
DE  Interaction: Q969Y2; IntAct: EBI-740290,EBI-748917; Score: 0.37
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003950;
GO  GO:1990404;
GO  GO:0030154;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0070213;
GO  GO:0140289;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWEANPEMFHKAEELFSKTTNNEVDDMDTSDTQWGWFYLAECGKWHMFQPDTNSQCSVSSEDIEKSFKTNPCGSISFTTS
SQ  KFSYKIDFAEMKQMNLTTGKQRLIKRAPFSISAFSYICENEAIPMPPHWENVNTQVPYQLIPLHNQTHEYNEVANLFGKT
SQ  MDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGIHGAVFGKGTYFARD
SQ  AAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKI
SQ  FVVFDANQIYPEYLIDFH
//
ID  O95476;
PN  CTD nuclear envelope phosphatase 1;
GN  CTDNEP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: O95476;
DR  UNIPROT: D3DTN7;
DR  UNIPROT: Q96GQ9;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DR  OMIM: 610684;
DE  Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling. {ECO:0000269|PubMed:17420445, ECO:0000269|PubMed:22134922}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y5M8; IntAct: EBI-355393,EBI-5323433; Score: 0.35
DE  Interaction: Q9UHD9; IntAct: EBI-947187,EBI-5323433; Score: 0.56
DE  Interaction: O00624-2; IntAct: EBI-21654602,EBI-5323433; Score: 0.35
DE  Interaction: Q6UX71; IntAct: EBI-6115410,EBI-5323433; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-2872118,EBI-5323433; Score: 0.35
DE  Interaction: O95897; IntAct: EBI-721741,EBI-5323433; Score: 0.35
DE  Interaction: P81408-2; IntAct: EBI-21516401,EBI-5323433; Score: 0.35
DE  Interaction: O60602; IntAct: EBI-3505951,EBI-5323433; Score: 0.35
DE  Interaction: P01911; IntAct: EBI-1033104,EBI-5323433; Score: 0.35
DE  Interaction: Q8WV48; IntAct: EBI-947033,EBI-5323433; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-641237,EBI-5323433; Score: 0.35
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0007276;
GO  GO:0007498;
GO  GO:0007077;
GO  GO:0006998;
GO  GO:0090263;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQH
SQ  CTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  B0LSW3;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  PAFAH1B1;
OS  9685;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: B0LSW3;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. {ECO:0000250|UniProtKB:P43034, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0000235;
GO  GO:1904115;
GO  GO:0005623;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0005813;
GO  GO:0005881;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0031514;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0045202;
GO  GO:0070840;
GO  GO:0042802;
GO  GO:0051010;
GO  GO:0051219;
GO  GO:0001675;
GO  GO:0030036;
GO  GO:0008344;
GO  GO:0001667;
GO  GO:0060117;
GO  GO:0048854;
GO  GO:0051301;
GO  GO:0007268;
GO  GO:0090102;
GO  GO:0021540;
GO  GO:0043622;
GO  GO:0000132;
GO  GO:0042249;
GO  GO:0007281;
GO  GO:0021766;
GO  GO:0021819;
GO  GO:0007611;
GO  GO:0016042;
GO  GO:0051661;
GO  GO:0090176;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0046329;
GO  GO:0007405;
GO  GO:0050885;
GO  GO:0001764;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0036035;
GO  GO:0001961;
GO  GO:0061003;
GO  GO:0040019;
GO  GO:0009306;
GO  GO:0043087;
GO  GO:0070507;
GO  GO:2000574;
GO  GO:0008090;
GO  GO:0019226;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q0WPU1;
PN  Myosin-15;
GN  XI;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}. Nucleus membrane {ECO:0000269|PubMed:23973298}. Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or organelles. Nucleus membrane localization is dependent of the WIT2 association. {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}.
DR  UNIPROT: Q0WPU1;
DR  UNIPROT: Q9SMY9;
DR  Pfam: PF01843;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF02736;
DR  PROSITE: PS51126;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosin heavy chain that is required for the cell cycle- regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks and mitochondria. Plays a role in nuclear shape determination. Drives nuclear movement along actin filaments (PubMed:23973298). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656, ECO:0000269|PubMed:23973298, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016459;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0007015;
GO  GO:0030048;
GO  GO:0007097;
GO  GO:2000769;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRNCLPMELNLRKGDKVWVEDKDLAWIAADVLDSFDNKLHVETSTGKKVFVSPEKLFRRDPDDEEHNGVDDMTKLTYLHE
SQ  AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS
SQ  GESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR
SQ  TYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ
SQ  EGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTS
SQ  RDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRK
SQ  EEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTY
SQ  QTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNS
SQ  LNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSKLGLGNYQLGRT
SQ  KVFLRAGQIGILDSRRAEVLDASARLIQRRLRTFVTHQNFISARASAISIQAYCRGCLSRNAYATRRNAAAAVLVQKHVR
SQ  RWLSRCAFVKLVSAAIVLQSCIRADSTRLKFSHQKEHRAASLIQAHWRIHKFRSAFRHRQSSIIAIQCRWRQKLAKREFR
SQ  KLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARLATINECNKNAVLE
SQ  KQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLE
SQ  EKLSHLENENQVLMQKTLITSPERIGQILGEKHSSAVVPAQNDRRSVFETPTPSKHIMPFSHSLSESRRSKLTAERNLEN
SQ  YELLSRCIKENLGFNDDKPLAACVIYKCLLHWRAFESESTAIFNIIIEGINEALKGGDENGVLPYWLSNASALLCLLQRN
SQ  LRSNSFLNASAQRSGRAAYGVKSPFKLHGPDDGASHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPLLGSCIQAP
SQ  KASRGIAGKSRSPGGVPQQSPSSQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNG
SQ  EYVKSGISELEKWIANAKEEFAGTSWHELNYIRQAVGFLVIHQKKKKSLDEIRQDLCPVLTIRQIYRISTMYWDDKYGTQ
SQ  SVSSEVVSQMRVLVDKDNQKQTSNSFLLDDDMSIPFSAEDIDKAIPVLDPSEIEPPKFVSEYTCAQSLVKKPSIASTSKQ
SQ  II
//
ID  Q9NZM1;
PN  Myoferlin;
GN  MYOF;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane; Single-pass type II membrane protein. Nucleus membrane; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Note=Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels (By similarity). Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures. {ECO:0000250}.
DR  UNIPROT: Q9NZM1;
DR  UNIPROT: B3KQN5;
DR  UNIPROT: Q5VWW2;
DR  UNIPROT: Q5VWW3;
DR  UNIPROT: Q5VWW4;
DR  UNIPROT: Q5VWW5;
DR  UNIPROT: Q7Z642;
DR  UNIPROT: Q8IWH0;
DR  UNIPROT: Q9HBU3;
DR  UNIPROT: Q9NZM0;
DR  UNIPROT: Q9ULL3;
DR  UNIPROT: Q9Y4U4;
DR  PDB: 2DMH;
DR  PDB: 2K2O;
DR  PDB: 6EEL;
DR  Pfam: PF00168;
DR  Pfam: PF08165;
DR  Pfam: PF08150;
DR  Pfam: PF08151;
DR  Pfam: PF16165;
DR  PROSITE: PS50004;
DR  OMIM: 604603;
DR  DisGeNET: 26509;
DE  Function: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1994363; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-1994363; Score: 0.35
DE  Interaction: P09613; IntAct: EBI-21497244,EBI-1994363; Score: 0.35
DE  Interaction: P49716; IntAct: EBI-7962058,EBI-1994363; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1994363; Score: 0.35
DE  Interaction: P38606; IntAct: EBI-1054757,EBI-1994363; Score: 0.35
GO  GO:0005901;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005543;
GO  GO:0008015;
GO  GO:0034605;
GO  GO:0006071;
GO  GO:0061025;
GO  GO:0006936;
GO  GO:0048747;
GO  GO:0007520;
GO  GO:0007009;
GO  GO:0001778;
GO  GO:0030947;
GO  GO:0033292;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRVIVESASNIPKTKFGKPDPIVSVIFKDEKKKTKKVDNELNPVWNEILEFDLRGIPLDFSSSLGIIVKDFETIGQNKL
SQ  IGTATVALKDLTGDQSRSLPYKLISLLNEKGQDTGATIDLVIGYDPPSAPHPNDLSGPSVPGMGGDGEEDEGDEDRLDNA
SQ  VRGPGPKGPVGTVSEAQLARRLTKVKNSRRMLSNKPQDFQIRVRVIEGRQLSGNNIRPVVKVHVCGQTHRTRIKRGNNPF
SQ  FDELFFYNVNMTPSELMDEIISIRVYNSHSLRADCLMGEFKIDVGFVYDEPGHAVMRKWLLLNDPEDTSSGSKGYMKVSM
SQ  FVLGTGDEPPPERRDRDNDSDDVESNLLLPAGIALRWVTFLLKIYRAEDIPQMDDAFSQTVKEIFGGNADKKNLVDPFVE
SQ  VSFAGKKVCTNIIEKNANPEWNQVVNLQIKFPSVCEKIKLTIYDWDRLTKNDVVGTTYLHLSKIAASGGEVEDFSSSGTG
SQ  AASYTVNTGETEVGFVPTFGPCYLNLYGSPREYTGFPDPYDELNTGKGEGVAYRGRILVELATFLEKTPPDKKLEPISND
SQ  DLLVVEKYQRRRKYSLSAVFHSATMLQDVGEAIQFEVSIGNYGNKFDTTCKPLASTTQYSRAVFDGNYYYYLPWAHTKPV
SQ  VTLTSYWEDISHRLDAVNTLLAMAERLQTNIEALKSGIQGKIPANQLAELWLKLIDEVIEDTRYTLPLTEGKANVTVLDT
SQ  QIRKLRSRSLSQIHEAAVRMRSEATDVKSTLAEIEDWLDKLMQLTEEPQNSMPDIIIWMIRGEKRLAYARIPAHQVLYST
SQ  SGENASGKYCGKTQTIFLKYPQEKNNGPKVPVELRVNIWLGLSAVEKKFNSFAEGTFTVFAEMYENQALMFGKWGTSGLV
SQ  GRHKFSDVTGKIKLKREFFLPPKGWEWEGEWIVDPERSLLTEADAGHTEFTDEVYQNESRYPGGDWKPAEDTYTDANGDK
SQ  AASPSELTCPPGWEWEDDAWSYDINRAVDEKGWEYGITIPPDHKPKSWVAAEKMYHTHRRRRLVRKRKKDLTQTASSTAR
SQ  AMEELQDQEGWEYASLIGWKFHWKQRSSDTFRRRRWRRKMAPSETHGAAAIFKLEGALGADTTEDGDEKSLEKQKHSATT
SQ  VFGANTPIVSCNFDRVYIYHLRCYVYQARNLLALDKDSFSDPYAHICFLHRSKTTEIIHSTLNPTWDQTIIFDEVEIYGE
SQ  PQTVLQNPPKVIMELFDNDQVGKDEFLGRSIFSPVVKLNSEMDITPKLLWHPVMNGDKACGDVLVTAELILRGKDGSNLP
SQ  ILPPQRAPNLYMVPQGIRPVVQLTAIEILAWGLRNMKNFQMASITSPSLVVECGGERVESVVIKNLKKTPNFPSSVLFMK
SQ  VFLPKEELYMPPLVIKVIDHRQFGRKPVVGQCTIERLDRFRCDPYAGKEDIVPQLKASLLSAPPCRDIVIEMEDTKPLLA
SQ  SKLTEKEEEIVDWWSKFYASSGEHEKCGQYIQKGYSKLKIYNCELENVAEFEGLTDFSDTFKLYRGKSDENEDPSVVGEF
SQ  KGSFRIYPLPDDPSVPAPPRQFRELPDSVPQECTVRIYIVRGLELQPQDNNGLCDPYIKITLGKKVIEDRDHYIPNTLNP
SQ  VFGRMYELSCYLPQEKDLKISVYDYDTFTRDEKVGETIIDLENRFLSRFGSHCGIPEEYCVSGVNTWRDQLRPTQLLQNV
SQ  ARFKGFPQPILSEDGSRIRYGGRDYSLDEFEANKILHQHLGAPEERLALHILRTQGLVPEHVETRTLHSTFQPNISQGKL
SQ  QMWVDVFPKSLGPPGPPFNITPRKAKKYYLRVIIWNTKDVILDEKSITGEEMSDIYVKGWIPGNEENKQKTDVHYRSLDG
SQ  EGNFNWRFVFPFDYLPAEQLCIVAKKEHFWSIDQTEFRIPPRLIIQIWDNDKFSLDDYLGFLELDLRHTIIPAKSPEKCR
SQ  LDMIPDLKAMNPLKAKTASLFEQKSMKGWWPCYAEKDGARVMAGKVEMTLEILNEKEADERPAGKGRDEPNMNPKLDLPN
SQ  RPETSFLWFTNPCKTMKFIVWRRFKWVIIGLLFLLILLLFVAVLLYSLPNYLSMKIVKPNV
//
ID  Q06148;
PN  Non-homologous end-joining protein 1;
GN  NEJ1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: Q06148;
DR  UNIPROT: D6VYR3;
DR  UNIPROT: Q0P6Z6;
DR  UNIPROT: Q0P6Z7;
DR  UNIPROT: Q0P707;
DR  Pfam: PF09302;
DE  Function: Involved in non-homologous end joining (NHEJ). Facilitates the transport of LIF1 into the nucleus, where it can interact with DNA ligase DNL4 to repair double-strand breaks (DSB). Mediates mating-type regulation of NHEJ. Prevents chromosome circularisation by NHEJ in absence of telomerase. {ECO:0000269|PubMed:11676923, ECO:0000269|PubMed:11701889, ECO:0000269|PubMed:11711435, ECO:0000269|PubMed:11740566, ECO:0000269|PubMed:12399380, ECO:0000269|PubMed:12769859}.
DE  Reference Proteome: Yes;
DE  Interaction: P10592; IntAct: EBI-34047,EBI-8603; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-34047,EBI-8627; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-34047; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-34047,EBI-17244; Score: 0.35
DE  Interaction: P38316; IntAct: EBI-34047,EBI-2692; Score: 0.37
GO  GO:0005737;
GO  GO:0032807;
GO  GO:0016021;
GO  GO:0070419;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0045027;
GO  GO:0006303;
GO  GO:0045002;
GO  GO:0035825;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSELKGQQLSDAEWCVKKINGEGNCLLLFLPMSSPTTIVMIVLVSLERLVPYVFKLSQTQLSQQCQSQGFTDSISLNLI
SQ  KLKLMDILQAPQEINQIGLVDSNLVFSFDVSADITVSINSVPSHVTKDMFYMILQSLCMLLLKLVNLSTQYHYVQRDILN
SQ  EKQKCLDFLLISLRDLDGGSKVISQWAPENSKNYESLQQCTDDDIIKKLLHKGKFQHQEFLADSLKTLLSLRNKFQDVSR
SQ  FEESGELNKKERVRFPAVNHFYNDDFELQADPTNEARPNSRGKIKPKTDFKPKSRESSTSSQLRLENFSESEATPEKTKS
SQ  SSSLVEEYPQKKRKFGKVRIKN
//
ID  Q9CAF4;
PN  Nuclear pore complex protein NUP1;
GN  NUP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:25081480}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:21189294}. Cytoplasm, cytosol {ECO:0000269|PubMed:21189294}. Note=Interacts dynamically with the NPC and localizes to the cytosolic pool following nuclear envelope breakdown during mitosis. {ECO:0000269|PubMed:21189294}.
DR  UNIPROT: Q9CAF4;
DR  UNIPROT: Q9LPN4;
DE  Function: Nucleoporin required for nuclear mRNA export. Functions as an adapter and/or regulator molecule in the periphery of the nuclear pore complex (NPC). May interact with importin proteins and mediate active nucleocytoplasmic transport through the NPC. Involved in regulation of nuclear morphology. {ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:21818409, ECO:0000305|PubMed:21189294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GWE6; IntAct: EBI-2619706,EBI-2619711; Score: 0.49
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0071763;
GO  GO:0006997;
GO  GO:0016973;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASAARGESSNPYGGGLGTGGKFRKPTARRSQKTPYDRPTTSVRNAGLGGGDVRGGGWLSKLVDPAQRLITYSAQRLFGS
SQ  LSRKRLGSGETPLQSPEQQKQLPERGVNQETKVGHKEDVSNLSMKNGLIRMEDTNASVDPPKDGFTDLEKILQGKTFTRS
SQ  EVDRLTTLLRSKAADSSTMNEEQRNEVGMVVRHPPSHERDRTHPDNGSMNTLVSTPPGSLRTLDECIASPAQLAKAYMGS
SQ  RPSEVTPSMLGLRGQAGREDSVFLNRTPFPQKSPTMSLVTKPSGQRPLENGFVTPRSRGRSAVYSMARTPYSRPQSSVKI
SQ  GSLFQASPSKWEESLPSGSRQGFQSGLKRRSSVLDNDIGSVGPVRRIRQKSNLSSRSLALPVSESPLSVRANGGEKTTHT
SQ  SKDSAEDIPGSSFNLVPTKSSEMASKILQQLDKLVSTREKSPSKLSPSMLRGPALKSLQNVEAPKFLGNLPEKKANSPDS
SQ  SYQKQEISRESVSREVLAQSEKTGDAVDGTSKTGSSKDQDMRGKGVYMPLTNSLEEHPPKKRSFRMSAHEDFLELDDDLG
SQ  AASTPCEVAEKQNAFEVEKSHISMPIGEKPLTPSEAMPSTSYISNGDASQGTSNGSLETERNKFVAFPIEAVQQSNMASE
SQ  PTSKFIQGTEKSSISSGKPTSEEKRIPLEEPKKPAAVFPNISFSPPATGLLNQNSGASADIKLEKTSSTAFGVSEAWAKP
SQ  TESKKTFSNSASGAESSTSAAPTLNGSIFSAGANAVTPPPSNGSLTSSPSFPPSISNIPSDNSVGDMPSTVQSFAATHNS
SQ  SSIFGKLPTSNDSNSQSTSASPLSSTSPFKFGQPAAPFSAPAVSESSGQISKETEVKNATFGNTSTFKFGGMASADQSTG
SQ  IVFGAKSAENKSRPGFVFGSSSVVGGSTLNPSTAAASAPESSGSLIFGVTSSSTPGTETSKISASSAATNTGNSVFGTSS
SQ  FAFTSSGSSMVGGVSASTGSSVFGFNAVSSASATSSQSQASNLFGAGNAQTGNTGSGTTTSTQSIPFQFGSSPSAPSFGL
SQ  SGNSSLASNSSPFGFSKSEPAVFTSVSTPQLSSTNSSASSSSTMSSPLFGTSWQAPNSSPNSGPVFSSSFTTSSTPTTFS
SQ  FGGSSAATVSSTTTPIFGASTNNTPSPSPIFGFGSTPPTTPQQPVFGNSGTPSQSLFGNSTPGFAFGAPNNGNGINNNQQ
SQ  VSMEDSMAEDTDQANRASMVAPMFGQAAVSMPQPNFAFGGGAATQPPSMANPFQFGGQPMASTLQNASPFQASQSLEFQG
SQ  GGSFSLGSTGGGDKSGRRIFKAKKSTRKK
//
ID  Q69ZQ1;
PN  Myogenesis-regulating glycosidase;
GN  Myorg;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
DR  UNIPROT: Q69ZQ1;
DR  UNIPROT: A2ANN6;
DR  UNIPROT: B2RU42;
DR  Pfam: PF01055;
DE  Function: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2 (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004553;
GO  GO:0005975;
GO  GO:0043568;
GO  GO:0051897;
GO  GO:0048741;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQNLQETSQAYPRHRPGSHAGPKSLKVTPRATMYTFLPDNFSPAKPKPTKELRPLLCSAVLGLLLVLAAVVAWCYYSAS
SQ  LRKAERLRAELLDLNRGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSRAADGRPLHFFIQTVRPKDTVMCYRV
SQ  RWEEAVPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVND
SQ  SVPFHLGWNSTERSMRLQARYHDTSYKPPAGRTAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPASEAFRDPIWSTW
SQ  ALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSS
SQ  FGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLS
SQ  DPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMIGGNAVPE
SQ  RTAGRQDGPGPERELYVRWLEVAAFMPAMQFSIPPWQYDAEVVAIAHKFAALRASLVAPLLLELAGEITDTGDPIVRPLW
SQ  WIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEVAYFTWAS
//
ID  Q23544;
PN  Protein adenylyltransferase fic-1;
GN  fic;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27138431}; Single-pass membrane protein. Nucleus membrane {ECO:0000269|PubMed:27138431}; Single-pass membrane protein. Note=Predominantly localized to the endoplasmic reticulum and to the nucleus. {ECO:0000269|PubMed:27138431}.
DR  UNIPROT: Q23544;
DR  PDB: 5JJ6;
DR  PDB: 5JJ7;
DR  Pfam: PF02661;
DR  PROSITE: PS51459;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-274 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (PubMed:27138431). In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2 (PubMed:27138431). Can AMPylate core histone H3 in vitro (PubMed:27138431). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (PubMed:27138431). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6, ECO:0000269|PubMed:27138431}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016787;
GO  GO:0070733;
GO  GO:0050829;
GO  GO:0018117;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSS
SQ  PPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKD
SQ  GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVH
SQ  DLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLS
SQ  KEHDEISIDDILEMHRRVLGNADPVEAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIERAAIAHYKL
SQ  VLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSDN
SQ  ILNSGDSKLTPEESEVSEKIEAECRAGN
//
ID  O75608;
PN  Acyl-protein thioesterase 1;
GN  LYPLA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000269|PubMed:19439193}.
DR  UNIPROT: O75608;
DR  UNIPROT: O43202;
DR  UNIPROT: Q9UQF9;
DR  PDB: 1FJ2;
DR  PDB: 5SYM;
DR  Pfam: PF02230;
DR  OMIM: 605599;
DR  DisGeNET: 10434;
DE  Function: Acts as a acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Has depalmitoylating activity toward KCNMA1 (PubMed:22399288). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (PubMed:21393252). {ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:19439193, ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:21393252, ECO:0000269|PubMed:22399288}.
DE  Reference Proteome: Yes;
DE  Interaction: P03496; IntAct: EBI-1052185,EBI-2547442; Score: 0.37
DE  Interaction: Q8N3Z0; IntAct: EBI-20628340,EBI-1052185; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-1052185; Score: 0.35
DE  Interaction: Q14164; IntAct: EBI-1052185,EBI-307369; Score: 0.40
DE  Interaction: P40337; IntAct: EBI-1052185,EBI-301246; Score: 0.40
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-1052185; Score: 0.56
DE  Interaction: Q5VUG0; IntAct: EBI-12025260,EBI-1052185; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-1052185; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0052689;
GO  GO:0016298;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0042997;
GO  GO:0002084;
GO  GO:0050999;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSP
SQ  DSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGA
SQ  NRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
//
ID  Q9SZN7;
PN  Heavy metal-associated isoprenylated plant protein 26;
GN  HIPP26;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18974936}. Cell membrane {ECO:0000269|PubMed:18823312}. Note=PubMed:18974936 shows that isopernylation may be important for a speckle-like nuclear localization in a heterologous system, while PubMed:18823312 shows a plasma membrane localization. {ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936}.
DR  UNIPROT: Q9SZN7;
DR  UNIPROT: Q8LGG1;
DR  UNIPROT: Q9ZRE4;
DR  Pfam: PF00403;
DE  Function: Heavy-metal-binding protein. Binds lead, cadmium and copper. May be involved in heavy-metal transport (PubMed:18823312). May be involved in cadmium transport and play a role in cadmium detoxification (PubMed:21072340). {ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:21072340}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9SEZ1; IntAct: EBI-2008207,EBI-1806317; Score: 0.51
DE  Interaction: Q9STP8; IntAct: EBI-2008207,EBI-368234; Score: 0.59
DE  Interaction: Q9LK09; IntAct: EBI-9161785,EBI-2008207; Score: 0.35
DE  Interaction: Q9SZU7; IntAct: EBI-25519488,EBI-2008207; Score: 0.56
DE  Interaction: Q9SQR3; IntAct: EBI-2008207,EBI-25530219; Score: 0.56
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0046870;
GO  GO:0005507;
GO  GO:0032791;
GO  GO:0010286;
GO  GO:0030001;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18974936};
SQ  MGVLDHVSEMFDCSHGHKIKKRKQLQTVEIKVKMDCEGCERKVRRSVEGMKGVSSVTLEPKAHKVTVVGYVDPNKVVARM
SQ  SHRTGKKVELWPYVPYDVVAHPYAAGVYDKKAPSGYVRRVDDPGVSQLARASSTEVRYTTAFSDENPAACVVM
//
ID  A0A0B4K7J2;
PN  E3 SUMO-protein ligase RanBP2;
GN  Nup358;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:0000269|PubMed:31626769}.
DR  UNIPROT: A0A0B4K7J2;
DR  UNIPROT: D3DMF2;
DR  UNIPROT: Q8SWV7;
DR  UNIPROT: Q9VBU7;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS50196;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but also for the nuclear import of specific proteins such as phosphorylated Mad or the sesquiterpenoid juvenile hormone receptor Met as part of the juvenile hormone signal transduction pathway (PubMed:27979731, PubMed:17682050, PubMed:17682050). Plays a role in nuclear mRNA export by recruiting the mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC (PubMed:14729961). Essential during germline development for transposon silencing and piRNA biogenesis probably by regulating piwi localization to the nucleus (PubMed:29735528). During oogenesis, required to form granules that modulate the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: P34082; IntAct: EBI-868243,EBI-191234; Score: 0.53
DE  Interaction: Q24090; IntAct: EBI-191234,EBI-151570; Score: 0.37
DE  Interaction: Q9XZC2; IntAct: EBI-191234,EBI-458892; Score: 0.37
DE  Interaction: Q9VWE4; IntAct: EBI-191234,EBI-122539; Score: 0.37
DE  Interaction: Q9VU13; IntAct: EBI-191234,EBI-137049; Score: 0.37
DE  Interaction: A1ZAC2; IntAct: EBI-152117,EBI-191234; Score: 0.37
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0008536;
GO  GO:0019789;
GO  GO:0007281;
GO  GO:0035626;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051292;
GO  GO:0034587;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:0043547;
GO  GO:1900182;
GO  GO:0046833;
GO  GO:0006606;
GO  GO:1903827;
GO  GO:0010528;
GO  GO:0007419;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEA
SQ  LQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGE
SQ  QNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNW
SQ  RFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREV
SQ  LANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDR
SQ  ENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHI
SQ  ENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQI
SQ  QREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKAD
SQ  AIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMF
SQ  RIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRN
SQ  SRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVG
SQ  MEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVP
SQ  NPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSM
SQ  FPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVP
SQ  TVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLP
SQ  KPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEE
SQ  AEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCD
SQ  KATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKAS
SQ  EAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAP
SQ  ASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEY
SQ  VPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCN
SQ  QRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPI
SQ  KGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGF
SQ  SFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDT
SQ  VPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAA
SQ  KEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVM
SQ  RREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVG
SQ  SVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSL
SQ  SRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAA
SQ  EQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFG
SQ  IPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLA
SQ  SNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAI
SQ  VELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMD
SQ  YMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS
//
ID  Q6ZRP7;
PN  Sulfhydryl oxidase 2;
GN  QSOX2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000269|PubMed:14633699}; Single- pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single- pass membrane protein {ECO:0000305}. Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane.
DR  UNIPROT: Q6ZRP7;
DR  UNIPROT: A2CEE0;
DR  UNIPROT: A6NLB0;
DR  UNIPROT: Q5TB37;
DR  UNIPROT: Q7Z7B6;
DR  UNIPROT: Q86VV7;
DR  UNIPROT: Q8N3G2;
DR  Pfam: PF04777;
DR  Pfam: PF18371;
DR  Pfam: PF18108;
DR  Pfam: PF00085;
DR  PROSITE: PS51324;
DR  PROSITE: PS51352;
DR  OMIM: 612860;
DR  DisGeNET: 169714;
DE  Function: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. {ECO:0000269|PubMed:14633699}.
DE  Reference Proteome: Yes;
DE  Interaction: P05161; IntAct: EBI-746466,EBI-11127401; Score: 0.35
DE  Interaction: Q99614; IntAct: EBI-11127401,EBI-742074; Score: 0.35
DE  Interaction: Q5VYS8; IntAct: EBI-11127401,EBI-2810086; Score: 0.35
DE  Interaction: Q9C0F1; IntAct: EBI-11127401,EBI-744115; Score: 0.35
DE  Interaction: Q8IZH2-2; IntAct: EBI-11127401,EBI-10965083; Score: 0.35
DE  Interaction: Q86YS7; IntAct: EBI-11127401,EBI-1051086; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-11127401,EBI-358419; Score: 0.35
DE  Interaction: Q9UBD5-2; IntAct: EBI-11127401,EBI-10962124; Score: 0.35
DE  Interaction: Q6ZNJ1-3; IntAct: EBI-11127401,EBI-11028033; Score: 0.35
DE  Interaction: F8VY35; IntAct: EBI-11127401,EBI-10968005; Score: 0.35
DE  Interaction: Q9P2X3; IntAct: EBI-11127401,EBI-2857352; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-11127401,EBI-1237183; Score: 0.35
DE  Interaction: Q8TB52; IntAct: EBI-11127401,EBI-2556210; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25475871,EBI-11127401; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-11127401; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-11127401; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-2802853,EBI-11127401; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-79165,EBI-11127401; Score: 0.35
GO  GO:0005623;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0016971;
GO  GO:0003756;
GO  GO:0045454;
GO  GO:0006457;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSA
SQ  AWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKG
SQ  PDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTR
SQ  ALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKS
SQ  KLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNN
SQ  KMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECG
SQ  EHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQ
SQ  HYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPG
SQ  AHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV
//
ID  Q8NFH4;
PN  Nucleoporin Nup37;
GN  NUP37;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.
DR  UNIPROT: Q8NFH4;
DR  UNIPROT: Q9H644;
DR  PDB: 5A9Q;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 609264;
DR  OMIM: 618179;
DR  DisGeNET: 79023;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900, ECO:0000269|PubMed:30179222}.
DE  Disease: Microcephaly 24, primary, autosomal recessive (MCPH24) [MIM:618179]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH24 patients additionally manifest mildly impaired intellectual development, cerebellar vermis hypoplasia, and fifth finger clinodactyly. {ECO:0000269|PubMed:30179222}. Note=The disease may be caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-351935,EBI-2563158; Score: 0.35
DE  Interaction: P12270; IntAct: EBI-2563158,EBI-1048528; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-286779,EBI-2563158; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-2563158,EBI-1046596; Score: 0.55
DE  Interaction: P57740; IntAct: EBI-295687,EBI-2563158; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-2563158; Score: 0.35
DE  Interaction: Q60952; IntAct: EBI-643450,EBI-2563158; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-2563158; Score: 0.56
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-2563158; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-1059321,EBI-2563158; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-2563158; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-2563158; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-716392,EBI-2563158; Score: 0.40
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-2563158; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-2563158; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-2563158; Score: 0.35
DE  Interaction: O88952; IntAct: EBI-821316,EBI-2563158; Score: 0.35
DE  Interaction: Q8R023; IntAct: EBI-1216526,EBI-2563158; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-2563158; Score: 0.35
DE  Interaction: Q8WXG6; IntAct: EBI-310528,EBI-2563158; Score: 0.40
GO  GO:0000777;
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKQDASRNAAYTVDCEDYVHVVEFNPFENGDSGNLIAYGGNNYVVIGTCTFQEEEADVEGIQYKTLRTFHHGVRVDGIAW
SQ  SPETRLDSLPPVIKFCTSAADMKIRLFTSDLQDKNEYKVLEGHTDFINGLVFDPKEGQEIASVSDDHTCRIWNLEGVQTA
SQ  HFVLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLLAQQAILSLESEQVPLMSAHWCLKNTFKVGAVAGNDWLIWDITRS
SQ  SYPQNKRPVHMDRACLFRWSTISENLFATTGYPGKMASQFQIHHLGHPQPILMGSVAVGSGLSWHRTLPLCVIGGDHKLL
SQ  FWVTEV
//
ID  Q9UTK4;
PN  Nucleoporin nup96;
GN  nup189;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin nup98]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:26137436}. [Nucleoporin nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:26137436}.
DR  UNIPROT: Q9UTK4;
DR  UNIPROT: A0A0E3VYD1;
DR  UNIPROT: A0A0E4FZX7;
DR  UNIPROT: P78796;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (PubMed:15116432). Nup189 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC (PubMed:26137436). Nup98 as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. Nup96 as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export (By similarity). {ECO:0000250|UniProtKB:P49687, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:26137436}.
DE  Reference Proteome: Yes;
DE  Interaction: O74910; IntAct: EBI-904918,EBI-904913; Score: 0.37
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0031080;
GO  GO:0008139;
GO  GO:0008233;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0010389;
GO  GO:0006405;
GO  GO:0006407;
GO  GO:0034398;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGQNNSSGFGGGTGAFGQNNQQTGGLFGSNSNTPGNTLFGSQNTSTTGFGQNTTQPLFGSNTNGGLFGNRNNTTTTGGT
SQ  GFGMSSGTGMFGQSNTPAFGGTNNATNPSGGGLFGSNTANNNANTGTSFSFGSNAGSTGFGNTASNTGTGGGLFGSQNNA
SQ  GNTAGNTGFGSQGTGGGLFGSSTTPATTNAFGTSGFVSSNANAVNGTANPPYAVTSEKDPQTNGTSVFQSITCMPAYRSY
SQ  SFEELRLQDYNQGRRFGNASSTNTTSAFGSTPAFGASTTPFGQNLSGTTNNATPFGTSNATNTTPGSGLFGGGSAFGSNT
SQ  TNTGFGSGTNNASGGLFGQNNNTTSTPSTGLFGGSTFNQQKPAFSGFGSTTNTTNTGTGTGLFGSNNATNTGTGQTTGGL
SQ  FGGAATGTGTGFGSSTGGFGSNTNNQPNSGTMGTGLFGFGANNNTANNNTAPTSTFGGNNSSNFSFGANNNAATKPSGFG
SQ  FGSTTTTPASGGFSFGQNANNAPKPAFGSTATTAPKPAGTGLFGGLGAGANTNTATNATGTGGSLFGNANTAGSNMFGSA
SQ  NSSTPGTGLFGSTQTNNATSNTGTGLFGSNNANTTNTGGSLFNKPSTTTGGLFGNTTAQQPSTTTSGLFGASNTNNQAQT
SQ  SNFGTGLFGGSQAGQQQQPLQASIDQNPYGNNPLFSSTTSQVAPTSIQEPIASPLTSKPTPKKAASLPQFWLSPRSHNTA
SQ  RLASISSFAKSAVMNSTSASGKPKSLHLFDSLNDDVLLSADAFTPRQNIKKLVITHKISKDDILQNGVKNGNDAKSDSKV
SQ  QEKAPQNEADGSLKKDEHVVLSDDYWMKPSIEELSKYPKEKLCSVHQFSVGRTGYGQVAFLKPVDLSGFEKLEDIPGKVV
SQ  VFERKICAVYPVEGSSPPLGEGLNVPAIITLEKTWPLSRETREPIKDPQNPRYIQHVKRLHRIKDTEFIDFNDGKWIFKV
SQ  QHFSRYGLLDDEEEENDMSSTSNEAGNLKKYDQPNLKVSGKNDSFVTHHTPGAFPNDSKNKELNRHFLKVDDSAPLDDTF
SQ  MSKKVKLDFSSDSNVSERGDYDDNAKKVDEVISIEKVDGYSKENNVPLSEDDLSNSSESSNESVYSLVEESDASLAADNM
SQ  DIEDISEESDREELSSMRFGAQDFHGLVVTDNWRDQLNLSVQRSALIKAAFPESQSNANLKNSRGIYYNEHDLVTDIFGN
SQ  QNLDTDRPWQSLDKPGAFIPSKFHFTANGSCIYVLKSSDVKIRSIYDFIPTKDPNGTKLLEYQLDQTEVYLDLSGTHAAS
SQ  PRSSMTVKPLSLCSSGYESIVWDLTSILFDPKNYSLPSELSSEAREVLYQKLVRESLSEWITKTLEHETTTLAKEAETSE
SQ  ERIYILLTGNLIGQACEEAVQSQNNRLSTLIPLVNSDVDIQQEVKQQLEEWRKHGDLPFINKFTRLIFELLSGNTDIAEG
SQ  CGTKGDEDYVQSIPITKNMTWLRAFGLKLWYNTDISIGEAMQLYVESLQKFPEIMQKPIATSAVQGIEVYDIIYLLLKAY
SQ  AMGTSLEELTIPESAKCSPLNYRVVWQLAIYLSKARSLCDFSDRVVDINMAEDLKPISVHSDQLTLAYASQLEASGQWLW
SQ  SLFVLLHLENVETRTSTITSCLARNLRGGLGAGAVEMIEKLCIPESWLNEAKALYARYVGDHLNELYFLQEAALYEDAHK
SQ  VLLDTLAPQAVISGNKTQLKKALEGFNGQTDGLASWRFGGQIYSDYLDLLEGNFDANQELKLFTLRKISVALKELNATNL
SQ  LQKAALHKISRFVNALCNEESLTDAICNLPLPLADSLANLQNISVQF
//
ID  O14657;
PN  Torsin-1B;
GN  TOR1B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}.
DR  UNIPROT: O14657;
DR  Pfam: PF06309;
DR  OMIM: 608050;
DR  DisGeNET: 27348;
DE  Function: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non- neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.
DE  Reference Proteome: Yes;
DE  Interaction: P16104; IntAct: EBI-494830,EBI-2564400; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-10973834,EBI-2564400; Score: 0.35
DE  Interaction: P32971; IntAct: EBI-13076860,EBI-2564400; Score: 0.35
DE  Interaction: Q9H3K2; IntAct: EBI-2564400,EBI-2868909; Score: 0.35
DE  Interaction: Q9H0V9-2; IntAct: EBI-2564400,EBI-21511115; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-2564400; Score: 0.35
DE  Interaction: A4D1S0; IntAct: EBI-21511322,EBI-2564400; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-2802853,EBI-2564400; Score: 0.35
DE  Interaction: Q9UBM8; IntAct: EBI-21494458,EBI-2564400; Score: 0.35
DE  Interaction: Q9NRD1; IntAct: EBI-3938499,EBI-2564400; Score: 0.35
DE  Interaction: Q9UG22; IntAct: EBI-15891037,EBI-2564400; Score: 0.35
DE  Interaction: P29016; IntAct: EBI-1033762,EBI-2564400; Score: 0.35
DE  Interaction: Q9BRR6-2; IntAct: EBI-21524597,EBI-2564400; Score: 0.35
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0070062;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051085;
GO  GO:0007029;
GO  GO:0071763;
GO  GO:0034504;
GO  GO:0006986;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRAGWLRGAAALALLLAARVVAAFEPITVGLAIGAASAITGYLSYNDIYCRFAECCREERPLNASALKLDLEEKLFGQH
SQ  LATEVIFKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLHPKGLKSNFVHLFVSTLHFPHEQKIKLYQDQLQK
SQ  WIRGNVSACANSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGVSYRKAIFIFLSNAGGDLITKTALDFWRAGRKREDIQL
SQ  KDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYRHVKMCVRAEMRARGSAIDEDIVTRVAEEMTFFPRDEKI
SQ  YSDKGCKTVQSRLDFH
//
ID  P38757;
PN  Nuclear envelope morphology protein 1;
GN  NEM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}.
DR  UNIPROT: P38757;
DR  UNIPROT: D3DKU7;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Catalytic component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265). {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
DE  Reference Proteome: Yes;
DE  Interaction: P18410; IntAct: EBI-17857,EBI-24435; Score: 0.56
DE  Interaction: P38074; IntAct: EBI-8394,EBI-24435; Score: 0.37
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005739;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0004721;
GO  GO:0071072;
GO  GO:0006998;
GO  GO:1903740;
GO  GO:0006470;
GO  GO:0071071;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNALKYFSNHLITTKKQKKINVEVTKNQDLLGPSKEVSNKYTSHSENDCVSEVDQQYDHSSSHLKESDQNQERKNSVPKK
SQ  PKALRSILIEKIASILWALLLFLPYYLIIKPLMSLWFVFTFPLSVIERRVKHTDKRNRGSNASENELPVSSSNINDSSEK
SQ  TNPKNCNLNTIPEAVEDDLNASDEIILQRDNVKGSLLRAQSVKSRPRSYSKSELSLSNHSSSNTVFGTKRMGRFLFPKKL
SQ  IPKSVLNTQKKKKLVIDLDETLIHSASRSTTHSNSSQGHLVEVKFGLSGIRTLYFIHKRPYCDLFLTKVSKWYDLIIFTA
SQ  SMKEYADPVIDWLESSFPSSFSKRYYRSDCVLRDGVGYIKDLSIVKDSEENGKGSSSSLDDVIIIDNSPVSYAMNVDNAI
SQ  QVEGWISDPTDTDLLNLLPFLEAMRYSTDVRNILALKHGEKAFNIN
//
ID  P18410;
PN  Sporulation-specific protein SPO7;
GN  SPO7;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}.
DR  UNIPROT: P18410;
DR  UNIPROT: D6VPK9;
DR  Pfam: PF03907;
DE  Function: Regulatory component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265). {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
DE  Reference Proteome: Yes;
DE  Interaction: P38757; IntAct: EBI-17857,EBI-24435; Score: 0.56
DE  Interaction: P10664; IntAct: EBI-17857,EBI-15390; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-17857,EBI-20254; Score: 0.35
DE  Interaction: P32591; IntAct: EBI-17857,EBI-18622; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-17857,EBI-8648; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-17857,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-17857,EBI-8603; Score: 0.35
DE  Interaction: P02407; IntAct: EBI-17857,EBI-14526; Score: 0.35
DE  Interaction: P05737; IntAct: EBI-17857,EBI-15422; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-17857,EBI-15409; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-17857,EBI-15394; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-17857,EBI-12823; Score: 0.35
DE  Interaction: P12945; IntAct: EBI-17857,EBI-11868; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-17857,EBI-6270; Score: 0.35
DE  Interaction: P38631; IntAct: EBI-17857,EBI-7708; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0019888;
GO  GO:0006629;
GO  GO:0071072;
GO  GO:0006998;
GO  GO:1903740;
GO  GO:0006470;
GO  GO:0071071;
GO  GO:0061709;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPESIGDVGNHAQDDSASIVSGPRRRSTSKTSSAKNIRNSSNISPASMIFRNLLILEDDLRRQAHEQKILKWQFTLFLA
SQ  SMAGVGAFTFYELYFTSDYVKGLHRVILQFTLSFISITVVLFHISGQYRRTIVIPRRFFTSTNKGIRQFNVKLVKVQSTW
SQ  DEKYTDSVRFVSRTIAYCNIYCLKKFLWLKDDNAIVKFWKSVTIQSQPRIGAVDVKLVLNPRAFSAEIREGWEIYRDEFW
SQ  AREGARRRKQAHELRPKSE
//
ID  Q558Z2;
PN  Sun domain-containing protein 1;
GN  sun1;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}; Single-pass membrane protein {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}; Nucleoplasmic side {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}.
DR  UNIPROT: Q558Z2;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: May have an important role in defining the spacing of the nuclear envelope lumen. Essential for centrosome attachment to the nucleus, maintenance of correct ploidy, proper mitosis, association of the centromere cluster with the centrosome and the maintenance of genome stability. Requires direct chromatin binding for inner nuclear membrane targeting. {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0042802;
GO  GO:0043495;
GO  GO:0051301;
GO  GO:0034508;
GO  GO:0007098;
GO  GO:0051642;
GO  GO:0000070;
GO  GO:0006998;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINI
SQ  RNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDEN
SQ  PKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQID
SQ  NNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYF
SQ  PSFSTTKTNSPFNSTNNNIQFSNLITKEQLYPIIDEYFKKNEILKSYNKLFEKIENDIKYLSEREQYKDIINEIKEELKL
SQ  VKLSNMDEDRVNQLISKMINHYNNNENNKQELKELLSKSIEELTKLKSDSKEQLIQISTESMNQLGQLKSESINQLGQVK
SQ  SESIDKFQSTLKSLSKEEQSKIEREFNHQFNQLNKDADQLLSQHSLKIEKLREEINENQQSSLLKLTQEYKQLEERLKEF
SQ  SSKLQQSISSSSMDQFESWKLVFIKDIEERINKESSKLTNQYIQLTQQFTKIQSFIKDNPSIDSLTNTIESLEGIKLLIE
SQ  DILEVYSADKIAKVDYALGLAGASIEYNALHYRVSETYPPIKGSGSGSGSGGANGNSLGLYYYNLATNWIFPQPKPNPPE
SQ  TILDPMVNTGSCWGFYTGNGTIVIRLAKKIAITEVTMEHISSNISHHIDSAPKEFQVFGLINSSDIGQSLGVFTYDTTIN
SQ  RHLQTFKVNKIQSTTTTTTNQDQNDDDNIQEFSHVALRILSNHGYRYTCIYRFRVHGYQIPHPEQEQIQIIQEEQSFKQE
SQ  EINQQQIEQIEQIEQIEKQQQSDEL
//
ID  Q8N114;
PN  Protein shisa-5;
GN  SHISA5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein {ECO:0000269|PubMed:12135983}. Nucleus membrane {ECO:0000269|PubMed:12135983}.
DR  UNIPROT: Q8N114;
DR  UNIPROT: B3KW99;
DR  UNIPROT: F8W9N8;
DR  UNIPROT: Q69YY9;
DR  UNIPROT: Q7Z433;
DR  UNIPROT: Q8NHL9;
DR  UNIPROT: Q96MW8;
DR  UNIPROT: Q9BV58;
DR  Pfam: PF13908;
DR  OMIM: 607290;
DR  DisGeNET: 51246;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92905; IntAct: EBI-2115556,EBI-594661; Score: 0.37
DE  Interaction: P12815; IntAct: EBI-309164,EBI-2115556; Score: 0.60
DE  Interaction: Q92754; IntAct: EBI-2115556,EBI-937309; Score: 0.37
DE  Interaction: Q9NZC7; IntAct: EBI-2115556,EBI-4320739; Score: 0.52
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0050699;
GO  GO:0044267;
GO  GO:0042771;
GO  GO:0043123;
GO  GO:0043687;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAPVPAPRILLPLLLLLLLTPPPGARGEVCMASRGLSLFPESCPDFCCGTCDDQYCCSDVLKKFVWSEERCAVPEASVP
SQ  ASVEPVEQLGSALRFRPGYNDPMSGFGATLAVGLTIFVLSVVTIIICFTCSCCCLYKTCRRPRPVVTTTTSTTVVHAPYP
SQ  QPPSVPPSYPGPSYQGYHTMPPQPGMPAAPYPMQYPPPYPAQPMGPPAYHETLAGGAAAPYPASQPPYNPAYMDAPKAAL
//
ID  P06782;
PN  Carbon catabolite-derepressing protein kinase;
GN  SNF1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269|PubMed:25869125}.
DR  UNIPROT: P06782;
DR  UNIPROT: D6VTA0;
DR  PDB: 2FH9;
DR  PDB: 2QLV;
DR  PDB: 3DAE;
DR  PDB: 3HYH;
DR  PDB: 3MN3;
DR  PDB: 3T4N;
DR  PDB: 3TDH;
DR  PDB: 3TE5;
DR  Pfam: PF16579;
DR  Pfam: PF00069;
DR  Pfam: PF08587;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831). {ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989, ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125, ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512, ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}.
DE  Reference Proteome: Yes;
DE  Interaction: Q84VQ1; IntAct: EBI-2042415,EBI-17516; Score: 0.37
DE  Interaction: Q9SCY5; IntAct: EBI-2042436,EBI-17516; Score: 0.37
DE  Interaction: Q42384; IntAct: EBI-17516,EBI-1382964; Score: 0.37
DE  Interaction: P12904; IntAct: EBI-17537,EBI-17516; Score: 0.97
DE  Interaction: P32562; IntAct: EBI-4440,EBI-17516; Score: 0.35
DE  Interaction: P34164; IntAct: EBI-17516,EBI-17187; Score: 0.91
DE  Interaction: P10591; IntAct: EBI-8591,EBI-17516; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-17516,EBI-8627; Score: 0.53
DE  Interaction: P25491; IntAct: EBI-10420,EBI-17516; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-17516; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-17516,EBI-8611; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-17516,EBI-8659; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-17516,EBI-8648; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-17516,EBI-8050; Score: 0.35
DE  Interaction: P11792; IntAct: EBI-16703,EBI-17516; Score: 0.44
DE  Interaction: P30822; IntAct: EBI-20589,EBI-17516; Score: 0.35
DE  Interaction: Q99750; IntAct: EBI-724076,EBI-17516; Score: 0.56
DE  Interaction: Q9BQ66; IntAct: EBI-17516,EBI-739863; Score: 0.56
DE  Interaction: Q9UKT9; IntAct: EBI-747204,EBI-17516; Score: 0.56
DE  Interaction: P50222; IntAct: EBI-748397,EBI-17516; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-17516,EBI-719493; Score: 0.56
DE  Interaction: O43597; IntAct: EBI-742487,EBI-17516; Score: 0.56
DE  Interaction: P54619; IntAct: EBI-1181439,EBI-17516; Score: 0.56
DE  Interaction: P32578; IntAct: EBI-17516,EBI-17179; Score: 0.67
DE  Interaction: Q00816; IntAct: EBI-17516,EBI-8270; Score: 0.72
DE  Interaction: P38990; IntAct: EBI-17516,EBI-12863; Score: 0.56
DE  Interaction: Q04739; IntAct: EBI-17516,EBI-7244; Score: 0.86
DE  Interaction: P22204; IntAct: EBI-5569,EBI-17516; Score: 0.35
DE  Interaction: P32598; IntAct: EBI-13715,EBI-17516; Score: 0.35
DE  Interaction: P07270; IntAct: EBI-13378,EBI-17516; Score: 0.35
DE  Interaction: P36047; IntAct: EBI-16783,EBI-17516; Score: 0.35
DE  Interaction: P14693; IntAct: EBI-17516,EBI-24602; Score: 0.37
GO  GO:0005623;
GO  GO:0000144;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005641;
GO  GO:0031965;
GO  GO:0031588;
GO  GO:0005634;
GO  GO:0005774;
GO  GO:0004679;
GO  GO:0005086;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0005975;
GO  GO:0007155;
GO  GO:0006995;
GO  GO:0000132;
GO  GO:0071940;
GO  GO:0035556;
GO  GO:0001403;
GO  GO:0017148;
GO  GO:1900436;
GO  GO:0045722;
GO  GO:0016239;
GO  GO:2000222;
GO  GO:0006468;
GO  GO:0001302;
GO  GO:0006986;
GO  GO:0090606;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17237508};
SQ  MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQK
SQ  VALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQ
SQ  IISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGV
SQ  ILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLK
SQ  PHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANK
SQ  SVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRA
SQ  NMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNE
SQ  KIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN
//
ID  P53541;
PN  Putative meiotic phospholipase SPO1;
GN  SPO1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: P53541;
DR  UNIPROT: D6W1G5;
DR  Pfam: PF01735;
DR  PROSITE: PS51210;
DE  Function: Regulates spindle pole duplication in meiosis I, but not in mitosis. Required for meiosis I, meiosis II chromosome segregation and spore formation. Binds phosphatidylinositol (4)P mono- and polyphosphates. {ECO:0000269|PubMed:10855497, ECO:0000269|PubMed:17179081}.
DE  Reference Proteome: Yes;
DE  Interaction: P11484; IntAct: EBI-17851,EBI-8627; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-17851; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-17851,EBI-8603; Score: 0.35
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005576;
GO  GO:0000324;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005628;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0032120;
GO  GO:0046475;
GO  GO:0030474;
GO  GO:0070583;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQKLLFVFSVLLTVVLATAPFQVQCPSSPLIREAKHELCPEETLYLKKKKIKTKNKLIQFLKSLTEAKFSSKFYKRVLKD
SQ  PPKIGIAISGGGYRSMLVGTGFISQMNDYGLFEYSDYIAGLSGGSWILMDLVVQNFEVKSLLQEWDLEEDLLLGIPEFDI
SQ  SEEEIVTNAKKEYNDNDLKMKKRQGGSLITSSSNFYEQIEEIMNSIEEIPEDYMITKRNLNPLARLKKIFFPNNTFTGTD
SQ  AKIETFKKVLDFYKSLHLKIKPKKMEGFQISFTDYWGKAIVQRLKKNFDDDPNHSFSFSKLVNSSKKFKECSVPIPIFVA
SQ  NCKNGLLSNVIFEFTPFEFGSWENILRLFVKLPYLGSKIVSGKAEKCINNFDDLGFITATSSSIFNNVLIFIWNLASQSS
SQ  REAMKALNMVMGIFGLGKEEIFSISKDSSRLETDYAVYQPNPFYLYPEKDNVLTNKNHLYLVDGGEDGENIPLRTLVIPE
SQ  RELDVIFVLDSSSDIDNYPNGSKLKRIFEKLDEENVHYQFPNNVKTFTHPIVIGCNATKRTGHDSFLPIIIYHANANHGN
SQ  ASNTSTFKITYNQSEVSSMLPTGRGVFSNDYDLYYKNCLGCILTKRTMDRLPRKKKFSPFCLQCFKDYCYS
//
ID  Q23529;
PN  Zygote defective protein 12;
GN  zyg;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14697201}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14697201}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14697201}. Note=Localizes to the minus end of microtubules, proximal to the centrosome. Centrosomal localization requires sun-1 and microtubules.
DR  UNIPROT: Q23529;
DR  UNIPROT: Q2V4T6;
DR  UNIPROT: Q7JPD4;
DR  Pfam: PF05622;
DR  PROSITE: PS50021;
DE  Function: Cytoskeletal linker protein, which is essential for attachment of the centrosome to the nucleus (PubMed:14697201). Required for dynein localization to the nuclear envelope (PubMed:14697201). Forms a LINC (LInker of Nucleoskeleton and Cytoskeleton) complex together with unc-84, that may be involved in DNA damage repair (PubMed:27956467). {ECO:0000269|PubMed:14697201, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9U2Z1; IntAct: EBI-1570263,EBI-2006699; Score: 0.37
DE  Interaction: P91409; IntAct: EBI-1570263,EBI-326499; Score: 0.37
DE  Interaction: G5ED30; IntAct: EBI-1570263,EBI-11465218; Score: 0.51
DE  Interaction: H2KYA1; IntAct: EBI-1570263,EBI-11466183; Score: 0.37
DE  Interaction: Q93198; IntAct: EBI-1570263,EBI-11468631; Score: 0.37
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051959;
GO  GO:0008017;
GO  GO:0043621;
GO  GO:0051642;
GO  GO:0007059;
GO  GO:0031122;
GO  GO:0030705;
GO  GO:0009792;
GO  GO:0051647;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLDLTNKESESSDNGNSKYEDSIDGREVGTSKPFKEERSLEDLQADLADMAVWMEGLDATKLPLNDPQLLCNGRAFSEVL
SQ  HNVDKNFFTDGWLETMPENRTTNIMVFRSCTRKLWRKMFDYVNHINRTVVSSRWTDIHERIDGIYESDLPAMVNLGMAVV
SQ  TLAHIGKNAKRFVDYSKALTSTHKSMMSNVAKMVTTVIDEMPENPCFHEISELHGSQSELNSLSESSGKLNGNGSSERRS
SQ  NADQILVDAELEIERLRTETENQRKEIERLTKSFETAQHDMSSNSESGDISILEKQNEELRQKRRELEEKNLELDAAVDQ
SQ  FKGIVFELTNENDVLRRSDKERQRLQTVLDAAQSDLDEWKTVANQYQKEAELSKQQDKEIKELLSQNKALKSRLDHHVKS
SQ  ATLEDANKNGIAQLRTQVGGLTALNTELKASLDSKKRCVEQLEIQLIQHKEKVKELEDRKDELIEERNRLENQLIFKEAV
SQ  TPRSLHESMFEAGNLSFEPFSEKNTLPLEIENKRLTERIQELESLEPLKGELITLKSKNGVLEEEKLFATKQIEELQQQI
SQ  EDLQENLLKNQEHASGDVVGLKIQLEKAEVEAQQMREAKMRAETNQAQVDEILKKRTAELEVNATALQKAKAVIDELEYN
SQ  SRPVSEDSMTSVQAFKEMKEENEKLRQKVEKLEIELNTVTQGFEQENRLLTSASHQQVLNRSIDEVMSMRAHAGSEEPQT
SQ  LLDTQKMSGALPWRSLASETRRELPTAMASILVLGFLVFIAWMFININSALNAPPNA
//
ID  O35387;
PN  HCLS1-associated protein X-1;
GN  Hax1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:16814492}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle {ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}.
DR  UNIPROT: O35387;
DR  UNIPROT: Q542F8;
DE  Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165}.
DE  Reference Proteome: Yes;
DE  Interaction: O14925; IntAct: EBI-642449,EBI-1047996; Score: 0.35
DE  Interaction: Q9H477; IntAct: EBI-642449,EBI-10982959; Score: 0.35
DE  Interaction: H3BS42; IntAct: EBI-642449,EBI-10984149; Score: 0.35
DE  Interaction: P56199; IntAct: EBI-642449,EBI-2554465; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-642449,EBI-352528; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-642449,EBI-347978; Score: 0.35
DE  Interaction: Q92604; IntAct: EBI-642449,EBI-6116942; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-642449,EBI-356254; Score: 0.35
DE  Interaction: Q9H061; IntAct: EBI-642449,EBI-10963884; Score: 0.35
DE  Interaction: Q7KZ85; IntAct: EBI-642449,EBI-2515547; Score: 0.35
DE  Interaction: O15066; IntAct: EBI-642449,EBI-3931791; Score: 0.35
DE  Interaction: Q9H078-2; IntAct: EBI-642449,EBI-10984145; Score: 0.35
DE  Interaction: O75165; IntAct: EBI-642449,EBI-4324603; Score: 0.35
DE  Interaction: G3XAN4; IntAct: EBI-642449,EBI-10982949; Score: 0.35
DE  Interaction: B4E1G1; IntAct: EBI-642449,EBI-10984153; Score: 0.35
DE  Interaction: P42227; IntAct: EBI-642449,EBI-602878; Score: 0.37
DE  Interaction: Q8BWG8; IntAct: EBI-642449,EBI-641778; Score: 0.37
DE  Interaction: Q8CIH5; IntAct: EBI-642449,EBI-617954; Score: 0.37
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0005758;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0000932;
GO  GO:0016529;
GO  GO:0005667;
GO  GO:0019966;
GO  GO:0019904;
GO  GO:0047485;
GO  GO:0007166;
GO  GO:0071345;
GO  GO:0043066;
GO  GO:2000251;
GO  GO:0030854;
GO  GO:0033138;
GO  GO:0050731;
GO  GO:0014068;
GO  GO:0051897;
GO  GO:0045944;
GO  GO:0030833;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O00165};
SQ  MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNF
SQ  GFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPD
SQ  WGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETT
SQ  VTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR
//
ID  P20592;
PN  Interferon-induced GTP-binding protein Mx2;
GN  MX2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15184662}. Nucleus {ECO:0000269|PubMed:15184662}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15184662}. Note=Localization to nuclear pores requires GTP-binding.
DR  UNIPROT: P20592;
DR  UNIPROT: B7Z5D3;
DR  UNIPROT: D3DSI7;
DR  PDB: 4WHJ;
DR  PDB: 4X0R;
DR  PDB: 5UOT;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DR  OMIM: 147890;
DR  DisGeNET: 4600;
DE  Function: Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression. {ECO:0000269|PubMed:15184662, ECO:0000269|PubMed:24048477, ECO:0000269|PubMed:24055605, ECO:0000269|PubMed:24121441}.
DE  Reference Proteome: Yes;
DE  Interaction: A2ABF9; IntAct: EBI-10174566,EBI-10200618; Score: 0.56
DE  Interaction: O75928; IntAct: EBI-348555,EBI-10200618; Score: 0.56
DE  Interaction: Q8WXE1; IntAct: EBI-10200618,EBI-747353; Score: 0.56
DE  Interaction: Q96KQ7; IntAct: EBI-744366,EBI-10200618; Score: 0.56
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0044327;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0031966;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098844;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0045202;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0006952;
GO  GO:0051607;
GO  GO:0061025;
GO  GO:0000266;
GO  GO:0051028;
GO  GO:0048285;
GO  GO:0098884;
GO  GO:0031623;
GO  GO:0051726;
GO  GO:0046822;
GO  GO:0050803;
GO  GO:0035455;
GO  GO:0009615;
GO  GO:0016185;
GO  GO:0060337;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQP
SQ  RAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLK
SQ  KQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRD
SQ  IGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKK
SQ  GYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKA
SQ  TEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEV
SQ  EKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKH
SQ  TAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKR
SQ  LANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH
//
ID  Q8WUM0;
PN  Nuclear pore complex protein Nup133;
GN  NUP133;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DR  UNIPROT: Q8WUM0;
DR  UNIPROT: B2RAZ8;
DR  UNIPROT: Q5T8N0;
DR  UNIPROT: Q9H9W2;
DR  UNIPROT: Q9NV71;
DR  UNIPROT: Q9NVC4;
DR  PDB: 1XKS;
DR  PDB: 3CQC;
DR  PDB: 3CQG;
DR  PDB: 3I4R;
DR  PDB: 5A9Q;
DR  Pfam: PF03177;
DR  OMIM: 607613;
DR  OMIM: 618177;
DR  OMIM: 618349;
DR  DisGeNET: 55746;
DE  Function: Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:30179222}.
DE  Disease: Nephrotic syndrome 18 (NPHS18) [MIM:618177]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS18 is an autosomal recessive, steroid-resistant progressive form with onset in the first decade of life. {ECO:0000269|PubMed:30179222}. Note=The disease is caused by mutations affecting the gene represented in this entry. Galloway-Mowat syndrome 8 (GAMOS8) [MIM:618349]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS8 inheritance is autosomal recessive. {ECO:0000269|PubMed:30427554}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-295695; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-295695; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-295644,EBI-295695; Score: 0.35
DE  Interaction: P35729; IntAct: EBI-11713,EBI-295695; Score: 0.40
DE  Interaction: P46673; IntAct: EBI-295695,EBI-12345; Score: 0.51
DE  Interaction: P49790; IntAct: EBI-286779,EBI-295695; Score: 0.53
DE  Interaction: P52891; IntAct: EBI-295695,EBI-12337; Score: 0.40
DE  Interaction: P52948; IntAct: EBI-295695,EBI-295727; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-295695,EBI-16940; Score: 0.40
DE  Interaction: P55735; IntAct: EBI-1046596,EBI-295695; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-295695; Score: 0.86
DE  Interaction: Q12769; IntAct: EBI-295695,EBI-295715; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-295695; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-295695; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-295695; Score: 0.37
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-295695; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-295695; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-1059321,EBI-295695; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-295695; Score: 0.69
DE  Interaction: Q9Y275; IntAct: EBI-519169,EBI-295695; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-295695; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-295695; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-295695; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-716392,EBI-295695; Score: 0.57
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-295695; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-2551981,EBI-295695; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-295695; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-295695; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-295695; Score: 0.35
DE  Interaction: Q80YV4; IntAct: EBI-8344124,EBI-295695; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-295695; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-353844,EBI-295695; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-295695; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-295695; Score: 0.35
DE  Interaction: Q6XPS3-3; IntAct: EBI-21801316,EBI-295695; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-365996,EBI-295695; Score: 0.27
DE  Interaction: O15273; IntAct: EBI-295695,EBI-954089; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-447544,EBI-295695; Score: 0.56
DE  Interaction: P10412; IntAct: EBI-358163,EBI-295695; Score: 0.40
DE  Interaction: P06821; IntAct: EBI-2547404,EBI-295695; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-3912901,EBI-295695; Score: 0.37
DE  Interaction: P78406; IntAct: EBI-724495,EBI-295695; Score: 0.37
DE  Interaction: C5E526; IntAct: EBI-12577179,EBI-295695; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585275,EBI-295695; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-295695; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-295695; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-6050648,EBI-295695; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12561553,EBI-295695; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579807,EBI-295695; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-2547514,EBI-295695; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-295695; Score: 0.27
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-295695; Score: 0.35
DE  Interaction: Q9UBP0-2; IntAct: EBI-21757051,EBI-295695; Score: 0.35
GO  GO:0000777;
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0031081;
GO  GO:0006999;
GO  GO:0048339;
GO  GO:0006606;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0061053;
GO  GO:0000972;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYD
SQ  VKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSY
SQ  SSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKI
SQ  HQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENI
SQ  TDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSE
SQ  DLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVS
SQ  ILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRA
SQ  VTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLL
SQ  CEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIE
SQ  WAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNI
SQ  VTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTD
SQ  NQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANME
SQ  TRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEEN
SQ  RRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLP
SQ  EVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI
//
ID  Q96RT1;
PN  Erbin;
GN  ERBIN;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell junction, hemidesmosome {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q96RT1;
DR  UNIPROT: A0AVR1;
DR  UNIPROT: B4E3F1;
DR  UNIPROT: B7ZLV9;
DR  UNIPROT: E7EQW9;
DR  UNIPROT: E9PCR8;
DR  UNIPROT: Q1RMD0;
DR  UNIPROT: Q86W38;
DR  UNIPROT: Q9NR18;
DR  UNIPROT: Q9NW48;
DR  UNIPROT: Q9ULJ5;
DR  PDB: 1MFG;
DR  PDB: 1MFL;
DR  PDB: 1N7T;
DR  PDB: 2H3L;
DR  PDB: 2QBW;
DR  PDB: 3CH8;
DR  PDB: 6Q0M;
DR  PDB: 6Q0N;
DR  PDB: 6Q0U;
DR  Pfam: PF13855;
DR  Pfam: PF00595;
DR  PROSITE: PS51450;
DR  PROSITE: PS50106;
DR  OMIM: 606944;
DR  DisGeNET: 55914;
DE  Function: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XI72; IntAct: EBI-993903,EBI-22238565; Score: 0.35
DE  Interaction: Q6AXS5; IntAct: EBI-993903,EBI-931289; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-993903; Score: 0.35
DE  Interaction: Q9HC29; IntAct: EBI-7445625,EBI-993903; Score: 0.66
DE  Interaction: P57078; IntAct: EBI-4422308,EBI-993903; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-993903,EBI-727707; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-447544,EBI-993903; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-1056902,EBI-993903; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-993903; Score: 0.35
DE  Interaction: P49841; IntAct: EBI-373586,EBI-993903; Score: 0.35
DE  Interaction: P25791; IntAct: EBI-993903,EBI-739696; Score: 0.37
DE  Interaction: P40763; IntAct: EBI-993903,EBI-518675; Score: 0.37
DE  Interaction: Q8CZQ2; IntAct: EBI-993903,EBI-2865703; Score: 0.37
DE  Interaction: Q8CZZ5; IntAct: EBI-2841603,EBI-993903; Score: 0.37
DE  Interaction: Q5NID9; IntAct: EBI-993903,EBI-2798201; Score: 0.37
DE  Interaction: Q9UQ13; IntAct: EBI-993879,EBI-993903; Score: 0.62
DE  Interaction: Q2LC84; IntAct: EBI-993903,EBI-7865699; Score: 0.35
DE  Interaction: Q04970; IntAct: EBI-993903,EBI-7341579; Score: 0.35
DE  Interaction: P60868; IntAct: EBI-993903,EBI-931416; Score: 0.35
DE  Interaction: A0A0G2K8Z9; IntAct: EBI-993903,EBI-22249508; Score: 0.35
DE  Interaction: G3V7V7; IntAct: EBI-993903,EBI-22242012; Score: 0.35
DE  Interaction: D4A9L2; IntAct: EBI-993903,EBI-16221426; Score: 0.35
DE  Interaction: A0A0G2K654; IntAct: EBI-993903,EBI-16220437; Score: 0.35
DE  Interaction: Q27W01; IntAct: EBI-993903,EBI-22258009; Score: 0.35
DE  Interaction: B2RYP6; IntAct: EBI-993903,EBI-22252219; Score: 0.35
DE  Interaction: G3V6S1; IntAct: EBI-993903,EBI-22257984; Score: 0.35
DE  Interaction: P62890; IntAct: EBI-993903,EBI-437905; Score: 0.35
DE  Interaction: P35427; IntAct: EBI-993903,EBI-917340; Score: 0.35
DE  Interaction: Q8K1Q0; IntAct: EBI-993903,EBI-22239154; Score: 0.35
DE  Interaction: B5DFM8; IntAct: EBI-993903,EBI-22240024; Score: 0.35
DE  Interaction: Q6AYK8; IntAct: EBI-993903,EBI-21997253; Score: 0.35
DE  Interaction: Q4V8C8; IntAct: EBI-993903,EBI-22249471; Score: 0.35
DE  Interaction: Q920F5; IntAct: EBI-993903,EBI-22257951; Score: 0.35
DE  Interaction: D4A3K5; IntAct: EBI-993903,EBI-16220000; Score: 0.35
DE  Interaction: E9PT65; IntAct: EBI-993903,EBI-21020461; Score: 0.35
DE  Interaction: P62850; IntAct: EBI-993903,EBI-354479; Score: 0.35
DE  Interaction: G3V9L1; IntAct: EBI-993903,EBI-22251988; Score: 0.35
DE  Interaction: M0R6J0; IntAct: EBI-993903,EBI-22244748; Score: 0.35
DE  Interaction: P62278; IntAct: EBI-993903,EBI-351861; Score: 0.35
DE  Interaction: Q6IMY8; IntAct: EBI-993903,EBI-931601; Score: 0.35
DE  Interaction: Q62780; IntAct: EBI-993903,EBI-22243653; Score: 0.35
DE  Interaction: P24368; IntAct: EBI-993903,EBI-916926; Score: 0.35
DE  Interaction: A0A0G2K719; IntAct: EBI-993903,EBI-16219520; Score: 0.35
DE  Interaction: Q7TT49; IntAct: EBI-993903,EBI-692673; Score: 0.35
DE  Interaction: P09875; IntAct: EBI-993903,EBI-22253732; Score: 0.35
DE  Interaction: P09895; IntAct: EBI-993903,EBI-916235; Score: 0.35
DE  Interaction: P62893; IntAct: EBI-993903,EBI-22253129; Score: 0.35
DE  Interaction: Q9R0T3; IntAct: EBI-993903,EBI-8761889; Score: 0.35
DE  Interaction: A0A0G2JW88; IntAct: EBI-993903,EBI-22249209; Score: 0.35
DE  Interaction: M0R9L3; IntAct: EBI-993903,EBI-22245393; Score: 0.35
DE  Interaction: Q5RK00; IntAct: EBI-993903,EBI-22245576; Score: 0.35
DE  Interaction: E9PU01; IntAct: EBI-993903,EBI-22250811; Score: 0.35
DE  Interaction: Q3KRF2; IntAct: EBI-993903,EBI-6250493; Score: 0.35
DE  Interaction: F1M124; IntAct: EBI-993903,EBI-22243823; Score: 0.35
DE  Interaction: D3ZZT9; IntAct: EBI-993903,EBI-22252032; Score: 0.35
DE  Interaction: Q9JJ31; IntAct: EBI-993903,EBI-22250160; Score: 0.35
DE  Interaction: Q63186; IntAct: EBI-993903,EBI-22243899; Score: 0.35
DE  Interaction: P17078; IntAct: EBI-993903,EBI-21233671; Score: 0.35
DE  Interaction: P13471; IntAct: EBI-993903,EBI-916488; Score: 0.35
DE  Interaction: F1MAF2; IntAct: EBI-993903,EBI-22251970; Score: 0.35
DE  Interaction: Q6AYE2; IntAct: EBI-993903,EBI-22256450; Score: 0.35
DE  Interaction: D4AD15; IntAct: EBI-993903,EBI-6249876; Score: 0.35
DE  Interaction: P50904; IntAct: EBI-993903,EBI-5747849; Score: 0.35
DE  Interaction: B2GV09; IntAct: EBI-993903,EBI-22242066; Score: 0.35
DE  Interaction: P05197; IntAct: EBI-993903,EBI-915895; Score: 0.35
DE  Interaction: G3V9N7; IntAct: EBI-993903,EBI-22243718; Score: 0.35
DE  Interaction: Q9Z1W6; IntAct: EBI-993903,EBI-920297; Score: 0.35
DE  Interaction: P62961; IntAct: EBI-993903,EBI-917053; Score: 0.35
DE  Interaction: A0A096MK30; IntAct: EBI-993903,EBI-22249084; Score: 0.35
DE  Interaction: D4A4R1; IntAct: EBI-993903,EBI-22257933; Score: 0.35
DE  Interaction: P30009; IntAct: EBI-993903,EBI-22252236; Score: 0.35
DE  Interaction: Q5M7V8; IntAct: EBI-993903,EBI-22257898; Score: 0.35
DE  Interaction: P47198; IntAct: EBI-993903,EBI-931434; Score: 0.35
DE  Interaction: P31000; IntAct: EBI-993903,EBI-368510; Score: 0.35
DE  Interaction: P61314; IntAct: EBI-993903,EBI-22245322; Score: 0.35
DE  Interaction: D3Z898; IntAct: EBI-993903,EBI-22257865; Score: 0.35
DE  Interaction: Q5U2Q7; IntAct: EBI-993903,EBI-22243406; Score: 0.35
DE  Interaction: Q5XIM5; IntAct: EBI-993903,EBI-22236933; Score: 0.35
DE  Interaction: P13086; IntAct: EBI-993903,EBI-916468; Score: 0.35
DE  Interaction: Q5M963; IntAct: EBI-993903,EBI-22242417; Score: 0.35
DE  Interaction: P81795; IntAct: EBI-993903,EBI-22251872; Score: 0.35
DE  Interaction: M0R9T2; IntAct: EBI-993903,EBI-22257831; Score: 0.35
DE  Interaction: P41743; IntAct: EBI-286199,EBI-993903; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-356283,EBI-993903; Score: 0.60
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-993903; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-993903; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-357253,EBI-993903; Score: 0.46
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-993903; Score: 0.35
GO  GO:0009925;
GO  GO:0005604;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030056;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0005176;
GO  GO:0005102;
GO  GO:0005200;
GO  GO:0045175;
GO  GO:0007155;
GO  GO:0071356;
GO  GO:0007173;
GO  GO:0038128;
GO  GO:0045197;
GO  GO:0007229;
GO  GO:0045104;
GO  GO:0071638;
GO  GO:0032088;
GO  GO:0070433;
GO  GO:0006605;
GO  GO:0099072;
GO  GO:0032496;
GO  GO:0032495;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDND
SQ  LTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRL
SQ  TKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKN
SQ  NIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQ
SQ  LTNLRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSD
SQ  NQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPSLWEEQRKQRAQVAFECDEDKDEREAPPREGNL
SQ  KRYPTPYPDELKNMVKTVQTIVHRLKDEETNEDSGRDLKPHEDQQDINKDVGVKTSESTTTVKSKVDEREKYMIGNSVQK
SQ  ISEPEAEISPGSLPVTANMKASENLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDTKET
SQ  DSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTHIDINSKIRQEDENFNSLLQNGDILNSSTEEKF
SQ  KAHDKKDFNLPEYDLNVEERLVLIEKSVDSTATADDTHKLDHINMNLNKLITNDTFQPEIMERSKTQDIVLGTSFLSINS
SQ  KEETEHLENGNKYPNLESVNKVNGHSEETSQSPNRTEPHDSDCSVDLGISKSTEDLSPQKSGPVGSVVKSHSITNMEIGG
SQ  LKIYDILSDNGPQQPSTTVKITSAVDGKNIVRSKSATLLYDQPLQVFTGSSSSSDLISGTKAIFKFDSNHNPEEPNIIRG
SQ  PTSGPQSAPQIYGPPQYNIQYSSSAAVKDTLWHSKQNPQIDHASFPPQLLPRSESTENQSYAKHSANMNFSNHNNVRANT
SQ  AYHLHQRLGPARHGEMWAISPNDRLIPAVTRSTIQRQSSVSSTASVNLGDPGSTRRAQIPEGDYLSYREFHSAGRTPPMM
SQ  PGSQRPLSARTYSIDGPNASRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPRDWREQV
SQ  LRHIEAKKLEKKHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMKMPLSNGQMGQPLRPQANYSQIHHPPQAS
SQ  VARHPSREQLIDYLMLKVAHQPPYTQPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQ
SQ  PEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVREVSS
//
ID  Q7JXF5;
PN  Nuclear pore glycoprotein p62;
GN  Nup62;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:26341556}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:7641726}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin (PubMed:20144760). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760}.
DR  UNIPROT: Q7JXF5;
DR  Pfam: PF05064;
DE  Function: Essential component of the nuclear pore complex (By similarity). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein- protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity). Binds to transcriptionally active genes (PubMed:20144760). Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154 (PubMed:26341556). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}.
DE  Reference Proteome: Yes;
DE  Interaction: P17886; IntAct: EBI-127204,EBI-108202; Score: 0.37
DE  Interaction: Q9W053; IntAct: EBI-127204,EBI-87615; Score: 0.37
DE  Interaction: Q7KW14; IntAct: EBI-127204,EBI-101492; Score: 0.37
DE  Interaction: Q9VF74; IntAct: EBI-127204,EBI-208005; Score: 0.37
DE  Interaction: Q9GYU8; IntAct: EBI-127204,EBI-161961; Score: 0.37
DE  Interaction: Q9VSF3; IntAct: EBI-127204,EBI-96764; Score: 0.37
DE  Interaction: Q9V6B9; IntAct: EBI-127204,EBI-179307; Score: 0.37
DE  Interaction: Q9VVB4; IntAct: EBI-127204,EBI-94400; Score: 0.37
DE  Interaction: Q9VDS5; IntAct: EBI-127204,EBI-176038; Score: 0.37
DE  Interaction: Q9VBM3; IntAct: EBI-127204,EBI-83994; Score: 0.37
DE  Interaction: Q9VDK2; IntAct: EBI-127204,EBI-87444; Score: 0.37
DE  Interaction: Q9VG59; IntAct: EBI-127204,EBI-194851; Score: 0.37
DE  Interaction: Q9VBJ9; IntAct: EBI-127204,EBI-147550; Score: 0.37
DE  Interaction: Q9VBH0; IntAct: EBI-127204,EBI-171538; Score: 0.37
DE  Interaction: Q8T414; IntAct: EBI-127204,EBI-95177; Score: 0.37
DE  Interaction: Q9W4H1; IntAct: EBI-127204,EBI-107424; Score: 0.37
DE  Interaction: Q9VP67; IntAct: EBI-127204,EBI-113469; Score: 0.37
DE  Interaction: Q9VIY1; IntAct: EBI-127204,EBI-151825; Score: 0.37
DE  Interaction: Q9VYT1; IntAct: EBI-127204,EBI-103162; Score: 0.37
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0000922;
GO  GO:0031490;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0097240;
GO  GO:0051028;
GO  GO:0030717;
GO  GO:0006606;
GO  GO:0097298;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLG
SQ  SGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAA
SQ  STTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQI
SQ  NAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQL
SQ  KQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF
//
ID  Q9UBU9;
PN  Nuclear RNA export factor 1;
GN  NXF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:25662211}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus speckle {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus envelope {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:23591820}. Cytoplasm {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:19864460}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18596238}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles (PubMed:23826332). Nucleus; nuclear rim (PubMed:25662211). {ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25662211}.
DR  UNIPROT: Q9UBU9;
DR  UNIPROT: B4E269;
DR  UNIPROT: Q99799;
DR  UNIPROT: Q9UQL2;
DR  PDB: 1FO1;
DR  PDB: 1FT8;
DR  PDB: 1GO5;
DR  PDB: 1JKG;
DR  PDB: 1JN5;
DR  PDB: 1KOH;
DR  PDB: 1KOO;
DR  PDB: 1OAI;
DR  PDB: 2Z5K;
DR  PDB: 2Z5M;
DR  PDB: 3RW6;
DR  PDB: 3RW7;
DR  PDB: 4WYK;
DR  PDB: 6E5U;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DR  OMIM: 602647;
DR  DisGeNET: 10482;
DE  Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}.
DE  Reference Proteome: Yes;
DE  Interaction: O15234; IntAct: EBI-398874,EBI-299118; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-398874,EBI-347978; Score: 0.88
DE  Interaction: P49790; IntAct: EBI-286779,EBI-398874; Score: 0.76
DE  Interaction: P57740; IntAct: EBI-295687,EBI-398874; Score: 0.35
DE  Interaction: Q06609; IntAct: EBI-297202,EBI-398874; Score: 0.37
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-398874; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-398874,EBI-1955541; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-398874; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-398874; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-398874; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-398874; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-398874; Score: 0.56
DE  Interaction: Q9NRR5; IntAct: EBI-711226,EBI-398874; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-398874; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-398874; Score: 0.35
DE  Interaction: B4DYC6; IntAct: EBI-9357028,EBI-398874; Score: 0.40
DE  Interaction: Q96RS6; IntAct: EBI-2512429,EBI-398874; Score: 0.40
DE  Interaction: O95751; IntAct: EBI-398874,EBI-740738; Score: 0.67
DE  Interaction: P14136; IntAct: EBI-744302,EBI-398874; Score: 0.78
DE  Interaction: Q13625-3; IntAct: EBI-398874,EBI-10175039; Score: 0.56
DE  Interaction: Q6A162; IntAct: EBI-398874,EBI-10171697; Score: 0.56
DE  Interaction: Q92997; IntAct: EBI-398874,EBI-739789; Score: 0.56
DE  Interaction: Q96CG3; IntAct: EBI-398874,EBI-740711; Score: 0.72
DE  Interaction: Q9UJV3-2; IntAct: EBI-10172526,EBI-398874; Score: 0.56
DE  Interaction: O95166; IntAct: EBI-712001,EBI-398874; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-398874; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-398874; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-398874; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-398874; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-398874; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-80168,EBI-398874; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-398874,EBI-351962; Score: 0.40
DE  Interaction: P46013; IntAct: EBI-876367,EBI-398874; Score: 0.35
DE  Interaction: Q9NPJ8-2; IntAct: EBI-21528382,EBI-398874; Score: 0.35
DE  Interaction: Q9Y2Z4; IntAct: EBI-398874,EBI-1049286; Score: 0.35
DE  Interaction: Q9UKK6; IntAct: EBI-398874,EBI-301889; Score: 0.84
DE  Interaction: Q9H000; IntAct: EBI-398874,EBI-2341005; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-398874,EBI-2511609; Score: 0.35
DE  Interaction: Q53F19-2; IntAct: EBI-398874,EBI-21666124; Score: 0.35
DE  Interaction: P35658-2; IntAct: EBI-398874,EBI-10969485; Score: 0.35
DE  Interaction: Q86WS4; IntAct: EBI-398874,EBI-10286004; Score: 0.56
DE  Interaction: Q6P1L6; IntAct: EBI-398874,EBI-10252492; Score: 0.56
DE  Interaction: Q9C0B1-2; IntAct: EBI-398874,EBI-18138793; Score: 0.56
DE  Interaction: Q9P2M4; IntAct: EBI-398874,EBI-2797718; Score: 0.56
DE  Interaction: P68400; IntAct: EBI-347804,EBI-398874; Score: 0.44
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-398874; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-359390,EBI-398874; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-398874; Score: 0.35
DE  Interaction: P11474; IntAct: EBI-372412,EBI-398874; Score: 0.37
DE  Interaction: O43765; IntAct: EBI-398874,EBI-347996; Score: 0.37
DE  Interaction: Q07955; IntAct: EBI-398874,EBI-398920; Score: 0.76
DE  Interaction: P62995; IntAct: EBI-725485,EBI-398874; Score: 0.37
DE  Interaction: Q9NXV2; IntAct: EBI-1056857,EBI-398874; Score: 0.49
DE  Interaction: Q13595; IntAct: EBI-398874,EBI-2685506; Score: 0.37
DE  Interaction: Q9BTP6; IntAct: EBI-398874,EBI-3924044; Score: 0.37
DE  Interaction: Q81WW5; IntAct: EBI-2828492,EBI-398874; Score: 0.37
DE  Interaction: Q81WF3; IntAct: EBI-398874,EBI-2810353; Score: 0.37
DE  Interaction: P10644; IntAct: EBI-476431,EBI-398874; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-358028,EBI-398874; Score: 0.40
DE  Interaction: P41219; IntAct: EBI-752074,EBI-398874; Score: 0.56
DE  Interaction: Q5JR59-3; IntAct: EBI-11522433,EBI-398874; Score: 0.56
DE  Interaction: Q13555-5; IntAct: EBI-12020154,EBI-398874; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-5916454,EBI-398874; Score: 0.56
DE  Interaction: Q9NQY0; IntAct: EBI-2653038,EBI-398874; Score: 0.56
DE  Interaction: Q9BYV9; IntAct: EBI-1642333,EBI-398874; Score: 0.56
DE  Interaction: Q8N6V9; IntAct: EBI-746341,EBI-398874; Score: 0.56
DE  Interaction: A0A1B0GWI1; IntAct: EBI-10181422,EBI-398874; Score: 0.56
DE  Interaction: Q5T5B0; IntAct: EBI-10245456,EBI-398874; Score: 0.56
DE  Interaction: Q9H7T9; IntAct: EBI-10693257,EBI-398874; Score: 0.56
DE  Interaction: Q96DF8; IntAct: EBI-3928124,EBI-398874; Score: 0.56
DE  Interaction: Q9NR46; IntAct: EBI-749607,EBI-398874; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-11962468,EBI-398874; Score: 0.56
DE  Interaction: Q5SWW7; IntAct: EBI-12809220,EBI-398874; Score: 0.56
DE  Interaction: Q96P16-3; IntAct: EBI-12840198,EBI-398874; Score: 0.56
DE  Interaction: Q8TDR4; IntAct: EBI-3923210,EBI-398874; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-632715,EBI-398874; Score: 0.56
DE  Interaction: Q9H079; IntAct: EBI-715394,EBI-398874; Score: 0.56
DE  Interaction: Q9ULR0-1; IntAct: EBI-18398632,EBI-398874; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-744871,EBI-398874; Score: 0.56
DE  Interaction: Q9BZL4; IntAct: EBI-721802,EBI-398874; Score: 0.56
DE  Interaction: Q8IZU3; IntAct: EBI-7574149,EBI-398874; Score: 0.56
DE  Interaction: Q14457; IntAct: EBI-949378,EBI-398874; Score: 0.56
DE  Interaction: Q13829; IntAct: EBI-2505861,EBI-398874; Score: 0.56
DE  Interaction: Q8ND83; IntAct: EBI-10269374,EBI-398874; Score: 0.56
DE  Interaction: Q96MP8-2; IntAct: EBI-11954971,EBI-398874; Score: 0.56
DE  Interaction: Q9H0A9-2; IntAct: EBI-11995806,EBI-398874; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-744556,EBI-398874; Score: 0.56
DE  Interaction: Q8NCU1; IntAct: EBI-750686,EBI-398874; Score: 0.56
DE  Interaction: Q8WWY6; IntAct: EBI-12516603,EBI-398874; Score: 0.56
DE  Interaction: Q86WP2; IntAct: EBI-2349758,EBI-398874; Score: 0.56
DE  Interaction: P31321; IntAct: EBI-2805516,EBI-398874; Score: 0.56
DE  Interaction: Q8N8U2; IntAct: EBI-8467076,EBI-398874; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-741480,EBI-398874; Score: 0.56
DE  Interaction: Q13490; IntAct: EBI-514538,EBI-398874; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-8468186,EBI-398874; Score: 0.56
DE  Interaction: Q8WWB5; IntAct: EBI-10232538,EBI-398874; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-7116203,EBI-398874; Score: 0.56
DE  Interaction: P49639; IntAct: EBI-740785,EBI-398874; Score: 0.56
DE  Interaction: P49761; IntAct: EBI-745579,EBI-398874; Score: 0.56
DE  Interaction: Q6ZUT1; IntAct: EBI-3920396,EBI-398874; Score: 0.56
DE  Interaction: B2RXH4; IntAct: EBI-18298734,EBI-398874; Score: 0.56
DE  Interaction: P79522; IntAct: EBI-2803328,EBI-398874; Score: 0.56
DE  Interaction: P15622-3; IntAct: EBI-10177272,EBI-398874; Score: 0.56
DE  Interaction: Q9UK41-2; IntAct: EBI-12146727,EBI-398874; Score: 0.56
DE  Interaction: Q6NTE8; IntAct: EBI-2857471,EBI-398874; Score: 0.56
DE  Interaction: Q9BX10; IntAct: EBI-6115579,EBI-398874; Score: 0.56
DE  Interaction: Q13867; IntAct: EBI-718504,EBI-398874; Score: 0.56
DE  Interaction: P49760; IntAct: EBI-750020,EBI-398874; Score: 0.56
DE  Interaction: Q9BQ95; IntAct: EBI-712452,EBI-398874; Score: 0.56
DE  Interaction: Q96M83-3; IntAct: EBI-18211613,EBI-398874; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-398874; Score: 0.35
DE  Interaction: O15354; IntAct: EBI-15639515,EBI-398874; Score: 0.35
DE  Interaction: P22575; IntAct: EBI-866709,EBI-398874; Score: 0.62
DE  Interaction: Q16629; IntAct: EBI-398874,EBI-398885; Score: 0.67
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0042405;
GO  GO:0005643;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006405;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADEGKSYSEHDDERVNFPQRKKKGRGPFRWKYGEGNRRSGRGGSGIRSSRLEEDDGDVAMSDAQDGPRVRYNPYTTRPN
SQ  RRGDTWHDRDRIHVTVRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYENTRAQ
SQ  FFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVA
SQ  QNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNNRLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEEL
SQ  WLDGNSLCDTFRDQSTYISAIRERFPKLLRLDGHELPPPIAFDVEAPTTLPPCKGSYFGTENLKSLVLHFLQQYYAIYDS
SQ  GDRQGLLDAYHDGACCSLSIPFIPQNPARSSLAEYFKDSRNVKKLKDPTLRFRLLKHTRLNVVAFLNELPKTQHDVNSFV
SQ  VDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASSEEIQRAFAMPAPTPSSSPV
SQ  PTLSPEQQEMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTHLKAKGEIPEVAFMK
//
ID  Q9H0H0;
PN  Integrator complex subunit 2;
GN  INTS2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16239144}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23904267}.
DR  UNIPROT: Q9H0H0;
DR  UNIPROT: Q9ULD3;
DR  Pfam: PF14750;
DR  OMIM: 611346;
DR  DisGeNET: 57508;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
DE  Reference Proteome: Yes;
DE  Interaction: Q86WV6; IntAct: EBI-2800345,EBI-8471507; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-8471507; Score: 0.35
DE  Interaction: O43639; IntAct: EBI-8471507,EBI-713635; Score: 0.56
DE  Interaction: Q9H4E7; IntAct: EBI-8471507,EBI-745369; Score: 0.56
DE  Interaction: Q2TAC2-2; IntAct: EBI-8471507,EBI-10961624; Score: 0.56
DE  Interaction: P30153; IntAct: EBI-302388,EBI-8471507; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-712311,EBI-8471507; Score: 0.35
DE  Interaction: Q86XK7; IntAct: EBI-18323486,EBI-8471507; Score: 0.35
DE  Interaction: Q9NZQ7; IntAct: EBI-4314282,EBI-8471507; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-18539709,EBI-8471507; Score: 0.35
DE  Interaction: P16444; IntAct: EBI-749514,EBI-8471507; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-18636064,EBI-8471507; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-2875891,EBI-8471507; Score: 0.35
DE  Interaction: P46059; IntAct: EBI-21560873,EBI-8471507; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-1753048,EBI-8471507; Score: 0.35
DE  Interaction: P25445-6; IntAct: EBI-21766332,EBI-8471507; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671881,EBI-8471507; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0005622;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0034472;
GO  GO:0016180;
GO  GO:0042795;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKDQQTVIMTECTSLQFVSPFAFEAMQKVDVVCLASLSDPELRLLLPCLVRMALCAPADQSQSWAQDKKLILRLLSGVEA
SQ  VNSIVALLSVDFHALEQDASKEQQLRHKLGGGSGESILVSQLQHGLTLEFEHSDSPRRLRLVLSELLAIMNKVSESNGEF
SQ  FFKSSELFESPVYLEEAADVLCILQAELPSLLPIVDVAEALLHVRNGAWFLCLLVANVPDSFNEVCRGLIKNGERQDEES
SQ  LGGRRRTDALRFLCKMNPSQALKVRGMVVEECHLPGLGVALTLDHTKNEACEDGVSDLVCFVSGLLLGTNAKVRTWFGTF
SQ  IRNGQQRKRETSSSVLWQMRRQLLLELMGILPTVRSTRIVEEADVDMEPNVSVYSGLKEEHVVKASALLRLYCALMGIAG
SQ  LKPTEEEAEQLLQLMTSRPPATPAGVRFVSLSFCMLLAFSTLVSTPEQEQLMVVWLSWMIKEEAYFESTSGVSASFGEML
SQ  LLVAMYFHSNQLSAIIDLVCSTLGMKIVIKPSSLSRMKTIFTQEIFTEQVVTAHAVRVPVTSNLSANITGFLPIHCIYQL
SQ  LRSRSFTKHKVSIKDWIYRQLCETSTPLHPQLLPLIDVYINSILTPASKSNPEATNQPVTEQEILNIFQGVIGGDNIRLN
SQ  QRFSITAQLLVLYYILSYEEALLANTKTLAAMQRKPKSYSSSLMDQIPIKFLIRQAQGLQQELGGLHSALLRLLATNYPH
SQ  LCIVDDWICEEEITGTDALLRRMLLTNNAKNHSPKQLQEAFSAVPVNNTQVMQIIEHLTLLSASELIPYAEVLTSNMSQL
SQ  LNSGVPRRILQTVNKLWMVLNTVMPRRLWVMTVNALQPSIKFVRQQKYTQNDLMIDPLIVLRCDQRVHRCPPLMDITLHM
SQ  LNGYLLASKAYLSAHLKETEQDRPSQNNTIGLVGQTDAPEVTREELKNALLAAQDSAAVQILLEICLPTEEEKANGVNPD
SQ  SLLRNVQSVITTSAPNKGMEEGEDNLLCNLREVQCLICCLLHQMYIADPNIAKLVHFQGYPCELLPLTVAGIPSMHICLD
SQ  FIPELIAQPELEKQIFAIQLLSHLCIQYALPKSLSVARLAVNVMGTLLTVLTQAKRYAFFMPTLPSLVSFCRAFPPLYED
SQ  IMSLLIQIGQVCASDVATQTRDIDPIITRLQQIKEKPSGWSQICKDSSYKNGSRDTGSMDPDVQLCHCIERTVIEIINMS
SQ  VSGI
//
ID  P59044;
PN  NACHT, LRR and PYD domains-containing protein 6;
GN  NLRP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12387869}. Inflammasome {ECO:0000269|PubMed:12387869}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Nucleus membrane {ECO:0000250|UniProtKB:Q63035}.
DR  UNIPROT: P59044;
DR  UNIPROT: A8K9F3;
DR  UNIPROT: E9PJZ8;
DR  PDB: 6NCV;
DR  PDB: 6NDJ;
DR  Pfam: PF05729;
DR  Pfam: PF17776;
DR  Pfam: PF17779;
DR  Pfam: PF02758;
DR  PROSITE: PS50824;
DR  PROSITE: PS50837;
DR  OMIM: 609650;
DR  DisGeNET: 171389;
DE  Function: As the sensor component of the NLRP6 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP6, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. The precise NLRP6 activation stimulus has not been identified yet (By similarity) (PubMed:12387869). Essential for gut mucosal self-renewal and proliferation. Maintains intestinal homeostasis and a healthy intestinal microbiota. This function is, at least partially, mediated by IL18, and not IL1B, produced by nonhematopoietic cells. Influences intestinal barrier function and microbial homeostasis through the regulation of goblet cell mucus secretion. Acts by promoting autophagy in goblet cells, an essential step for mucus granule exocytosis. Its role in goblet cell physiology is inflammasome-dependent, but IL1B- and IL18-independent. During systemic bacterial infections, may negatively regulate inflammatory signaling and inhibit the influx of monocytes and neutrophils to the circulation and to the peritoneum. May promote peripheral nerve recovery following injury via an inflammasome- independent mechanism (By similarity). {ECO:0000250|UniProtKB:Q91WS2, ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:12387869}.
DE  Reference Proteome: Yes;
GO  GO:0061702;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0005000;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:0002862;
GO  GO:0034122;
GO  GO:0010506;
GO  GO:0050727;
GO  GO:0070255;
GO  GO:0009617;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQPEAPCSSTGPRLAVARELLLAALEELSQEQLKRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEV
SQ  ARKTLKRADARDVAAQLQERRLQRLGLGSGTLLSVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPE
SQ  EAMGPAEEPEPGRARRSDTHTFNRLFRRDEEGRRPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVDFAFFMPCGEL
SQ  LERPGTRSLADLILDQCPDRGAPVPQMLAQPQRLLFILDGADELPALGGPEAAPCTDPFEAASGARVLGGLLSKALLPTA
SQ  LLLVTTRAAAPGRLQGRLCSPQCAEVRGFSDKDKKKYFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQ
SQ  QLELGRDLSRTSKTTTSVYLLFITSVLSSAPVADGPRLQGDLRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFL
SQ  SKKELPGVLETEVTYQFIDQSFQEFLAALSYLLEDGGVPRTAAGGVGTLLRGDAQPHSHLVLTTRFLFGLLSAERMRDIE
SQ  RHFGCMVSERVKQEALRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCR
SQ  FPELALQRVRFCRMDVAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLF
SQ  QAMTDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQCRVQTVRVQLPDPQRG
SQ  LQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDG
SQ  HPQPPKELISTF
//
ID  Q12769;
PN  Nuclear pore complex protein Nup160;
GN  NUP160;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DR  UNIPROT: Q12769;
DR  UNIPROT: B4DYE8;
DR  UNIPROT: B4E2J9;
DR  UNIPROT: Q08AD3;
DR  UNIPROT: Q7Z5X6;
DR  UNIPROT: Q96GB3;
DR  UNIPROT: Q9H660;
DR  PDB: 5A9Q;
DR  OMIM: 607614;
DR  OMIM: 618178;
DR  DisGeNET: 23279;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:11564755, PubMed:11684705). Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DE  Disease: Nephrotic syndrome 19 (NPHS19) [MIM:618178]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS19 is an autosomal recessive, steroid-resistant form with onset in the first or second decade of life, resulting in chronic kidney disease. {ECO:0000269|PubMed:30179222, ECO:0000269|PubMed:30910934}. Note=The disease may be caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-295715; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-295715; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-286779,EBI-295715; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-1046596,EBI-295715; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295687,EBI-295715; Score: 0.53
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-295715; Score: 0.53
DE  Interaction: Q9NRI5; IntAct: EBI-295715,EBI-529989; Score: 0.55
DE  Interaction: P62508; IntAct: EBI-295715,EBI-2834260; Score: 0.56
DE  Interaction: Q7TSJ6; IntAct: EBI-6305003,EBI-295715; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-396018,EBI-295715; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-716392,EBI-295715; Score: 0.40
DE  Interaction: Q9P2Y5; IntAct: EBI-2952704,EBI-295715; Score: 0.35
DE  Interaction: O94966; IntAct: EBI-2511895,EBI-295715; Score: 0.40
DE  Interaction: O75317; IntAct: EBI-2511507,EBI-295715; Score: 0.40
DE  Interaction: Q8BH74; IntAct: EBI-2554056,EBI-295715; Score: 0.56
DE  Interaction: Q6PFD9; IntAct: EBI-646104,EBI-295715; Score: 0.56
DE  Interaction: Q9ERU9; IntAct: EBI-643756,EBI-295715; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-295715; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-8006911,EBI-295715; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-80180,EBI-295715; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-295715; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-295715; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-922818,EBI-295715; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-295715; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-295715; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-295715; Score: 0.35
DE  Interaction: Q8NBZ7-2; IntAct: EBI-21514721,EBI-295715; Score: 0.35
DE  Interaction: A8K8V0-2; IntAct: EBI-21612038,EBI-295715; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-1059321,EBI-295715; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-365996,EBI-295715; Score: 0.27
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-295715; Score: 0.35
DE  Interaction: Q9Y5V3; IntAct: EBI-295715,EBI-716006; Score: 0.40
DE  Interaction: P63000; IntAct: EBI-413628,EBI-295715; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-10249550,EBI-295715; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12577179,EBI-295715; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12561553,EBI-295715; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579807,EBI-295715; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-18539709,EBI-295715; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-4319734,EBI-295715; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-18052611,EBI-295715; Score: 0.35
DE  Interaction: Q9Y3B2; IntAct: EBI-295715,EBI-371892; Score: 0.37
DE  Interaction: Q8WUM0; IntAct: EBI-295695,EBI-295715; Score: 0.35
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0016925;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYS
SQ  ESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQT
SQ  VHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFV
SQ  LKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLM
SQ  VADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFA
SQ  LTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFC
SQ  RGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLL
SQ  KKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAE
SQ  QILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGV
SQ  HKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLS
SQ  VLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLE
SQ  CLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRL
SQ  QYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVV
SQ  LCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEK
SQ  QGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHD
SQ  PSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTK
SQ  ESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDA
SQ  VLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL
//
ID  P32567;
PN  Phosphatidic acid phosphohydrolase 1;
GN  PAH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
DR  UNIPROT: P32567;
DR  UNIPROT: D6VZY7;
DR  Pfam: PF04571;
DR  Pfam: PF08235;
DE  Function: Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation. {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16467296, ECO:0000269|PubMed:16968695, ECO:0000269|PubMed:17910939, ECO:0000269|PubMed:17971454, ECO:0000269|PubMed:20876142, ECO:0000269|PubMed:21081492, ECO:0000269|PubMed:21422231, ECO:0000269|PubMed:8437575}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-20589,EBI-17478; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-17478,EBI-8591; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-17478,EBI-8632; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-17478,EBI-8627; Score: 0.53
DE  Interaction: Q06677; IntAct: EBI-30084,EBI-17478; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-17478,EBI-8603; Score: 0.53
DE  Interaction: P16140; IntAct: EBI-17478,EBI-20254; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-17478,EBI-14372; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-17478,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-17478,EBI-18976; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-17478,EBI-9890; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0019898;
GO  GO:0005811;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005773;
GO  GO:0008195;
GO  GO:0044212;
GO  GO:0009060;
GO  GO:0009062;
GO  GO:0034389;
GO  GO:0008654;
GO  GO:0006276;
GO  GO:0019432;
GO  GO:0042144;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MQYVGRALGSVSKTWSSINPATLSGAIDVIVVEHPDGRLSCSPFHVRFGKFQILKPSQKKVQVFINEKLSNMPMKLSDSG
SQ  EAYFVFEMGDQVTDVPDELLVSPVMSATSSPPQSPETSILEGGTEGEGEGENENKKKEKKVLEEPDFLDINDTGDSGSKN
SQ  SETTGSLSPTESSTTTPPDSVEERKLVEQRTKNFQQKLNKKLTEIHIPSKLDNNGDLLLDTEGYKPNKNMMHDTDIQLKQ
SQ  LLKDEFGNDSDISSFIKEDKNGNIKIVNPYEHLTDLSPPGTPPTMATSGSVLGLDAMESGSTLNSLSSSPSGSDTEDETS
SQ  FSKEQSSKSEKTSKKGTAGSGETEKRYIRTIRLTNDQLKCLNLTYGENDLKFSVDHGKAIVTSKLFVWRWDVPIVISDID
SQ  GTITKSDALGHVLAMIGKDWTHLGVAKLFSEISRNGYNILYLTARSAGQADSTRSYLRSIEQNGSKLPNGPVILSPDRTM
SQ  AALRREVILKKPEVFKIACLNDIRSLYFEDSDNEVDTEEKSTPFFAGFGNRITDALSYRTVGIPSSRIFTINTEGEVHME
SQ  LLELAGYRSSYIHINELVDHFFPPVSLDSVDLRTNTSMVPGSPPNRTLDNFDSEITSGRKTLFRGNQEEKFTDVNFWRDP
SQ  LVDIDNLSDISNDDSDNIDEDTDVSQQSNISRNRANSVKTAKVTKAPQRNVSGSTNNNEVLAASSDVENASDLVSSHSSS
SQ  GSTPNKSTMSKGDIGKQIYLELGSPLASPKLRYLDDMDDEDSNYNRTKSRRASSAAATSIDKEFKKLSVSKAGAPTRIVS
SQ  KINVSNDVHSLGNSDTESRREQSVNETGRNQLPHNSMDDKDLDSRVSDEFDDDEFDEDEFED
//
ID  Q14542;
PN  Equilibrative nucleoside transporter 2;
GN  SLC29A2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Basolateral cell membrane {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein {ECO:0000269|PubMed:12527552}. Nucleus membrane {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein {ECO:0000269|PubMed:12527552}. Note=Localized at the basolateral cell membrane in polarized MDCK cells.
DR  UNIPROT: Q14542;
DR  UNIPROT: B3KPY7;
DR  UNIPROT: O43530;
DR  UNIPROT: Q52M84;
DR  UNIPROT: Q96R00;
DR  UNIPROT: Q9UPE0;
DR  Pfam: PF01733;
DR  OMIM: 602110;
DR  DisGeNET: 3177;
DE  Function: Mediates equilibrative transport of purine, pyrimidine nucleosides and the purine base hypoxanthine. Very less sensitive than SLC29A1 to inhibition by nitrobenzylthioinosine (NBMPR), dipyridamole, dilazep and draflazine. {ECO:0000269|PubMed:9396714}.
DE  Reference Proteome: Yes;
GO  GO:0016323;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005337;
GO  GO:0015853;
GO  GO:0015854;
GO  GO:0035344;
GO  GO:0098810;
GO  GO:0006139;
GO  GO:0015858;
GO  GO:0035364;
GO  GO:0015862;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNNWVTLLSQLPLL
SQ  LFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYS
SQ  TLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAE
SQ  LLQSDENGIPSSPQKVALTLDLDLEKEPESEPDEPQKPGKPSVFTVFQKIWLTALCLVLVFTVTLSVFPAITAMVTSSTS
SQ  PGKWSQFFNPICCFLLFNIMDWLGRSLTSYFLWPDEDSRLLPLLVCLRFLFVPLFMLCHVPQRSRLPILFPQDAYFITFM
SQ  LLFAVSNGYLVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
//
ID  Q9V3J4;
PN  Protein SEC13 homolog;
GN  Sec13;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20144761}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20144761}. Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000305|PubMed:27166823}. Note=Localizes to chromatin, specifically to areas undergoing transcriptional activation. Chromatin localization is independent of the nuclear pore complex (PubMed:20144761).
DR  UNIPROT: Q9V3J4;
DR  UNIPROT: Q7KLW8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Recruited to transcriptionally active chromatin at the time of transcription initiation by RNA polymerase II (PubMed:20144761). Required for proper expression of ecdysone-responsive genes such as Eip74EF and Eip75B during larval development (PubMed:20144761). Required for reactivation of transcription after heat shock (PubMed:20144761). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:20547758}. A component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development (PubMed:27166823). {ECO:0000269|PubMed:27166823}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24323; IntAct: EBI-167965,EBI-169056; Score: 0.35
DE  Interaction: Q7KN04; IntAct: EBI-94713,EBI-169056; Score: 0.35
DE  Interaction: A1Z7J7; IntAct: EBI-169056,EBI-155002; Score: 0.37
DE  Interaction: Q9VPR6; IntAct: EBI-169056,EBI-83394; Score: 0.37
DE  Interaction: Q9VM98; IntAct: EBI-169056,EBI-134049; Score: 0.37
GO  GO:0000785;
GO  GO:0030127;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0000139;
GO  GO:0005765;
GO  GO:0005815;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005703;
GO  GO:0035859;
GO  GO:0003682;
GO  GO:0005198;
GO  GO:0034605;
GO  GO:0035293;
GO  GO:0090114;
GO  GO:0035077;
GO  GO:0008363;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0045944;
GO  GO:0060261;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MVSLLQEIDTEHEDMVHHAALDFYGLLLATCSSDGSVRIFHSRKNNKALAELKGHQGPVWQVAWAHPKFGNILASCSYDR
SQ  KVIVWKSTTPRDWTKLYEYSNHDSSVNSVDFAPSEYGLVLACASSDGSVSVLTCNTEYGVWDAKKIPNAHTIGVNAISWC
SQ  PAQAPDPAFDQRVTSRSAAVKRLVSGGCDNLVKIWREDNDRWVEEHRLEAHSDWVRDVAWAPSIGLPRSQIATASQDRHV
SQ  IVWSSNADLSEWTSTVLHTFDDAVWSISWSTTGNILAVTGGDNNVTLWKENTEGQWIRINYESGTAIQSKQPSHLPHSHS
SQ  QQQQALQQHQQQAPSHPGPSSDSEHSSNLSNSQLSN
//
ID  Q5JVF3;
PN  PCI domain-containing protein 2;
GN  PCID2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}.
DR  UNIPROT: Q5JVF3;
DR  UNIPROT: A6NK09;
DR  UNIPROT: Q3ZCX1;
DR  UNIPROT: Q5TC57;
DR  UNIPROT: Q5TC58;
DR  UNIPROT: Q9H7K1;
DR  UNIPROT: Q9HBZ7;
DR  UNIPROT: Q9NUK6;
DR  UNIPROT: Q9NVY1;
DR  UNIPROT: Q9NW44;
DR  UNIPROT: Q9NWH3;
DR  PDB: 3T5X;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DR  OMIM: 613713;
DR  DisGeNET: 55795;
DE  Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:22307388) (Probable). Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability. R-loop accumulation does not increase in PCID2-depleted cells (PubMed:24896180). {ECO:0000250|UniProtKB:Q8BFV2, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180, ECO:0000305|PubMed:23591820}.
DE  Reference Proteome: Yes;
DE  Interaction: P49336; IntAct: EBI-394377,EBI-1051701; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-448665,EBI-1051701; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1051701; Score: 0.35
DE  Interaction: Q9UKT9; IntAct: EBI-1051701,EBI-747204; Score: 0.56
DE  Interaction: Q8XA11; IntAct: EBI-10038919,EBI-1051701; Score: 0.37
DE  Interaction: P62753; IntAct: EBI-356625,EBI-1051701; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-1051701; Score: 0.35
DE  Interaction: P60896; IntAct: EBI-1051701,EBI-79819; Score: 0.56
DE  Interaction: Q99AU3; IntAct: EBI-6150155,EBI-1051701; Score: 0.35
DE  Interaction: C3W5S7; IntAct: EBI-6152135,EBI-1051701; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-2547442,EBI-1051701; Score: 0.35
DE  Interaction: Q9WPI5; IntAct: EBI-6149678,EBI-1051701; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-1051701; Score: 0.35
DE  Interaction: Q9HC98; IntAct: EBI-1051701,EBI-740364; Score: 0.40
DE  Interaction: Q13418; IntAct: EBI-1051701,EBI-747644; Score: 0.40
DE  Interaction: Q9HAW0; IntAct: EBI-1051701,EBI-1055224; Score: 0.40
DE  Interaction: Q53F19; IntAct: EBI-6657994,EBI-1051701; Score: 0.35
DE  Interaction: Q96PV6; IntAct: EBI-1051701,EBI-739546; Score: 0.56
DE  Interaction: C5E524; IntAct: EBI-12561527,EBI-1051701; Score: 0.35
DE  Interaction: Q194T2; IntAct: EBI-11515076,EBI-1051701; Score: 0.35
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0043066;
GO  GO:2000117;
GO  GO:0071033;
GO  GO:0016973;
GO  GO:0045579;
GO  GO:0090267;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0043488;
GO  GO:0048536;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEA
SQ  YKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGI
SQ  EDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHC
SQ  HRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEAFFIRCGIFLILEKLKII
SQ  TYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
//
ID  Q09825;
PN  Spindle pole body-associated protein sad1;
GN  sad1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: Q09825;
DR  UNIPROT: Q9UU40;
DR  PDB: 6A6W;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres. {ECO:0000269|PubMed:16615890}.
DE  Reference Proteome: Yes;
DE  Interaction: O13712; IntAct: EBI-1542405,EBI-929731; Score: 0.55
DE  Interaction: Self; IntAct: EBI-929731,EBI-929731; Score: 0.55
DE  Interaction: Q92358; IntAct: EBI-929731,EBI-929655; Score: 0.46
DE  Interaction: Q9US52; IntAct: EBI-929731,EBI-929651; Score: 0.32
DE  Interaction: O13787; IntAct: EBI-21242328,EBI-929731; Score: 0.37
DE  Interaction: Q10322; IntAct: EBI-1125055,EBI-929731; Score: 0.37
DE  Interaction: P10815; IntAct: EBI-929731,EBI-1187843; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0061497;
GO  GO:0005639;
GO  GO:0031021;
GO  GO:0034993;
GO  GO:0035974;
GO  GO:0005874;
GO  GO:0044732;
GO  GO:0071958;
GO  GO:0005635;
GO  GO:0071957;
GO  GO:0035861;
GO  GO:0043495;
GO  GO:0051301;
GO  GO:0072766;
GO  GO:0071790;
GO  GO:0032121;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSN
SQ  IRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRK
SQ  SQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKV
SQ  GGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLS
SQ  TGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEH
SQ  VQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQ
SQ  VRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS
//
ID  P35658;
PN  Nuclear pore complex protein Nup214;
GN  NUP214;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8108440}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000269|PubMed:8108440}.
DR  UNIPROT: P35658;
DR  UNIPROT: A6NFQ0;
DR  UNIPROT: Q15010;
DR  UNIPROT: Q3KQZ0;
DR  UNIPROT: Q5JUP7;
DR  UNIPROT: Q75R47;
DR  UNIPROT: Q86XD3;
DR  PDB: 2OIT;
DR  PDB: 3FHC;
DR  PDB: 3FMO;
DR  PDB: 3FMP;
DR  PDB: 5DIS;
DR  Pfam: PF18617;
DR  OMIM: 114350;
DR  OMIM: 618426;
DR  DisGeNET: 8021;
DE  Function: Has a critical role in nucleocytoplasmic transport (PubMed:31178128). May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (PubMed:31178128, PubMed:8108440). {ECO:0000269|PubMed:31178128, ECO:0000303|PubMed:8108440}.
DE  Disease: Note=A chromosomal aberration involving NUP214 is found in a subset of acute myeloid leukemia (AML); also known as acute non- lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It results in the formation of a DEK-CAN fusion gene. {ECO:0000269|PubMed:1549122}. Note=A chromosomal aberration involving NUP214 is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with SET. {ECO:0000269|PubMed:1630450}. Encephalopathy, acute, infection-induced, 9 (IIAE9) [MIM:618426]: An autosomal recessive disorder characterized by infancy- onset of episodic neurodevelopmental regression in association with infection-induced febrile illness. Clinical features include poor overall growth, seizures, myoclonic jerks, microcephaly, ataxia, and cerebellar atrophy. {ECO:0000269|PubMed:30758658, ECO:0000269|PubMed:31178128}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q6UXB4; IntAct: EBI-2114729,EBI-1222270; Score: 0.37
DE  Interaction: Q9GZM8; IntAct: EBI-1222270,EBI-928842; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-395506,EBI-1222270; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-1222270; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-727707,EBI-1222270; Score: 0.37
DE  Interaction: Q5NFS5; IntAct: EBI-1222270,EBI-2797271; Score: 0.37
DE  Interaction: Q80U93; IntAct: EBI-2551193,EBI-1222270; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2552999,EBI-1222270; Score: 0.40
DE  Interaction: Q9UN86; IntAct: EBI-1044298,EBI-1222270; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-1047359,EBI-1222270; Score: 0.40
DE  Interaction: P24386; IntAct: EBI-2515129,EBI-1222270; Score: 0.40
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-1222270; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-1222270; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-1222270; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-1222270; Score: 0.35
DE  Interaction: Q8D1L8; IntAct: EBI-1222270,EBI-2862395; Score: 0.37
DE  Interaction: Q81KT8; IntAct: EBI-1222270,EBI-2809955; Score: 0.37
DE  Interaction: Q5NGV7; IntAct: EBI-2796192,EBI-1222270; Score: 0.37
DE  Interaction: A0A2S9PJQ7; IntAct: EBI-2846239,EBI-1222270; Score: 0.37
DE  Interaction: A0A2P0HLN8; IntAct: EBI-1222270,EBI-2810906; Score: 0.37
DE  Interaction: P01857; IntAct: EBI-356114,EBI-1222270; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-726178,EBI-1222270; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475877,EBI-1222270; Score: 0.35
DE  Interaction: Q15811; IntAct: EBI-602041,EBI-1222270; Score: 0.35
DE  Interaction: Q3KR16-1; IntAct: EBI-25408239,EBI-1222270; Score: 0.35
DE  Interaction: Q9Y4F1; IntAct: EBI-5235630,EBI-1222270; Score: 0.35
DE  Interaction: Q63358; IntAct: EBI-6251137,EBI-1222270; Score: 0.35
GO  GO:1990876;
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005049;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0075733;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0016925;
GO  GO:0051726;
GO  GO:1900034;
GO  GO:0060964;
GO  GO:0006110;
GO  GO:0043488;
GO  GO:0046822;
GO  GO:0006405;
GO  GO:0006409;
GO  GO:0016032;
GO  GO:0019083;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGLVFAGGASGLQIFPTKNLLIQNKPGDDPNKI
SQ  VDKVQGLLVPMKFPIHHLALSCDNLTLSACMMSSEYGSIIAFFDVRTFSNEAKQQKRPFAYHKLLKDAGGMVIDMKWNPT
SQ  VPSMVAVCLADGSIAVLQVTETVKVCATLPSTVAVTSVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHP
SQ  VRVLDVLWIGTYVFAIVYAAADGTLETSPDVVMALLPKKEEKHPEIFVNFMEPCYGSCTERQHHYYLSYIEEWDLVLAAS
SQ  AASTEVSILARQSDQINWESWLLEDSSRAELPVTDKSDDSLPMGVVVDYTNQVEITISDEKTLPPAPVLMLLSTDGVLCP
SQ  FYMINQNPGVKSLIKTPERLSLEGERQPKSPGSTPTTPTSSQAPQKLDASAAAAPASLPPSSPAAPIATFSLLPAGGAPT
SQ  VFSFGSSSLKSSATVTGEPPSYSSGSDSSKAAPGPGPSTFSFVPPSKASLAPTPAASPVAPSAASFSFGSSGFKPTLEST
SQ  PVPSVSAPNIAMKPSFPPSTSAVKVNLSEKFTAAATSTPVSSSQSAPPMSPFSSASKPAASGPLSHPTPLSAPPSSVPLK
SQ  SSVLPSPSGRSAQGSSSPVPSMVQKSPRITPPAAKPGSPQAKSLQPAVAEKQGHQWKDSDPVMAGIGEEIAHFQKELEEL
SQ  KARTSKACFQVGTSEEMKMLRTESDDLHTFLLEIKETTESLHGDISSLKTTLLEGFAGVEEAREQNERNRDSGYLHLLYK
SQ  RPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDQHLEQKKKQRHLLVPERETLFNTLANNREIINQQRKRLNHLVD
SQ  SLQQLRLYKQTSLWSLSSAVPSQSSIHSFDSDLESLCNALLKTTIESHTKSLPKVPAKLSPMKQAQLRNFLAKRKTPPVR
SQ  STAPASLSRSAFLSQRYYEDLDEVSSTSSVSQSLESEDARTSCKDDEAVVQAPRHAPVVRTPSIQPSLLPHAAPFAKSHL
SQ  VHGSSPGVMGTSVATSASKIIPQGADSTMLATKTVKHGAPSPSHPISAPQAAAAAALRRQMASQAPAVNTLTESTLKNVP
SQ  QVVNVQELKNNPATPSTAMGSSVPYSTAKTPHPVLTPVAANQAKQGSLINSLKPSGPTPASGQLSSGDKASGTAKIETAV
SQ  TSTPSASGQFSKPFSFSPSGTGFNFGIITPTPSSNFTAAQGATPSTKESSQPDAFSSGGGSKPSYEAIPESSPPSGITSA
SQ  SNTTPGEPAASSSRPVAPSGTALSTTSSKLETPPSKLGELLFPSSLAGETLGSFSGLRVGQADDSTKPTNKASSTSLTST
SQ  QPTKTSGVPSGFNFTAPPVLGKHTEPPVTSSATTTSVAPPAATSTSSTAVFGSLPVTSAGSSGVISFGGTSLSAGKTSFS
SQ  FGSQQTNSTVPPSAPPPTTAATPLPTSFPTLSFGSLLSSATTPSLPMSAGRSTEEATSSALPEKPGDSEVSASAASLLEE
SQ  QQSAQLPQAPPQTSDSVKKEPVLAQPAVSNSGTAASSTSLVALSAEATPATTGVPDARTEAVPPASSFSVPGQTAVTAAA
SQ  ISSAGPVAVETSSTPIASSTTSIVAPGPSAEAAAFGTVTSGSSVFAQPPAASSSSAFNQLTNNTATAPSATPVFGQVAAS
SQ  TAPSLFGQQTGSTASTAAATPQVSSSGFSSPAFGTTAPGVFGQTTFGQASVFGQSASSAASVFSFSQPGFSSVPAFGQPA
SQ  SSTPTSTSGSVFGAASSTSSSSSFSFGQSSPNTGGGLFGQSNAPAFGQSPGFGQGGSVFGGTSAATTTAATSGFSFCQAS
SQ  GFGSSNTGSVFGQAASTGGIVFGQQSSSSSGSVFGSGNTGRGGGFFSGLGGKPSQDAANKNPFSSASGGFGSTATSNTSN
SQ  LFGNSGAKTFGGFASSSFGEQKPTGTFSSGGGSVASQGFGFSSPNKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAF
SQ  TSPLGSTGGKVFGEGTAAASAGGFGFGSSSNTTSFGTLASQNAPTFGSLSQQTSGFGTQSSGFSGFGSGTGGFSFGSNNS
SQ  SVQGFGGWRS
//
ID  F4I1T7;
PN  Nuclear pore complex protein NUP214;
GN  NUP214;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4I1T7;
DR  UNIPROT: F4I1T6;
DR  UNIPROT: Q94C88;
DR  UNIPROT: Q9ZVV0;
DE  Function: Required for normal embryogenesis and seed viability. Involved in the first asymmetrical cell division of the zygote. Regulates the number and planes of cell divisions required for generating the normal embryo proper and suspensor, apical-basal axis, cotyledons and meristem. {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:22898497}.
DE  Reference Proteome: Yes;
GO  GO:0005739;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0009793;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0010070;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNS
SQ  NGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKH
SQ  SYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVD
SQ  SIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLA
SQ  VTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPY
SQ  FVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQ
SQ  RLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKL
SQ  QKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTG
SQ  YVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGP
SQ  LRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDK
SQ  TIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARR
SQ  GVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNA
SQ  SSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSE
SQ  RLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSN
SQ  TTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFES
SQ  SKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIP
SQ  ISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSL
SQ  FPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQ
SQ  STVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASS
SQ  PTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSG
SQ  ELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGG
SQ  SNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGF
SQ  GGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK
//
ID  Q84K11;
PN  Serine/threonine-protein phosphatase 5;
GN  PP5;
OS  4081;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. [Isoform 2]: Cytoplasm. Nucleus, nucleoplasm. Nucleus speckle. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with phytochromes into speckles. {ECO:0000250}.
DR  UNIPROT: Q84K11;
DR  UNIPROT: Q8H1H4;
DR  Pfam: PF00149;
DR  Pfam: PF08321;
DR  Pfam: PF00515;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses (By similarity). Can use para-nitrophenylphosphate (pNPP) and phosphorylated casein as substrate at pH 7.5 and 5.0. {ECO:0000250, ECO:0000269|PubMed:12972652}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0009506;
GO  GO:0046872;
GO  GO:0004722;
GO  GO:0046906;
GO  GO:0010019;
GO  GO:1902325;
GO  GO:0010017;
GO  GO:0046686;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPGMEAENSNASRAEELKQLANEAFKGHKYSQAIDLYTQAIELNGENAVYYANRAFAHTKLEEYGSAIQDGTRAIEIDPR
SQ  YSKGYYRRGAAYLAMGKFKDALKDFQQVKKLCPNDPDATKKLKECEKAVMKLKFEEAISVPESQRRSVADSIDYRSVGSG
SQ  PGSSYVPTKTTAVSAAAALMGVLVVYMGTKAATMVAAAASAALLVVLITFLWGRCSDGFFTKSRTLELEVEPQYAGARIE
SQ  GDVVTLDFVKKMLDDFKNQKNLHKRYAYQIVLQTREMLRALPSLVDIVVPEGKHFTVCGDVHGQFYDLLNIFELNGLPSE
SQ  DNPYLFNGDFVDRGSFSLEVILTLFAFKCMCPSAIHLARGNHESKSMNKIYGFEGEVRSKLSEIFVELFAEVFCCLPLAH
SQ  VINEKVFVVHGGLFSVDGVKLSDIRAIDRFCEPPEEGLMCELLWSDPQPQPGRGPSKRGVGLSFGGDVTKRFLQENNLDL
SQ  VVRSHEVKDEGYEIEHDGKLITVFSAPNYCDQMGNKGAFIRFEAPDMKPNIVTFSAVPHPDVKPMAYANNFLRMFS
//
ID  O00159;
PN  Unconventional myosin-Ic;
GN  MYO1C;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:22736583}. Nucleus {ECO:0000269|PubMed:22736583}. Note=Colocalizes with RNA polymerase II. Absent from nucleoli and does not colocalize with RNA polymerase I. Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription. [Isoform 2]: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, stereocilium membrane {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity). {ECO:0000250}. [Isoform 3]: Nucleus, nucleoplasm. Nucleus, nucleolus. Nucleus, nuclear pore complex. Note=Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli (By similarity). In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level. {ECO:0000250}.
DR  UNIPROT: O00159;
DR  UNIPROT: Q4LE56;
DR  UNIPROT: Q6NVJ7;
DR  UNIPROT: Q86Y95;
DR  PDB: 4BYF;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF06017;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS51757;
DR  OMIM: 606538;
DR  DisGeNET: 4641;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. {ECO:0000269|PubMed:24636949}. Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P32121; IntAct: EBI-714559,EBI-350423; Score: 0.35
DE  Interaction: P49407; IntAct: EBI-743313,EBI-350423; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-350423; Score: 0.53
DE  Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-350423; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-351007,EBI-350423; Score: 0.35
DE  Interaction: P25786; IntAct: EBI-359352,EBI-350423; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-350423; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-714746,EBI-350423; Score: 0.35
DE  Interaction: P29353; IntAct: EBI-78835,EBI-350423; Score: 0.35
DE  Interaction: Q9Y2K6; IntAct: EBI-2511991,EBI-350423; Score: 0.40
DE  Interaction: Q8IY92; IntAct: EBI-2370740,EBI-350423; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-350423; Score: 0.46
DE  Interaction: P03372; IntAct: EBI-78473,EBI-350423; Score: 0.46
DE  Interaction: Q9UH99; IntAct: EBI-1044964,EBI-350423; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-949059,EBI-350423; Score: 0.35
DE  Interaction: Q8IXM2; IntAct: EBI-350423,EBI-4280811; Score: 0.35
DE  Interaction: Q8N726; IntAct: EBI-350423,EBI-625922; Score: 0.35
DE  Interaction: Q7Z7F7; IntAct: EBI-350423,EBI-7825445; Score: 0.35
DE  Interaction: Q96BQ5; IntAct: EBI-350423,EBI-7219131; Score: 0.35
DE  Interaction: Q9UPN6; IntAct: EBI-350423,EBI-7954236; Score: 0.35
DE  Interaction: Q6P4F7; IntAct: EBI-350423,EBI-7543265; Score: 0.35
DE  Interaction: P21333-2; IntAct: EBI-350423,EBI-9641086; Score: 0.35
DE  Interaction: O95425-2; IntAct: EBI-350423,EBI-10965323; Score: 0.35
DE  Interaction: P23528; IntAct: EBI-350423,EBI-352733; Score: 0.35
DE  Interaction: Q8N9B5-2; IntAct: EBI-350423,EBI-10268138; Score: 0.35
DE  Interaction: Q14151; IntAct: EBI-350423,EBI-352869; Score: 0.35
DE  Interaction: P52756; IntAct: EBI-350423,EBI-714003; Score: 0.35
DE  Interaction: Q6PJ61; IntAct: EBI-350423,EBI-2322982; Score: 0.35
DE  Interaction: O95425; IntAct: EBI-350423,EBI-487145; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-350423,EBI-743375; Score: 0.35
DE  Interaction: Q8N302; IntAct: EBI-350423,EBI-747899; Score: 0.35
DE  Interaction: Q9BWT7; IntAct: EBI-350423,EBI-3866279; Score: 0.35
DE  Interaction: Q9Y2T2; IntAct: EBI-350423,EBI-2371151; Score: 0.35
DE  Interaction: P55884; IntAct: EBI-350423,EBI-366696; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-350423,EBI-351479; Score: 0.35
DE  Interaction: O75528; IntAct: EBI-350423,EBI-473249; Score: 0.35
DE  Interaction: O60292; IntAct: EBI-350423,EBI-2559690; Score: 0.35
DE  Interaction: Q9P0K7-3; IntAct: EBI-350423,EBI-10977843; Score: 0.35
DE  Interaction: P11233; IntAct: EBI-350423,EBI-1036803; Score: 0.35
DE  Interaction: G3V1L9; IntAct: EBI-350423,EBI-10969999; Score: 0.35
DE  Interaction: Q9Y5J9; IntAct: EBI-350423,EBI-1049085; Score: 0.35
DE  Interaction: Q6IBS0; IntAct: EBI-350423,EBI-722204; Score: 0.35
DE  Interaction: P52943; IntAct: EBI-350423,EBI-947590; Score: 0.35
DE  Interaction: Q92828; IntAct: EBI-350423,EBI-2835660; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-350423,EBI-352614; Score: 0.35
DE  Interaction: Q27J81-2; IntAct: EBI-350423,EBI-11025144; Score: 0.35
DE  Interaction: O75128; IntAct: EBI-350423,EBI-3446582; Score: 0.35
DE  Interaction: Q0ZGT2-4; IntAct: EBI-350423,EBI-10977819; Score: 0.35
DE  Interaction: Q9Y4F1; IntAct: EBI-350423,EBI-5235630; Score: 0.35
DE  Interaction: Q96I25; IntAct: EBI-350423,EBI-740272; Score: 0.35
DE  Interaction: O15042-2; IntAct: EBI-350423,EBI-10973137; Score: 0.35
DE  Interaction: Q9NR12; IntAct: EBI-350423,EBI-350517; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-350423,EBI-1059012; Score: 0.35
DE  Interaction: Q8TB52; IntAct: EBI-350423,EBI-2556210; Score: 0.35
DE  Interaction: Q8WYL5; IntAct: EBI-350423,EBI-1222387; Score: 0.35
DE  Interaction: O14974; IntAct: EBI-350423,EBI-351726; Score: 0.35
DE  Interaction: Q9Y281; IntAct: EBI-350423,EBI-351218; Score: 0.35
DE  Interaction: O75533; IntAct: EBI-350423,EBI-876542; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-350423,EBI-351394; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-350423,EBI-353389; Score: 0.35
DE  Interaction: P26583; IntAct: EBI-350423,EBI-1057009; Score: 0.35
DE  Interaction: O43795-2; IntAct: EBI-350423,EBI-10965344; Score: 0.35
DE  Interaction: Q0ZGT2-2; IntAct: EBI-350423,EBI-11030061; Score: 0.35
DE  Interaction: Q96FS4; IntAct: EBI-350423,EBI-1054981; Score: 0.35
DE  Interaction: B4E1Q4; IntAct: EBI-350423,EBI-11030799; Score: 0.35
DE  Interaction: Q96RN5-2; IntAct: EBI-350423,EBI-11030807; Score: 0.35
DE  Interaction: Q9H2D6-5; IntAct: EBI-350423,EBI-1023227; Score: 0.35
DE  Interaction: Q9Y6N5; IntAct: EBI-350423,EBI-1170418; Score: 0.35
DE  Interaction: O94875; IntAct: EBI-350423,EBI-311323; Score: 0.35
DE  Interaction: O15143; IntAct: EBI-350423,EBI-1044647; Score: 0.35
DE  Interaction: Q86SQ0; IntAct: EBI-350423,EBI-2798483; Score: 0.35
DE  Interaction: P28289; IntAct: EBI-350423,EBI-2659631; Score: 0.35
DE  Interaction: Q71RC2; IntAct: EBI-350423,EBI-2878091; Score: 0.35
DE  Interaction: Q9H0L4; IntAct: EBI-350423,EBI-747012; Score: 0.35
DE  Interaction: P0DP23; IntAct: EBI-350423,EBI-397435; Score: 0.35
DE  Interaction: Q13813; IntAct: EBI-350423,EBI-351450; Score: 0.35
DE  Interaction: Q13435; IntAct: EBI-350423,EBI-749111; Score: 0.35
DE  Interaction: O14639-3; IntAct: EBI-350423,EBI-11030070; Score: 0.35
DE  Interaction: Q0ZGT2; IntAct: EBI-350423,EBI-351705; Score: 0.35
DE  Interaction: Q96N67-4; IntAct: EBI-350423,EBI-11017737; Score: 0.35
DE  Interaction: Q12792; IntAct: EBI-350423,EBI-1056675; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-350423,EBI-6657994; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-350423,EBI-351384; Score: 0.35
DE  Interaction: Q9Y5L4; IntAct: EBI-350423,EBI-1057344; Score: 0.35
DE  Interaction: P80723; IntAct: EBI-350423,EBI-358583; Score: 0.35
DE  Interaction: E9PR71; IntAct: EBI-350423,EBI-11030795; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-350423,EBI-357253; Score: 0.35
DE  Interaction: Q93074-3; IntAct: EBI-350423,EBI-11030781; Score: 0.35
DE  Interaction: Q5M775; IntAct: EBI-350423,EBI-350473; Score: 0.35
DE  Interaction: Q155Q3; IntAct: EBI-350423,EBI-1104700; Score: 0.35
DE  Interaction: Q01082-3; IntAct: EBI-350423,EBI-4400743; Score: 0.35
DE  Interaction: Q9UHB6-4; IntAct: EBI-350423,EBI-10977805; Score: 0.35
DE  Interaction: Q9H0G5; IntAct: EBI-350423,EBI-5464397; Score: 0.35
DE  Interaction: Q8WX93; IntAct: EBI-350423,EBI-2803991; Score: 0.35
DE  Interaction: Q7Z460; IntAct: EBI-350423,EBI-913476; Score: 0.35
DE  Interaction: A1L390; IntAct: EBI-350423,EBI-4401429; Score: 0.35
DE  Interaction: Q8IVT2; IntAct: EBI-350423,EBI-2555085; Score: 0.35
DE  Interaction: Q6WCQ1-2; IntAct: EBI-350423,EBI-10965272; Score: 0.35
DE  Interaction: P35611-2; IntAct: EBI-350423,EBI-11030777; Score: 0.35
DE  Interaction: Q13347; IntAct: EBI-350423,EBI-354047; Score: 0.35
DE  Interaction: Q9BSF4; IntAct: EBI-350423,EBI-10974729; Score: 0.35
DE  Interaction: Q9NVS9; IntAct: EBI-350423,EBI-11030787; Score: 0.35
DE  Interaction: O75083; IntAct: EBI-350423,EBI-351917; Score: 0.35
DE  Interaction: P60981; IntAct: EBI-350423,EBI-745191; Score: 0.35
DE  Interaction: Q9H3U1-2; IntAct: EBI-350423,EBI-10977801; Score: 0.35
DE  Interaction: Q7Z4V5; IntAct: EBI-350423,EBI-1049136; Score: 0.35
DE  Interaction: Q6IN84; IntAct: EBI-350423,EBI-5454865; Score: 0.35
DE  Interaction: Q8IWX8; IntAct: EBI-350423,EBI-2555370; Score: 0.35
DE  Interaction: J3KP15; IntAct: EBI-350423,EBI-11030773; Score: 0.35
DE  Interaction: P28290; IntAct: EBI-350423,EBI-722905; Score: 0.35
DE  Interaction: O15145; IntAct: EBI-350423,EBI-351829; Score: 0.35
DE  Interaction: Q01082; IntAct: EBI-350423,EBI-351561; Score: 0.35
DE  Interaction: Q9UDY2; IntAct: EBI-350423,EBI-1042602; Score: 0.35
DE  Interaction: Q96EV2; IntAct: EBI-350423,EBI-1210748; Score: 0.35
DE  Interaction: Q5T5U3; IntAct: EBI-350423,EBI-1642518; Score: 0.35
DE  Interaction: P20839; IntAct: EBI-350423,EBI-2866691; Score: 0.35
DE  Interaction: P35269; IntAct: EBI-350423,EBI-457886; Score: 0.35
DE  Interaction: O15020; IntAct: EBI-350423,EBI-308449; Score: 0.35
DE  Interaction: Q13045; IntAct: EBI-350423,EBI-351549; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-350423,EBI-2505886; Score: 0.35
DE  Interaction: Q8IX12-2; IntAct: EBI-350423,EBI-10972011; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-400906,EBI-350423; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-375096,EBI-350423; Score: 0.35
DE  Interaction: P98175-2; IntAct: EBI-350423,EBI-10974418; Score: 0.35
DE  Interaction: Q9Y4I1-2; IntAct: EBI-350423,EBI-10965332; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-350423,EBI-762451; Score: 0.35
DE  Interaction: Q13838; IntAct: EBI-350423,EBI-348622; Score: 0.35
DE  Interaction: Q8WW12; IntAct: EBI-350423,EBI-10972020; Score: 0.35
DE  Interaction: Q8N573-2; IntAct: EBI-350423,EBI-11030811; Score: 0.35
DE  Interaction: P63261; IntAct: EBI-350423,EBI-351292; Score: 0.35
DE  Interaction: Q4KMQ1; IntAct: EBI-350423,EBI-3942777; Score: 0.35
DE  Interaction: Q9Y2X0-2; IntAct: EBI-350423,EBI-10970047; Score: 0.35
DE  Interaction: O43707; IntAct: EBI-350423,EBI-351526; Score: 0.35
DE  Interaction: Q8N556; IntAct: EBI-350423,EBI-3893163; Score: 0.35
DE  Interaction: Q9BQ61; IntAct: EBI-350423,EBI-744881; Score: 0.35
DE  Interaction: Q8N3V7-2; IntAct: EBI-350423,EBI-10965260; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-10983249,EBI-350423; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-350423; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-350423; Score: 0.35
DE  Interaction: Q15051; IntAct: EBI-2805823,EBI-350423; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-2547442,EBI-350423; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-350423,EBI-725145; Score: 0.40
DE  Interaction: Q14240; IntAct: EBI-73473,EBI-350423; Score: 0.40
DE  Interaction: O14908; IntAct: EBI-350423,EBI-373132; Score: 0.40
DE  Interaction: Q9Y5J5; IntAct: EBI-350423,EBI-1055859; Score: 0.40
DE  Interaction: Q9HC98; IntAct: EBI-350423,EBI-740364; Score: 0.40
DE  Interaction: O75365; IntAct: EBI-350423,EBI-1043866; Score: 0.40
DE  Interaction: Q9P2S5; IntAct: EBI-350423,EBI-1054904; Score: 0.40
DE  Interaction: O75368; IntAct: EBI-2854777,EBI-350423; Score: 0.35
DE  Interaction: P20936; IntAct: EBI-1026476,EBI-350423; Score: 0.35
DE  Interaction: O60496; IntAct: EBI-1046024,EBI-350423; Score: 0.35
DE  Interaction: P17252; IntAct: EBI-1383528,EBI-350423; Score: 0.35
DE  Interaction: P28324; IntAct: EBI-11277718,EBI-350423; Score: 0.35
DE  Interaction: Q8IZP0; IntAct: EBI-375446,EBI-350423; Score: 0.35
DE  Interaction: Q15139; IntAct: EBI-1181072,EBI-350423; Score: 0.35
DE  Interaction: Q13115; IntAct: EBI-6591081,EBI-350423; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-355924,EBI-350423; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-350989,EBI-350423; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-350423; Score: 0.35
DE  Interaction: P17706-3; IntAct: EBI-14013987,EBI-350423; Score: 0.35
DE  Interaction: P30307; IntAct: EBI-974439,EBI-350423; Score: 0.35
DE  Interaction: Q14761; IntAct: EBI-722217,EBI-350423; Score: 0.35
DE  Interaction: Q16829; IntAct: EBI-1265847,EBI-350423; Score: 0.35
DE  Interaction: Q8NI37; IntAct: EBI-9089276,EBI-350423; Score: 0.35
DE  Interaction: Q9H0C8; IntAct: EBI-2620298,EBI-350423; Score: 0.35
DE  Interaction: Q9H596; IntAct: EBI-7357329,EBI-350423; Score: 0.35
DE  Interaction: Q9UQK1; IntAct: EBI-2506727,EBI-350423; Score: 0.35
DE  Interaction: Q9NYA1-1; IntAct: EBI-12512636,EBI-350423; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-350423; Score: 0.35
DE  Interaction: Q9Y572; IntAct: EBI-350423,EBI-298250; Score: 0.40
DE  Interaction: Q9Y6K9; IntAct: EBI-350423,EBI-81279; Score: 0.40
DE  Interaction: Q99759; IntAct: EBI-350423,EBI-307281; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-401755,EBI-350423; Score: 0.35
GO  GO:0009925;
GO  GO:0005903;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0031941;
GO  GO:0016328;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005902;
GO  GO:0016604;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0045335;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0060171;
GO  GO:0016461;
GO  GO:0051015;
GO  GO:0030898;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0000146;
GO  GO:0008022;
GO  GO:0017160;
GO  GO:0005102;
GO  GO:0071346;
GO  GO:0038096;
GO  GO:0051028;
GO  GO:0030838;
GO  GO:0030335;
GO  GO:0038089;
GO  GO:1900078;
GO  GO:0045815;
GO  GO:0090314;
GO  GO:1900748;
GO  GO:0006605;
GO  GO:0006612;
GO  GO:2000810;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYI
SQ  GPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAET
SQ  CPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIF
SQ  YQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFA
SQ  ANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRS
SQ  LASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIIC
SQ  DLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLD
SQ  KNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEV
SQ  LIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFP
SQ  KTLFATEDALEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFVLRHAP
SQ  RCPENAFFLDHVRTSFLLNLRRQLPQNVLDTSWPTPPPALREASELLRELCIKNMVWKYCRSISPEWKQQLQQKAVASEI
SQ  FKGKKDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRID
SQ  YANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPG
SQ  SELLITKAKNGHLAVVAPRLNSR
//
ID  P09917;
PN  Arachidonate 5-lipoxygenase;
GN  ALOX5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus matrix. Nucleus membrane; Peripheral membrane protein. Note=Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser- 272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association.
DR  UNIPROT: P09917;
DR  UNIPROT: B7ZLS0;
DR  UNIPROT: E5FPY5;
DR  UNIPROT: E5FPY7;
DR  UNIPROT: E5FPY8;
DR  UNIPROT: Q5JQ14;
DR  PDB: 2ABV;
DR  PDB: 3O8Y;
DR  PDB: 3V92;
DR  PDB: 3V98;
DR  PDB: 3V99;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DR  OMIM: 152390;
DR  DisGeNET: 240;
DE  Function: Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. {ECO:0000269|PubMed:21233389}.
DE  Reference Proteome: Yes;
DE  Interaction: P50221; IntAct: EBI-2864512,EBI-79934; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-307352,EBI-79934; Score: 0.56
DE  Interaction: Q6UWX4; IntAct: EBI-79934,EBI-10196655; Score: 0.72
DE  Interaction: Q86Y26; IntAct: EBI-10178410,EBI-79934; Score: 0.67
DE  Interaction: Q8IYX8-2; IntAct: EBI-79934,EBI-10181988; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-79934,EBI-6872807; Score: 0.72
DE  Interaction: Q96MT8; IntAct: EBI-741977,EBI-79934; Score: 0.67
DE  Interaction: Q9Y6D9; IntAct: EBI-79934,EBI-742610; Score: 0.81
DE  Interaction: Q92542-2; IntAct: EBI-21836984,EBI-79934; Score: 0.35
DE  Interaction: Q9Y252; IntAct: EBI-2341483,EBI-79934; Score: 0.35
DE  Interaction: Q15811-2; IntAct: EBI-79934,EBI-8052395; Score: 0.35
DE  Interaction: O94830; IntAct: EBI-79934,EBI-8444979; Score: 0.35
DE  Interaction: Q9UQ49; IntAct: EBI-79934,EBI-21699246; Score: 0.35
DE  Interaction: Q9UPU7; IntAct: EBI-79934,EBI-2947180; Score: 0.35
DE  Interaction: Q9NYA4; IntAct: EBI-79934,EBI-1052346; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-79934,EBI-2514786; Score: 0.35
DE  Interaction: Q9BWT6; IntAct: EBI-79934,EBI-11137441; Score: 0.35
DE  Interaction: Q96RR4-2; IntAct: EBI-79934,EBI-21545123; Score: 0.35
DE  Interaction: Q96L93-2; IntAct: EBI-79934,EBI-21618523; Score: 0.35
DE  Interaction: Q96C34-2; IntAct: EBI-79934,EBI-21601272; Score: 0.35
DE  Interaction: Q96AD5; IntAct: EBI-79934,EBI-716499; Score: 0.35
DE  Interaction: Q92530; IntAct: EBI-79934,EBI-945916; Score: 0.35
DE  Interaction: Q8WXG6-2; IntAct: EBI-79934,EBI-21599664; Score: 0.35
DE  Interaction: Q8ND83; IntAct: EBI-79934,EBI-10269374; Score: 0.35
DE  Interaction: Q8N3R9-2; IntAct: EBI-79934,EBI-16399750; Score: 0.35
DE  Interaction: Q8IY63-2; IntAct: EBI-79934,EBI-11041933; Score: 0.35
DE  Interaction: Q86SX3-2; IntAct: EBI-79934,EBI-10989467; Score: 0.35
DE  Interaction: Q7Z2K6; IntAct: EBI-79934,EBI-10976398; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-79934,EBI-2511832; Score: 0.35
DE  Interaction: Q6PJ69; IntAct: EBI-79934,EBI-2130441; Score: 0.35
DE  Interaction: Q6P474; IntAct: EBI-79934,EBI-1048095; Score: 0.35
DE  Interaction: Q6P1M9; IntAct: EBI-79934,EBI-10252512; Score: 0.35
DE  Interaction: Q6P1K2; IntAct: EBI-79934,EBI-713832; Score: 0.35
DE  Interaction: Q4VCS5-2; IntAct: EBI-79934,EBI-3891843; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-79934,EBI-1042535; Score: 0.35
DE  Interaction: Q15349-2; IntAct: EBI-79934,EBI-21578316; Score: 0.35
DE  Interaction: Q15042; IntAct: EBI-79934,EBI-1053078; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-79934,EBI-389449; Score: 0.35
DE  Interaction: Q14008-2; IntAct: EBI-79934,EBI-21500522; Score: 0.35
DE  Interaction: Q13615-2; IntAct: EBI-79934,EBI-21502132; Score: 0.35
DE  Interaction: Q13042-2; IntAct: EBI-79934,EBI-10974085; Score: 0.35
DE  Interaction: Q09019; IntAct: EBI-79934,EBI-724564; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-79934,EBI-307326; Score: 0.35
DE  Interaction: P48449; IntAct: EBI-79934,EBI-3930711; Score: 0.35
DE  Interaction: P30566; IntAct: EBI-79934,EBI-2511688; Score: 0.35
DE  Interaction: P29144; IntAct: EBI-79934,EBI-1044672; Score: 0.35
DE  Interaction: P31025; IntAct: EBI-1052433,EBI-79934; Score: 0.56
DE  Interaction: Q9P0N9; IntAct: EBI-3258000,EBI-79934; Score: 0.56
DE  Interaction: Q8CLD8; IntAct: EBI-2851532,EBI-79934; Score: 0.37
DE  Interaction: Q8D078; IntAct: EBI-79934,EBI-2840175; Score: 0.37
DE  Interaction: Q96MT8-3; IntAct: EBI-11522539,EBI-79934; Score: 0.72
DE  Interaction: A6NGQ2; IntAct: EBI-18583589,EBI-79934; Score: 0.56
DE  Interaction: O43716; IntAct: EBI-6929453,EBI-79934; Score: 0.56
DE  Interaction: Q6PII3; IntAct: EBI-747830,EBI-79934; Score: 0.56
DE  Interaction: Q8IYJ2-2; IntAct: EBI-13381098,EBI-79934; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-79934; Score: 0.56
DE  Interaction: P14061; IntAct: EBI-12867244,EBI-79934; Score: 0.56
DE  Interaction: Q6P2R3; IntAct: EBI-12696312,EBI-79934; Score: 0.56
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:1904813;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0034774;
GO  GO:0004051;
GO  GO:0005506;
GO  GO:0019221;
GO  GO:0036336;
GO  GO:0042593;
GO  GO:0006959;
GO  GO:0035655;
GO  GO:0002232;
GO  GO:0002523;
GO  GO:1901753;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0002540;
GO  GO:2001301;
GO  GO:0019372;
GO  GO:0042759;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0050728;
GO  GO:1903573;
GO  GO:1903671;
GO  GO:0061044;
GO  GO:0061045;
GO  GO:0043312;
GO  GO:0030501;
GO  GO:1904999;
GO  GO:1900407;
GO  GO:1900015;
GO  GO:0045598;
GO  GO:0050727;
GO  GO:0106014;
GO  GO:0050796;
GO  GO:1903426;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDD
SQ  WYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKC
SQ  HKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNG
SQ  CNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANK
SQ  IVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAH
SQ  VRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWE
SQ  AIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYD
SQ  WCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRK
SQ  NLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI
//
ID  P47069;
PN  Spindle pole body assembly component MPS3;
GN  MPS3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass type II membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to the spindle pole body half bridge throughout the cell cycle.
DR  UNIPROT: P47069;
DR  UNIPROT: D6VWG1;
DR  UNIPROT: P47070;
DR  PROSITE: PS51469;
DE  Function: Required for the first step of spindle pole body duplication in G1. Essential for nuclear division and fusion. Functions in sister chromatid cohesion establishment. Connects the spindle pole body with the nuclear envelope through its interaction with MPS2 and mediates meiotic bouquet formation and rapid chromosome movements in meiotic prophase. Functions as an integral membrane anchor for telomeres and is a nuclear receptor for the SIR4 pathway of telomere tethering and gene inactivation. recruits double-strand breaks (DSBs) to the nuclear periphery for chromosome healing. {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774, ECO:0000269|PubMed:15355977, ECO:0000269|PubMed:16682351, ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:17245108, ECO:0000269|PubMed:17495028, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18585352, ECO:0000269|PubMed:19217407, ECO:0000269|PubMed:19390086, ECO:0000269|PubMed:19390087, ECO:0000269|PubMed:20016273}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-25811,EBI-25811; Score: 0.37
DE  Interaction: Q08955; IntAct: EBI-25811,EBI-31728; Score: 0.50
DE  Interaction: Q12366; IntAct: EBI-25811,EBI-34568; Score: 0.50
DE  Interaction: P40348; IntAct: EBI-25811,EBI-14992; Score: 0.37
DE  Interaction: Q12743; IntAct: EBI-25811,EBI-33192; Score: 0.37
DE  Interaction: P53966; IntAct: EBI-9999,EBI-25811; Score: 0.37
DE  Interaction: Q12404; IntAct: EBI-25811,EBI-11184; Score: 0.37
DE  Interaction: P06197; IntAct: EBI-25811,EBI-13458; Score: 0.37
DE  Interaction: Q06616; IntAct: EBI-36065,EBI-25811; Score: 0.37
DE  Interaction: P32562; IntAct: EBI-4440,EBI-25811; Score: 0.37
DE  Interaction: P43605; IntAct: EBI-25811,EBI-22988; Score: 0.68
DE  Interaction: Q12692; IntAct: EBI-8080,EBI-25811; Score: 0.67
DE  Interaction: Q03362; IntAct: EBI-25811,EBI-2057915; Score: 0.37
DE  Interaction: P28791; IntAct: EBI-25811,EBI-16572; Score: 0.37
DE  Interaction: P40504; IntAct: EBI-10011,EBI-25811; Score: 0.37
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-25811; Score: 0.35
DE  Interaction: P40857; IntAct: EBI-25811,EBI-26003; Score: 0.37
DE  Interaction: P47007; IntAct: EBI-25811,EBI-26105; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005825;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0000784;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005816;
GO  GO:0005524;
GO  GO:0043495;
GO  GO:0006348;
GO  GO:0034087;
GO  GO:0000741;
GO  GO:0045141;
GO  GO:0007064;
GO  GO:0006998;
GO  GO:0000743;
GO  GO:0030474;
GO  GO:0007129;
GO  GO:0034398;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLD
SQ  FPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGL
SQ  FFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLP
SQ  SNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSA
SQ  LISDVIESPGIGTAGSAESRWEYDLNRYVKEILSNELQYIDKDYFIQEMNRRLQSNKQEIWEEITNRLETQQQQQQQQVQ
SQ  QDYSNVPQQYSSILMKRLIHQIYNSNQHQWEDDLDFATYVQGTKLLNHLTSPTWRQGSGVQPIELLTDSKQSSSTYWQCE
SQ  NEPGCSWAIRFKTPLYLTKISYMHGRFTNNLHIMNSAPRLISLYVKLSQTKEIKALQTLANQYGFGQHHKRDRNYIKIAK
SQ  FEYRLTDSRIRQQMYLPPWFIQLKPLVRSIVFQVDENYGNKKFISLRKFIINGVTPQDLQIIENNEFPVLLGDTPEYGVT
SQ  QNTDEGKRKVLLSKPPYASSSTSTKFHPASNVPSFGQDELDQ
//
ID  Q9H0J4;
PN  Glutamine-rich protein 2;
GN  QRICH2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q3V2A7}. Nucleus {ECO:0000250|UniProtKB:Q3V2A7}. Cytoplasm {ECO:0000250|UniProtKB:Q3V2A7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:30683861}. Note=Localization varies during spermatozoa development. The protein is distributed in the nuclear membrane of the spermatogonia, in the nucleus of round spermatids, in the nucleus and cytoplasm of early elongating spermatids, in the cytoplasm of late elongating spermatids, and in the flagella of epididymal spermatozoa. {ECO:0000250|UniProtKB:Q3V2A7}.
DR  UNIPROT: Q9H0J4;
DR  UNIPROT: A2RRE1;
DR  UNIPROT: Q96LM3;
DR  Pfam: PF16043;
DR  OMIM: 618304;
DR  OMIM: 618341;
DR  DisGeNET: 84074;
DE  Function: Has an essential role in the formation of sperm flagella and flagellar structure maintainance. It acts as a suppressor of ubiquitination and degradation of proteins involved in flagellar development and motility. {ECO:0000269|PubMed:30683861}.
DE  Disease: Spermatogenic failure 35 (SPGF35) [MIM:618341]: An autosomal recessive infertility disorder caused by spermatogenesis defects that result in multiple abnormalities of sperm flagellum and severely impaired spermatozoa motility. {ECO:0000269|PubMed:30683861}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04406; IntAct: EBI-1053637,EBI-354056; Score: 0.40
DE  Interaction: P52948; IntAct: EBI-1053637,EBI-295727; Score: 0.40
DE  Interaction: Q9NRI5; IntAct: EBI-1053637,EBI-529989; Score: 0.37
DE  Interaction: O95863; IntAct: EBI-1053637,EBI-1045459; Score: 0.40
DE  Interaction: O60232; IntAct: EBI-1053637,EBI-741415; Score: 0.40
DE  Interaction: O15479; IntAct: EBI-1053637,EBI-1057615; Score: 0.40
DE  Interaction: Q53HC9; IntAct: EBI-1053637,EBI-1055422; Score: 0.40
DE  Interaction: Q9BZ23; IntAct: EBI-1053637,EBI-1058434; Score: 0.40
DE  Interaction: O75352; IntAct: EBI-1053637,EBI-1046501; Score: 0.40
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0036126;
GO  GO:0030031;
GO  GO:0030317;
GO  GO:2000059;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKDAAEELSFARVLLQRVDELEKLFKDREQFLELVSRKLSLVPGAEEVTMVTWEELEQAITDGWRASQAGSETLMGFSKH
SQ  GGFTSLTSPEGTLSGDSTKQPSIEQALDSASGLGPDRTASGSGGTAHPSDGVSSREQSKVPSGTGRQQQPRARDEAGVPR
SQ  LHQSSTFQFKSDSDRHRSREKLTSTQPRRNARPGPVQQDLPLARDQPSSVPASQSQVHLRPDRRGLEPTGMNQPGLVPAS
SQ  TYPHGVVPLSMGQLGVPPPEMDDRELIPFVVDEQRMLPPSVPGRDQQGLELPSTDQHGLVSVSAYQHGMTFPGTDQRSME
SQ  PLGMDQRGCVISGMGQQGLVPPGIDQQGLTLPVVDQHGLVLPFTDQHGLVSPGLMPISADQQGFVQPSLEATGFIQPGTE
SQ  QHDLIQSGRFQRALVQRGAYQPGLVQPGADQRGLVRPGMDQSGLAQPGADQRGLVWPGMDQSGLAQPGRDQHGLIQPGTG
SQ  QHDLVQSGTGQGVLVQPGVDQPGMVQPGRFQRALVQPGAYQPGLVQPGADQIDVVQPGADQHGLVQSGADQSDLAQPGAV
SQ  QHGLVQPGVDQRGLAQPRADHQRGLVPPGADQRGLVQPGADQHGLVQPGVDQHGLAQPGEVQRSLVQPGIVQRGLVQPGA
SQ  VQRGLVQPGAVQRGLVQPGVDQRGLVQPGAVQRGLVQPGAVQHGLVQPGADQRGLVQPGVDQRGLVQPGVDQRGLVQPGM
SQ  DQRGLIQPGADQPGLVQPGAGQLGMVQPGIGQQGMVQPQADPHGLVQPGAYPLGLVQPGAYLHDLSQSGTYPRGLVQPGM
SQ  DQYGLRQPGAYQPGLIAPGTKLRGSSTFQADSTGFISVRPYQHGMVPPGREQYGQVSPLLASQGLASPGIDRRSLVPPET
SQ  YQQGLMHPGTDQHSPIPLSTGLGSTHPDQQHVASPGPGEHDQVYPDAAQHGHAFSLFDSHDSMYPGYRGPGYLSADQHGQ
SQ  EGLDPNRTRASDRHGIPAQKAPGQDVTLFRSPDSVDRVLSEGSEVSSEVLSERRNSLRRMSSSFPTAVETFHLMGELSSL
SQ  YVGLKESMKDLDEEQAGQTDLEKIQFLLAQMVKRTIPPELQEQLKTVKTLAKEVWQEKAKVERLQRILEGEGNQEAGKEL
SQ  KAGELRLQLGVLRVTVADIEKELAELRESQDRGKAAMENSVSEASLYLQDQLDKLRMIIESMLTSSSTLLSMSMAPHKAH
SQ  TLAPGQIDPEATCPACSLDVSHQVSTLVRRYEQLQDMVNSLAVSRPSKKAKLQRQDEELLGRVQSAILQVQGDCEKLNIT
SQ  TSNLIEDHRQKQKDIAMLYQGLEKLEKEKANREHLEMEIDVKADKSALATKVSRVQFDATTEQLNHMMQELVAKMSGQEQ
SQ  DWQKMLDRLLTEMDNKLDRLELDPVKQLLEDRWKSLRQQLRERPPLYQADEAAAMRRQLLAHFHCLSCDRPLETPVTGHA
SQ  IPVTPAGPGLPGHHSIRPYTVFELEQVRQHSRNLKLGSAFPRGDLAQMEQSVGRLRSMHSKMLMNIEKVQIHFGGSTKAS
SQ  SQIIRELLHAQCLGSPCYKRVTDMADYTYSTVPRRCGGSHTLTYPYHRSRPQHLPRGLYPTEEIQIAMKHDEVDILGLDG
SQ  HIYKGRMDTRLPGILRKDSSGTSKRKSQQPRPHVHRPPSLSSNGQLPSRPQSAQISAGNTSER
//
ID  Q96T37;
PN  RNA-binding protein 15;
GN  RBM15;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus speckle {ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495, ECO:0000269|PubMed:24100041}. Nucleus envelope {ECO:0000269|PubMed:19586903}. Nucleus membrane {ECO:0000269|PubMed:19786495}; Peripheral membrane protein {ECO:0000269|PubMed:19786495}. Note=Colocalizes at the nuclear pore with DBP5 and NXF1. {ECO:0000269|PubMed:19786495}.
DR  UNIPROT: Q96T37;
DR  UNIPROT: A1A693;
DR  UNIPROT: Q3ZB86;
DR  UNIPROT: Q4V760;
DR  UNIPROT: Q5D058;
DR  UNIPROT: Q5T613;
DR  UNIPROT: Q86VW9;
DR  UNIPROT: Q96PE4;
DR  UNIPROT: Q96SC5;
DR  UNIPROT: Q96SC6;
DR  UNIPROT: Q96SC9;
DR  UNIPROT: Q96SD0;
DR  UNIPROT: Q96T38;
DR  UNIPROT: Q9BRA5;
DR  UNIPROT: Q9H6R8;
DR  UNIPROT: Q9H9Y0;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DR  OMIM: 606077;
DR  DisGeNET: 64783;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311). {ECO:0000250|UniProtKB:Q0VBL3, ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:27602518, ECO:0000305|PubMed:11344311}.
DE  Disease: Note=A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene. {ECO:0000269|PubMed:11344311, ECO:0000269|PubMed:11431691}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13137; IntAct: EBI-2514922,EBI-739580; Score: 0.56
DE  Interaction: Q12824; IntAct: EBI-358419,EBI-2514922; Score: 0.35
DE  Interaction: Q7TSJ6; IntAct: EBI-6305003,EBI-2514922; Score: 0.35
DE  Interaction: Q8IVL1; IntAct: EBI-741200,EBI-2514922; Score: 0.56
DE  Interaction: Q92841; IntAct: EBI-746012,EBI-2514922; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-741037,EBI-2514922; Score: 0.56
DE  Interaction: Q9C0F1; IntAct: EBI-744115,EBI-2514922; Score: 0.56
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-2514922; Score: 0.35
DE  Interaction: O60346; IntAct: EBI-2511516,EBI-2514922; Score: 0.40
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-2514922; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-743488,EBI-2514922; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-447544,EBI-2514922; Score: 0.35
DE  Interaction: O60825; IntAct: EBI-764425,EBI-2514922; Score: 0.35
DE  Interaction: Q6PDM2; IntAct: EBI-2550360,EBI-2514922; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-593303,EBI-2514922; Score: 0.44
DE  Interaction: Q9UJV9; IntAct: EBI-1046350,EBI-2514922; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-2361917,EBI-2514922; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12561553,EBI-2514922; Score: 0.35
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0036396;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0001569;
GO  GO:0009048;
GO  GO:0045638;
GO  GO:0060674;
GO  GO:0007221;
GO  GO:0000381;
GO  GO:0045652;
GO  GO:0001510;
GO  GO:0048536;
GO  GO:0038163;
GO  GO:0060412;
GO  GO:0016032;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:19786495};
SQ  MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGS
SQ  NGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSA
SQ  PGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVL
SQ  YDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPP
SQ  PPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVI
SQ  TEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGT
SQ  IRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDAFGHRAPDP
SQ  LRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRTAATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPR
SQ  KRRLPEESGGRHLDRSPESDRPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRK
SQ  NSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASASPKLCLAWQGMLLLKNSNFP
SQ  SNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDT
SQ  ATSTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRGFGFQI
SQ  GVRYENKKRENLALTLL
//
ID  P10687;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  Plcb1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250}.
DR  UNIPROT: P10687;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
DE  Reference Proteome: Yes;
DE  Interaction: P51692; IntAct: EBI-1186119,EBI-7551252; Score: 0.35
DE  Interaction: P17948; IntAct: EBI-1026718,EBI-7551252; Score: 0.35
DE  Interaction: Q96T51; IntAct: EBI-3941207,EBI-7551252; Score: 0.35
DE  Interaction: P54578; IntAct: EBI-1048016,EBI-7551252; Score: 0.35
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0000790;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0060466;
GO  GO:0007420;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032959;
GO  GO:0032957;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0007613;
GO  GO:2000438;
GO  GO:0045892;
GO  GO:0031161;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:2000344;
GO  GO:2000560;
GO  GO:0048639;
GO  GO:0040019;
GO  GO:1900087;
GO  GO:0032735;
GO  GO:0046330;
GO  GO:0045663;
GO  GO:0045893;
GO  GO:0099170;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0051209;
GO  GO:0034284;
GO  GO:0010243;
GO  GO:0043434;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKA
SQ  PKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFETSKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTATLAPKPPSQAPH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHKEIRQQILDEKPKLQMELEQEYQDKFKRLPLEILEFVQEAMKGKVSEDSNHGSAPPSLASDPAKVNLKSPSS
SQ  EEVQGENAGREFDTPL
//
ID  B9EJ86;
PN  Oxysterol-binding protein-related protein 8;
GN  Osbpl8;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BZF1}.
DR  UNIPROT: B9EJ86;
DR  UNIPROT: G3X9N6;
DR  UNIPROT: Q69ZJ4;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9BZF1}.
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0015485;
GO  GO:0008289;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0140343;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0032148;
GO  GO:0045444;
GO  GO:0030336;
GO  GO:0010891;
GO  GO:0015914;
GO  GO:0046326;
GO  GO:0046628;
GO  GO:0051897;
GO  GO:0090204;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKED
SQ  ISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGT
SQ  LKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPS
SQ  SYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQH
SQ  FKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVS
SQ  EENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGL
SQ  KKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFL
SQ  NRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWD
SQ  SEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDR
SQ  KTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSP
SQ  EPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILL
SQ  QVIINFIFK
//
ID  Q9WTR8;
PN  PH domain leucine-rich repeat protein phosphatase 1;
GN  Phlpp1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12594205}. Membrane {ECO:0000269|PubMed:12594205}; Peripheral membrane protein {ECO:0000269|PubMed:12594205}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:20819118}. Cell membrane {ECO:0000269|PubMed:20819118}. [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:20819118}. Nucleus membrane {ECO:0000269|PubMed:20819118}. Cytoplasm {ECO:0000269|PubMed:20819118}. Cell membrane {ECO:0000269|PubMed:20819118}.
DR  UNIPROT: Q9WTR8;
DR  Pfam: PF00560;
DR  Pfam: PF13516;
DR  Pfam: PF13855;
DR  Pfam: PF00169;
DR  Pfam: PF00481;
DR  PROSITE: PS51450;
DR  PROSITE: PS50003;
DR  PROSITE: PS51746;
DE  Function: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:20819118). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons while isoform 1 may promote Akt and PKC activation and inhibit ERK signaling (PubMed:20819118). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (By similarity). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (By similarity). Inhibits cancer cell proliferation and may act as a tumor suppressor (By similarity). Dephosphorylates RAF1 inhibiting its kinase activity (By similarity). May act as a negative regulator of K-Ras signaling in membrane rafts (PubMed:12594205). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T-cells (By similarity). {ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q8CHE4, ECO:0000269|PubMed:12594205, ECO:0000269|PubMed:20819118}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0004722;
GO  GO:0006915;
GO  GO:0007623;
GO  GO:0009649;
GO  GO:0021766;
GO  GO:0070373;
GO  GO:0051898;
GO  GO:0090038;
GO  GO:0051897;
GO  GO:0090037;
GO  GO:0006470;
GO  GO:0042981;
GO  GO:0046328;
GO  GO:0043408;
GO  GO:1900744;
GO  GO:0051896;
GO  GO:0090036;
GO  GO:0001932;
GO  GO:0002667;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12594205};
SQ  MEPAAAAPAQRLADPTGEDRAPAAAAAAEGGRSPDSVLSAAAPSGGNGGAAREEAPCEAPPGPLPGRAGGTGRRRRRGVP
SQ  QPAAGGAAPVTAAGGGANSLLLRRGRLKRNLSAAASSSSSPSSASSAAGGLPASCSASASLCTRSLDRKTLLQKHRQLLQ
SQ  LQPSDRDWVRHQLQRGCVHVFDRHMASSYLRPVLCTLDTTAAEVAARLLQLGHKGGGVVKVLGHGPPPAAAPAASDQTPA
SQ  TELGRDVEPPPSSSTVGAVRGPARAPPADLPLPGGAWTRCAPRVNPAPSDSSPGELFAGGPCSPSRAPRPASDTESFSLS
SQ  PSAESVSDRLDPYSSGGGSSSSSEELEADPATVLTGPSGPPHHPVRSSQPRPPSPKTSALLQPKAPTGVDGTGLVVGEGP
SQ  GDDKAVAAAAPGVPLWTPGRIRETVQKTSSPPSLYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEI
SQ  GCLIRFYAGKPHSTGSSERIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSSSGKMHVLPLIGGKVEEVKK
SQ  HQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNPS
SQ  LPAARGLGELQRFTKLKSLNLSNNHLGAFPSAVCSIPTLAELNVSCNALQEVPAAVGAMQNLQTFLLDGNFLQSLPAELE
SQ  NMHQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMAGNCMETLRLQALRRMPHIKHVDLRLNILRKLITDEVDFLQHVTQLD
SQ  LRDNKLGDLDAMIFNNIEVLHCERNQLVTLNICGYFLKALYASSNELVQLDVYPVPNYLSYMDVSRNCLESVPEWVCESR
SQ  KLEVLDIGHNQICELPARLFCNSSLRKLLAGHNRLARLPERLERTSVEVLDVQHNQIIELPPNLLMKADSLRFLNASANK
SQ  LETLPPATLSEETSSILQELYLTNNSLTDKCVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKAIPT
SQ  TIMNCRRMHTVIAHSNCIEVFPEVMQLPEVKCVDLSCNELSEITLPENLPPKLQELDLTGNPRLALDHKSLELLNNIRCF
SQ  KIDQPSAGDASGAPAVWSHGYTEASGVKNKLCVAALSVNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTK
SQ  NEEEYMVNTFIVMQRKLGTAGQKLGGAAVLCHIRHDPVDLGGSFTLTSANVGKCQTVLCRNGKPLSLSRSYTMSCEEERK
SQ  RIKQHKAIITEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIEEAVEAVRNVPDALA
SQ  AAKKLCTLAQSYGCHDSISAVVVQLSVTEDSFCCCELSVGGSMPPPSPGIFPPSVSMVIKDRPSDGLGVPSSSSGMASEI
SQ  SSELSTSEMSSEVGSTASDEPPSGALSESSPAYPSEQRCMLHPVCLSNSFQRQLSSATFSSAFSDNGLDSDDEEPIEGVF
SQ  SNGSRVEVEVDIHCSRAKEKERQQHLLQVPAEASDEGIVISANEDESGLSKKTDISAVGTIGRRRANGSVPPQERSHNVI
SQ  EVATDAPLRKPGGYFAAPAQPDPDDQFIIPPELEEEVKEIMKHHQEQQQQQQQQQQQQQQQPPPPPQPPQAQAQAQAQAQ
SQ  RPFQMDHLPDCYDTPL
//
ID  P21279;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  Gnaq;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:19001095}; Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000269|PubMed:18802028}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
DR  UNIPROT: P21279;
DR  UNIPROT: Q6PFF5;
DR  PDB: 2BCJ;
DR  PDB: 2RGN;
DR  PDB: 3AH8;
DR  PDB: 3OHM;
DR  PDB: 4EKC;
DR  PDB: 4EKD;
DR  PDB: 4GNK;
DR  PDB: 4QJ3;
DR  PDB: 4QJ4;
DR  PDB: 4QJ5;
DR  PDB: 5DO9;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM- derived neutrophils and dendritic cells (in vitro). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs). {ECO:0000250|UniProtKB:P50148, ECO:0000269|PubMed:17938235, ECO:0000269|PubMed:20624888}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3UHD9; IntAct: EBI-771911,EBI-771975; Score: 0.35
DE  Interaction: P62871; IntAct: EBI-771975,EBI-357141; Score: 0.40
DE  Interaction: P63278-2; IntAct: EBI-22091956,EBI-771975; Score: 0.35
DE  Interaction: Q9CQV8; IntAct: EBI-771608,EBI-771975; Score: 0.35
GO  GO:0005901;
GO  GO:0044297;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005834;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0047391;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0031826;
GO  GO:0001508;
GO  GO:0007202;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:0048066;
GO  GO:0042733;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0007215;
GO  GO:0007507;
GO  GO:0042711;
GO  GO:0043066;
GO  GO:0043267;
GO  GO:0006469;
GO  GO:0016322;
GO  GO:0060158;
GO  GO:0007200;
GO  GO:0048661;
GO  GO:0009791;
GO  GO:0050821;
GO  GO:0060828;
GO  GO:0045634;
GO  GO:0001501;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8227063};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  P40069;
PN  Importin subunit beta-4;
GN  KAP123;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9321403}.
DR  UNIPROT: P40069;
DR  UNIPROT: D3DM16;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Its predominant cargo substrate seems to be ribosomal proteins (PubMed:9321403). Required for import of the ribbosomal assembly factor NMD3 (PubMed:12612077). May be involved in nuclear transport of YAP1 (PubMed:11274141). Mediates the nuclear import of histones H3 and H4 (PubMed:11694505). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP- Ran binding leads to release of the cargo (PubMed:9321403). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). {ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:9321403, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P12683; IntAct: EBI-8377,EBI-9166; Score: 0.35
DE  Interaction: P12684; IntAct: EBI-8384,EBI-9166; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-12401,EBI-9166; Score: 0.35
DE  Interaction: P34077; IntAct: EBI-12056,EBI-9166; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-9152,EBI-9166; Score: 0.35
DE  Interaction: P38242; IntAct: EBI-21477,EBI-9166; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-9166,EBI-20731; Score: 0.67
DE  Interaction: P10591; IntAct: EBI-8591,EBI-9166; Score: 0.35
DE  Interaction: P02309; IntAct: EBI-8113,EBI-9166; Score: 0.53
DE  Interaction: P61830; IntAct: EBI-8098,EBI-9166; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-8076,EBI-9166; Score: 0.35
DE  Interaction: Q12692; IntAct: EBI-8080,EBI-9166; Score: 0.35
DE  Interaction: Q12529; IntAct: EBI-2887498,EBI-9166; Score: 0.35
DE  Interaction: P40340; IntAct: EBI-19030,EBI-9166; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-9166,EBI-8627; Score: 0.53
DE  Interaction: P32835; IntAct: EBI-7926,EBI-9166; Score: 0.44
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-9166; Score: 0.35
DE  Interaction: P46675; IntAct: EBI-18471,EBI-9166; Score: 0.35
DE  Interaction: P52910; IntAct: EBI-2136,EBI-9166; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-28374,EBI-9166; Score: 0.53
DE  Interaction: P11075; IntAct: EBI-16882,EBI-9166; Score: 0.35
DE  Interaction: P38152; IntAct: EBI-19672,EBI-9166; Score: 0.35
DE  Interaction: P25360; IntAct: EBI-13344,EBI-9166; Score: 0.35
DE  Interaction: P35200; IntAct: EBI-11337,EBI-9166; Score: 0.35
DE  Interaction: P39004; IntAct: EBI-8790,EBI-9166; Score: 0.35
DE  Interaction: P40319; IntAct: EBI-6423,EBI-9166; Score: 0.35
DE  Interaction: P32340; IntAct: EBI-11961,EBI-9166; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-6302,EBI-9166; Score: 0.35
DE  Interaction: P07246; IntAct: EBI-2227,EBI-9166; Score: 0.35
DE  Interaction: Q05881; IntAct: EBI-37369,EBI-9166; Score: 0.35
DE  Interaction: P32502; IntAct: EBI-6260,EBI-9166; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-37072,EBI-9166; Score: 0.44
DE  Interaction: P25454; IntAct: EBI-14709,EBI-9166; Score: 0.35
DE  Interaction: P21304; IntAct: EBI-14328,EBI-9166; Score: 0.35
DE  Interaction: P46956; IntAct: EBI-13337,EBI-9166; Score: 0.53
DE  Interaction: P13663; IntAct: EBI-5803,EBI-9166; Score: 0.35
DE  Interaction: P32476; IntAct: EBI-6545,EBI-9166; Score: 0.35
DE  Interaction: P32467; IntAct: EBI-8774,EBI-9166; Score: 0.35
DE  Interaction: P32803; IntAct: EBI-6431,EBI-9166; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-9619,EBI-9166; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-26585,EBI-9166; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-13686,EBI-9166; Score: 0.53
DE  Interaction: P53965; IntAct: EBI-28668,EBI-9166; Score: 0.35
DE  Interaction: P22211; IntAct: EBI-12207,EBI-9166; Score: 0.35
DE  Interaction: P00546; IntAct: EBI-4253,EBI-9166; Score: 0.35
DE  Interaction: P40499; IntAct: EBI-25109,EBI-9166; Score: 0.35
DE  Interaction: P53045; IntAct: EBI-6506,EBI-9166; Score: 0.35
DE  Interaction: Q04182; IntAct: EBI-13072,EBI-9166; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-2186,EBI-9166; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-25128,EBI-9166; Score: 0.35
DE  Interaction: P50108; IntAct: EBI-11043,EBI-9166; Score: 0.53
DE  Interaction: P33748; IntAct: EBI-11407,EBI-9166; Score: 0.35
DE  Interaction: P46985; IntAct: EBI-11052,EBI-9166; Score: 0.35
DE  Interaction: P22202; IntAct: EBI-8621,EBI-9166; Score: 0.35
DE  Interaction: P32903; IntAct: EBI-13545,EBI-9166; Score: 0.35
DE  Interaction: Q02785; IntAct: EBI-13065,EBI-9166; Score: 0.35
DE  Interaction: P38310; IntAct: EBI-20959,EBI-9166; Score: 0.35
DE  Interaction: P36013; IntAct: EBI-10412,EBI-9166; Score: 0.35
DE  Interaction: P38085; IntAct: EBI-20222,EBI-9166; Score: 0.35
DE  Interaction: P20107; IntAct: EBI-29667,EBI-9166; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-28532,EBI-9166; Score: 0.35
DE  Interaction: P07262; IntAct: EBI-5823,EBI-9166; Score: 0.35
DE  Interaction: P32454; IntAct: EBI-2641,EBI-9166; Score: 0.35
DE  Interaction: P35723; IntAct: EBI-26730,EBI-9166; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-16032,EBI-9166; Score: 0.53
DE  Interaction: P33441; IntAct: EBI-10841,EBI-9166; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-2098,EBI-9166; Score: 0.35
DE  Interaction: P39522; IntAct: EBI-9078,EBI-9166; Score: 0.35
DE  Interaction: P48563; IntAct: EBI-28333,EBI-9166; Score: 0.35
DE  Interaction: P40416; IntAct: EBI-3181,EBI-9166; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-11191,EBI-9166; Score: 0.35
DE  Interaction: P32629; IntAct: EBI-2595,EBI-9166; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-20647,EBI-9166; Score: 0.63
DE  Interaction: Q07560; IntAct: EBI-5153,EBI-9166; Score: 0.35
DE  Interaction: P16550; IntAct: EBI-2631,EBI-9166; Score: 0.35
DE  Interaction: P38687; IntAct: EBI-18004,EBI-9166; Score: 0.35
DE  Interaction: P23500; IntAct: EBI-11297,EBI-9166; Score: 0.35
DE  Interaction: P05626; IntAct: EBI-9166,EBI-3264; Score: 0.40
DE  Interaction: P53881; IntAct: EBI-29042,EBI-9166; Score: 0.35
DE  Interaction: Q07084; IntAct: EBI-18184,EBI-9166; Score: 0.35
DE  Interaction: Q07804; IntAct: EBI-36254,EBI-9166; Score: 0.35
DE  Interaction: P38707; IntAct: EBI-18775,EBI-9166; Score: 0.35
DE  Interaction: P36148; IntAct: EBI-26471,EBI-9166; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-6533,EBI-9166; Score: 0.35
DE  Interaction: P54837; IntAct: EBI-6642,EBI-9166; Score: 0.35
DE  Interaction: P38703; IntAct: EBI-10035,EBI-9166; Score: 0.35
DE  Interaction: P29496; IntAct: EBI-10549,EBI-9166; Score: 0.35
DE  Interaction: Q99190; IntAct: EBI-31149,EBI-9166; Score: 0.35
DE  Interaction: P32798; IntAct: EBI-5006,EBI-9166; Score: 0.35
DE  Interaction: P18414; IntAct: EBI-6526,EBI-9166; Score: 0.35
DE  Interaction: P40060; IntAct: EBI-22617,EBI-9166; Score: 0.35
DE  Interaction: Q12029; IntAct: EBI-34730,EBI-9166; Score: 0.35
DE  Interaction: Q04013; IntAct: EBI-24564,EBI-9166; Score: 0.53
DE  Interaction: Q12345; IntAct: EBI-35758,EBI-9166; Score: 0.35
DE  Interaction: Q06616; IntAct: EBI-36065,EBI-9166; Score: 0.53
DE  Interaction: P36008; IntAct: EBI-6329,EBI-9166; Score: 0.35
DE  Interaction: P53217; IntAct: EBI-23120,EBI-9166; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-6587,EBI-9166; Score: 0.35
DE  Interaction: P32843; IntAct: EBI-15626,EBI-9166; Score: 0.35
DE  Interaction: P0CI39; IntAct: EBI-18360,EBI-9166; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-7727,EBI-9166; Score: 0.35
DE  Interaction: P22215; IntAct: EBI-17397,EBI-9166; Score: 0.35
DE  Interaction: Q03771; IntAct: EBI-36525,EBI-9166; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-1797,EBI-9166; Score: 0.53
DE  Interaction: P38719; IntAct: EBI-5633,EBI-9166; Score: 0.53
DE  Interaction: P35191; IntAct: EBI-10603,EBI-9166; Score: 0.35
DE  Interaction: P39743; IntAct: EBI-14500,EBI-9166; Score: 0.53
DE  Interaction: P40541; IntAct: EBI-16667,EBI-9166; Score: 0.35
DE  Interaction: P33333; IntAct: EBI-13494,EBI-9166; Score: 0.35
DE  Interaction: Q04062; IntAct: EBI-15944,EBI-9166; Score: 0.35
DE  Interaction: P27929; IntAct: EBI-11843,EBI-9166; Score: 0.35
DE  Interaction: P38689; IntAct: EBI-9877,EBI-9166; Score: 0.35
DE  Interaction: P40081; IntAct: EBI-22701,EBI-9166; Score: 0.35
DE  Interaction: P51998; IntAct: EBI-450,EBI-9166; Score: 0.35
DE  Interaction: P47054; IntAct: EBI-25846,EBI-9166; Score: 0.35
DE  Interaction: P52593; IntAct: EBI-11763,EBI-9166; Score: 0.35
DE  Interaction: Q03529; IntAct: EBI-16747,EBI-9166; Score: 0.35
DE  Interaction: P32492; IntAct: EBI-11681,EBI-9166; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-9166,EBI-15270; Score: 0.35
DE  Interaction: P40010; IntAct: EBI-9166,EBI-22449; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-9166,EBI-9145; Score: 0.35
DE  Interaction: P25605; IntAct: EBI-9166,EBI-9087; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-9166,EBI-8883; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-9166,EBI-7442; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-9166,EBI-29516; Score: 0.53
DE  Interaction: P07259; IntAct: EBI-9166,EBI-14372; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-9166,EBI-9017; Score: 0.56
DE  Interaction: P02994; IntAct: EBI-9166,EBI-6314; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-9166,EBI-8632; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-9166,EBI-8603; Score: 0.35
DE  Interaction: Q12464; IntAct: EBI-9166,EBI-31814; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-9166,EBI-16150; Score: 0.53
DE  Interaction: P23248; IntAct: EBI-9166,EBI-16136; Score: 0.53
DE  Interaction: P33442; IntAct: EBI-9166,EBI-16132; Score: 0.53
DE  Interaction: P32566; IntAct: EBI-17452,EBI-9166; Score: 0.35
DE  Interaction: P39011; IntAct: EBI-3544,EBI-9166; Score: 0.35
DE  Interaction: Q04305; IntAct: EBI-28183,EBI-9166; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-3727,EBI-9166; Score: 0.35
DE  Interaction: P40035; IntAct: EBI-22551,EBI-9166; Score: 0.35
DE  Interaction: Q12296; IntAct: EBI-33338,EBI-9166; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-10067,EBI-9166; Score: 0.35
DE  Interaction: P38264; IntAct: EBI-13350,EBI-9166; Score: 0.35
DE  Interaction: P39676; IntAct: EBI-6905,EBI-9166; Score: 0.35
DE  Interaction: P19262; IntAct: EBI-12464,EBI-9166; Score: 0.35
DE  Interaction: Q06338; IntAct: EBI-33582,EBI-9166; Score: 0.27
DE  Interaction: P54115; IntAct: EBI-5798,EBI-9166; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-2293,EBI-9166; Score: 0.51
DE  Interaction: P16522; IntAct: EBI-4216,EBI-9166; Score: 0.35
DE  Interaction: P53012; IntAct: EBI-16742,EBI-9166; Score: 0.35
DE  Interaction: P36046; IntAct: EBI-26978,EBI-9166; Score: 0.35
DE  Interaction: Q02776; IntAct: EBI-30302,EBI-9166; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-25778,EBI-9166; Score: 0.35
DE  Interaction: P47026; IntAct: EBI-25989,EBI-9166; Score: 0.35
DE  Interaction: P38720; IntAct: EBI-1965,EBI-9166; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0008536;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006606;
GO  GO:2000220;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQQFLSQLEQTLHAITSGVGLKEATKTLQTQFYTQPTTLPALIHILQNGSDDSLKQLAGVEARKLVSKHWNAIDESTRA
SQ  SIKTSLLQTAFSEPKENVRHSNARVIASIGTEELDGNKWPDLVPNLIQTASGEDVQTRQTAIFILFSLLEDFTSSLSGHI
SQ  DDFLALFSQTINDPSSLEIRSLSAQALNHVSALIEEQETINPVQAQKFAASIPSVVNVLDAVIKADDTMNAKLIFNCLND
SQ  FLLLDSQLTGNFIVDLIKLSLQIAVNSEIDEDVRVFALQFIISSLSYRKSKVSQSKLGPEITVAALKVACEEIDVDDELN
SQ  NEDETGENEENTPSSSAIRLLAFASSELPPSQVASVIVEHIPAMLQSANVFERRAILLAISVAVTGSPDYILSQFDKIIP
SQ  ATINGLKDTEPIVKLAALKCIHQLTTDLQDEVAKFHEEYLPLIIDIIDSAKNIVIYNYATVALDGLLEFIAYDAIAKYLD
SQ  PLMNKLFYMLESNESSKLRCAVVSAIGSAAFAAGSAFIPYFKTSVHYLEKFIQNCSQIEGMSEDDIELRANTFENISTMA
SQ  RAVRSDAFAEFAEPLVNSAYEAIKTDSARLRESGYAFIANLAKVYGENFAPFLKTILPEIFKTLELDEYQFNFDGDAEDL
SQ  AAFADSANEEELQNKFTVNTGISYEKEVASAALSELALGTKEHFLPYVEQSLKVLNEQVDESYGLRETALNTIWNVVKSV
SQ  LLASKVEPESYPKGIPASSYVNADVLAVIQAARETSMGNLSDEFETSMVITVMEDFANMIKQFGAIIIMDNGDSSMLEAL
SQ  CMQVLSVLKGTHTCQTIDIEEDVPRDEELDASETEATLQDVALEVLVSLSQALAGDFAKVFDNFRPVVFGLFQSKSKNKR
SQ  SSAVGAASELALGMKEQNPFVHEMLEALVIRLTSDKSLEVRGNAAYGVGLLCEYASMDISAVYEPVLKALYELLSAADQK
SQ  ALAAEDDEATREIIDRAYANASGCVARMALKNSALVPLEQTVPALLAHLPLNTGFEEYNPIFELIMKLYQENSPVITNET
SQ  PRIIEIFSAVFTKENDRIKLEKESTLGREENMERLKQFQTEEMKHKVIELLKYLNTTYNGIVAQNPVLAAVIA
//
ID  Q96S66;
PN  Chloride channel CLIC-like protein 1;
GN  CLCC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:31653868}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi- pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000269|PubMed:31653868}.
DR  UNIPROT: Q96S66;
DR  UNIPROT: O94861;
DR  UNIPROT: Q8WYP8;
DR  UNIPROT: Q8WYP9;
DR  UNIPROT: Q9BU25;
DR  Pfam: PF05934;
DR  OMIM: 268000;
DR  OMIM: 617539;
DE  Function: Seems to act as a chloride ion channel (PubMed:30157172). Plays a role in retina development (PubMed:30157172). {ECO:0000269|PubMed:30157172}.
DE  Disease: Retinitis pigmentosa (RP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:30157172}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-2836109; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-2836109; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-2836109; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21259559,EBI-2836109; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-2836109; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11333674,EBI-2836109; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-2836109; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-2836109; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-2836109; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-2836109; Score: 0.35
DE  Interaction: Q99JN2; IntAct: EBI-11026094,EBI-2836109; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-2836109; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-2836109; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-2836109; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-2836109; Score: 0.35
DE  Interaction: A0A1Q4LZ40; IntAct: EBI-2827404,EBI-2836109; Score: 0.37
DE  Interaction: P0DTC3; IntAct: EBI-25475894,EBI-2836109; Score: 0.35
DE  Interaction: Q9UKW4-1; IntAct: EBI-25410537,EBI-2836109; Score: 0.35
DE  Interaction: Q92888-2; IntAct: EBI-21604343,EBI-2836109; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-2836109; Score: 0.35
GO  GO:0034707;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDE
SQ  CEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILI
SQ  NFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQH
SQ  QAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTG
SQ  EFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHY
SQ  RGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGE
SQ  GTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG
//
ID  Q24246;
PN  Cytoplasmic dynein 1 intermediate chain;
GN  sw;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9774695}. [Isoform 2c]: Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around lysosomes. [Isoform 2a]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus. [Isoform 2b]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus.
DR  UNIPROT: Q24246;
DR  UNIPROT: O96508;
DR  UNIPROT: O96510;
DR  UNIPROT: O96511;
DR  UNIPROT: O96512;
DR  UNIPROT: O96513;
DR  UNIPROT: O96514;
DR  UNIPROT: O96515;
DR  UNIPROT: O96516;
DR  UNIPROT: Q5U0Z1;
DR  UNIPROT: Q86BQ5;
DR  UNIPROT: Q9NG49;
DR  UNIPROT: Q9TZR7;
DR  UNIPROT: Q9TZR8;
DR  UNIPROT: Q9TZR9;
DR  UNIPROT: Q9TZS0;
DR  UNIPROT: Q9VR78;
DR  PDB: 2P2T;
DR  PDB: 3FM7;
DR  PDB: 3L9K;
DR  Pfam: PF11540;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the help dynein bind to dynactin 150 kDa component (By similarity). {ECO:0000250, ECO:0000269|PubMed:11071907}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005765;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0031965;
GO  GO:0032991;
GO  GO:0034452;
GO  GO:0045504;
GO  GO:0045503;
GO  GO:0003774;
GO  GO:0008088;
GO  GO:0007349;
GO  GO:0051642;
GO  GO:0001754;
GO  GO:0000226;
GO  GO:0007018;
GO  GO:2000582;
GO  GO:0034501;
GO  GO:0007291;
GO  GO:0007051;
GO  GO:0010970;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMT
SQ  SDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWW
SQ  RPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVN
SQ  ELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMD
SQ  WSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQK
SQ  RTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINS
SQ  LVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDY
SQ  VMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQP
SQ  SRDEWSRFNTHLSEIKMNQSDEV
//
ID  O14681;
PN  Etoposide-induced protein 2.4 homolog;
GN  EI24;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:21154811}; Multi-pass membrane protein {ECO:0000269|PubMed:21154811}. Cytoplasm {ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: O14681;
DR  UNIPROT: A8K7D6;
DR  UNIPROT: B4DKL6;
DR  UNIPROT: Q9BUQ1;
DR  OMIM: 605170;
DR  DisGeNET: 9538;
DE  Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.
DE  Disease: Note=EI24 is on a chromosomal region frequently deleted in solid tumors, and it is thought to play a role in breast and cervical cancer. Particularly, expression analysis of EI24 in cancerous tissues shows that EI24 loss is associated with tumor invasiveness.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-2339413; Score: 0.35
DE  Interaction: P51668; IntAct: EBI-2339413,EBI-743540; Score: 0.37
DE  Interaction: P62837; IntAct: EBI-2339413,EBI-347677; Score: 0.37
DE  Interaction: F5H1C8; IntAct: EBI-21259559,EBI-2339413; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-2339413; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-2339413; Score: 0.35
DE  Interaction: Q8N4P2; IntAct: EBI-6958994,EBI-2339413; Score: 0.51
DE  Interaction: P11234; IntAct: EBI-2339413,EBI-752162; Score: 0.51
DE  Interaction: P27105; IntAct: EBI-1211440,EBI-2339413; Score: 0.51
DE  Interaction: Q9NUH8; IntAct: EBI-8638294,EBI-2339413; Score: 0.56
DE  Interaction: O15173; IntAct: EBI-1050125,EBI-2339413; Score: 0.56
DE  Interaction: Q6PL24; IntAct: EBI-2339413,EBI-11603430; Score: 0.56
DE  Interaction: Q12982; IntAct: EBI-2339413,EBI-752094; Score: 0.56
DE  Interaction: Q9UI14; IntAct: EBI-2339413,EBI-712367; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-2339413; Score: 0.35
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0006915;
GO  GO:0016236;
GO  GO:0030308;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGG
SQ  VFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRK
SQ  PHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWP
SQ  YYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTS
SQ  AEKFPSPHPSPAKLKATAGH
//
ID  Q06142;
PN  Importin subunit beta-1;
GN  KAP95;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: Q06142;
DR  UNIPROT: D6VYY6;
DR  PDB: 2BKU;
DR  PDB: 3EA5;
DR  PDB: 3ND2;
DR  PDB: 5OWU;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the classical nuclear localization signal (cNLS) in cargo substrates (PubMed:7622450). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:8521485). At the nucleoplasmic side of the NPC, GTP- Ran binds to importin beta and the three components separate, leading to release of the cargo (PubMed:15864302). Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). Mediates the nuclear import of histones H2A and H2B (PubMed:11309407). {ECO:0000269|PubMed:11309407, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:7622450, ECO:0000269|PubMed:8521485, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-9145,EBI-12265; Score: 0.72
DE  Interaction: P20676; IntAct: EBI-9145,EBI-12392; Score: 0.77
DE  Interaction: P32499; IntAct: EBI-9145,EBI-12401; Score: 0.78
DE  Interaction: P34160; IntAct: EBI-745,EBI-9145; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-9145,EBI-20731; Score: 0.77
DE  Interaction: P40069; IntAct: EBI-9166,EBI-9145; Score: 0.35
DE  Interaction: P40477; IntAct: EBI-11747,EBI-9145; Score: 0.61
DE  Interaction: P48837; IntAct: EBI-9145,EBI-12324; Score: 0.44
DE  Interaction: P49686; IntAct: EBI-12310,EBI-9145; Score: 0.44
DE  Interaction: P49687; IntAct: EBI-9145,EBI-11730; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-9145,EBI-12315; Score: 0.59
DE  Interaction: Q02629; IntAct: EBI-9145,EBI-11698; Score: 0.82
DE  Interaction: Q02630; IntAct: EBI-9145,EBI-11703; Score: 0.67
DE  Interaction: Q02821; IntAct: EBI-1797,EBI-9145; Score: 0.94
DE  Interaction: Q03790; IntAct: EBI-9145,EBI-27321; Score: 0.44
DE  Interaction: Q05166; IntAct: EBI-9145,EBI-3035; Score: 0.44
DE  Interaction: P32562; IntAct: EBI-4440,EBI-9145; Score: 0.53
DE  Interaction: P53687; IntAct: EBI-8705,EBI-9145; Score: 0.35
DE  Interaction: P22216; IntAct: EBI-17843,EBI-9145; Score: 0.67
DE  Interaction: P36124; IntAct: EBI-16993,EBI-9145; Score: 0.53
DE  Interaction: Q04116; IntAct: EBI-2889005,EBI-9145; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-9145,EBI-8627; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-9145,EBI-8632; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-9145,EBI-8603; Score: 0.53
DE  Interaction: P39079; IntAct: EBI-9145,EBI-19077; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-9145; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-9145; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-9145,EBI-8666; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-9145,EBI-29684; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-9145,EBI-3949; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-9145; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-3003,EBI-9145; Score: 0.35
DE  Interaction: Q12495; IntAct: EBI-3913,EBI-9145; Score: 0.53
DE  Interaction: Q12529; IntAct: EBI-2887498,EBI-9145; Score: 0.35
DE  Interaction: P39723; IntAct: EBI-20675,EBI-9145; Score: 0.35
DE  Interaction: P27692; IntAct: EBI-17937,EBI-9145; Score: 0.35
DE  Interaction: P39004; IntAct: EBI-8790,EBI-9145; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-26585,EBI-9145; Score: 0.35
DE  Interaction: Q04182; IntAct: EBI-13072,EBI-9145; Score: 0.35
DE  Interaction: Q04673; IntAct: EBI-18198,EBI-9145; Score: 0.35
DE  Interaction: Q12149; IntAct: EBI-1782,EBI-9145; Score: 0.69
DE  Interaction: Q12476; IntAct: EBI-31475,EBI-9145; Score: 0.35
DE  Interaction: Q02724; IntAct: EBI-20050,EBI-9145; Score: 0.56
DE  Interaction: P13259; IntAct: EBI-5254,EBI-9145; Score: 0.35
DE  Interaction: Q04779; IntAct: EBI-28153,EBI-9145; Score: 0.35
DE  Interaction: P38703; IntAct: EBI-10035,EBI-9145; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-13638,EBI-9145; Score: 0.35
DE  Interaction: Q00578; IntAct: EBI-14683,EBI-9145; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-17136,EBI-9145; Score: 0.35
DE  Interaction: Q12504; IntAct: EBI-30749,EBI-9145; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-29626,EBI-9145; Score: 0.35
DE  Interaction: P26755; IntAct: EBI-14981,EBI-9145; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-14971,EBI-9145; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-33556,EBI-9145; Score: 0.67
DE  Interaction: P32337; IntAct: EBI-9159,EBI-9145; Score: 0.35
DE  Interaction: P38111; IntAct: EBI-6668,EBI-9145; Score: 0.27
DE  Interaction: P14832; IntAct: EBI-5463,EBI-9145; Score: 0.27
DE  Interaction: Q06218; IntAct: EBI-5640,EBI-9145; Score: 0.27
DE  Interaction: P19414; IntAct: EBI-2104,EBI-9145; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-9145; Score: 0.27
DE  Interaction: P38219; IntAct: EBI-9145,EBI-21409; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-9145,EBI-14372; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-9145,EBI-18986; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-9145,EBI-6314; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-9145,EBI-7218; Score: 0.35
DE  Interaction: P18888; IntAct: EBI-9145,EBI-17550; Score: 0.35
DE  Interaction: P19358; IntAct: EBI-9145,EBI-10795; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-9145,EBI-10789; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-9145,EBI-16037; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-9145,EBI-11191; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-9145,EBI-7442; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-25778,EBI-9145; Score: 0.35
DE  Interaction: P47026; IntAct: EBI-25989,EBI-9145; Score: 0.35
DE  Interaction: P53911; IntAct: EBI-28927,EBI-9145; Score: 0.56
GO  GO:0005737;
GO  GO:0042564;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0097718;
GO  GO:0061676;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0005087;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051292;
GO  GO:0006656;
GO  GO:0006606;
GO  GO:0006612;
GO  GO:0046822;
GO  GO:0060188;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRILAALTLKNELVSKDSVKTQQF
SQ  AQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIAAIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALG
SQ  YMCESADPQSQALVSSSNNILIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV
SQ  QAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDIAYELAQFPQSPLQSYNFALS
SQ  SIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQNCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGP
SQ  DKVQRTYYVHQALPSILNLMNDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL
SQ  VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSASISTFVMDKLGQTMSVDENQ
SQ  LTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMGLFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETF
SQ  SPYLLKALNQVDSPVSITAVGFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY
SQ  LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIFQFIAQVAEDPQLYSEDATSR
SQ  AAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLFSQATKDTARWAREQQKRQLSL
//
ID  Q13261;
PN  Soluble interleukin-15 receptor subunit alpha;
GN  IL15RA;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000269|PubMed:10480910}; Single- pass type I membrane protein {ECO:0000269|PubMed:10480910}. Nucleus membrane {ECO:0000269|PubMed:10480910}; Single-pass type I membrane protein {ECO:0000269|PubMed:10480910}. Cell surface {ECO:0000269|PubMed:15123770}. Note=Mainly found associated with the nuclear membrane. [Isoform 5]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 6]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 7]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space {ECO:0000269|PubMed:15265897}.
DR  UNIPROT: Q13261;
DR  UNIPROT: B4E2C2;
DR  UNIPROT: Q3B769;
DR  UNIPROT: Q5JVA1;
DR  UNIPROT: Q5JVA2;
DR  UNIPROT: Q5JVA4;
DR  UNIPROT: Q6B0J2;
DR  UNIPROT: Q7LDR4;
DR  UNIPROT: Q7Z609;
DR  PDB: 2ERS;
DR  PDB: 2Z3Q;
DR  PDB: 2Z3R;
DR  PDB: 4GS7;
DR  PROSITE: PS50923;
DR  OMIM: 601070;
DR  DisGeNET: 3601;
DE  Function: High-affinity receptor for interleukin-15 (PubMed:8530383). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (By similarity). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (PubMed:15123770). In neutrophils, required for IL15- induced phagocytosis in a SYK-dependent manner (PubMed:15123770). Expression of different isoforms may alter or interfere with signal transduction (PubMed:10480910). {ECO:0000250|UniProtKB:Q60819, ECO:0000269|PubMed:10480910, ECO:0000269|PubMed:15123770, ECO:0000269|PubMed:8530383}. [Isoform 5]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 6]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 7]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 8]: Does not bind IL15. {ECO:0000269|PubMed:10480910}.
DE  Reference Proteome: Yes;
DE  Interaction: O95999; IntAct: EBI-958922,EBI-980354; Score: 0.37
DE  Interaction: P11802; IntAct: EBI-295644,EBI-980354; Score: 0.37
DE  Interaction: P24941; IntAct: EBI-980354,EBI-375096; Score: 0.37
DE  Interaction: P35243; IntAct: EBI-954661,EBI-980354; Score: 0.37
DE  Interaction: O14936; IntAct: EBI-1215506,EBI-980354; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-980354,EBI-473160; Score: 0.37
DE  Interaction: P40933; IntAct: EBI-980354,EBI-980274; Score: 0.66
GO  GO:0009986;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0004896;
GO  GO:0042010;
GO  GO:0019901;
GO  GO:0035723;
GO  GO:0050766;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKA
SQ  TNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPST
SQ  GTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVE
SQ  MEAMEALPVTWGTSSRDEDLENCSHHL
//
ID  P39962;
PN  Casein kinase I homolog 3;
GN  YCK3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane; Lipid-anchor; Cytoplasmic side. Nucleus membrane; Lipid-anchor; Cytoplasmic side. Vacuole membrane; Lipid-anchor; Cytoplasmic side. Note=Targeting to the vacuolar membrane may depend on AP-3 pathway.
DR  UNIPROT: P39962;
DR  UNIPROT: D3DM29;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
DE  Reference Proteome: Yes;
DE  Interaction: P50222; IntAct: EBI-748397,EBI-4740; Score: 0.56
GO  GO:0005737;
GO  GO:0000324;
GO  GO:0000329;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:14668479};
SQ  MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRI
SQ  LNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQ
SQ  YQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLG
SQ  HVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALR
SQ  LNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKS
SQ  RISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTN
SQ  LANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC
//
ID  Q91ZP3;
PN  Phosphatidate phosphatase LPIN1;
GN  Lpin1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Mitochondrion outer membrane {ECO:0000269|PubMed:21397848}. Cytoplasm {ECO:0000269|PubMed:21397848}. Nucleus membrane {ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion outer membrane following phosphatidic acid formation mediated by PLD6. In neuronals cells, isoform 1 is exclusively cytoplasmic. In 3T3-L1 pre-adipocytes, it primarily located in the cytoplasm. [Isoform 2]: Nucleus. Cytoplasm. Endoplasmic reticulum membrane. Note=Nuclear localization requires both CNEP1R1 and CTDNEP1. In neuronals cells, localized in both the cytoplasm and the nucleus. In 3T3-L1 pre-adipocytes, it is predominantly nuclear.
DR  UNIPROT: Q91ZP3;
DR  UNIPROT: Q9CQI2;
DR  UNIPROT: Q9JLG6;
DR  Pfam: PF16876;
DR  Pfam: PF04571;
DR  Pfam: PF08235;
DE  Function: Plays important roles in controlling the metabolism of fatty acids at different levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression. Is involved in adipocyte differentiation. Isoform 1 is recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol. {ECO:0000269|PubMed:16950137}.
DE  Disease: Note=Defects in Lpin1 are the cause of the fatty liver dystrophy phenotype (fld). Fld mutant mices are characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. Adipose tissue deficiency, glucose intolerance and increased susceptibility to atherosclerosis are associated with this mutation too. Two independent mutant alleles are characterized in this phenotype, fld and fld2j.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005667;
GO  GO:0042826;
GO  GO:0042975;
GO  GO:0008195;
GO  GO:0001085;
GO  GO:0003713;
GO  GO:0031532;
GO  GO:0044255;
GO  GO:0032869;
GO  GO:0045444;
GO  GO:0009062;
GO  GO:0006955;
GO  GO:0006629;
GO  GO:0000266;
GO  GO:0000122;
GO  GO:0120162;
GO  GO:0031065;
GO  GO:0045944;
GO  GO:0045598;
GO  GO:0031529;
GO  GO:0019432;
GO  GO:0006642;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL
SQ  GDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRR
SQ  KAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSP
SQ  SSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSS
SQ  PHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKA
SQ  PYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSG
SQ  IDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAM
SQ  QAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHA
SQ  AAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRS
SQ  DTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHRE
SQ  VIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVV
SQ  DHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA
//
ID  Q93WC9;
PN  Adenylate isopentenyltransferase 3, chloroplastic;
GN  IPT3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Plastid, chloroplast {ECO:0000269|PubMed:14726522}. Nucleus membrane {ECO:0000269|PubMed:18184738}; Lipid-anchor {ECO:0000269|PubMed:18184738}. Cytoplasm {ECO:0000269|PubMed:18184738}. Note=Farnesylation directs most of the protein to the nucleus/cytoplasm despite the presence of a chloroplast transit peptide (PubMed:18184738).
DR  UNIPROT: Q93WC9;
DR  UNIPROT: Q9LYB1;
DR  Pfam: PF01715;
DE  Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP. {ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742, ECO:0000269|PubMed:17062755}.
DE  Reference Proteome: Yes;
GO  GO:0009507;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0009536;
GO  GO:0052623;
GO  GO:0009824;
GO  GO:0005524;
GO  GO:0052622;
GO  GO:0052381;
GO  GO:0009691;
GO  GO:0006400;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18184738};
SQ  MIMKISMAMCKQPLPPSPTLDFPPARFGPNMLTLNPYGPKDKVVVIMGATGTGKSRLSVDIATRFRAEIINSDKIQVHQG
SQ  LDIVTNKITSEESCGVPHHLLGVLPPEADLTAANYCHMANLSIESVLNRGKLPIIVGGSNSYVEALVDDKENKFRSRYDC
SQ  CFLWVDVALPVLHGFVSERVDKMVESGMVEEVREFFDFSNSDYSRGIKKAIGFPEFDRFFRNEQFLNVEDREELLSKVLE
SQ  EIKRNTFELACRQREKIERLRKVKKWSIQRVDATPVFTKRRSKMDANVAWERLVAGPSTDTVSRFLLDIASRRPLVEAST
SQ  AVAAAMERELSRCLVA
//
ID  Q22663;
PN  Globin-like protein 26;
GN  glb;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Nucleus lamina {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Cell membrane {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Note=Transported to the nucleus by myristoylation of the N-terminal glycine. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}.
DR  UNIPROT: Q22663;
DR  Pfam: PF00042;
DE  Function: Plays a role in electron transport. Utilizes the bis-histidyl hexacoordinated complex with iron to transfer electrons to cytochrome c and molecular oxygen. Plays a regulatory role in the periodicity of the defecation cycle under oxidative stress conditions. Not involved in imparting protection against general conditions of oxidative stress. May participate in redox reactions under anaerobic conditions. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:21674044, ECO:0000269|PubMed:23251335}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005652;
GO  GO:0005886;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0019825;
GO  GO:0005344;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23251335};
SQ  MGSSTSTPAPPPKKNKPEGRKADNQILNSYQKSIVRNAWRHMSQKGPSNCGSTITRRMMARKSTIGDILDRSTLDYHNLQ
SQ  IVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYRRSKGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQ
SQ  LRFGYSRGLHVQGSRETKEDDEE
//
ID  Q6P9B9;
PN  Integrator complex subunit 5;
GN  INTS5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:23904267}.
DR  UNIPROT: Q6P9B9;
DR  UNIPROT: Q8N6W5;
DR  UNIPROT: Q9C0G5;
DR  Pfam: PF14838;
DR  Pfam: PF14837;
DR  OMIM: 611349;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-7600112; Score: 0.35
DE  Interaction: Q76MZ3; IntAct: EBI-400413,EBI-7600112; Score: 0.35
DE  Interaction: E9Q512; IntAct: EBI-11157440,EBI-7600112; Score: 0.35
DE  Interaction: Q96SY0; IntAct: EBI-4409724,EBI-7600112; Score: 0.35
DE  Interaction: Q8IX90; IntAct: EBI-1773976,EBI-7600112; Score: 0.35
DE  Interaction: P80315; IntAct: EBI-772370,EBI-7600112; Score: 0.35
DE  Interaction: Q8BH65; IntAct: EBI-11109879,EBI-7600112; Score: 0.35
DE  Interaction: Q9D1D4; IntAct: EBI-6999360,EBI-7600112; Score: 0.35
DE  Interaction: Q9CY25; IntAct: EBI-2553800,EBI-7600112; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-8322817,EBI-7600112; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-712311,EBI-7600112; Score: 0.53
DE  Interaction: P46013; IntAct: EBI-876367,EBI-7600112; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-1046513,EBI-7600112; Score: 0.35
DE  Interaction: P60410; IntAct: EBI-7600112,EBI-10171774; Score: 0.56
DE  Interaction: P30153; IntAct: EBI-302388,EBI-7600112; Score: 0.46
DE  Interaction: A5YKK6; IntAct: EBI-1222758,EBI-7600112; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-18539709,EBI-7600112; Score: 0.35
DE  Interaction: P35613-2; IntAct: EBI-11037868,EBI-7600112; Score: 0.35
DE  Interaction: Q9UQV4; IntAct: EBI-3924202,EBI-7600112; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-6655721,EBI-7600112; Score: 0.35
DE  Interaction: Q8WWB7-2; IntAct: EBI-21518323,EBI-7600112; Score: 0.35
DE  Interaction: Q9UN75-2; IntAct: EBI-21510478,EBI-7600112; Score: 0.35
DE  Interaction: O43493-2; IntAct: EBI-21537762,EBI-7600112; Score: 0.35
DE  Interaction: Q8WVE6; IntAct: EBI-10264837,EBI-7600112; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-1047508,EBI-7600112; Score: 0.35
DE  Interaction: P08173; IntAct: EBI-6655217,EBI-7600112; Score: 0.35
DE  Interaction: P40259-2; IntAct: EBI-21668936,EBI-7600112; Score: 0.35
DE  Interaction: P01375; IntAct: EBI-359977,EBI-7600112; Score: 0.35
DE  Interaction: P10909-2; IntAct: EBI-16399180,EBI-7600112; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0034472;
GO  GO:0016180;
GO  GO:0042795;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGV
SQ  FDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYS
SQ  GQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIIS
SQ  RVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDS
SQ  LAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASG
SQ  AGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNH
SQ  VGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLAR
SQ  VHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALS
SQ  PSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVS
SQ  ASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWG
SQ  APILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRG
SQ  LLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKF
SQ  IFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT
//
ID  P38217;
PN  Importin subunit beta-2;
GN  KAP104;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:8849456}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:8849456}. Nucleus {ECO:0000269|PubMed:8849456}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:8849456}.
DR  UNIPROT: P38217;
DR  UNIPROT: D6VQ19;
DR  Pfam: PF02985;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins (PubMed:8849456, PubMed:9488461, PubMed:10506153, PubMed:19366694). The complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran- mediated substrate release requires RNA (PubMed:10506153). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). {ECO:0000269|PubMed:10506153, ECO:0000269|PubMed:19366694, ECO:0000269|PubMed:8849456, ECO:0000269|PubMed:9488461, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P22147; IntAct: EBI-9152,EBI-9642; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-9152,EBI-10420; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-9152; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-9152,EBI-8648; Score: 0.35
DE  Interaction: P46988; IntAct: EBI-9152,EBI-13224; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-9152; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-9152; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-9152,EBI-8632; Score: 0.35
DE  Interaction: P25303; IntAct: EBI-16711,EBI-9152; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-11178,EBI-9152; Score: 0.53
DE  Interaction: P32340; IntAct: EBI-11961,EBI-9152; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-13686,EBI-9152; Score: 0.35
DE  Interaction: P50085; IntAct: EBI-23530,EBI-9152; Score: 0.35
DE  Interaction: P53045; IntAct: EBI-6506,EBI-9152; Score: 0.35
DE  Interaction: Q04182; IntAct: EBI-13072,EBI-9152; Score: 0.35
DE  Interaction: Q99190; IntAct: EBI-31149,EBI-9152; Score: 0.35
DE  Interaction: P18414; IntAct: EBI-6526,EBI-9152; Score: 0.35
DE  Interaction: P53217; IntAct: EBI-23120,EBI-9152; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-9152,EBI-20254; Score: 0.53
DE  Interaction: P07259; IntAct: EBI-9152,EBI-14372; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-9152,EBI-18986; Score: 0.53
DE  Interaction: P09733; IntAct: EBI-9152,EBI-18976; Score: 0.53
DE  Interaction: P02994; IntAct: EBI-9152,EBI-6314; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-9152,EBI-8603; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-9152,EBI-16054; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-9152,EBI-16037; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-9152,EBI-15447; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-9152,EBI-15398; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-9152,EBI-11191; Score: 0.35
DE  Interaction: P32505; IntAct: EBI-9152,EBI-11770; Score: 0.85
DE  Interaction: P40069; IntAct: EBI-9152,EBI-9166; Score: 0.35
DE  Interaction: Q99383; IntAct: EBI-9152,EBI-11783; Score: 0.74
DE  Interaction: P33892; IntAct: EBI-9152,EBI-7442; Score: 0.44
DE  Interaction: P38737; IntAct: EBI-9152,EBI-24359; Score: 0.44
DE  Interaction: Q03690; IntAct: EBI-9152,EBI-8989; Score: 0.44
DE  Interaction: P40035; IntAct: EBI-22551,EBI-9152; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-10067,EBI-9152; Score: 0.35
DE  Interaction: P19414; IntAct: EBI-2104,EBI-9152; Score: 0.27
DE  Interaction: P37898; IntAct: EBI-1998,EBI-9152; Score: 0.27
GO  GO:0005935;
GO  GO:0005934;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0010458;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASTWKPAEDYVLQLATLLQNCMSPNPEIRNNAMEAMENFQLQPEFLNYLCYILIEGESDDVLKQHYSLQDLQNNRATAG
SQ  MLLKNSMLGGNNLIKSNSHDLGYVKSNIIHGLYNSNNNLVSNVTGIVITTLFSTYYRQHRDDPTGLQMLYQLLELTSNGN
SQ  EPSIKALSKIMEDSAQFFQLEWSGNTKPMEALLDSFFRFISNPNFSPVIRSESVKCINTVIPLQTQSFIVRLDKFLEIIF
SQ  QLAQNDENDLVRAQICISFSFLLEFRPDKLVSHLDGIVQFMLHLITTVNEEKVAIEACEFLHAFATSPNIPEHILQPYVK
SQ  DIVPILLSKMVYNEESIVLLEASNDDDAFLEDKDEDIKPIAPRIVKKKEAGNGEDADDNEDDDDDDDDEDGDVDTQWNLR
SQ  KCSAATLDVMTNILPHQVMDIAFPFLREHLGSDRWFIREATILALGAMAEGGMKYFNDGLPALIPFLVEQLNDKWAPVRK
SQ  MTCWTLSRFSPWILQDHTEFLIPVLEPIINTLMDKKKDVQEAAISSVAVFIENADSELVETLFYSQLLTSFDKCLKYYKK
SQ  KNLIILYDAIGRFAEKCALDETAMQIILPPLIEKWALLSDSDKELWPLLECLSCVASSLGERFMPMAPEVYNRAFRILCH
SQ  CVELEAKSHQDPTIVVPEKDFIITSLDLIDGLVQGLGAHSQDLLFPQGTKDLTILKIMLECLQDPVHEVRQSCFALLGDI
SQ  VYFFNSELVIGNLEDFLKLIGTEIMHNDDSDGTPAVINAIWALGLISERIDLNTYIIDMSRIILDLFTTNTQIVDSSVME
SQ  NLSVTIGKMGLTHPEVFSSGAFANDSNWNKWCLSVNALDDVEEKSSAYMGFLKIINLTSTEVTMSNDTIHKIVTGLSSNV
SQ  EANVFAQEIYTFLMNHSAQISAINFTPDEISFLQQFTS
//
ID  P40358;
PN  DnaJ-like chaperone JEM1;
GN  JEM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9148890}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9148890}. Nucleus membrane {ECO:0000269|PubMed:15282802}.
DR  UNIPROT: P40358;
DR  UNIPROT: D6VWB0;
DR  Pfam: PF00226;
DR  PROSITE: PS50076;
DE  Function: Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating. {ECO:0000269|PubMed:9148890}.
DE  Reference Proteome: Yes;
DE  Interaction: P32499; IntAct: EBI-12401,EBI-25940; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-11756,EBI-25940; Score: 0.35
DE  Interaction: P39685; IntAct: EBI-25940,EBI-12739; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-20731,EBI-25940; Score: 0.35
DE  Interaction: P80210; IntAct: EBI-25940,EBI-14267; Score: 0.35
DE  Interaction: P38009; IntAct: EBI-25940,EBI-14223; Score: 0.35
DE  Interaction: P53730; IntAct: EBI-25940,EBI-28496; Score: 0.35
DE  Interaction: P36000; IntAct: EBI-2206,EBI-25940; Score: 0.35
DE  Interaction: P38328; IntAct: EBI-25940,EBI-2777; Score: 0.35
DE  Interaction: Q12386; IntAct: EBI-25940,EBI-2967; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-25940,EBI-3003; Score: 0.35
DE  Interaction: P43583; IntAct: EBI-25940,EBI-22761; Score: 0.35
DE  Interaction: P48361; IntAct: EBI-2993,EBI-25940; Score: 0.35
DE  Interaction: P14682; IntAct: EBI-19730,EBI-25940; Score: 0.35
DE  Interaction: P53622; IntAct: EBI-4860,EBI-25940; Score: 0.35
DE  Interaction: P53859; IntAct: EBI-1731,EBI-25940; Score: 0.35
DE  Interaction: Q03375; IntAct: EBI-30409,EBI-25940; Score: 0.35
DE  Interaction: P40487; IntAct: EBI-25162,EBI-25940; Score: 0.35
DE  Interaction: P32898; IntAct: EBI-25940,EBI-22092; Score: 0.35
DE  Interaction: P32461; IntAct: EBI-25940,EBI-6090; Score: 0.35
DE  Interaction: P40557; IntAct: EBI-24929,EBI-25940; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-28537,EBI-25940; Score: 0.35
DE  Interaction: P53849; IntAct: EBI-25940,EBI-29244; Score: 0.35
DE  Interaction: P25569; IntAct: EBI-21727,EBI-25940; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-25940,EBI-5612; Score: 0.35
DE  Interaction: P61830; IntAct: EBI-25940,EBI-8098; Score: 0.35
DE  Interaction: P00815; IntAct: EBI-25940,EBI-8334; Score: 0.35
DE  Interaction: P17629; IntAct: EBI-8526,EBI-25940; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-9068,EBI-25940; Score: 0.35
DE  Interaction: P50094; IntAct: EBI-9195,EBI-25940; Score: 0.35
DE  Interaction: P25642; IntAct: EBI-25940,EBI-9217; Score: 0.35
DE  Interaction: P40089; IntAct: EBI-25940,EBI-10236; Score: 0.35
DE  Interaction: P40070; IntAct: EBI-188,EBI-25940; Score: 0.35
DE  Interaction: P35192; IntAct: EBI-10346,EBI-25940; Score: 0.35
DE  Interaction: Q12387; IntAct: EBI-5736,EBI-25940; Score: 0.35
DE  Interaction: P46151; IntAct: EBI-11567,EBI-25940; Score: 0.35
DE  Interaction: P33441; IntAct: EBI-25940,EBI-10841; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-3903,EBI-25940; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-25940,EBI-11835; Score: 0.35
DE  Interaction: P12945; IntAct: EBI-11868,EBI-25940; Score: 0.35
DE  Interaction: Q07896; IntAct: EBI-25940,EBI-36093; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-25940,EBI-28532; Score: 0.35
DE  Interaction: Q12499; IntAct: EBI-12126,EBI-25940; Score: 0.35
DE  Interaction: P53261; IntAct: EBI-13145,EBI-25940; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-25940,EBI-12114; Score: 0.35
DE  Interaction: P50874; IntAct: EBI-12584,EBI-25940; Score: 0.35
DE  Interaction: P32896; IntAct: EBI-25940,EBI-13004; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-25940,EBI-9428; Score: 0.35
DE  Interaction: P16862; IntAct: EBI-25940,EBI-9435; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-13275,EBI-25940; Score: 0.35
DE  Interaction: P32345; IntAct: EBI-25940,EBI-12759; Score: 0.35
DE  Interaction: P32263; IntAct: EBI-25940,EBI-13885; Score: 0.35
DE  Interaction: Q12417; IntAct: EBI-25940,EBI-710; Score: 0.35
DE  Interaction: P40164; IntAct: EBI-29107,EBI-25940; Score: 0.35
DE  Interaction: P06777; IntAct: EBI-14752,EBI-25940; Score: 0.35
DE  Interaction: Q04231; IntAct: EBI-27726,EBI-25940; Score: 0.35
DE  Interaction: P12753; IntAct: EBI-25940,EBI-14700; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-25940,EBI-14971; Score: 0.35
DE  Interaction: P26754; IntAct: EBI-25940,EBI-14976; Score: 0.35
DE  Interaction: P21524; IntAct: EBI-15234,EBI-25940; Score: 0.35
DE  Interaction: P27999; IntAct: EBI-15798,EBI-25940; Score: 0.35
DE  Interaction: P07703; IntAct: EBI-15831,EBI-25940; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-25940,EBI-15913; Score: 0.35
DE  Interaction: Q05022; IntAct: EBI-16011,EBI-25940; Score: 0.35
DE  Interaction: P40856; IntAct: EBI-25940,EBI-16384; Score: 0.35
DE  Interaction: Q12745; IntAct: EBI-31898,EBI-25940; Score: 0.35
DE  Interaction: Q03067; IntAct: EBI-25940,EBI-34550; Score: 0.35
DE  Interaction: P39000; IntAct: EBI-25940,EBI-22627; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-25940,EBI-17148; Score: 0.35
DE  Interaction: P17883; IntAct: EBI-25940,EBI-1861; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-17402,EBI-25940; Score: 0.35
DE  Interaction: P43321; IntAct: EBI-529,EBI-25940; Score: 0.35
DE  Interaction: P32558; IntAct: EBI-4334,EBI-25940; Score: 0.35
DE  Interaction: P32585; IntAct: EBI-25940,EBI-18032; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-6329,EBI-25940; Score: 0.35
DE  Interaction: P43637; IntAct: EBI-9668,EBI-25940; Score: 0.35
DE  Interaction: P22515; IntAct: EBI-19703,EBI-25940; Score: 0.35
DE  Interaction: P39538; IntAct: EBI-25940,EBI-19884; Score: 0.35
DE  Interaction: P50101; IntAct: EBI-19898,EBI-25940; Score: 0.35
DE  Interaction: P54860; IntAct: EBI-20003,EBI-25940; Score: 0.35
DE  Interaction: P32861; IntAct: EBI-25940,EBI-19987; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-25940,EBI-20627; Score: 0.35
DE  Interaction: Q12457; IntAct: EBI-25940,EBI-33699; Score: 0.35
DE  Interaction: P40521; IntAct: EBI-3655056,EBI-25940; Score: 0.35
DE  Interaction: P40566; IntAct: EBI-25940,EBI-3657860; Score: 0.35
DE  Interaction: P36076; IntAct: EBI-26778,EBI-25940; Score: 0.35
DE  Interaction: P38746; IntAct: EBI-27201,EBI-25940; Score: 0.35
DE  Interaction: Q07825; IntAct: EBI-32387,EBI-25940; Score: 0.35
DE  Interaction: Q08422; IntAct: EBI-30793,EBI-25940; Score: 0.35
DE  Interaction: Q12532; IntAct: EBI-25940,EBI-33283; Score: 0.35
DE  Interaction: P46951; IntAct: EBI-25940,EBI-23455; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-13246,EBI-25940; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0051087;
GO  GO:0051787;
GO  GO:0051082;
GO  GO:0000742;
GO  GO:0034975;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIY
SQ  YKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDV
SQ  SVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNS
SQ  DASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDT
SQ  NFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCK
SQ  KSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSES
SQ  TNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLN
SQ  LTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFK
SQ  MNFGL
//
ID  O60318;
PN  Germinal-center associated nuclear protein;
GN  MCM3AP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: [Isoform GANP]: Nucleus envelope {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:28633435}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20005110}. Chromosome {ECO:0000269|PubMed:23652018}. Note=Predominantly located at the nuclear envelope, facing the nucleus interior (PubMed:20005110, PubMed:21195085, PubMed:23591820). Localization at the nuclear pore complex requires NUP153, TPR and ALYREF/ALY (PubMed:23591820, PubMed:22307388). Also found associated with chromatin (PubMed:23652018). In B-cells, targeted to the immunoglobulin variable region genes (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}. [Isoform MCM3AP]: Cytoplasm {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Nucleus {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Note=Translocates into the nucleus in the presence of MCM3 (PubMed:12226073). Associates with chromatin possibly through interaction with MCM3 (PubMed:12226073). {ECO:0000269|PubMed:12226073}.
DR  UNIPROT: O60318;
DR  UNIPROT: C9JL56;
DR  UNIPROT: Q2M3C1;
DR  UNIPROT: Q6PJP6;
DR  UNIPROT: Q9BSY5;
DR  UNIPROT: Q9UMT4;
DR  PDB: 4DHX;
DR  Pfam: PF16766;
DR  Pfam: PF16769;
DR  Pfam: PF16768;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DR  OMIM: 603294;
DR  OMIM: 618124;
DR  DisGeNET: 8888;
DE  Function: [Isoform GANP]: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:20005110, PubMed:20384790, PubMed:23591820, PubMed:22307388). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:20384790, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}. [Isoform MCM3AP]: Binds to and acetylates the replication protein MCM3. Plays a role in the initiation of DNA replication and participates in controls that ensure that DNA replication initiates only once per cell cycle (PubMed:11258703, PubMed:12226073). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:11258703, ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:23652018}.
DE  Disease: Peripheral neuropathy, autosomal recessive, with or without impaired intellectual development (PNRIID) [MIM:618124]: An autosomal recessive disorder characterized by early childhood-onset of peripheral sensorimotor neuropathy, progressive distal muscle weakness, atrophy in hands and feet, and gait difficulties, often with loss of ambulation. Most affected individuals also have impaired intellectual development, although some have normal cognition. Additional features may include eye movement abnormalities, claw hands, foot deformities, and scoliosis. {ECO:0000269|PubMed:24123876, ECO:0000269|PubMed:28633435, ECO:0000269|PubMed:28969388, ECO:0000269|PubMed:29982295}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRI5; IntAct: EBI-308480,EBI-529989; Score: 0.37
DE  Interaction: P25054; IntAct: EBI-308480,EBI-727707; Score: 0.37
DE  Interaction: P60953; IntAct: EBI-81752,EBI-308480; Score: 0.37
DE  Interaction: P63000; IntAct: EBI-308480,EBI-413628; Score: 0.37
DE  Interaction: Q5NGE6; IntAct: EBI-2796264,EBI-308480; Score: 0.37
DE  Interaction: P30304; IntAct: EBI-747671,EBI-308480; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-308480,EBI-347928; Score: 0.37
DE  Interaction: Q8BUH2; IntAct: EBI-10962405,EBI-308480; Score: 0.35
DE  Interaction: Q9BVG8; IntAct: EBI-2125614,EBI-308480; Score: 0.35
DE  Interaction: Q9NSK0; IntAct: EBI-949319,EBI-308480; Score: 0.35
DE  Interaction: P13533; IntAct: EBI-1048066,EBI-308480; Score: 0.35
DE  Interaction: Q9CYN2; IntAct: EBI-9986662,EBI-308480; Score: 0.35
DE  Interaction: Q9R1K9; IntAct: EBI-2553037,EBI-308480; Score: 0.35
DE  Interaction: P54132; IntAct: EBI-621372,EBI-308480; Score: 0.35
DE  Interaction: Q09472; IntAct: EBI-447295,EBI-308480; Score: 0.37
DE  Interaction: Q7CIS2; IntAct: EBI-308480,EBI-2864684; Score: 0.37
DE  Interaction: A0A0H2W148; IntAct: EBI-2847163,EBI-308480; Score: 0.37
DE  Interaction: Q81KK8; IntAct: EBI-2822258,EBI-308480; Score: 0.37
DE  Interaction: Q81YE8; IntAct: EBI-2811064,EBI-308480; Score: 0.37
DE  Interaction: Q5NIJ3; IntAct: EBI-308480,EBI-2798422; Score: 0.37
DE  Interaction: A0A384KUI4; IntAct: EBI-2846272,EBI-308480; Score: 0.37
DE  Interaction: Q9NPA8; IntAct: EBI-308480,EBI-719226; Score: 0.37
DE  Interaction: Q9P0N5; IntAct: EBI-308480,EBI-721260; Score: 0.37
DE  Interaction: Q9UKK9; IntAct: EBI-308480,EBI-721623; Score: 0.37
DE  Interaction: Q14194; IntAct: EBI-473101,EBI-308480; Score: 0.37
DE  Interaction: Q15149; IntAct: EBI-308480,EBI-297903; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-308480; Score: 0.35
DE  Interaction: C5E524; IntAct: EBI-12561527,EBI-308480; Score: 0.35
DE  Interaction: Q194T2; IntAct: EBI-11515076,EBI-308480; Score: 0.35
DE  Interaction: Q9H0B3-2; IntAct: EBI-21526503,EBI-308480; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-2512818,EBI-308480; Score: 0.35
DE  Interaction: Q9BTL4; IntAct: EBI-2806011,EBI-308480; Score: 0.35
DE  Interaction: Q9NYQ7; IntAct: EBI-308480,EBI-308417; Score: 0.37
DE  Interaction: O94985; IntAct: EBI-308480,EBI-522075; Score: 0.37
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003682;
GO  GO:0010484;
GO  GO:0004402;
GO  GO:0042393;
GO  GO:0003676;
GO  GO:0006406;
GO  GO:0034728;
GO  GO:0016973;
GO  GO:0016446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSS
SQ  VGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGA
SQ  ESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKS
SQ  IFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDH
SQ  PPDKRPVRLNRPRGGTLFGRTIQDVFKSNKEVGRLGNKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETE
SQ  SREKKEDSLRGTPARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKKLAVVHFFD
SQ  HASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTEDAPFQHSPLGKAAGRTGASSLLNKSSPVK
SQ  KPSLLKAHQFEGDSFDSASEGSEGLGPCVLSLSTLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDM
SQ  CPEKERYMRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQKEGSLRDWY
SQ  DFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFC
SQ  ASEAEFQGYNVLLSLNKGDILREVQQFHPAVRNSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKD
SQ  ALRALNFAYTVSTQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSVFITRKLTV
SQ  SVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPVSTQRPGSDTVGGGRGEECGVEPDAPLSSLPQSLPAPAPSP
SQ  VPLPPVLALTPSVAPSLFQLSVQPEPPPPEPVPMYSDEDLAQVVDELIQEALQRDCEEVGSAGAAYAAAALGVSNAAMED
SQ  LLTAATTGILRHIAAEEVSKERERREQERQRAEEERLKQERELVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETD
SQ  QRVRVARCCEDVCAHLVDLFLVEEIFQTAKETLQELQCFCKYLQRWREAVTARKKLRRQMRAFPAAPCCVDVSDRLRALA
SQ  PSAECPIAEENLARGLLDLGHAGRLGISCTRLRRLRNKTAHQMKVQHFYQQLLSDVAWASLDLPSLVAEHLPGRQEHVFW
SQ  KLVLVLPDVEEQSPESCGRILANWLKVKFMGDEGSVDDTSSDAGGIQTLSLFNSLSSKGDQMISVNVCIKVAHGALSDGA
SQ  IDAVETQKDLLGASGLMLLLPPKMKSEDMAEEDVYWLSALLQLKQLLQAKPFQPALPLVVLVPSPGGDAVEKEVEDGLML
SQ  QDLVSAKLISDYTVTEIPDTINDLQGSTKVLQAVQWLVSHCPHSLDLCCQTLIQYVEDGIGHEFSGRFFHDRRERRLGGL
SQ  ASQEPGAIIELFNSVLQFLASVVSSEQLCDLSWPVTEFAEAGGSRLLPHLHWNAPEHLAWLKQAVLGFQLPQMDLPPLGA
SQ  PWLPVCSMVVQYASQIPSSRQTQPVLQSQVENLLHRTYCRWKSKSPSPVHGAGPSVMEIPWDDLIALCINHKLRDWTPPR
SQ  LPVTSEALSEDGQICVYFFKNDLKKYDVPLSWEQARLQTQKELQLREGRLAIKPFHPSANNFPIPLLHMHRNWKRSTECA
SQ  QEGRIPSTEDLMRGASAEELLAQCLSSSLLLEKEENKRFEDQLQQWLSEDSGAFTDLTSLPLYLPQTLVSLSHTIEPVMK
SQ  TSVTTSPQSDMMREQLQLSEATGTCLGERLKHLERLIRSSREEEVASELHLSALLDMVDI
//
ID  Q9QZ85;
PN  Interferon-inducible GTPase 1;
GN  Iigp1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Parasitophorous vacuole membrane. Note=Localizes to the bacterial inclusions formed following C.trachomatis infection. Accumulates in a GTP-bound form on the parasitophorous vacuole membranes formed following T.gondii infection but exists in a GDP-bound form in uninfected cells.
DR  UNIPROT: Q9QZ85;
DR  UNIPROT: Q9Z1M3;
DR  PDB: 1TPZ;
DR  PDB: 1TQ2;
DR  PDB: 1TQ4;
DR  PDB: 1TQ6;
DR  PDB: 1TQD;
DR  PDB: 4LV5;
DR  PDB: 4LV8;
DR  PDB: 5FPH;
DR  Pfam: PF05049;
DR  PROSITE: PS51716;
DE  Function: GTPase with low activity. Has higher affinity for GDP than for GTP. Plays a role in resistance to intracellular pathogens. Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite. Mediates resistance to C.trachomatis infection by targeting bacterial inclusions to autophagosomes for subsequent lysosomal destruction. {ECO:0000269|PubMed:11907101, ECO:0000269|PubMed:12732635, ECO:0000269|PubMed:16304607, ECO:0000269|PubMed:19242543}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0032580;
GO  GO:0031965;
GO  GO:0020005;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0035458;
GO  GO:0019221;
GO  GO:0006952;
GO  GO:0050829;
GO  GO:0042832;
GO  GO:0045087;
GO  GO:0010506;
GO  GO:0009617;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MGQLFSSPKSDENNDLPSSFTGYFKKFNTGRKIISQEILNLIELRMRKGNIQLTNSAISDALKEIDSSVLNVAVTGETGS
SQ  GKSSFINTLRGIGNEEEGAAKTGVVEVTMERHPYKHPNIPNVVFWDLPGIGSTNFPPNTYLEKMKFYEYDFFIIISATRF
SQ  KKNDIDIAKAISMMKKEFYFVRTKVDSDITNEADGKPQTFDKEKVLQDIRLNCVNTFRENGIAEPPIFLLSNKNVCHYDF
SQ  PVLMDKLISDLPIYKRHNFMVSLPNITDSVIEKKRQFLKQRIWLEGFAADLVNIIPSLTFLLDSDLETLKKSMKFYRTVF
SQ  GVDETSLQRLARDWEIEVDQVEAMIKSPAVFKPTDEETIQERLSRYIQEFCLANGYLLPKNSFLKEIFYLKYYFLDMVTE
SQ  DAKTLLKEICLRN
//
ID  Q96LT7;
PN  Guanine nucleotide exchange C9orf72;
GN  C9orf72;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:27037575}. Cytoplasm {ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:27037575, ECO:0000269|PubMed:27193190}. Cytoplasm, P-body {ECO:0000269|PubMed:27037575}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27037575}. Endosome {ECO:0000269|PubMed:24549040}. Lysosome {ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27559131}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24549040}. Secreted {ECO:0000269|PubMed:24549040}. Cell projection, axon {ECO:0000269|PubMed:27723745}. Cell projection, growth cone {ECO:0000269|PubMed:27723745}. Perikaryon {ECO:0000250|UniProtKB:Q6DFW0}. Note=Detected in the cytoplasm of neurons from brain tissue (PubMed:21944778). Detected in the nucleus in fibroblasts (PubMed:21944779). During corticogenesis, transitions from being predominantly cytoplasmic to a more even nucleocytoplasmic distribution (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:27037575}. [Isoform 1]: Perikaryon {ECO:0000269|PubMed:26174152}. Cell projection, dendrite {ECO:0000269|PubMed:26174152}. Note=Expressed diffusely throughout the cytoplasm and dendritic processes of cerebellar Purkinje cells. Also expressed diffusely throughout the cytoplasm of spinal motor neurons. {ECO:0000269|PubMed:26174152}. [Isoform 2]: Nucleus membrane {ECO:0000269|PubMed:26174152}; Peripheral membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:26174152}. Note=Detected at the nuclear membrane of cerebellar Purkinje cells and spinal motor neurons. Also shows diffuse nuclear expression in spinal motor neurons. {ECO:0000269|PubMed:26174152}.
DR  UNIPROT: Q96LT7;
DR  UNIPROT: A8K5W0;
DR  UNIPROT: D3DRK6;
DR  UNIPROT: G8I0B6;
DR  UNIPROT: Q6NUS9;
DR  Pfam: PF15019;
DR  PROSITE: PS51835;
DR  OMIM: 105550;
DR  OMIM: 614260;
DR  DisGeNET: 203228;
DE  Function: Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:27193190, PubMed:27103069, PubMed:27617292, PubMed:28195531). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP- bound form, thereby promoting autophagosome maturation (PubMed:27103069). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and modulating its protein kinase activity (PubMed:27617292). Positively regulates initiation of autophagy by regulating the RAB1A- dependent trafficking of the ATG1/ULK1 kinase complex to the phagophore which leads to autophagosome formation (PubMed:27334615). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131). Plays a role in endosomal trafficking (PubMed:24549040). May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:27559131, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:28195531}. [Isoform 1]: Regulates stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}. [Isoform 2]: Does not play a role in regulation of stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}.
DE  Disease: Frontotemporal dementia and/or amyotrophic lateral sclerosis 1 (FTDALS1) [MIM:105550]: An autosomal dominant neurodegenerative disorder characterized by adult onset of frontotemporal dementia and/or amyotrophic lateral sclerosis in an affected individual. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. {ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:22936364}. Note=The disease is caused by mutations affecting the gene represented in this entry. In the first intron of the gene, the expansion of a GGGGCC hexanucleotide that can vary from 10 to thousands of repeats, represents the most common genetic cause of both familial and sporadic FTDALS. The hexanucleotide repeat expansion (HRE) is structurally polymorphic and during transcription, is responsible for the formation of RNA and DNA G-quadruplexes resulting in the production of aborted transcripts at the expense of functional transcripts. The accumulation of those aborted transcripts may cause nucleolar stress and indirectly cell death (PubMed:24598541). The expanded GGGGCC repeats are bidirectionally transcribed into repetitive RNA, which forms sense and antisense RNA foci. Remarkably, despite being within a non-coding region, these repetitive RNAs can be translated in every reading frame to form five different dipeptide repeat proteins (DPRs) -- poly-GA, poly-GP, poly-GR, poly-PA and poly- PR -- via a non-canonical mechanism known as repeat-associated non-ATG (RAN) translation. These dipeptide repeat proteins (DPRs) co-aggregate in the characteristic SQSTM1-positive TARDBP negative inclusions found in FTLD/ALS patients with C9orf72 repeat expansion (PubMed:24132570). {ECO:0000269|PubMed:24132570, ECO:0000269|PubMed:24598541}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-2961725; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-2961725; Score: 0.35
DE  Interaction: Q96I36; IntAct: EBI-6570698,EBI-2961725; Score: 0.35
DE  Interaction: O43186; IntAct: EBI-748171,EBI-2961725; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-307352,EBI-2961725; Score: 0.56
DE  Interaction: Q13287; IntAct: EBI-372942,EBI-2961725; Score: 0.56
DE  Interaction: Q53XC2; IntAct: EBI-10288660,EBI-2961725; Score: 0.56
DE  Interaction: Q9BPX4; IntAct: EBI-2961725,EBI-10288788; Score: 0.56
DE  Interaction: Q8TDY2; IntAct: EBI-1047793,EBI-2961725; Score: 0.35
DE  Interaction: Q61539; IntAct: EBI-2312731,EBI-2961725; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-2961725; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-1047508,EBI-2961725; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-2961725; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-2961725; Score: 0.35
DE  Interaction: P62820; IntAct: EBI-2961725,EBI-716845; Score: 0.40
DE  Interaction: O75385; IntAct: EBI-2961725,EBI-908831; Score: 0.40
DE  Interaction: Q9H8Y1; IntAct: EBI-2961725,EBI-12894399; Score: 0.60
DE  Interaction: Q96SB4; IntAct: EBI-539478,EBI-2961725; Score: 0.44
DE  Interaction: P38432; IntAct: EBI-945751,EBI-2961725; Score: 0.56
DE  Interaction: Q86UV6-2; IntAct: EBI-10259086,EBI-2961725; Score: 0.56
DE  Interaction: Q8TEV9; IntAct: EBI-2961718,EBI-2961725; Score: 0.70
DE  Interaction: Q17R54; IntAct: EBI-12820047,EBI-2961725; Score: 0.56
DE  Interaction: P49770; IntAct: EBI-718773,EBI-2961725; Score: 0.67
DE  Interaction: O75817; IntAct: EBI-366574,EBI-2961725; Score: 0.56
DE  Interaction: Q9NP66; IntAct: EBI-740641,EBI-2961725; Score: 0.56
GO  GO:0005776;
GO  GO:0044295;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0032045;
GO  GO:0005764;
GO  GO:0044304;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0043204;
GO  GO:0005085;
GO  GO:0017137;
GO  GO:0006914;
GO  GO:0048675;
GO  GO:0006897;
GO  GO:1902774;
GO  GO:1904425;
GO  GO:0001933;
GO  GO:0016239;
GO  GO:0110053;
GO  GO:2000785;
GO  GO:0010506;
GO  GO:1903432;
GO  GO:0034063;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAI
SQ  DVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILE
SQ  GTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSS
SQ  AEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPP
SQ  CHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQ
SQ  FLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMT
SQ  F
//
ID  Q94F30;
PN  Ubiquitin-like-specific protease ESD4;
GN  ESD4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}; Peripheral membrane protein {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}. Note=The nuclear envelope localization is independent of the presence of the nuclear pore anchor NUA.
DR  UNIPROT: Q94F30;
DR  UNIPROT: B9DFG4;
DR  UNIPROT: O23439;
DR  UNIPROT: Q70G10;
DR  UNIPROT: Q7DLT0;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Acts predominantly as an isopeptidase, cleaving SUMO-conjugated proteins better than SUMO peptides. Plays an important role in the control of flowering time. {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:16740136}.
DE  Reference Proteome: Yes;
DE  Interaction: A4GSN8; IntAct: EBI-1545660,EBI-1545674; Score: 0.37
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0019900;
GO  GO:0070139;
GO  GO:0009911;
GO  GO:0016926;
GO  GO:0009909;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGAVAINRKRSDESFNFINQQSTNPLRNSPYFQASKKRRFSFAMSEDSGKPASSNPTISRISRYPDAKAPLRREIHAPSR
SQ  GILRYGKAKSNDYCEKDANFFVRKYDDAKRSALEALRFVNKGKDFVDLGDEVEKEEVVSDDSSVQAIEVIDCDDDEEKKN
SQ  LQPSFSSGVTDVKKGENFRVEDTSMMLDSLSLDRDVDNDASSLEAYRKLMQSAEKRNSKLEALGFEIVLNEKKLSLLRQS
SQ  RPKTVEKRVEVPREPFIPLTEDEEAEVYRAFSGRNRRKVLATHENSNIDITGEVLQCLTPSAWLNDEVINVYLELLKERE
SQ  TREPKKYLKCHYFNTFFYKKLVSDSGYNFKAVRRWTTQRKLGYALIDCDMIFVPIHRGVHWTLAVINNRESKLLYLDSLN
SQ  GVDPMILNALAKYMGDEANEKSGKKIDANSWDMEFVEDLPQQKNGYDCGMFMLKYIDFFSRGLGLCFSQEHMPYFRLRTA
SQ  KEILRLRAD
//
ID  Q96KC8;
PN  DnaJ homolog subfamily C member 1;
GN  DNAJC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
DR  UNIPROT: Q96KC8;
DR  UNIPROT: B0YIZ8;
DR  UNIPROT: Q5VX89;
DR  UNIPROT: Q9H6B8;
DR  PDB: 2CQQ;
DR  PDB: 2CQR;
DR  Pfam: PF00226;
DR  Pfam: PF00249;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51293;
DR  OMIM: 611207;
DR  DisGeNET: 64215;
DE  Function: May modulate protein synthesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-296550; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-296550; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-296550; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-296550; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-296550; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-296550; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-296550; Score: 0.35
DE  Interaction: Q5QGZ9-1; IntAct: EBI-21633104,EBI-296550; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-625518,EBI-296550; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-2903122,EBI-296550; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-8636612,EBI-296550; Score: 0.35
DE  Interaction: Q9NWS8; IntAct: EBI-296550,EBI-4401316; Score: 0.35
DE  Interaction: P31146; IntAct: EBI-296550,EBI-1046676; Score: 0.35
DE  Interaction: P10321; IntAct: EBI-296550,EBI-1051396; Score: 0.35
DE  Interaction: P80294; IntAct: EBI-296567,EBI-296550; Score: 0.37
DE  Interaction: P01011; IntAct: EBI-296550,EBI-296557; Score: 0.58
DE  Interaction: Q14409; IntAct: EBI-296550,EBI-20829609; Score: 0.40
DE  Interaction: P78329; IntAct: EBI-1752413,EBI-296550; Score: 0.56
DE  Interaction: P27449; IntAct: EBI-296550,EBI-721179; Score: 0.56
DE  Interaction: Q96FZ5; IntAct: EBI-296550,EBI-2807956; Score: 0.56
DE  Interaction: Q6RW13-2; IntAct: EBI-296550,EBI-11522760; Score: 0.56
DE  Interaction: O14798; IntAct: EBI-296550,EBI-717441; Score: 0.56
DE  Interaction: Q04941; IntAct: EBI-296550,EBI-608347; Score: 0.56
DE  Interaction: Q5SNT2-2; IntAct: EBI-296550,EBI-11994282; Score: 0.56
DE  Interaction: Q13296-2; IntAct: EBI-21513440,EBI-296550; Score: 0.35
DE  Interaction: Q9UHP7-2; IntAct: EBI-21517399,EBI-296550; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-2872118,EBI-296550; Score: 0.35
DE  Interaction: Q8NBR6-2; IntAct: EBI-21714163,EBI-296550; Score: 0.35
DE  Interaction: O95870; IntAct: EBI-296550,EBI-348517; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0045861;
GO  GO:0006457;
GO  GO:0050708;
GO  GO:0006417;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAPCSQPAQLPGRRQLGLVPFPPPPPRTPLLWLLLLLLAAVAPARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSAD
SQ  IRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFI
SQ  ILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPH
SQ  LIQDAGQFYAKYKETRLKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLETTYIQSYDHGTSIEEIEEQMDDWLENRN
SQ  RTQKKQAPEWTEEDLSQLTRSMVKFPGGTPGRWEKIAHELGRSVTDVTTKAKQLKDSVTCSPGMVRLSELKSTVQNSRPI
SQ  KTATTLPDDMITQREDAEGVAAEEEQEGDSGEQETGATDARPRRRKPARLLEATAKPEPEEKSRAKRQKDFDIAEQNESS
SQ  DEESLRKERARSAEEPWTQNQQKLLELALQQYPRGSSDRWDKIARCVPSKSKEDCIARYKLLVELVQKKKQAKS
//
ID  P10415;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000269|PubMed:2250705}. Nucleus membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000269|PubMed:2250705}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000269|PubMed:2250705}.
DR  UNIPROT: P10415;
DR  UNIPROT: C9JHD5;
DR  UNIPROT: P10416;
DR  UNIPROT: Q13842;
DR  UNIPROT: Q16197;
DR  PDB: 1G5M;
DR  PDB: 1GJH;
DR  PDB: 1YSW;
DR  PDB: 2O21;
DR  PDB: 2O22;
DR  PDB: 2O2F;
DR  PDB: 2W3L;
DR  PDB: 2XA0;
DR  PDB: 4AQ3;
DR  PDB: 4IEH;
DR  PDB: 4LVT;
DR  PDB: 4LXD;
DR  PDB: 4MAN;
DR  PDB: 5AGW;
DR  PDB: 5AGX;
DR  PDB: 5FCG;
DR  PDB: 5JSN;
DR  PDB: 5VAU;
DR  PDB: 5VAX;
DR  PDB: 5VAY;
DR  PDB: 6GL8;
DR  PDB: 6IWB;
DR  PDB: 6O0K;
DR  PDB: 6O0L;
DR  PDB: 6O0M;
DR  PDB: 6O0O;
DR  PDB: 6O0P;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DR  OMIM: 151430;
DR  DisGeNET: 596;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871}.
DE  Disease: Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.
DE  Reference Proteome: Yes;
DE  Interaction: O60238; IntAct: EBI-77694,EBI-849893; Score: 0.44
DE  Interaction: Self; IntAct: EBI-77694,EBI-77694; Score: 0.59
DE  Interaction: P22736; IntAct: EBI-721550,EBI-77694; Score: 0.67
DE  Interaction: Q07817-1; IntAct: EBI-287195,EBI-77694; Score: 0.44
DE  Interaction: O43521-1; IntAct: EBI-526416,EBI-77694; Score: 0.70
DE  Interaction: O43521-2; IntAct: EBI-77694,EBI-526420; Score: 0.71
DE  Interaction: Q14790; IntAct: EBI-77694,EBI-78060; Score: 0.37
DE  Interaction: Q9BXH1; IntAct: EBI-519884,EBI-77694; Score: 0.82
DE  Interaction: P38398; IntAct: EBI-77694,EBI-349905; Score: 0.46
DE  Interaction: P0DM65; IntAct: EBI-77694,EBI-8839540; Score: 0.40
DE  Interaction: Q14457; IntAct: EBI-77694,EBI-949378; Score: 0.95
DE  Interaction: A8MW95; IntAct: EBI-77694,EBI-8839517; Score: 0.40
DE  Interaction: Q9NYF8; IntAct: EBI-77694,EBI-437804; Score: 0.50
DE  Interaction: Q7CHR0; IntAct: EBI-2853517,EBI-77694; Score: 0.37
DE  Interaction: Q16611; IntAct: EBI-77694,EBI-519866; Score: 0.61
DE  Interaction: O43521; IntAct: EBI-77694,EBI-526406; Score: 0.92
DE  Interaction: Q07812; IntAct: EBI-77694,EBI-516580; Score: 0.94
DE  Interaction: P04637; IntAct: EBI-366083,EBI-77694; Score: 0.56
DE  Interaction: P55957; IntAct: EBI-519672,EBI-77694; Score: 0.87
DE  Interaction: O43521-4; IntAct: EBI-6137933,EBI-77694; Score: 0.35
DE  Interaction: O43521-5; IntAct: EBI-2123756,EBI-77694; Score: 0.35
DE  Interaction: O43521-6; IntAct: EBI-2123760,EBI-77694; Score: 0.35
DE  Interaction: O43521-3; IntAct: EBI-2123748,EBI-77694; Score: 0.35
DE  Interaction: Q96LC9; IntAct: EBI-77694,EBI-3919268; Score: 0.40
DE  Interaction: Q61337; IntAct: EBI-400328,EBI-77694; Score: 0.72
DE  Interaction: Q13323; IntAct: EBI-700794,EBI-77694; Score: 0.82
DE  Interaction: Q13794; IntAct: EBI-77694,EBI-707392; Score: 0.52
DE  Interaction: Q9C000; IntAct: EBI-77694,EBI-1220518; Score: 0.75
DE  Interaction: P62136; IntAct: EBI-77694,EBI-357253; Score: 0.40
DE  Interaction: P36873-1; IntAct: EBI-356289,EBI-77694; Score: 0.40
DE  Interaction: P62140; IntAct: EBI-352350,EBI-77694; Score: 0.40
DE  Interaction: Q86Y07; IntAct: EBI-77694,EBI-1207615; Score: 0.37
DE  Interaction: Q91ZE9; IntAct: EBI-708032,EBI-77694; Score: 0.62
DE  Interaction: P59635; IntAct: EBI-25492879,EBI-77694; Score: 0.40
DE  Interaction: Q7L3V2; IntAct: EBI-10697720,EBI-77694; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-700771,EBI-77694; Score: 0.81
DE  Interaction: O54918; IntAct: EBI-77694,EBI-526067; Score: 0.44
DE  Interaction: Q07813; IntAct: EBI-700711,EBI-77694; Score: 0.40
DE  Interaction: P51572; IntAct: EBI-77683,EBI-77694; Score: 0.52
DE  Interaction: Q9BXH1-1; IntAct: EBI-519891,EBI-77694; Score: 0.40
DE  Interaction: Q9BXH1-2; IntAct: EBI-519896,EBI-77694; Score: 0.40
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046930;
GO  GO:0032991;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0042802;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0051721;
GO  GO:0070491;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0006915;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0001658;
GO  GO:0043375;
GO  GO:0007569;
GO  GO:0098609;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0021747;
GO  GO:0019221;
GO  GO:0051607;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0007565;
GO  GO:0048041;
GO  GO:0022612;
GO  GO:0032835;
GO  GO:0031069;
GO  GO:0048873;
GO  GO:0006959;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:2001234;
GO  GO:0010507;
GO  GO:0010523;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0032848;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:1902166;
GO  GO:0051902;
GO  GO:0033033;
GO  GO:0043524;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0051402;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:2001244;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:1900740;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0051924;
GO  GO:0001952;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0034097;
GO  GO:0042493;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0042542;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:0035094;
GO  GO:0009314;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0048536;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0048538;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGA
SQ  AAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVE
SQ  SVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
//
ID  O76329;
PN  Interaptin;
GN  abpD;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass type IV membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane. Golgi apparatus, Golgi stack membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, the Golgi membrane or the endoplasmic reticulum membrane.
DR  UNIPROT: O76329;
DR  UNIPROT: Q54KE8;
DR  Pfam: PF00307;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DE  Function: May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. {ECO:0000269|PubMed:10704840}.
DE  Reference Proteome: Yes;
DE  Interaction: Q54CH1; IntAct: EBI-922673,EBI-922333; Score: 0.40
DE  Interaction: Q55FK4; IntAct: EBI-922673,EBI-923109; Score: 0.40
DE  Interaction: Q55CS9; IntAct: EBI-922673,EBI-922719; Score: 0.40
DE  Interaction: Q23858; IntAct: EBI-922673,EBI-922479; Score: 0.40
DE  Interaction: P34122; IntAct: EBI-922673,EBI-922223; Score: 0.40
DE  Interaction: P25870; IntAct: EBI-922673,EBI-922873; Score: 0.40
DE  Interaction: P34121; IntAct: EBI-922673,EBI-922516; Score: 0.40
DE  Interaction: Q54HL0; IntAct: EBI-922673,EBI-922776; Score: 0.40
DE  Interaction: Q54KG1; IntAct: EBI-922673,EBI-922528; Score: 0.40
DE  Interaction: Q54T81; IntAct: EBI-922673,EBI-922504; Score: 0.40
DE  Interaction: Q54NB6; IntAct: EBI-922673,EBI-922647; Score: 0.40
DE  Interaction: P46800; IntAct: EBI-922673,EBI-922628; Score: 0.40
DE  Interaction: Q552M5; IntAct: EBI-922673,EBI-922619; Score: 0.40
DE  Interaction: Q557E0; IntAct: EBI-922673,EBI-922634; Score: 0.40
DE  Interaction: P54651; IntAct: EBI-922673,EBI-922325; Score: 0.40
DE  Interaction: Q55GF9; IntAct: EBI-922673,EBI-922339; Score: 0.40
DE  Interaction: Q6RZZ9; IntAct: EBI-922673,EBI-922684; Score: 0.40
DE  Interaction: Q54BF6; IntAct: EBI-922673,EBI-923149; Score: 0.40
DE  Interaction: P34118; IntAct: EBI-922673,EBI-922706; Score: 0.40
DE  Interaction: Q86HW7; IntAct: EBI-922673,EBI-922768; Score: 0.40
DE  Interaction: Q869Y7; IntAct: EBI-922673,EBI-922419; Score: 0.40
DE  Interaction: Q23921; IntAct: EBI-922673,EBI-922745; Score: 0.40
DE  Interaction: Q54JM5; IntAct: EBI-922673,EBI-922759; Score: 0.40
DE  Interaction: Q54BH4; IntAct: EBI-922673,EBI-923145; Score: 0.40
DE  Interaction: Q54BP1; IntAct: EBI-922673,EBI-923138; Score: 0.40
DE  Interaction: Q54DL5; IntAct: EBI-922673,EBI-922272; Score: 0.40
DE  Interaction: Q54FU0; IntAct: EBI-922673,EBI-923247; Score: 0.40
DE  Interaction: Q54G01; IntAct: EBI-922673,EBI-923094; Score: 0.40
DE  Interaction: Q54G31; IntAct: EBI-922673,EBI-923215; Score: 0.40
DE  Interaction: Q54GS4; IntAct: EBI-922673,EBI-923090; Score: 0.40
DE  Interaction: Q54GY1; IntAct: EBI-922673,EBI-922371; Score: 0.40
DE  Interaction: Q54H23; IntAct: EBI-922673,EBI-922580; Score: 0.40
DE  Interaction: Q54I73; IntAct: EBI-922673,EBI-923085; Score: 0.40
DE  Interaction: Q54NB4; IntAct: EBI-922673,EBI-922353; Score: 0.40
DE  Interaction: Q54R55; IntAct: EBI-922673,EBI-922697; Score: 0.40
DE  Interaction: Q54RZ4; IntAct: EBI-922673,EBI-922740; Score: 0.40
DE  Interaction: Q54TQ6; IntAct: EBI-922673,EBI-922268; Score: 0.40
DE  Interaction: Q54U97; IntAct: EBI-922673,EBI-923179; Score: 0.40
DE  Interaction: Q54U98; IntAct: EBI-922673,EBI-923175; Score: 0.40
DE  Interaction: Q54VJ7; IntAct: EBI-922673,EBI-923191; Score: 0.40
DE  Interaction: Q54VQ1; IntAct: EBI-922673,EBI-922276; Score: 0.40
DE  Interaction: Q54W02; IntAct: EBI-922673,EBI-923183; Score: 0.40
DE  Interaction: Q54XP9; IntAct: EBI-922673,EBI-922287; Score: 0.40
DE  Interaction: Q556V8; IntAct: EBI-922673,EBI-922522; Score: 0.40
DE  Interaction: Q55CE3; IntAct: EBI-922673,EBI-923130; Score: 0.40
DE  Interaction: Q55CZ0; IntAct: EBI-922673,EBI-923125; Score: 0.40
DE  Interaction: Q55F82; IntAct: EBI-922673,EBI-923195; Score: 0.40
DE  Interaction: Q55F84; IntAct: EBI-922673,EBI-923117; Score: 0.40
DE  Interaction: Q55GC0; IntAct: EBI-922673,EBI-923102; Score: 0.40
DE  Interaction: Q55GC5; IntAct: EBI-922673,EBI-923098; Score: 0.40
DE  Interaction: Q75JY8; IntAct: EBI-922673,EBI-923167; Score: 0.40
DE  Interaction: P33519; IntAct: EBI-922673,EBI-922261; Score: 0.40
DE  Interaction: Q86K01; IntAct: EBI-922673,EBI-923199; Score: 0.40
DE  Interaction: Q559R0; IntAct: EBI-922673,EBI-922602; Score: 0.40
DE  Interaction: P52285; IntAct: EBI-922673,EBI-922789; Score: 0.40
DE  Interaction: Q95ZG4; IntAct: EBI-922673,EBI-922344; Score: 0.40
DE  Interaction: P32255; IntAct: EBI-922673,EBI-922437; Score: 0.40
DE  Interaction: P32256; IntAct: EBI-922673,EBI-922454; Score: 0.40
DE  Interaction: Q55AR3; IntAct: EBI-922673,EBI-922237; Score: 0.40
DE  Interaction: Q54TH8; IntAct: EBI-922673,EBI-922491; Score: 0.40
DE  Interaction: Q54LP7; IntAct: EBI-922673,EBI-922254; Score: 0.40
DE  Interaction: Q54WN5; IntAct: EBI-922673,EBI-923208; Score: 0.40
DE  Interaction: Q55EX9; IntAct: EBI-922673,EBI-923160; Score: 0.40
GO  GO:0005789;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0003779;
GO  GO:0098609;
GO  GO:0007275;
GO  GO:0009847;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRL
SQ  HYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQI
SQ  SDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTY
SQ  ISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSF
SQ  EGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEV
SQ  EKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKI
SQ  GGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTN
SQ  SSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQE
SQ  THRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERIN
SQ  QQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSN
SQ  IDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIE
SQ  NQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEK
SQ  DENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLI
SQ  EKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIE
SQ  KENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDS
SQ  QFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKV
SQ  KQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQ
SQ  LKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQS
SQ  ELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLK
SQ  EKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPP
SQ  TASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIA
SQ  QEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT
//
ID  P35368;
PN  Alpha-1B adrenergic receptor;
GN  ADRA1B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes.
DR  UNIPROT: P35368;
DR  UNIPROT: B0LPE1;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  OMIM: 104220;
DR  DisGeNET: 147;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.
DE  Reference Proteome: Yes;
DE  Interaction: P25106; IntAct: EBI-490017,EBI-1965291; Score: 0.50
DE  Interaction: P35348; IntAct: EBI-489756,EBI-490017; Score: 0.40
DE  Interaction: Self; IntAct: EBI-490017,EBI-490017; Score: 0.40
DE  Interaction: P61073; IntAct: EBI-490017,EBI-489411; Score: 0.73
DE  Interaction: P25100; IntAct: EBI-489993,EBI-490017; Score: 0.40
DE  Interaction: P02768; IntAct: EBI-714423,EBI-490017; Score: 0.35
DE  Interaction: P01857; IntAct: EBI-356114,EBI-490017; Score: 0.35
DE  Interaction: Q14315; IntAct: EBI-490017,EBI-489954; Score: 0.37
GO  GO:0005901;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004935;
GO  GO:0004937;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007188;
GO  GO:0007267;
GO  GO:0007186;
GO  GO:0042593;
GO  GO:0035556;
GO  GO:0150099;
GO  GO:0001994;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0043410;
GO  GO:0045987;
GO  GO:0045907;
GO  GO:0055117;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPT
SQ  NYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRR
SQ  KAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAG
SQ  VMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLF
SQ  STLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERS
SQ  QSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLT
SQ  EPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF
//
ID  Q9M077;
PN  Serine/threonine-protein kinase Aurora-1;
GN  AUR1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast. Note=Nuclear membrane in interphase cells, spindle poles at prophase, mitotic spindle from metaphase to telophase and equatorial cell plate at telophase.
DR  UNIPROT: Q9M077;
DR  UNIPROT: Q8LBX4;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Phosphorylates specifically 'Ser-10' of histone H3 in vitro and colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. Colocalizes also with gamma-tubulin and function in microtubule organizing centers (MTOCs). In contrast with the mammalian B-type Aurora, AUR1 has no kinase activity toward 'Ser-28' of histone H3. {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:22150830}.
DE  Reference Proteome: Yes;
GO  GO:0009504;
GO  GO:0032133;
GO  GO:0000780;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009524;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0051233;
GO  GO:0000922;
GO  GO:0005524;
GO  GO:0035175;
GO  GO:0035174;
GO  GO:0004674;
GO  GO:0051301;
GO  GO:0016572;
GO  GO:0007052;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAIPTETQHQEKEASDASAAAAQKRWTLSDFDIGKPLGRGKFGHVYLAREKRSNHVVALKVLFKSQLQQSQVEHQLRREV
SQ  EIQSHLRHPNILRLYGYFYDQKRVYLILEYAARGELYKDLQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENL
SQ  LIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAMEHSDTYRRIVQ
SQ  VDLKFPPKPIISASAKDLISQMLVKESSQRLPLHKLLEHPWIVQNADPSGIYRV
//
ID  P41208;
PN  Centrin-2;
GN  CETN2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus {ECO:0000305}.
DR  UNIPROT: P41208;
DR  UNIPROT: B2R4T4;
DR  UNIPROT: Q53XW1;
DR  PDB: 1M39;
DR  PDB: 1ZMZ;
DR  PDB: 2A4J;
DR  PDB: 2GGM;
DR  PDB: 2K2I;
DR  PDB: 2OBH;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 300006;
DR  DisGeNET: 1069;
DE  Function: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1789926; Score: 0.35
DE  Interaction: Q8NA72; IntAct: EBI-2561090,EBI-1789926; Score: 0.80
DE  Interaction: Q2NKQ1-4; IntAct: EBI-10182463,EBI-1789926; Score: 0.72
DE  Interaction: Q96PV4; IntAct: EBI-1789926,EBI-10171633; Score: 0.56
DE  Interaction: A8K8P3; IntAct: EBI-743371,EBI-1789926; Score: 0.65
DE  Interaction: Q70CQ1; IntAct: EBI-2511022,EBI-1789926; Score: 0.40
DE  Interaction: Q9H0E7; IntAct: EBI-2512823,EBI-1789926; Score: 0.59
DE  Interaction: Q9R1K9; IntAct: EBI-2553037,EBI-1789926; Score: 0.40
DE  Interaction: O43303; IntAct: EBI-1566217,EBI-1789926; Score: 0.52
DE  Interaction: P15289; IntAct: EBI-1789926,EBI-2117357; Score: 0.37
DE  Interaction: Q96LA8; IntAct: EBI-1789926,EBI-912440; Score: 0.37
DE  Interaction: Q6P5D4; IntAct: EBI-647072,EBI-1789926; Score: 0.35
DE  Interaction: P52732; IntAct: EBI-355697,EBI-1789926; Score: 0.35
DE  Interaction: O14640; IntAct: EBI-1789926,EBI-723489; Score: 0.35
DE  Interaction: Q8N0X7; IntAct: EBI-1789926,EBI-2643803; Score: 0.35
DE  Interaction: P53680; IntAct: EBI-1789926,EBI-297662; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-1789926,EBI-356876; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-1789926,EBI-356673; Score: 0.35
DE  Interaction: P20290; IntAct: EBI-1789926,EBI-1054687; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-1789926,EBI-357046; Score: 0.35
DE  Interaction: Q9UNY4; IntAct: EBI-1789926,EBI-2322921; Score: 0.35
DE  Interaction: Q16513; IntAct: EBI-1789926,EBI-2511350; Score: 0.35
DE  Interaction: Q9BYS8; IntAct: EBI-1789926,EBI-5665279; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-1789926,EBI-357407; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-1789926,EBI-355710; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-1789926,EBI-356553; Score: 0.35
DE  Interaction: Q8WUY9; IntAct: EBI-1789926,EBI-3924857; Score: 0.35
DE  Interaction: Q01831; IntAct: EBI-1789926,EBI-372610; Score: 0.71
DE  Interaction: Q9NYP9; IntAct: EBI-1789926,EBI-1104552; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-1789926,EBI-356687; Score: 0.35
DE  Interaction: P35606; IntAct: EBI-1789926,EBI-1056534; Score: 0.35
DE  Interaction: O14737; IntAct: EBI-1789926,EBI-712290; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-1789926,EBI-954531; Score: 0.60
DE  Interaction: Q8WU90; IntAct: EBI-1789926,EBI-1042636; Score: 0.35
DE  Interaction: Q6PD62; IntAct: EBI-1019583,EBI-1789926; Score: 0.35
DE  Interaction: P48754; IntAct: EBI-6876136,EBI-1789926; Score: 0.35
DE  Interaction: O88286; IntAct: EBI-5737907,EBI-1789926; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-299674,EBI-1789926; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-2266839,EBI-1789926; Score: 0.35
DE  Interaction: P29341; IntAct: EBI-773902,EBI-1789926; Score: 0.35
DE  Interaction: Q9NTX7-2; IntAct: EBI-11750630,EBI-1789926; Score: 0.35
DE  Interaction: P15927-2; IntAct: EBI-21839513,EBI-1789926; Score: 0.35
DE  Interaction: Q8IW19; IntAct: EBI-1256044,EBI-1789926; Score: 0.35
DE  Interaction: Q96DD0-2; IntAct: EBI-21832535,EBI-1789926; Score: 0.35
DE  Interaction: Q8NEE6-2; IntAct: EBI-1789926,EBI-21867651; Score: 0.40
DE  Interaction: O14874; IntAct: EBI-1046765,EBI-1789926; Score: 0.35
DE  Interaction: Q8NA72-3; IntAct: EBI-11751537,EBI-1789926; Score: 0.67
DE  Interaction: Q5VW00; IntAct: EBI-3951747,EBI-1789926; Score: 0.35
DE  Interaction: P08887-2; IntAct: EBI-16630231,EBI-1789926; Score: 0.35
DE  Interaction: Q0VDD8-2; IntAct: EBI-21543829,EBI-1789926; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-741297,EBI-1789926; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-494830,EBI-1789926; Score: 0.35
DE  Interaction: Q96A08; IntAct: EBI-3951855,EBI-1789926; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-2512818,EBI-1789926; Score: 0.35
DE  Interaction: Q9BQ69; IntAct: EBI-5324932,EBI-1789926; Score: 0.35
DE  Interaction: Q6ZNE5; IntAct: EBI-2690371,EBI-1789926; Score: 0.35
DE  Interaction: Q99598; IntAct: EBI-742638,EBI-1789926; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005829;
GO  GO:0005622;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0071942;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0032795;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0007099;
GO  GO:0097711;
GO  GO:0000086;
GO  GO:0070911;
GO  GO:0000278;
GO  GO:0051028;
GO  GO:0006289;
GO  GO:0000715;
GO  GO:0000717;
GO  GO:0006294;
GO  GO:0015031;
GO  GO:0032465;
GO  GO:0010389;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEG
SQ  TGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQ
SQ  EFLRIMKKTSLY
//
ID  Q9P2K9;
PN  Protein dispatched homolog 3;
GN  DISP3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi- pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:B9U3F2}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within the membrane (PubMed:19179482). Localizes to cytoplasmic punctate vesicular structures (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000269|PubMed:19179482}.
DR  UNIPROT: Q9P2K9;
DR  UNIPROT: Q5VTU9;
DR  UNIPROT: Q9UJD6;
DR  Pfam: PF02460;
DR  PROSITE: PS50156;
DR  OMIM: 611251;
DE  Function: Plays a role in neuronal proliferation and differentiation (PubMed:25281927). Plays a role in the accumulation of cellular cholesterol (By similarity). Involved in intracellular lipid droplet formation (PubMed:25281927). May contribute to cholesterol homeostasis in neuronal cells (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000269|PubMed:25281927}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99417; IntAct: EBI-721461,EBI-716185; Score: 0.37
DE  Interaction: Q7LDG7; IntAct: EBI-722325,EBI-721461; Score: 0.37
DE  Interaction: P00918; IntAct: EBI-724062,EBI-721461; Score: 0.37
DE  Interaction: Q9NR30; IntAct: EBI-357942,EBI-721461; Score: 0.40
DE  Interaction: P62263; IntAct: EBI-352783,EBI-721461; Score: 0.40
DE  Interaction: P49286; IntAct: EBI-721461,EBI-1188341; Score: 0.37
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0042632;
GO  GO:0008203;
GO  GO:0045665;
GO  GO:0045834;
GO  GO:2000179;
GO  GO:0032368;
GO  GO:0007224;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDTEDDPLLQDVWLEEEQEEEEATGETFLGAQKPGPQPGAGGQCCWRHWPLASRPPASGFWSTLGWAFTNPCCAGLVLFL
SQ  GCSIPMALSAFMFLYYPPLDIDISYNAFEIRNHEASQRFDALTLALKSQFGSWGRNRRDLADFTSETLQRLISEQLQQLH
SQ  LGNRSRQASRAPRVIPAASLGGPGPYRDTSAAQKPTANRSGRLRRETPPLEDLAANQSEDPRNQRLSKNGRYQPSIPPHA
SQ  AVAANQSRARRGASRWDYSRAYVSANTQTHAHWRIELIFLARGDAERNIFTSERLVTIHEIERKIMDHPGFREFCWKPHE
SQ  VLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIRGSLELAMTHPEFYWYVDEGLSADNLKSSLLRSEIL
SQ  FGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYIL
SQ  TSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTVQT
SQ  AGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVSCCWLAVLVTMPAALGLWSLYLAPLESSCQTSCHQNCSRKTS
SQ  LHFPGDVFAAPEQVGGSPAQGPIPYLDDDIPLLEVEEEPVSLELGDVSLVSVSPEGLQPASNTGSRGHLIVQLQELLHHW
SQ  VLWSAVKSRWVIVGLFVSILILSLVFASRLRPASRAPLLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNN
SQ  IRTSLEKKRRGSGVPWASRPEATLQDFPGTVYISKVKSQGHPAVYRLSLNASLPAPWQAVSPGDGEVPSFQVYRAPFGNF
SQ  TKKLTACMSTVGLLQAASPSRKWMLTTLACDAKRGWKFDFSFYVATKEQQHTRKLYFAQSHKPPFHGRVCMAPPGCLLSS
SQ  SPDGPTKGFFFVPSEKVPKARLSATFGFNPCVNTGCGKPAVRPLVDTGAMVFVVFGIIGVNRTRQVDNHVIGDPGSVVYD
SQ  SSFDLFKEIGHLCHLCKAIAANSELVKPGGAQCLPSGYSISSFLQMLHPECKELPEPNLLPGQLSHGAVGVREGRVQWIS
SQ  MAFESTTYKGKSSFQTYSDYLRWESFLQQQLQALPEGSVLRRGFQTCEHWKQIFMEIVGVQSALCGLVLSLLICVAAVAV
SQ  FTTHILLLLPVLLSILGIVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPPHQAEDARTQRQW
SQ  RTLEAVRHVGVAIVSSALTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLGIMAPSSFTRTRTSFLKAL
SQ  GAVLLAGALGLGACLVLLQSGYKIPLPAGASL
//
ID  P24385;
PN  G1/S-specific cyclin-D1;
GN  CCND1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:20399237, ECO:0000269|PubMed:9106657}. Cytoplasm {ECO:0000269|PubMed:9106657}. Nucleus membrane {ECO:0000269|PubMed:9106657}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. {ECO:0000269|PubMed:9106657}.
DR  UNIPROT: P24385;
DR  UNIPROT: Q6LEF0;
DR  PDB: 2W96;
DR  PDB: 2W99;
DR  PDB: 2W9F;
DR  PDB: 2W9Z;
DR  PDB: 5VZU;
DR  PDB: 6P8E;
DR  PDB: 6P8F;
DR  PDB: 6P8G;
DR  PDB: 6P8H;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DR  OMIM: 168461;
DR  OMIM: 254500;
DR  DisGeNET: 595;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:9106657}.
DE  Disease: Note=A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle. Note=A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer. Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence- Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:8695815}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.
DE  Reference Proteome: Yes;
DE  Interaction: P11802; IntAct: EBI-295644,EBI-375001; Score: 0.98
DE  Interaction: P38398; IntAct: EBI-349905,EBI-375001; Score: 0.46
DE  Interaction: Q02224; IntAct: EBI-375001,EBI-1375040; Score: 0.35
DE  Interaction: O95239; IntAct: EBI-375001,EBI-1057516; Score: 0.35
DE  Interaction: O94880; IntAct: EBI-375001,EBI-2680164; Score: 0.35
DE  Interaction: P38936; IntAct: EBI-375077,EBI-375001; Score: 0.95
DE  Interaction: Q13761; IntAct: EBI-925990,EBI-375001; Score: 0.46
DE  Interaction: Q00534; IntAct: EBI-375001,EBI-295663; Score: 0.73
DE  Interaction: P42771; IntAct: EBI-375053,EBI-375001; Score: 0.49
DE  Interaction: P49841; IntAct: EBI-375001,EBI-373586; Score: 0.40
DE  Interaction: P11142; IntAct: EBI-351896,EBI-375001; Score: 0.40
DE  Interaction: Q96TE0; IntAct: EBI-10201595,EBI-375001; Score: 0.56
DE  Interaction: Q9BQA1; IntAct: EBI-1237307,EBI-375001; Score: 0.35
DE  Interaction: O60477; IntAct: EBI-375001,EBI-3904864; Score: 0.37
DE  Interaction: P06858; IntAct: EBI-715909,EBI-375001; Score: 0.37
DE  Interaction: Q9H9Y6; IntAct: EBI-355441,EBI-375001; Score: 0.37
DE  Interaction: P46527; IntAct: EBI-375001,EBI-519280; Score: 0.76
DE  Interaction: P20020-6; IntAct: EBI-375001,EBI-10972265; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-375001,EBI-355133; Score: 0.35
DE  Interaction: P43251; IntAct: EBI-375001,EBI-2907478; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-375001,EBI-444308; Score: 0.53
DE  Interaction: O60673-2; IntAct: EBI-375001,EBI-10977129; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-375096,EBI-375001; Score: 0.74
DE  Interaction: Q9UJK0; IntAct: EBI-375001,EBI-11035689; Score: 0.35
DE  Interaction: Q07283; IntAct: EBI-375001,EBI-1046116; Score: 0.35
DE  Interaction: Q00535; IntAct: EBI-375001,EBI-1041567; Score: 0.35
DE  Interaction: P49918-2; IntAct: EBI-375001,EBI-11103414; Score: 0.35
DE  Interaction: P42773; IntAct: EBI-375001,EBI-711290; Score: 0.35
DE  Interaction: Q15276; IntAct: EBI-447043,EBI-375001; Score: 0.37
DE  Interaction: P36873-1; IntAct: EBI-375001,EBI-356289; Score: 0.40
DE  Interaction: P62140; IntAct: EBI-352350,EBI-375001; Score: 0.40
DE  Interaction: P11802-1; IntAct: EBI-22122649,EBI-375001; Score: 0.37
DE  Interaction: P06400; IntAct: EBI-375001,EBI-491274; Score: 0.62
DE  Interaction: Q9UH17; IntAct: EBI-2967317,EBI-375001; Score: 0.27
DE  Interaction: P49815; IntAct: EBI-375001,EBI-396587; Score: 0.40
DE  Interaction: O43929; IntAct: EBI-375001,EBI-374889; Score: 0.44
DE  Interaction: Q7L590; IntAct: EBI-375001,EBI-374912; Score: 0.44
GO  GO:0005923;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005622;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0070064;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0003714;
GO  GO:0008134;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0019221;
GO  GO:0030968;
GO  GO:0045444;
GO  GO:0000082;
GO  GO:0007595;
GO  GO:0033327;
GO  GO:0097421;
GO  GO:0060749;
GO  GO:0033598;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0071157;
GO  GO:0030857;
GO  GO:0000122;
GO  GO:0045787;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0033601;
GO  GO:0001934;
GO  GO:0000320;
GO  GO:0000079;
GO  GO:0051592;
GO  GO:0051412;
GO  GO:0042493;
GO  GO:0032355;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0010039;
GO  GO:0044321;
GO  GO:0032026;
GO  GO:0010243;
GO  GO:0070141;
GO  GO:0033197;
GO  GO:0010165;
GO  GO:0006367;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCD
SQ  PDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI
//
ID  P35233;
PN  Tyrosine-protein phosphatase non-receptor type 2;
GN  Ptpn2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. {ECO:0000250}. [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:8900155}. Nucleus membrane {ECO:0000269|PubMed:8900155}. [Isoform 2]: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: P35233;
DR  Pfam: PF00102;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DR  PROSITE: PS50055;
DE  Function: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T- cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA (By similarity). {ECO:0000250|UniProtKB:P17706}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0003677;
GO  GO:0005178;
GO  GO:0004726;
GO  GO:0019901;
GO  GO:0004725;
GO  GO:0030971;
GO  GO:0097677;
GO  GO:0019905;
GO  GO:0030183;
GO  GO:0030218;
GO  GO:0042593;
GO  GO:0008286;
GO  GO:0008285;
GO  GO:0050922;
GO  GO:0042059;
GO  GO:0070373;
GO  GO:0050728;
GO  GO:0046627;
GO  GO:0060336;
GO  GO:1902206;
GO  GO:1902215;
GO  GO:0070104;
GO  GO:0010888;
GO  GO:1902227;
GO  GO:0045650;
GO  GO:2000587;
GO  GO:1902233;
GO  GO:0061099;
GO  GO:0050860;
GO  GO:0000122;
GO  GO:0010804;
GO  GO:0060339;
GO  GO:0042532;
GO  GO:0035335;
GO  GO:1902237;
GO  GO:0045722;
GO  GO:1903899;
GO  GO:0006470;
GO  GO:1902202;
GO  GO:0030217;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSATIEREFEELDAQCRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSAENDYINASLVDIEEAQ
SQ  RSYILTQGPLPNTCCHFWLMVWQQKTRAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQ
SQ  LENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE
SQ  DVNVKQILLSMRKYRMGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWKELSKEDLSPVCRHSQNRTMTEKYNGKRIGS
SQ  EDEKLTGLSSKVPDTVEESSESILRKRIREDRKATTAQKVQQMRQRLNETERKRKRWLYWQPILTKMGFVSVILVGALVG
SQ  WTLLFQLNVLPRLTDT
//
ID  Q9VIW3;
PN  Ran GTPase-activating protein;
GN  RanGAP;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17032737}. Nucleus membrane {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:31626769}; Peripheral membrane protein {ECO:0000269|PubMed:17032737}; Cytoplasmic side {ECO:0000269|PubMed:17032737}. Note=Association to cytoplasmic side of the nuclear pore complex is promoted by Nup214 (PubMed:17032737). Co-localizes with Nup358/RanBP2 to annulate lamellae (PubMed:31626769). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:31626769}.
DR  UNIPROT: Q9VIW3;
DR  UNIPROT: Q9XZI5;
DR  Pfam: PF13516;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state (By similarity). Trans-acting factor necessary for meiotic distortion (PubMed:10073941). Distortion is only seen in individuals that carry the RanGAP tandem duplication and express a RanGAP truncated protein. Binding of truncated RanGAP product to the Responder(RSP) locus initiates events that lead to sperm dysfunction (PubMed:10073941). During oogenesis, plays a role in the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:Q684P5, ECO:0000269|PubMed:10073941, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24570; IntAct: EBI-192313,EBI-167445; Score: 0.37
DE  Interaction: Q9UKK6; IntAct: EBI-301889,EBI-192313; Score: 0.35
DE  Interaction: P51521; IntAct: EBI-186918,EBI-192313; Score: 0.37
DE  Interaction: O77237; IntAct: EBI-92779,EBI-192313; Score: 0.37
DE  Interaction: Q9VL21; IntAct: EBI-119676,EBI-192313; Score: 0.37
DE  Interaction: Q9V428; IntAct: EBI-96007,EBI-192313; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0003723;
GO  GO:0045132;
GO  GO:0006913;
GO  GO:0043547;
GO  GO:0006611;
GO  GO:0046822;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17032737};
SQ  MSTFNFASMAAQLGQEQGISFENKVLSWNTAADVQDVVDALNKQTTVHYLNLDGNTLGVEAAKAIGEGLKRHPEFRKALW
SQ  KNMFTGRLISEIPEALKHLGAALIVAGAKLTVLDLSDNALGPNGMRGLEELLRSPVCYSLQELLLCNCGLGPEGGSMLSR
SQ  ALIDLHANANKAGFPLQLRVFIGSRNRLEDAGATEMATAFQTLKTFEEIVLEQNSIYIEGVEALAESFKHNPHLRVLNMN
SQ  DNTLKSEGAEKIAEALPFLPLLREMSFGDCLIKTNGAYHFGEALERGNERLEVIDLGFNEINSDGGLVLVNAMGNKPKLR
SQ  ILNLDGNSFGEEGSEKIISEMSKLPTAAALQPFQHQEEEDLEDEYQADKQDADYEEEEEVHEHANDTTEEADEDSEGDED
SQ  DEEDEGDEEYSNVAEETAYVTTNAYTTKLFNDTTNSMASETFAVANKTISQKCTPEKFCLSQKPCSQEDFDSLDMDNKLE
SQ  ALQSIVNQFTGDNHLLLLVFTTLKCAHLSQSSKAALDLAVSLYQATFDYAIKTKQETRVLNYVLMQLRLLPCKEVFHSDY
SQ  DVKNCRFALREALKQPTFANDNIKNSFKTFLEGAES
//
ID  P06105;
PN  Protein SCP160;
GN  SCP160;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic surface of the ER-nuclear envelope membranes.
DR  UNIPROT: P06105;
DR  UNIPROT: D6VWA3;
DR  Pfam: PF00013;
DR  PROSITE: PS50084;
DE  Function: Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER- nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes.
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-8591,EBI-16374; Score: 0.53
DE  Interaction: P53863; IntAct: EBI-29183,EBI-16374; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-16374; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-8603,EBI-16374; Score: 0.53
DE  Interaction: P02829; IntAct: EBI-16374,EBI-8659; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-16374,EBI-24570; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-8632,EBI-16374; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-16374; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-16374,EBI-8666; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-16374,EBI-8050; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-10420,EBI-16374; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-16374,EBI-29684; Score: 0.53
DE  Interaction: P46997; IntAct: EBI-26138,EBI-16374; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-16374,EBI-17244; Score: 0.35
DE  Interaction: P38934; IntAct: EBI-3593,EBI-16374; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-16374,EBI-20254; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-16374,EBI-6329; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-16374,EBI-6314; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-16374,EBI-16150; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-16374,EBI-16032; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-16374,EBI-15447; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-16374,EBI-15398; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-16374,EBI-15394; Score: 0.35
DE  Interaction: P14120; IntAct: EBI-16374,EBI-15333; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-16374,EBI-15270; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-16374,EBI-9428; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-16374,EBI-6270; Score: 0.35
DE  Interaction: P15790; IntAct: EBI-16374,EBI-9533; Score: 0.35
DE  Interaction: P38011; IntAct: EBI-16374,EBI-7405; Score: 0.44
DE  Interaction: P34160; IntAct: EBI-745,EBI-16374; Score: 0.35
DE  Interaction: P38285; IntAct: EBI-20853,EBI-16374; Score: 0.27
DE  Interaction: Q12476; IntAct: EBI-31475,EBI-16374; Score: 0.27
DE  Interaction: P32357; IntAct: EBI-340,EBI-16374; Score: 0.27
DE  Interaction: P15646; IntAct: EBI-6838,EBI-16374; Score: 0.27
DE  Interaction: P39960; IntAct: EBI-3517,EBI-16374; Score: 0.27
DE  Interaction: P06101; IntAct: EBI-4266,EBI-16374; Score: 0.27
DE  Interaction: P23293; IntAct: EBI-17078,EBI-16374; Score: 0.27
DE  Interaction: P36041; IntAct: EBI-16374,EBI-26995; Score: 0.40
GO  GO:0005623;
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000329;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0005844;
GO  GO:0001965;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0043577;
GO  GO:0030466;
GO  GO:0006348;
GO  GO:0007059;
GO  GO:0045141;
GO  GO:0000750;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKP
SQ  AVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVA
SQ  ANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFE
SQ  SVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYL
SQ  KKLASNLDEEKVKIPSKFQFLIDAEELKEKYNVIVTFPSTPDDELVSFVGLRDKVGEAITYARSSSKSYVVESLDISKAH
SQ  SKNLTHAKNLIMYFTKYSVLKGLEESHPNVKISLPSIQSLPTAETVTIHISAKSDEANDIKAVRKELISFVNNIPPSETL
SQ  VITDLDYELFGGSIKHCLLASESSVAFVQFGDYYPNDNSILLVALTEDEDFKPSIEEIQASLNKANESLNSLRTKQNNME
SQ  TKTYEFSEEVQDSLFKPSSATWKLIMEDISEQEGHLQIKLHTPEENQLTVRGDEKAAKAANKIFESILNSPSSKSKMTVN
SQ  IPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVTLTGLEYNLTHAKKYLAAEAKKWADIITKELIVP
SQ  VKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLDFEMENGHKMVINVPAEHVPRIIGK
SQ  NGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAAKRVESIVAEASDFVTEVLKIDHKYHKSIVGSG
SQ  GHILREIISKAGGEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKDAENSVTKTIDIPAERKGALIGPGGI
SQ  VRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRENFDREVDVPASIYEYVSERGAFIQKLRMDLSV
SQ  NVRFGNTSKKANKLARAPIEIPLEKVCGSTEGENAEKTKFTIEEVGAPTSSEEGDITMRLTYEPIDLSSILSDGEEKEVT
SQ  KDTSNDSAKKEEALDTAVKLIKERIAKAPSATYAGYVWGADTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVV
SQ  YIRGTKAGVEKAGEMVLKSLRR
//
ID  F4I3V6;
PN  Protein SHORT HYPOCOTYL IN WHITE LIGHT 1;
GN  SHW1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00768, ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:26474641}; Multi-pass membrane protein {ECO:0000255}. Note=Constitutively localized in the nucleus of hypocotyl cells. {ECO:0000269|PubMed:18375596}.
DR  UNIPROT: F4I3V6;
DR  UNIPROT: Q0WTQ6;
DR  UNIPROT: Q8LGA9;
DE  Function: Negative regulator of photomorphogenesis modulating both light and abscisic acid (ABA) signaling pathways (PubMed:19704523, PubMed:18375596, PubMed:26474641). Regulates negatively the light- mediated inhibition of hypocotyl elongation, probably in a PHYB- mediated signaling pathway, but promotes flowering time (especially in long days) and lateral root formation (PubMed:18375596, PubMed:19704523). Enhances light-regulated gene expression (PubMed:18375596). Promotes COP1-mediated degradation of HY5 during seedling development (e.g. hypocotyl growth) through enhanced ubiquitination in the darkness. Also involved in root gravitropism (PubMed:26474641, PubMed:18375596). {ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:19704523, ECO:0000269|PubMed:26474641}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0009738;
GO  GO:0009908;
GO  GO:0010100;
GO  GO:0009958;
GO  GO:1901333;
GO  GO:0048578;
GO  GO:0009787;
GO  GO:0031540;
GO  GO:0010380;
GO  GO:0090227;
GO  GO:0009642;
GO  GO:0009416;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAATTTLSSSSSSPSLTLINASHRFVSVTPFSSNSIFLRRRFRRLNRSLASSSSHSRRRYESDDRFFGGGDNYDVVPDD
SQ  DGFSDDDDEEDERESSVDLLIRFLRSMFKKVSKRTKKASRRILPAAMSPRLVSFAVDGILLLGSLSITRAFLEVICNLGG
SQ  TVFTVILLIRLFWAAASFFQTYGNSFGPNPVN
//
ID  Q9TVM2;
PN  Exportin-1;
GN  emb;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:17032737}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Nucleoplasmic side. Note=Localization to the nuclear pore complex is promoted by Nup214. {ECO:0000269|PubMed:17032737}.
DR  UNIPROT: Q9TVM2;
DR  UNIPROT: Q9I7N7;
DR  UNIPROT: Q9U699;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES) (PubMed:10636888, PubMed:14638854, PubMed:16103875). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (PubMed:10636888, PubMed:14638854). Involved in the export of dl, RpS2 and the pre-40S ribosome from the nucleus to the cytoplasm (PubMed:14638854, PubMed:25858587, PubMed:17032737). Plays an important role in nuclear pore assembly by mediating nucleoporin condensation and biogenesis of annulate lamellae (PubMed:31626769). Required for the function or maintenance of certain tissues such as brain and gut (PubMed:10924475). {ECO:0000269|PubMed:10636888, ECO:0000269|PubMed:10924475, ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:25858587, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: O61307; IntAct: EBI-118556,EBI-133375; Score: 0.35
DE  Interaction: Q9VLS7; IntAct: EBI-190906,EBI-133375; Score: 0.35
DE  Interaction: Q24114; IntAct: EBI-86112,EBI-133375; Score: 0.35
DE  Interaction: P13709; IntAct: EBI-112846,EBI-133375; Score: 0.35
DE  Interaction: Q9W258; IntAct: EBI-3417884,EBI-133375; Score: 0.46
DE  Interaction: Q0KHS0; IntAct: EBI-89349,EBI-133375; Score: 0.35
DE  Interaction: Q7KN04; IntAct: EBI-94713,EBI-133375; Score: 0.35
DE  Interaction: Q8IRE7; IntAct: EBI-3420003,EBI-133375; Score: 0.35
DE  Interaction: Q9VRP5; IntAct: EBI-3420716,EBI-133375; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9933576,EBI-133375; Score: 0.35
DE  Interaction: Q9VTM1; IntAct: EBI-154342,EBI-133375; Score: 0.37
DE  Interaction: Q7KML2; IntAct: EBI-128385,EBI-133375; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005049;
GO  GO:0008536;
GO  GO:0007099;
GO  GO:0051028;
GO  GO:0007275;
GO  GO:0051168;
GO  GO:0051292;
GO  GO:0006611;
GO  GO:0015031;
GO  GO:1900037;
GO  GO:0046825;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATMLTSDEAGKLLDFSQKLDINLLDKIVEVVYTAQGEQLRLAQSILTTLKEHPEAWTRVDSILEYSQNQRTKFYALQIL
SQ  EEVIKTRWKVLPRNQCEGIKKYVVSLIIKTSSDPIVMEQNKVYLNKLNMILVHILKREWPRNWETFISDIVGASKTNESL
SQ  CMNNMVILKNLSEEVFDFSQGQITQTKAKHLKDTMCSEFSQIFTLCSFVLENSMNAALIHVTLETLLRFLNWIPLGYIFE
SQ  TQQIETLIFKFLSVPMFRNVTLKCLSEIAGLTAANYDENFATLFKDTMVQLEQIVGQNMNMNHVFKHGSDTEQELVLNLA
SQ  MFLCTFLKEHGKLVEDAKYVDYLNQALMYLVMISEVEDVEVFKICLEYWNSLVEDLYNSEFFHPTLESTKRQQVYPRRRF
SQ  YAPILSKVRFIMISRMAKPEEVLVVENENGEVVREFMKDTNSINLYKNMRETLVFLTHLDSVDTDRIMTLKLLNQVNGSE
SQ  FSWKNLNTLCWAIGSISGAFCEEDEKRFLVTVIKDLLGLCEQKKGKDNKAIIASNIMYVVGQYPRFLRAHWKFLKTVVNK
SQ  LFEFMHETHDGVQDMACDTFIKIAIKCRRYFVTIQPNEACTFIDEILTTMSSIICDLQPQQVHTFYEAVGYMISAQVDQV
SQ  QQDVLIERYMQLPNQVWDDIISRASKNVDFLKNMTAVKQLGSILKTNVAACKALGHAYVIQLGRIYLDMLNVYKITSENI
SQ  IQAIEVNGVNVNNQPLIKTMHVVKKETLNLISEWVSRSNDNQLVMDNFIPPLLDAILLDYQRCKVPSAREPKVLSAMAII
SQ  VHKLRQHITNEVPKIFDAVFECTLDMINKNFEDFPQHRLSFYELLQAVNAHCFKAFLNIPPAQFKLVFDSVVWAFKHTMR
SQ  NVADMGLNILFKMLQNLDQHPGAAQSFYQTYFTDILMQIFSVVTDTSHTAGLPNHAIILAYMFSLVENRKITVNLGPIPD
SQ  NMIFIQEYVASLLKSAFTHLSDNQVKVFVTGLFNLDENVQAFKEHLRDFLIQIREATGEDDSDLYLEEREAALAEEQSNK
SQ  HQMQRNIPGMLNPHELPEDMQDE
//
ID  Q9NUQ3;
PN  Gamma-taxilin;
GN  TXLNG;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15911876}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BHN1}.
DR  UNIPROT: Q9NUQ3;
DR  UNIPROT: Q2KQ75;
DR  UNIPROT: Q5JNZ7;
DR  UNIPROT: Q9P0X1;
DR  Pfam: PF09728;
DR  OMIM: 300677;
DR  DisGeNET: 55787;
DE  Function: May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:18068885}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92844; IntAct: EBI-356349,EBI-3445062; Score: 0.35
DE  Interaction: Q9UNE7; IntAct: EBI-357085,EBI-3445062; Score: 0.35
DE  Interaction: P61244; IntAct: EBI-3445062,EBI-751711; Score: 0.37
DE  Interaction: Q9Y2D8; IntAct: EBI-2212028,EBI-3445062; Score: 0.35
DE  Interaction: Q9Y2I6; IntAct: EBI-719716,EBI-3445062; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-716327,EBI-3445062; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-741421,EBI-3445062; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-1059012,EBI-3445062; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-1046993,EBI-3445062; Score: 0.35
DE  Interaction: Q8TES7; IntAct: EBI-2350063,EBI-3445062; Score: 0.35
DE  Interaction: Q96ST8; IntAct: EBI-2799206,EBI-3445062; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-2873150,EBI-3445062; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-2563266,EBI-3445062; Score: 0.35
DE  Interaction: P0C0A3; IntAct: EBI-11116518,EBI-3445062; Score: 0.35
DE  Interaction: P97801; IntAct: EBI-309807,EBI-3445062; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-745632,EBI-3445062; Score: 0.35
DE  Interaction: P40222; IntAct: EBI-359793,EBI-3445062; Score: 0.51
DE  Interaction: Q96HH9; IntAct: EBI-2832937,EBI-3445062; Score: 0.35
DE  Interaction: Q8N3L3; IntAct: EBI-6116822,EBI-3445062; Score: 0.35
DE  Interaction: Q96DX7; IntAct: EBI-8787399,EBI-3445062; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-2361917,EBI-3445062; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-741977,EBI-3445062; Score: 0.35
DE  Interaction: Q9C0F1; IntAct: EBI-744115,EBI-3445062; Score: 0.35
DE  Interaction: Q8WVK2; IntAct: EBI-2512550,EBI-3445062; Score: 0.35
DE  Interaction: B3KSW4; IntAct: EBI-21551620,EBI-3445062; Score: 0.35
DE  Interaction: Q8N4N8; IntAct: EBI-443523,EBI-3445062; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-7097057,EBI-3445062; Score: 0.35
DE  Interaction: Q9NYP9; IntAct: EBI-1104552,EBI-3445062; Score: 0.35
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0033613;
GO  GO:0019905;
GO  GO:0008134;
GO  GO:0007049;
GO  GO:0030500;
GO  GO:0051726;
GO  GO:0010564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATRVEEAARGRGGGAEEATEAGRGGRRRSPRQKFEIGTMEEAGICGLGVKADMLCNSQSNDILQHQGSNCGGTSNKHSL
SQ  EEDEGSDFITENRNLVSPAYCTQESREEIPGGEARTDPPDGQQDSECNRNKEKTLGKEVLLLMQALNTLSTPEEKLAALC
SQ  KKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEA
SQ  TAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADE
SQ  KHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWR
SQ  TKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAAIKAANRDLATPVMQPC
SQ  TALDSHKELNTSSKRALGAHLEAEPKSQRSAVQKPPSTGSAPAIESVD
//
ID  G4SLH0;
PN  Titin homolog;
GN  ttn;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:20346955}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20346955}. Nucleus membrane {ECO:0000269|PubMed:16410549}; Peripheral membrane protein {ECO:0000269|PubMed:16410549}. Note=Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1- dependent(PubMed:16410549). {ECO:0000269|PubMed:16410549, ECO:0000269|PubMed:20346955}.
DR  UNIPROT: G4SLH0;
DR  UNIPROT: A7DT28;
DR  UNIPROT: G4SLD6;
DR  UNIPROT: G5EDP1;
DR  UNIPROT: G5EDT5;
DR  UNIPROT: G5EF69;
DR  UNIPROT: G5EFF0;
DR  UNIPROT: Q65XY2;
DR  UNIPROT: Q8ISF3;
DR  UNIPROT: Q8ISF4;
DR  Pfam: PF00041;
DR  Pfam: PF07679;
DR  Pfam: PF00069;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity). {ECO:0000250|UniProtKB:Q9I7U4, ECO:0000269|PubMed:18390597, ECO:0000269|PubMed:20346955}.
DE  Reference Proteome: Yes;
DE  Interaction: G5ECY0; IntAct: EBI-312458,EBI-2914644; Score: 0.37
GO  GO:0031672;
GO  GO:0031674;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0004674;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16410549};
SQ  MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSE
SQ  ITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKC
SQ  VTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFV
SQ  NGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRA
SQ  LGNNGRNSRQAVNMFELNYTQRSSSVPRGVRHLESHIEVSNMTGEEKKTQQQTRTDAASIVESRFHPQPPKPPRAGTSRR
SQ  FLPEPPKFVTTLPSVITVNAEEKLVLSVDVQAIPAAEFAWHVNGFEVKKSQSVVLLDEHNKSTLVLHPPVKQGKYKVTAR
SQ  NDVGSDSVTTQVTRIGEVKDGAGSEPPDIVESAVTVTCSHEEDVGSHSSLQTVRRIQEMQEEDEVDPIKPFIEATSPKVK
SQ  ESVEHPFANILNPKKREERLSPSGKGKHLLFAPRITAHPSESVFKILDGSPLKLRVMASSLPPATFLWMLNNFELRSNQN
SQ  VTIRNDEENSSEIEFQKAPNGNVTVSAKNHLGEDRWTGKVILQYESPPPGQKITTIEKVTESWTLEEAVITQVVPTAADP
SQ  GDRIVIIVRFDENKTSNCQFNWTINGVNIEKLEENLVAVESTEFESSLIVEKLEEQLCGEVVCVVKNQHGEVFSSSAHLR
SQ  IRDDDSSFEIVPPNLPEECAPKIVEPLHSASFLDGQAMSLRCKITANPSAAVVWSKDDVNVEDWVLNKDVTTTVLDGGVC
SQ  ELLNPECFAEDAGLYKCTATNPHGTAETAAFINVEGAEYIKDHEEAEISESVLTDDVHIILPPKFIETLTAETDNFQQLG
SQ  YVRMVATVRSVAPITVSWQKDGMDIYENEKYEVMQFADGAQILTIRAPTNLDSGVYTCTAESEHGVSNSSCQVELTISAE
SQ  SSPESFEKVEITPPEEVKETGIDDDIEVILKEEVSGTAQIEKREEEFKLLVKVADQVASTLVANVFLEAVHEAVKKIVET
SQ  EDEEEDNQIEATQEPRFETSTDEYHVKENGTIKMAATISGHPTPFLEWYFGEEKLQVSQNVSMYYEAGTSAIILKNVQKR
SQ  QGGNYFLRAHNCHGESILPMKLTVDPIEAVTHVLETSIPKVVVEQDAKEEEVRRAAEIISEQFAQLWVQDAQTEAVSAQA
SQ  HQTPVVAEQASEEPTLPEVVAALQEQKPSVEKAPQPQFEVLETEDQDVVEQMQKQLPPVQKSMSVQEEKASSQRTPSPMN
SQ  YEDKVKTIQSNLLRVNSHEAMEPIEATNLLLNTALQLKNEHVCDETTTVIVTQQPQKYDQLVTVVESNIEYHALRLSTSS
SQ  SSPLKFIDLETIIQKPSTSCESIDRMFVEKSKRTANAQHRIVVLQGMSNTFHNAITWSLKKVKKLVGDAEAKAYADVEVV
SQ  KQDETNEQVMTIIDNDTIVPQLLQVAAAANKLKLENVSVALIKEGDRAHQELVIEYESSIDEPMFEPVHNTSHLTFHQQQ
SQ  PTGPDQHVWSRRSKFEEDEAHVVAVFVEVDANCPDQSVEIVATVNAAYEGDNRQGIEDEPFTEVSQSLATESSAAPQAPK
SQ  FLRKLVNCFGRIGEPVQLKCLIAGMPQPEIEWTVDGDPIVPNDEYSIVYEDGVCILRIESTLIEDEGEYCCTASNVAGTT
SQ  FSKCYLKLSEADDDAVDLLRQLSEIKIIDPTLSTGYPMSMISDEENTSHQLLSNVLLTDKEVPITATYNEDLSRAESFRR
SQ  FFESAETTVKVTELYQGESVEAQFQQPEKREQVSTSNTDVMFVNQKVDVMESTVSTVGNAVRQSVSSSTNSWDYMFNDPF
SQ  PESQEINVIENELYEPRVPLLPQKLSYKGQEIFANTNTVERNSKAGAKAKGEVENLKKCVETLLLFDAEMDMKDIKESSP
SQ  KKEIISKKDQQSLDDQIKVTQQILKDVERDLNKMERTSPGKSLSPNKRTFAPKDVEDIEAAIFSISDQLADRQSSEEALR
SQ  EALQEMILSNSSPMKELSRNNETSKPEVLKSEIQKIPEVETKISEVYPIVKLKQAISAIENSLLEDTEVTEIMKRKGSDK
SQ  DKRKATRIKRVPSAHSARITPITSNLRDRLNQLHQLTVSEDSGSLKQNEEAKEIQELFVKIEKEINTIAELCKEKMTKKG
SQ  ADTVTHVLNSVLQHVASIINVILVAQDHQPIEVHAETTKTAEVSVWYSFDVHPESEDIIGIVDEEPTNRRPSSTPRGSTR
SQ  SSNLTTSQDSQATTKMTVSSEDTIEAPIAPPRKGRSLSRDAERLLEIQPRAPPRRSRQSGDTLSPEPTPVLTLVKSDETP
SQ  APVRPPRSRSRHSGDELAETSPEAQPIRPPRSHSRHSGDELEEVQPVRPPRSKSKTADANCLQIESMDESQYSLSCIHIQ
SQ  KTNFAFTNSTHETSNASVVVDLRNMAQLECTVQSLDDLASIQMLCEESDYPSDTDRSLLLAGTVRYFNRASPSLHEVSPS
SQ  LNMESVSMDLKPETEPEEIVQDVYVNVELHSVPSLSSLVEVNPNTLMQTLASEKSSLKAAEEDEKEGEEEGEEEVTADVS
SQ  FIGRSVLSTETLDVVLEEKDMSQMNSTLPLDYERAFSSNTIRETDILSDESITVDSSYHKSPEPTVDFARSQVKSEEVTE
SQ  NFSLIHKPARRRVTGIVVNSLIYTIAANIAEDNTFDVDVVQEPQRYNISIKVIEDIVDFTSLTIMSDCEDDPPADVLVLK
SQ  QDTSKLQALSYDDISVATTRTGITVSIVARSLNDGIYASLEEIAWGEVEMTVPDIMQMSTEEKSSLQFNVTVSESNLEEA
SQ  KSLKSQVSFRSSQNSVSEMDNTISSTATISIPSYVVKLESTATITCELNNYLPKNCTIDWYCGKTKIIIDHEQFDRISHD
SQ  LLEVLIIRSVEAINGNLYSLKINEDLFPVAYLIVENTNLTTSANILTRPETQFVMEGQPTVITVELDDPNVIVNWLKDRR
SQ  PLHENERIRLETDGQGNHRVIIPNTCVGDQGTYLALTSSESVAITLVVEERIEEKEVMVIASGTESEEDDVQEYLVPPGS
SQ  TATIACELEECELKRSIRWLRDGKDIRFEQGKTEHVQNGLKHYLVVHDATSLDSGLYKTERSEEQCEETIIPRGVVATIQ
SQ  CQTSEPQESIQWSKDGNIIPSDISRFEFRSLDNNQSHEMVISNISWSDAGVYSVLINGKSSFVSKIVVVESELITQSVEE
SQ  EPEAEPEIDVSLHIVESEQIIELNVPQSPKLGASHETLVPIGQDDIEVIDKQEAAPVVESIEETSSIGSEEFEIIEKFTE
SQ  EEVPKVAEPSEPTQADVPKIAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMV
SQ  AAPLEPTQADVPKVAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEP
SQ  IQEEVPKEAAPSEPTQEDVPKGAAPLEPTQEDVPKEAAPSGPTQEDVPKEEAPSEPTQEDVPKEAAPSEPTQENVPKEAA
SQ  PSEPTKDVPKEAAPSEPIQEEVPKEATLSEPTQEQSEVSKRSEPVEPTQIQQAASEEETPLEETNETVVQTNEDVKEAEV
SQ  PENAEAQKVVDSSDLQVAASEIAHLAIDEAVLETSNQPSQFDSLQEQKPSVVHENEHVRSVCVDLTFSRDSEQIVSDVIV
SQ  AEVGYDEDECSTIADTITSLSSSPLYTAPVFTERLPSSACFANSKLTLEVMFSGVPQPTISWLIDDHELVSDGERISIKC
SQ  ENGVSAIRFFNVDRNAGGFLKCRATNCAGQVETSCEIVAADEISVISDSSITSSTRPHFVVPLPERVTHTVNDHITIKCK
SQ  FSGQPLPAAMWEKDGVLLDLQKYQVTTEDGTSILKIESASLDDKAVYTCTIANEAGCESTSCTIDVVDDHLGLQQTGLHV
SQ  MCERDQNDVELDILVQSPNHLGVTFNFPPVNRTLARQPPYFLLPLSDKVVIDEKCTLKCVVMGIPLVIVKWIVDGVVVTE
SQ  DDNHEIHFEDGIALLRMKNIKKDKSVVQCEAINCKGKVTTSCVLTKCGVEESEAGDLQKPSFVLSLKDTCTTTDHATLKC
SQ  IVVGTPLPDVSCSFNGVTDNSKIRSEDGIVLIQVNDVTEEGIVVECTISNETGSSTSNCVVKIIKQEEKNYQRPIIVFNQ
SQ  AGSVNNERELSVKVGVIASPEPTLFWKHNGKSIEEGGDYYLIFEDGIGILKVFNIQDGSHEFTCIAKNEYGQTTVEIPVE
SQ  IGLKTENKLTLVKTLNDIAVVDDIVQLKIVAEGDLPIEFKWFEDGQILEDDSSHKITVDKCISTLQLKLEETGTRIITCE
SQ  VSNSSSKVNASCNVERVHNTVSDFVMTNDNSTRFLAVGRKCTRERNNTILKAVVVARENIGDICEIDGEKIPDAYIEGNS
SQ  LSIKVDTLSKKLSNVSFKVSASEGKVFETRKIEIAQEDTDEENFEINYSLRIDEQSGNTTYTFENSELYQGNQSRELDNT
SQ  ERNFTVNKEKDESKKPSEVQPAEIVEQKDVPVQETSAPTVEKLAPVESKETPEVQAAEIVEQKDVPVPETRAPTVEPTVE
SQ  KHTPVDSKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKHTPVESKEKSEVQPAEIVEQKDVTCEEEIKELLTEVEVEL
SQ  FFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPSVEPTV
SQ  EKLAPVESKETSEVQQAEIVEQKDVPVPETSAPSVEPTVEKLAPAESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVE
SQ  LFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPT
SQ  VEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVE
SQ  KLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKL
SQ  KPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAP
SQ  VESKETPEVQPAEILEQKDVTCEEEIKELLTEVEVELFFSKAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEK
SQ  LAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLA
SQ  PVDSKETSEVEPAEIVEQKDVTCEEEIKELLTEVEVELLFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVE
SQ  KLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKH
SQ  APVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAP
SQ  VESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVE
SQ  SKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESK
SQ  ETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKET
SQ  SEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSE
SQ  VQPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVE
SQ  PAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSAPTVEPTIEKLAPVESKETSEVEPA
SQ  EIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVQPAEI
SQ  VEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAHEPTVEKLAPVESKETSEVEP
SQ  AEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDLPVPETSAPTVEPTVEKLAPVESKKTSEVEPAE
SQ  IVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIV
SQ  EQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQ
SQ  KDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKD
SQ  VQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVP
SQ  VPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETTATTFEPTKEKLAPVDSKETSEVQTAEIVEQKDVPVP
SQ  ETSATTVEPTKEKLAPGESKETSEVQQAAIVEQKDVAVPETSATTVEPTKEKLAPVESKETSEIQTAEIVEQKDVPVPET
SQ  STSYVEPTKEKLAPGESKETSEVQQAAIVEQKDVPVPETSATTVEPTKEKLAPVESKETSEIQQAAVVEQKDVPVPETSA
SQ  TTVEPTKEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTFEPTVEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPT
SQ  VEPTVEKLAPVESKETSVESKETQADAKLKKEKDDKHKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKE
SQ  NDDKLKQEADAKLKKENDDKLKQEAAAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLQKENDDKLKQEADAKLQKE
SQ  NDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKE
SQ  KHDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDRLKKDADAKLQKEKDDKLKQEADAKLKKE
SQ  KDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKHEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLKKEKDDKLKHEADAKLQKE
SQ  KDDNFKQEANAKLQKEKDDKLKQEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKE
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKE
SQ  KDDKLKQEKNDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKDKDDKLKQE
SQ  ADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQE
SQ  ADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEANAKLQKEKDDKLKQEADAKLQKEKDDKLKQE
SQ  ADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKD
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKE
SQ  KDNKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKD
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKE
SQ  KGDKLKLEDQTNQSRIFEETSIEVTSLLKCKQQAIIVSKSFALCERVVLNAEEPFTLEVFCNAVFVKQRTDKIGIGIIFE
SQ  RSGASKKDESRPDRLDDNCVLTDVTDGLSILSPPPKAKKHLKKKKKHHKKEKIAVKETEQDEKTVSHLKPEISGMERKRS
SQ  NSGSSDIFVDVDIEAGEESIHTDALVDLNFYDYDQMELSIFEDYDSDDDSASIDCDVSLSNVAADDGIDVFPSDGDTQEV
SQ  EQKVTLPKKHQSDEDVISKEEENLETSVSYGSIEETVSFTIGTGQSIIEHPKSHAVGQMNSEVIIKCKTSQPISDAKWFC
SQ  NGMVLLPDEQVNMTVTGCEAVLRLVKFLPQNKGNYHVLIDGSIGSQPAILSGPVPPVILNKLTKPITHQAGKSFTYKFNF
SQ  MGAPAPRLRVLSNGEPVSFDVKYEIYDNIASLYIPKMSKRDGGEYTVVLENKYGKDESDLHITMVDTPLKPRKAQLVALT
SQ  DTSATFKWLPPHTGESDILHYIVMRRSTESRRWRNIGHVQEKTFTAIELVPNEFYAFRIVAVNGFGEGAPSEIIEVNTLD
SQ  YDQEESFDFAGEEELKLDDVQVNNEVVTEITIEESEVTIEEHRKLKKKSKKSKKTTDEPELDSEIALEVSSDITSSLEIT
SQ  TESTIPDTAPESQETLNVEIAVTETTVQKITNPSDESAKKDVNEDTAVSSIVKKDDKDVNKKSLPESGLTTKKEIQGKPE
SQ  KKIMKKKTEKADSSISETSETLTKDLTQTKQSEPEPAKRTTETSVQDEVKRKTETTSKSKQTTEEHPQPGGKSDSSISST
SQ  SDASEVKQVQQSESEAQKVTEKPETAKLESKSKMTEDTTKESDNKETVDEKPKKKVLKKKTEKSDSTISETSETSAVESA
SQ  GPSESETQNVAAVDKEKKQKETDEKQKLEAEIAGKKSTEQKSKLEAEAKLKRAAEEDAAKKQKEKTEAASKKAAAEKLEL
SQ  EKQAQINKAAEADAVKKQNELDEQNKLEATKKLAAEKLKLEEQSAAKSKQAAEEQAKLDAQTKAKAAEKQTGLEKDEKSN
SQ  KDSGSNETVEEKPKKKVLKKKTEKSDSSISQKSDTSKTVAESAGSSESETQKVADATSKQKETDKKQKLEAEITAKKSAD
SQ  EKSKLETESKLIKAAEDAAKKQKEKEDKLKLEADVASKKAAAEKLELEKQAQIKKAAEADAVKKQKELAEKQKLESEAAT
SQ  KKAAAEKLKLEEQAQINKAAEADAVKKQKELDEKNKLEANKKSAAEKLKLEEESAAKSKQTVEEQAKLDAQTKEKTAEKQ
SQ  TGLEKDDKSTKDSESKETVDEKPKKKVLKKKTEKSDSSISQKSVTSKTVVESGGPSESETQKVADAARKQKETDEKQKLE
SQ  AEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAEADAVKKEKELA
SQ  EKQKLESEAATKKAAAEKLKLEEQKKKDAETASIEKQKEQEKLAQEQSKLEVDAKKSAEKQKLESETKSKKTEEAPKESV
SQ  DEKPKKKVLKKKTEKSDSSISQKSDTAKTVAESAGQSDSETQKVSEADKAHKQKESDEKQKLESEIAAKKSAEQKSKLET
SQ  EAKTKKVIEDESAKKQKEQEDKKKGDDSAKKQKDQKEKQKLESEATSKKPTSEKQKDEKTPQEKAKSENETVMTTEPQQL
SQ  EVKSEPKKSDKTETVEKEVASSTEKSDDSKTKEPKEKKKIIKKKKDTTKPQEASKELSSDESRIDLESDISLSLDTVTES
SQ  DDLSTASTIKLQKESDESGIDSRMGQTSEAEDSPFISQPVSATVTEMAGEAKFTVKFSRKPIYVKWMRDDREIRVAYGKA
SQ  SVETTDDSSVLVIKNIDGKDVGNIYAVFDSEYRSAMARLDLRVPCKITLESSSNAPEIVAGKNLDLSFKISGYPLPTNIE
SQ  LLHNNENLRTRSDVTDFDDSISIRMKRLKLEDSGEIKIIGKNDSSEDQLRIPINVIEVTSKPTSLQVTSTERETVTLTWS
SQ  LPTELNGSNVNEYLVERKTVDGGRWRHACTVTDSRAVVDGLFSGTEYVFRVVAVNGAGQSAPSDTIEATTQAEEEIDETV
SQ  PTSPVEKVKEPVSKKPENTKESEGHKKRDRKESEDHDENNLGKSGKDEFATSGESGTSNQNEESAQLNTSFTSTEQHGQT
SQ  EKQVRKGTRKSLTRSLNIRESDIDADVVEVEYDEQGDDIPSDPTTSGTYAFDKIEEEPARTSGEMAMAEKDSDAMEVRGL
SQ  NKKLSKKGGKEGTSTEKSSSKTKKQEKSALSVQEMNKSLKKKGEKGEAETAASDFIENADQTGMSIQDLNKSMKKKVESG
SQ  EATGQINDASNNKDADELSIQDSQQSLKKKSENESVTGEQLDKSQEVEDDKMTIQSLKKSIKKKPESREVSGGKSEKSKE
SQ  KESDEMSIQQLNKSVKKKPENEAVTQGKSGKSQEQESDKMSIQALNKSMKKKDGVDGVEGNINIGRSDGDQLSVNDIDAE
SQ  LSTSEQVENASQNLGATADSDGDSLSLQTLKKRISKKGIHGEAESKLGEKQSGSDSFTLQDLYEELKAKEDAVEAGAETS
SQ  NADQSAEKTSLEVRDMKKKMKKKQVSGTAENLIGESNRDETSMEIRDLNTQHSNQTGEDESSTFNFGQKDQEQYSMVMKD
SQ  VSKKLARQNAEEIQSGKLIPTTNEEKTGLALTGKNKNLKKGEENEKTKFEAKHLGSSSASDSLAESTLRSKKTKKGEVEK
SQ  SELSIDMKNQDKTTLATTLLEDDLAKTTSAEESEAEHLVALQNKEKTSLAMRRKRVSFDSSTKSESIEDVIPDKNRDSDK
SQ  MSITGIKKKMSQKSESAEAQKNESPEVKEISSFEEKTLKSKKKSKADRNQGTEANLGDKTIDKDYLSVTDKNQSLEKSEA
SQ  SGQAEKSIKAPNKSKVTTSFADESLTSELDRLMADEEMAEMMFAEEEKAADLLNVMNKNKGLNKSEQEESQEISLKSQSK
SQ  VKDSDSLSSTDKKIGLKKSDKDQKLGTSKIFGSKDQESVGYEEKTSNFSKQRRGVSDLGSDAMTDQKNVQESQYAEISAD
SQ  DHMSKTGADGEISATRTIVDGSDAAQGSEYAEISKKRKFKRAEQIGEAETSLCDSRENTHDSLSISDVNPELRRSNVEIS
SQ  AFGQIDLTAEEVTSLTDINKDAQLTKKQDENDAKKSVSKNLKAGAKKDSDTLSITSKKDKFGKRQDSREASATVEQQGEE
SQ  KVTKNLKGSRGKKEKLGDAGIDVNFENQEEFASTTGDIESIVSEKGHDTYSEKTVKSSKKKSPQTAGAEYGGSESLNASS
SQ  ALSTTDVDAQLKNQEKDGVAESSIGKSNQKDSYSEQELNVNKKKKQAVGAAMNQGSGSTKESDNLAVASVESNLAKDSAN
SQ  QEASLHGLVDNDATSLSQLDSEHRLKKRDDELSAHTKLGKHTQSENIALTETDDSLVKGDSEESAELNIKQQGETAEDKY
SQ  VESRKKTTLKKKPEQKQVTDTLSAVDGRHDTTSLSVADSGISFDKSMENELAGSGDGTASASVSAKVRGADGNAKTNLIS
SQ  SFEKPGQESKTSKTLSGKQKKQEKSSFAEKNAGFDLSMGEGKNDESVESSLQKNRDADSLALQGTDLAFSKPSDSSANAH
SQ  LDMPQRELTLRICQAETVDWSDDSEVEEGTRTSAPGEVKKKKKFIISAISQDGEFSDAESITFDENGVRVEKRRRKKRDP
SQ  KEYMGAGELAMRIPAFAKKMQYIGCIEGDVVVFTIKVVSDDVPLIRMYRNDFPVANFDKMAFEGFTKGSEHSFNVTINDI
SQ  RKLDGGKLVFEAKNDYGVDKCTILLDVRDSGSFIEDYSEIHRSAEIQNSVGDVQVKEGETAKLTGRVDGFPLPELIWIKN
SQ  GKEIDMMVPSTKYQLDYHSDGEFEARIANCTFEDDDDYSLLVENLAGVDSCNFQVFVDCNEYPDDEHFNRRRRLQRGRRV
SQ  MEASSDSELDDAKKRKKRRIKRVVERRNPNAPRLTQLIPPRFDKILSDHDAIEGENVVMMVETLGEPEPQVRFYRDGKLI
SQ  DDGSGDRMEVRHEDEMRKHWLILKDICKDEEAEYACQAINVAGEAWCFSDVVVHMSEESRDDDKSVDEVDDSTVLEEKKD
SQ  DGDDKSKPKTKKKIIKKKETPESEQVTAAEPEQQKISEVDVQSVAETEVGAKKKPDAEKPTDLSKAKKDSKSKKSDEPEA
SQ  STEEKSTTEKPTNDKTSKKSAEKKTVKPKKEVTGKPLEAKKPVEDKKDASQPSSSKESSPPTDGKKKKQIPKALFIPDEI
SQ  SSRFGDPSTMHSETNITTTIRGREGSADAKTPLVEPLSASVSMKVESAKEKAEFSFKRRSETPDDKSRKKEGLPPAKKSE
SQ  KKDEVTAEKQSTEALIESKKKEVDESKISEQQPSDKNKSEVVGVPEKAAGPETKKDVSEIEEVPKKKTIKKKTEKSDSSI
SQ  SQKSNVLKPADDDKSKSDDVTDKSKKTTEDQTKVATDSKLEKAADTTKQIETETVVDDKSKKKVLKKKTEKSDSFISQKS
SQ  ETPPVVEPTKPAESEAQKIAEVNKAKKQKEVDDNLKREAEVAAKKIADEKLKIEAEANIKKTAEVEAAKKQKEKDEQLKL
SQ  ETEVVSKKSAAEKLELEKQAQIKKAAEADAVKKQKELNEKNKLEAAKKSAADKLKLEEESAAKSKKVSEESVKFGEEKKT
SQ  KAGEKTVQVESEPTSKKTIDTKDVGATEPADETPKKKIIKKKTEKSDSSISQKSATDSEKVSKQKEQDEPTKPAVSETQM
SQ  VTEADKSKKQKETDEKLKLDAEIAAKTKQEADEKSKLDAQEKIKKVSEDDAARKEKELNDKLKLESEIATKKASADKLKL
SQ  EEQAQAKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAGADAVKKQKELDEKNKLEANKKSAAGK
SQ  LKIEEESAAKSKQTVEEQAKLDAQTKAKTAEKQTKLEKDEKSTKESESKETVDEKPKKKVLKKKTEKSDSSISQKSETSK
SQ  TVVESAGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAA
SQ  SKKAAAEKLELEKQSHIKKAAEVDAVKKQKELEEKQRLESEAATKKADAEKLKLEEQKKKAAEIALIEIQKEQEKLAQEQ
SQ  SRLEDEAKKSAEKQKLESETKSKQTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSKSAKSTVDAAETLESDFNLVEKK
SQ  TVQKVEQSPDESTSATIKRDPAQKTEEISKQDDGDEKKTTTDGKPPKPEDSEATPKKRVVKKKTQKSDSVASDASLADVS
SQ  KLSDDVEEKPKKKVLKKKTEKSDSVISETSSVDTIKPESVEIPTEKAEQMILHNRFSTDSAVESEPKNAHKDDTEKTTDD
SQ  MMTRRKSSAIFSDDEQSISSKTSSEGRRRRRRTGFASKFASDTLALRGDNVEIEAELLAEDDTVTWKVNGKDADLNSRCH
SQ  EMSHTFFRTLIIDEVEPTDSGMEITATCGTESHTTILKVEELPVDFVKYLPRKTSGKEGQEVTISVTLNHPIDISKVVWL
SQ  KDGKPLEINKDYSIDTVGCSVSLTLRRAKYEDSGKYKVVCDGVDCSTHLSIQGKPVLKNVSETKPVITVDKDDQFSLLVA
SQ  YDSNPEASFSMTVDGKDLEFDGRSRIDVVDDGLKLTKRGVSKTDAGEYEVKLKNEFGEVAQKFDVKVNDTPSAPGDVSVV
SQ  KAESDCLHIEWTAPTEDNGAEVTSYVIEKKESGRRKFHKVATVNGKKTSYVVDDLEIETPYIVRIAAVNKFGTGEFIETK
SQ  PVQTGSPFQVPTVEFPPTIDNVTSTSCSLSWPKPIEDGGSPVYGYDVYKRENEGEWQKMNGEELVFTESFNVRALSSGKE
SQ  YEFKIEACNEAGLRSNSNVVSKKLTVEGLVPEIILDMPMVKVLDNDKVEVTWKSDGEKEFVVQYKSDGSSIWASVDIGGP
SQ  RSESAATSKCIIDGLREGIPYVFRVAARNQHGTGEFSEPTIPVVVLADDAPRVLKAIKPVKIPKKGELRLECHAAGHPAP
SQ  EYIWYKDGKEIIPTDENTEIVNEGSMSALIIHELAGEDVGLYKVLVENIHGTAESEAEVGISDVRAHFNSSFSELTEIEE
SQ  GHDIELTCEVSDEEAVVNWYKDGKKLVASDRVQFYAMARKRTLRIKGSTDADSGVYKCETTDGRSRTEGEVIVNEQEPHI
SQ  LVGPQDAIVKDFGETMVLFCETSKPVRKVKWFKNGVEIWPQMNKAIMENDGKRATLEIKNFDKHDIGAYTASVSEKETSA
SQ  PAKLVFEVAPNLIIPTEIRDGVTVHAGNEFDFAVEFSGFPIPTIHLTNNGTPLKAIAVVTEYDDSVSVRMKDVTLDNSGT
SQ  VRVIAESPLGQCIKEIPLKIIDKPSAPCDLQFKEVTEDSVFLSWQPPLETNGAPLTGYVIERKAVDNNRWRPCGQVKPTK
SQ  LTFVAEDLFCNQVYGFRILAVNEVGESEPCDTVDVLTLESSEPVSESSELFVPKIAILRTPQVTVAVDETKVTLRWEECP
SQ  ETSLYKVERKKVGDSDWLEIANTDRNKFKDRSLTESGEYVYQVTATGIHAVSSPSEETNPVKILVPGSEMPASKTEKKTD
SQ  AAKSESEQKSAEEIVAEKQVDQSQASESTTEAVEEKKTKKVVKKKVAENKGEETLQEVKEKLKKGKAVEKVQDESRRGSL
SQ  QASSDNESVTTTSEKRSEAELEKNSEKSAEKKSTSADLEAADKAETEKSETGKETTEKKKKVVKKVAKKGLVKADKSKIE
SQ  LTAGKEGEISAQVAETGVSVEWKKDGKALDASYTVTSTGGVSTVKIPIVDVNTSGVFTCKVKSSEGDEEEVSIAVTVKLP
SQ  EVPKVEAEQSIVEVKVGDVAKLSAKISEPASSVNWTKDDKPIKEDGNVKAQLSPDGTAQLTISKTDSAHSGIYKLNVEND
SQ  AGKGKVEIALRIKGAAKGAPGIPTGPIVFDDVTESSAEFSWKAPENNGGCEITGYNVERKESKNKGWKQCGKTKELKFKA
SQ  DGLEEGTDYDVKVSAVNTMGTGSALEGKITTLKKKEETGKQKSEKSESDEKKSESDKVSELKQIGKPEYVSSTATSIALK
SQ  WTSDNDEVTYTVQMKEANSKRPWAVVAKEISECSATIAQLKEGTSYLFRVIAQNKTGQTVTSEQSESIECKDTTESKKPA
SQ  FTNAPTDLTAVKNGKTKITAEFTGHPAPEIHWFKNKKEIFSGKRQWIENIAGATSLTIGEMREDDEGEYKIVVKNTAGSV
SQ  EHSCKLTMDQLPEINRVDRYASTLVFDKGETVKLRLSFSGRPQPEVIWIDNNGKVIEESRKMKIEKTVLNTVLTINSIDS
SQ  QDQGEFALKIKNRCGEDKYAIGIQVTDRPAAPGKPAVEDQNVDSVRLRWAAPTNDGGSPVRNYTVEMCTEKGKTWTKAEV
SQ  TKQAFITLFNLVPGESYRFRVRADNTFGQSEPSDESELVVVKNVSRVVEEPKKKEVKVKEQESVDYERVAKDSEPSEYKT
SQ  IDIHRLPNDLQAKYIIHEELGKGAYGTVYRATEKATGKTWAAKMVQVRPGVKKENVIHEISMMNQLHHEKLLNLHEAFDM
SQ  GNEMWLIEEFVSGGELFEKILEDDSLMSEEEVRDYMHQILLGVSHMHKNQIVHLDLKPENILLKAKNSNELKIIDFGLAR
SQ  KLDPKKSVKLLFGTPEFCAPEVVNYQPVGLSTDMWTVGVISYVLLSGLSPFLGDSDEDTLANVSASDWDFDDPSWDDVSD
SQ  LAKDFICRLMIKDKRKRMSVQDALRHPWITGPLLSAFNDLSEYVKKMQPKLDKSGVPARQKRNFLSLKRWSDDLLPIGRL
SQ  AKRGAIFRRLTMDGVFERNIAFDTDAAPSVKKQLEDIVANVGDLIATLSCDVDGVPSPKVQWYKDDKELTVPSMKYDSFY
SQ  NEGLAELTVKNIVESDAGKYTCRATNDLGSIMTHAKLSVKADEKKKKKSKTSPAVIEKKKDRKTSKVVVIEEMIDMPPNF
SQ  HHLLQDDEAKIGEPKILVVTNTTLPEPTVDWYHNGEHISINDSNYLRKHDKGRYELHILSVDSTDEGKWKAVGKNAFGEC
SQ  ESEAKLTVVIPDGQYAPSFGKQLSDVKCSESDILKLEVNIQANPAPEINWFRNESEIEHSQHHRLQFDDGSGNYSLTIID
SQ  AYAEDSGEYKCVAKNKIGKAHTVCCVRIEELLSKRSKKIDGSKAPRFRMQLPTPREVPQGADLTLVCSVSGTPHPNIKWT
SQ  KDDKPIDMSNKQVRHENGVCTLHIIGARDDDQGRYVCEAENIHGVAQSFSVVEIKEAVDKDHVRPKFLEPLVNCSTCEGN
SQ  EMVLECCVTGKPIPTITWYKDGLKLIIENRMLQYTDRKGVSRLNIMNVVMNDDGEYTCEAVNSLGKDFTHCTVKVVDMGL
SQ  SKTRLTPVRSRSRSRSRSPSVVGGEIQRPPVVTRPLADATVTEGNRELLEVEVDGFPTPTIEWYHDGKLVAESRTLRTYF
SQ  DGRVAFLKIYEAHEEHNGQYVCKVSNKLGAVETRAIVVVEAPDAAEHVTQMPTFVKKLQDVVLKTAGETATFTCQSYANP
SQ  AAQVVWLHNGKALQQTKSNYKTRLFDDNTATLVIENVTDELCGTYTAVANNQFGDVHTSAQLTISGSEAKKIAASLPYFI
SQ  IELKPKINVVEGATLSIQADLNGSPIPEVVWLKDNSELVESDRIQMKCDGVNYQLLVRDVGLEDEGTYTITAENEKGKIR
SQ  QNTEVSVTKSKEVKEKKEKKKVEKKDEGKKKPGRPGLPRPSGASKTEQVTMAFDAPSEGPADSYEVERRCPDQREWVSCG
SQ  STKSLELEIKGLTPNTEYIFRVAGKNKQGLGEWSEMTSTLKTASVGQAPQFTISPQSKIIANRDDEFEIAVEFSGTPTPS
SQ  VKWYKENLQIVPDEKIDVATTSTSSILNLKSQEENGTFNCLIENELGQASASCQVTIFNKPASLQSTPDHSLERNLVPTL
SQ  QKALNNESAQAGQQIMLTCRISSRSESTVAWFKDDERIESAGRYELSSDKKSNHKLVCHAVQSQDTGKYRCVVTNKYGYA
SQ  ESECNVAVEDVTKFIAPSFSATLSDSTAILGHNITLECKVEGSPAPEVSWTKDGERISTTRRIRQTQDENGNCKLSISKA
SQ  ESDDMGVYVCSATSVAGVDSTSSMVMIAKTTGTDSHLVIAQTADEKHEKPRFTRAPPSLIEVNESGQFTLIAKAVGEPKP
SQ  TVTWLKDGREILRTNRIYHHFVTGDGESHLIAECVVSKTSGIFSCKAENPNGTVIAETQVIVQRMKPANQLANVAPKFTI
SQ  PLTDMGIVNGHPTTLSCNVTGSPEPTLEWIYIDDSGHKINLTSSTTDWTECRFGKVAELKSERVLREQRGTYQCIATNSS
SQ  GQATTQCYLLVGELSDEPAGPPRFVKCLQDTWTPLKESIEFSVELAGFPTPDLTWYHNEKKINEGKDVKITFPSDTTSVL
SQ  SIKNVSLASLGMYFVEASNIHGVLRTAGRLNVSDERRKAEPPQFKHVLEPVLAVQPKVAFSEEHPRASSSAATARVKKGA
SQ  APMFLQGLEDMDLKAGASAAVAGKLGRKLRPHRSTTNDADKLAKALAQSLRLDEPRASIDSRPESAANAALDEVRAAINS
SQ  RNKRVCRPKFMVKPKPRKVLEEYKSLRLKTAISGNPMPQVHWDKEGIILETGNKYSIYNDGDFYYLEVHHVSTFDKGFYN
SQ  CTAANNEGIITCTSEIDVLPNKEDSAAQVAKRKSRKEAKAPNFIEVLPGRSQANLNESLCVECSVSAYPCASIIWTRNSV
SQ  RLLPQADRYTMSYDGECASLKFISVTPGDEGTYACEAVNELGSAVTNMNLQVSGVDPNAAEGIPPLFRFEKIKSVRKVVD
SQ  GSRVELAAELVQASEPLQIRWLRNKVTIVDSPSFSYSRSENMVFLTIADVFPEDGGEYTVEAKNQSGIARCTMQLDVRNN
SQ  ERSVADEAPRVFDFEPTTRSDPGVSVELRAKVIGHPDPVISWTKAGQKLNNEEKYMMRNEGDKFILRIANVTRADAGKYE
SQ  LTAINPSGQANAELELTVVQSTKTVGAKPKFNESPISVQTCEKNRAELRASFSGTPAPACRWFYNGNELIDGLDGYTITS
SQ  SDTNSSLLINSVDKKHFGEYLCTIRNQNGEELANAMILSEVLSMFYSSLFLVVFVDIVAQCHVARLLHFLNEERFVGRNI
SQ  FA
//
ID  Q09349;
PN  Ubiquitin conjugation factor E4 ufd-2;
GN  ufd;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27669035}. Nucleus membrane {ECO:0000269|PubMed:27669035}; Peripheral membrane protein {ECO:0000269|PubMed:27669035}; Cytoplasmic side {ECO:0000269|PubMed:27669035}. Nucleus, nucleolus {ECO:0000269|PubMed:27669035}. Note=Localizes to germline syncytium. In the late pachytene, accumulates at the nuclear periphery forming a ring. Following ionizing radiation-mediated DNA damage, localizes to foci within nucleoli where it colocalizes with cdc-48.1 and/or cdc- 48.2, atx-3, proteasome alpha subunit and ubiquitinated proteins. Localization to foci is ubiquitin-dependent and regulated by E3 ligase hecd-1 and deubiquitinating enzyme atx-3. ufd-2 foci are formed following the initiation of homologous recombination (HR) and persist until HR is completed. ufd-2 foci are also formed upon cep-1 activation. {ECO:0000269|PubMed:27669035}.
DR  UNIPROT: Q09349;
DR  UNIPROT: Q6BEV4;
DR  UNIPROT: Q95QB5;
DR  Pfam: PF04564;
DR  Pfam: PF10408;
DR  PROSITE: PS51698;
DE  Function: Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (PubMed:27669035). The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues (PubMed:27669035). Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases (PubMed:15294159, PubMed:27669035, PubMed:29396393). Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline (PubMed:27669035). Required for germline apoptosis in response to DNA damage downstream of cep-1 (PubMed:27669035). Involved in the resolution of DNA-repair sites by promoting the release of rad-51 from DNA damage foci (PubMed:27669035). In association with protein-ligase chn-1, acts as an E3/E4 ligase to poly-ubiquitinate lysine residues in the UCS domain of myosin chaperone unc-45 (PubMed:15294159, PubMed:29396393). By targeting myosin chaperone unc-45 for proteasomal degradation, regulates myosin assembly in body wall muscles in association with cdc- 48.1 and chn-1 (PubMed:15294159, PubMed:17369820). However, in a contrasting study, acts as an E3 ligase, independently of chn-1, to poly-ubiquitinate unc-45 without promoting unc-45 proteasomal degradation (PubMed:29396393). Instead, uses unc-45 as an adapter protein to recruit and poly-ubiquitinate unfolded myosin heavy chain B unc-54 (PubMed:29396393). {ECO:0000269|PubMed:15294159, ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:27669035, ECO:0000269|PubMed:29396393}.
DE  Reference Proteome: Yes;
DE  Interaction: P90879; IntAct: EBI-2417964,EBI-317233; Score: 0.49
DE  Interaction: G5EEM6; IntAct: EBI-317233,EBI-317215; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0000151;
GO  GO:0051087;
GO  GO:0031625;
GO  GO:0034450;
GO  GO:0008340;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0000209;
GO  GO:0016567;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27669035};
SQ  MIEDEKAGLQPMDISDASVFFFQADVESKDFLTSLFDCEGKSDDRMLRYADAIIDVQNLNFDVSPQCLQSNIAEIITKFV
SQ  LLSQDGSRRGLSRSFNFIDPDIIAGCREEDAIEFLLINFVRCHHELGKSGTSNCYKKTLESTRKAVFSVFVMIQRGYLES
SQ  QLRSQHASLVFTKRLLEDTVSNVFLRTLVEYLASTDECDEDAITETFNPIFGILRSGIICQRFEDNKDEIVRQILRVMNL
SQ  LLSIRLPSNGPRPLSNLLVNREDFLPTPSEKIQGREFGLMSFLGPFFSYGLESSARRPNHRVFVDCEEDARKYDGSVNTE
SQ  QKLYFQRMDPIRTMLHQLMLPLASDQGSRNKTLRWIATIISTNDIRTRSHYDPSDVLCDHYMTNFLSVMYMFSEKIDLSK
SQ  IIVDYPFLPSSLINISKETRLKMDESGAVAFASQFADRPDEYHFSTVCFFLTIAAQRLVIPPLMNQISEYSRHLKELKHK
SQ  INALKEKLNTVSGFERAEVEKKLNYETEHWKLMSRHLLCVKTQAQDPALMASSMDFVDKQMKFILNLLCDNLDLLGDDSQ
SQ  LPTEVSQMFCALPEYFLEDALDFYIFAISNGMKLLMERNADWISRLTVLFTQYHYIKSPFLVSKLVRVLSSIQPPLWFNV
SQ  VRLRMAQENLLMCMIKFYSDFEDNGDFYEKFNVRGNIQYMLEKMEEDMFYKGKFMDMARECGAEFIRFVNMVINDATWCI
SQ  DESLSGLKSIHDVEKKMANKVEWDNTDQEIRNQDLGVYEEAKRKVKGWLGTAKSNLKLLLSITVNSPEPFRTPVLGERLA
SQ  AMLNHNLSQLIGSKASELKVKDPRSYGWEPREFVSLLISIYLKLNMPAFVKYIAYDERTYSPEFFHNAIECMRKNSIVGF
SQ  SQLESFEHLAEDVKKEYEAKAELEEEYDDVPEEFKDPIMDAIMVDPVKLPSGHVMDRAVIERHLLSTPNNPFNRAPLSHN
SQ  ELSPDSELKAKIQEWICQKRNSKK
//
ID  P40075;
PN  Vesicle-associated membrane protein-associated protein SCS2;
GN  SCS2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Nucleus membrane; Single-pass type IV membrane protein.
DR  UNIPROT: P40075;
DR  UNIPROT: D3DM26;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1. {ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15668246}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-16735,EBI-10420; Score: 0.35
DE  Interaction: P35845; IntAct: EBI-16735,EBI-12611; Score: 0.55
DE  Interaction: P39523; IntAct: EBI-16735,EBI-27256; Score: 0.62
DE  Interaction: Q07657; IntAct: EBI-22083,EBI-16735; Score: 0.63
DE  Interaction: Q00402; IntAct: EBI-16735,EBI-12386; Score: 0.69
DE  Interaction: Q08229; IntAct: EBI-16735,EBI-36841; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-16735,EBI-11191; Score: 0.35
DE  Interaction: P07149; IntAct: EBI-16735,EBI-6795; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-16735,EBI-2218; Score: 0.35
DE  Interaction: P18759; IntAct: EBI-16735,EBI-16565; Score: 0.35
DE  Interaction: P22137; IntAct: EBI-16735,EBI-4766; Score: 0.35
DE  Interaction: P38616; IntAct: EBI-16735,EBI-24029; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-16735,EBI-13517; Score: 0.35
DE  Interaction: Q03661; IntAct: EBI-16735,EBI-2346381; Score: 0.35
DE  Interaction: P19097; IntAct: EBI-16735,EBI-6806; Score: 0.35
DE  Interaction: P28834; IntAct: EBI-16735,EBI-8878; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-16735,EBI-18986; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-16735,EBI-8603; Score: 0.53
DE  Interaction: P47079; IntAct: EBI-16735,EBI-19072; Score: 0.35
DE  Interaction: P41277; IntAct: EBI-16735,EBI-7829; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-16735,EBI-8883; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-16735,EBI-14372; Score: 0.35
DE  Interaction: P22203; IntAct: EBI-16735,EBI-20268; Score: 0.35
DE  Interaction: P34216; IntAct: EBI-16735,EBI-21243; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-16735,EBI-4308; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-16735,EBI-20254; Score: 0.53
DE  Interaction: P34760; IntAct: EBI-16735,EBI-19623; Score: 0.35
DE  Interaction: P32610; IntAct: EBI-16735,EBI-20264; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-16735,EBI-9890; Score: 0.35
DE  Interaction: P00358; IntAct: EBI-16735,EBI-7212; Score: 0.35
DE  Interaction: Q12230; IntAct: EBI-16735,EBI-34978; Score: 0.35
DE  Interaction: P53252; IntAct: EBI-16735,EBI-23225; Score: 0.53
DE  Interaction: P15108; IntAct: EBI-16735,EBI-8666; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-16735,EBI-8591; Score: 0.53
DE  Interaction: Q06385; IntAct: EBI-16735,EBI-35395; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-16735,EBI-8627; Score: 0.53
DE  Interaction: P19882; IntAct: EBI-16735,EBI-8586; Score: 0.35
DE  Interaction: Q12377; IntAct: EBI-16735,EBI-308; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-16735,EBI-6475; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-16735,EBI-7218; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-16735,EBI-2169; Score: 0.35
DE  Interaction: P21672; IntAct: EBI-16735,EBI-15246; Score: 0.35
DE  Interaction: P38713; IntAct: EBI-12630,EBI-16735; Score: 0.57
DE  Interaction: O15209; IntAct: EBI-16735,EBI-723574; Score: 0.56
DE  Interaction: Q08984; IntAct: EBI-16735,EBI-3719178; Score: 0.37
DE  Interaction: Q12451; IntAct: EBI-16735,EBI-12621; Score: 0.55
DE  Interaction: P21957; IntAct: EBI-12555,EBI-16735; Score: 0.59
DE  Interaction: P37297; IntAct: EBI-16735,EBI-18454; Score: 0.35
DE  Interaction: P38886; IntAct: EBI-16735,EBI-15949; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-16735,EBI-15394; Score: 0.35
DE  Interaction: P38631; IntAct: EBI-16735,EBI-7708; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-6533,EBI-16735; Score: 0.27
DE  Interaction: P47088; IntAct: EBI-16735,EBI-26307; Score: 0.37
GO  GO:0005935;
GO  GO:0005934;
GO  GO:0000781;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0071561;
GO  GO:0005886;
GO  GO:0033149;
GO  GO:0035091;
GO  GO:0006348;
GO  GO:0048309;
GO  GO:0090158;
GO  GO:0061163;
GO  GO:0061817;
GO  GO:0042308;
GO  GO:0008654;
GO  GO:0032377;
GO  GO:0060304;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFK
SQ  CRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPA
SQ  VVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLG
SQ  WFYR
//
ID  Q8IZQ1;
PN  WD repeat and FYVE domain-containing protein 3;
GN  WDFY3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Cytoplasm, cytosol {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Nucleus, PML body {ECO:0000269|PubMed:20168092}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:15292400}; Cytoplasmic side {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q6VNB8}. Cell projection, axon {ECO:0000250|UniProtKB:Q6VNB8}. Note=Relocalization from the nucleus to the cytosol is stimulated by cellular stress, such as starvation or proteasomal inhibition. In the cytosol of starved cells, colocalizes with autophagic structures (PubMed:15292400, PubMed:20168092, PubMed:20971078, PubMed:20417604). This redistribution is dependent on p62/SQSTM1 (PubMed:20168092). When nuclear export is blocked by treatment with leptomycin B, accumulates in nuclear bodies, that completely or partially colocalize with promyelocytic leukemia (PML) bodies (PubMed:20168092). Localizes throughout neurons, including within axons. In neurons, enriched in the light membrane fraction along with the synaptosomal membrane protein synaptophysin and the membrane- bound form of LC3/MAP1LC3A/MAP1LC3B, called LC3-II, a classic marker for autophagic vesicles (By similarity). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}.
DR  UNIPROT: Q8IZQ1;
DR  UNIPROT: Q4W5K5;
DR  UNIPROT: Q6P0Q5;
DR  UNIPROT: Q8N1T2;
DR  UNIPROT: Q8NAV6;
DR  UNIPROT: Q96BS7;
DR  UNIPROT: Q96D33;
DR  UNIPROT: Q96N85;
DR  UNIPROT: Q9Y2J7;
DR  PDB: 3WIM;
DR  Pfam: PF02138;
DR  Pfam: PF01363;
DR  Pfam: PF14844;
DR  PROSITE: PS50197;
DR  PROSITE: PS51783;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  PROSITE: PS50178;
DR  OMIM: 617485;
DR  OMIM: 617520;
DR  DisGeNET: 23001;
DE  Function: Required for selective macroautophagy (aggrephagy). Acts as an adapter protein by linking specific proteins destined for degradation to the core autophagic machinery members, such as the ATG5- ATG12-ATG16L E3-like ligase, SQSTM1 and LC3 (PubMed:20417604). Along with p62/SQSTM1, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with SQSTM1, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Important for normal brain development. Essential for the formation of axonal tracts throughout the brain and spinal cord, including the formation of the major forebrain commissures. Involved in the ability of neural cells to respond to guidance cues. Required for cortical neurons to respond to the trophic effects of netrin-1/NTN1 (By similarity). Regulates Wnt signaling through the removal of DVL3 aggregates, likely in an autophagy-dependent manner. This process may be important for the determination of brain size during embryonic development (PubMed:27008544). May regulate osteoclastogenesis by acting on the TNFSF11/RANKL - TRAF6 pathway (By similarity). After cytokinetic abscission, involved in midbody remnant degradation (PubMed:24128730). In vitro strongly binds to phosphatidylinositol 3-phosphate (PtdIns3P) (PubMed:15292400). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:27008544}.
DE  Disease: Microcephaly 18, primary, autosomal dominant (MCPH18) [MIM:617520]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH18 affected individuals manifest microcephaly with mild to moderate intellectual disability. {ECO:0000269|PubMed:27008544}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-1569256; Score: 0.71
DE  Interaction: Q63HR2; IntAct: EBI-949753,EBI-1569256; Score: 0.37
DE  Interaction: Q92569; IntAct: EBI-1569256,EBI-79893; Score: 0.51
DE  Interaction: Q5R372-2; IntAct: EBI-1569256,EBI-10692254; Score: 0.49
DE  Interaction: P62993; IntAct: EBI-1569256,EBI-401755; Score: 0.49
DE  Interaction: P40763; IntAct: EBI-1569256,EBI-518675; Score: 0.49
DE  Interaction: O95166; IntAct: EBI-712001,EBI-1569256; Score: 0.35
DE  Interaction: Q9H1Y0; IntAct: EBI-1569256,EBI-1047414; Score: 0.63
DE  Interaction: P42858; IntAct: EBI-466029,EBI-1569256; Score: 0.58
DE  Interaction: P37840; IntAct: EBI-985879,EBI-1569256; Score: 0.35
DE  Interaction: P54253; IntAct: EBI-930964,EBI-1569256; Score: 0.27
DE  Interaction: Q13501; IntAct: EBI-1569256,EBI-307104; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-447544,EBI-1569256; Score: 0.35
DE  Interaction: O00418; IntAct: EBI-6255306,EBI-1569256; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-1569256; Score: 0.40
GO  GO:0005776;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097635;
GO  GO:0019898;
GO  GO:0016234;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0005545;
GO  GO:0003831;
GO  GO:0046872;
GO  GO:0035973;
GO  GO:0007275;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15292400};
SQ  MNMVKRIMGRPRQEECSPQDNALGLMHLRRLFTELCHPPRHMTQKEQEEKLYMMLPVFNRVFGNAPPNTMTEKFSDLLQF
SQ  TTQVSRLMVTEIRRRASNKSTEAASRAIVQFLEINQSEEASRGWMLLTTINLLASSGQKTVDCMTTMSVPSTLVKCLYLF
SQ  FDLPHVPEAVGGAQNELPLAERRGLLQKVFVQILVKLCSFVSPAEELAQKDDLQLLFSAITSWCPPYNLPWRKSAGEVLM
SQ  TISRHGLSVNVVKYIHEKECLSTCVQNMQQSDDLSPLEIVEMFAGLSCFLKDSSDVSQTLLDDFRIWQGYNFLCDLLLRL
SQ  EQAKEAESKDALKDLVNLITSLTTYGVSELKPAGITTGAPFLLPGFAVPQPAGKGHSVRNVQAFAVLQNAFLKAKTSFLA
SQ  QIILDAITNIYMADNANYFILESQHTLSQFAEKISKLPEVQNKYFEMLEFVVFSLNYIPCKELISVSILLKSSSSYHCSI
SQ  IAMKTLLKFTRHDYIFKDVFREVGLLEVMVNLLHKYAALLKDPTQALNEQGDSRNNSSVEDQKHLALLVMETLTVLLQGS
SQ  NTNAGIFREFGGARCAHNIVKYPQCRQHALMTIQQLVLSPNGDDDMGTLLGLMHSAPPTELQLKTDILRALLSVLRESHR
SQ  SRTVFRKVGGFVYITSLLVAMERSLSCPPKNGWEKVNQNQVFELLHTVFCTLTAAMRYEPANSHFFKTEIQYEKLADAVR
SQ  FLGCFSDLRKISAMNVFPSNTQPFQRLLEEDVISIESVSPTLRHCSKLFIYLYKVATDSFDSRAEQIPPCLTSESSLPSP
SQ  WGTPALSRKRHAYHSVSTPPVYPPKNVADLKLHVTTSSLQSSDAVIIHPGAMLAMLDLLASVGSVTQPEHALDLQLAVAN
SQ  ILQSLVHTERNQQVMCEAGLHARLLQRCSAALADEDHSLHPPLQRMFERLASQALEPMVLREFLRLASPLNCGAWDKKLL
SQ  KQYRVHKPSSLSYEPEMRSSMITSLEGLGTDNVFSLHEDNHYRISKSLVKSAEGSTVPLTRVKCLVSMTTPHDIRLHGSS
SQ  VTPAFVEFDTSLEGFGCLFLPSLAPHNAPTNNTVTTGLIDGAVVSGIGSGERFFPPPSGLSYSSWFCIEHFSSPPNNHPV
SQ  RLLTVVRRANSSEQHYVCLAIVLSAKDRSLIVSTKEELLQNYVDDFSEESSFYEILPCCARFRCGELIIEGQWHHLVLVM
SQ  SKGMLKNSTAALYIDGQLVNTVKLHYVHSTPGGSGSANPPVVSTVYAYIGTPPAQRQIASLVWRLGPTHFLEEVLPSSNV
SQ  TTIYELGPNYVGSFQAVCMPCKDAKSEGVVPSPVSLVPEEKVSFGLYALSVSSLTVARIRKVYNKLDSKAIAKQLGISSH
SQ  ENATPVKLIHNSAGHLNGSARTIGAALIGYLGVRTFVPKPVATTLQYVGGAAAILGLVAMASDVEGLYAAVKALVCVVKS
SQ  NPLASKEMERIKGYQLLAMLLKKKRSLLNSHILHLTFSLVGTVDSGHETSIIPNSTAFQDLLCDFEVWLHAPYELHLSLF
SQ  EHFIELLTESSEASKNAKLMREFQLIPKLLLTLRDMSLSQPTIAAISNVLSFLLQGFPSSNDLLRFGQFISSTLPTFAVC
SQ  EKFVVMEINNEEKLDTGTEEEFGGLVSANLILLRNRLLDILLKLIYTSKEKTSINLQACEELVKTLGFDWIMMFMEEHLH
SQ  STTVTAAMRILVVLLSNQSILIKFKEGLSGGGWLEQTDSVLTNKIGTVLGFNVGRSAGGRSTVREINRDACHFPGFPVLQ
SQ  SFLPKHTNVPALYFLLMALFLQQPVSELPENLQVSVPVISCRSKQGCQFDLDSIWTFIFGVPASSGTVVSSIHNVCTEAV
SQ  FLLLGMLRSMLTSPWQSEEEGSWLREYPVTLMQFFRYLYHNVPDLASMWMSPDFLCALAATVFPFNIRPYSEMVTDLDDE
SQ  VGSPAEEFKAFAADTGMNRSQSEYCNVGTKTYLTNHPAKKFVFDFMRVLIIDNLCLTPASKQTPLIDLLLEASPERSTRT
SQ  QQKEFQTYILDSVMDHLLAADVLLGEDASLPITSGGSYQVLVNNVFYFTQRVVDKLWQGMFNKESKLLIDFIIQLIAQSK
SQ  RRSQGLSLDAVYHCLNRTILYQFSRAHKTVPQQVALLDSLRVLTVNRNLILGPGNHDQEFISCLAHCLINLHVGSNVDGF
SQ  GLEAEARMTTWHIMIPSDIEPDGSYSQDISEGRQLLIKAVNRVWTELIHSKKQVLEELFKVTLPVNERGHVDIATARPLI
SQ  EEAALKCWQNHLAHEKKCISRGEALAPTTQSKLSRVSSGFGLSKLTGSRRNRKESGLNKHSLSTQEISQWMFTHIAVVRD
SQ  LVDTQYKEYQERQQNALKYVTEEWCQIECELLRERGLWGPPIGSHLDKWMLEMTEGPCRMRKKMVRNDMFYNHYPYVPET
SQ  EQETNVASEIPSKQPETPDDIPQKKPARYRRAVSYDSKEYYMRLASGNPAIVQDAIVESSEGEAAQQEPEHGEDTIAKVK
SQ  GLVKPPLKRSRSAPDGGDEENQEQLQDQIAEGSSIEEEEKTDNATLLRLLEEGEKIQHMYRCARVQGLDTSEGLLLFGKE
SQ  HFYVIDGFTMTATREIRDIETLPPNMHEPIIPRGARQGPSQLKRTCSIFAYEDIKEVHKRRYLLQPIAVEVFSGDGRNYL
SQ  LAFQKGIRNKVYQRFLAVVPSLTDSSESVSGQRPNTSVEQGSGLLSTLVGEKSVTQRWERGEISNFQYLMHLNTLAGRSY
SQ  NDLMQYPVFPWILADYDSEEVDLTNPKTFRNLAKPMGAQTDERLAQYKKRYKDWEDPNGETPAYHYGTHYSSAMIVASYL
SQ  VRMEPFTQIFLRLQGGHFDLADRMFHSVREAWYSASKHNMADVKELIPEFFYLPEFLFNSNNFDLGCKQNGTKLGDVILP
SQ  PWAKGDPREFIRVHREALECDYVSAHLHEWIDLIFGYKQQGPAAVEAVNVFHHLFYEGQVDIYNINDPLKETATIGFINN
SQ  FGQIPKQLFKKPHPPKRVRSRLNGDNAGISVLPGSTSDKIFFHHLDNLRPSLTPVKELKEPVGQIVCTDKGILAVEQNKV
SQ  LIPPTWNKTFAWGYADLSCRLGTYESDKAMTVYECLSEWGQILCAICPNPKLVITGGTSTVVCVWEMGTSKEKAKTVTLK
SQ  QALLGHTDTVTCATASLAYHIIVSGSRDRTCIIWDLNKLSFLTQLRGHRAPVSALCINELTGDIVSCAGTYIHVWSINGN
SQ  PIVSVNTFTGRSQQIICCCMSEMNEWDTQNVIVTGHSDGVVRFWRMEFLQVPETPAPEPAEVLEMQEDCPEAQIGQEAQD
SQ  EDSSDSEADEQSISQDPKDTPSQPSSTSHRPRAASCRATAAWCTDSGSDDSRRWSDQLSLDEKDGFIFVNYSEGQTRAHL
SQ  QGPLSHPHPNPIEVRNYSRLKPGYRWERQLVFRSKLTMHTAFDRKDNAHPAEVTALGISKDHSRILVGDSRGRVFSWSVS
SQ  DQPGRSAADHWVKDEGGDSCSGCSVRFSLTERRHHCRNCGQLFCQKCSRFQSEIKRLKISSPVRVCQNCYYNLQHERGSE
SQ  DGPRNC
//
ID  O43463;
PN  Histone-lysine N-methyltransferase SUV39H1;
GN  SUV39H1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
DR  UNIPROT: O43463;
DR  UNIPROT: B2R6E8;
DR  UNIPROT: B4DST0;
DR  UNIPROT: Q53G60;
DR  UNIPROT: Q6FHK6;
DR  PDB: 3MTS;
DR  Pfam: PF00385;
DR  Pfam: PF05033;
DR  Pfam: PF00856;
DR  PROSITE: PS00598;
DR  PROSITE: PS50013;
DR  PROSITE: PS50868;
DR  PROSITE: PS50867;
DR  PROSITE: PS51579;
DR  PROSITE: PS50280;
DR  OMIM: 300254;
DR  DisGeNET: 6839;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126, ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776, ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871}.
DE  Reference Proteome: Yes;
DE  Interaction: O43159; IntAct: EBI-2008793,EBI-349968; Score: 0.52
DE  Interaction: P17987; IntAct: EBI-349968,EBI-356553; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-349968,EBI-357046; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-349968,EBI-355710; Score: 0.35
DE  Interaction: P45973; IntAct: EBI-349968,EBI-78219; Score: 0.92
DE  Interaction: P78371; IntAct: EBI-349968,EBI-357407; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-349968,EBI-356876; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-349968,EBI-356687; Score: 0.35
DE  Interaction: P83916; IntAct: EBI-349968,EBI-78129; Score: 0.67
DE  Interaction: P01106; IntAct: EBI-349968,EBI-447544; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-349968,EBI-356673; Score: 0.35
DE  Interaction: O75556; IntAct: EBI-349968,EBI-8830751; Score: 0.35
DE  Interaction: Q8IWI9; IntAct: EBI-349968,EBI-2815196; Score: 0.35
DE  Interaction: Q14839; IntAct: EBI-349968,EBI-372916; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-349968,EBI-356507; Score: 0.35
DE  Interaction: O60281; IntAct: EBI-349968,EBI-1224010; Score: 0.35
DE  Interaction: Q13185; IntAct: EBI-349968,EBI-78176; Score: 0.67
DE  Interaction: P60409; IntAct: EBI-10172290,EBI-349968; Score: 0.72
DE  Interaction: Q8NHQ1; IntAct: EBI-739624,EBI-349968; Score: 0.56
DE  Interaction: Q96ED9; IntAct: EBI-349968,EBI-743290; Score: 0.67
DE  Interaction: Q9BRK4; IntAct: EBI-741037,EBI-349968; Score: 0.72
DE  Interaction: V9HWG0; IntAct: EBI-349968,EBI-10183977; Score: 0.56
DE  Interaction: Q63HR2; IntAct: EBI-949753,EBI-349968; Score: 0.37
DE  Interaction: Q8TB24; IntAct: EBI-1570523,EBI-349968; Score: 0.37
DE  Interaction: P52732; IntAct: EBI-355697,EBI-349968; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-717058,EBI-349968; Score: 0.35
DE  Interaction: P24588; IntAct: EBI-703640,EBI-349968; Score: 0.35
DE  Interaction: P83917; IntAct: EBI-78119,EBI-349968; Score: 0.35
DE  Interaction: Q9UER7; IntAct: EBI-77321,EBI-349968; Score: 0.35
DE  Interaction: Q13371; IntAct: EBI-349968,EBI-5772890; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-349968,EBI-1642365; Score: 0.35
DE  Interaction: Q9NPA3; IntAct: EBI-349968,EBI-750096; Score: 0.35
DE  Interaction: Q9H582-2; IntAct: EBI-349968,EBI-21512288; Score: 0.35
DE  Interaction: Q9H0I2-2; IntAct: EBI-349968,EBI-20831259; Score: 0.35
DE  Interaction: Q9BTE3-2; IntAct: EBI-349968,EBI-9384556; Score: 0.35
DE  Interaction: Q96KQ7-2; IntAct: EBI-349968,EBI-744391; Score: 0.35
DE  Interaction: Q93008-1; IntAct: EBI-349968,EBI-10964523; Score: 0.35
DE  Interaction: Q70CQ2-2; IntAct: EBI-349968,EBI-21521617; Score: 0.35
DE  Interaction: Q6VMQ6-2; IntAct: EBI-349968,EBI-12070560; Score: 0.35
DE  Interaction: Q5TDH0-3; IntAct: EBI-349968,EBI-21659653; Score: 0.35
DE  Interaction: Q15047-3; IntAct: EBI-349968,EBI-11149962; Score: 0.35
DE  Interaction: Q15018; IntAct: EBI-349968,EBI-1056583; Score: 0.35
DE  Interaction: O60732; IntAct: EBI-349968,EBI-1188463; Score: 0.35
DE  Interaction: O00257; IntAct: EBI-349968,EBI-722425; Score: 0.44
DE  Interaction: Q92997; IntAct: EBI-739789,EBI-349968; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10171774,EBI-349968; Score: 0.56
DE  Interaction: Q8WV44; IntAct: EBI-725997,EBI-349968; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-710402,EBI-349968; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-527853,EBI-349968; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-11962468,EBI-349968; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-740727,EBI-349968; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-349968,EBI-750487; Score: 0.56
DE  Interaction: Q8N680; IntAct: EBI-2515601,EBI-349968; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-5916454,EBI-349968; Score: 0.56
DE  Interaction: Q96ED9-2; IntAct: EBI-10961706,EBI-349968; Score: 0.56
DE  Interaction: Q6TGC4; IntAct: EBI-10892722,EBI-349968; Score: 0.56
DE  Interaction: Q15156; IntAct: EBI-349968,EBI-867256; Score: 0.52
DE  Interaction: P29590; IntAct: EBI-295890,EBI-349968; Score: 0.40
DE  Interaction: P68432; IntAct: EBI-349968,EBI-79764; Score: 0.44
GO  GO:0005677;
GO  GO:0000775;
GO  GO:0000794;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0033553;
GO  GO:0003682;
GO  GO:0042054;
GO  GO:0046974;
GO  GO:0018024;
GO  GO:0047485;
GO  GO:0008757;
GO  GO:0000976;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0071456;
GO  GO:0006325;
GO  GO:0000183;
GO  GO:0036123;
GO  GO:0036124;
GO  GO:0034968;
GO  GO:0042754;
GO  GO:0000122;
GO  GO:0045892;
GO  GO:0048511;
GO  GO:0006364;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNL
SQ  KCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAF
SQ  VYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
SQ  IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH
SQ  FVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIEC
SQ  KCGTESCRKYLF
//
ID  Q9NQ40;
PN  Solute carrier family 52, riboflavin transporter, member 3;
GN  SLC52A3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Apical cell membrane {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:21512156, ECO:0000269|PubMed:24264046}; Multi-pass membrane protein {ECO:0000269|PubMed:20463145}. Cell membrane {ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:27702554}. [Isoform 1]: Cell membrane {ECO:0000269|PubMed:29428966}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:29428966}; Multi- pass membrane protein. Cytoplasm {ECO:0000269|PubMed:29428966}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:29428966}.
DR  UNIPROT: Q9NQ40;
DR  UNIPROT: A0A2I6BQ49;
DR  UNIPROT: A8K6P1;
DR  UNIPROT: K0A6P4;
DR  UNIPROT: Q5W1A0;
DR  UNIPROT: Q5W1A1;
DR  UNIPROT: Q8NCL7;
DR  UNIPROT: Q96GD5;
DR  Pfam: PF06237;
DR  OMIM: 211500;
DR  OMIM: 211530;
DR  OMIM: 613350;
DR  DisGeNET: 113278;
DE  Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism (PubMed:20463145, PubMed:22273710, PubMed:24264046, PubMed:27702554). Humans are unable to synthesize vitamin B2/riboflavin and must obtain it via intestinal absorption (PubMed:20463145). {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:24264046, ECO:0000269|PubMed:27702554, ECO:0000303|PubMed:20463145}.
DE  Disease: Brown-Vialetto-Van Laere syndrome 1 (BVVLS1) [MIM:211530]: A rare neurologic disorder characterized by sensorineural hearing loss and a variety of cranial nerve palsies, which develop over a relatively short period of time in a previously healthy individual. Sensorineural hearing loss may precede the neurological signs. The course is invariably progressive, but the rate of decline is variable within and between families. With disease evolution, long tract signs, lower motor neuron signs, cerebellar ataxia and lower cranial nerve (III-VI) palsies develop, giving rise to a complex picture resembling amyotrophic lateral sclerosis. Diaphragmatic weakness and respiratory compromise are some of the most distressing features, leading to recurrent chest infections and respiratory failure, which are often the cause of patients' demise. {ECO:0000269|PubMed:20206331, ECO:0000269|PubMed:20920669, ECO:0000269|PubMed:21110228, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:22633641, ECO:0000269|PubMed:22718020, ECO:0000269|PubMed:22824638, ECO:0000269|PubMed:27702554}. Note=The disease is caused by mutations affecting the gene represented in this entry. Fazio-Londe disease (FALOND) [MIM:211500]: A rare neurological disease characterized by progressive weakness of the muscles innervated by cranial nerves of the lower brain stem. It may present in childhood with severe neurological deterioration with hypotonia, respiratory insufficiency leading to premature death, or later in life with bulbar weakness which progresses to involve motor neurons throughout the neuroaxis. Clinical manifestations include dysarthria, dysphagia, facial weakness, tongue weakness, and fasciculations of the tongue and facial muscles. {ECO:0000269|PubMed:21110228}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0032217;
GO  GO:0034605;
GO  GO:0006771;
GO  GO:0032218;
GO  GO:0007605;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAFLMHLLVCVFGMGSWVTINGLWVELPLLVMELPEGWYLPSYLTVVIQLANIGPLLVTLLHHFRPSCLSEVPIIFTLLG
SQ  VGTVTCIIFAFLWNMTSWVLDGHHSIAFLVLTFFLALVDCTSSVTFLPFMSRLPTYYLTTFFVGEGLSGLLPALVALAQG
SQ  SGLTTCVNVTEISDSVPSPVPTRETDIAQGVPRALVSALPGMEAPLSHLESRYLPAHFSPLVFFLLLSIMMACCLVAFFV
SQ  LQRQPRCWEASVEDLLNDQVTLHSIRPREENDLGPAGTVDSSQGQGYLEEKAAPCCPAHLAFIYTLVAFVNALTNGMLPS
SQ  VQTYSCLSYGPVAYHLAATLSIVANPLASLVSMFLPNRSLLFLGVLSVLGTCFGGYNMAMAVMSPCPLLQGHWGGEVLIV
SQ  ASWVLFSGCLSYVKVMLGVVLRDLSRSALLWCGAAVQLGSLLGALLMFPLVNVLRLFSSADFCNLHCPA
//
ID  P49903;
PN  Selenide, water dikinase 1;
GN  SEPHS1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:20471958}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:20471958}; Peripheral membrane protein {ECO:0000305}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:20471958}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20471958}. [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:20471958}.
DR  UNIPROT: P49903;
DR  UNIPROT: B4DWK0;
DR  UNIPROT: D3DRS9;
DR  UNIPROT: D6PSQ9;
DR  UNIPROT: Q5T5U8;
DR  UNIPROT: Q5T5U9;
DR  UNIPROT: Q9BVT4;
DR  PDB: 3FD5;
DR  PDB: 3FD6;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DR  OMIM: 600902;
DR  DisGeNET: 22929;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}.
DE  Reference Proteome: Yes;
DE  Interaction: P32456; IntAct: EBI-714388,EBI-714091; Score: 0.37
DE  Interaction: Self; IntAct: EBI-714091,EBI-714091; Score: 0.80
DE  Interaction: Q9NRI5; IntAct: EBI-714091,EBI-529989; Score: 0.37
DE  Interaction: Q2TAL8; IntAct: EBI-714091,EBI-2798044; Score: 0.72
DE  Interaction: P24278; IntAct: EBI-714091,EBI-739899; Score: 0.78
DE  Interaction: Q6GPH4; IntAct: EBI-2815120,EBI-714091; Score: 0.56
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-714091; Score: 0.35
DE  Interaction: O60739; IntAct: EBI-714091,EBI-1043343; Score: 0.40
DE  Interaction: Q9UBN6; IntAct: EBI-714091,EBI-1044859; Score: 0.40
DE  Interaction: P21673; IntAct: EBI-714091,EBI-711613; Score: 0.37
DE  Interaction: Q8N357; IntAct: EBI-713484,EBI-714091; Score: 0.37
DE  Interaction: Q96ID5; IntAct: EBI-713314,EBI-714091; Score: 0.37
DE  Interaction: Q13432; IntAct: EBI-711260,EBI-714091; Score: 0.37
DE  Interaction: Q96E40; IntAct: EBI-722584,EBI-714091; Score: 0.37
DE  Interaction: Q8TF50; IntAct: EBI-11035148,EBI-714091; Score: 0.56
DE  Interaction: O95125; IntAct: EBI-751960,EBI-714091; Score: 0.56
DE  Interaction: Q6S9Z5; IntAct: EBI-17269964,EBI-714091; Score: 0.56
DE  Interaction: Q8N554; IntAct: EBI-750821,EBI-714091; Score: 0.56
DE  Interaction: Q9UPG8; IntAct: EBI-2876622,EBI-714091; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-714091; Score: 0.35
DE  Interaction: Q14774; IntAct: EBI-6678255,EBI-714091; Score: 0.35
DE  Interaction: Q9UKR5; IntAct: EBI-711490,EBI-714091; Score: 0.37
DE  Interaction: Q14194; IntAct: EBI-473101,EBI-714091; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0005525;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0006464;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
//
ID  O95271;
PN  Poly [ADP-ribose] polymerase tankyrase-1;
GN  TNKS;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:22864114}. Golgi apparatus membrane {ECO:0000269|PubMed:22864114}; Peripheral membrane protein {ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523501}. Chromosome, telomere {ECO:0000305|PubMed:9822378}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16076287}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (PubMed:22864114). A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres (PubMed:10523501). During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1 (PubMed:12768206). Localizes to spindle poles at mitosis onset via interaction with NUMA1 (PubMed:12080061). {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:22864114}.
DR  UNIPROT: O95271;
DR  UNIPROT: O95272;
DR  UNIPROT: Q4G0F2;
DR  PDB: 2RF5;
DR  PDB: 3UDD;
DR  PDB: 3UH2;
DR  PDB: 3UH4;
DR  PDB: 4DVI;
DR  PDB: 4I9I;
DR  PDB: 4K4E;
DR  PDB: 4K4F;
DR  PDB: 4KRS;
DR  PDB: 4LI6;
DR  PDB: 4LI7;
DR  PDB: 4LI8;
DR  PDB: 4MSG;
DR  PDB: 4MSK;
DR  PDB: 4MT9;
DR  PDB: 4N3R;
DR  PDB: 4N4V;
DR  PDB: 4OA7;
DR  PDB: 4TOR;
DR  PDB: 4TOS;
DR  PDB: 4U6A;
DR  PDB: 4UUH;
DR  PDB: 4UW1;
DR  PDB: 4W5S;
DR  PDB: 4W6E;
DR  PDB: 5EBT;
DR  PDB: 5ECE;
DR  PDB: 5ETY;
DR  PDB: 5GP7;
DR  PDB: 5JHQ;
DR  PDB: 5JTI;
DR  PDB: 5JU5;
DR  PDB: 5KNI;
DR  PDB: 6QXU;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  Pfam: PF13606;
DR  Pfam: PF00644;
DR  Pfam: PF07647;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51059;
DR  PROSITE: PS50105;
DR  OMIM: 603303;
DR  DisGeNET: 8658;
DE  Function: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379). Acts as an activator of the Wnt signaling pathway by mediating poly- ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation (PubMed:19759537, PubMed:21478859). Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859). Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length (PubMed:11739745). Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI (PubMed:22864114). May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles (PubMed:10988299). May be involved in spindle pole assembly through PARsylation of NUMA1 (PubMed:16076287). Stimulates 26S proteasome activity (PubMed:23622245). {ECO:0000269|PubMed:10988299, ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:22864114, ECO:0000269|PubMed:23622245, ECO:0000269|PubMed:25043379}.
DE  Reference Proteome: Yes;
DE  Interaction: O60239; IntAct: EBI-1105254,EBI-624860; Score: 0.55
DE  Interaction: Q9NRI5; IntAct: EBI-1105254,EBI-529989; Score: 0.55
DE  Interaction: P21709; IntAct: EBI-1105254,EBI-968453; Score: 0.37
DE  Interaction: Q9NWT6; IntAct: EBI-745632,EBI-1105254; Score: 0.78
DE  Interaction: P62826; IntAct: EBI-1105254,EBI-286642; Score: 0.40
DE  Interaction: Q9NWV8; IntAct: EBI-745725,EBI-1105254; Score: 0.56
DE  Interaction: O95235; IntAct: EBI-2551319,EBI-1105254; Score: 0.35
DE  Interaction: Q3UES3; IntAct: EBI-11025893,EBI-1105254; Score: 0.35
DE  Interaction: P80314; IntAct: EBI-772351,EBI-1105254; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-710997,EBI-1105254; Score: 0.60
DE  Interaction: O60232; IntAct: EBI-741415,EBI-1105254; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-2130320,EBI-1105254; Score: 0.35
DE  Interaction: Q9H201-2; IntAct: EBI-21644004,EBI-1105254; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-1104799,EBI-1105254; Score: 0.35
DE  Interaction: Q9BS91; IntAct: EBI-18915901,EBI-1105254; Score: 0.35
DE  Interaction: Q8N6W0; IntAct: EBI-12139335,EBI-1105254; Score: 0.35
DE  Interaction: Q7L775; IntAct: EBI-6255981,EBI-1105254; Score: 0.56
DE  Interaction: Q06649; IntAct: EBI-1105254,EBI-5323518; Score: 0.40
DE  Interaction: O15084; IntAct: EBI-359567,EBI-1105254; Score: 0.37
DE  Interaction: A0A384L0P2; IntAct: EBI-1105254,EBI-2841116; Score: 0.37
DE  Interaction: Q8TER5-1; IntAct: EBI-25399492,EBI-1105254; Score: 0.35
DE  Interaction: Q86WJ1-2; IntAct: EBI-21569730,EBI-1105254; Score: 0.35
DE  Interaction: P54274-2; IntAct: EBI-711018,EBI-1105254; Score: 0.35
DE  Interaction: O75298-3; IntAct: EBI-21508625,EBI-1105254; Score: 0.35
DE  Interaction: O60547; IntAct: EBI-746373,EBI-1105254; Score: 0.35
DE  Interaction: P12956; IntAct: EBI-353208,EBI-1105254; Score: 0.40
DE  Interaction: P56279; IntAct: EBI-1105254,EBI-749995; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-1105254,EBI-727004; Score: 0.56
DE  Interaction: Q9Y530; IntAct: EBI-8502288,EBI-1105254; Score: 0.56
DE  Interaction: Q9NX46; IntAct: EBI-1105254,EBI-718580; Score: 0.56
DE  Interaction: Q8TF42; IntAct: EBI-1105254,EBI-1380492; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-1105254; Score: 0.35
DE  Interaction: O75367-2; IntAct: EBI-1105254,EBI-6249599; Score: 0.52
DE  Interaction: O75367; IntAct: EBI-1105254,EBI-2868511; Score: 0.40
DE  Interaction: A4D1S0; IntAct: EBI-21511322,EBI-1105254; Score: 0.35
DE  Interaction: Q96CW1-2; IntAct: EBI-10965256,EBI-1105254; Score: 0.35
DE  Interaction: Q9H2G9; IntAct: EBI-2548012,EBI-1105254; Score: 0.35
DE  Interaction: Q9BSI4-2; IntAct: EBI-11057768,EBI-1105254; Score: 0.35
DE  Interaction: Q7L8J4; IntAct: EBI-747389,EBI-1105254; Score: 0.35
DE  Interaction: Q2T9K0-6; IntAct: EBI-21768440,EBI-1105254; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-1046087,EBI-1105254; Score: 0.35
DE  Interaction: Q6P1L5; IntAct: EBI-3893327,EBI-1105254; Score: 0.35
DE  Interaction: Q9UPT6; IntAct: EBI-717887,EBI-1105254; Score: 0.35
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0097431;
GO  GO:0016604;
GO  GO:0000784;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000242;
GO  GO:0042393;
GO  GO:0003950;
GO  GO:1990404;
GO  GO:0008270;
GO  GO:0051301;
GO  GO:0031670;
GO  GO:0007052;
GO  GO:0051028;
GO  GO:1904908;
GO  GO:1904357;
GO  GO:1904743;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0090263;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0045944;
GO  GO:0006471;
GO  GO:0070213;
GO  GO:0070198;
GO  GO:0070212;
GO  GO:0000209;
GO  GO:0015031;
GO  GO:0032210;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:22864114};
SQ  MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRS
SQ  PDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVS
SQ  STAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGA
SQ  NVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALD
SQ  LADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDK
SQ  GGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPEL
SQ  RERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMT
SQ  PLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILS
SQ  ESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVP
SQ  LHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDL
SQ  LRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASY
SQ  GHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEA
SQ  LPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGL
SQ  EHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQS
SQ  VEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDER
SQ  HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIG
SQ  RPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
//
ID  Q9Y7Z5;
PN  Tetra-spanning protein 1;
GN  tts1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: Q9Y7Z5;
DR  Pfam: PF03661;
DE  Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator. {ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:1990809;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0006998;
GO  GO:0071789;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPKQRVVKPLKERVLPVVKNTQFVWFSGQVIVLISSVLYALQAIPFRSAPPFLFKSAAFGAIVAYAIVLYKTYSPNLTS
SQ  RASWNKHFFARLMLDDNVQYFILALSMLIDRPILFSLAPYAIYATFHISTYLRSVLLPAIYPNISDAKTASYASRVSNLL
SQ  NQYTRSQFQPAMQLVASLETFLLFRLFFGVFLRKNSISRLVGYIFFLRMRYTNSHFTRASIKAVSLRMDRLVADNRVPPV
SQ  IKNAWHTFKTYVSKFGASPVGTAQSRPTASSSTTAPSST
//
ID  Q99523;
PN  Sortilin;
GN  SORT1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin.
DR  UNIPROT: Q99523;
DR  UNIPROT: B4DWI3;
DR  UNIPROT: C0JYZ0;
DR  UNIPROT: Q8IZ49;
DR  PDB: 3F6K;
DR  PDB: 3G2U;
DR  PDB: 3G2V;
DR  PDB: 4MSL;
DR  PDB: 4N7E;
DR  PDB: 4PO7;
DR  PDB: 5MRH;
DR  PDB: 5MRI;
DR  PDB: 6EHO;
DR  Pfam: PF15902;
DR  Pfam: PF15901;
DR  OMIM: 602458;
DR  OMIM: 613589;
DR  DisGeNET: 6272;
DE  Function: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10085125, ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:12209882, ECO:0000269|PubMed:12598608, ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763, ECO:0000269|PubMed:15313463, ECO:0000269|PubMed:15930396, ECO:0000269|PubMed:15987945}.
DE  Disease: Note=A common polymorphism located in a non-coding region between CELSR2 and PSRC1 alters a CEBP transcription factor binding site and is responsible for changes in hepatic expression of SORT1. Altered SORT1 expression in liver affects low density lipoprotein cholesterol levels in plasma and is associated with susceptibility to myocardial infarction.
DE  Reference Proteome: Yes;
DE  Interaction: Q86WG5; IntAct: EBI-1057058,EBI-2683289; Score: 0.35
DE  Interaction: Q8NC56; IntAct: EBI-1057058,EBI-6149955; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-1057058; Score: 0.35
DE  Interaction: Q8IVD9; IntAct: EBI-744342,EBI-1057058; Score: 0.35
DE  Interaction: Q8IXK0-2; IntAct: EBI-1057058,EBI-3951965; Score: 0.35
DE  Interaction: Q7Z7F7; IntAct: EBI-1057058,EBI-7825445; Score: 0.35
DE  Interaction: O43543; IntAct: EBI-1057058,EBI-3918457; Score: 0.35
DE  Interaction: Q8IZY2; IntAct: EBI-1057058,EBI-2838910; Score: 0.35
DE  Interaction: Q6KCM7-3; IntAct: EBI-1057058,EBI-11135015; Score: 0.35
DE  Interaction: Q8N8A6; IntAct: EBI-1057058,EBI-3893408; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-1057058,EBI-2949715; Score: 0.35
DE  Interaction: Q6PKC3-2; IntAct: EBI-1057058,EBI-11072463; Score: 0.35
DE  Interaction: J3KP15; IntAct: EBI-1057058,EBI-11030773; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-1057058,EBI-1103245; Score: 0.35
DE  Interaction: Q8IXQ6; IntAct: EBI-1057058,EBI-11154653; Score: 0.35
DE  Interaction: Q86YS7; IntAct: EBI-1057058,EBI-1051086; Score: 0.35
DE  Interaction: Q9H6R4-4; IntAct: EBI-1057058,EBI-10307896; Score: 0.35
DE  Interaction: G5E9A6; IntAct: EBI-1057058,EBI-10976685; Score: 0.35
DE  Interaction: Q9P0T7; IntAct: EBI-1057058,EBI-723976; Score: 0.35
DE  Interaction: O43504; IntAct: EBI-1057058,EBI-713382; Score: 0.35
DE  Interaction: H3BS42; IntAct: EBI-1057058,EBI-10984149; Score: 0.35
DE  Interaction: Q96AY2; IntAct: EBI-1057058,EBI-2370825; Score: 0.35
DE  Interaction: O43674; IntAct: EBI-1057058,EBI-1246293; Score: 0.35
DE  Interaction: Q9UHR4; IntAct: EBI-1057058,EBI-2483278; Score: 0.35
DE  Interaction: Q9H2D6-5; IntAct: EBI-1057058,EBI-1023227; Score: 0.35
DE  Interaction: Q9BXF6; IntAct: EBI-1057058,EBI-1387068; Score: 0.35
DE  Interaction: H3BNT4; IntAct: EBI-1057058,EBI-11060136; Score: 0.35
DE  Interaction: P78368; IntAct: EBI-1057058,EBI-748380; Score: 0.35
DE  Interaction: Q6T4R5-2; IntAct: EBI-1057058,EBI-11152427; Score: 0.35
DE  Interaction: Q9Y2H6-2; IntAct: EBI-1057058,EBI-10968529; Score: 0.35
DE  Interaction: Q8IWU2; IntAct: EBI-1057058,EBI-2008933; Score: 0.35
DE  Interaction: Q86WP2-2; IntAct: EBI-1057058,EBI-10967055; Score: 0.35
DE  Interaction: Q9Y6X9; IntAct: EBI-1057058,EBI-11125700; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-1057058,EBI-372051; Score: 0.35
DE  Interaction: Q9BZF9; IntAct: EBI-1057058,EBI-350510; Score: 0.35
DE  Interaction: Q7Z7K6; IntAct: EBI-1057058,EBI-1210604; Score: 0.35
DE  Interaction: P12882; IntAct: EBI-1057058,EBI-366238; Score: 0.35
DE  Interaction: Q8N8R5; IntAct: EBI-1057058,EBI-4407391; Score: 0.35
DE  Interaction: G5E9S8; IntAct: EBI-1057058,EBI-11092590; Score: 0.35
DE  Interaction: P98170; IntAct: EBI-1057058,EBI-517127; Score: 0.35
DE  Interaction: O94782; IntAct: EBI-1057058,EBI-2513396; Score: 0.35
DE  Interaction: Q9H792; IntAct: EBI-1057058,EBI-2609701; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-1057058,EBI-700771; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-1057058,EBI-444308; Score: 0.35
DE  Interaction: Q9NYU1; IntAct: EBI-1057058,EBI-1054215; Score: 0.35
DE  Interaction: E9PRI1; IntAct: EBI-1057058,EBI-11054721; Score: 0.35
DE  Interaction: O00308; IntAct: EBI-1057058,EBI-743923; Score: 0.35
DE  Interaction: Q9NP74; IntAct: EBI-1057058,EBI-2811699; Score: 0.35
DE  Interaction: O60506-3; IntAct: EBI-1057058,EBI-5455760; Score: 0.35
DE  Interaction: Q16222-3; IntAct: EBI-1057058,EBI-11038788; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-1057058,EBI-2878099; Score: 0.35
DE  Interaction: O15020; IntAct: EBI-1057058,EBI-308449; Score: 0.35
DE  Interaction: Q92900-2; IntAct: EBI-1057058,EBI-373492; Score: 0.35
DE  Interaction: Q8WW22; IntAct: EBI-1057058,EBI-2555157; Score: 0.35
DE  Interaction: Q15646; IntAct: EBI-1057058,EBI-3918068; Score: 0.35
DE  Interaction: Q8TED0; IntAct: EBI-1057058,EBI-1048301; Score: 0.35
DE  Interaction: Q6PCT2-3; IntAct: EBI-1057058,EBI-10981750; Score: 0.35
DE  Interaction: Q13867; IntAct: EBI-1057058,EBI-718504; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-1057058,EBI-350864; Score: 0.35
DE  Interaction: G3V5I9; IntAct: EBI-1057058,EBI-11154663; Score: 0.35
DE  Interaction: P00738; IntAct: EBI-1057058,EBI-1220767; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-1057058,EBI-356811; Score: 0.35
DE  Interaction: Q9Y2L1; IntAct: EBI-1057058,EBI-373539; Score: 0.35
DE  Interaction: Q8TDN6; IntAct: EBI-1057058,EBI-1052326; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-1057058,EBI-1762349; Score: 0.35
DE  Interaction: H0YAJ5; IntAct: EBI-1057058,EBI-11108103; Score: 0.35
DE  Interaction: Q96MF7; IntAct: EBI-1057058,EBI-2557388; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-1057058,EBI-354065; Score: 0.35
DE  Interaction: Q9Y4E8; IntAct: EBI-1057058,EBI-1043104; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-1057058,EBI-356273; Score: 0.35
DE  Interaction: A7KAX9-2; IntAct: EBI-1057058,EBI-11016522; Score: 0.35
DE  Interaction: Q96A35; IntAct: EBI-1057058,EBI-1045743; Score: 0.35
DE  Interaction: Q9NXA8; IntAct: EBI-1057058,EBI-6556144; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-1057058,EBI-2807346; Score: 0.35
DE  Interaction: P42680; IntAct: EBI-1057058,EBI-1383480; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-1057058,EBI-355782; Score: 0.35
DE  Interaction: Q8NCE0-3; IntAct: EBI-1057058,EBI-11050086; Score: 0.35
DE  Interaction: P07949; IntAct: EBI-1057058,EBI-2480756; Score: 0.35
DE  Interaction: Q6IN84; IntAct: EBI-1057058,EBI-5454865; Score: 0.35
DE  Interaction: Q13428-4; IntAct: EBI-1057058,EBI-11053935; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-1057058,EBI-358398; Score: 0.35
DE  Interaction: C9J6P4; IntAct: EBI-1057058,EBI-10969973; Score: 0.35
DE  Interaction: Q659A1; IntAct: EBI-1057058,EBI-4322746; Score: 0.35
DE  Interaction: Q6L8Q7; IntAct: EBI-1057058,EBI-2515865; Score: 0.35
DE  Interaction: Q14146; IntAct: EBI-1057058,EBI-9996029; Score: 0.35
DE  Interaction: Q14232; IntAct: EBI-1057058,EBI-491065; Score: 0.35
DE  Interaction: P00966; IntAct: EBI-1057058,EBI-536842; Score: 0.35
DE  Interaction: J3KNB8; IntAct: EBI-1057058,EBI-11020906; Score: 0.35
DE  Interaction: A1X283; IntAct: EBI-1057058,EBI-2481776; Score: 0.35
DE  Interaction: Q9Y2U9; IntAct: EBI-1057058,EBI-715326; Score: 0.35
DE  Interaction: P51153; IntAct: EBI-1057058,EBI-1780121; Score: 0.35
DE  Interaction: Q53SF7-4; IntAct: EBI-1057058,EBI-10961669; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-1057058,EBI-1055805; Score: 0.35
DE  Interaction: Q01970; IntAct: EBI-1057058,EBI-4289548; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-1057058,EBI-395506; Score: 0.35
DE  Interaction: Q92733; IntAct: EBI-1057058,EBI-4397741; Score: 0.35
DE  Interaction: Q8IYD8; IntAct: EBI-1057058,EBI-3957237; Score: 0.35
DE  Interaction: P13533; IntAct: EBI-1057058,EBI-1048066; Score: 0.35
DE  Interaction: Q6UVK1; IntAct: EBI-1057058,EBI-5327894; Score: 0.35
DE  Interaction: Q9UHL9-2; IntAct: EBI-1057058,EBI-11152432; Score: 0.35
DE  Interaction: P42356; IntAct: EBI-1057058,EBI-723050; Score: 0.35
DE  Interaction: Q5JRA6; IntAct: EBI-1057058,EBI-2291868; Score: 0.35
DE  Interaction: Q71F56; IntAct: EBI-1057058,EBI-394435; Score: 0.35
DE  Interaction: P54577; IntAct: EBI-1057058,EBI-1048893; Score: 0.35
DE  Interaction: Q8TE77; IntAct: EBI-1057058,EBI-8743776; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-1057058,EBI-1384320; Score: 0.35
DE  Interaction: Q8NFA0; IntAct: EBI-1057058,EBI-2511075; Score: 0.35
DE  Interaction: Q9Y490; IntAct: EBI-1057058,EBI-2462036; Score: 0.35
DE  Interaction: Q9UMF0; IntAct: EBI-1057058,EBI-6398041; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-1057058,EBI-356319; Score: 0.35
DE  Interaction: Q7Z2E3-9; IntAct: EBI-1057058,EBI-11153339; Score: 0.35
DE  Interaction: Q9NQY0-2; IntAct: EBI-1057058,EBI-11019047; Score: 0.35
DE  Interaction: Q9NUQ7; IntAct: EBI-1057058,EBI-11153325; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-1057058,EBI-375096; Score: 0.56
DE  Interaction: Q13488; IntAct: EBI-1057058,EBI-3914669; Score: 0.35
DE  Interaction: Q96A73-3; IntAct: EBI-1057058,EBI-11040309; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-1057058,EBI-714168; Score: 0.35
DE  Interaction: Q6PL45-2; IntAct: EBI-1057058,EBI-12244618; Score: 0.56
DE  Interaction: Q96K78; IntAct: EBI-1057058,EBI-10290200; Score: 0.56
DE  Interaction: P05231; IntAct: EBI-720533,EBI-1057058; Score: 0.57
DE  Interaction: P01580; IntAct: EBI-25396641,EBI-1057058; Score: 0.44
DE  Interaction: Self; IntAct: EBI-1057058,EBI-21474780; Score: 0.68
DE  Interaction: Q9JLC4; IntAct: EBI-25300487,EBI-1057058; Score: 0.54
DE  Interaction: Q8WY21; IntAct: EBI-21198627,EBI-1057058; Score: 0.54
DE  Interaction: P30990; IntAct: EBI-1057058,EBI-6655799; Score: 0.61
DE  Interaction: Q8WY21-3; IntAct: EBI-25301114,EBI-1057058; Score: 0.40
DE  Interaction: Q8WY21-1; IntAct: EBI-25301175,EBI-1057058; Score: 0.53
DE  Interaction: P06280; IntAct: EBI-2513305,EBI-1057058; Score: 0.59
DE  Interaction: P01266; IntAct: EBI-2800425,EBI-1057058; Score: 0.54
DE  Interaction: P06882; IntAct: EBI-1549657,EBI-1057058; Score: 0.54
DE  Interaction: P20068; IntAct: EBI-1057058,EBI-25406762; Score: 0.40
DE  Interaction: P30533; IntAct: EBI-1057058,EBI-715927; Score: 0.70
DE  Interaction: P01267; IntAct: EBI-25408016,EBI-1057058; Score: 0.40
DE  Interaction: Q92520; IntAct: EBI-1057058,EBI-2876774; Score: 0.56
DE  Interaction: O95183; IntAct: EBI-1057058,EBI-10191195; Score: 0.56
DE  Interaction: P02787; IntAct: EBI-1057058,EBI-714319; Score: 0.56
DE  Interaction: P23560-2; IntAct: EBI-1057058,EBI-12275524; Score: 0.56
DE  Interaction: Q8TBE1; IntAct: EBI-1057058,EBI-12208021; Score: 0.56
DE  Interaction: Q20MH8; IntAct: EBI-12576433,EBI-1057058; Score: 0.35
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030140;
GO  GO:0019899;
GO  GO:0048406;
GO  GO:0010465;
GO  GO:0030379;
GO  GO:0006897;
GO  GO:0008333;
GO  GO:0032509;
GO  GO:0008625;
GO  GO:0007186;
GO  GO:0046323;
GO  GO:0006895;
GO  GO:0007275;
GO  GO:0014902;
GO  GO:0045599;
GO  GO:0051005;
GO  GO:0007218;
GO  GO:0048011;
GO  GO:0001503;
GO  GO:0048227;
GO  GO:1904037;
GO  GO:0006892;
GO  GO:0006622;
GO  GO:0010468;
GO  GO:0032868;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGLRAAAAGGAFPRGGRWRRSAP
SQ  GEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDL
SQ  INNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLW
SQ  VSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMAD
SQ  KDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGG
SQ  ETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLS
SQ  EPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCWQTY
SQ  TFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKE
SQ  QFLRLRKSSVCQNGRDYVVTKQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPG
SQ  DKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAE
SQ  ANGVDGVDALDTASHTNKSGYHDDSDEDLLE
//
ID  F4I316;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: F4I316;
DR  UNIPROT: O23133;
DR  UNIPROT: Q8GX04;
DR  UNIPROT: Q8H7G6;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0043621;
GO  GO:0042742;
GO  GO:0009409;
GO  GO:0009651;
GO  GO:0009414;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPL
SQ  SLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINN
SQ  TGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNS
SQ  RNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTI
SQ  KIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGV
SQ  DAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSE
SQ  PVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQ
SQ  EGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTG
SQ  SGAWLLLLISSTFIMFVLSL
//
ID  P53895;
PN  Protein ASI2;
GN  ASI2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P53895;
DR  UNIPROT: D6W124;
DE  Function: Negative regulator of SPS-sensor signaling. Together with ASI1 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor- regulated genes in the absence of inducing signals. {ECO:0000269|PubMed:17085444}.
DE  Reference Proteome: Yes;
DE  Interaction: P25294; IntAct: EBI-17244,EBI-28975; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-28975,EBI-8603; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-28975,EBI-5127; Score: 0.40
DE  Interaction: P53983; IntAct: EBI-28603,EBI-28975; Score: 0.46
DE  Interaction: P54074; IntAct: EBI-27241,EBI-28975; Score: 0.46
DE  Interaction: P38074; IntAct: EBI-28975,EBI-8394; Score: 0.37
GO  GO:0097658;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0071230;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARPQNHRRSNWTERDDNDDYLFQRFLEESETRHSREPSPVTEQSQQELQQDVQQAIDGIFNSLRRNMSSTSNINRAANM
SQ  DATTNGNGGINADTIRATNANTADSPFTARQQSPLRTFLRNLFILDYFIGLILFPFSVYNILRSGFNSMTFSENDFIIEI
SQ  VGYWKFAKIFGSGGTTLIAYKDTGKLGLLGKFHNIIVFYSSPVIKHIMKSRDGNEPNLNWIRLMFAKAFELFVKVSTILI
SQ  YLAYGVSGTVYMVTAGFFFVLCLLFTVIRRYKGVHRMLVSQRITGPGVF
//
ID  O13898;
PN  Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
GN  ogm1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. Nucleus membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}.
DR  UNIPROT: O13898;
DR  Pfam: PF02815;
DR  Pfam: PF02366;
DR  Pfam: PF16192;
DR  PROSITE: PS50919;
DE  Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1. {ECO:0000269|PubMed:15809069, ECO:0000269|PubMed:15948957}.
DE  Reference Proteome: Yes;
GO  GO:0097582;
GO  GO:0012505;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004169;
GO  GO:0000032;
GO  GO:0044845;
GO  GO:0031505;
GO  GO:0035269;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMD
SQ  VYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIF
SQ  DNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLW
SQ  NLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVT
SQ  IRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHK
SQ  PIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQRE
SQ  VTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFY
SQ  EQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHY
SQ  LPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDN
SQ  LSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASE
SQ  AAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQ
SQ  EENVAESAQARVE
//
ID  O13681;
PN  Integral inner nuclear membrane protein ima1;
GN  IMA1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:18692466}.
DR  UNIPROT: O13681;
DR  Pfam: PF09779;
DE  Function: Inner nuclear membrane protein that specifically binds to heterochromatic regions and promotes the tethering of centromeric DNA to the SUN-KASH complex. Couples centromeres to the nuclear envelope, thus contributing to their association with the microtubule organizing center attachment site and to the positioning of the nucleus at the cell center by microtubules. {ECO:0000269|PubMed:18692466}.
DE  Reference Proteome: Yes;
GO  GO:0034506;
GO  GO:0016021;
GO  GO:0034992;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0071765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPF
SQ  YAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDAND
SQ  YEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLL
SQ  DGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFL
SQ  LRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISIL
SQ  NNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSK
SQ  FSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNR
SQ  RNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA
//
ID  Q54TL0;
PN  Kinesin-related protein 7;
GN  kif7;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:9693369}; Single-pass membrane protein {ECO:0000269|PubMed:9693369}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9693369}.
DR  UNIPROT: Q54TL0;
DR  UNIPROT: Q94463;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DE  Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. May be involved in cell motility or cell differentiation during prestalk formation. {ECO:0000269|PubMed:9693369}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0008574;
GO  GO:0016887;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0030705;
GO  GO:0007018;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESPVVEGNSGEVATPTLPQPPTPVSSNIRVVCRVRPLTELEKGRNEHSIVHFFDSKSISIRANGPQFTFDRIFGYQETQ
SQ  SQIFEDVAEPIVNDFLDGYHGTIIAYGQTASGKTFTMVGDPDSHGIIPRVIESIFVGISKMREKDTSLSLAFCLKISALE
SQ  LYNEKLYDLYDASKSNLNIREHKQNGIYVEGISEIVITSIEEAYNFLNISNNNRAIASTKMSAASSRSHSVLMIELSQQN
SQ  LSMESSKISKLFLVDLAGSERAHKTGAEGDRMQEAKNINLSLSALGKVINALTCGANYVPYRDSKLTRVLQDSLGGNSKT
SQ  SLIINCSPSNNNEHETITTLQFGTRAKTIKNQPKINKKITYHELELFIIKLAKDLEKSRKECEEITRSKNLEINNLLIQL
SQ  ENNQKMVVESNQKLELLNSQISSNHSFDNTFKEIENTCENSKIIFDDLNDHINNNNNVDENNNTNNNDNNNNDNNNNNQY
SQ  QEESNQYQQENNQKDGDQNNSSFDSIKVEDLRDLDDEPDIEDIILNSTLGNISDDDDDDDDHHSNNNNVDDNNNGEINND
SQ  SDGYLNRSLKDIKIPEISDLNDHNINNNNNNNNNINNDNNSNSGGLRVSTSYITSSPNLSPSKSMDVNNSPPLFSYFKTK
SQ  DFPPSSDENDKFFNDLIAKGENEQQQQQQQHNDDDEDIKSTTSNATTTTITTIDMNASHPSGIDDPIEFTIIKSDKTITS
SQ  TIERETIQPSSLSNSTSLLDIETVESSTLPAPPPVTTTTTLTTVTTTKLTKTTNIPSNTNDINSIDDFGFSKIEEEGSSS
SQ  NRKPNDTAILSFGDDDDEENEDNENEDVIVDSDEDTHSGKNNLLNTFKNDHHRGDFGATPTKSIFNKNGNITIKEFETPQ
SQ  QQQQQQQQQQQQQQQQQQQQQPLILQTTSTNPTIISIKSNKEPSPSSSTTTSIKKKNFNKRRSWIIFTIILTITLVSSSL
SQ  LCLYLPEYKERLVQRRGYLNKLGIYSDYPTNEKISLAQHNQISLAKELYGGNSKQYYDEMSSFNTAYNHLIEMNHLETAV
SQ  SKIFGSAIDLRFSGDDVINSIECKRAIHKLKTNNYVNGDLDQQQQQHNYITKIDQLSEQSKEQNQLIENFKLDLKNKTSE
SQ  IEKLEKEIKQKDNKIKEKEEKIELIESRVLNEEKGGEKVLEDQIISLRNDKNTLSTQILNLEGDKKSLGVLVIKLNSDKT
SQ  EIQNEVKELKRKVQELEDAPIALIPNPFVKWVKSFYVEKKSWFVENIYKIWNWFK
//
ID  F4KHD8;
PN  Nuclear pore complex protein GP210;
GN  GB210;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4KHD8;
DR  UNIPROT: Q9FI62;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVSFCFFFLLLLLSAGESSSQLVSGPHITDVNILLPPKMKNPVEYRLQGSDGCFKWSWDHHDILSVTPEFNSSSHCST
SQ  SARLRSISPYSGRKETAVYATDIQTGMVIRCKVFIDNFSRIQIFHNSIKLDLDGLSMLRVRAFDNEDNEFSSLVGLQFIW
SQ  KLMPESGGSTHHLAHVPLKESPLTDCGGLCGYLDIQKKLEDSGVFADLFVVKGTKIGHEKVSVHLLEAPLTHIADEIVLT
SQ  VAEAMSLEPRSPVYVLMGASFGYTLKVMRGNVPQAVDLPSPHHRWSVLNSSVAQVDSLIGLTKALSLGVTTVVVEDTRVA
SQ  GHIQGSSINVVTPDTLILYISPWSMSGDLITESKPFPSSMHWYVVSGRQYLIQMKIFSGRPDAHEIYITETDDIKLYGKD
SQ  SDYWKIVSLPDELSSEYGQRNSRILNAISPGLGELTSTLTYFSGHQESKEVLKVVQEIRVCEKVQFTLNSEDDTPKVLLP
SQ  WTPAVYQEMELIVTGGCAKASSDYKWFTSDISILSVSAYGIIQAKRPGIATVKVVSTFDSQNFDEVIVEVSIPSSMVMLQ
SQ  NFPVETVVGSHLKAAVTMKALNGATFSRCDAFNSLIKWKTGSESFVIVNATSEMMMLDELRSMDSSPPCSRASIYTASTG
SQ  RTVLQATLAKEFHYFDKSLSESIDLKATLTIGAYLPLSVRQDSDGNHHGGYWFDKAQEETDFGVSKLYLVPGTYVDVMLL
SQ  GGPERWDDNVEFTETVKTLYEDEEDLTSRVNVHHEVDRRANMYRISCQKLGSYKLVFLRGNLLGIDHPVPAVAEALLSVH
SQ  CSLPSSVVLIVDEPVNKLDVIRAASQADRAPGRLRVTPVTVANGQIIRVAAVGISEFGEAFSNSSTLSLRWELTSCNNLA
SQ  YWDDDYNSKMTKSGWERFLALRNESGLCTVRATVSGIDYSFKSQYSTLLPQGSESTLTDAVRLQLVSTLRVTPEFNLVFF
SQ  NPNAKVNLSMTGGSCLWEAVVNNSRVAEVIRPPSGLQCSQMMLSPKGLGTTIVTVYDIGVSPPLSALALIKVADVDWIKI
SQ  ASGDEISIMEGSTHSIDLLTGIDDGMTFDSSQYSLMDIMVHIEDDLVEHVTVDEDSLSVGEHVATSSFKIAARRLGITTL
SQ  YVSARQQSGGKVLSQTIKVEVYSPPRLHPQGIFLVPGASYVLTIEGGPTMNVSVDYTTVDNEVAKIEKSGRLYATSPGNT
SQ  TIYATIYGSEGAVICQAIGNAEVGLPATAMLVAQSDTVAVGHEMPVSPSFPEGDLLSFYELCSAYKWTIEDEKVLIFIAS
SQ  SINVEENAGFVNVVQGRSAGKTRVTIAFSCDFVSPGLYSESRTYEASMILSVVPDLPLSLGAPMTWVLPPFYTSSGLLPS
SQ  SSEPQKHRDGQSHRGNIVYSILKDCSSRADFERDTISINGGSVKTTDSNNVACIQAKDRTSGRIEIAACVRVAEVAQIRM
SQ  KSEGIPFHVIDLAVGGELELPINYYDTLGIPFLEAHGVTTYNVETNHRDVVFIKTVNDQPSAYIKGIKHGKALIRVSIGD
SQ  NLRKSDYVLVSVGAHIFPQNPVIHTGNLLNFSITGADNEVTGQWFTSNRSVISVNVASGQAKAISQGSTHVTFKGHGLKL
SQ  QTKVTVLFGNTIYVDSPGETLTNVHVPAEGYKFPVKFRENKFAVTEHGNKATFNCQVDPPFIGYTKPWMDLDTGNTYCLF
SQ  FPYSPEHLVHSMSITKDMKPHVSFSVDASLKEARRVSGSASALLIGGFSVTGPDKLNINPDSNTTIISLVGNTDVQIHCR
SQ  NKGRLSISLIKRDDFGIAGHAQYKVNVLRSEQFTDRIIITLPATGQIVEIDVCYDTGESLVASSKDGYSVLLKILWGVLV
SQ  LVVSVIILMKVIDRQVPTGATGTATYSGNAAQGTPERRSGTVIYHEESPRTPSPFMEYVKRTVDETPYYRREGRRRFNPQ
SQ  NTM
//
ID  Q9U3V9;
PN  Protein xmas-2;
GN  xmas;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:28472469}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28472469}.
DR  UNIPROT: Q9U3V9;
DR  UNIPROT: Q8IR02;
DR  UNIPROT: Q8MQS3;
DR  UNIPROT: Q9VX76;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DR  PROSITE: PS50102;
DE  Function: Required for spermatogenesis, oogenesis and embryogenesis.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0007275;
GO  GO:0048477;
GO  GO:0016973;
GO  GO:0045944;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPRPGGYNYKTLLCRNIPELFLDKYVARSHFGRFGTLVNFVLRPRRMTCTVSYASEDEAARALLDGASFQGHLFDISY
SQ  ADNETAPAQKTEEWVDPDIQAELSALQSGWRNEYGSGKPIKKPQNGSSGSGGSSMLPAIPVGPATAPVSRDRTPAQLRDL
SQ  ENMMRRPAHTSEEKFSVLDARDKLLRLNRTQHKLSGATQGHCADMCPEKERVLREFQRQVAYYELQPGSDELICHERALK
SQ  QYSRSSADQETPLPHELRNETALHMTMSYLMHEIMDISERQDPQSHMGDWFHFVWDRTRSIRKEITQQELCSLGAVKLVE
SQ  QCARFHIHCAARLVDADPSVFDSKINAENLTKCLQTLKYMYHDLRIKGVPCPKEAEFRGYIVLLNLADANFLWDIGQLPA
SQ  ELQSCPEVRQAIQFYLALQDTNFVRFFQLLADKDTSYLSACILVNYFTRLRVLGLHRLIQAYRSPRKDEVSSLPLSYIAE
SQ  LLSFASEQEAADFVQHYGLQINEAGRVVLSRMHTVETEYKLPRQYELVEVKRVKSVGEVVSGEPLPPRDLYLNHRPHNSF
SQ  DDYGMLKSIAWTAKDQLAGMQQEEMQPQMPSQPPAVSKHSDTLFKVPMQPDGTAAGFGVFAAAAVPPASSIDGFSFVLPK
SQ  SRAQEFQEQAPATQQRRAQEEAKHQALQVAIAAAKKREAELMAIHEAKVAEAERVRQQKLRERQEQQRRQQQELEEQRQR
SQ  EQEKLQLEKERQLKLEQLFFVQQQEREAHKQTRTLELYQEIFQDTLAEICQSEFMSHSRACRSYESMLDSITRDLVERQM
SQ  EQSIYELGVMRVCIRRWRKYRRTQQEKDTLFNQLPLSFGAENPEGVVNKRSMEDSLRLSRRYRLGEPCDYGKLLAGLEEH
SQ  SWLKLDLWHVLDKCLPVAQPGARRFYKLLISLSGGQEGLQLNCDLDRGLLQQPQSPDARFVDGGYIRGFSQGIGLSVMKI
SQ  RDDDHDWKATDLAEANGIICLIGLDDIRLLPDRLKPLLQASRCHDVAVIVQHPANTAFVQPDIPLQELCLRSFNIFRLRK
SQ  SGNNRQRLMIALESAVKFLAKATERKRVGHLHQVETREYLLVNLGSELFRRLKYAAEHDTAIRSDTQLNPQRCVDLFNEA
SQ  VHRLQLVAGEDLSDWPQFPEELRVFVQPLPIESSLNTNRLEHFEPGWHLPERRQRIVQLLERCKLPKMPVLPRSSSLAEA
SQ  QCQWVLDYAQISQQEDCVEQIALQAIKILQYDTDDYLNFVEYLAGERMQYILRQERNPPQGIVYNTKTLKRRFLSAWYYE
SQ  FREPQIYEPVPAEENAQMLEKQPSSQAEVQQLDFDEITSKAEAVLKRFHQRQDERHTLRELNRSHKSRKRRDASDHKHAS
SQ  KHKRKRSKSK
//
ID  P16733;
PN  Envelope glycoprotein M;
GN  gM;
OS  10360;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP- Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P16733;
DR  UNIPROT: Q7M6T7;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11090188, ECO:0000269|PubMed:15681419, ECO:0000269|PubMed:19761540}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCY
SQ  AVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVH
SQ  FFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAV
SQ  FVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVR
SQ  YFRGRGSGSVKYQALATASGEEVAVLSHHDSLESRRLREEEDDDDDEDFEDA
//
ID  Q9FH18;
PN  WPP domain-interacting protein 2;
GN  WIP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips.
DR  UNIPROT: Q9FH18;
DR  UNIPROT: Q5XUY7;
DR  UNIPROT: Q5XUY8;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779466,EBI-1779367; Score: 0.62
DE  Interaction: Q9C500; IntAct: EBI-1779466,EBI-1779618; Score: 0.37
DE  Interaction: Self; IntAct: EBI-1779466,EBI-1779466; Score: 0.55
DE  Interaction: Q9LE82; IntAct: EBI-1779466,EBI-1779351; Score: 0.59
DE  Interaction: Q9M651; IntAct: EBI-1779567,EBI-1779466; Score: 0.37
DE  Interaction: Q9FMH6; IntAct: EBI-1779597,EBI-1779466; Score: 0.37
GO  GO:0009504;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLESESSVLESVEDNNGLIGDLDKELNSPVETSPLISKGFGLRKWKRRLRRDLVKDDTSVSMENSKALKRVLSGLVDPN
SQ  AKQMHLPGPEVRQDSVGSVGSVNSVVGFVMGGESYGNGLAFAAGVDSDNSEDRSSTMSHSWDKHRGKVSGGKSVISSGDS
SQ  SQQRKSSVEKSNKLRGERIKIEKENSHSSMESADSRSSNFVFMQGASYSLSSREQGGRRMMDYDDENSDHDAHTSKRKDN
SQ  VEEEEEETEDYSQGDCVEESQIKSNGSSDNLDPLIVAVNSFQTLQEALQKELQKFQELGKEEPITSLHDGGESSSCIHAG
SQ  HEGASEASSSYRFGSEKMGEMELTSLDSEILNLVNNVEHLEIKLEEAKRILEVKETQIRELESTINVSETCNGGTEIGIE
SQ  DIFQQKVEAEIEYIIFSRSVGNLKRRIKLIEEEKTLGLSKLDKAETKAENLKNQAQDLQNHCVEITEIQEVECLKKRAFK
SQ  TTRCLLLQLGLLFILYYSLLPEPEIAVPT
//
ID  Q4PT37;
PN  Nuclear envelope-associated protein 3;
GN  NEAP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:27630107}; Single-pass membrane protein {ECO:0000255}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27630107}.
DR  UNIPROT: Q4PT37;
DR  UNIPROT: O80530;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0043621;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTSVSLREDDPLLKDLSEKKQSFRRNVVSLATELKEARTRLAEQERSCSKEAMSRQEAETRVKRMEDEMHELAKELNEK
SQ  VEQIRASDVATEKFVKELADIKSQLAATHATAEASALSAESAHSHCRVLSKQLHERTGSLKEHEDQVTRLGEQLENLRKE
SQ  LRVRESSQKQLRDELLKVEGDIMRAVSVVKTKENSEVRNMLNEDTPKNSERINKLLTAKDDEIARLRDELKIISAHWRFK
SQ  TKELEDQVENQRRIDQELKKKVLKLEFCLRETRIQTRKLQKMGERNDVAIQELKEQLAAKKQHEADHSSNQNLWDKSGFK
SQ  IVVSMSMLILVAFSRR
//
ID  F1P963;
PN  7,8-dihydro-8-oxoguanine triphosphatase;
GN  NUDT1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}.
DR  UNIPROT: F1P963;
DR  PDB: 5MZF;
DR  Pfam: PF00293;
DR  PROSITE: PS51462;
DR  PROSITE: PS00893;
DE  Function: Antimutagenic. Plays a redundant role in sanitizing oxidized nucleotide pools, such as 8-oxo-dGTP pools (PubMed:29281266). Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo- dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo- ATP (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:P36639, ECO:0000250|UniProtKB:P53368, ECO:0000305|PubMed:29281266}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0005829;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0035539;
GO  GO:0008413;
GO  GO:0047693;
GO  GO:0036219;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0030515;
GO  GO:0046061;
GO  GO:0006203;
GO  GO:0042262;
GO  GO:0006281;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGTSRLYTLVLVLQPERVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELREESGLTVDTLHKVGQIMFEFVGEPEL
SQ  MDVHIFCTDSVQGTPVESDEMRPQWFQLDQIPFTDMWPDDSYWFPLLLQKKKFHGYFRFQGPNTILDYTLREVDKL
//
ID  P40548;
PN  HSP70 co-chaperone SNL1;
GN  SNL1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein {ECO:0000269|PubMed:9450961}. Nucleus membrane {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein {ECO:0000269|PubMed:9450961}.
DR  UNIPROT: P40548;
DR  UNIPROT: D6VVR3;
DR  Pfam: PF02179;
DR  PROSITE: PS51035;
DE  Function: Stimulator of ATPase activity of molecular chaperones of the HSP70 family (principally of the SSA class). Stimulation is important for HSP70-substrate complex dissociation after folding of newly synthesized or refolded proteins. SNL1 is probably involved in nuclear pore biogenesis and in particular the folding or refolding of misfolded NUP116, GLE2 and NIC96. {ECO:0000269|PubMed:12105220, ECO:0000269|PubMed:9450961}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06247; IntAct: EBI-24950,EBI-38452; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-24950,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-24950,EBI-18976; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-24950,EBI-6314; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-24950,EBI-7218; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-24950,EBI-8632; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-24950,EBI-8627; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-24950,EBI-8591; Score: 0.35
DE  Interaction: P11075; IntAct: EBI-24950,EBI-16882; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-24950,EBI-16136; Score: 0.35
DE  Interaction: P14127; IntAct: EBI-24950,EBI-14531; Score: 0.35
DE  Interaction: P06367; IntAct: EBI-24950,EBI-14460; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-24950,EBI-16054; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-24950,EBI-15447; Score: 0.35
DE  Interaction: P29453; IntAct: EBI-24950,EBI-15435; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-24950,EBI-15409; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-24950,EBI-15394; Score: 0.35
DE  Interaction: P14120; IntAct: EBI-24950,EBI-15333; Score: 0.35
DE  Interaction: P38754; IntAct: EBI-24950,EBI-14475; Score: 0.35
DE  Interaction: P40212; IntAct: EBI-24950,EBI-14456; Score: 0.35
DE  Interaction: P50108; IntAct: EBI-24950,EBI-11043; Score: 0.35
DE  Interaction: P38631; IntAct: EBI-24950,EBI-7708; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051087;
GO  GO:0043022;
GO  GO:0006999;
GO  GO:0006457;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHNAMEHWKSKLSKTSTSTYVLLAVIAVVFLVTIRRPNGSKGKSSKKRASKKNKKGKNQFEKAPVPLTLEEQIDNVSLR
SQ  YGNELEGRSKDLINRFDVEDEKDIYERNYCNEMLLKLLIELDSIDLINVDESLRRPLKEKRKGVIKEIQAMLKSLDSLK
//
ID  Q5XIS2;
PN  Ceramide-1-phosphate transfer protein;
GN  Cptp;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q5XIS2;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0008289;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0050713;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MDGPERDFNLKVVLISFKKCLTDKGEVLLDHYTASWKGLVRFLNSLGAVFSFISKDVVSKLQIMEHLRSGPQSEHYISLQ
SQ  SMVAYEVSNKLVDRDSRSRPRHPNSGCRTVLRLHRALHWLQLFLEGLRTSSEDARTSTLCSEAYNATLAAYHSWIVRQAV
SQ  NVAFHALPPRKVFLEAMNMGSSEQAVEMLGEALPFIEQVYDISQKLYAEHSLLDLP
//
ID  O13712;
PN  Meiotically up-regulated gene 61 protein;
GN  mug61;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: O13712;
DR  UNIPROT: Q9USD6;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Required for correct meiotic chromosome segregation. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P7F8; IntAct: EBI-1542405,EBI-15798909; Score: 0.37
DE  Interaction: O42841; IntAct: EBI-1542405,EBI-21242362; Score: 0.37
DE  Interaction: Q9UUJ1; IntAct: EBI-1542405,EBI-443389; Score: 0.37
DE  Interaction: Q10436; IntAct: EBI-1542405,EBI-21242299; Score: 0.37
DE  Interaction: Q10169; IntAct: EBI-1542405,EBI-7989032; Score: 0.37
DE  Interaction: O13787; IntAct: EBI-1542405,EBI-21242328; Score: 0.37
DE  Interaction: Q9P6P8; IntAct: EBI-1542405,EBI-21242420; Score: 0.37
DE  Interaction: Q9P6M1; IntAct: EBI-1542405,EBI-1542559; Score: 0.37
DE  Interaction: Q09835; IntAct: EBI-1542405,EBI-21242393; Score: 0.37
DE  Interaction: O14223; IntAct: EBI-1542405,EBI-21242449; Score: 0.37
DE  Interaction: Q9UT35; IntAct: EBI-1542405,EBI-21242469; Score: 0.37
DE  Interaction: O42901; IntAct: EBI-1542405,EBI-21242494; Score: 0.37
DE  Interaction: Q09825; IntAct: EBI-1542405,EBI-929731; Score: 0.55
DE  Interaction: Q9Y806; IntAct: EBI-1542405,EBI-21242528; Score: 0.37
DE  Interaction: Q9Y7X6; IntAct: EBI-1542405,EBI-1559673; Score: 0.37
DE  Interaction: P36596; IntAct: EBI-1542405,EBI-1794119; Score: 0.37
DE  Interaction: P10815; IntAct: EBI-1542405,EBI-1187843; Score: 0.37
DE  Interaction: O94361; IntAct: EBI-1542405,EBI-21242566; Score: 0.37
GO  GO:0005623;
GO  GO:0034506;
GO  GO:0005789;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005720;
GO  GO:0031965;
GO  GO:1990707;
GO  GO:1990421;
GO  GO:0005524;
GO  GO:0070197;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGV
SQ  TNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPF
SQ  ETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNT
SQ  TSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLV
SQ  GLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKF
SQ  DSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWH
SQ  QEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFG
SQ  LKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVY
SQ  LKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAA
SQ  ITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSI
SQ  QLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL
//
ID  A6XA80;
PN  Leukotriene C4 synthase;
GN  LTC4S;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A6XA80;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0004464;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKDEVALLATVTLLGVLLQAYFSLQVIRARRAHRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGVYFHEGAAA
SQ  LCGLVYLFTRLRYFWGYARSAQLRLAPLYASARALWLLLALATLGLLAHFLPAAARAALLRLLRALLRTA
//
ID  Q9UUE5;
PN  Nucleoporin nup85;
GN  nup85;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15226438}. Note=Localizes to the nuclear envelope and spindle pole body. {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UUE5;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005719;
GO  GO:0005720;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0005816;
GO  GO:1990188;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0006407;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESSDEVDLPVYHLQNAPIENGKLNDWRSKGRTVAFKLHPFLRKGLAYINNKEFDENTLKSDKFEEVESLVYEFSTPSTL
SQ  IEPNYLLTAWHELWEELQDTYMTPILDSEANLLLLTQFYGKISSLFRSKIIQVLEELQSRINEGEKDCQPVLDSLWEVES
SQ  AWRCAEAIYFPPSSPYTLSTGILDWVNAYDPQPIADDGLEIMAYRIPYQHPEFWPYVNKTAIRGLFEQTISCLEMSGLTK
SQ  EWPVLKETVDELIDILRYSPCTHQKRIRSVSDFERRWKLWRSRLANLRHVVKKHRDIDSEVLDDFVVLLDILNGNKEVIM
SQ  LSCAHWQEYFSALAFLYGPLDCKNPEDISLLYQLATGEDSKFYVNGTIEYEQICVNLCSNEPLNAIKHAYLLDLGLAVHL
SQ  ADLLSKSGHLRDYITEEYPITLREHLILEYGQCVLESRNLWQTSFAYWKCVADSGYQRIKACIPYVPLSDVDAKETALQL
SQ  CKQLKLRDEAQLVLTHWADELIARNHYGEALIALDNAANYSALNRVTWELFDICIAEKKSFSPDKDELLYELFSSPKACT
SQ  PTLASIISPAATIHQYFFYLQHKKELNASELLVGLLTMVDFPSSRFPKLLELLHEFLNNPLQSNSTDFKLSLVNVYDCIA
SQ  VLQDQQSTVKDQQLLLSIHERLSSAISWYFLHLKK
//
ID  O74500;
PN  Nucleoporin nup60;
GN  nup60;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}.
DR  UNIPROT: O74500;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0017056;
GO  GO:0008298;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0006611;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSGPIRTLHKGKAARNRTPYDRIAASKDGNHSNGPQTPSKSIFQRAKEWLTPSSWKKAISIFSSPVVNKHEDSFDSKTD
SQ  EEYLQNVSTTTEDVSMLINTPVTEKYEQEHRDTSAQATPSIVEQSPNQMLANFFSKKGKTPLNEIEKEGIISILNKSASP
SQ  SSSVISPAASLNRFQTPRAAAISKRESGVSSEPRARTSSLTPGNTPNSAKQWSAFRSTFSPLREQDQLSTISPNSLLPAQ
SQ  RLSYYGPTLSTPYNRRLRHKRHSTTPISLSNSIAPSLSFQPKKARYESANVSFNDTSFTNVPTSSPLHQSTTANHPEKTP
SQ  SRAAASLLSILDSKEKNTPSITAKAGSPQSAPSKASYISPYARPGITTSRRRHDQIRPSSEKSEPEKKEPSAFETLEKSS
SQ  NVQTYKPSLMPEFLEKASTHGSFAKQKEGEQTSLSEKTALSEPENKTPVFSFKAPSATTDKPSPPVSSIFSFNAPSAAST
SQ  KPSPAVSSTFSFNAPTTTPSATSFSIINKEKPARSPNETIDVDLEEEGSGISAEVEVANEGEDLQKNATEVKASTSEKPV
SQ  FRFEAVTDEKNSEVSSSNQASSSTMISQPNTGFSFGSFNKPAGQEEKPQQRSLFSASFTTQKPELPAAKIEPEVQMTNVA
SQ  IDQRSFEQAEKSPISVSESTSLVEVEKPSAEGTNEHKQDATMTLEKTDKQGSLEEEPFPKFSFTVLPKENGENLSTMEST
SQ  QELPKFSFSVLKEEKN
//
ID  P53067;
PN  Importin subunit beta-5;
GN  KAP114;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P53067;
DR  UNIPROT: D6VV94;
DR  PDB: 6AHO;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA- binding protein (TBP) and of histones H2A and H2B. {ECO:0000269|PubMed:10535958, ECO:0000269|PubMed:11309407}.
DE  Reference Proteome: Yes;
DE  Interaction: P04912; IntAct: EBI-8076,EBI-9174; Score: 0.67
DE  Interaction: Q12692; IntAct: EBI-8080,EBI-9174; Score: 0.67
DE  Interaction: P38910; IntAct: EBI-4553,EBI-9174; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-9174; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-9174; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-9174,EBI-8603; Score: 0.53
DE  Interaction: P46988; IntAct: EBI-9174,EBI-13224; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-9174,EBI-8680; Score: 0.35
DE  Interaction: P13393; IntAct: EBI-19129,EBI-9174; Score: 0.53
DE  Interaction: P25635; IntAct: EBI-14332,EBI-9174; Score: 0.35
DE  Interaction: P02293; IntAct: EBI-8088,EBI-9174; Score: 0.56
DE  Interaction: P25293; IntAct: EBI-11850,EBI-9174; Score: 0.56
DE  Interaction: P16140; IntAct: EBI-9174,EBI-20254; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-9174,EBI-14372; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-9174,EBI-6314; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-9174,EBI-11191; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-9174,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-9174,EBI-18976; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-7238,EBI-9174; Score: 0.27
DE  Interaction: Q02486; IntAct: EBI-2028,EBI-9174; Score: 0.27
DE  Interaction: P49956; IntAct: EBI-4560,EBI-9174; Score: 0.27
DE  Interaction: P02294; IntAct: EBI-8094,EBI-9174; Score: 0.56
DE  Interaction: Q02159; IntAct: EBI-9174,EBI-19749; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008536;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLSLRKLITMYWSPGFESYRSTS
SQ  NVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISAVDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSE
SQ  EMFFEGGIGLATMEIVFKVLNTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGN
SQ  VDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTESEPLLETVHDCSIYIVEFLTS
SQ  VCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFVSKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIE
SQ  HSTCNYSTLESLLYLLQCILLNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPL
SQ  TSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQVSSDAEEDTNGALMEVLSQVI
SQ  SYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQECLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYS
SQ  PLLSLVLEFITVFLKKKPNDGFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLER
SQ  LLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVLCFLTCNDPKQTVDFLSSFQI
SQ  DNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLNDKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLY
SQ  TKIIKLFVSELSFQSKQPNPEQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMD
SQ  VKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
//
ID  P53148;
PN  Spindle pole body component SPC105;
GN  SPC105;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Chromosome, centromere, kinetochore. Note=Localizes to the nuclear side of the spindle pole body.
DR  UNIPROT: P53148;
DR  UNIPROT: D6VU52;
DR  PDB: 4BL0;
DR  Pfam: PF08317;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint. {ECO:0000269|PubMed:19893618}.
DE  Reference Proteome: Yes;
DE  Interaction: Q04431; IntAct: EBI-32446,EBI-23870; Score: 0.66
DE  Interaction: P40568; IntAct: EBI-25398,EBI-23870; Score: 0.35
DE  Interaction: Q12143; IntAct: EBI-33666,EBI-23870; Score: 0.35
DE  Interaction: P39731; IntAct: EBI-11606,EBI-23870; Score: 0.35
DE  Interaction: P40460; IntAct: EBI-23870,EBI-25247; Score: 0.50
DE  Interaction: P33895; IntAct: EBI-23870,EBI-12377; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-23870,EBI-10154; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-23870,EBI-8627; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-23870,EBI-8632; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-30084,EBI-23870; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-23870,EBI-8648; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-23870; Score: 0.64
DE  Interaction: P14693; IntAct: EBI-23870,EBI-24602; Score: 0.37
GO  GO:0005623;
GO  GO:0000941;
GO  GO:0000778;
GO  GO:0005739;
GO  GO:0031617;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0008017;
GO  GO:1990758;
GO  GO:0007094;
GO  GO:0034501;
GO  GO:0031134;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNVDERSRIGGREKDAGPGKGILKQNQSSQMTSSFLENPGVRIPTRIITKKEVLDGSNTTSRINTSNLQSMVKRRVSFAP
SQ  DVTLHSFTFVPEQNNEIKEPRRRKTSTNSPTKISSQEEPLVTSTQIDDARTEEKTAAEEDPDTSGMELTEPIVATPDSNK
SQ  ASQHDPTSMEMTEVFPRSIRQKNPDVEGESIESSQQIDDVEAVREETMELTAIHNVHDYDSISKDTVEGEPIDLTEYESK
SQ  PYVPNSVSRSTGKSSDYSVERSNDKSDLSKSENKTNSSQPMEITDIFHADPQNPMSLHSDNNINNDGNEMELTQIQTNFD
SQ  RDNHHIDESPSEKHAFSSNKRRKLDTVSDYAASVTTPVKEAKDTSGEDNDGDLEMMEKMSPITFSDVDNKIGTRSNDVFT
SQ  IEPGTEDTGMQTATDDEEDGENVDDNGNKIVEKTRLPEIDKEGQSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKV
SQ  NFPLNSFNFVENQRIDNVFSAFYIDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLM
SQ  RDQLQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIRKLNEAIKEEIRSLKNLP
SQ  SDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKLAIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKL
SQ  RDTLKILESLTGVRFLKFSKATLSIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDS
SQ  MLSNLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFAQGVFSENGQIPMKVHIS
SQ  TQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT
//
ID  Q09684;
PN  Nuclear fusion protein tht1;
GN  tht1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein {ECO:0000269|PubMed:9442101}. Nucleus membrane {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein {ECO:0000269|PubMed:9442101}.
DR  UNIPROT: Q09684;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:9442101}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLL
SQ  NTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEV
SQ  NMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEIL
SQ  STIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSV
SQ  QSNIDFVNSGFQPLYDLTIQLKEELQSLKRLSSEQQNLQHEQILQWKSDFLNVSKDHLKVLQQLRPLIDIVEKFMNVYFK
SQ  GLSNIISSFAFIGFTLFATLSSLFFKVLKIHRRPIIVFGSLSIIFIHIYCFKITSWVNLYGWITCTIARTLSFIKLNIRT
SQ  FYLTAFLCALLNFLRYLKYRNSKKDTELSLFLPAPEECNIYHNEHIQVQEDNYLCPIENSLIDLFGSENNKEKLGKQENV
SQ  RFAFLNSESLEQSPWWD
//
ID  H2KZB2;
PN  Ankyrin repeat and LEM domain-containing protein 2 homolog;
GN  lem;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22770216}; Single-pass membrane protein {ECO:0000269|PubMed:22770216}.
DR  UNIPROT: H2KZB2;
DR  UNIPROT: Q5W7E5;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of baf-1 during mitotic exit. Coordinates the control of baf-1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of baf-1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}.
DE  Reference Proteome: Yes;
DE  Interaction: Q03565; IntAct: EBI-6258914,EBI-2535603; Score: 0.44
DE  Interaction: Q19848; IntAct: EBI-6258914,EBI-2414048; Score: 0.56
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051721;
GO  GO:0051301;
GO  GO:0007084;
GO  GO:0042326;
GO  GO:0035307;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGT
SQ  PREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEG
SQ  FRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRV
SQ  LTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATV
SQ  TVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAF
SQ  LREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEK
SQ  SINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQIS
SQ  SELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI
//
ID  Q1XG89;
PN  Putative ATP-dependent RNA helicase TDRD12;
GN  TDRD12;
OS  7091;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome {ECO:0000269|PubMed:17098166}. Cytoplasm, cytosol {ECO:0000269|PubMed:17098166}. Nucleus membrane {ECO:0000269|PubMed:17098166}; Peripheral membrane protein. Note=At 36 hours after oviposition, detected in the nucleus and the cytosol where it is associated with chromosomes and to the surface of the nuclear membrane (PubMed:17098166). Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:24067652). {ECO:0000269|PubMed:17098166, ECO:0000269|PubMed:24067652}.
DR  UNIPROT: Q1XG89;
DR  UNIPROT: H9JJS3;
DR  Pfam: PF04969;
DR  Pfam: PF00270;
DR  Pfam: PF00567;
DR  PROSITE: PS51203;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50304;
DE  Function: Probable ATP-binding RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. {ECO:0000305|PubMed:26669262}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0043186;
GO  GO:1990923;
GO  GO:0005524;
GO  GO:0003676;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0031047;
GO  GO:0051321;
GO  GO:0007275;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MASDYYQVEILHYLNPNLIWVEVLNSPNEISFEQLGVYGILPIDASLDVERPGLKLQRSEDWMPATAILMKNIFQNLEQV
SQ  WFSPTHIDRRSSIFDNNIHKYGELIIKKNGVQLYLSKELVKAGLATEDPCQFHQYMSLGKIKTKLSNTETRAVIKNLEEY
SQ  YRKSSKPKELWQKSVHQNTSIFHAGERLQALTVKNLERHNNRQNIMLLENKLKDLEQCKGSDEVSLGRGVCRVPSNKSEM
SQ  VMLTNKRLKNRLELLSKINMKSDATDAVKSTKRNFSGDGQRKNFENDFESDDESVKKVSIANTINTSDGSANVVDKLLDE
SQ  KQIDNVFNNKKQICYTESTRRNPVKKAACIVYGPPSINIDKLPLKEAPKMTKTVKWTPHVDCDKEASEVSFGDVDSHVKL
SQ  DVKNLDKFHEIADRIEIEKTIPVDVNIHKDLYDSMINNKNESESKIMETANLKTEMKNLRKSSILQSKLKQFDKFNVSSN
SQ  SAASESSTKSSMDSSRISDEDDLSSDDEMSEIMETFKLNLATPKKSEAKHTIDHIEVNNTKLNANPFKNLDGSKSVFVDK
SQ  LTSPVLLVHTKRNNKVQPCSLLRDVPFGTSIHVVLRNMGIKHPTRLQTVSWGTILRGLSTFLISPPRSGKTMGYLPAVCR
SQ  LVRDFRKESPDSCGPKCIIVCATSKSVSEVERISKMLLGLEDKVFACYSGMDNLSVTTALLNGCDLLICTPKSIVRLLQN
SQ  DLSVDLRDLTTFVVDDCERISDVYSNEVKYVLYEIKNMLKNRVNKELKVQIVVASRIWCDFLEPIVLKAPDSVVCIGAFQ
SQ  ELILYSKISTTVDFLRPENKIANVLQFIDSVQGPKRTVVVCRADNEVKAVESSLRYNNRVVFACDNTMNIHDLYNLNVVW
SQ  GDFEDPTLGPILVCCDSNLVHLNVTDASYLIHYSLPALFSTFCKRFSVLNDNYPSIFKNESRDLKVKVLMDESNVEQLPK
SQ  ILNFLKRCTENVPKILDEVSEKILNEKDLAKVKDLVPLCDNLLSLGICPDTWNCTERHRIFKECDSPADWIPKNGVVTFQ
SQ  ILYFHSAVMYSARLLSNTVDGETTKYPQTYSTLSLKMGMYFSKESSRRLHGIPMVGDVCAVSKKQNFFIRCQVVKIISFY
SQ  KNGNPNYVVIKLIDEEKFEQSRDIYLYHLPDEFKDMKTYVVQVRLANIQPQDKDITFSCLAKNELEKIVEKNEDLFMRGH
SQ  VAMSVGSCIFVDTLEACLDLSSLSETVVRHNFKQELLNAHAVPNPKHLSILEEMCEKSGLIVKAVTNEQVVPKPIPVLPA
SQ  AQWAHLEDDLSSVYLASVEDMDKLFVRLVKFESCMKLLNIEINKYVSENTVPLDGSNVGDIVLAKFPDDSMYERARIDHI
SQ  YSEDKVKCFFVDQGDWRDVSTNDLATITENFITQLPFQAIECRLIGIRPFGEQWTEFSTNWFSDHCFEDAKGNLKHLYVK
SQ  HFTKEKADCTGGHKYGVALIDTYTNEDIIVNQLLIDLNLAKENVDEIAYLSEIKCNKTVLNNDATVDEEEGSLSGVSEPE
SQ  SNINVPLDKVFLKAPIRSVPLVDSEYETSDSDTWQINRPEDFKALFMRTRPESSKIIPMITANEVQNNADGETSKDTSTI
SQ  LEEKGQLPEKVKDDELKLSKPKICWSQNKNTVKLKILIAGIEDYKLKIEDRAVAFSANHCDVEYGFKLELYGVVDVNKSR
SQ  HSNKGQYVLVTMTKLMCRNWLALTKEGDSQKWIVYDVDTIEASSDEEVYRDDTLEVIKNIHNTNNGSDSEDDDFLDDVS
//
ID  Q8GXA4;
PN  WPP domain-interacting protein 1;
GN  WIP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips.
DR  UNIPROT: Q8GXA4;
DR  UNIPROT: O65589;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715, PubMed:18591351). As component of the SUN- WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-1779367,EBI-1779367; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1796628,EBI-1779367; Score: 0.57
DE  Interaction: Q9LE82; IntAct: EBI-1779367,EBI-1779351; Score: 0.74
DE  Interaction: Q9M651; IntAct: EBI-1779367,EBI-1779567; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779466,EBI-1779367; Score: 0.62
DE  Interaction: Q9FMH6; IntAct: EBI-1779597,EBI-1779367; Score: 0.37
DE  Interaction: Q9C500; IntAct: EBI-1779367,EBI-1779618; Score: 0.37
DE  Interaction: Q94AV5; IntAct: EBI-1779487,EBI-1779367; Score: 0.37
DE  Interaction: Q84MC7; IntAct: EBI-1779367,EBI-2349513; Score: 0.56
DE  Interaction: Q8GYN0; IntAct: EBI-4450073,EBI-1779367; Score: 0.37
DE  Interaction: Q8GYS8; IntAct: EBI-4450061,EBI-1779367; Score: 0.37
DE  Interaction: Q8L603; IntAct: EBI-4446515,EBI-1779367; Score: 0.37
DE  Interaction: Q8RXL7; IntAct: EBI-4427323,EBI-1779367; Score: 0.37
DE  Interaction: Q8RY98; IntAct: EBI-1779367,EBI-4452570; Score: 0.37
DE  Interaction: Q8S8K0; IntAct: EBI-4453700,EBI-1779367; Score: 0.37
DE  Interaction: Q8VYV9; IntAct: EBI-4463541,EBI-1779367; Score: 0.37
DE  Interaction: Q8VZ48; IntAct: EBI-4455850,EBI-1779367; Score: 0.37
DE  Interaction: Q8VZ95; IntAct: EBI-2010972,EBI-1779367; Score: 0.37
DE  Interaction: Q93V66; IntAct: EBI-4453472,EBI-1779367; Score: 0.37
DE  Interaction: Q93V85; IntAct: EBI-4438153,EBI-1779367; Score: 0.37
DE  Interaction: Q93ZQ3; IntAct: EBI-1779367,EBI-4450641; Score: 0.37
DE  Interaction: Q946Y7; IntAct: EBI-4438441,EBI-1779367; Score: 0.37
DE  Interaction: Q94A32; IntAct: EBI-1779367,EBI-4438745; Score: 0.37
DE  Interaction: Q94A99; IntAct: EBI-4451043,EBI-1779367; Score: 0.37
DE  Interaction: Q94AP3; IntAct: EBI-4449665,EBI-1779367; Score: 0.37
DE  Interaction: Q94CK3; IntAct: EBI-1779367,EBI-4450097; Score: 0.37
DE  Interaction: Q9LVZ7; IntAct: EBI-4443708,EBI-1779367; Score: 0.37
DE  Interaction: Q9FH92; IntAct: EBI-1779367,EBI-4443876; Score: 0.37
DE  Interaction: Q9FK55; IntAct: EBI-1779367,EBI-4426223; Score: 0.37
DE  Interaction: Q9FKK1; IntAct: EBI-1779367,EBI-4453688; Score: 0.37
DE  Interaction: Q9FL61; IntAct: EBI-1779367,EBI-4432515; Score: 0.37
DE  Interaction: Q9FVX3; IntAct: EBI-1779367,EBI-4436871; Score: 0.37
DE  Interaction: Q9FZ54; IntAct: EBI-1779367,EBI-4430708; Score: 0.37
DE  Interaction: Q9FZ98; IntAct: EBI-4425682,EBI-1779367; Score: 0.37
DE  Interaction: Q9LDU6; IntAct: EBI-1779367,EBI-4439540; Score: 0.37
DE  Interaction: Q9LJD9; IntAct: EBI-1779367,EBI-4440036; Score: 0.37
DE  Interaction: Q9LPF1; IntAct: EBI-4466346,EBI-1779367; Score: 0.37
DE  Interaction: Q9LQ32; IntAct: EBI-4436710,EBI-1779367; Score: 0.37
DE  Interaction: Q9LSF6; IntAct: EBI-4434839,EBI-1779367; Score: 0.37
DE  Interaction: Q9M2J9; IntAct: EBI-4434027,EBI-1779367; Score: 0.37
DE  Interaction: Q9M9S6; IntAct: EBI-4434173,EBI-1779367; Score: 0.37
DE  Interaction: Q9SA23; IntAct: EBI-4436558,EBI-1779367; Score: 0.37
DE  Interaction: Q9SCL4; IntAct: EBI-1779367,EBI-4463558; Score: 0.37
DE  Interaction: Q9SCZ8; IntAct: EBI-4458901,EBI-1779367; Score: 0.37
DE  Interaction: Q9SEL6; IntAct: EBI-1162795,EBI-1779367; Score: 0.37
DE  Interaction: Q9SHG7; IntAct: EBI-4436589,EBI-1779367; Score: 0.37
DE  Interaction: Q9SIH4; IntAct: EBI-4451446,EBI-1779367; Score: 0.37
DE  Interaction: O80594; IntAct: EBI-4428472,EBI-1779367; Score: 0.37
DE  Interaction: O80895; IntAct: EBI-4456509,EBI-1779367; Score: 0.37
DE  Interaction: O81062; IntAct: EBI-1779367,EBI-4440921; Score: 0.37
DE  Interaction: O82245; IntAct: EBI-1779367,EBI-4455652; Score: 0.37
DE  Interaction: P47192; IntAct: EBI-1779367,EBI-4433747; Score: 0.37
DE  Interaction: P59229; IntAct: EBI-4432491,EBI-1779367; Score: 0.37
DE  Interaction: P82874; IntAct: EBI-1779367,EBI-2352074; Score: 0.37
DE  Interaction: Q41975; IntAct: EBI-1779367,EBI-4449798; Score: 0.37
DE  Interaction: Q42342; IntAct: EBI-2295493,EBI-1779367; Score: 0.37
DE  Interaction: Q5XEV3; IntAct: EBI-1779367,EBI-4431808; Score: 0.37
DE  Interaction: Q5XF13; IntAct: EBI-1779367,EBI-4431954; Score: 0.37
DE  Interaction: Q6NLF5; IntAct: EBI-4431243,EBI-1779367; Score: 0.37
DE  Interaction: Q6NQG3; IntAct: EBI-1779367,EBI-4429694; Score: 0.37
DE  Interaction: Q84MC9; IntAct: EBI-4427374,EBI-1779367; Score: 0.37
DE  Interaction: Q8GWH4; IntAct: EBI-4426287,EBI-1779367; Score: 0.37
DE  Interaction: Q8GX70; IntAct: EBI-4430355,EBI-1779367; Score: 0.37
DE  Interaction: Q9SRE4; IntAct: EBI-4434931,EBI-1779367; Score: 0.37
DE  Interaction: Q9STW3; IntAct: EBI-4429423,EBI-1779367; Score: 0.37
DE  Interaction: Q9SY29; IntAct: EBI-1779367,EBI-4454735; Score: 0.37
DE  Interaction: Q9XI60; IntAct: EBI-4424450,EBI-1779367; Score: 0.37
DE  Interaction: Q9ZQ38; IntAct: EBI-1779367,EBI-4454302; Score: 0.37
DE  Interaction: Q9ZSR7; IntAct: EBI-4449636,EBI-1779367; Score: 0.37
DE  Interaction: Q9ZUJ2; IntAct: EBI-4424518,EBI-1779367; Score: 0.37
DE  Interaction: Q9ZVX8; IntAct: EBI-1779367,EBI-4425116; Score: 0.37
GO  GO:0009504;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLESESSALESVDDNVLIQQSASNVCDDGRSLDNGSCSDESVKLLSTSNSVELGKPMSFDSPGDGGGAYSPVLKGQGLR
SQ  KWRRIRRDLVKDTSANMENSKALKRGLSGVAHSHGKQMQFQSPEVEQESQGSVGSVNMLKSSGDGFDILGSSGYDSRFVA
SQ  GVGFSAGMDLEIDDDRSSKSSTVARAPKVIRYEKPMISSGQGGNIRVENSKKHRGESVDFEKENSYSSLESDSRKQSGRM
SQ  MDYNGENGETSMRKDDAGGEGGESINTDNRYSDEMDPLTEAINGFLALQDALEKEVQQFQEIGNEPMPQHHEQVSEANSP
SQ  HPEIVTLVNNVEQLENMLEETRSMLEVKESHIRDLESTTNQSKHSWGGTEIVVEDIFRQKIEAEIEYLIYSRSIDNLNSQ
SQ  MKLIDEQESLAEEQTHETLNKLGRVQTKAANFTNRAQDLQNDCIEITGTIKKRACKITSYVLIQLVLLSTVVLLLLSQLL
SQ  PEPDTVVPT
//
ID  Q0WSX8;
PN  TIR domain-containing protein;
GN  TIK;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q0WSX8;
DR  UNIPROT: Q9FLA6;
DR  Pfam: PF01582;
DR  PROSITE: PS50104;
DE  Function: Could play a role in nuclear morphology, specifically nuclear size. {ECO:0000269|PubMed:25217773}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050135;
GO  GO:0061809;
GO  GO:0043621;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDEQVQEPLSDQVFINFRGDELREIFVNHLELQLRNAGINVFIDTKEQKGRRLQYLFTRIKKSKIALAIFSKRYCESKWC
SQ  LDELVTMNEQMKEKKLVVIPIFYNVRSDDVKRAANPDGEGNLDGEFSLPFKQLKQNHAGEPERVEGWERALRSVTKRIGF
SQ  SRSNSKYKHDTDFVLDIVKEVKKQLNIPTDNSWSAIGVAFLAITINLIFSFFIAPKYLPDQKFFQTPEWFIGTLAVVLAS
SQ  WFWYKNNQNKAPPPS
//
ID  Q9VKJ3;
PN  Nuclear pore complex protein Nup160 homolog;
GN  Nup160;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19197064}.
DR  UNIPROT: Q9VKJ3;
DR  UNIPROT: C0KG65;
DR  UNIPROT: C0KG66;
DR  UNIPROT: C0KG67;
DR  UNIPROT: C0KG68;
DR  UNIPROT: C0KG69;
DR  UNIPROT: C0KG70;
DR  UNIPROT: C0KG71;
DR  UNIPROT: C0KG74;
DR  UNIPROT: C0KG75;
DR  UNIPROT: Q6AWI7;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:19197064). Involved in poly(A)+ RNA transport (By similarity). Required for nuclear import of Mad (PubMed:20547758). May play a role in double strand break DNA repair (PubMed:26502056). Essential for nephrocyte development (PubMed:30910934). {ECO:0000250|UniProtKB:Q12769, ECO:0000269|PubMed:19197064, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:30910934}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8IGE8; IntAct: EBI-141018,EBI-466337; Score: 0.37
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0000724;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0046822;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTSKLQANMSYREVIPRNLSPAEWIEVKINTGTQSTLQDLKTFETSGGYCYKNTKNVQTRNRFIYWRTYQDVLELSEVS
SQ  LDISLQRNHLRLRFTDSAVLNVSLTEQGTSVTLLVVTVSSVHRYVFPLKVAGQEGGAASPEDLLSQSIFYDVNDKINDPS
SQ  TYYVTDGFGTMPNAAVSYLTQDSQSAYFAVAYQSKLLLHVMKCSTGHTITHEIKEPKLMPWFLSNLKGALTGRSETLEAA
SQ  TSMAFSEIGGEIFILVLYRNNELRLWSVDNLQTVASINCSTELGQDSAAQGPQNSQLRKISDQNFCLFLSHNSRAEFICV
SQ  SIMPDADDASVINLVQNMVPAPQTDLVDFDATSSHIWALWSNAEGDFHVSAAYFASNNAIKWVSAALEPPPDRYCLTMEQ
SQ  GVDPRETYCSYIFHPGRFDRNVIAKALYMFRRVNLQFDVKQLSMSVLKEQVCQAVEDEIQNELKDFVVTDEEYLEISTRL
SQ  WDRFYSCCEQYHIKLSEPTGLAVLGGMDAVCLVRRQSFALLRPCEVLEHLLLIGEHNDEVATYVAPLFRNDPEMAKGFVE
SQ  LMNVVTLLDKLISEDIKIELDKQLYQRESPVEVISKLVARISMIDDNGPILPSNCVRQIQQKLQNIPNLEPALEMLLDVL
SQ  CMIDPDEPPHDYSLSTRFLQSSGALMGSEYGLSILSETVKQMAMIRFSVCRNLLVLQYMAYGQNEMESENVLTNLNYLNS
SQ  YYTLVWIAETPISSSTPAGFEASIQRLSRAQLFSGYNRPYSSHLKHNGNDQTTLLRLFLESKGLFSALTMLLKHDSLSLD
SQ  SEQLNLRQSLLQLVGYINKMLWPGSPIYVFPEWLFGTCHHIIVQDYVRILSNWCSVQKHARRFMLAVSLLDCGEAHKAVH
SQ  LFHEAESGIVEDDFLFEHVLKNTPLYGKLQNSVSRGDTISPEDTKLAIVHYYLKVIQLFEQHSALDYIIQLADMAIRVLQ
SQ  PDDPQLPMFQSIVFNNHLQLGHYVEAYTALVNNADISRRKDCLRQLVITLFQNKCLPLLMQFSYIGLQDEFESIVESRAR
SQ  SMSIDQNEVYNFLYAFHTNKGNMRKASTVMYEQAMRFQVDSDAPNALEKRCSSLLICLNCLHLVDSRYRWIAKPVLGDEQ
SQ  VITIDQDNDDGEPKCDEDKRGQEVVVLELADIRRELVHAEALRELSFYRKDTAAYERATPEELSYLLASSGLYTAALKLS
SQ  RGHSFSVLPIFESLTSACVAATEDKSSDAWNWLQNNDMADLPHRSNAADMAWTLLQKLVVDNEAKDSTLIRKSVVQRLLG
SQ  LNAFLPQWLINSYKLSHSRELLHLLVKHNRLLEAADLGCEIIAGMLGAGSEYFEFKHAVNIANPQLCFPISTIDLLLHGL
SQ  KINGKDDLDYEMAYFKLEEEVQRYIETIKRTTDDKMSMAVLQMRTDLQEER
//
ID  P03215;
PN  Envelope glycoprotein M;
GN  gM;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P03215;
DR  UNIPROT: Q777D4;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11070013}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVY
SQ  ITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLH
SQ  FLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMV
SQ  LGAVNLFLILPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLI
SQ  RICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSE
SQ  EEIFP
//
ID  Q8RY25;
PN  Nuclear pore complex protein NUP98A;
GN  NUP98A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RY25;
DR  UNIPROT: Q9SY83;
DR  Pfam: PF04096;
DR  PROSITE: PS51434;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P94077; IntAct: EBI-5849461,EBI-20796369; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:1902446;
GO  GO:0006405;
GO  GO:0034398;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGSSNPFGQSSGTSPFGSQSLFGQTSNTSSNNPFAPATPFGTSAPFAAQSGSSIFGSTSTGVFGAPQTSSPFASTPTFG
SQ  ASSSPAFGNSTPAFGASPASSPFGGSSGFGQKPLGFSTPQSNPFGNSTQQSQPAFGNTSFGSSTPFGATNTPAFGAPSTP
SQ  SFGATSTPSFGASSTPAFGATNTPAFGASNSPSFGATNTPAFGASPTPAFGSTGTTFGNTGFGSGGAFGASNTPAFGASG
SQ  TPAFGASGTPAFGASSTPAFGASSTPAFGASSTPAFGGSSTPSFGASNTSSFSFGSSPAFGQSTSAFGSSAFGSTPSPFG
SQ  GAQASTPTFGGSGFGQSTFGGQQGGSRAVPYAPTVEADTGTGTQPAGKLESISAMPAYKEKNYEELRWEDYQRGDKGGPL
SQ  PAGQSPGNAGFGISPSQPNPFSPSPAFGQTSANPTNPFSSSTSTNPFAPQTPTIASSSFGTATSNFGSSPFGVTSSSNLF
SQ  GSGSSTTTSVFGSSSAFGTTTPSPLFGSSSTPGFGSSSSIFGSAPGQGATPAFGNSQPSTLFNSTPSTGQTGSAFGQTGS
SQ  AFGQFGQSSAPAFGQNSIFNKPSTGFGNMFSSSSTLTTSSSSPFGQTMPAGVTPFQSAQPGQASNGFGFNNFGQNQAANT
SQ  TGNAGGLGIFGQGNFGQSPAPLNSVVLQPVAVTNPFGTLPAMPQISINQGGNSPSIQYGISSMPVVDKPAPVRISSLLTS
SQ  RHLLHRRVRLPARKYRPGENGPKVPFFTDDEESSSTPKADALFIPRENPRALVIRPVQQWSSRDKSILPKEQRPTAPLHD
SQ  NGKSPDMATDAANHDRNGNGELGATGERIHTSVNANQKPNGTTRSDQASEKERPYKTLSGHRAGEAAIVYEHGADIEALM
SQ  PKLRQSDYFTEPRIQELAAKERADPGYCRRVRDFVVGRHGYGSIKFMGETDVRRLDLESLVQFNTREVIVYMDESKKPAV
SQ  GQGLNKPAEVTLLNIKCIDKKTGKQFTEGERVEKYKMMLKKKAEAQGAEFVSFDPVKGEWKFRVEHFSSYKLGDEDEEDG
SQ  V
//
ID  P47054;
PN  Nucleoporin NUP192;
GN  NUP192;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution).
DR  UNIPROT: P47054;
DR  UNIPROT: D6VWE4;
DR  PDB: 4IFQ;
DR  Pfam: PF11894;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs. {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:11121302}.
DE  Reference Proteome: Yes;
DE  Interaction: P34077; IntAct: EBI-12056,EBI-25846; Score: 0.55
DE  Interaction: P35729; IntAct: EBI-25846,EBI-11713; Score: 0.37
DE  Interaction: P40066; IntAct: EBI-22648,EBI-25846; Score: 0.27
DE  Interaction: P40069; IntAct: EBI-25846,EBI-9166; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-25846; Score: 0.35
DE  Interaction: P32472; IntAct: EBI-2883297,EBI-25846; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-25846,EBI-8591; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-25846,EBI-24570; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-25846; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-25846; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-25846,EBI-8659; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-25846,EBI-8571; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-25846; Score: 0.53
DE  Interaction: Q05166; IntAct: EBI-25846,EBI-3035; Score: 0.55
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-25846; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-11178,EBI-25846; Score: 0.35
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-25846; Score: 0.59
DE  Interaction: P49687; IntAct: EBI-25846,EBI-11730; Score: 0.59
DE  Interaction: Q03790; IntAct: EBI-27321,EBI-25846; Score: 0.37
DE  Interaction: P02994; IntAct: EBI-25846,EBI-6314; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-25846,EBI-24471; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-25846,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-25846,EBI-18976; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-25846,EBI-7218; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-25846,EBI-11191; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-25846,EBI-2218; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-24359,EBI-25846; Score: 0.27
DE  Interaction: Q06625; IntAct: EBI-37861,EBI-25846; Score: 0.27
DE  Interaction: P43587; IntAct: EBI-22913,EBI-25846; Score: 0.35
DE  Interaction: P47087; IntAct: EBI-26303,EBI-25846; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-20939,EBI-25846; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-7635,EBI-25846; Score: 0.32
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
GO  GO:0046822;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKWSAIPFQTLYRSIESGEFDFDLFKEVLPDLQNLNLNTDKLKNNASRSQLEKGEIELSDGSTFKVNQEFIFEAISLSDE
SQ  LNLDEIVACELILSGDTTANNGKVQYFLRRQYILQIVSFIVNCFHEDTELYQELIKNGALVSNILSAFKFIHTQLSEIKQ
SQ  QINKAQILENYNALFQQNIKFRRDFLLREYDILSQILYGLVDKGAIMKNKDFILSLLHHVSELDSNDFFIIYYTPAFFHL
SQ  FASLRVLPDADVKLLHSQFMKDLKDDSIYTKPVKVALIFIFFAYFIGWCKEDPKRRADTMDFKTDVDEPMTSAVELGAIE
SQ  QILIFAADTSIVEQDKSMELFYDIRSLLERHIPRLIPKQLLDDEKIFSQTTNSTYNPASATDNMSGRGLWNPSYPGMMST
SQ  TGTARLNSMPNNVNEYSYTTIVLSDQTQEFFLSSFDDVLQTIITDCAFLLTKIKDAEEDSLLSGEDLTLDDISLKADLER
SQ  FFLSIYFFYASRPEYSCTFWSDKESNAYGFIEWCSRCNDNLMRSCFYLMVSSLSFGPENALNVYHYFGENSSISWKNIAQ
SQ  CLSDYTKKISNFNSSLHKRQQFSESTHNDIDSTAVALEEGLNEEAVIFLSSLLTLVGSVTYQVDEDVKSSLSKVFSDVLF
SQ  EFTKINTPLVGAAFKVISNLVPKLESSRTKFWSFLDSLIFKDSSLNYSSESYRNAFTNVLTKYSDVLGFLQLFHNLISIH
SQ  SRENNSEYMVFGKLAFPTRLGQGYRKVGIWPYFDYIFNDILAHVDQIVDIRNKRAVQLPILKIIYTGLCSFDYSVILNSI
SQ  PAAANLDALVDCENFFNYVQECPAIPIFNYIFTEKIYKSIFNVVDVGVDQLSIELEGGKNQAELLQLAVKIINKVLDYQE
SQ  TYVEELFPIVKKHGKTDYFLPKNYSLHGLRSFYDAIFFNIPLVAHLGLYVGVDDQILATNSLRILAKLSERSNGSVASLS
SQ  KRNKLLTIFDSVDESARIKDAFITQLESSITDAGVLALKLELLDFLTSNLSNYSRTMTISHLLLGFQVSNVISLGPNLAT
SQ  FISSGTSLLDSLISVLEASLNSITKDNIDYAPMRLATAALEIILKLCRNPLTSGLLYSYLIKENFFERIMILDPQVTRFT
SQ  TWNGSPFDNSTEEKCKNFIESESVGAFLSFLAYRNYWTQYLGLFIHKISFSGTKSEVLTYVNYLISNTMYSVRLFSFLDP
SQ  LNYGNICEPKETLSIFTNVPLNLEQVTLNKYCSGNIYDFHKMENLMRLIKRVRAESLHSNSFSLTVSKEQFLKDADVECI
SQ  KAKSHFTNIISRNKALELNLSVLHSWVQLVQIIVTDGKLEPSTRSNFILEVFGTIIPKISDYIEFNITFSEELVSLAVFL
SQ  FDIYNRDRKLITDKGTVDGRLYQLFKTCIQGINSPLSSVALRSDFYILANHYLSRVLSDQVGSEKVLQDLRLGSKKLVEI
SQ  IWNDVVYGEGTSRVTGILLLDSLIQLANRSKENFILDSLMKTTRLLLIIRSLKNTDALLNSTTEHINIDDLLYELTAFKA
SQ  TVFFLIRVAETRGGASALIENNLFRIIAELSFLKVDPDLGLDLMFDEVYVQNSKFLKVNVTLDNPLLVDKDANGVSLFEL
SQ  IVPIFQLISAVLVSMGSSNKAVVQTVKGLLNTYKRLVIGIFKRDLLREKEDKKNSSDPNNQSLNEMVKLIVMLCTLTGYQ
SQ  NND
//
ID  Q12063;
PN  Dehydrodolichyl diphosphate synthase complex subunit NUS1;
GN  NUS1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:11086160, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q12063;
DR  UNIPROT: D6VRG0;
DR  PDB: 6JCN;
DE  Function: With SRT1 or RER2, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). {ECO:0000269|PubMed:25066056}.
DE  Reference Proteome: Yes;
DE  Interaction: P15108; IntAct: EBI-34546,EBI-8666; Score: 0.56
DE  Interaction: P32589; IntAct: EBI-8648,EBI-34546; Score: 0.35
DE  Interaction: Q04432; IntAct: EBI-35591,EBI-34546; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-34546,EBI-8659; Score: 0.40
GO  GO:1904423;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0016765;
GO  GO:0019408;
GO  GO:0006486;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTMIKKDDKAMEPPNEKPHRKIERDDVPESSNHIPPPESGVLKGGKVNSKTRALKAVTSIIADADENPQKKVNNETNGV
SQ  QKQKTEDLSKRIGKFEYLFYKFLLVLLYICFGLFRYGQYQYNKMKLRIFSIIYNHAYTPQLIRQDVIPLKKIPKRLAAIL
SQ  EVKPVGDVGGGVTGLLNDASEIVCWTVSAGIKHLMLYDYDGILQRNVPELRMEIHSNLAKYFGPAHVPNYAVKIPHSNKI
SQ  FYNLDGIETETDVGNEIEANQEKDKIAIEISLLSNRDGRETIVDLTKTMAELCAVNELSVSDITMDLVDSELKQLVGPEP
SQ  DLLLYFGPSLDLQGFPPWHIRLTEFYWEKDNNEVIYSVFIRGLRQYAGCKVNVGK
//
ID  Q9VWE6;
PN  Protein ELYS homolog;
GN  Elys;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:28472469}. Chromosome {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:31784359}. Note=Interacts with chromatin. {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9VWE6;
DR  UNIPROT: Q95TR2;
DR  Pfam: PF13934;
DE  Function: Component of the nuclear pore complex (PubMed:28366641, PubMed:29773558). Binds to transcriptionally active chromatin including regulatory regions (PubMed:28366641, PubMed:31784359). {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:29773558, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-91923; Score: 0.35
DE  Interaction: P31007; IntAct: EBI-389374,EBI-91923; Score: 0.35
DE  Interaction: Q9VUH7; IntAct: EBI-149500,EBI-91923; Score: 0.35
DE  Interaction: Q24276; IntAct: EBI-91923,EBI-167469; Score: 0.37
DE  Interaction: Q961V9; IntAct: EBI-91923,EBI-466296; Score: 0.37
DE  Interaction: Q9VHC7; IntAct: EBI-91923,EBI-188505; Score: 0.37
DE  Interaction: Q9V470; IntAct: EBI-91923,EBI-85683; Score: 0.37
DE  Interaction: P49657; IntAct: EBI-91923,EBI-466373; Score: 0.37
GO  GO:0005694;
GO  GO:0005643;
GO  GO:0003682;
GO  GO:0031490;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEWHEVELDGSRTIAFPERIVPGFGREPSAHLDAAEYLGGIIRDGQWGWVTWRYGSDATLLVCSMSTGDYLSWHCFWSES
SQ  DDLGPRKSIRCVEELFPGEHERPAMLAICLESWNSGDQRPIDCPLSTQVLIYAIRNSQVLRRFDLHGITCSALTFLDKRI
SQ  YGLTRLRRFKGCLAVATEEGTVLLVDLNSDSLQASTQRRSLCSPSSKDEPSDGNLYFVSSEESKRQLSSKLTHCRSKGAH
SQ  LAVRMDVASIGISCLMGISMAPGYAAGLEDGRILIYDLINFDVTTDLNSPVKRKGVNRAVKRMCLIMPPDDPKPCFYICA
SQ  LYQNIDVLQMMLHSVCYRGSYRDRETHTIRFKDYRSRTVRNRQILDGGICSVIGCATASTFSFAGDNGTLLIVISWHSSA
SQ  DKKNKLVLFDINQWYKDEMPTSVHKNEVPNYMSGYILSGLQTGLALDLRSTTILHFVSLQRYDEHFYPNSLTFDCSLLTP
SQ  TGKRYYAQDGVQHRFLNALRCDRATLFLRPQIYHEDIVRLRLLPQFCELNPNATFSKIAMYELILSVALEHNCGALLNDC
SQ  ARSWMDGSFLCNMIDNTQLSLSTLTNWILKRAGQIKTRCSELCHGIFDYGGYPLDQRERREFQVLSGQLRELVRLQSYIV
SQ  EQGRRRLTSSILDDCRANERALKTVLEYQRVLLWFIDHGLLPEGQHMDNLVPGEQAFVRLQHEYSEKRAQGKILYIDSLG
SQ  KRASFPEPYPPDSLHAYIHLMLSPDIELCHKHALILYLLMDLNQQLVGRFQIAFQLDKDLATSLRCFWYLDHGDYERGVE
SQ  ELYKEPAPAKNLKSWQMRLLIDKLLAEGAVKAAKKVVSRPPGPLSSALHMKVLLANENITEAFQIARLDDDEDGQPLLER
SQ  FFRHCIEIRRFKVLAELYLREPEERLLYSLLRQCRSRQTDCVQLIMLLQKSKFIEAVSFMDEVAAERERDESSNTILPAY
SQ  SATMGPVTQNIAGTYLRIRDTLEPYQKTGPLEPFSCQLVKQNASGQLGGIFQSSAVSAHWATQCESPPKMTPVSIQSKIG
SQ  YTNVPFLRHAQYGHSELPLPRRIVKPVPHQVVEKRQRELEDQRTNLQDQRQLGTERPNKRPCLMVERMVEDVKDYVRSIR
SQ  EKSSNQMEQEEVKQNEATNLLQPPNFLQARQSTTIRQSSSSPQPIPPILKGSGAVDAVKRAPPVATFTALAGPKRFRFVP
SQ  PIPLRTDKSDKSTEMGSEGAAEGEEETDEIIVEIESRSEPRSACSYESDEEDEFLSPLVSANVSLVDPVPSRNSPHYFAP
SQ  PAGPQPRNSLLHGGNGSGSKIGTATGSESSSGFGSFSTVQPAQTSSHSQFVPTVCSSKMGETQSQVFSSGSCGIKISERT
SQ  TICGEMESTDLGAELTAAPSAQWSLPSARPAIQGHHQMMDTTLGMSTYDVASLEQQDTQDVENEEELKLGDTKSLEEQQN
SQ  PQDEQKPEQEQDQDEDQAQEPLATGGQLAFLSNSEGTAQEPLSSPIYSLSSEDSNVSSAGIRNPMLPTLHTDDPMYSIVV
SQ  ESPGSITTSRSVTHTPTSFLPSDTNVSQTSSPQAPHGEDGDGTPISLYRANSLETVDDLDTTKGSLEEEEEYDDDDCVIA
SQ  LDGTEVRGYVARPQQSAASSSAELFAFKDECQEEAAGVPSPFLSLGATVNSDSDVADTIVLDSDEETAKEKDTQPEQRKD
SQ  WPMEEETPSNESVATVEFSEQKQPRADMDIGMEVDAVPDVLEVLEVPEMEPLPVLSDVDIEMAVDEVPNVLEVLEVPELE
SQ  PLPAGQATQSSGLGEIPEEDVDAEAEEQVVVKVEHVADEQPKEGDKTESKEASEEETQHNPEPLLPEEEDSRHSLKLIFS
SQ  GDEDEEEQDVPTRAIHTLRPRRSFTEHQDSPRTLRPRRVSQEHRDSPTPVAGRTMSLRSTDAPTLSPASNPPVSTPKRRG
SQ  LQHKYLLEVIDEHSPSDLSLPRTRSRTRLSVDSEATSSRPGTPTMTKARGKRATSQAPPTASPSVRRSLRGHSEPPAALS
SQ  AQLVRKPKTARAGVRSRKTSSGVQSPVAVSPTPIDAPIDVPDSTAPEEEQPRLRRTARRRISELSDQSANGTGDLRSEAS
SQ  SSRTGSKSNSAASTQNRELRPRLRRTSKSEH
//
ID  Q8RWH9;
PN  Nuclear pore complex protein NUP58;
GN  NUP58;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:23840761}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RWH9;
DR  UNIPROT: O23173;
DE  Function: Involved in nucleocytoplasmic trafficking. May have regulatory roles in the gibberellin pathway, in auxin signaling and in light perception. {ECO:0000269|PubMed:23840761}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFFPPQQQQTPQPLFQTQQTSLFQPQQTNSIFSQSQPQQTNSIFSQSQPQQTNSIFSQPQQQQQTSLFQPQQFQQQQQQ
SQ  LNQQQQQQVQQQLYLFTNDKAPANYSTKWADLHPDSQKLLLQIEEKILEHRSESQRLDQCSRLYDSSVSSEGFEFDASRI
SQ  VQELGGINTAMDRQKAVLHELMIVAKDMLRNAEIAVRSFMMLQPRFPHWKQGGGVVSVGSQPSQGQGTNPAPASSGQQQA
SQ  VTTTVQVSDFYRGIPKKPTAFLLQTVVRFEKYLNECRQWVEELEQLLALDSDKYSRHASLLESLPKVMSNVHDFFVHVAA
SQ  KVESIHQYIESMRTSYLADQRRRGECHDPFLEADRRETAKQEAAAKRVHPTLHLPASTTSTQPSTQVAGLIASSATPGGS
SQ  NPPQTSVPTSNPSSGAGFSFLNTPASGPSSSLFATPSSTAPTSSLFGPSPTPTQTPLFGSSPASTFGSTQSLFGQTTPSL
SQ  TMPSQFGGATPGSGASFGSMTKSSRPKSRTTRR
//
ID  Q9W1F4;
PN  THO complex subunit 5;
GN  thoc5;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:28472469}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q9W1F4;
DR  UNIPROT: Q95RL0;
DR  Pfam: PF09766;
DE  Function: The THO complex is required for cell proliferation and for proper export of heat-shock mRNAs under heat stress. {ECO:0000269|PubMed:15133499}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y091; IntAct: EBI-101869,EBI-15143944; Score: 0.49
DE  Interaction: Q8SY07; IntAct: EBI-173458,EBI-15143944; Score: 0.49
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0000347;
GO  GO:0000445;
GO  GO:0000346;
GO  GO:0003729;
GO  GO:0007140;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0032786;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METILNTQFDQLQKAIEGIKEAKSKGQSTDEARIATTLMFVALKHANREVKHKIKAGRDKLHLEKCKVDLSRLQLQNLLY
SQ  EVSHLKKEIVRCQKFKSRDTSLELLSEAEYSSELPDMPNDAEELSSHKQHLHRLDCELRLRKALDKQYSALLSSKQELLQ
SQ  DNLSHAQRYVSFAPALRTLQSATKPLHDALQLSLDVEWKLSAVVKYLPKPLYVLFIVLQSLQRVSEEQSFTAEVVGYESE
SQ  AQMQELLKEKKCSTLNYRQTKKESGDREKIADKNNLDDSLAPHPLHICLTIGAAGSNQLVLQIRYFDFIKCATVWGQLNC
SQ  SRNANGQGDTNFVHHLLRHLYPNDLGNELPIPGIQYELRSSDLTAEECVRYLKAKDYGKPFCWLQSMCSIATVNSSMLYK
SQ  HELNLNKNNKEIIDRIARRLNSWQRLSQQIRGLTFKDIDLYSLQENIYPAGLSCSLVQWTAITHEELHSQISDALNSSSA
SQ  DKGITYNSYRAVIVRGSAKMECFIRIPSNYPLEMPLWILNVHWNGCLTAQNNSAIKMMEFWTNSLQPKHLEPNDCILYAQ
SQ  LFRTIYSFDIFLETEGSMQNTIEYNKEKPYISAFAKRSRSRPYKYIKKGSVYAFKQ
//
ID  Q9FFK6;
PN  Nuclear pore complex protein NUP88;
GN  NUP88;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19700630, ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:19700630, ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9FFK6;
DR  UNIPROT: Q0WPM6;
DR  Pfam: PF10168;
DE  Function: Involved in the regulation of exportin-mediated nuclear protein export. Required for resistance mediated by multiple R proteins and for the appropriate nuclear accumulation of SNC1 and of the downstream defense signaling components EDS1 and NPR1. Not involved in salt tolerance, ethylene and auxin responses, but required for systemic acquired resistance. {ECO:0000269|PubMed:19700630, ECO:0000269|PubMed:21327081}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0045087;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0009627;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKFNFNETEDAPDSRRSPTPKEPVRWVPLQSHPVFASLPSSQDEPAVSQLFPRNFMAWDGDSRVYYWDSRRYLLHRLSLR
SQ  LGEPEPSSVLAAVPSKVMQPDLQVTFSVSKISINKSGSAVLLAGSDGICVMYLFGRASVIEDNVICRVVSIGSEIYTSSD
SQ  SAITLLQASWHPDSDTHLGILSSDAVFRLFDLSSDTELPEQEYYLQPGEPGRSRTASSIYPADFSFGGDHLWDRFTVFIL
SQ  FTDGSIYILCPVVPFGSVYKWESVMEIYNDANMYGVKSSNSLAVSNSSLAIEWLEATFPDLTEQGTRGENILVVKAQPYA
SQ  LLDASLALQGPLYKASSGDGDEDFAVREAECKGRAVSLLYNLVSKDSILVTAWSAGQLQVDALVDEIQPVWISGNSSRLR
SQ  MNSHNKIQGVAMICESNISELPVATSNLPLDHTVWLGHPPPLLRLAMVDLALPKMREGGSLVTLFADSLLPERIYSLHDG
SQ  GIDSTVLHSLPFTSQASGKDEALKTPSVHTVLSTCQEESAVSPLLGFVPLSDSFGYSWIVAVLSSGECIVAEMKTWDLLL
SQ  PIHVSTDKTVSSSAIEKKEQENSCIISKELLAGPKIRIAPHALPNQRSTPANSVEGRSILLDYVKLFHENYIEYAHKVHF
SQ  ELQHHAPNLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLRSLPGTHKKPLTRAELDFKSEL
SQ  DQYAGVEVDALQSSIETLRARVKKSTQKSHKGTVVAASQKKQYSKKNLIQDTQMSQLQSTLAKLSLMNSDNSKKVKIVES
SQ  ALKSQESSFM
//
ID  P20484;
PN  Protein MAK11;
GN  MAK11;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:2826479}. Nucleus membrane {ECO:0000269|PubMed:2826479}; Peripheral membrane protein {ECO:0000269|PubMed:2826479}. Note=Membrane associated.
DR  UNIPROT: P20484;
DR  UNIPROT: D6VXR4;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Essential for cell growth. Plays a role in assembly of 60S pre-ribosomal particles in the nucleolus. Also required for replication of the M1 double-stranded RNA of the L-A virus. This latter function may reflect an enhanced requirement for free 60S ribosomal particles for the translation of viral mRNAs which lack poly-A tails. {ECO:0000269|PubMed:12808088, ECO:0000269|PubMed:2826479, ECO:0000269|PubMed:7739558}.
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-8591,EBI-10930; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-10930; Score: 0.35
DE  Interaction: Q06511; IntAct: EBI-34602,EBI-10930; Score: 0.57
DE  Interaction: P0CX43; IntAct: EBI-10930,EBI-7433060; Score: 0.35
DE  Interaction: Q07915; IntAct: EBI-10930,EBI-35766; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-15881,EBI-10930; Score: 0.35
DE  Interaction: P53136; IntAct: EBI-10930,EBI-23920; Score: 0.35
DE  Interaction: Q12024; IntAct: EBI-10930,EBI-29589; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-10930,EBI-6314; Score: 0.53
DE  Interaction: Q05022; IntAct: EBI-10930,EBI-16011; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-10930,EBI-15394; Score: 0.35
DE  Interaction: Q03532; IntAct: EBI-10930,EBI-8170; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-20589,EBI-10930; Score: 0.35
DE  Interaction: P39014; IntAct: EBI-10930,EBI-11507; Score: 0.37
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0000466;
GO  GO:0000463;
GO  GO:0000027;
GO  GO:0042273;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:2826479};
SQ  MSAIGDKNQFRIIVGSYEHNILCLSLDIPNQKENDAAKTPHFMPIFHFQAHSLSIKCLAVSRRYLVSGSNDEHIRIYDLQ
SQ  KRKELGTLLSHQGSITALQFSHPASSSEDAAVSKGSKNSKWLLSASEDHKIMVWRVKDWETVGTLKGHTARVNDVDIHPT
SQ  NRIAISVSDDHSIRLWNLMTLRNAAVLKLRKYNTNGTCVRWLGAKGDYFAVGLRDRVLIYETGSAKVFKEIVFQRKTLMH
SQ  IETHILPFDNKEYLSVGISDGNVHFYPCEELFEKVEENEKQEDDDDKEDISPAFSLLGHTNRIKDFKFYTNEFGTYLVTI
SQ  GSDGKIVVWDMSTKEQVAVYDCGERLNCLTLCDESIEKYNTMKKRDAETADIGDQSEVESDTEELKKIMFGEKKKLNKKK
SQ  RKQLKKSKVSVELE
//
ID  Q5XVI1;
PN  Protein SINE1;
GN  SINE1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5XVI1;
DR  UNIPROT: Q1KS90;
DR  UNIPROT: Q9SLJ5;
DE  Function: Plays a role in nucleus positioning in guard cells. {ECO:0000269|PubMed:24891605}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0032797;
GO  GO:0003779;
GO  GO:0000387;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLNLNPILRQELANLDKDTESRKSAMKALKSYVKDLDSKAIPGFLAQVFETKETNSLSGEYTISLYEILARVHGPNIVP
SQ  QIDTIMSTIVKTLASSAGSFPLQQACSKVIPAIARYGIDPTTTEDKKRVIIHSLCKPLTDSLLASQESLTSGAALCLKAL
SQ  VDSDNWRFASDEMVNRVCQNVVVALDSNSNQTHLQMGLVMSLAKHNPLIVEAYARLLIHTGLRILGFGVSEGNSQKRLSA
SQ  VQMLNFLMKCLDPRSIYSEVELIIKEMERCQSDQMAYVRGAAYEAMMTSKRIAAELESKMEKGCRSVTGSNFSRRNCSSI
SQ  VPDYSLSPESQTLGSFSGYDSPVESSPISHTSCNSEFDRRSVNRKLWRRDENGGVVDISLKDGLFSRVTKGSTTVSDSPL
SQ  VPYDTCENGDEFEGFLMESLRNTTPSPQRQRSRRINAEDFNIFSTPRKLISSLQYPDDVDLDHSDIQSPILRGEREKTIG
SQ  SRKNPKLRKQFPTMVETMSSTITVSEDTAQTQMITGKKKKKKMSYAKLVIAISFVVVALFATVILMVNQDDDVGYYTVPT
//
ID  Q3ZC98;
PN  Nuclear pore complex protein Nup85;
GN  NUP85;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q3ZC98;
DR  UNIPROT: A7E3X3;
DR  Pfam: PF07575;
DE  Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0017056;
GO  GO:0030032;
GO  GO:0048246;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEFDGEPTVTWIPGVNSQKKQMCFDWGPGEMLVCETSFNKKEKSEMVAGCPFIHIIRKDIDVYSKILRKLFNESHGIFV
SQ  GLQRIEEELTGKSRKAQLVRVSKNYRSVIRACMEEMHQFAVADKDSAIGRQFSSQVSILSAVELIWNLCEILFIEVAPAG
SQ  PLLLYLLDWVRLHVCEVDSLSADVLGSENPSKHESFWNLVTTLVLQGRLDEARQMLSKEADSNPTSAGMCRVLGDLMRTM
SQ  PILSPGNTQTLTELELRWQHWHEECERHLQDGTFASNPHLESLCKVLLGDDAALLEHKELLSNWYHFLVTRLLYSQPTVK
SQ  PMDLHLYAQSSLDLFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMRE
SQ  FLLLEYASGLFAHHSLWQLGVDYCDHCPELGRVSLELHIERIPLTTEQKALKVLRVCEQRQMTEQVRSICKVLAMKAVRN
SQ  NRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKCFVDAASLL
SQ  LSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELLRCLEDLTSGRPLCGEPDAQQLQDDDIETTKVEILRLALA
SQ  RNLARSIIKEGSLEGS
//
ID  Q54EQ8;
PN  Nuclear pore complex protein Nup96;
GN  nup98;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Nup96 is localized to the nucleoplasmic side of the nuclear pore complex, at or near the nucleoplasmic basket. {ECO:0000250}.
DR  UNIPROT: Q54EQ8;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The repeat domain in Nup98 has a direct role in the transport (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0008139;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFGGQFGSFGAKPAATASPFGAPSAAPTTSLFGSTAPSSGFGGFGSTAQTTQPTTGGFGGFGGFGGATTTQQPAASPFGG
SQ  GGTGGSGLFGSSAQTTTQQPGASPFGGGFGTTTTTTTQQPGASPFGGTGGGLFGSSAQTTTQQQGASPFGGFGGATTTQP
SQ  SLLSGATGGFGGFGGSTTSGTQLGGGGGATSGAFGGSSSPFGGSGGATTSSPFGGGGGSFGATTQKQYGTPIPYQQTTIE
SQ  GNTFVSISAMPQYNDRSFEELRFEDITHRKDIVYKTGGGSGGGNSLFGSTPTTQPSSPFGAQTTTQTTGGLFGGQTTTSP
SQ  FGGQTSATPGSSLFGSTQPTQQQTSGGLFGSVQPTQQQAGGGLFGSMPSTGGSSLFGSTQPTQQQTGGAQPTQSLFGGQT
SQ  QTTTSPFGSQTSTPFGQPQQTNTGSGLFGAQQTQQTNTGGGLFGAQPTQQTSGGGLFGTQPTSGTGLFGTSPTAGGTGLF
SQ  GTTQPTSQGTGLFGTTQPTTQGTGLFGTSPTSGTGLFGSTPTSGTGLFGSTPTSGTGLFGSAQPPQNQQSQTSLFGNTGT
SQ  GATNTGTGLFGSAQPSSNPGGGLFGSAQPSTTTGGLFGSNQPTAQPTTSLFGNTTGSVGGLGATPNITSGLFGSNPAQTG
SQ  GLFGSTQPTTQTSLFGNTGSTGGLGAQNGGGLFGNLSQPTATAGQGLSGGLFGNLSQPTATAGQGLSSGGLFGNTLLGQP
SQ  STQGLSSALPTLGLGLMGGQPQQTQQLPQGSLMLQQTQQPLQQQPLQQQQQPLQQSTIQLNNQINSASPYFPISSPAPFA
SQ  TFVKDLTSTSKVVSPPSYTQRSLSHHGYIPKSTTKLVPRRGPNNVDLGFSVIQNQNGLFPIDKFITKHSKSLNINTTNET
SQ  EDTLRSLNTKSSSLFNNNNNNNNNNNNRNVNTNVNDYQNNGLPSSSLYNSNINQLSNNNNNNNNIYNNNNNNNINNNNNN
SQ  NNISTQFNLRNNQSSSDNLNNDKSLSSSSSNKSQQQQQKEQKEEQPPKPIKEKEFINPNAPKLTRDGYQCVPSIKELSKK
SQ  TDKELSSVQGFTISRDGCGSIYFPGSTNLVALDLDDIVDIEPREVSVYKDEETKPEIGYGLNRDAVVTLENCWPKNKNGE
SQ  VVKEDGTILDKYENALKKVSAKSDCGFVSYSRSNGTWVFTVKHFSKYSAPDFDEDDQQMQQQTQQKQQQTQPSKVTFQQP
SQ  STKLTKPKFTANLDNFDSDSETSSGDENQDEMVPQKKTPFIKRVSNRESGLFDTPSVVPMSEKIETTPSKIARVSEPTSQ
SQ  SSRMSNNALKFSTFNPQQQQLQSSRFKSTGLSILSNPVKNLIQSDVNNEQSMFSNTTTTSTTRIQPLPSQQHLVQPIPTT
SQ  ISLNKNYFSKVRIDPQVYDRIVPKEESITNQYRMKNERLNHSTQDVSLFMRRSFRVGWAPGGKLISITKSSFKNLLIKKL
SQ  PTDTKEDKKESIIKFLKNHHSHSSLVPENLKSIGWFSISNVQEQIESQLTLNVPSSQSVYYNRIWSLISNLWGNVLKGNG
SQ  SKYINTNYSEDTIRKLNLNQWLKDVIAPLLRDEMDSLRKKTNSNYLEQIFSYLSAKQIKEASDLANENKDFRLATMMSQI
SQ  WSSSESGKELILKQLTTYHSNGSDEFINEKRLEILHLIAGSVNKIYKNLNDWIRCFAVSFWFKYSLEYSIEDSVENFERS
SQ  FNAHRSVYPLPPYLIKSTSTNSKQIEEQQHYYDICFLLLKLFAVNRGSSHFDKFKNIFYPENIGQDLLDYHLSWNLYTVL
SQ  KSIPSLNKQPDLVNASNLHSSFALQLERLGLWQWSIYVLLHTPDQSNHVREEAVKSLIARAAPVITSEDRVFLTTKLHIP
SQ  EIWIDEAKAWYSGYDCNNDIYDQIDALFKSYQYTKIHDIIFSNIGPNYIIQKRYHSLKDLLIRLEPHSSFISTWRYGGSI
SQ  FLEFADICIQYKEILSQLSNTAEEIQRTKYYVNLKDITTRIVNILSDISKITQSSEIKNTSASYKQSLSFMSEALITKAS
SQ  LLRDLPESIVKLVSTNNLVSTLNSLPLTQDYRSKNLESLTDQIQDTLLNSIYQ
//
ID  Q39134;
PN  Amino acid permease 3;
GN  AAP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15361541}. Nucleus membrane {ECO:0000269|PubMed:15361541}. Endomembrane system {ECO:0000269|PubMed:15361541}. Note=Not found in vacuole membrane.
DR  UNIPROT: Q39134;
DR  UNIPROT: Q8LE75;
DR  Pfam: PF01490;
DE  Function: Amino acid-proton symporter. Stereospecific transporter with a broad specificity for GABA, tryptophan and both neutral and basic amino acids. High affinity transport of cationic amino acids. {ECO:0000269|PubMed:7608199}.
DE  Reference Proteome: Yes;
DE  Interaction: Q39222; IntAct: EBI-16894298,EBI-4463452; Score: 0.37
DE  Interaction: Q84N34; IntAct: EBI-1810738,EBI-4463452; Score: 0.37
DE  Interaction: Q8LAA6; IntAct: EBI-4440607,EBI-4463452; Score: 0.37
DE  Interaction: Q9SHI7; IntAct: EBI-4476710,EBI-4463452; Score: 0.37
DE  Interaction: Q9LSP7; IntAct: EBI-16895382,EBI-4463452; Score: 0.37
DE  Interaction: Q9FN48; IntAct: EBI-7889805,EBI-4463452; Score: 0.37
DE  Interaction: Q9FNH6; IntAct: EBI-4461284,EBI-4463452; Score: 0.37
DE  Interaction: P57752; IntAct: EBI-2008339,EBI-4463452; Score: 0.37
DE  Interaction: F4I1Z0; IntAct: EBI-16882439,EBI-4463452; Score: 0.37
DE  Interaction: Q9LPN5; IntAct: EBI-6392819,EBI-4463452; Score: 0.37
DE  Interaction: Q9C7D7; IntAct: EBI-16893154,EBI-4463452; Score: 0.37
DE  Interaction: Q8GW19; IntAct: EBI-16897007,EBI-4463452; Score: 0.37
DE  Interaction: O04265; IntAct: EBI-16897382,EBI-4463452; Score: 0.37
DE  Interaction: O64852; IntAct: EBI-16882559,EBI-4463452; Score: 0.37
DE  Interaction: Q8RY98; IntAct: EBI-4452570,EBI-4463452; Score: 0.37
DE  Interaction: Q94F23; IntAct: EBI-16891935,EBI-4463452; Score: 0.37
DE  Interaction: Q9FJB4; IntAct: EBI-16890988,EBI-4463452; Score: 0.37
DE  Interaction: Q93Z82; IntAct: EBI-16897870,EBI-4463452; Score: 0.37
DE  Interaction: Q9LHA6; IntAct: EBI-4430467,EBI-4463452; Score: 0.37
DE  Interaction: Q1JPM5; IntAct: EBI-16884610,EBI-4463452; Score: 0.37
DE  Interaction: Q8L8T2; IntAct: EBI-16890309,EBI-4463452; Score: 0.37
DE  Interaction: Q9LVU1; IntAct: EBI-16889489,EBI-4463452; Score: 0.37
DE  Interaction: Q8L9S0; IntAct: EBI-16889232,EBI-4463452; Score: 0.37
DE  Interaction: C0LGW2; IntAct: EBI-16888393,EBI-4463452; Score: 0.37
DE  Interaction: Q9SVG8; IntAct: EBI-16888161,EBI-4463452; Score: 0.37
DE  Interaction: Q9LMN8; IntAct: EBI-2320063,EBI-4463452; Score: 0.37
DE  Interaction: Q9AST5; IntAct: EBI-4448696,EBI-4463452; Score: 0.37
DE  Interaction: Q8H129; IntAct: EBI-16886692,EBI-4463452; Score: 0.37
DE  Interaction: Q944J0; IntAct: EBI-16885927,EBI-4463452; Score: 0.37
DE  Interaction: Q9C835; IntAct: EBI-16885299,EBI-4463452; Score: 0.37
DE  Interaction: F4JN35; IntAct: EBI-4463452,EBI-4426607; Score: 0.37
DE  Interaction: Q94F58; IntAct: EBI-2319707,EBI-4463452; Score: 0.37
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0015171;
GO  GO:0015293;
GO  GO:0003333;
GO  GO:0015802;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVQNHQTVLAVDMPQTGGSKYLDDDGKNKRTGSVWTASAHIITAVIGSGVLSLAWATAQLGWLAGPVVMLLFSAVTYFTS
SQ  SLLAACYRSGDPISGKRNYTYMDAVRSNLGGVKVTLCGIVQYLNIFGVAIGYTIASAISMMAIKRSNCFHKSGGKDPCHM
SQ  NSNPYMIAFGLVQILFSQIPDFDQLWWLSILAAVMSFTYSSAGLALGIAQVVVNGKVKGSLTGISIGAVTETQKIWRTFQ
SQ  ALGDIAFAYSYSIILIEIQDTVKSPPSEEKTMKKATLVSVSVTTMFYMLCGCMGYAAFGDLSPGNLLTGFGFYNPYWLLD
SQ  IANAAIVIHLIGAYQVYCQPLFAFIEKQASIQFPDSEFIAKDIKIPIPGFKPLRLNVFRLIWRTVFVIITTVISMLLPFF
SQ  NDVVGLLGALGFWPLTVYFPVEMYIAQKKIPRWSTRWVCLQVFSLGCLVVSIAAAAGSIAGVLLDLKSYKPFRSEY
//
ID  P0CQ86;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: P0CQ86;
DR  UNIPROT: Q55NB1;
DR  UNIPROT: Q5KBP4;
DR  UNIPROT: Q5KBP5;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAG
SQ  ASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLM
SQ  KGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVIDQ
SQ  IGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLP
SQ  PNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVT
SQ  ADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETY
SQ  IHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA
//
ID  Q9H1E5;
PN  Thioredoxin-related transmembrane protein 4;
GN  TMX4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0L0}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q9H1E5;
DR  UNIPROT: Q8N4P7;
DR  UNIPROT: Q8NCC1;
DR  UNIPROT: Q9UJA1;
DR  UNIPROT: Q9ULQ8;
DR  Pfam: PF00085;
DR  PROSITE: PS00194;
DR  PROSITE: PS51352;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P10588; IntAct: EBI-2681496,EBI-2685885; Score: 0.40
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-2685885; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-19027521,EBI-2685885; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-10267100,EBI-2685885; Score: 0.35
DE  Interaction: O14944; IntAct: EBI-17272224,EBI-2685885; Score: 0.35
DE  Interaction: Q969P0-3; IntAct: EBI-21535887,EBI-2685885; Score: 0.35
DE  Interaction: Q9UN42-2; IntAct: EBI-21789418,EBI-2685885; Score: 0.35
DE  Interaction: P28845; IntAct: EBI-3918817,EBI-2685885; Score: 0.35
DE  Interaction: Q8TDX6; IntAct: EBI-13624785,EBI-2685885; Score: 0.35
DE  Interaction: Q01113; IntAct: EBI-3910754,EBI-2685885; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-10249550,EBI-2685885; Score: 0.35
DE  Interaction: Q401N2; IntAct: EBI-21749821,EBI-2685885; Score: 0.35
DE  Interaction: P46098-2; IntAct: EBI-21749217,EBI-2685885; Score: 0.35
DE  Interaction: Q9UHP7-2; IntAct: EBI-21517399,EBI-2685885; Score: 0.35
DE  Interaction: Q8TDD5; IntAct: EBI-6658430,EBI-2685885; Score: 0.35
DE  Interaction: Q9NV96-2; IntAct: EBI-12921610,EBI-2685885; Score: 0.35
DE  Interaction: Q8IZF4; IntAct: EBI-6658275,EBI-2685885; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-2837401,EBI-2685885; Score: 0.35
DE  Interaction: P55290; IntAct: EBI-7205595,EBI-2685885; Score: 0.35
DE  Interaction: P54709; IntAct: EBI-1054481,EBI-2685885; Score: 0.35
DE  Interaction: Q6UWB1; IntAct: EBI-19045531,EBI-2685885; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-6911574,EBI-2685885; Score: 0.35
GO  GO:0005623;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0045454;
GO  GO:0055114;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGRCGPQLTALLAAWIAAVAATAGPEEAALPPEQSRVQPMTASNWTLVMEGEWMLKFYAPWCPSCQQTDSEWEAFAKN
SQ  GEILQISVGKVDVIQEPGLSGRFFVTTLPAFFHAKDGIFRRYRGPGIFEDLQNYILEKKWQSVEPLTGWKSPASLTMSGM
SQ  AGLFSISGKIWHLHNYFTVTLGIPAWCSYVFFVIATLVFGLFMGLVLVVISECFYVPLPRHLSERSEQNRRSEEAHRAEQ
SQ  LQDAEEEKDDSNEEENKDSLVDDEEEKEDLGDEDEAEEEEEEDNLAAGVDEERSEANDQGPPGEDGVTREEVEPEEAEEG
SQ  ISEQPCPADTEVVEDSLRQRKSQHADKGL
//
ID  Q9UND3;
PN  Nuclear pore complex-interacting protein family member A1;
GN  NPIPA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11586358}. Nucleus membrane {ECO:0000269|PubMed:11586358}. Note=Colocalizes with nuclear pore complex protein NUP62.
DR  UNIPROT: Q9UND3;
DR  UNIPROT: O15102;
DR  OMIM: 606406;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P01100; IntAct: EBI-2692961,EBI-852851; Score: 0.40
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFCCLGYEWLSGGCKTWHSAWVINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDG
SQ  STDVQQRARRSNRRRQEGIKIVLEDIFTLWRQVETKVRAKIRKMKVTTKVNRHDKINGKRKTAKEHLRKLSMKEREHGEK
SQ  ERQVSEAEENGKLDMKEIHTYMEMFQRAQALRRRAEDYYRCKITPSARKPLCNRVRMAAVEHRHSSGLPYWPYLTAETLK
SQ  NRMGHQPPPPTQQHSIIDNSLSLKTPSECLLTPLPPSALPSADDNLKTPAECLLYPLPPSADDNLKTPPECLLTPLPPSA
SQ  PPSVDDNLKTPPECVCSLPFHPQRMIISRN
//
ID  Q9M651;
PN  RAN GTPase-activating protein 2;
GN  RANGAP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Localized in patchy areas at the nuclear envelope of interphase cells. During mitosis, associates with mitotic spindles at the anaphase. Associated to the microtubular phragmoplast and the surface of the daughter nuclei at the telophase.
DR  UNIPROT: Q9M651;
DR  Pfam: PF13516;
DR  Pfam: PF13943;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:12061901}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779367,EBI-1779567; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1779567,EBI-1796628; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779567,EBI-1779466; Score: 0.37
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0009524;
GO  GO:0009536;
GO  GO:0005819;
GO  GO:0005774;
GO  GO:0005096;
GO  GO:0006913;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADILDSRPHAFSIKLWPPSLPTRKALIERITNNFSSKTIFTEKYGSLTKDQATENAKRIEDIAFSTANQQFEREPDGDG
SQ  GSAVQLYAKECSKLILEVLKKGPVAKVAARELISEDSVSPRETFFDISKGKRAFIEAEEAEELLKPLKEPGNAYTKICFS
SQ  NRSFGLGAARVAEPILASLKDQLKEVDLSDFVAGRPELEALEVMNIFSDALQGSILSSLNLSDNALGEKGVRAFGALLKS
SQ  LSSLEELYLMNDGISKEAAQAVSELIPSTENLRVLHFHNNMTGDEGALAIAEVVKRSPLLENFRCSSTRVGSKGGIALSE
SQ  ALEHCTHMEKLDLRDNMFGTEAGVSLSKTLSSFKHMTELYLSYLNLEDEGAIAIVNALKESASPIEVLEMAGNDITVEAA
SQ  SAIAACVAAKQDLNKLNLSENELKDEGCVQIANCIEEGHSKLQYIDMSTNYIRRAGARALAHVVVKKEAFKLLNIDGNII
SQ  SEEGIEELKEIFKKSPELLGALDENDPDGEEDDDDEEDEEDEENEGNGNGELESKLKNLEVNQED
//
ID  O13918;
PN  Zinc homeostasis factor 1;
GN  zhf1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}. Nucleus membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}.
DR  UNIPROT: O13918;
DR  UNIPROT: P78885;
DR  Pfam: PF01545;
DE  Function: Involved in zinc homeostasis, where it plays a role in its accumulation in the endoplasmic reticulum/nucleus. Also has a role in the sequestration of cadmium into the endoplasmic reticulum. {ECO:0000269|PubMed:11886869}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005789;
GO  GO:0000324;
GO  GO:0000329;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005385;
GO  GO:0006877;
GO  GO:0098849;
GO  GO:0006882;
GO  GO:0140209;
GO  GO:0062111;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILG
SQ  ALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESV
SQ  LPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGD
SQ  ALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHE
SQ  LHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS
//
ID  O94385;
PN  Nucleoporin pom152;
GN  pom152;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein. Note=Central core structure of the nuclear pore complex. {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94385;
DR  UNIPROT: Q9USB0;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250|UniProtKB:P39685}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVTRVASSERPRPLVPESIVDAPTQRLYAIGVFVALQAYKIYDLLKLETSSISDVPKSGFLVKWIIIDAIYLRLLPKFRI
SQ  PWLSFQPAATLLQIAIFAAINLLLSSLSSLKWISIGSILLPYFKKKELSISEHKINPNNVIHNSSRILGQYTLQVLPEGT
SQ  AKINPLHENYCLNSLRKDQYVDLAIQFNSTIPKYIQYSHVDLETKEETLVEVSGRSLRKLLSSSSKNPKEPRLQTIYLKT
SQ  NKRGLYTLKHVVDKSKLDVRIFRSEAVVVSCPTATFASRQSGGRLRERCVGDTDNAELKVTGVAPLQVTYRNWDGKHFNT
SQ  HIIDSTIPDDFHPPAVVLSSNPKDIVFYKGIDIQWARSSEIFVPINTLLKAPGQWIYAVTQVTDALGNSQQFPSNDQFLL
SQ  RFAHGYTEADGESHSLPENVYSVFVHQRPDIQFRGCSIESPANLFPNKETSLSLYSSFSEYNSLEVGVDRYELGLDPQNI
SQ  TVPPLSHKTYQISPRSSANINVKKPGIYVLSSVSSQYCSGEVLEPNTCLVVTPPEAKVSVSFEEISDQCAGSIGARADLE
SQ  LEGTPPFTIAYRMTKDNEASRIQYVTTDRTRYQLNFTPKKAGKYRYIILGIQDANYGYRELSGSSFYKDQTVFPLADASF
SQ  EERRNGDLSTVVKTSCIGDTMSLPVLLTGSAPWTLEYEIFRNNKREESHVVESKDPRYILEVPMLVHGSQYTITLVSVKD
SQ  SNGCKRSLNTADTVIKVRRQRPTATFYSSDNTYTLKSVEGALMKIPLRLAGEKPWYVEYSHTSGLNKVSHHKEVLNDPNS
SQ  YLTVRKSGTYTLLSVSDSSCPGTIQNVEQKYQVEWLPRPFLSIPSLESSVKGKTRYYEQNAVCAGDSSAFEVQLSGSGPF
SQ  LLKHDKILVDEKSKTYPKQKSELSTVQNTVLVKADTAVPGVYHYEFTKLSDSLYSDSDAVTIVNNQSYQAVVLQRVNSLP
SQ  KASFMNVEKLYTFCINTDVTQSNAQLIAIQLQGASPFSLVIGIKNELTGSVSKYTLNDIHESVYKFAFPQEQLTLGKHVV
SQ  RLLQVRDANGCAASITKTQPAAKVSVVEMASLAPLGSRQYYCVGDRLSFALQGLPPFDVEYEFNGVTQHATSDSHILTRL
SQ  IELPGVVAMKSISDHGSHCKSYINPPIEQIVHDIPTVRISNGKDVIENIHEGDQAEISFHFTGTPPFSFSYARRALGKKR
SQ  PGKVLETHTVTGINEYEYKVLSSVEGVYTVLSVQDKYCRYPQDSTSSSNI
//
ID  P03185;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P03185;
DR  UNIPROT: Q777G7;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:15731264, ECO:0000269|PubMed:16406456}.
DE  Reference Proteome: Yes;
DE  Interaction: P0CK47; IntAct: EBI-2620196,EBI-2620189; Score: 0.51
DE  Interaction: P04275; IntAct: EBI-981819,EBI-2620196; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-2620196,EBI-747754; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-2620196,EBI-748420; Score: 0.55
DE  Interaction: O75094; IntAct: EBI-2620196,EBI-2622593; Score: 0.37
DE  Interaction: Q99873; IntAct: EBI-2620196,EBI-78738; Score: 0.37
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MASPEERLLDELNNVIVSFLCDSGSLEVERCSGAHVFSRGSSQPLCTVKLRHGQIYHLEFVYKFLAFKLKNCNYPSSPVF
SQ  VISNNGLATTLRCFLHEPSGLRSGQSGPCLGLSTDVDLPKNSIIMLGQDDFIKFKSPLVFPAELDLLKSMVVCRAYITEH
SQ  RTTMQFLVFQAANAQKASRVMDMISDMSQQLSRSGQVEDTGARVTGGGGPRPGVTHSGCLGDSHVRGRGGWDLDNFSEAE
SQ  TEDEASYAPWRDKDSWSESEAAPWKKELVRHPIRRHRTRETRRMRGSHSRVEHVPPETRETVVGGAWRYSWRATPYLARV
SQ  LAVTAVALLLMFLRWT
//
ID  Q03455;
PN  Probable zinc transporter MSC2;
GN  MSC2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: Q03455;
DR  UNIPROT: D6VSI6;
DR  Pfam: PF01545;
DE  Function: Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution. {ECO:0000269|PubMed:11058603}.
DE  Reference Proteome: Yes;
DE  Interaction: P53735; IntAct: EBI-28507,EBI-34990; Score: 0.67
DE  Interaction: Q06677; IntAct: EBI-34990,EBI-30084; Score: 0.35
DE  Interaction: P53919; IntAct: EBI-28887,EBI-34990; Score: 0.37
GO  GO:0005623;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005385;
GO  GO:0006882;
GO  GO:0055085;
GO  GO:0006829;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFN
SQ  FINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPS
SQ  FDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIV
SQ  NKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFN
SQ  EITSSIKTDLLSLLFVVVAEYVSSFSNKQPDSHSHNHAHHHSHLTDSLPLENESMFKQMALNKDTRSIFSFLLLNTAFMF
SQ  VQLLYSFRSKSLGLLSDSLHMALDCTSLLLGLIAGVLTKKPASDKFPFGLNYLGTLAGFTNGVLLLGIVCGIFVEAIERI
SQ  FNPIHLHATNELLVVATLGLLVNLVGLFAFDHGAHDHGGTDNENMKGIFLHILADTLGSVGVVISTLLIKLTHWPIFDPI
SQ  ASLLIGSLILLSALPLLKSTSANILLRLDDKKHNLVKSALNQISTTPGITGYTTPRFWPTESGSSGHSHAHTHSHAENHS
SQ  HEHHHDQKNGSQEHPSLVGYIHVQYVDGENSTIIKKRVEKIFENVSIKAWVQVEPQNSTCWCRATSMNTISANPNSLPLQ
SQ  PIAN
//
ID  Q8L7F7;
PN  Nuclear pore complex protein NUP62;
GN  NUP62;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8L7F7;
DR  UNIPROT: Q9SHD8;
DR  Pfam: PF05064;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9FFV8; IntAct: EBI-4428604,EBI-4428580; Score: 0.37
DE  Interaction: Q9SB65; IntAct: EBI-4428604,EBI-4439069; Score: 0.37
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0044613;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0010930;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFPFGQSNSVGGFSFGSSSATNSSSASSTTSPLSFSFNQSSNPSSTGFGFGSSVSSTPASSTTPSFGFGASSTPSFGF
SQ  GSSASSSTPSFGFGSSASVTPASTTPSFGFGTAASSSAPAPSLFGSSTTNASSAAPGSSPFGFVTSSASSTATPSSSLFG
SQ  APASSAATPSSSPFGAAPASGSTPLFGSSPSLFSAPSSASASNSSLFGASSSAATSTSPLFGAPSSATGATPSFSVASSA
SQ  PGSSSSIFGATGSSPSFSVASSASGSSPSIFGATGSSPFFGSSSSAGSTPSLFASSSSGATTSSPSPFGVSTFNSSSTSN
SQ  TSNASASPFSASTGFSFLKSTASSTTSSTTPSAPPQTASSSSSFSFGTSANSGFNLSTGSSAAPASSTSGAVFSIATTTT
SQ  TSSSTPAATSAPASSAPASTMAFPSFGVTSSATNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPASSSQ
SQ  PQTTSPAFSFSLPSSTSTTAPATSSATTTQTTLVVPSSSGTSTAVAPVAGSPKLPSEITGKTVEEIIKEWNTELQERTGR
SQ  FRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSMEEEAERIYNDERKSLLDDEA
SQ  ASTRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAIDGMSPLDVVVRILNNQLSSLMWIDEKAEEFSSRIQKI
SQ  ALQGSGGDRELMAPKHWMS
//
ID  Q06833;
PN  Nucleus-vacuole junction protein 2;
GN  NVJ2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass type II membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:22250200}; Single- pass type II membrane protein {ECO:0000305}. Note=Enriched at the nucleus-vacuole junction where it becomes increasingly concentrated as cells enter into the late-logarithmic growth phase (PubMed:22250200). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (PubMed:28011845). {ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:28011845}.
DR  UNIPROT: Q06833;
DR  UNIPROT: D6W491;
DR  Pfam: PF10296;
DR  Pfam: PF00169;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial- Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000269|PubMed:28011845}.
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-8591,EBI-37290; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-37290,EBI-8603; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-37290; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-37290; Score: 0.35
DE  Interaction: P39743; IntAct: EBI-37290,EBI-14500; Score: 0.65
DE  Interaction: P43603; IntAct: EBI-37290,EBI-22980; Score: 0.44
DE  Interaction: Q02159; IntAct: EBI-37290,EBI-19749; Score: 0.37
GO  GO:0071944;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071561;
GO  GO:0008289;
GO  GO:0035621;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASLKVFLAVYLLGGITFLPLVLFTLYKIHLLYSNLKSASKKELDHDTADEIDEKTRLLARDIDPEFKARKLEEQLGVKV
SQ  FNKGWITVTKQYYYHSSEVAVILKNSNNNKDSDTALQEQILQRTDLKKKQRFFAVLRHGNLFLYKDDSQNANLVHAISLQ
SQ  NRFITIWPRFDELGKEELPDASLFTKRTCIAIFKNDLVSIDSKNHNVILPHFDPLTSAESNNGDISTNDTTHEYQSQFHS
SQ  SNQFFLYFDNNMDKEDWYYQLINASKNSNSLSTGLLDPNVSANAAHLKTKDMLQLIQDINSTENQLTTKWLNALLGRLFL
SQ  SLQQTDTLNKFIHEKICKKLNKIKTPGFLDDLVVEKVDVGDSAPLFTSPELLELSPEGSTKIAIDVQYRGNLTIIIATKA
SQ  SINLGSRFKQREVSLQLSIKIKEFSGPLLFLIKPPPSNRIWYAFRTEPIMDFEIEPIVSSSKLSYNVVTNAIKSKFAEAV
SQ  KESLVVPFMDDIVFYPTPNEVYRGGIWEEQDPEAAARARTAAAASDMNNTSAKEHLEALQEGGMKTQSRIKKALRPERKK
SQ  ENLKDLVDASGVATKTTTQTTVTTATNDDVSSSENSTKSRKYFKNSIKKIGRWYKDNVGNSSDTEDMDEIDVQDKKNDDS
SQ  ADERESDNPILTSNPKMISNRRPVPRRPSQPLNTLSPKLEGRKEKDTENFPVPPSASNMNASKMFANKENRKFSVSSNDS
SQ  QNSLKNGDPHVKASKLESSQAFVKKTSQNRFNDGFFKQDLEFEEQREPKL
//
ID  Q12164;
PN  Pore membrane protein of 33 kDa;
GN  POM33;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex.
DR  UNIPROT: Q12164;
DR  UNIPROT: D6VXY1;
DR  Pfam: PF03661;
DE  Function: Contributes to proper distribution and/or efficient assembly of nuclear pores. Required for normal pore density in the daughter nucleus during telophase. {ECO:0000269|PubMed:20498018}.
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-30000,EBI-8591; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-30000,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-30000; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-30000; Score: 0.35
DE  Interaction: P32793; IntAct: EBI-30000,EBI-24460; Score: 0.62
DE  Interaction: P43603; IntAct: EBI-30000,EBI-22980; Score: 0.44
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0031309;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0051028;
GO  GO:0031081;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSRPANNQGPPNLPARDKSLVQRFMAVAKSLQFAWFTGHSVVLISSILYLLKMSEFYYRSAYLGVIESFGIIIYQQFFT
SQ  RNEPLQTQDAAATKASIKSRVAGLLKSEDVLYLVLANFWLFTPRFSFSLIPFFAFAVFHVLIYVEKVLLPKVFHLSSKDS
SQ  SKILSFIDKFVVQYNDLCMHWVGTAELLIFILVLFRAILCFQRSWIILVVYAIFIKLRYENSKYMKAAFAQWRVRMDGII
SQ  SHPSIPPFVKRAYNAIKMSLIRLSEYRLSGAPQVTKKQN
//
ID  Q93454;
PN  mRNA export factor rae-1;
GN  rae;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12937276}. Nucleus {ECO:0000269|PubMed:22357847}. Cell projection, axon {ECO:0000269|PubMed:22357847}. Cell junction, synapse {ECO:0000269|PubMed:22357847}.
DR  UNIPROT: Q93454;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:12937276). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). It is specifically important for nuclear mRNA export (PubMed:12937276). Has a role in neuronal development, where it acts downstream of rpm-1 to control axon termination and synapse formation in anterior lateral microtubule (ALM) and posterior lateral microtubule (PLM) mechanosensory neurons (PubMed:22357847). {ECO:0000250|UniProtKB:P40066, ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:22357847}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0030054;
GO  GO:0005643;
GO  GO:0045202;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0006406;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGSSGFGNKSMFGGSNISTSTTTPAANTTQNDDFLVDGAPEDTIQVIKFSPTPQDKPMLACGSWDGTIRVWMFNDANTF
SQ  EGKAQQNIPAPILDIAWIEDSSKIFIACADKEARLWDLASNQVAVVGTHDGPVKTCHWINGNNYQCLMTGSFDKTLRFWD
SQ  MKNLPNQTQMAQIQLPERVYAADVLYPMAVVALANKHIKVYNLENGPTEVKDIESQLKFQIRCISIFKDKSNQNPAGFAL
SQ  GSIEGRVAVQYVDVANPKDNFTFKCHRSAELVNGFQEIYAVNDICFHPQHGTLVTIGSDGRYSMWDKDARTKLKTSEPHP
SQ  MPLTCCDVHSSGAFLVYALGYDWSRGHEGNTQPGSKIVIHKCIEDMKPRPTKK
//
ID  G0S024;
PN  Nucleoporin NIC96;
GN  NIC96;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Cytoplasmic side {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Nucleoplasmic side {ECO:0000250|UniProtKB:P34077}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P34077}.
DR  UNIPROT: G0S024;
DR  UNIPROT: G0ZGU3;
DR  PDB: 5CWS;
DR  PDB: 5HB2;
DR  PDB: 5HB3;
DR  Pfam: PF04097;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. {ECO:0000250|UniProtKB:P34077}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S4T0; IntAct: EBI-4325187,; Score: 0.73
DE  Interaction: G0SFH5; IntAct: EBI-4325173,EBI-4325194; Score: 0.52
DE  Interaction: G0S156; IntAct: EBI-4325171,EBI-4325173; Score: 0.70
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P34077};
SQ  MSLIGNGPSVPPSSTKASLFSSPTTSANPTGGLFGSTTGGSSLFAPKTAGSTTTSTTQPTSTTGLGTSLFGTSTTANTQN
SQ  TANAARPSLFTAGNSIFGTSTTQPGLGASSLTTAATSNQQAQQQQQQRQQHQQAAPTGALFDSLLARNKKQAEGETALGE
SQ  LPSLQLGLADLRQRLRKLGPSSDRPIEPGKAHYFLAASGVDPGAAVRDLGALGLQAKTERTAASVGPAAGPSGVSTTGFG
SQ  TGLGEVDVDTYLSNLQTKTTLSMIADGLERSARDFDAFLEENVTLEWEAQRKRIYQHFGIKPRDSSVAGTTTAQPTATPS
SQ  KDGQGTFGRSRRKASQPPPGERPAQRMSILGRSTMMRSVIGTPTRIGAHAPEFSDVEARKDSSGAAVASVDDRFLREKQA
SQ  KLAEKIREFNDARQRGTPFYICRDLADLESKSGDRHGPHIVEAYRAVMEMVGEHPDAGEAPRERQFAKMYLDPNTQSANA
SQ  LAMRKQILKGATTFLEKQFWNEVNSLIAKYPQDANLGGLPDVVSKIKAYIRLRIARKTLVPDNVELQQINGEYVWAIVFY
SQ  LLRAGFVTEAAQYVNSNQAHFRAIDRTFSGYINSYASSEERRLKRQMQDRCMSEYNQRIRNAPEGSIDPFRMACYKIIGR
SQ  CDLSNRSLDGLQTDVNDWIWLQFNLARETDRSLELAGESYGLAELQASIREIGLKHFPKTAAEDTNGSFGMFFYLQILAG
SQ  MFEQAIAYLYPFSYVDAVHFAIALTYYGLLRPVDAASAGNELLSHNTRSMPQINFGRMLGYYTRDFRAANPAAAVDYLVL
SQ  ICLNADEAAGGQQAQAALCHEALRELVLESREFSRLIGDIRPDGRRIRGVIEERGPLIALGQEDDFIRTITLQAASFADD
SQ  NGRTTDAVLLYHLAEDYDTVVSIVSRALSEAISLEIGEDPMRLIPVKPRVTNAEGQVEEAAPGSSLSLAAIDDPVELAKA
SQ  MMGMYERDHMFWQKIREPNRVACSVLLQMADIKSLVEQGRWAECLDKIRALDILPLTARGDPGTIRSYAARFPSLAQPVA
SQ  INVPNLLMWTVLCCMRQRERLAGGQFAGNESTARLMMDELKQMTVDLMAYTSQLRYRLPPHLHEALARASAD
//
ID  Q5R7K7;
PN  Sentrin-specific protease 2;
GN  SENP2;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}.
DR  UNIPROT: Q5R7K7;
DR  UNIPROT: Q5RDS3;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000250|UniProtKB:Q9EQE1, ECO:0000250|UniProtKB:Q9HC62}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070140;
GO  GO:0045444;
GO  GO:0051028;
GO  GO:0016926;
GO  GO:0015031;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HC62};
SQ  MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKP
SQ  MVTSACNGTRNVAPSGEVFSNPSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGYNR
SQ  RPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHRTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYH
SQ  SSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTEKMVGIRFENESRRGYQLEPD
SQ  LSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRG
SQ  DIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWS
SQ  LVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNIDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYIS
SQ  RDKPITFTQHQMPLFRKKMVWEILHQQLL
//
ID  A7WLH8;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: A7WLH8;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0031386;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0044389;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  O14329;
PN  Probable zinc transporter zrg17;
GN  zrg17;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14329;
DR  Pfam: PF01545;
DE  Function: Probable transporter involved in the regulation of zinc homeostasis. {ECO:0000269|PubMed:18199682}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9HGQ3; IntAct: EBI-21242769,EBI-21242755; Score: 0.37
GO  GO:0005623;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005385;
GO  GO:0006882;
GO  GO:1904257;
GO  GO:0062111;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQNHNIPTAIQIQNPINNNVSVTISDQLPKPSANNPNLLSVDTRPTHRKGHHHKHSLSHQYFLPPKNRQPLEIPASYPI
SQ  PTFKETFAILTFPQKLKLTSSILFFLVAVGVLLSGDATILLTLSCSLIVEGVLIIINVWRETLDSFLVWRHTCLRYPFGM
SQ  QQMELLVDFSFSILLIFLGMNLLKEPAEHAIEDWGNLHHAGDHEEETVHIHLTISLFASAIISGFALLLDHPSAHIRELN
SQ  SRFFHGLTLVPSLILVLLLSLGYQVGSFLSHLLSLTIAVTALVNGFSIAKSLALMLLLTYSNKEKVFECVSLIKEDTRID
SQ  QLNYAAIWQPHYNTCIANIGLTVSGGEREQAAVREDIIRIIQKTVGSIFGAGVQPKWEISVDIQRA
//
ID  Q04175;
PN  Importin beta SMX1;
GN  SXM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex.
DR  UNIPROT: Q04175;
DR  UNIPROT: D6VT29;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of ribosomal proteins (RPL11, RPL16, RPL25, RPL31A), the poly(A)-binding protein PAB1, the HO endonuclease or the tRNA and snRNA chaperone LHP1. Indirectly involved in nuclear mRNA export through its PAB1 nuclear import activity. {ECO:0000269|PubMed:12684370, ECO:0000269|PubMed:15004228, ECO:0000269|PubMed:15769879, ECO:0000269|PubMed:16507575, ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-10420,EBI-35508; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-6679,EBI-35508; Score: 0.35
DE  Interaction: Q03833; IntAct: EBI-35786,EBI-35508; Score: 0.35
DE  Interaction: P53688; IntAct: EBI-2066550,EBI-35508; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-35508; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-35508,EBI-22339; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-35508; Score: 0.53
DE  Interaction: P40564; IntAct: EBI-35508,EBI-25380; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-505,EBI-35508; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-6302,EBI-35508; Score: 0.53
DE  Interaction: P16140; IntAct: EBI-35508,EBI-20254; Score: 0.35
DE  Interaction: P36144; IntAct: EBI-35508,EBI-26459; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-35508,EBI-14372; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-35508,EBI-6314; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-35508,EBI-8603; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-35508,EBI-16037; Score: 0.35
DE  Interaction: P26785; IntAct: EBI-35508,EBI-14513; Score: 0.35
DE  Interaction: P0C0W9; IntAct: EBI-35508,EBI-15275; Score: 0.56
DE  Interaction: P41940; IntAct: EBI-35508,EBI-11191; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-35508,EBI-25128; Score: 0.35
DE  Interaction: P33399; IntAct: EBI-35508,EBI-10046; Score: 0.70
DE  Interaction: P33892; IntAct: EBI-35508,EBI-7442; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-35508,EBI-9890; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-340,EBI-35508; Score: 0.27
DE  Interaction: P38697; IntAct: EBI-9186,EBI-35508; Score: 0.27
DE  Interaction: P07702; IntAct: EBI-10271,EBI-35508; Score: 0.27
DE  Interaction: P36000; IntAct: EBI-2206,EBI-35508; Score: 0.27
DE  Interaction: Q03862; IntAct: EBI-31385,EBI-35508; Score: 0.27
DE  Interaction: P53230; IntAct: EBI-35508,EBI-23156; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008536;
GO  GO:0006406;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVQEQAILSCIEQTMVADAKIIKEAEQQLFEFQKQPGFTSFLLNIVSDDNFALNVRLSSAIYLKNKIHRSWDTKREDGIK
SQ  ADEKLSIKERLIETLVKNCENNHIRPILTETINGILVGQEDWDLAPIIKNLLSSGDASYIYPGLLLLFQLCKAHRWDMVG
SQ  SRDYIDSVIEELFPIVEGIASNIGSQTDYRSNEILYLILKSFKYACLNNLPQYFSQPERIMSWVQLHLYLCSKPLPVEVM
SQ  ELDPADRSLDKRVKVNKWGFGNLNRFLQRYNKITKAITKEFIDYIFNTIVPIILREFFKDIEAWGNNSLWLSDSSLYFLI
SQ  SFLEKCVTIDQLYPLIEPHLQIIFENVIFPCLCANEQSIELLEDDQEEYTRRYFDINREGSTPDAASADFIFLIGSKRPE
SQ  KLNNILPFINDIFTRFDANSSDINMAFKEEGALRTLSNLFSFIDEPSVLENIFGHFIVPLLSQDKYMFLVARSLETIALY
SQ  SEEFKDMNILSQLFELTYTNFLNSNVLPVQIEAADAIKCLIVSNPQIHPAVSAHVPGMMEKLLKLSKIFEIDILSEVMEA
SQ  LVERFSDELSPFAKDLASNLVEQFLRIAQALVENPSETYSASDQEQEIQASGLLQTMTTMVMSMNKVPLIESLAPVVKFV
SQ  VLHAQISFITEAVDLLDALTISSHLLYNQIAPPIWELLHDILDSFQTYAMDYFEAYSIFFETIVMTGFPQDQTYVQPLLE
SQ  ILSAKLESEVDYDIEHVMQILMYFALSMRDIPLFSKAIKVSTNDELGLDSKCIVKLGLANLFAKPIETLQIMENEGFTIN
SQ  FFTNWFNEKFYSVFAIKLQVLVILTLLKMPEVPNSVSPLLNNLTNKLVELTLSLPKAIRNRDAVTEGKSLEGDLTPEEEE
SQ  EYFIECDDDMKETVLDQINVFQEVHTFFKNLQNEDAGKYEKIINYLDESKRDSLQVILEFVSQH
//
ID  F1N4E5;
PN  Torsin-1A-interacting protein 1;
GN  TOR1AIP1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: F1N4E5;
DR  Pfam: PF05609;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0032781;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKA
SQ  RVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSE
SQ  EDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVR
SQ  SGDSVESGDQTTRSSSQYKESFWQSSQSGDFTAFDEQPLKLSSGYQKTPQEWAEKTVRIRTRMLTSSPGMRSIYGSFSDD
SQ  DSVQKSELGNQSPSTSNQQMTGQPKSVSSVKTKRYWPFAVIAALLIGGFLYTRPPEAETTAVQEFQNQMKQLMNKYQGQD
SQ  EKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQ
SQ  ELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNS
SQ  DTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL
//
ID  Q9QXS4;
PN  N-acetyltransferase family 8 member 3;
GN  Nat8f3;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9JIY8}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9JIY8}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIY8}. Note=C-terminally tagged constructs localize to the nuclear membrane and perinuclear region. N-terminally tagged constructs show a punctate cytoplasmic distribution. {ECO:0000250|UniProtKB:Q9JIY8}.
DR  UNIPROT: Q9QXS4;
DR  Pfam: PF00583;
DR  PROSITE: PS51186;
DE  Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4. {ECO:0000250|UniProtKB:Q9JIY8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0010485;
GO  GO:0008080;
GO  GO:0001702;
GO  GO:0016573;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPYHIRKYQDSDHRSVVNLFCRGTEEHISASFRYMLLLPGTLLILLGVPLTLFLASGSWLLVLLSTLTLLVSLWLLAKY
SQ  PWEKYTAMCLHSDMADIPRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDPLLQRKQLQLRHLSVSLEHRREGIGRAMVRT
SQ  ALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEFFYTFVSRLRNSPMICLKYCLTSALNDLKT
//
ID  P12827;
PN  Protein E26;
GN  DA26;
OS  46015;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:9448690}. Virion {ECO:0000269|PubMed:9448690}. Host cytoplasm {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:9448690}. Host nucleus {ECO:0000269|PubMed:17169392}. Note=Early in infection, localizes both in the host nucleus and cytoplasm while later in infection localizes in viral-induced microvesicles within the host nucleus. {ECO:0000269|PubMed:17169392}.
DR  UNIPROT: P12827;
DR  Pfam: PF11050;
DE  Function: Plays a role in the sorting of ODV envelope proteins to the host inner nuclear membrane. May facilitate the fusion and release of nucleocapsids into the cytoplasm. Modulates the expression levels of IE0 and IE1. {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:19019955, ECO:0000269|PubMed:19150105}.
DE  Reference Proteome: Yes;
GO  GO:0030430;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0019012;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESVQTRLCASSNQFAPFKKRQLAVPVGSVNSLTHTITSTTVTSVIPKNYQEKRQKICHIISSLRNTHLNFNKIQSVHKK
SQ  KLRHLQNLLRKKNEIIAELVRKLESAQKKTTHRNISKPAHWKYFGVVRCDNTIRTIIGNEKFVRRRLAELCTLYNAEYVF
SQ  CQARADGDKDRQALASLLTAAFGSRVIVYENSRRFEFINPDEIASGKRLIIKHLQDESQSDINAY
//
ID  Q5JTH9;
PN  RRP12-like protein;
GN  RRP12;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q5JTH9;
DR  UNIPROT: B4DK00;
DR  UNIPROT: E9PCK7;
DR  UNIPROT: Q5JTH8;
DR  UNIPROT: Q69YK4;
DR  UNIPROT: Q96E87;
DR  UNIPROT: Q9BUH3;
DR  UNIPROT: Q9Y4C7;
DR  Pfam: PF08161;
DR  OMIM: 617723;
DR  DisGeNET: 23223;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-310743; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-310743; Score: 0.35
DE  Interaction: P62491; IntAct: EBI-745098,EBI-310743; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-310743; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-448665,EBI-310743; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-310743; Score: 0.60
DE  Interaction: F5H1C8; IntAct: EBI-21259559,EBI-310743; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-310743; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-310743; Score: 0.46
DE  Interaction: P01100; IntAct: EBI-310743,EBI-852851; Score: 0.40
DE  Interaction: Q9JMK2; IntAct: EBI-771709,EBI-310743; Score: 0.40
DE  Interaction: P62960; IntAct: EBI-529779,EBI-310743; Score: 0.40
DE  Interaction: Q99661; IntAct: EBI-1642317,EBI-310743; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-310743; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-2829677,EBI-310743; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-310743; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-351126,EBI-310743; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104531,EBI-310743; Score: 0.35
DE  Interaction: Q16666-2; IntAct: EBI-6273540,EBI-310743; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054761,EBI-310743; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-396034,EBI-310743; Score: 0.35
DE  Interaction: Q9QZD9; IntAct: EBI-7466616,EBI-310743; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-78579,EBI-310743; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-358318,EBI-310743; Score: 0.46
DE  Interaction: P68431; IntAct: EBI-79722,EBI-310743; Score: 0.46
DE  Interaction: P62753; IntAct: EBI-356625,EBI-310743; Score: 0.46
DE  Interaction: P27824; IntAct: EBI-355947,EBI-310743; Score: 0.46
DE  Interaction: Q15075; IntAct: EBI-298113,EBI-310743; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-310743; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-310743; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-624291,EBI-310743; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-310743; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-310743; Score: 0.35
DE  Interaction: P55075-2; IntAct: EBI-21635150,EBI-310743; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-2008793,EBI-310743; Score: 0.35
DE  Interaction: Q86VZ2; IntAct: EBI-996170,EBI-310743; Score: 0.35
DE  Interaction: P01127; IntAct: EBI-1554925,EBI-310743; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-486838,EBI-310743; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-310743; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-359390,EBI-310743; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-310743; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-310743; Score: 0.35
DE  Interaction: Q9NY93; IntAct: EBI-372376,EBI-310743; Score: 0.40
DE  Interaction: P56180-2; IntAct: EBI-11960323,EBI-310743; Score: 0.46
DE  Interaction: Q96KR7; IntAct: EBI-717068,EBI-310743; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-352783,EBI-310743; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-310743; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-2561019,EBI-310743; Score: 0.35
DE  Interaction: P18124; IntAct: EBI-350806,EBI-310743; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-310743; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-1056618,EBI-310743; Score: 0.35
DE  Interaction: P11487; IntAct: EBI-11478259,EBI-310743; Score: 0.35
DE  Interaction: Q6AW86; IntAct: EBI-4395769,EBI-310743; Score: 0.35
DE  Interaction: Q96HE9; IntAct: EBI-3957108,EBI-310743; Score: 0.35
DE  Interaction: Q9NY72; IntAct: EBI-17247926,EBI-310743; Score: 0.35
DE  Interaction: P19438-2; IntAct: EBI-21717938,EBI-310743; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-358049,EBI-310743; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-358058,EBI-310743; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-308619,EBI-310743; Score: 0.35
DE  Interaction: Q5T3I0-3; IntAct: EBI-21605187,EBI-310743; Score: 0.35
DE  Interaction: Q8N0W7; IntAct: EBI-21682158,EBI-310743; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-358163,EBI-310743; Score: 0.35
DE  Interaction: O14836-2; IntAct: EBI-12023110,EBI-310743; Score: 0.35
DE  Interaction: Q8WYQ3; IntAct: EBI-16721660,EBI-310743; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-443446,EBI-310743; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-310743,EBI-358011; Score: 0.40
DE  Interaction: Q96CW1; IntAct: EBI-297683,EBI-310743; Score: 0.37
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0003723;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRSGKLPSGVSAKLKRWKKGHSSDSNPAICRHRQAARSRFFSRPSGRSDLTVDAVKLHNELQSGSLRLGKSEAPETPME
SQ  EEAELVLTEKSSGTFLSGLSDCTNVTFSKVQRFWESNSAAHKEICAVLAAVTEVIRSQGGKETETEYFAALMTTMEAVES
SQ  PESLAAVAYLLNLVLKRVPSPVLIKKFSDTSKAFMDIMSAQASSGSTSVLRWVLSCLATLLRKQDLEAWGYPVTLQVYHG
SQ  LLSFTVHPKPKIRKAAQHGVCSVLKGSEFMFEKAPAHHPAAISTAKFCIQEIEKSGGSKEATTTLHMLTLLKDLLPCFPE
SQ  GLVKSCSETLLRVMTLSHVLVTACAMQAFHSLFHARPGLSTLSAELNAQIITALYDYVPSENDLQPLLAWLKVMEKAHIN
SQ  LVRLQWDLGLGHLPRFFGTAVTCLLSPHSQVLTAATQSLKEILKECVAPHMADIGSVTSSASGPAQSVAKMFRAVEEGLT
SQ  YKFHAAWSSVLQLLCVFFEACGRQAHPVMRKCLQSLCDLRLSPHFPHTAALDQAVGAAVTSMGPEVVLQAVPLEIDGSEE
SQ  TLDFPRSWLLPVIRDHVQETRLGFFTTYFLPLANTLKSKAMDLAQAGSTVESKIYDTLQWQMWTLLPGFCTRPTDVAISF
SQ  KGLARTLGMAISERPDLRVTVCQALRTLITKGCQAEADRAEVSRFAKNFLPILFNLYGQPVAAGDTPAPRRAVLETIRTY
SQ  LTITDTQLVNSLLEKASEKVLDPASSDFTRLSVLDLVVALAPCADEAAISKLYSTIRPYLESKAHGVQKKAYRVLEEVCA
SQ  SPQGPGALFVQSHLEDLKKTLLDSLRSTSSPAKRPRLKCLLHIVRKLSAEHKEFITALIPEVILCTKEVSVGARKNAFAL
SQ  LVEMGHAFLRFGSNQEEALQCYLVLIYPGLVGAVTMVSCSILALTHLLFEFKGLMGTSTVEQLLENVCLLLASRTRDVVK
SQ  SALGFIKVAVTVMDVAHLAKHVQLVMEAIGKLSDDMRRHFRMKLRNLFTKFIRKFGFELVKRLLPEEYHRVLVNIRKAEA
SQ  RAKRHRALSQAAVEEEEEEEEEEEPAQGKGDSIEEILADSEDEEDNEEEERSRGKEQRKLARQRSRAWLKEGGGDEPLNF
SQ  LDPKVAQRVLATQPGPGRGRKKDHGFKVSADGRLIIREEADGNKMEEEEGAKGEDEEMADPMEDVIIRNKKHQKLKHQKE
SQ  AEEEELEIPPQYQAGGSGIHRPVAKKAMPGAEYKAKKAKGDVKKKGRPDPYAYIPLNRSKLNRRKKMKLQGQFKGLVKAA
SQ  RRGSQVGHKNRRKDRRP
//
ID  P58742;
PN  Aladin;
GN  Aaas;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NRG9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NRG9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRG9}. Note=In metaphase cells localizes within the spindle with some accumulation around spindle poles, with the highest concentration between the centrosome and metaphase plate. The localization to the spindle is microtubule-mediated. {ECO:0000250|UniProtKB:Q9NRG9}.
DR  UNIPROT: P58742;
DR  UNIPROT: Q544M6;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50294;
DE  Function: Plays a role in the normal development of the peripheral and central nervous system. Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment. {ECO:0000250|UniProtKB:Q9NRG9}.
DE  Reference Proteome: Yes;
DE  Interaction: P45561-1; IntAct: EBI-22092288,EBI-21917416; Score: 0.35
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0009566;
GO  GO:0007612;
GO  GO:0001578;
GO  GO:0090307;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCSLGLFPPPPPRGQVTLYEHNNELVTGNSYESPPPDFRGQWINLPVLHLTKDPLKAPGRLDHGTRTAFIHHREQVWKRC
SQ  INVWHDVGLFGVLNEIANSEEEVFEWVKTACSWALALCGRASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWH
SQ  PHTNKFAVALLDDSIRVYNANSTIVPSLKHRLQRNVAALAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLS
SQ  HPGHTPVTSLAWAPNGGWLLSASPVDAVILVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKVLATTPSAVFRVWEAQMWT
SQ  CEAWPTLSGRCQTGCWSPDGNRLLFTVLGEALIYSLSFPERCGTGKGHVGGAKSATIVADLSETTIQTPDGEERLGGEAH
SQ  SMVWDPSGERLAVLMKGNPQVQDGNPVILLFRTRNSPVFELLPCGIIQGEPGAQAQLITFHPSFNKGALLSVCWSTGRIT
SQ  HIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHEVPLFTETSPTSAPWDPLPGQSSAQPHSPHSHL
//
ID  P10160;
PN  Eukaryotic translation initiation factor 5A-1;
GN  EIF5A;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: P10160;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045727;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
GO  GO:0006452;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDSGEEILITVLSAMTEEAAVAIKAMAK
//
ID  Q20924;
PN  Sun domain-containing protein 1;
GN  sun;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305|PubMed:14697201}; Single-pass membrane protein {ECO:0000305|PubMed:14697201}. Nucleus envelope {ECO:0000269|PubMed:24297748}.
DR  UNIPROT: Q20924;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in centrosome attachment to the nucleus. Required for zyg-12 localization to the nuclear envelope. Together with pot-1, it is required to anchor telomeres to the nuclear envelope in embryos (PubMed:24297748). {ECO:0000269|PubMed:14697201, ECO:0000269|PubMed:24297748}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0009792;
GO  GO:0006998;
GO  GO:0008104;
GO  GO:0010824;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYK
SQ  EITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFH
SQ  QTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTP
SQ  EKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVL
SQ  SPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQE
SQ  QFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA
//
ID  A1YK02;
PN  Nuclear pore complex protein Nup75;
GN  Nup75;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: A1YK02;
DR  UNIPROT: Q8SZH5;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). Facilitates the interaction between Nup93 and sec13 with msk (PubMed:20547758). {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-144629; Score: 0.35
DE  Interaction: Q9VZU6; IntAct: EBI-500389,EBI-144629; Score: 0.37
DE  Interaction: Q9VR15; IntAct: EBI-107845,EBI-144629; Score: 0.37
DE  Interaction: Q03017-1; IntAct: EBI-200614,EBI-144629; Score: 0.37
DE  Interaction: Q7JYZ0; IntAct: EBI-189350,EBI-144629; Score: 0.37
DE  Interaction: Q9VLT9; IntAct: EBI-174393,EBI-144629; Score: 0.37
DE  Interaction: Q9VLP3; IntAct: EBI-144629,EBI-179169; Score: 0.37
DE  Interaction: Q7K0E3; IntAct: EBI-157547,EBI-144629; Score: 0.37
DE  Interaction: P39769; IntAct: EBI-300360,EBI-144629; Score: 0.37
DE  Interaction: Q9W087; IntAct: EBI-140047,EBI-144629; Score: 0.37
DE  Interaction: Q9VDI5; IntAct: EBI-144629,EBI-166488; Score: 0.37
DE  Interaction: Q9VXS4; IntAct: EBI-144629,EBI-138783; Score: 0.37
DE  Interaction: Q8T0S6; IntAct: EBI-144629,EBI-101858; Score: 0.37
DE  Interaction: Q9VX05; IntAct: EBI-144629,EBI-172809; Score: 0.37
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:2000331;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVTHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAE
SQ  ANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQ
SQ  SNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKS
SQ  MPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPELEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKP
SQ  FELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLP
SQ  ALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKR
SQ  SYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSA
SQ  SELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENV
SQ  DEIMNLLRLACARNLARALIIENTLPVV
//
ID  F4IMH3;
PN  Protein NUCLEOLAR COMPLEX ASSOCIATED 4;
GN  NOC4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000269|PubMed:23382868}.
DR  UNIPROT: F4IMH3;
DR  UNIPROT: O22737;
DR  UNIPROT: Q8VZE1;
DR  Pfam: PF03914;
DE  Function: Essential protein required during embryogenesis (PubMed:15266054, PubMed:23382868). Involved in nucleolar processing of ribosomal RNA (rRNA) 40S and 90S ribosomal subunits and ribosome assembly; early in ribosome biogenesis, especially required during the maturation of 5.8S rRNA (PubMed:23382868). Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q06512, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:23382868}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0032040;
GO  GO:0009793;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASILSKKQKKNEKYTLKELKSLGHDLLTSRSHINNLPLLLTFVSPESPPQFVVESLLSLQSFFTPLLSQLPPTSSSPSS
SQ  TKTEDPEVVFKAWLRSKFDEFVKLLLDVLVSQQSEDSLRGIVLGTLMEFVKLLNAGRFHSSIYHRLLDAIIHSEVDIEIF
SQ  LDILTSKYFKYIDVRYFTYISMEKFVKTLEASVSADRTVIENNEAESDSKESLELSVRKIYQVLSQIPPPEKQAEKSQHE
SQ  MWSGSDESISEKPTDKKKKTEKGDSTLLSPATISKRMKLKFTKAWISFLRLPLPIDVYKEVLASIHLTVIPHLSNPTMLC
SQ  DFLTKSYDIGGVVSVMALSSLFILMTQHGLEYPFFYEKLYALLVPSVFVAKHRAKFLQLLDACLKSSMLPAYLAASFTKK
SQ  LSRLSLSIPPAGSLVITALIYNLLRRNPTINHLVQEIVENADEANTEAGEHNESQPKTIKKRKLGIDYFNNQESDPKKSG
SQ  ALKSSLWEIDTLRHHYCPPVSRFISSLETNLTIRSKTTEMKIEDFCSGSYATIFGDEIRRRVKQVPLAFYKTVPTSLFAD
SQ  SDFPGWTFTIPQEEGTC
//
ID  O74510;
PN  Bouquet formation protein 3;
GN  bqt3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: O74510;
DE  Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. {ECO:0000269|PubMed:19948484}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:1990862;
GO  GO:0051301;
GO  GO:0044821;
GO  GO:0044820;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLT
SQ  KYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNG
SQ  LILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYL
SQ  SQIWIITFICWALSL
//
ID  Q5XGN1;
PN  Nucleoporin NUP42;
GN  nup42;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q5XGN1;
DR  UNIPROT: Q4QQY9;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MAICNFFLQGRCRYGEKCWNEHPRGGGGGGGNRYQSQNRYQEQSRYQEQSRYPEQSRYPEQNRYQEPAGNAKGTWGASSQ
SQ  RYVQPSNFSKSTTWINRDSEKPSAGSFSGFGSRNVKSTAATGLPSTQNRFAALSSQDNSRDGQTDKGNILDDIMKDMEIW
SQ  ESSGQWMFSVYSMLKEKKNISGFTDFSPEELRLEYSVCQAEGNPLKYINAVQQLGSKWKQRILELKNPNPSIKTALLNEL
SQ  NSPSPDVTPGYSGQQNSAFGALSFPTSNTAPTAVTFSFKADTTTAAKPAVPNALAGSDFSAFGNKPTSAPSFGSGVAAAA
SQ  ASFSFAPSTISGFGSTASNSGFGAASNAAGFQGAANIAAAPAFGVASSTAPASGFGGGFGTTVNTGAKTSSVRDLFSAGT
SQ  AVPVQTTLLFGQATGSLNTTASSTSLAGQPFKASTSATAVSGSFTSDNTSNPLFTPRNELSVEDLAQFEAKQFTLGKTPI
SQ  KPPSADLLKVT
//
ID  Q9C100;
PN  Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
GN  ogm2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. Nucleus membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}.
DR  UNIPROT: Q9C100;
DR  Pfam: PF02815;
DR  Pfam: PF02366;
DR  Pfam: PF16192;
DR  PROSITE: PS50919;
DE  Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. {ECO:0000269|PubMed:15809069}.
DE  Reference Proteome: Yes;
GO  GO:0097582;
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004169;
GO  GO:0071712;
GO  GO:0035269;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSYEQLHAQSGQLRQRFPSKHSEIEDEVANEKEELKDATKSALGEVKTNKKYYILGYFLVPLLLTVIAGFVRVWKIADSN
SQ  VVIWDEAHFGKFASYYLKHEFYFDVHPPLGKMLNAVAGKLVGYDGSFDFSSGATYPEDLNYKFMRLWNAAFGTLCIPLVY
SQ  FTALNFNYSFLAATLCTLMVALDNHLATISRFILLDSMLLFFIISTFFCLSRYHVYHKAPFTFYWFKWLFLTGVCIGCVC
SQ  SVKLVGLFITAVVGLYTVDELWCLLNDKRVTWKAYAGHWIARVCLLIFLPILIYAFTFWIQFAVLYRSGPGDAQMPSLFQ
SQ  ARLEGSPLTKNPIDLMYGSKFTLKSRNPTGALLHSHVQTYPEGSEQQQVTGYHHKDGNNEWMFVPTHGVAYNYEENDPMN
SQ  PILNGSVVRLIHPFTNRNLHTHKIPAPLNKRMYEVSGYGLGDVGDEKDYWIVNILYDTAHRDAYNVRSLSTVFQLYNPVV
SQ  GCYLSSSSSSLPSWGFGQIEMYCDPDPDPSNTDTQWNVEEHINPRLPEGSINDYPSSFWSDFLHLNRAMLRANNGLIPDE
SQ  DKLDALRSEAYQWPFLLATLRMCGWGDNQIKYLLVGNPVAYWFATSSLIVFALFVVGAVLAWRRRVLRWSQEACDTFHYA
SQ  GIYPFLGWFFNYLPYYIMGRVLYVHHYEPSYALSTFTAAFVVDWFTKKMPKIVRVVVFISLYAIIAGVFIYFKDVTFGMH
SQ  GPASDFHRLRWLNSWNVHD
//
ID  P91193;
PN  Macoilin;
GN  maco;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:21437263}; Multi-pass membrane protein {ECO:0000255}. Note=Restricted to neuronal cell bodies, absent from dendrites and axons (PubMed:21437263). {ECO:0000269|PubMed:21437263}.
DR  UNIPROT: P91193;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0051015;
GO  GO:0008017;
GO  GO:0006935;
GO  GO:0040011;
GO  GO:0023041;
GO  GO:0043052;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESI
SQ  QMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWP
SQ  IVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDV
SQ  SNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTT
SQ  SSRKKKHNGNSGFNSTPPNDKKKGKSIRDVDMDDGDDSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAWLFSFVFE
SQ  SSTPSENSLSNQQIDDDEDYEDGDGDKKNGRTDSMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNH
SQ  QKSNGNSNGHARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLK
SQ  VEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRI
SQ  ELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEF
SQ  QIKNGSSIGGGSSETLMNGRSSTEANNENDTTASDQSSPHQHSAMGSPVPFAKMPLSVNVSNRHGSPFNGKVSPIASIGS
SQ  VLAAAGGPAPPDYMMAVGANVTATTGPVPQKQPRAGFHGISRYNEFTNIASGGEHRLFDTPASAISASAINGSNPEDDFL
SQ  MNKGKFGAPSQPAARLA
//
ID  Q9USG8;
PN  Meiotically up-regulated gene 190 protein;
GN  mug190;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single- pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9USG8;
DR  Pfam: PF00168;
DR  PROSITE: PS50004;
DR  PROSITE: PS51847;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005816;
GO  GO:0005543;
GO  GO:0061817;
GO  GO:0006869;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTHSGDSTKQQHYRSSDPYSGRRPIPTIPKFFRDRKQRAEKKEEQQREQTENEKLFDPITQRDVEINDVHFDYAKTYDD
SQ  PSFTVPNQSIQGSSLPSEKPYLSSNQPTNVYKQHQDDLAPPEADNQITRDVPISDEKTNILFFPSPSIDLSYVSKEVKQK
SQ  TGQYSLFAYIFSLVISWFFTHSIIISAVLPLAISSCMYLWMQNIYAVAKDAEWGAEQKRGEYARLNLIPESAEWMNHLLE
SQ  KVWPLINPEMFSSVADQIEDVMQASIPSFVENVRVASLDQGSHPVRVVSIRSLPSGEASESFSEKQASEAEHKDEPEQQR
SQ  KQFYNFELCLAYHAKPVEDATSTSARASNLHLRIVFYPGIKGTVGFPLPIWVEIKGFVARIRFRCELMPEVPFLKNVTFS
SQ  LMGLPELNVSAVPVAEGGVNIFGLPLISKFVNDAISAAANEYVSPKSMTIDLSKTLLGDDIKKEVNALGVIFVHINRAED
SQ  LSKQDVNGLSDAYITVGFHKFGKPLYCTRVVKQDLNPIWNEYAFIPVFPDQVKAGEKISIELWDSDRFSPDDVVGRTKIG
SQ  LHLLIQDSGKMHERCDTLTGISEDTSLPGRVFYEIGYFPRAEFKPSLKTSGHDITIPRSMRDDPAFQNPHGSLDNKEEEA
SQ  AVTTAPDEEYPSGILSFTVHQAVNLQMNHPTGTFGNVSGNYNTSPAQSVGDVTAEEGSELPSSYVCVDLDDTLVYKTRTK
SQ  VFTSNPIYNAGSEKFVKDWRNAMLCFTVRDFKLREHDSILGVVNIPLATTLTTSSQLTKWYPIQGGIGFGSVRISILFRS
SQ  MKLKIPRNLLGWDIGTLEFMDRQIVAEGTGSVSDVSFSSIRVNIAGVKITAKSSTSNSSSTAEYHVRSRHAVIPVNNRYR
SQ  SAVVFEFRKQLQRKHNVFAMVWLVDLEDNVEQNIRVPIFTSSKPAHVLQNMIDFDHPDKESEFKIIGYLSTRICFHRGLD
SQ  DSHEQLVDNDDEAAIFETYRCLKSMGLRRGYVKDMKNPLADQRASLDESRETTTASSKFESDDSVDTEDEETTTDRTPIE
SQ  CTQTVSMVDPNVNGDIQGRNSLGTMNSNERNLEQEFISLGYASKNRPKAHAQEGTNQPGASENVEPVLADDSDAVTIHSN
SQ  ISSDDQKRKLVNADDRELEKRLHRGPYNSKIVRTGEWVKDGAKMGWRNLRRKFALNGRQPDVETEISK
//
ID  P53694;
PN  Reticulon-like protein 1;
GN  rtn1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Nucleus membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: P53694;
DR  Pfam: PF02453;
DR  PROSITE: PS50845;
DE  Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator. Overexpression causes cell lysis. {ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:1990809;
GO  GO:0071790;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEQHSLNPFESGSVTASDVAAAKSGAEDLVNTLTAHTVHPSTELPSATSFPSALPNSENPVIQNISSSSSEPHHTSQST
SQ  PGETSSPVCPVSGAHGGADKKCPALEAGCPFTNTTKQNVDPEISNALWSVLTWKNTSCSFSTLMSILALVYVPSWINLPR
SQ  LFFRTFRYVFLITSIIEFGGLFASNGKRGVLSHFRSSYITCDSKALDRIVNSIVDIFNVMLIQFQRILFAESPILTFTAS
SQ  VAAFIEFFLSGFLSYKSLFVWNVLFAFILPRLYVCNERSIKHLVASLERSGDKLKKQATETINTTVNK
//
ID  Q6P0U9;
PN  Nucleoporin NUP42;
GN  nup42;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q6P0U9;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MPVCNFFLQGRCRYGDTCWNEHPTGGRGGDYRGNQQPSNRGGFGNRVWINPSQRGGGGSSSAGGSNEWGRGAASARDVQS
SQ  SEFSFSQNRFSALETQRAGAEDTHTTLDTIQKEMEVWQTSGQWPFSCYSAVNRQISGFIELCPEELRLEYYTSRASGDIQ
SQ  PYINSVQQLANQWRSRVQELRNMSSSTQISVIAELKSSSPPASAPGFGSPGPGFGSATSGFGNTSLSSPPAGFGGAGFGS
SQ  GPQSSSTFSFAQSKTDFGASNTQQASGFGSSAFAQPSSGFGNPAPSAASFSFAAADSESKPSAGGFGSASGFSFKTATAG
SQ  QGSGFGSGFGSSSGFGSSSGFGSSSGFGSAFGSAAPAQSSSFGSTGGAADTQSGHGLFTANSELTPEELKEFMAKRFTLG
SQ  QIPLRPPPADLLMI
//
ID  B8PYG1;
PN  NMDA receptor synaptonuclear signaling and neuronal migration factor;
GN  nsmf;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}.
DR  UNIPROT: B8PYG1;
DE  Function: Stimulates outgrowth of olfactory axons and migration of hypophysiotropic gonadotropin-releasing hormone 3 (GnRH3) neurons. May couple NMDA-sensitive glutamate receptor signaling to the nucleus and trigger long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. {ECO:0000269|PubMed:19097186}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0030054;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045773;
GO  GO:2001224;
GO  GO:0048168;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLI
SQ  VKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSE
SQ  PSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQR
SQ  SLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVD
SQ  RKAKSFSRSWSDPTPVKPDSLHDSRDSGDLQASSGNLDEEDCDDVDWEEERELERVACEGDDFIPPKLMLISSKVPKAEY
SQ  VPNIIRRDDPSIIPILYDHEHATFDDILEEIEKKLTAYRKGCKIWNMLIFCQGGPGHLYLLKNKVATFAKVEKEEGMMQF
SQ  WKKLGRFMSLLNPEPNLIHIMGCYVLGNANGEKLFQNLKRLMKPHGIEFKSPLELSAQGKEMIEMYFDFRLYRLWKTRQH
SQ  SKLHDYDDLL
//
ID  Q9VFS6;
PN  Integrator complex subunit 5;
GN  omd;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q6P9B9}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B9}.
DR  UNIPROT: Q9VFS6;
DR  UNIPROT: Q95R54;
DR  Pfam: PF14838;
DR  Pfam: PF14837;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q6P9B9, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VA83; IntAct: EBI-110115,EBI-92367; Score: 0.35
DE  Interaction: O96607; IntAct: EBI-92367,EBI-164947; Score: 0.37
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0010628;
GO  GO:0045666;
GO  GO:0034472;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRQNLLDQLKHFIETVSNGHSCPQLLTSPNLIKLALGFLEELPATRDIVFEYFALLAEISVQLYVSPEMADPKTGMPVS
SQ  QVKLAGNRQQQQRAPEYEAFNLVKTALQSLVWKGPPAWSPLIANWSLELVAKLSDKYTQRRMTITASCNYWLECSAMHGL
SQ  MTLINSCFRKLTQPEEEACVEIMLNAFHRFPMTFDWIVARLGGCFPYKIIMQILQCGIKRFVDDYRCHLDSEAGILDYMT
SQ  SCHEQHLRAAFREMLREGFAPKKPLDVAVVPFLLITTNYSDTILQSLVNVLVEIYTEDMCEVIVQKAPLWLSNKMFAGMQ
SQ  PTLNNAVLRLNERGATLLLTAAKMAEKYVWCQDFLDNSMQELEQWVLNQRNFPLLADLAYEETKYMLWKSCLSTNLFEQQ
SQ  TAVRLLLVVSSQHPNIYYQTISQLLKKSYAQNPNGIGALIRLLGGQSGMVNFPGFTPGFKMVLEDITLDVQVNNRLPVPP
SQ  GTPTEAFNTFSNLNILARMHKSKNVAPYIKAQHLNQALNECLPKILQIFDCTVNKLVLRIDRDAAERIADKFRAQQSKNS
SQ  NNNNELCNGKDYGKRTKLEPGEDKVDDEDATRMRLAHLIVDLLNNIEAGSRTTVLRTPLVLKLATLSVKYFFVGLTEKTV
SQ  IRRAAASHRSYTLLQRQCSARKIARTVCLRELVERALFYHGHLLGQLEVYQLDELEIPEHEHLILQNLHTSSGANSNRSV
SQ  LHSGIIGRGLRPVLPPSERNCDAEKQALYLKALNACCADLEKPNNVEGYSLVSLLLVELVSTDVMYNGLPFPDEEFTRVT
SQ  MERDMLIRRAFINSPVLWAVLGLIAGHRPALCYSSVLLRALCATCLHHWRGKNVNRFQPTAANDELMLCTKKMLQLLAMS
SQ  QLIPPPLTNLHLIIEHFESAEIALLLRECIWNYLKDHVPSPALFHVDNNGLHWRNTNTQLAKVPPQYVDPLRHLMQRKLS
SQ  TLGPHYHQMFIMGELMEGDSEPDPTARLQIVEID
//
ID  Q8R322;
PN  Nucleoporin GLE1;
GN  Gle1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q8R322;
DR  UNIPROT: A3KGV8;
DR  UNIPROT: Q3TT10;
DR  UNIPROT: Q3TU23;
DR  UNIPROT: Q3UD65;
DR  UNIPROT: Q8BT16;
DR  UNIPROT: Q9D4A6;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005730;
GO  GO:0042802;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSDGRCWETLRALRNTSKGRLRYDREWLLRYEDVLEECMSLPKLSSYSGWVVDHILPNTSGHTQESAPSSDNSPSSGSA
SQ  SGLYQSSLLKSPVRSSPQSPSPSSPNGTQSTHESPFTEPIAPQSSRAIKVEGCIRMYELAHRMRGTEGLRQWQEEQERKV
SQ  RALSEMASEQLKRFDELKELKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQAEQEQLRK
SQ  EEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESGYPTAENQAEAERALQEM
SQ  RDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQGPAPPTQTSAPSPSPVGAQNEDLQVKVQDSTMQWYQQLQDASAK
SQ  CVLAFEDLTSSKDSQTKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYK
SQ  LAEKFVKQGEEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVTDSK
SQ  VEQQDNFLKRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQV
SQ  QFWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQRREIPVPRGFLTTSFWRS
//
ID  G0S156;
PN  Nucleoporin NUP53;
GN  NUP53;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q03790}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:Q03790}.
DR  UNIPROT: G0S156;
DR  UNIPROT: G3EQ73;
DR  PDB: 5HAX;
DR  PDB: 5HB3;
DR  PDB: 5HB7;
DR  PDB: 5HB8;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:Q03790}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-4325171,EBI-4325173; Score: 0.70
DE  Interaction: G0S4T0; IntAct: EBI-4325187,; Score: 0.68
DE  Interaction: G0SFH5; IntAct: EBI-4325194,EBI-4325171; Score: 0.52
DE  Interaction: G0S7B6; IntAct: EBI-4325479,EBI-4325171; Score: 0.68
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q03790};
SQ  MPPLILHNVPDDELYVGDDGIQRPFAMVFPQQDGSLRSRKANLETGAFGKSTRRTRSKAATPAKREDPTIAAADKIFSNW
SQ  LASQNQSAPQTSVPAPAQRKPNLIPSSSSQNLAQGHDESSAPSQTRFFRKQEPTEVILRGYRNAQHQYAAINHYEQIAGR
SQ  ICEDYPREPPVESRRYKSELRDPAFTHRRALTPEERAKVNRAMSGEHWVKVTFESAEAADKAVYSSPQLIQGHLVYAEYY
SQ  KGVPPAQDEAIPDPSVAAFGAALSRTQTLRQRNRGSFSLSGTQEAGGPDASPTSSLTADTGTLASGVEISTSTSNTLNGG
SQ  AAAGGAEKSQDDEFCRVIPTVRKAKLLPMEEALLPAPTFTQRIANHIPFLRWFNGAMIGSEVPRTETGEFDWVRASLFWK
SQ  LMWWLDFLLGLFGGDIRDAEKDDKED
//
ID  Q9P382;
PN  Nucleoporin nup82;
GN  nup82;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000305|PubMed:16823372}; Peripheral membrane protein {ECO:0000305|PubMed:16823372}; Cytoplasmic side {ECO:0000305|PubMed:16823372}.
DR  UNIPROT: Q9P382;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250|UniProtKB:P40368}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044612;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:16823372};
SQ  MASTIMSQEVSWTDILEKHPALRWIKPIPEDWEIFPKHLCAFESFLYVAVGQEVRSLDCRLLKHKNEASHKNFYKKLFNP
SQ  ELDFMIEQICLSKNGRFLAVVGKSKIVILGLRSKLSEQNPLAESVSNFGESVNNFSNSEHQENGTNSLKLSEVTICSVAV
SQ  INPSSQIVSVRFHPLGKSGRSLVVLTETSLLLYEAGNGVLMPDYEIPLKLTHQASNSFDADVDLHIPTAFCFSNVSQGWG
SQ  VFTIYILTRGGDVFSVCPVMPANAMIPQDVLKQIRLILTKKEDDADAENHRRNVHWITKLLGEAALANDLSTSFVISEGS
SQ  SELFDSSDYVSVRRPDDFSFIPSMQGPFLLQPAVADDELIEDYCDIYSFGMNPIDVLAIGGSEGRLDLLLLVSEVSGRWS
SQ  KLNDHGLASMKLIVSQVHSLYLSNNNPYMVLQPDIQSPYSLIAYHANGLHVVDIESWARDLNLNFENSEFLNNEEENDED
SQ  ELSNVLVSIPSRTSVLERLDTNPLNESTDAVVGCAQLYYPSLGKILISLTRNWQTTVFDDSDLATMGVNKESLSNEMDYS
SQ  KSLGTSSLEQVDDLDEKLTYTPLYVSLLEKTPFTDPSIPSLVERTIVPAELQNEITVSSASLRFLGKVVARYRETLNLLD
SQ  HGCSELHHRLKLQREEYERQQNHIYKLSDRISNFREKAWSTEHLEHLTSDMSMCEKRIDQVLQRVMDLRVPDLSDKEKQF
SQ  IKEIGNYKEKVTGERGIEKRVETLKTLLQRTKPRDAQTTLVASSSDMRLAAIEQLQKLLAQQSLSIKELKTKTVSFQRLL
SQ  QTS
//
ID  Q93VR9;
PN  Protein SEH1;
GN  SEH1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:22902705}. Nucleus {ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}. Cytoplasm {ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. Note=Part of the cellular SEH1 pool is not permanently associated with the Nup107-160 complex. {ECO:0000305|PubMed:22902705}.
DR  UNIPROT: Q93VR9;
DR  UNIPROT: Q8LB12;
DR  UNIPROT: Q9C5X7;
DR  UNIPROT: Q9C7V9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Required for proper export of mRNAs from the nucleus to the cytoplasm. {ECO:0000269|PubMed:22288649}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0034629;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAKSMATLDSGTTCSSWNQSGDRLAAGSLNGKLSIYESSTSSSSTFSCTSKVRVSESSIVKIVWLPSEYGDAVACVCEDG
SQ  SLSIWEELSEDAHGLEWKLCKSMKNKSSQVLDVQFGVSRKSLKMVAAYSDGYLRVFELLNPLELKNWQLQAEFQNVIDSL
SQ  STLGKPSSLSASVSWNPMKGEEQEPSFVLAFNSDSPHLNSSKIWEFDEAHNRWLAVAELALPEDKGDPVYALSWAPNIGR
SQ  PYEVVAVATHKGIGIWHVGLAPDLEGRLPVKKVSSLSGHQGEVWQMEWDMSGMTLASTGSDGMVKLWQSNLNGEWHEQAT
SQ  LEPVPS
//
ID  P38770;
PN  Nucleus export protein BRL1;
GN  BRL1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15882446}; Multi-pass membrane protein {ECO:0000269|PubMed:15882446}.
DR  UNIPROT: P38770;
DR  UNIPROT: D3DKY3;
DR  Pfam: PF10104;
DE  Function: Involved in mRNA and protein export from nucleus. {ECO:0000269|PubMed:15882446}.
DE  Reference Proteome: Yes;
DE  Interaction: P46985; IntAct: EBI-24507,EBI-11052; Score: 0.37
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-24507; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-24507,EBI-8648; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-24507,EBI-8627; Score: 0.53
DE  Interaction: P33416; IntAct: EBI-24507,EBI-8680; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-24507,EBI-8603; Score: 0.53
DE  Interaction: P10591; IntAct: EBI-24507,EBI-8591; Score: 0.35
DE  Interaction: Q9BXL8; IntAct: EBI-1773949,EBI-24507; Score: 0.56
DE  Interaction: Q9UJW9; IntAct: EBI-24507,EBI-748621; Score: 0.56
DE  Interaction: P02829; IntAct: EBI-24507,EBI-8659; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-24507,EBI-20254; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-24507,EBI-18976; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-24507,EBI-7238; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-24507,EBI-5687; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-24507,EBI-12823; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-24507,EBI-8666; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-24507,EBI-26307; Score: 0.37
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRNTLDFSAAKADEEEDDRMEID
SQ  EVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQKQEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAA
SQ  TKVEGVVPLPPSANQDDNESSNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNT
SQ  HNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQLFLNAITTVVIFSFILSFIIA
SQ  LQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPALGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFID
SQ  PLNWKTLFVIFCGVITWCFSSNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ
//
ID  Q0WPZ7;
PN  Protein GLE1;
GN  GLE1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q0WPZ7;
DR  UNIPROT: Q9SAE5;
DR  Pfam: PF07817;
DE  Function: Required for seed viability. {ECO:0000269|PubMed:22898497}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
GO  GO:0048316;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIVLEPPCPKSVDGISIDPEPNWNFESLVAEIASVEKKLNGFSMYPQPITNTTLRMGRRGGGFVMHVSEDEMESDEGEE
SQ  SDDEEEEEDHSQICTAGKRFACDELYLSDESDEEFDHEPEYMMNKLGLAESALYEVINDHQTEIKDDIRNQVSVVETEIM
SQ  NEIETSLSAIARVEKYSETRKEVERKLDLQYQRKVAEALDTHLTAVQREHKIKSQIEERKIRSEEAQEEARRKERAHQEE
SQ  KIRQEKARAEAQMLAKIRAEEEKKEVERKAAREVAEKEVADRKAAEQKLAEQKAVIESVTGSSATSNAQAGGNSIRAAES
SQ  ALILENHRLKKLEELETTNQSLKSRSNENFSSFEKHIGRVIRQISGTKDSVSGKINDIVKIFKDPRCPVSISIAAFAKKM
SQ  VTTKEKPNPFACSYVIVYINSQFPQVMDILLAEFHKACIYTVPKHIVNSQSAWDSDAYERLDSIMRLYGALVQTDIRVGN
SQ  ATNVHGIEHGWAWLARFLNKIPANRATATALNSFLQTAGFGLHQRYKSQFLKVVNVVREHFLQKLRAKKDTSDLLVIIAE
SQ  ITAYLDDRMYLKEPEGRAMKTTSTLSSELTAELNQPNYNQNYQRNDYRNYY
//
ID  Q54NA0;
PN  Nuclear pore complex protein nup85;
GN  nup85;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q54NA0;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSLNPQSNGNSNNLFGNVTLGNFSNNSNNLFGGSSTTSTNTNNSNNLFGGSSTTNSNNLFGSGGSSTTNNNNFNSNFNN
SQ  NNIKNENKIKNGKKFYNFRWSPTGEILLYNTLNNFDNHNFDQKNGGSDTIRYEMNTTLSTIKKFYNDLYTNFETMQRIAG
SQ  LSNQVIPDDRVREISHHSRTYLSVILAAINQMSKSQKTGSYIDDEDSCMNCDPLDNDLIKIQTPRVLEYFKQYPNKTLIF
SQ  FCGSIDSIYPYLCSKLSMETKSKCILIARESNVPNSKRLDLIRTISNQGELKILNKDEYSNRYQIANENYGELDDVLTLE
SQ  IDDTYLAYEREIDNLICMSTMWRVANLFYFSVSSSSNSVSPTQLLDCIELERKELLNSIEQQGTQDPMDSEYYNQIARLL
SQ  VCGCIDQVIQQLNILSRAPRSASQIKSTSRKSPINLLIDILSSIPLKKKSINGGGGAPLYPNEHLIQWNKWHQETQKILS
SQ  QYIESGSSSTNQVDENLLPIVKILLGDQQTIMSTCNSFLQLVVSNILFVEYTTSTTQLRQLFTQCYQTIQAPTTVDKIFL
SQ  SFATKDLDITLKKIFKHSPAWLAVHLSDLLYHHPYVMRKLPNSESQLTNIREYLLSDFGQSLASDSSLLSIGCNYLKYVK
SQ  NGGLEMIDQFISRQPIHFEKNAIKMLDKWATSVETKNSIYKMLSLQDFKRKRYAASLNWLMLANDNSHITLLSNYLLENQ
SQ  LNSEFLNDLQSLLEKNDEIDCNINNNNNNNNNNNSNNRISGNNNNNMIIDENKFEITNNSELIFLIRYRELISLWKERSF
SQ  KEYSSSLCLMFKDRVIPKRFWLRLLIDCVPLLESLKNLYFTYQDTLLLQSCLEEIIQSHLFDQYSFNISNQDIQILRSAL
SQ  ARNLAKSIIS
//
ID  Q95LV7;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q5SS91}. Nucleus inner membrane {ECO:0000305}.
DR  UNIPROT: Q95LV7;
DR  UNIPROT: G7P1S8;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q5SS91}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGKAKARRAAMFFRGCSEDASGSTSGSTLLSEDENPDTNGVTRSWKIILSTMFTLTFLLVGLLSHQWLKETEVPQKSRQ
SQ  LYAIIAEYGSRLYKYQARLRMPKEQLELLKKESQTLENNFHKILLLIEQIDVLKALLRDMKDGTDNNHSWNTHGDPVEDP
SQ  DHTEVLDEEMSNLVNYVLKKLREDQVQMADYALKSAGASIIEAGTSESYKNNKAKLYWHGISFLNHEMPPDIILQPDVYP
SQ  GNCWAFPGSQGHTLIKLATKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGITKKCEGEEIFLGQFIYNKTGTTVQTFE
SQ  LQHAVSEYLLCVKLNIFSNWGHPKYTCLYRFRVHGTPGKHI
//
ID  Q1LX29;
PN  Telomere repeats-binding bouquet formation protein 1;
GN  ccdc79;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during meiotic prophase. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q8C0V1}.
DR  UNIPROT: Q1LX29;
DR  UNIPROT: A3KQ98;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex. {ECO:0000250|UniProtKB:Q8C0V1}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0000781;
GO  GO:0000784;
GO  GO:0005637;
GO  GO:0003677;
GO  GO:0070197;
GO  GO:0045141;
GO  GO:0007129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEATKTDLRLLLECLKYQMKWPGSQKQALLTIISICKQNDQYVEFLREIGGISFIYNLSKSSTFSQVKETALFTLASLAE
SQ  LHESCKQALCREEMFRDFVQHLEQEMPLTEKRVAVYMLSVLVANNRCGQTLAKTSRCIEALLRLFRQSFPVPGESYEQLQ
SQ  LWITVSSALCGSVNNPQNEENQNVCMSVFPEIKPWLQEVALPRAELAQPLCSFIGMTVANNPCAQEYFVSVGGLDSLSDT
SQ  LTRVLSQSTHSASVCKMATIITKTLSACISNNELLGSSLSKLRVIPGLLRLLSSPNLDPQDQLAVVLTTGHLTDACVEQQ
SQ  SQLLSAGGLPIIITLLTETSDEELKKAAIFVLHTCNRITESLGPGMSTIDPNECDREGQWRSAGQILQRIQLLEKKIGKK
SQ  LWERDPESQPHSMKRSDSHVECDDELWEGSVMRKVKGNHRVYGEFRAIPAGTPITSEILQDQDSLQPDSSEEGLSPVQVN
SQ  LFKGPNWEKSKKRKHKQKRENERSDNQETRREGVNKRELKRNVKSERVVKRLKMMNLESDDDGYELLQNCSTPTEGNRDT
SQ  QGPDIFRHPDPVKRNQREPSLSDDNMSLCTELLDKEINKFLKPPSASKSNTLRCAGCVKHMNELNSRSFGAVLSSCRFQC
SQ  DFHLTLREAEDRFRRSQPLKRTSHTPTHTHINTHRKIREHSTSAQEHKQKSKREKHKLSHQSSDRCYRLTPLRRPRETYS
SQ  PDVKQWTDHRHLKKSSEDARSKNSSGRHRKRQNWSDKELCYLTKGVKRFGHSWNTILWKYPFHPGRTNVDLAKKFYHMQK
SQ  AKAQGVDLSVAKAL
//
ID  Q08955;
PN  Chromosome segregation in meiosis protein 4;
GN  CSM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12514182}; Single-pass membrane protein {ECO:0000269|PubMed:12514182}. Nucleus membrane {ECO:0000305|PubMed:12514182}; Single-pass membrane protein {ECO:0000305|PubMed:12514182}.
DR  UNIPROT: Q08955;
DR  UNIPROT: D6W3G9;
DE  Function: Involved in chromosome segregation during meiosis. Involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements. {ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:18585352}.
DE  Reference Proteome: Yes;
DE  Interaction: P47069; IntAct: EBI-25811,EBI-31728; Score: 0.50
GO  GO:0005623;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0000784;
GO  GO:0031965;
GO  GO:0045132;
GO  GO:0045141;
GO  GO:0010520;
GO  GO:0030435;
GO  GO:0007129;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKEMIAFLESQLFCTTQNFVAQE
SQ  THDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIYLSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV
//
ID  O14310;
PN  Nucleoporin npp106;
GN  npp106;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:9372936}.
DR  UNIPROT: O14310;
DR  Pfam: PF04097;
DE  Function: Has a role in promoting mRNA export from the nucleus. {ECO:0000269|PubMed:9372936}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLA
SQ  ESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEF
SQ  MEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTT
SQ  NIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSS
SQ  SAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLM
SQ  RSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHR
SQ  VSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFER
SQ  AISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPA
SQ  YQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGD
SQ  YDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVV
SQ  KVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYR
SQ  TISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL
//
ID  Q80Y24;
PN  Prickle-like protein 2;
GN  Prickle2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}.
DR  UNIPROT: Q80Y24;
DR  UNIPROT: A6H652;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016327;
GO  GO:0005737;
GO  GO:0016328;
GO  GO:0031965;
GO  GO:0008270;
GO  GO:0045197;
GO  GO:0031175;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTVMPLEMEKTISKLMFDFQRSSTSDDDSGCALEEYAWVPPGLKPEQVHQYYSCLPEEKVPYVNSAGEKLRIKQLLHQL
SQ  PPHDNEVRYCNSLDEEEKRELKLFSNQRKRENLGRGNVRPFPVTMTGAICEQCGGQIKGGDIAVFASRAGHGICWHPPCF
SQ  VCTVCNELLVDLIYFYQDGKIYCGRHHAECLKPRCAACDEIIFADECTEAEGRHWHMRHFCCFECETVLGGQRYIMKEGR
SQ  PYCCHCFESLYAEYCDTCAQHIGIDQGQMTYDGQHWHATETCFCCAHCKKSLLGRPFLPKQGQIFCSRACSAGEDPNGSD
SQ  SSDSAFQNARAKESRRSAKIGKNKGKTEEAMLNQHSQLQVSSNRLSADVDPLSVQMDLLSLSSQTPSLNRDPIWRSREEP
SQ  FHYGNKMEQNQSQSPLQLLSQCNIRTSYSPGGQGAGAQPDMWAKHFSNPKRSSSMALKGHGGSFIQECREDYYPGRLMSQ
SQ  ESYSDMSSQSFNETRGSIPVPKYEEEEEEEEGGISTQQCRPRRPLSSLKYTEDMTPTEQTPRGSMESLALSNATGLSAEG
SQ  GAKRQEHLSRFSMPDLSKDSGMNVSEKLSNMGTLNSSMQFRSAESVRSLLSAQQYQEMEGNLHQLSNPLGYRDLQSHGRM
SQ  HQSFDFDGGIASSKLPGQEGVHIQPMSERTRRRTTSRDDNRRFRPHRSRRSRRSRSDNALHLASEREVIARLKERPPLRA
SQ  REDYDQFMRQRSFQESLGQGSRRDLYSQCPRTVSDLALQNAFGERWGPYFTEYDWCSTCSSSSESDNEGYFLGEPIPQPA
SQ  RLRYVTSDELLHKYSSYGVPKSSTLGGRGQLHSRKRQKSKNCIIS
//
ID  P39547;
PN  ULP1-interacting protein 3;
GN  UIP3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11056382}; Multi-pass membrane protein {ECO:0000269|PubMed:11056382}. Cell membrane {ECO:0000269|PubMed:11056382}; Multi-pass membrane protein {ECO:0000269|PubMed:11056382}.
DR  UNIPROT: P39547;
DR  UNIPROT: D6VPM9;
DR  Pfam: PF00674;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-20760,EBI-20760; Score: 0.55
DE  Interaction: Q12743; IntAct: EBI-33192,EBI-20760; Score: 0.37
DE  Interaction: O13540; IntAct: EBI-31374,EBI-20760; Score: 0.37
DE  Interaction: P39548; IntAct: EBI-20760,EBI-2344928; Score: 0.55
DE  Interaction: P47111; IntAct: EBI-20760,EBI-25497; Score: 0.37
DE  Interaction: P53868; IntAct: EBI-2490,EBI-20760; Score: 0.37
DE  Interaction: P38226; IntAct: EBI-20760,EBI-21429; Score: 0.37
DE  Interaction: P06197; IntAct: EBI-13458,EBI-20760; Score: 0.37
DE  Interaction: Q02724; IntAct: EBI-20050,EBI-20760; Score: 0.37
DE  Interaction: Q06144; IntAct: EBI-34916,EBI-20760; Score: 0.37
DE  Interaction: P40107; IntAct: EBI-7764,EBI-20760; Score: 0.37
DE  Interaction: P40857; IntAct: EBI-20760,EBI-26003; Score: 0.37
DE  Interaction: P46956; IntAct: EBI-20760,EBI-13337; Score: 0.37
DE  Interaction: P53142; IntAct: EBI-20760,EBI-23899; Score: 0.37
DE  Interaction: P32453; IntAct: EBI-3306,EBI-20760; Score: 0.37
DE  Interaction: P53845; IntAct: EBI-28230,EBI-20760; Score: 0.37
DE  Interaction: P53337; IntAct: EBI-20760,EBI-23662; Score: 0.55
DE  Interaction: P32621; IntAct: EBI-20760,EBI-7511; Score: 0.37
DE  Interaction: Q12016; IntAct: EBI-20760,EBI-29309; Score: 0.37
DE  Interaction: Q03860; IntAct: EBI-37537,EBI-20760; Score: 0.37
DE  Interaction: Q04767; IntAct: EBI-20760,EBI-28141; Score: 0.37
DE  Interaction: P47088; IntAct: EBI-26307,EBI-20760; Score: 0.37
DE  Interaction: Q8TGQ7; IntAct: EBI-20760,EBI-2343396; Score: 0.37
DE  Interaction: Q04969; IntAct: EBI-27827,EBI-20760; Score: 0.37
DE  Interaction: P02829; IntAct: EBI-8659,EBI-20760; Score: 0.35
DE  Interaction: Q9BSE2; IntAct: EBI-8649725,EBI-20760; Score: 0.56
GO  GO:0005783;
GO  GO:0000329;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQTPSENTDVKLDTLDEPSAHLIEENVALPEDTFNSYWSYILNEIARCKPLMIMFLIPVCLVLLITFFHDIKGILVFLVI
SQ  SLILSIIILLIGITAFVSETLNKGFIIKLLVEVITRKPAVGGKEWRIIAYNMNQYLFDHGIWHTPYYFFCEHRCHKFFKS
SQ  LIKQTRSNAHLSSPTNGAENTQSNTPAKEVSNEMVKPYIFSSDPVLEAYLIKAAEIHKEAEFEYWRKQYPEVDLP
//
ID  G7IBJ4;
PN  Protein CNGC15a;
GN  CNGC15A;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: G7IBJ4;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  PROSITE: PS50042;
DE  Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations (PubMed:27230377). Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors (PubMed:27230377). Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations (PubMed:27230377). May function during fertilization in both female and male gametophytic Ca(2+) signaling (PubMed:27230377). {ECO:0000269|PubMed:27230377}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005262;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0036377;
GO  GO:0009877;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRIN
SQ  LWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELII
SQ  DSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEK
SQ  AWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHF
SQ  FQFGIFDDAVTLEITSSNFLTKYYYCLWWGLRNLSSSGENLLTSTHVAEINFAVIVAILGLVLFALLIGNMQTYLQSTTI
SQ  RLEEWRIRRTDTERWMHHRQLPHYLKENVRRHDQFRWVATRGVDEEAILRDLPVDLRRDIKRHLCLNLVRQVPLFDQMDD
SQ  RMLDAICERLKPTLCTPGTCIVREGDPVDEMLFIVRGRLDSCTTNGGRTGFFNTCRIGSGDFCGEELLPWALDPRPTAVL
SQ  PSSTRTVRAITEVEAFALIAEDLKFVAAQFRRLHSKQLRQTFRFYSHQWRTWAACFIQAAWFRYKRMKETNEVKEKENLM
SQ  MMSNVKYYGNDDSQYFSAPLQVPKGSSYSMYSGKLVGSLRRGRSMRYGSELDMLGTLRKPIEPDFNDDGD
//
ID  O59718;
PN  Nuclear envelope morphology protein 1;
GN  nem1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}.
DR  UNIPROT: O59718;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Catalytic component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0004721;
GO  GO:0030437;
GO  GO:0071072;
GO  GO:0071763;
GO  GO:0023052;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHAN
SQ  IMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSY
SQ  SYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSG
SQ  HSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSR
SQ  GSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALV
SQ  DSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK
//
ID  Q9Y6X4;
PN  Soluble lamin-associated protein of 75 kDa;
GN  FAM169A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:22412018}. Nucleus inner membrane {ECO:0000269|PubMed:22412018}; Peripheral membrane protein {ECO:0000269|PubMed:22412018}; Nucleoplasmic side {ECO:0000269|PubMed:22412018}. Note=Enriched at the nuclear lamina.
DR  UNIPROT: Q9Y6X4;
DR  UNIPROT: A8K1T9;
DR  UNIPROT: Q6MZT0;
DR  UNIPROT: Q9H989;
DR  OMIM: 615769;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-351935,EBI-1220497; Score: 0.35
DE  Interaction: P20700; IntAct: EBI-1220497,EBI-968218; Score: 0.56
DE  Interaction: Q96QG7; IntAct: EBI-744593,EBI-1220497; Score: 0.56
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1220497; Score: 0.35
DE  Interaction: P58166; IntAct: EBI-21580393,EBI-1220497; Score: 0.35
DE  Interaction: P02647; IntAct: EBI-701692,EBI-1220497; Score: 0.35
GO  GO:0005637;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:22412018};
SQ  MAFPVDMLENCSHEELENSAEDYMSDLRCGDPENPECFSLLNITIPISLSNVGFVPLYGGDQTQKILALFAPEDSLTAVA
SQ  LYLADQWWAIDDIVKTSVPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAIGFYSV
SQ  KPTGSICASFLTQSYQLPVLDTMFLRKKYRGKDFGLHMLEDFVDSFTEDALGLRYPLSSLMYTACKQYFEKYPGDHELLW
SQ  EVEGVGHWYQRIPVTRALQREALKILALSQNEPKRPMSGEYGPASVPEYEARTEDNQSSEMQLTIDSLKDAFASTSEGHD
SQ  KTSVSTHTRSGNLKRPKIGKRFQDSEFSSSQGEDEKTSQTSLTASINKLESTARPSESSEEFLEEEPEQRGIEFEDESSD
SQ  RDARPALETQPQQEKQDGEKESELEPMNGEIMDDSLKTSLITEEEDSTSEVLDEELKLQPFNSSEDSTNLVPLVVESSKP
SQ  PEVDAPDKTPRIPDSEMLMDEGTSDEKGHMEEKLSLLPRKKAHLGSSDNVATMSNEERSDGGFPNSVIAEFSEEPVSENL
SQ  SPNTTSSLEDQGEEGVSEPQETSTALPQSSLIEVELEDVPFSQNAGQKNQSEEQSEASSEQLDQFTQSAEKAVDSSSEEI
SQ  EVEVPVVDRRNLRRKAKGHKGPAKKKAKLT
//
ID  P28948;
PN  Envelope glycoprotein M;
GN  gM;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P28948;
DR  UNIPROT: Q6DLF9;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:8648751}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MARRGAAVAEEPLLPSSGIVGIGPIEGINWRTWLVQVFCFALTTSVLFITLVTASLPQTGYPCFYGSLVDYTQKNHSVVD
SQ  GVWMRQIAGGVAPTLFLETTSLVAFLYYTTLVLVAISFYLIISAVLVRRYARGKECTAVAGCTRPTTTLIASHVTLVLGT
SQ  LATWLLQVVILLLSHKQAVLGAAVYVVHFVSLVFFCMSFSGLGTASAQYSSNLRILKTNLPALHKMAGPGRAVMTNLGMG
SQ  MLGISLPILSLMLGIILANSFHITLWQTVTVAVGVFVALGLMFLIIVELIVSHYVHVLVGPALAVLVASSTLAVATHSYF
SQ  VHFHAMVSVQAPNLATASKAIVGIMAVISIIMLVVRLVRAIMFHKKRNTEFYGRVKTVSSKARRYANKVRGPRRNPQPLN
SQ  VAESRGMLLAEDSETDAEEPIYDVVSEEFETEYYDDPQRVPERSHRREYR
//
ID  B2MVY4;
PN  Cyclin-dependent kinase 4;
GN  CDK4;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: B2MVY4;
DR  UNIPROT: B2CL06;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0007049;
GO  GO:0051301;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  ARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  DVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE
//
ID  Q3YBM2;
PN  Transmembrane protein 176B;
GN  TMEM176B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q3YBM2;
DR  UNIPROT: B2RDK2;
DR  UNIPROT: D3DWZ7;
DR  UNIPROT: E9PAV4;
DR  UNIPROT: Q5BJI2;
DR  UNIPROT: Q9BT42;
DR  UNIPROT: Q9Y609;
DR  Pfam: PF04103;
DR  OMIM: 610385;
DR  DisGeNET: 28959;
DE  Function: May play a role in the process of maturation of dendritic cells. Required for the development of cerebellar granule cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9RMZ4; IntAct: EBI-2821474,EBI-2821479; Score: 0.37
DE  Interaction: Q96HP8; IntAct: EBI-2800645,EBI-2821479; Score: 0.56
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0009887;
GO  GO:0030154;
GO  GO:2001199;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQNTVIVNGVAMASRPSQPTHVNVHIHQESALTQLLKAGGSLKKFLFHPGDTVPSTARIGYEQLALGVTQILLGVVSCV
SQ  LGVCLSLGPWTVLSASGCAFWAGSVVIAAGAGAIVHEKHPGKLAGYISSLLTLAGFATAMAAVVLCVNSFIWQTEPFLYI
SQ  DTVCDRSDPVFPTTGYRWMRRSQENQWQKEECRAYMQMLRKLFTAIRALFLAVCVLKVIVSLVSLGVGLRNLCGQSSQPL
SQ  NEEGSEKRLLGENSVPPSPSREQTSTAIVL
//
ID  Q8I4N3;
PN  Nucleoporin ndc-1;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q8I4N3;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P91001; IntAct: EBI-2001892,EBI-313007; Score: 0.37
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRL
SQ  AGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTF
SQ  ALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANI
SQ  SEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTV
SQ  HSPTPEQTRTLPNVIETDDSLLKFFALHDLRTIAWNDEKRRVDVFSLSQPGKHPRNWKAVSLPCVRMLDELCSRMTVSAA
SQ  RLVGYSWDDHDIENEDVPRDALLMPRKMREMAYRGTGQSRQQKSMAPIRSHNTQTVGLLSKISNFLGFGVTEKLVISRFD
SQ  AHMNAYAAEALYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTFLRIVDASLKSSLQRVVT
SQ  TFGSHLSSLNLPEEHSRTIRMICLTDEL
//
ID  Q6P4S8;
PN  Integrator complex subunit 1;
GN  Ints1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q6P4S8;
DR  UNIPROT: Q0KK58;
DR  UNIPROT: Q80UQ7;
DR  UNIPROT: Q91Z01;
DR  UNIPROT: Q9CTF7;
DR  Pfam: PF12432;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q8N201}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001832;
GO  GO:0001833;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:0016180;
GO  GO:0034474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNRAKPTTVRRPSAAAKPSGHPPPGDFIALGSKGQASESKTTSTLLKPAPSGLPSERKRDASASLSGTSALTGLTKRPKL
SQ  SSTPPLSALGRLAEAAVAEKRAISPSIKEPSVVPIEVLPTVLLDEIEAAELEGNDDRIEGVLCGAVKQLKVTRAKPDSTL
SQ  YLSLMYLAKIKPNIFATEGVIEALCSLLRRDASVNFKAKGNSLVSVLACNLLMAAYEEDENWPEIFVKVYIEDSLGERIW
SQ  VDSPHCRTFVDNIQTAFNTKMPPKSVLLQGEGARSGGELGAGSSPHPSLTEEEDSQTELLIAEEKLSPEQEGQLMPRPRY
SQ  DELTESVEEYVLDMLRDQLNRRQPIDNVSRNLLRLLTATCGYKEVRLLAVQRLEMWLQNPKLTRPAQDLLMSVCMNCNSH
SQ  GSEDMDVISHLIKIRLKPKVLLNHYMLCIRELLNAHKDNLGTTIKFVIFNELSNARNPNNMQILYTVLQHSSELAPKFLA
SQ  MVFQDLLTNKDDYLRASRALLREIIKQTKHEINFQAFCLGLMQERKEPQYLEMEFKERFVVHITDVLAVSMMLGITAQVK
SQ  EAGVAWDKGEKRNLEVLRTFQNQIAAIQRDAVWWLHTVVPSVSKLAPKDYVHCLHKVLFTEQPETYYKWDNWPPESDRNF
SQ  FLRLCSEVPILEDTLMRVLVIGLSRELPLGPADAMELADHLVKRAAAVQADDVEVLKVERIQLIDAVLNLCTYHHPENIQ
SQ  LPPGYQPPNLAISTLYWKAWPLLLVVAAFNPENIGLAAWEEYPTLKMLMEMVMTNNYSYPPCTLTDEETRTEMINRELQI
SQ  SQREKQEILAFEGHLAAASTKQTITESSSLLLSQLTSLDPQGPPRRPPPHILDQVKALNQSLRLGHLLCRSRNPDFLLHI
SQ  IQRQASSQSMPWLADLVQSSEGSLDVLPVQCLCEFLLHDAADSTASGEEDDEGESREQKAKKRQRQQKQRQLLGRLQDLL
SQ  LGPKADEQTTCEVLDYFLRRLGSSQVASRVLAMKGLSLVLSEGGLRDKEEKEPPMEEDIGETDALQGYQWLLRDLPRLPL
SQ  FDSVRTTTALALQQAIHMETDPQTISAYLIYLSQHTPVEEQGPHSDLALDVARLVVERSTIMAHLFSKPSCSTASDAVLS
SQ  ALLSVFSRYVRRMRKSKEGEEVYSWSESQDQVFLRWSSGETATMHILVVHAMVILLTLGPPRSGDSEFSELLDIWFPEKK
SQ  PLPTAFLVDTSEEALLLPDWLKLRMIRSEVPRLVDAALQDLEPQQLLLFVQSFGIPVSSMSKLLQYLDQAVAQDPQTLEQ
SQ  NIMDKNYMAHLVEVQHERGASGGQTFHSLLTASLPPRRDSTEAPKPESSPEPPPGQGRTRAGTQVPVLGPEDDLAGIFLQ
SQ  IFPLSPDPRWQSSSPRPLALALQQALGQELARVRQGNPEVPGITVRLLQAMTTLLSSPHGGTLALAMHHSHFLSCPLMRQ
SQ  LYQYQRAVPQDTGFSSLFLKVLMQILQWLDSPAVEDGPLQAQLKLFATRYSARHRISDVRSGLLHLADALSFHGDLEVAN
SQ  STARAVIATLRSGEKCPVEPELISKVLRGLIEVRSPHLEELLTALFSATTETSCPSPASGPIVVVSSLLLQEKEELLGPS
SQ  KQEVEGASTEAMRLGPASGLLVDWLETLDPEVVCSCPDLQWKLLFSRRKGKGHISAQVLSFRPYLLALLTHQASWSTLHC
SQ  CIRVLLGKSREQRLDPSASLDFLWACIHVPRIWQGRDQRTPQKRREELVLHVQGPELLSLVELILSEAETRSQDGDSAAR
SQ  TLIQTRLPLLLSCCRSNDESIGKVTEHLTSCIQQWGDSVLGQRCRDLLLQLYLQRPEVRVPVPEVLLQSEGATSSSICKL
SQ  DGLVHRFITLLADTSDSRSSESRVADANMACRKLAVAHPVLLLRHLPMIAALLHGRTHLNFQEFRQQNHLAFFLHVLGIL
SQ  ELLQPRVFQSEHQGALWDCLRSFIRLLLNYRKSSRHLAPFISKFVQFIHKYVGCSAPAAVAFLQKHAEPLHDLSFDNSDL
SQ  VMLKSLLAGLSLPSRDGRTDQGLDEEGEDERSAGSLPLVSVSLSTPLTVADVAPHMKRLSRGRAVEDVLETLSDIDEMSR
SQ  RRPEVLGFFSTNLQRLMSSAEESCRNLAFSLALRSIQNNPSIAADFLPTFMYCLGSRDFEVVQTALRNLPEYTLLCQEHA
SQ  AVLLHRAFLVGVYGQIDTSAQISEALKILHMEAVM
//
ID  Q09793;
PN  Nucleoporin nup45;
GN  nup45;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex.
DR  UNIPROT: Q09793;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0010389;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPG
SQ  LNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTT
SQ  GGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNA
SQ  NTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISS
SQ  RILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALS
SQ  NRFAQVHDEVKRLQVNTSTSLPFIS
//
ID  Q86CZ2;
PN  Hybrid signal transduction histidine kinase K;
GN  dhkK;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q86CZ2;
DR  UNIPROT: Q54Y10;
DR  UNIPROT: Q95PH2;
DR  Pfam: PF02518;
DR  Pfam: PF00512;
DR  Pfam: PF00072;
DR  PROSITE: PS50109;
DR  PROSITE: PS50110;
DE  Function: Involved in a signal transduction pathway that regulates morphogenesis and controls entry into the culmination stage. May act via the regA pathway, being activated by a morphogenesis-stimulated ligand, reducing phosphodiesterase regA levels and allowing cAMP level to rise to promote the culmination stage. This protein probably undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0000155;
GO  GO:0019933;
GO  GO:0031154;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIELNNHSKINKNENNTNTRNNSSNNNNNNNNINKTNTNKYFEYNQNSIIYSSIPNSFLSHHPNSVGSQCLSLNSFLPPK
SQ  PPILLSIFNSDTIGNNNNNNYSSSSSRNNSSGCSSSNNNNNNNNNNNNNNNNNNNNNNNNCNIEQYKNNQKQPKQQQQQK
SQ  DQTIATQHRISLSSSSSSSSLSSSSSSSSVKQSFQIVKRLFGSLSEYMFPQKDEILYETDPYYLYQDDTQSNDSNEFYDD
SQ  TDIGSDIDEANLNNTYNIQNCNKTLYNKQQQQAHFVNMNKNVNSNNGTGNSNQSNNVNKNQQNNNNNNNNNSHNNNNGNQ
SQ  NSSSSSSNSGASGSGGNGNNNNNNNNNNNNNNNNNNNSNSNSNNNSKSNNNNKKEGKDGATMNGSHPLIPFRKKPAQVPS
SQ  PCFRMNSPNSDNDQYLDQLALENSSKKSLVVYNTDNLDQWKHSHLNENFDILQNDLIDIQQQQQQQQQQDNTLQYSSPIN
SQ  KRQEQEQQHIPFQFTTEQQQQLQQQQQQQQQNKTKQHPILLQRQQQQKQKQQQQQQIQQEQIGNNNSNNNNNINNNNNIN
SQ  NNYNNVNDLMNKFEIDQKQHDSQQNLVEEKRTPSFHEHNIIFNSFNFICSIVLDGSNIKSTEKYKAKLIIGFCFTILSFI
SQ  PSWIIFFWLSGINKPAVMAIIAMPMSISSLVILKRTGSIHYPCHILCFTLCFALTINSYYTGGHQSTIRLLMSTVPIISA
SQ  LVLGRKASIQWSLMVLSIYLLFFVANLYGHEYVQGIPSIIIRSHMNFIIDVTIIIMTLIFTLCYQYFIDEAHRETKLKNA
SQ  QLTIAKDAAIEAYQARQEFLATMSHEIRTPLNGLIGMATLLRDSHNLPPEEKTMAKAVKSCGDILLRLVNDILDLSKLEA
SQ  NQMGLEHIPFRMRELTQQICHVLSGQANEKNIHLSCEVSDKIPSILLGDSGRILQILMNLTGNALKFTQSGYVKIIIDLI
SQ  EEESELVSLKKGEYNISFRVKDTGIGVPVESHQKIFEAFVQADPSDSRKYGGSGLGLYLCAKLVRLMKGEIGVYNNPDCD
SQ  GSTFWFILPLEEGTDQSMQQMNNGARHKAFPQDCVKVLIAEDNIINQRVAVKFLEKIGIKAEVAGNGNEVLEILERQHYD
SQ  LIFMDFQMPILDGLRCSKTIREFEQNHKWNRICPSIFICGLTANTMSTDKKRCFDHGMNHFISKPFQLEQLRSAIEMAIE
SQ  HKQRNLMNLNIRN
//
ID  Q5R9S8;
PN  Transmembrane protein 43;
GN  TMEM43;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum {ECO:0000250}. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5R9S8;
DR  Pfam: PF07787;
DE  Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAANYSSTSTRREHVKVKTGSQPGFLERLSETWGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSV
SQ  APENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDEQVKKETRYSYNTEWRSEIINSKN
SQ  FDREIGHKNPSAMAVESFTATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLR
SQ  VSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMF
SQ  MGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPIIVARTRVPAKKLE
//
ID  G5EEU2;
PN  Histone-lysine N-methyltransferase set-25;
GN  set;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000269|PubMed:22939621}. Chromosome {ECO:0000269|PubMed:22939621}. Nucleus lamina {ECO:0000269|PubMed:22939621}. Note=Colocalizes with its own product and hpl-1 in foci in the peripheral region of the nucleus, in a manner dependent on H3K9me3. {ECO:0000269|PubMed:22939621}.
DR  UNIPROT: G5EEU2;
DR  Pfam: PF00856;
DR  PROSITE: PS50280;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using mono- and dimethylated H3 'Lys-9' as substrate (PubMed:22939621). Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina (PubMed:22939621). Required for small-RNA-induced H3K9 methylation (PubMed:26365259). Together with met-2, protects and stabilizes repeat-rich genomic regions by suppressing transcription- induced replication stress through methylation of H3K9 (PubMed:27668659). {ECO:0000269|PubMed:22939621, ECO:0000269|PubMed:26365259, ECO:0000269|PubMed:27668659}.
DE  Reference Proteome: Yes;
GO  GO:0005720;
GO  GO:0005652;
GO  GO:0046872;
GO  GO:0008168;
GO  GO:0032259;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLR
SQ  QRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAV
SQ  DNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPN
SQ  NERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGW
SQ  TCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFW
SQ  IYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACEN
SQ  GTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGF
SQ  GVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRF
SQ  INHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF
//
ID  P53903;
PN  Processing of GAS1 and ALP protein 2;
GN  PGA2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P53903;
DR  UNIPROT: D6W133;
DR  Pfam: PF07543;
DE  Function: Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins. {ECO:0000269|PubMed:16943325}.
DE  Reference Proteome: Yes;
DE  Interaction: Q12154; IntAct: EBI-2344998,EBI-2989; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEVAETWVDTWMAKLVNYDYKHFIRLVIIVGGYLLLRNIASRELAKKQLAAQVEKDKRDKEEKRSKDLIDKPDDAATAE
SQ  TTSFGWGKKTRRRVKRQQELFENALEEAKRRNQGLDPDSDADIEELLEE
//
ID  P53062;
PN  Nucleus export protein BRR6;
GN  BRR6;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P53062;
DR  UNIPROT: D6VV88;
DR  Pfam: PF10104;
DE  Function: Required for mRNA nuclear export. Involved in the nuclear pore complex (NPC) distribution and nuclear envelope morphology. {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:15882446}.
DE  Reference Proteome: Yes;
DE  Interaction: P25611; IntAct: EBI-2347150,EBI-22052; Score: 0.37
DE  Interaction: P11484; IntAct: EBI-2347150,EBI-8627; Score: 0.35
GO  GO:0071944;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNL
SQ  KLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRS
SQ  FLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA
//
ID  A7MB64;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  ITPRIP;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: A7MB64;
DR  Pfam: PF03281;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0004860;
GO  GO:1902042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALGLFRVCLVVVTAIINHPLLFPRENTTVPENEEEIIRQMQAHQEKLQLEQLRLEEEMARLAADKEAEKEALERVAEEG
SQ  QQQNESRTAWDLWSTLCMILFLVIEVWRQDHQDAPSPECLGSDEDELPDLEGAPLRGLTLPNRATLDHFYERCIRGATAD
SQ  AARTREFVEGFVDDLLEALRSLCSRDSDMEVEDFIGVDSMYENWQVNKPLLCDLFVPFMPPEPYHFHPELWCSSRSVPLD
SQ  RQGYGQIKVVRADEDTLGCICGKTKLGEDMLCLLHGRNNVVHHGSKAADPLCAPNSPYLDTMRVMKWFQTALTRAWHRIE
SQ  HKYEFDLAFGQLDTPGSLKIRFRSGKFMPFNLIPVIQCDDSDLYFVSHLAREPGGGTRASSTDWLLSFAVYERHFLRVTS
SQ  KALPEGACHLSCLQIASFLLSKQSRLTGPSGLGSYHLKTALLHLLLARRPADWKAEQLDARLHELLCFLEKSLLEKKLQH
SQ  FFIGNRKVPQAMGLPEAVRRAEPLNLFRPFVLQRSLYRKTVDSFYEMLKNAPALISEYSLHIPSDHASLPPKTVIL
//
ID  Q5U249;
PN  Protein ELYS;
GN  ahctf1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}. Cytoplasm {ECO:0000250|UniProtKB:Q8CJF7}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17235358}. Note=Binds to chromatin during mitosis, and chromatin binding increases as nuclei assemble and grows through interphase (PubMed:17235358). Does not localize to the pores of annulate lamellae, which are cytoplasmic stacks of membrane that form in rapidly dividing cells (PubMed:18596237). {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}.
DR  UNIPROT: Q5U249;
DR  Pfam: PF13934;
DR  Pfam: PF16687;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex, which may in turn recruit membrane vesicles containing pom121 and tmem48/ndc1. Association with chromatin may require the presence of the mcm2-mcm7 complex, suggesting a mechanism for coordination of nuclear assembly and the inactivation of replication licensing. {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:17825564, ECO:0000269|PubMed:18596237}.
DE  Reference Proteome: No;
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-11609120; Score: 0.35
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQNLEAQVTGSLVAFPDVTQKALKEDEINLDSVLRGKFSTGRTSLAWLACGPQLEITNSVTGERISAYHFSGLTERPPVV
SQ  VAVKEFTWQKKTGLLVGLVEAEGSVLCLYDIGISKVVKAVVLPGSVTAVEPIINHGGASASTQHLHQSLRWFFGVTAVVT
SQ  DVGHVLLIDLCLDEVSSNQDELDASDLEVMSVIPTKIPKLREAATRERRHLCLQLAAPTGTTVSCLSYISRTNQLAVGYS
SQ  DGYFSLWNMKTLRRDYHVQIEGGRVPVCAVAFQEPENDPRNCCYLWAVQSSESGGDVSLHLLQLAFSDRKCLASGQIMYE
SQ  LLEYCEERYSLDLSGSTLSLRGQSNNTKLLGCQTIEKFRVHGEREDGVHEVTSPDTSVSVFSWQVNTYGQGKPSVYLGVF
SQ  DINRWYQAQMPDSLRSGQFLRNCSYFAFWSLEAVVNITTQDIIFDILVHERSLSRGIPPSYPPPEQFYYPSTYNFDATCL
SQ  LNSGLIHFACTGFQKETLHFLKKSGSSLNEAIPDGYNRCLAAGLLAPKFTDVQASSLSQEEQLQAILAAAVETSSLGLLT
SQ  SCIKRWTAEEQPRSAANLRFVLEWTWKKVTLTKQEFDRLCFRLFDGSCNFIDPHTLQSLQQCHLYFSNLTAVLNCFIAQA
SQ  KEVTQQGAVDLTNKQSVTRLLTLYASVVLWFCRSGMLPDSSDETVQLTRPFYNYQVIQQYYSDQRKKLERLARGKWDTSS
SQ  LMIDGLINQFGDRIQQLWSRDDNGTGKYPPANLHALLDVYLLENADEMSKHAITIYFLLDIMYSFPDKPDSSIESFPTAF
SQ  FVPGSLIKLIQGFWLLDHNDYQNSVDCILNPASSRVMSWQHSQIIENLLCHGDSRQALRYLQVMKPVATTSKEVKLHMTV
SQ  LLANRSILEAWNLQRLHSSRLNVEELLKHMYEMCQEMGLIEELLKLTFTDFEQGYLHKFLQTTGVQNQELLLVHHLQRAN
SQ  YISALQLNQSLKTNHLNDCDRRLRERSGARNAILDQYGKILPRVQRTLASERAKPYSLPSLVWREVARPKPLSTTAKQAA
SQ  PGSIITKANFICNVLSKIKEVSTANEKREEYSPYQSMVSEEPTAPPLQDIDVPDAFFGTPINKSRRVSRLLDSVVHPVLM
SQ  EPTPLTSSDTDNNQTPHKSPLLKTSSPLHSSLRRIAHMRSFAKASEFSLLETPLVVRKAKALAANTASSGYTSITPQSIL
SQ  RSSVRTTPLVSPSVSPGRSLTPPLRPKETKISFMELSFTRHAKAAHSSEGNLLAISPVLRSSPDAVWSVKGKVASFTQNT
SQ  PVKKLDEIDASSSGIQEESQDEMEVSKEISNISVRSEQASLEYHDAPTPEDLENDEISGTTNSQPQVNEVHHQMEDGQLT
SQ  EKPAELALTEMQEEFIDSEEREIEYISAPLNGPNALECMTAVPDIYLEDASQCILETPEGSSVSVTGEQECVSSAKDSES
SQ  VISIHDSDDAHSNLSENDQDSEEIEENNLRVPTTVTRCEEFDLIETKDLEVELEEADSEKTNYKDIYPDATVQLGFTVES
SQ  IEQRYTCELADRRETPSETDEIEGEHFETENNFSLVLEGDVTEEEILEPSSSKTDLELTRPPIAHQKLISENRENIENCE
SQ  TTEKIPANMSPLVDSDHESKTLETLPSEADLSVAEKVLKGTEEKDVPPEVHSEVVLESKLVGNAMMSLDSSESQEVIISQ
SQ  YDNVISIEKLEMTQEKMYGEKTEQINEGQVSPNRDQSTLVKPLTPRRSIRKSSKPADSSTDIIGNITLPTTPKRGLKKAK
SQ  ENVDTLKNSISVVPEEELTLGTRRITRKATLTALDNPEPLQIKEPPSGEDLQVQPSTPTRGRRGKVITSDDLKEPPSGED
SQ  LQVQPSTPTRGRRGRVITSDDLREPPPGEDLQVQPSTPTRGRRGRVITSDDIKESPSVEDLQVQPSTPTRGRRGKVITSD
SQ  DIKEPPSVEDLQVQPSTPTRGRKGKVITSDDIKEPLSGEDLQVQPSTPTRGRKGKVITSDDIKEPLSEEVLQEQPSTPTR
SQ  GRRGRVITSDGKGYECVEEKNALPLTPTRITRSKNILEPEKGISQIEPEKGISQIEPDKGLSQIEDTGETEHEVVTPRRG
SQ  RRGKRVVNELVKHFERNSSQPNIKADTSPPVSPKKVSLRWTRTRSENQRINATEEQASKIQEDLSDTPRKRYKKSSNKMG
SQ  FEETTDTVTEGAIVEDVQESLIISHLGKNPNTSIVRSARKTALPPVTEDHSEQPLLPPESHSKVHSSLAIADEENKTNTR
SQ  TRSGNKSSVDVSAITFEFSTPKARTKKTAKGSAVPTELIPSTQYVFSPPSTRTRRATRANVSEAVIEPQLQFQESCEIAE
SQ  TEVPEVPASKPRGRPPKHKAKAVTRVLKKPSWSTPPVEIKLISPPESPAVSETNTKTDSTEAKGAEKISVRRTRRRIIAK
SQ  PVTRRKMR
//
ID  Q94AV5;
PN  WPP domain-interacting protein 3;
GN  WIP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}.
DR  UNIPROT: Q94AV5;
DR  UNIPROT: Q9LTT2;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779487,EBI-1779367; Score: 0.37
DE  Interaction: Q9LE82; IntAct: EBI-1779351,EBI-1779487; Score: 0.49
DE  Interaction: Q9FMH6; IntAct: EBI-1779487,EBI-1779597; Score: 0.37
DE  Interaction: Q9C500; IntAct: EBI-1779618,EBI-1779487; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNESVPDSVEDNGNSVPANGLLVLPDNDHEEGGVGSPQRSNSVESPGGSVHSTRKGFGLKKWRRIKRDGPVRDEAAPVDD
SQ  GSKLLKRGLAGLVNPPSKHVEFSSVEARQSSEGSVGSVNMVHHPGVANGFSPDIGCMFAVGQAFEKSEEHSGNTIGGKNV
SQ  VGGKVVSGSQEKLWSDTIKRASEERGDIEKEKPCSSLDSDLRSSDFVFSTGSVSVGNHGEKDERLTMNYIGGFSNEGQVK
SQ  EEVQTYSRSENGNKEDDGESKKNNNHWADKDALADSIRSFAVLQEVLWKEVQSFQELGKESVLLHSNTDELSSDQPSHQN
SQ  CKEDNSTSSGSKALILKEKVKLLEHKLEEARAALEAKEARIQELENSKIESELECIFQRKIETEIEHLMLTRSLSSLQVL
SQ  QETKKLHSLKEDPVSNRGNILGKTCKLGFYILTQLILLVSILRFLVLQFSPASRLVIPT
//
ID  Q9UU91;
PN  Protein yop1;
GN  yop1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Nucleus membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: Q9UU91;
DR  Pfam: PF03134;
DE  Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator. {ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:1990809;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFQVRVKQNMQDLDNRLAAFPQLNSLEKNFGVSKLYVFLTAAGIYALFLFLNWGGFLLTNLLAFAMPAFFSINAIETTN
SQ  KADDTQWLTYYLVTSFLNVIEYWSQLILYYVPVYWLLKAIFLIWLALPKFNGATIIYRHLIRPYITPHVIRICKSVSRQN
SQ  AAPAPTASSFAHTTATDIPPSI
//
ID  Q5RBY5;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q5RBY5;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATAVSGPCAGRSRDILWRVLGWRIVASIIWSVLLLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYLLLLSVV
SQ  IIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGANSFGSPAAQT
SQ  CLNEYHLFFLLAGALMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKA
SQ  WISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGAFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLN
SQ  SNPPPIIKYLALQDLMLFSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLVLYQEAAATNGRVSSSYPVE
SQ  PKKLNSPEETTFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPEVVSPFGTPFGSSVMNRMAGIFDVNTCFGSPQSPQLIRR
SQ  GPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQM
SQ  HIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKT
SQ  AIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
//
ID  Q9V6B9;
PN  Probable nucleoporin Nup54;
GN  Nup54;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050}.
DR  UNIPROT: Q9V6B9;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner. {ECO:0000269|PubMed:17682050}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-179307; Score: 0.35
DE  Interaction: Q7JXF5; IntAct: EBI-127204,EBI-179307; Score: 0.37
DE  Interaction: Q7KKI9; IntAct: EBI-179307,EBI-2109596; Score: 0.37
DE  Interaction: Q6WAR0; IntAct: EBI-179307,EBI-2109775; Score: 0.37
DE  Interaction: Q86B83; IntAct: EBI-114500,EBI-179307; Score: 0.37
DE  Interaction: P18824; IntAct: EBI-216128,EBI-179307; Score: 0.35
DE  Interaction: Q8MRM0; IntAct: EBI-190634,EBI-179307; Score: 0.37
DE  Interaction: Q8I942; IntAct: EBI-15112591,EBI-179307; Score: 0.49
DE  Interaction: Q8IR83; IntAct: EBI-3403187,EBI-179307; Score: 0.49
DE  Interaction: Q95RR8; IntAct: EBI-179307,EBI-119468; Score: 0.49
DE  Interaction: Q9VZV3; IntAct: EBI-179307,EBI-15107563; Score: 0.49
DE  Interaction: Q9XZS4; IntAct: EBI-179307,EBI-98433; Score: 0.62
DE  Interaction: Q9VSJ8; IntAct: EBI-179307,EBI-107639; Score: 0.37
DE  Interaction: Q8MQZ0; IntAct: EBI-179307,EBI-496872; Score: 0.37
DE  Interaction: Q868Z9; IntAct: EBI-179307,EBI-128809; Score: 0.37
DE  Interaction: Q9VM05; IntAct: EBI-113729,EBI-179307; Score: 0.37
DE  Interaction: Q9VVT5; IntAct: EBI-179987,EBI-179307; Score: 0.37
DE  Interaction: Q7KLE5; IntAct: EBI-177679,EBI-179307; Score: 0.37
DE  Interaction: Q9VF05; IntAct: EBI-186487,EBI-179307; Score: 0.37
DE  Interaction: Q9VTU4; IntAct: EBI-178321,EBI-179307; Score: 0.37
DE  Interaction: Q9VRQ6; IntAct: EBI-179307,EBI-194555; Score: 0.37
DE  Interaction: Q9VLA6; IntAct: EBI-103034,EBI-179307; Score: 0.37
DE  Interaction: Q9W1A4; IntAct: EBI-91385,EBI-179307; Score: 0.37
DE  Interaction: Q9VGW6; IntAct: EBI-83298,EBI-179307; Score: 0.37
DE  Interaction: Q9VTC2; IntAct: EBI-122095,EBI-179307; Score: 0.37
DE  Interaction: Q9VWG2; IntAct: EBI-107089,EBI-179307; Score: 0.37
DE  Interaction: A1Z6W6; IntAct: EBI-155731,EBI-179307; Score: 0.37
DE  Interaction: Q24337; IntAct: EBI-179307,EBI-169459; Score: 0.37
DE  Interaction: Q9V9V0; IntAct: EBI-135868,EBI-179307; Score: 0.37
DE  Interaction: O46085; IntAct: EBI-151469,EBI-179307; Score: 0.37
DE  Interaction: Q9VS32; IntAct: EBI-179307,EBI-163732; Score: 0.37
DE  Interaction: Q8T965; IntAct: EBI-179307,EBI-130766; Score: 0.37
DE  Interaction: Q7JZJ3; IntAct: EBI-103820,EBI-179307; Score: 0.37
DE  Interaction: Q9W1H7; IntAct: EBI-117789,EBI-179307; Score: 0.37
DE  Interaction: Q9VYL7; IntAct: EBI-159418,EBI-179307; Score: 0.37
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006605;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFFGSNTSLGATSTPAKTTGGLFGSPFGGTAATSQPAPAFGAQATSTPAFGAQPATSAFGAGSAFGATAAAPAFGAATG
SQ  TSAFGGSAFGSTPAFGAATTTTAGTGLGGGGFGGFGAAPATSQAGLFGAPATSAAPPAFSGFGQQAAASTAPASGFSGFG
SQ  TTTTSAPAFGGFGTSQSTGFGGGAFGSTFGKPANTTVTPGFGGFGGTSFMLGQPQQQPAPISADEAFAQSILNVSIFGDE
SQ  RDKIVAKWNYLQATWGTGKMFYSQSAAPVDITPENVMCRFKAIGYSRMPGKDNKLGLVALNFCRELSAVKPHQQQVIQTL
SQ  HSLFGSKPNMLVHIDSIKELENKKCQIVIYVEEKLQHAPNESKRILATELSNYLNQATLKPQLNNLGVVEALALVLPDED
SQ  QLREYLENPPRGVDPRMWRQANSDNPDPTLYIPVPMVGFNDLKWRVKCQEQETDTHALYIKKVESELTELKKRHATATAK
SQ  ILEHKRKLAELSHRILRIIVKQECTRKVGTSLTPEEEALRTKLQNMLAVVSAPTQFKGRLSELLSQMRMQRNQFAANGGA
SQ  EYALDKEAEDEMKTFLTMQQRAMEVLSDTVNKDLRALDVIIKGLPELRQS
//
ID  F4HXV6;
PN  Nuclear pore complex protein NUP155;
GN  NUP155;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4HXV6;
DR  UNIPROT: Q9LQU6;
DR  Pfam: PF08801;
DE  Function: Major component of the nuclear pore complex (NPC). {ECO:0000305|PubMed:12034489}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQDDEIVMRDVTSAGICIGDRIGREAASQLDLEEALEASRYASHPYSTHPREWPPLIEVGETWELPSVLIERYNTAGGE
SQ  GTALCGIFPEIRRAWASVDNSLFLWRFDKRDGQCPEYSGEEQAICAVGLAKCRPGVFVEAIQYLLVLATPVELVLVGVCC
SQ  TEGPDGRDPYAEISVQPLPDYTISSDGVTMTCVTCTNKGRIFMAGRDGHIYELLYTTGSGWNKRCRKVCLTAGVGSMISR
SQ  WVVPNVFKFGAVDPVVEMVVDNERQILYARTEEMKLQAYVSGPNGEGPLKKVAEERNLLNQKDLSQGNRQSAVAGRSNKP
SQ  SIVSISPLSMLESKWLHLVAALSDGRRMYLSTSSSGSGSTISFSGFNNHRQTPNCLKVVSTRPSPPLGVGVGLGFGAASV
SQ  AGRTQNDDLSMKIETAYYSVGTLVLSDSSPPAMSSLLVVSRDSSVHSQAGSSSGPSSRSSRALREVVSSLPIEGRMLFVA
SQ  DVLPSPDTAATIQSLYSELEYCGVEVSGESYEKACGKLWARSDLSTQHILPRRKIVVFTTMGMMELVFNRPVDILRRLLE
SQ  SNSPRSLLEDFFTRFGVGEAAAMCLMLAARIINFEDLISNIVADKAAEAFEDPRIVGMPQFDGSSGLSNTRTATGGFSMG
SQ  QVVQEAEPIFSGAHEGLCLCTSRLLFPLWELPVMSKKTSSDTMSEDGVVICRLSTSAMHVLESKIRSLEKFLRSRRNQRR
SQ  GLYGCVAGLGDVTGSILYGTGSELGATERNMVRNLFGAYSNGGESANKRQRLPYSPAELAATEVRAMECIRQLLLRSAEA
SQ  LFLLQLLSQHHVARLVQELDANLKQALVQLTFHQLVCSEEGDQIATRLISAVMEYYTGSDGRGTVDDISPRLREGCPSYF
SQ  KESDYKFYLAVERLERAALTSDAEEKENVAREAFSFLSKVPGSADLQTVCKRFEDLRFYEAVVCLPLQKAQALDPAGDAF
SQ  NDQLDASIREHALAQRKQCYEIIANALRSLASPLASPTLDEASRSQYICQIVHLGVQSTDRAFREYLYKAMIELHLENEL
SQ  LEYGGPDLVPFLQNAGSHSESQVGAVSTGSSPLGHSGTQISSDQAKYFDLLAKYYVSKRQHVLAAHVFLRLAERRAISLG
SQ  DSPTLERRRDDLSQAVLQAKNASNSDGLVGSAQGVSDSGLLDLLEGKLAVLQFQIKIRDKLEAIASNFESSVAMQDSDQN
SQ  GQVLDGDSSDDTNLANAANEMAMEVSSELKSVTQLYNEYAVPFELWEICLEMLYFANYSGDADSSIIRETWARLIDQALS
SQ  QGGIREACAVLKRVGSHIYPGDGVVLPLDVLCLHLERAALERSERIENVRDEDIAKALLAACKGAAEPVLNAYDRLLSNA
SQ  AVVPSPNLRIRLLRSVLVVLREWAMSVLSDRMGSSPTRSSLILGGSFALENKAALNQGARDKIANAANRYMTEVRRLALP
SQ  PNKTDGVYAGFKELDESLLSPFSF
//
ID  P89457;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10315;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P89457;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10993927}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MAGMGKPYGGRPGDAFEGLVQRIRLIVPATLRGGGGESGPYSPSNPPSRCAFQFHGQDGSDEAFPIEYVLRLMNDWADVP
SQ  CNPYLRVQNTGVSVLFQGFFNRPHGAPGGAITAEQTNVILHSTETTGLSLGDLDDVKGRLGLDARPMMASMWISCFVRMP
SQ  RVQLAFRFMGPEDAVRTRRILCRAAEQALARRRRSRRSQDDYGAVVVAAAHHSSGAPGPGVAASGPPAPPGRGPARPWHQ
SQ  AVQLFRAPRPGPPALLLLAAGLFLGAAIWWAVGARL
//
ID  Q7Z2G1;
PN  Histone H2B type W-T;
GN  H2BW1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15475252}. Chromosome {ECO:0000269|PubMed:15475252}.
DR  UNIPROT: Q7Z2G1;
DR  UNIPROT: B1AK72;
DR  UNIPROT: Q147W3;
DR  Pfam: PF00125;
DR  OMIM: 300507;
DR  DisGeNET: 158983;
DE  Function: Atypical histone H2B. Nucleosomes containing it are structurally and dynamically indistinguishable from those containing conventional H2B. However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes. May be important for telomere function. {ECO:0000269|PubMed:16449661}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6NXS1; IntAct: EBI-18200422,EBI-10251630; Score: 0.56
GO  GO:0031965;
GO  GO:0000786;
GO  GO:0003677;
GO  GO:0046982;
GO  GO:0006334;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRTEVPRLPRSTTAIVWSCHLMATASAMAGPSSETTSEEQLITQEPKEANSTTSQKQSKQRKRGRHGPRRCHSNCRGDS
SQ  FATYFRRVLKQVHQGLSLSREAVSVMDSLVHDILDRIATEAGRLARSTKRQTITAWETRMAVRLLLPGQMGKLAESEGTK
SQ  AVLRTSLYAIQQQRK
//
ID  P14998;
PN  Agnoprotein;
GN  AGNO;
OS  10631;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000250}.
DR  UNIPROT: P14998;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFCEPKNLVVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS
//
ID  P34343;
PN  Nuclear pore complex protein 15;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12937276}. Note=Recruited early during nuclear envelope assembly after mitosis. {ECO:0000269|PubMed:16950114}.
DR  UNIPROT: P34343;
DR  UNIPROT: Q5WRU8;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Important for early nematode development. {ECO:0000269|PubMed:12937276}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0007275;
GO  GO:0031081;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGRDLELTLDRVSSIEYPALVKEAFLNNWHASAHRSEVTSNCASLNDRYCWVLSRNQIFIWERAKSSHRAIIPTQLPLP
SQ  TSGLPRSVKCVVVYDGVHRGANKTPCPGILVVSPEGVLRHWTSIESQTYIEEVLDINNEVALRVELTDEPIDGKSASFLL
SQ  TTTSGTVYFLNGKGQDSAKTGALECNKVAGREAHGFRRRLSSIMFGGESKESTSLITNSFQHQSKDLLVVTVSPDVLTVY
SQ  NMYTPCELWSLKTKEFFQPKIASFFEADLKRTPLKVRARLIDAAVFRDGLMILIGGTHEESQSVHMFMVWMSANWQTEQP
SQ  TGVVWSARVPMNEHRALFSKIDDSIYSNLTLCIPKNTAESKKADRTDGIIIINPYFAVSLYLPFDLAKPKKPESLYRHVS
SQ  IPPRDQLLGYAICSQYVYIMMLESGVSTIRLLPRGFADSSIYTHEQVVVPSLSVGTDDWPILSELLSEMVASGLPKTPLY
SQ  QSLHRAFELFAEKHMAESEEELKAIIKMPDQEIARIVSQFLYAIIDYSDAANKTDTELHAKRVLTSRIMLFLKHMGVYER
SQ  IISSPLGISRGGILSLRVGGTMLGEVSERVAASTAIWTWKTSNETNSAVFDAIIEKVLRIPEVQDLGLKDKDALFGRCGL
SQ  VHHIPVVAAQQLEKNVIGKTKSHRFEVFHAVCELLSGIKETIISWRNCRTKVAIPKFPIWWTLETFASCYRDVAEKIIEE
SQ  LKNGSSTDSERARLLMYILSIYDFYLSESDSQPDNDKVLQEMIALGKPADAMELAEKHKDFGTLVKNYLTTDVGTRQKTF
SQ  ERYKKMFEKDDFEMYLCDYLKEHGRNDVLLQQGGSRVDAYLDNFKELRYSREIANKQFGKAALTLMSLADAETKSFSKFV
SQ  EFLTRAYYCACSSIDGTDVSEVLDFYKRRYPEMKHRKRIPTEILKICFGNDLDAMMSVEDMLEWNMAVQPNDEASVEGFA
SQ  RAFHLLADLLAVHPDSDELKKKIDKTWKALVDYDEWNRVRSKEDVEKKTIFGKFCNYLINSYPADKGDSFPIWMPISRRL
SQ  IFPTDIDTVLDECIANTTGNHLSWIKGHLKWIGEQLCKQALLPKSAFFRPDMKQVGSISQAALEAFGPILQRREQRFIDQ
SQ  LNRDSMMET
//
ID  G0S7B6;
PN  Nucleoporin NUP170;
GN  NUP170;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P38181}. Nucleus membrane {ECO:0000250|UniProtKB:P38181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38181}; Cytoplasmic side {ECO:0000250|UniProtKB:P38181}. Nucleus membrane {ECO:0000250|UniProtKB:P38181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38181}; Nucleoplasmic side {ECO:0000250|UniProtKB:P38181}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P38181}.
DR  UNIPROT: G0S7B6;
DR  UNIPROT: G0ZGU4;
DR  PDB: 5HAX;
DR  PDB: 5HAY;
DR  PDB: 5HAZ;
DR  PDB: 5HB0;
DR  PDB: 5HB1;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. {ECO:0000250|UniProtKB:P38181}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S156; IntAct: EBI-4325479,EBI-4325171; Score: 0.68
DE  Interaction: G0S4T0; IntAct: EBI-4325187,; Score: 0.53
DE  Interaction: G0SFH5; IntAct: EBI-4325194,EBI-4325479; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P38181};
SQ  MEPMTPMRPIPGAYVNTPAPPTANPARRRLFTEASSSGAAATTQLGAAPAPLASTMAPGPEINSGLMTPQAREDLPPVAK
SQ  AAQVVNQTLQLDDSYPDLDSYCRPGASSDYEMQSSDSSWAPFHVVRHHNIPDKVFEHLNAGEVFTKLGLFAEIGYAWASI
SQ  DSSLFLWDYTHPNPELIGYEEATHTITAVALVPPKPGVFVKTITHVLVVATTSEIILLGVSATPTPSGSKSLTLYSTRMS
SQ  VHRGGSDVSFIVGTKDGRIFLGGESDTDIHEIFYQQEERWFSSRCGKINHSHPGWSAVVPSLAGLPFGSRQQEWLRGLYV
SQ  DDTRNLLYSLSNRSTIRTYHMEGPEKLTKVIEKDKTSCLRDFAHMADSSPLFTDKTNIVALSPIPATEASKLHLMALTDT
SQ  GCRLFLSATSSASYTMGGATSLAPQSMQLQFVKFPPRESPTRIRTLNGQIIDSQLDKTSRALDPSALGFRFSPGYFFDVV
SQ  RKHPNQDMLFVSAPDTGRIKVTQPASALKYFEQGTWIELENGNRTIEIGLTTAPFAAAKQPLGFGNELAVQFDQVPGEFA
SQ  VLTNTGVHIVRRRRLVDIFAKALGNCVSASDDALEREVRKFINQYGRVETIAAALAVACGQGSDLRTGTGRGMDRNTENL
SQ  ARAAFIEYGGQPRLAESDGKQSVSESVRLSSRHDALALYLTRLVRTLWKAKVVQVGSGSDISSTIPTSKLVTIQENVERL
SQ  RNFLEANKSTIQGLAPPSERLFGRQEDIANQKEHQALHALQKLMESISEGISFVLMLFDERVSDIYARLDAVSQQQLKDL
SQ  TYEQLFSQTPGKELAKVLVKAIVNRNIASGANVETVADALRRRCGSFCSPDDVVTFKAQEQLQRASEQAHNSPVLRALLA
SQ  ESLRLFEQVAGSLTPANLTTAVEQYISLKYYAGAIQLCLTVAQQKDRGNTALSWVNDGKPANDSRKKAFDERKICYNLIH
SQ  QVLDKLESDFAGEPELVDGRPTLAATKRMEAYNVVNDSSDEVFHFDLYEWYIEKGWTDRILSIDSPHVITYLQRLAETDF
SQ  RHAELLCRFYTTRSRFFEAAQVQTNLAKSDLNISLKDRIILLSRAKGNASVNTIGISRQQQQQLNHEASELLEIAHIQDD
SQ  LLERLVADPRIPEERKAEIEEFLDGPIRTLTDLFNDYADQANYYDLCLLIFHAADFHNPRTILDTWNNLINQSHFEAEQR
SQ  REYWEIVQAGGDLPAGVIAPIAEPPLPYVYVSQQIQLIAHRTSLDSLIFPVNSLLPVVCAYAINNGQDASIGADPCWPIQ
SQ  LFLNLGVPHALVVQVLENVLDTQEAPFTGRRRKLVVQWIAMAVDMWVREVERRGAMAAAAASGASGSEAVMGSWVSELLG
SQ  RADQVLTQIAGTGATLRGGAASDAEEIASLRRTVKGLKRSVDMLLGGEMARMSFFR
//
ID  G0S4X2;
PN  Nucleoporin NUP49;
GN  NUP49;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02199}. Nucleus membrane {ECO:0000250|UniProtKB:Q02199}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02199}; Cytoplasmic side {ECO:0000250|UniProtKB:Q02199}. Nucleus membrane {ECO:0000250|UniProtKB:Q02199}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02199}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q02199}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:Q02199}.
DR  UNIPROT: G0S4X2;
DR  UNIPROT: G3EQ72;
DR  PDB: 5CWS;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000250|UniProtKB:Q02199}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q02199};
SQ  MSLFGTNTTSQTPAGGGLFGTTTSQSAQTGSLFGTATSQPQQTGGLFGSTATQTPSSQLQSTGLFGSTTATSQPQQTGGL
SQ  FGSTTTTTSQPQQTGGLFGATATSQPQSTGGLFGNTTTTSQPAQTVGLFGTTTQPQPAQSGGLFGSATQQKPATGGLFGS
SQ  TTTNTGAGLFGNTSNTIGGGGLFGQTAKPATGGLFGQSTTQPQQQQNATPGLTMGQSTNTQQQVVPGVRIDLSNIKSTTR
SQ  FNDLTEALQQEIAKIDEEIQKCIRDKEAVDAFLPAHGEQLAAIPTDVNFVTRKSEGAHNALSSDILAIDQLRELVKQDAD
SQ  NARLSFKAIDNLKLPMQYHQAGLWSKQMGGAGTAGASGASADADGQSNADLISYFSKTADEMEEMMKKFEKTITEIEAHL
SQ  TGVEAHAMAMQNVAAQSRNAAQGGVDERVYELAAVLREFEESILKVAGVVGGVKEGVTELQLRDFMGHGS
//
ID  G0S8I1;
PN  Nucleoporin NUP56;
GN  NUP56;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32499}. Nucleus membrane {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side {ECO:0000250|UniProtKB:P32499}.
DR  UNIPROT: G0S8I1;
DR  UNIPROT: G0ZGV9;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:P32499}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P32499};
SQ  MADDPHNTSTSDVSELVPDNTEPSAANVKEDAETTAARRELKQTTISDKAKRDSAQLSQEDDKSASEEDDNKSDAGEPEK
SQ  KKPRTSRGLTPEVQLAAPKQEVPKETVASPKKRTHDELEQDGKEEEEKKEGEKPSSQNRAERDEPEKKRPRDRQASLSVE
SQ  RDGQKEVEPLSAQESRPSSAEKPKIEEKKDESKDTKVDKPQTSSSAFANSSMAKFASSTTSPFGAFGAAAAGKTNLFGLP
SQ  ATSSNIFGSKSADASAAPAGPPKLSFGSASAASPFASLNGQAGGMSSLFKSPFASAFSGGSSALKTAGATGFGKPGEPLK
SQ  TGKSAKPFGAPESDEEDEGEGEEGEENKSENGEGEEKEEEEKEEKASGEEKKKFKLQKVHIDDGEGNETTLLSVRAKMYV
SQ  MEKGVGWKERGAGMLKVNVPKQAVEVEEGNQPDADSFDPAALDDAARKLVRLIMRQDSTLRVILNTPILPAMKFQVNHKL
SQ  KAATVLFTAFEGGEARQVQMKMSQANATQFSNMVEKIKEKLAAA
//
ID  G0SBQ3;
PN  Nucleoporin NSP1;
GN  NSP1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14907}; Cytoplasmic side {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14907}; Nucleoplasmic side {ECO:0000250|UniProtKB:P14907}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P14907}.
DR  UNIPROT: G0SBQ3;
DR  UNIPROT: G0ZGU1;
DR  PDB: 5CWS;
DR  Pfam: PF05064;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport. {ECO:0000250|UniProtKB:P14907}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P14907};
SQ  MSFTFGQPSTSGASGQSNTSTAPASGGLFGSTTGSSTPAFSFGNTSGTQSGSLFGGATTGQKTSLFGNTSSTTPAGTPAT
SQ  SLFGQSTSSSSGPSLFGNASKPSGNLFGNTSTSAAGSSTPAGTPSLFGSKTATTSAGASSTTPAATAGSGSLFGSTTATT
SQ  QGSSTPTSTGLFGGSSTASKSLFGSTTTPATGTSGSQTTPAKPLFGSFGSTTPAGAPPTDATKTAGLFGNLSKPATTGTS
SQ  TPTLFGSTSATTQGQSSTPLFGAKPAETSTTTAASGAATPATSAPASTTPTLFGGATLTSSAPAASTSTSTATASTPAAT
SQ  KPLFGATATTSAPGSSTTTATPGLFSTTPATTAAAGSSTATSTLFGTKPATTTAAAASSTPAATSTPSLFGSKPASTTAP
SQ  ASGTPTTTTAPASTSAPATTTAAPTSGASATASTTTAGQDAKTTTAGLGASTVGPQSQLPRLKNKTMDEIITRWATDLAK
SQ  YQKEFKEQAAKVMEWDRLLVENGEKIQKLYTSTYEAERASNEIERQLSNVESQQEELTAWLDRYERELDELYAKQMGSAA
SQ  GEQAAGPDQERERTYKLAEKLTDQLDEMGKDLAKMIKEINDMSNTLSKGSKPDDPLTQIVRVLNGHLAQLQWIDTNAAAL
SQ  QAKVAAAQKAAGSMGANVPGTETDAAESFYRSYRGGLK
//
ID  P40532;
PN  Nuclear membrane organization protein APQ12;
GN  APQ12;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
DR  UNIPROT: P40532;
DR  UNIPROT: D6VVP2;
DR  Pfam: PF12716;
DE  Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport. {ECO:0000269|PubMed:15273328, ECO:0000269|PubMed:17724120, ECO:0000269|PubMed:20016074}.
DE  Reference Proteome: Yes;
DE  Interaction: P32589; IntAct: EBI-8648,EBI-25002; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-25002; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGI
SQ  YMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK
//
ID  G0S381;
PN  Nucleoporin AMO1;
GN  AMO1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49686}. Nucleus membrane {ECO:0000250|UniProtKB:P49686}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49686}; Cytoplasmic side {ECO:0000250|UniProtKB:P49686}.
DR  UNIPROT: G0S381;
DR  UNIPROT: G0ZGU0;
DR  PDB: 6B4G;
DR  PDB: 6B4H;
DR  Pfam: PF00642;
DR  PROSITE: PS50103;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). AMO1 is specifically important for nuclear protein and mRNA export. {ECO:0000250|UniProtKB:P49686}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P49686};
SQ  MTVCRFWQQGYCRNGNACKFEHPPKGGQNYNRFGALSGSGQGMGGRVSEPPHYPGLSEDAIQKDLTSELPTWILSCYGPG
SQ  RDAPEQLFGGYPREQSFEEIRLHFYNGLMAGNPQGALNEIQAAYQAAQQQIQNTLQNIPAAVQFILDAANKHPNRIDICR
SQ  ESSKGSSTGGSVFGRNVNPFQQSSAAPLNPFGAPSTPSTSAFGQPSPLGQKSSAFGTPAFGQPSQPVSAFGKPSALGGGS
SQ  AFGSPQTGSTFGQPSVLGAKPSAFGQPAFGQPAFGQPAFGQSAFGQPSALGPKPGAFGTSAGSAFGASTTTAPSPFGAAA
SQ  QATQPANPFGQPSQQAANSFGKPAAPASAFGQPSTTTAQNPFGQPSTQSSAFGQQQPQQAGTFGSPSLFGQQQQQPSNVF
SQ  GQPSTTSAFGSQAATSGFSQLGNATSTIGASPAGAQAPASKSPYHPGSTRQHPDLLSYATKNPAGGLDTFKGKPVVYETP
SQ  KGAAKPVPHIRQFDGTLVRIWMPDGAPAYTADTEAEDPKVYEDEGVKRQWQSFLEKGRFEGGMPEVPPRREWCVWDF
//
ID  O94756;
PN  Meiotic expression up-regulated protein 14;
GN  meu14;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:12759375}. Nucleus membrane {ECO:0000269|PubMed:12759375}; Peripheral membrane protein {ECO:0000269|PubMed:12759375}; Cytoplasmic side {ECO:0000269|PubMed:12759375}. Prospore membrane {ECO:0000269|PubMed:12759375}.
DR  UNIPROT: O94756;
DR  Pfam: PF13805;
DE  Function: Has a role in nuclear division during meiosis II where it stabilizes the proper segregation of the spindle pole bodies. Also has a role in the formation and extension of the forespore membrane. {ECO:0000269|PubMed:12759375}.
DE  Reference Proteome: Yes;
GO  GO:0036286;
GO  GO:0035974;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0070056;
GO  GO:0070057;
GO  GO:0008289;
GO  GO:0031322;
GO  GO:0070941;
GO  GO:0006897;
GO  GO:0140043;
GO  GO:0006469;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12759375};
SQ  MPKSSNLKMQRKGSLRENGLVKGLNKNKFSISKLKELSHADDSRKSHRIIRSGKSSGEAYKQAGKGLMNLGNHLSDWGAK
SQ  SSNLSLNDISDKIGVLVSELGETEIEFVKAFNENRIKFKAIRAMEDSIAPSRAHRQRLISSIEREEERDPLSPKLTDLQN
SQ  QLVRTEAENLVGEMQLDNTSREVFKSSFQGLMDAFQLRAQKQMTLSYYASQLAELINDEVAYPGDNPAAYSQKYATQIMH
SQ  QCVESMARLLAPVTSETTEHVGSDCEFTRKSSSSVEFSDHSQDSGDPSQQNILQVKNVQAVLSIPEAESYKAQLLSSIAE
SQ  EQKKKELQAKSTVFL
//
ID  G0SFH5;
PN  Nucleoporin NUP188;
GN  NUP188;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52593}. Nucleus membrane {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52593}; Cytoplasmic side {ECO:0000250|UniProtKB:P52593}. Nucleus membrane {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52593}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52593}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P52593}.
DR  UNIPROT: G0SFH5;
DR  UNIPROT: G0ZGU5;
DR  PDB: 5CWU;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization. {ECO:0000250|UniProtKB:P52593}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-4325173,EBI-4325194; Score: 0.52
DE  Interaction: G0S156; IntAct: EBI-4325194,EBI-4325171; Score: 0.52
DE  Interaction: G0S4T0; IntAct: EBI-4325194,EBI-4325187; Score: 0.35
DE  Interaction: G0S7B6; IntAct: EBI-4325194,EBI-4325479; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52593};
SQ  MATLTDRTYLPPLEDCLTGRTVILSWRLVASALEDADLARLTSPALSTFLRDGFVHELLKHPARVFEPKDLKQEFETKTS
SQ  SIQTVAPGVDTIKKDALWLADAVAINQVAALRIVLIEYQTRAHSHLVLPLSTQDVANIQEAAGVGDAHASSILSLLNPAS
SQ  AVDAETMWCDFETEARRRERILATYLSERRSFTAAVDALVTFLLHSAPGQHKDLDSLRRALLKDAFAFDEDLDVPDRSKL
SQ  LTMAPTYMNLVEDCIARAQALPAKLGESFKTEAFELDWLRTAITEAVHSLSIAFQALDLDTPYFAPHELLSEWFELMNSS
SQ  LFLESILGFEVVADLAMPARSLVSAICLKMLNIDRTIQFLHDFDYPDGEEPYLLSSQTLNKIHTAVTNAVNSGVAASLPV
SQ  AFAWSLIVHQMHLGYQERAERRDLLVNQRAQAGFELEFQPSASTPNRRRRNSAGSIVSLEASPYDDFLREQRLDNDIAPV
SQ  EQIAMLATSRGQVYQVMSEMALCLGTTHEAAFRPAVGARARLVFQDLLKRSAYLIPYQDEPVFSLLAILATGRQYWDVTD
SQ  ALSASSLNQVYTDMLDDETLFTQFTMQAINRFPYEFNPFSVLCRVLAAALITNKDKADVVTGWLWRTPTLTVDWNPAWDR
SQ  SYELCFEDENTNSFRLTRDVDLFGSASPARPRHLAAEERFIIPEGTLGRFVTDVGRTARLEFEHSALALLGKRLEVKAAE
SQ  EICDSGMAPLDVDEQAEAVAMLATVLRAESLKSTAKGGDPEAPLKFLKEASRLLPHNKDILTVISDTIDGLVEKELLELD
SQ  GPQIAVLASCLQFLHAALAVCPGRVWAYMSRCALIAGDARPGRLSRITGSLDMYAERFDLLSSAVKLFAALIDSAACSAV
SQ  QRRAGSTALVSVRSAVENPWLGTSEKILSRVALAIAQAALDVYESTTTWRFRSELDRSILVRDVVGLMHKLVVHAHTLSS
SQ  HLTSTLSPAAAHIISSFLTPPPSASSLRFQPLLGTLLVALITPRATLYPGQSRILAERVTSVLAFCTSLLRAADFLGQTH
SQ  IPLQTHLFQSACLLARLPAANAVYRAPVLELLRALVEVAGRAANGSGEPPSLLGYLGSHAARSFISLVEGIDKPFGRVEH
SQ  AVVTWRFFAAVIRNRQQWMAGCLLTGRTPREALKGGGEQKIERKVGEGSVLAAAMERLREVKSLDVQEAVAVMDFVVSAQ
SQ  NYWPWTIFAVRKEKEVVDALRGYVRGLKAPGMVMKTDGAAAAAFQARIAAYVAETFAMQLYHMRQMRQAEKFAGELVADL
SQ  DYFLREGVMVWGYNASLHGNFARNFAKRFPGVEVDDFKRTMWLPRELGKGYYYALEVAEQMLGFDAGWGGVKQSGFRKEM
SQ  ETANLNLSLVEAQVSLFHAWEYLLLELTLSLLPKKENAAFARQVLQVVEQCLEANQRSQPPENIFVVLGHARAGLALTLL
SQ  QRLADANQLPRDVTHLLALVSSAIHAVENPFGANDLPYFRTLLKILFVVLRAAKQGTAKPGESNVAITQQVLTILDRVVA
SQ  RCFRALAALVHEQQQNATDGTTTAPEDLALITAILQACLSVPGIEQCQVQVLNIMAAHDVFQVAVALFSWADRLLPANPS
SQ  PASSSTSTSATNPASGDPVYGELALLFLLELSALPALAEHLACDGLLGHLAAARLAGYMRRTNVGPFAENAGAARCYAIW
SQ  AKCLLPLLLNILAALGSTVAPEVAWVLNQFPNLLQSSVERIEPPGFSRPTLSLASTPPRQKFISLLEISEIHSLALLTRV
SQ  LAACRAQNARDVPEVTWDGAKVLECVEYWLRGRKVLRERLVPLGPREVEWRGMVATGGVVGVAGDGGEGCENRLEEKAVG
SQ  LLVGVREVLEGGLEGEGE
//
ID  Q9W351;
PN  Aladin;
GN  Aladin;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NRG9}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26246606}. Note=During mitosis localizes throughout the spindle, is excluded from chromatin, and is enriched on the nuclear envelope remnants that surround the spindle. Present in a ring that surrounds the centrosome in prometaphase and metaphase cells. {ECO:0000269|PubMed:26246606}.
DR  UNIPROT: Q9W351;
DR  Pfam: PF12894;
DR  Pfam: PF00400;
DE  Function: Involved in mitotic spindle assembly. {ECO:0000269|PubMed:26246606}.
DE  Reference Proteome: Yes;
DE  Interaction: P34082; IntAct: EBI-868243,EBI-128210; Score: 0.35
DE  Interaction: Q95TJ9; IntAct: EBI-458558,EBI-128210; Score: 0.37
DE  Interaction: O97143; IntAct: EBI-162366,EBI-128210; Score: 0.37
DE  Interaction: P50445; IntAct: EBI-128210,EBI-166782; Score: 0.37
DE  Interaction: Q9VTU3; IntAct: EBI-128210,EBI-168651; Score: 0.37
DE  Interaction: Q9VEH1; IntAct: EBI-128210,EBI-118316; Score: 0.37
DE  Interaction: Q95TP4; IntAct: EBI-128210,EBI-467019; Score: 0.37
DE  Interaction: Q8SXP8; IntAct: EBI-128210,EBI-169165; Score: 0.37
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0072686;
GO  GO:0005643;
GO  GO:0000922;
GO  GO:0001578;
GO  GO:0090307;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:1902365;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALSNLKQCPPFSTLPDLALRHNHIPELERYPQINLNSELLANPAGQRYYGGQSFVSVNEGVLKRIARSFFNGGFWKTL
SQ  EEARSPETREQAPLIAQAGDLIAQFLGLATGLRILPHTQQLSAERIAQFVETRDWLNSDVRYLAWNQHFFCLAVAGVDDV
SQ  VRIYTKSSSATTATVLKSPSQTQITCMAWRPLCASEIVIGCRQGLCFWEVDSTLHLGRTNAPSEIFKYPNNLPITSMQWN
SQ  KDGTQLATASIGDRSIIIWQPDTGMMQPLKRLGPPGSLLKWSPDNDWLFAATVDRVFRVWNCHQQWTTERWVCGPGGYVQ
SQ  TACWSPCGRFLLFVSSAEPILYRLQFVQQSLLSSSADEKEILPIADLNACSIDANRTLVGGPAQQLAWDPHGNYLVVTFK
SQ  ATNCIAVFRTFIQKFDLQISAAYYLSGETAAEHPSFICFQPLYEDNDRSVLTIAWSSGRIQYYAFD
//
ID  Q9USL4;
PN  Nucleoporin nup61;
GN  nup61;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9USL4;
DR  UNIPROT: Q9UTW5;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. May play a role in mitotic spindle formation and/or function. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0008536;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0043547;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKRGADHQLTKDQDDSDDDRHGPVEVPKEASADVMATRKIAKPKSRKRPTSGVSSPGIFANLAAKPVSLPASTTQFTFG
SQ  KPAVTANNDSDIHLKKRGLNKSFIDAVIKSVDNNPFGNLSPLFDEYRQHFSSIEKKPAEEQPTSNAVVSEVNPQQQKSQD
SQ  SSSFVTEKPASSEKEDKEKPLVPPGAPRFGFSAPALGSSFQFNSSAFTPKGSFGEKSATEAEAKEKETSSNQTATGTAAT
SQ  TTNQFSFNTAANPFAFAKKENEESKPLTPVFSFSTTMASADASKETKQTHETKDSKSEESKPSNNEKSENAVEPAKGNTM
SQ  SFSWTPDKPIKFDTPEKKFTFTNPLSSKKLPASSDVKPPSAAAVGFSFGTTTNPFSFAAPKSSFPTSSTPASVGAEKSEE
SQ  TSNGNKSEQEEKENGNDETRSNDSLVSGKGKGEENEDSVFETRAKIYRFDATSKSYSDIGIGPLKINVDRDTGSARILAR
SQ  VEGSGKLLLNVRLCQDFEYSLAGKKDVKVPAASTDGKSIEMYLIRVKEPSTAEKLLAELNEKKVSKSEN
//
ID  Q8L7E5;
PN  WPP domain-interacting tail-anchored protein 1;
GN  WIT1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope. Nucleus membrane; Single-pass membrane protein. Note=During cytokinesis, aggregates around nuclear pores at the cell plate.
DR  UNIPROT: Q8L7E5;
DR  UNIPROT: Q9LFL8;
DE  Function: Together with WIT2, required for the nuclear envelope docking of RANGAP proteins in root tips. {ECO:0000269|PubMed:18591351}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1796628,EBI-1779367; Score: 0.57
DE  Interaction: Self; IntAct: EBI-1796628,EBI-1796628; Score: 0.40
DE  Interaction: Q9C500; IntAct: EBI-1779618,EBI-1796628; Score: 0.35
DE  Interaction: Q9LE82; IntAct: EBI-1796628,EBI-1779351; Score: 0.62
DE  Interaction: Q9M651; IntAct: EBI-1779567,EBI-1796628; Score: 0.37
DE  Interaction: Q9FH18-1; IntAct: EBI-1954306,EBI-1796628; Score: 0.51
DE  Interaction: Q0WQ91; IntAct: EBI-1796778,EBI-1796628; Score: 0.40
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  METETEHDRTVSVDDNDSLVPEPSSTKESFFEDLSLTGQVMNPQLSSAGEVLTKVELDFAFVSEKLVNLSLLTMQLGTRE
SQ  NDFESFVSKKEEDEEEPSSNVDDDDDSAEKALEFDLLSSILNSEVKELESLLGFLQNEIQSARVMISPFQHDGEAFLDLE
SQ  GKLNDTEQSLGQLMEQVVEMKKQSSNFQRLSSGLDEQGSWSGGQTSVSQNDGEFGDLSAKINMQTADQQRNVLRMLEKSL
SQ  AKEMELEKKLSESRNTERELEMKLYSSEQDVVYMEEVTEDAFSRWLEADNAAEVFKGTSKEMSGKLQILQFNLSGSFKRE
SQ  DNLKSKLVDSKERLEAKECALHKLDSSNARLADFLVAQTEGLKESLQEAEEKLILLNTENSTLSEKVSSLEEQLNEYGIQ
SQ  TEDADATSGALITDLERINEELKDKLAKTEARAEETESKCKILEESKKELQDELGNFRDKGFTIHKLASLEKHLRDSDLQ
SQ  LEHAVAAVEASKEKQNLLYSTVSDMEDVIEDLKSKVLKAENRADITEEKLIMVSESNAEVNEELKFFKGRLKEGEKYLQQ
SQ  AEERKLRTAKDIGVHNKIMKKLVMQLAAERERLHKQITNLSRENCVLMVKLKKVGKTGYMESGNGSEVSPKSDQNASSCH
SQ  QGSRLQATFISLTNPEEEETGSKSDIGSVRRLDVGALRFKHILVAILVILISSIAYVISQQNM
//
ID  Q6UDH4;
PN  Envelope glycoprotein M;
GN  gM;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q6UDH4;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGNYYYGGQESRLERISWRMWMVEAACYIVLVLLTLVSSFASLSSTTGFPCFVGTVGESSFGGDLMGHGMTPARRDGVKI
SQ  FFMSSPSTLFVVFSAVFVWLVVAVYLLLGGVRVKMCNFDSSYGASELSSAVATMTSLVTLSITAWAWQVFVLMLSYRQLT
SQ  LAAVAFVGIFIAGLVFMLSFASGGKSPENYATFNSQLKTVCKDVHAVITAFKAVVLNLFCVVFGVWHLMLVMLGAVIMVL
SQ  NFGVSIPKATTGALVVFIVLGLVYLMMIELVVSRYVHVLLGPHLGMIIALGIAGTSALSYAETLDEIMYASWKPVAAGIL
SQ  GAFSVIVLALAVLRAVRSYKFHKAAQSKFLQQVASVAQTVKNRARRERNGPRVHKRYYDAVPVDAYEDDPYRQSPRRSRH
SQ  GEAEDVIYENMKY
//
ID  A7MBC7;
PN  Nuclear envelope integral membrane protein 1;
GN  NEMP1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}.
DR  UNIPROT: A7MBC7;
DR  Pfam: PF10225;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGMKVAVLPAVGAGPWSWGAGGCGAVRLLLVLFGCFVCGSAGIDLNVVTLRESEILFMNTSRQSCYKNVLIPKWHDIW
SQ  TRIQIRVNSSKLVRVTQVENEDKLKELEQFSIWNFFSSFLKEKLNDTYINVGLYSTKTCLKVEILEEDTKYSVIVTRRFD
SQ  PKLFLIFLLGLTLFFCGDLLSRSQIFYYSTGMSVGIVASLLIIIFIVSKFMPKKSPIYIILVGGWSFSLYLIQLVFKNLQ
SQ  EIWRCYWQYLLSYVLAVGFMSFAVCYKYGPLENERSINLLTWTLQLLGLCFMYSSIQIPHIALAIVVIALCTKNLDYPIH
SQ  WLYITYRKMCKATEKTVPPRLLTEEEYRLQGEVETRKALEQLREYCNSPDCSAWKTVSRIQSPKRFADFVEGSFHLTPNE
SQ  VSVHEQEYGLGSIIAQDELSEETSSEEEDSDSRYPLVVQQNSFLT
//
ID  Q09904;
PN  Nucleoporin nup124;
GN  nup124;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10409764}.
DR  UNIPROT: Q09904;
DR  Pfam: PF08604;
DR  Pfam: PF10599;
DE  Function: Nucleoporins may be involved in both binding and translocation of the proteins during nucleocytoplasmic transport. In S.pombe it is required for the nuclear localization of retrotransposon tf1. {ECO:0000269|PubMed:10409764}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0000054;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPPVSKNTRTSSKTVKKPYDPPQGSSRPFFTVLKRAFSSVLHPFTSGLDEKASGTASKDRKSGRAGTKSLLTPELTPHYL
SQ  GKSPRIIRVSNRSHVRTIDGIEEKVHTNTFEPRKPKQKQDYTNSPTLFKRHDELSLKSLNSLHPSSALSKKLGSTSQHQI
SQ  ATPKSSASLLNILRSLHDEQKNTLNISSVKQDRITEANPTCEKRKPSRSPSPMLSKKKSVARASENEPSAKQNKSFSGND
SQ  SHKSLTDIRDKENGETEVSAKNHVPHRSSRRRRRHQRLIPIIYETLEQMDLRKPVLVNAEVQTDSNPGNTMFIDKQDIYH
SQ  RLSTPTSRKRQTLEKGHIKAFSAVDEDLDEIFACEDDVHYTALPKQNPKSERILEPIIASPKDNTSDKGLLTKSAPTFEE
SQ  LQASITPKPVKTSPNDTALTLANAEDNKTFEHQPLSKDTEAPKSQFSSSPTKESTTRKSEVEPPSPSKEIKSSHFSVPEF
SQ  KFEPKTEATTDKKLNVPKFEFKPTATADVQTNRLKENEPKPTFFAQLPSKTQETPSITENKPSFFSQLSPKREETEKKDN
SQ  APSAPASTSGFSFGGFAPKTLEEKEETKAPTFNFSLNNASSTQDTTKPTLQFNFGSSFGKPTSNIFNDKKTSENGLASST
SQ  VASESKPSAPESKPSSGFGNTAGSSPFSFNLTKESKEVPPTNSFSFAKKGKDEANDSLSAKASTPFSFAKPNTENVTTTA
SQ  PQFSFNFTKPNTDAKTNLLPEKTFNEEAVKQKETEKEVPPTGPKASEIKDSVSSNNAVPSSTFNFVSPFAAVSEKTNENN
SQ  IPNDTTKTNGNATKRTLEQTEDAKPFAFSFGSTTEQANKKASTSNETTKPQLDTSSKTDGVTANAPFSFASAFNAPKPST
SQ  NTADGKDSASNLTTPSPAFSFGNNSGVKASSNNNPSTNSSTAPFSFGTSNKPAFSFGSATSKTTSEGTAPAASASAPAPT
SQ  TSAFSFGASNSSMNKEENTPMAKDAGDTAPASGFKSGFSFGANNSPQPASMFGTSTPAPSSAFAFGNQSGTNPAAPAGFG
SQ  GITNTATNNPPSTGFTFTPSNAGSTAAPMFGAGNTPNPSGSINNASQAFAFGSGEPSNPASNPPSTGFSFGAATPSAFNA
SQ  SASQSPAPNGIQFNLGSSNSQTNAPPGRKIAVPRSRRKR
//
ID  Q9E6Q6;
PN  Envelope glycoprotein M;
GN  gM;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q9E6Q6;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MASRARMERNYRGLSHIDYVHKKMWVVQAVCFGIAVLVFFGTLVAASINLTEGFPCFFAAVVDYRTVNTTLVHTGLTYPR
SQ  LGGVVPVLFFQTKAVVFFFYATSIVFVFLVCYITVGAIISSKKHVGAAYMGSGAFVFSLMASPLTILLGTVSIWLLQAVV
SQ  IVLAHKLIVLAAAVYLVHFSTITFFYGYFCGRGVDSKVYAEDISSAKDIDGSLHKLIGNVRAMMVNLLSIVYSIILIMSS
SQ  LMFGMLLANSFTLKFWHVIVTVLITTSVLTLIYLLVIEFLIARYVHIILGAYIGLLIGYGMLWTTTCDYVNRFYYAMGAN
SQ  ASNLRIACHSVLAVFTVLILLAMVVRLIRASLYHRRRSTRAYAKAMKLQQNVKHRLRQLRRSYKQRGSQSEDERALTQSR
SQ  SAEASDEDTIYDRVYSGSESEWDD
//
ID  Q9VWS2;
PN  Nucleoporin Nup35;
GN  Nup35;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000255|PIRNR:PIRNR038119}.
DR  UNIPROT: Q9VWS2;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (By similarity). May have a role in the organization of the inner nuclear membrane proteins at the nuclear envelope together with Nup154 (PubMed:22718353). {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:22718353}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VH02; IntAct: EBI-106650,EBI-3430080; Score: 0.35
DE  Interaction: O46339; IntAct: EBI-137488,EBI-3430080; Score: 0.35
DE  Interaction: Q8STG9; IntAct: EBI-111134,EBI-3430080; Score: 0.35
DE  Interaction: Q9W0N3; IntAct: EBI-167011,EBI-3430080; Score: 0.49
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPMNLGSPVNSPGSNQTQYLPPFLLGDPQGITPHKNTLSPKTGRSNISFATSPGGSSPHELNRSALSTRTLFAAQGGAH
SQ  TAVGANSSTTAHGQTHSHHQTGPPTQGLFDSLREQSVTPKKKNHLGMLQLQSPNQSYQSSYHTNDSFAPGAPNAINASMR
SQ  ALCSPLGATASPAGGLGTSVTTGGNSRLSDFWVTIFGFPPGAGSMVLQHFTVCGTIVDVVHAPQNGNWMYVRYSSRIESD
SQ  KALNYNEKIIAGNVMVGVSRCTDRSVIDKENIGSVPNAEIGDPPTSPSAIRPFSQQSYKLARKDNIISPQKDVPQKSSGL
SQ  MDKAMDLIFGW
//
ID  P09298;
PN  Envelope glycoprotein M;
GN  gM;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P09298;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFN
SQ  ATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWG
SQ  LLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMA
SQ  ALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSY
SQ  MDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRT
SQ  NYPSQGYGYVYENDSTYETDREDELLYERSNSGWE
//
ID  P38114;
PN  Uncharacterized transcriptional regulatory protein TBS1;
GN  TBS1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
DR  UNIPROT: P38114;
DR  UNIPROT: D6VQE5;
DR  UNIPROT: E9PAD3;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: Involved in tolerance to thiabendazole. {ECO:0000269|PubMed:10628851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q12343; IntAct: EBI-20833,EBI-31503; Score: 0.37
DE  Interaction: Q12180; IntAct: EBI-20833,EBI-37549; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-8591,EBI-20833; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-20833; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-20833; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-20833,EBI-8659; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-13246,EBI-20833; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-19054,EBI-20833; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-20833,EBI-8648; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-20833; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-20833; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0043565;
GO  GO:0008270;
GO  GO:0006351;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNMDSGITSSHGSMDKTQKQSSEWAANQKHNQRVENTRVLMGPAVPAMPPVPSNFPPVPTGTIMSPQLSPFPDHRLRHHP
SQ  LAHMMPADKNFLAYNMESFKSRVTKACDYCRKRKIRCTEIEPISGKCRNCIKYNKDCTFHFHEELKRRREEALNNKGNGK
SQ  SVKKPRLDKENKFKDENFDIAVRSRNTSSTDSSPKLHTNLSQEYIGVSAGKSASDKEDTWPDFVPIDRTVLEKIELNHTK
SQ  VAGKVFVLEEICKNMKGTIEKLAEKSKIDVIDKEYMKRPKRKQYSKALLTKQKMFHFRQNVLSHLTDEEFLSPINEMFTT
SQ  TFKYSILQTKLVLDFSFRSASSPSSDNILYPLPRLAIAKRLLKNIKCPSLASLLHIVDVDQCLQFADVHFDPAKGRLTSS
SQ  QAFLLNICLCLGATVTNFEEKQELVDEDNHETYYFEKFELWRLRSFTFLNSVYYYHKLSVARADMTALKALLLLAKFAQQ
SQ  KISASSAVKVLSVAIKVALDLRLNLHSTYEDLELDEIIKRRRLWCYCFSTDKFFSVVLSRPPFLKEENTDVLTDESYVEL
SQ  FRDKILPNLSIKYDDSKLEGVKDIVSVVNLLANHLEYVPYIQSYFLSRLSLIESQIYYSCFSIRTTLDDTLDEIIENVLE
SQ  NQKALDRMRDDLPTILSLENYKENMRILSLDSSKLDFEVSCCTTILLHLRWYHQKITLSLFVISIIGDNLDQRESSRHDI
SQ  AEIIRRSRLDFKRNCIEVLNILKDFEYYPTVQNEFLYFSLTTVFSMFLYLSEIMVNDEHAMETGYIIGLLRDTHTRMLGS
SQ  EERCLSVHNLKWQTSLFFYTFFLRSTMEKFNLTSKYAKFYAFDSNYYEGVLNRLVKHTRESKDDMVELLKTSFINKEKMA
SQ  AFGSFVTEDQEKMEVSFNIFNEITIQDLNFLQFSSIPKLWENKTLEPGEEYHHSNGTNTDNNETTGADDTDDNNNNNNNN
SQ  NKNGNNSSSTINNNNNNYSNSNNNDNDNNINDDDDDDDDDDDDDDDDDDDDDNDDDYSNNGADDDEEDDDYDRSLFPTGL
SQ  ASLLDASYPERTANDYRDENEQSNKLFEKIEGHLEHGVFFYDRDFFFKNVCVKM
//
ID  Q9LW88;
PN  Nuclear pore complex protein NUP50B;
GN  NUP50B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9LW88;
DR  UNIPROT: Q8GXC8;
DR  UNIPROT: Q8LG62;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding. {ECO:0000305|PubMed:21189294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LU93; IntAct: EBI-2131524,EBI-2131512; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0008536;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0043547;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSDNAIPFSRKRTALKELSRDNPGLDDDDEDTSALESGTFNTASKEVLASRRIIRVRRTDRSATAPPASNPFTGIRLV
SQ  PFTAPAPSTAAAETTKPLSAGKQETLADGRSDATKETDGDSKEKSDAIDAVGKQETQGDEISAKTKDIIDGGEKEMSEAV
SQ  NSVEGGGAVNKNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDGNEDTEKNGDSGALSS
SQ  FHQHSSSKNAFTGLASTGFSASSFSFGLVPQEGSTGSGSEQSSFSFGQANNGNSSLFGASVATSITTKSTETTTAFPSKQ
SQ  DVSVETGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKG
SQ  ITFACVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSKPSVAEAAAPLKTPENSPSAEDA
//
ID  Q9VDV3;
PN  Nuclear pore complex protein Nup58;
GN  Nup58;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15086791}. Note=Present also in annulate lamellae pore complexes (ALPCs). {ECO:0000269|PubMed:15086791}.
DR  UNIPROT: Q9VDV3;
DR  UNIPROT: Q8SYM7;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000269|PubMed:15086791}.
DE  Reference Proteome: Yes;
DE  Interaction: P19339-3; IntAct: EBI-123251,EBI-199603; Score: 0.37
DE  Interaction: Q9VL73; IntAct: EBI-123251,EBI-113702; Score: 0.37
DE  Interaction: P40798; IntAct: EBI-123251,EBI-88209; Score: 0.37
DE  Interaction: Q9VJ62; IntAct: EBI-123251,EBI-154062; Score: 0.37
DE  Interaction: Q9W1H5; IntAct: EBI-123251,EBI-149103; Score: 0.37
DE  Interaction: Q9VT59; IntAct: EBI-123251,EBI-163656; Score: 0.37
DE  Interaction: Q9W0R9; IntAct: EBI-123251,EBI-94281; Score: 0.37
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFTPTTNNAIGGATAATGAFAFGARPATTTAPPPSFGAATSTPTFGAAPATTSLFAAPAATPAFGAPAATPAFGAPASTP
SQ  GFGATSTAAPAFGTAAATPAFGIPAATSAFGAPAATPAFGAAAATPAFGAPAATPAFGAPAATSAFGAPAATTAFGAPAS
SQ  TQASAFGAPAPAVGTVAPTFSFATPATSAPTTAPPAFGFGTTATTAAAAMPASLSSGIGSFSFPKPQATTAASLNFNTTT
SQ  TTATAQPFNTGLKLGTTNATTTLGGGGIFSKPAGQAAAPAASTFVGLGGIDVTATQPKLGDNKQDGIKIKETQVPDEIIK
SQ  TVDGLKAYIKQQKTISSDIGRTSTSKFTNVSHEITNLKWALQNMATLVEGSNQQIRLMRQETVKAIQSLEMAQRTQDTPA
SQ  GLQFENNAPFQYFQCLVAKYEQDLIAFRQQIALTERHMHAISNPQSISPDDLKRGFRQLNESFISLAGRLHEVHQRVEEH
SQ  KEHYLNLRRYRLRDTTNVFERIDNPPLPTVEPQRISSGPTPFSNISALMNKSYAAAASSASNATGN
//
ID  Q5R601;
PN  Vesicle-associated membrane protein-associated protein A;
GN  VAPA;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
DR  UNIPROT: Q5R601;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0033149;
GO  GO:0008219;
GO  GO:0031175;
GO  GO:0070972;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVML
SQ  QPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMP
SQ  KPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFI
SQ  GFFLGKFIL
//
ID  Q28H54;
PN  Choline/ethanolaminephosphotransferase 1;
GN  cept1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q28H54;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0016780;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGQRAAKRRTGDLHTEFPTSCGNPYQTACLLSKFIELPTPPLTRHQLKRLEEHRYQSCGKSLLEPIMQGFWEWLVEQVP
SQ  QWIAPNLITIIGLLINIITTVVLVYYCPTATEKAPTWTYLSCAIGLFIYQSLDAIDGKQARRTNSSTPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIP
SQ  VLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYI
SQ  LTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEHLVLWIALVLSFIDLIRYSVSICNQIASHLH
SQ  IEVFRIKTKVARFNHH
//
ID  G0S450;
PN  Nucleoporin SEH1;
GN  SEH1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P53011}. Nucleus membrane {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53011}; Cytoplasmic side {ECO:0000250|UniProtKB:P53011}. Nucleus membrane {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53011}; Nucleoplasmic side {ECO:0000250|UniProtKB:P53011}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P53011}.
DR  UNIPROT: G0S450;
DR  UNIPROT: G0ZGV0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. {ECO:0000250|UniProtKB:P53011}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P53011};
SQ  MSKAAAFLTDPPLVDDRPSFETILKHGHQDLVQAVAFNGHGDRCATGSVDGKIRVFNRLKEGIWRLCDNWTAHAGEILEL
SQ  QWLPTTVYPNLLASLGIEGRFKLWAEDPSAAPGRRFAESTRNGPLITIPSPRLSSHPSHLTHSQHPQQQPHHHHAPESIL
SQ  PSNPPPTSNPPQATGSTTAGSGAKPAFETRNPRSPYRSFSIKHIDDTRTTYLALLSADGGLTVYENDRVENLAAFSLMDE
SQ  FNVLDPTAATGPGQASTAPRGQETSFRVRFDPNPDVCYTALRDGVLSDALGLVVAVQDTVKVYRTRDAVRASLGLAAATK
SQ  EFYLAAEVVAGVHRGLVRDVAWAPGNIRGYDIIATACQDGFVRVFRLDTLSPSTSDTTKFAREPSSIDLTQGGELDDEKR
SQ  AQESAPESRWSSSRVRRHATRRQGPSQDALTITTSGLRASLDSHNHQQTPSRELDAADRRSRRAWTNQPGQVRHTLTEIS
SQ  RLDNHRTPVWRVAFDDDGQILGSVGDEGKLLCYRQKPDGTWAKSSEMSVVKVKMAAPQ
//
ID  G0S235;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32500}. Nucleus membrane; Multi-pass membrane protein {ECO:0000255}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:P32500}.
DR  UNIPROT: G0S235;
DR  UNIPROT: G0ZGV7;
DR  Pfam: PF09531;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:P32500}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAAVRRSPYKDFLQPALQRRFATATLVVLATAYFEALLLARWSSWLWSWFPLGPTGFRAALFFLCGIFVIILRISQYHP
SQ  GIRTSDSPIATLVRYAPRWTTFETLFTYALSAWIFSLVYLGTVPDDAGFERITYFTYDRARLNEKPIFLTTHLVLLGIYQ
SQ  GVRHLYSDIDRLSLGTAQPSNGDSSKATGEDGHVSTQMRRFRDQLPKIVVHSLHQSVMGLLLSASLYPLLLRDLLWRVNM
SQ  TMLRPLYSLPRTNVPPANLPYSPSTLLRCLAASVMVMFAWTAANTAFSLLLVKSPLKNGKPLTADAKDPNGSLLNGLKNK
SQ  KLSIKCFAMWELAYIARDFPDRRKAIFEDMDRKDGPMWSQVYKICLDTLHTLSSNIDAYTAPPAPATTPQQAETALGDKP
SQ  RTSAPPKEDHIFAPLPSNKSAFRTSVSSAFQNAALAGPGGPPASLSPVAKRTLHAARSRLLEAAAPNAEIEVTPSSFFRE
SQ  LALKYVLSSPLAGYPFRQTRRRRLASAVLGSPYGEPSLYVNAASAVSGLAVSSLREDRYGHVQRDVASLIRELTSLGEKL
SQ  NAFVNEGGMGKHWTDVVELEGEDKCEEVEEVVNAVKHALKRVIVAFEPYARDLRLTRGEVKKAREVAGLEQEVEVREVMP
SQ  EMVQIR
//
ID  G0SDQ4;
PN  Nucleoporin NUP85;
GN  NUP85;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P46673}. Nucleus membrane {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46673}; Cytoplasmic side {ECO:0000250|UniProtKB:P46673}. Nucleus membrane {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46673}; Nucleoplasmic side {ECO:0000250|UniProtKB:P46673}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P46673}.
DR  UNIPROT: G0SDQ4;
DR  UNIPROT: G0ZGU8;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P46673}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P46673};
SQ  MFRVPDDSILSSSPAPSTPDKSRRAGSSNLFRDSTASSAASTTPAGTPPVKFLGSSIMRPSDKNASSSVDDDQPAVGLFT
SQ  GIGGGVGVGMGAGTGATAAAKAAKKNLFAAVSGERRRNVPLGRSGRGHDSRQPSRLRKSIGVDDLEDEEEEEEKKKKPQL
SQ  LKPKGKVQEKKKDEPVRGLFTGTSLAPPPLSKAAAAATTTTTTGPTKSFGLTYEEFGESEEEDSGLTGGQDAEGELDDSM
SQ  WLERSPERPAIGDESDLLLMATPAATERVRREAEDIFRATAMGAGATTRRHEYRYASLAKDVYTQLGTAPLVEPPQLILS
SQ  TEALLEQLYDEGVGTHDDDARLDETLAAVAVQLINLWQDHVDAIAQPEEDGHVADIGPGPRASPFEKAYWLATLALQLHH
SQ  TRALDGGVEPLPATLFQWLNDRHDMYAGQVEEILRYRPSPACHSLFWQAVFMSLLRGRVKDATQLLRRAGWEHVRRGGQQ
SQ  RGEYAYSDRALENVLRVVDETVSVLESCPGYDGNWEIWSSEWTLFRVRAQGALEHLRRFAEGKDTSFGDSLFGSSTGSNR
SQ  GYTGYRDHTLAGLARRAESQVPWDVYESLNVVFDIVLGQQASILEAAQDWLEATIGLFGWWDERNNNNNNNNNNNNNNNG
SQ  YQKPGRTQALVLHSSPAHHINNDSESYLDRLARAFHAAVASDFHFNSQNPVEIGMACIFEDNIKGVIGLLRSWSLPIAAA
SQ  VAQVASLGRWLPPHRPKGMYALEDLDMDDLEVLGVDPGAPDEVDGVKDSTLVQYAQALVEYEGLETVRDRAGVYREGWEL
SQ  AISVLGRMDSPERSEEMVRDIVEHLVQGLTVDSTETVDRLWTMLNELSMITYAEEMTETFGDILARESHRYGEAMWYYAL
SQ  AHRPNKVREVMNLLISYSLIQSTAFPPAADLDDYLHRLLSDRKHTLEQYAKQDMEAAELLGKMLSGYAALRQFYDIRDNV
SQ  DATSISPVSRRQQAAAALISVIASSDDNIRGGLVDQTRDGIVSEDFLLALLGEALVFVSNPDNTFVHHGHAAVPILSQDQ
SQ  IDVLLKAVEDLTAVSERVYNVCDEFLQLVLASAPGGALKGSKPADLLKKGQDGQQMVLAGSSLIASQLQKSLLGGSGSAL
SQ  GKVPVKRGWDWREGMPAKMKGEDVIRRLRLGLAKDLARLWLAEADALVW
//
ID  Q5T0L3;
PN  Spermatogenesis-associated protein 46;
GN  SPATA46;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q4FZF2}. Note=Located throughout the subacrosomal area. {ECO:0000250|UniProtKB:Q4FZF2}.
DR  UNIPROT: Q5T0L3;
DR  UNIPROT: Q6X961;
DR  UNIPROT: Q8NEC3;
DR  Pfam: PF17734;
DR  OMIM: 617257;
DR  DisGeNET: 284680;
DE  Function: Plays a role in spermiogenesis and fertilization. {ECO:0000250|UniProtKB:Q4FZF2}.
DE  Reference Proteome: Yes;
DE  Interaction: Q93062; IntAct: EBI-750105,EBI-740322; Score: 0.56
DE  Interaction: Q9H0I2; IntAct: EBI-750105,EBI-744099; Score: 0.56
DE  Interaction: Q15834; IntAct: EBI-750105,EBI-739674; Score: 0.37
DE  Interaction: Q13077; IntAct: EBI-359224,EBI-750105; Score: 0.56
DE  Interaction: O43711; IntAct: EBI-750105,EBI-3939165; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-1047093,EBI-750105; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-3867333,EBI-750105; Score: 0.56
DE  Interaction: P50747; IntAct: EBI-750105,EBI-3915568; Score: 0.67
DE  Interaction: Q9Y343-2; IntAct: EBI-750105,EBI-11075770; Score: 0.35
DE  Interaction: Q99685; IntAct: EBI-750105,EBI-721306; Score: 0.35
DE  Interaction: Q14C86-2; IntAct: EBI-750105,EBI-21529077; Score: 0.35
DE  Interaction: P48729-2; IntAct: EBI-750105,EBI-2040168; Score: 0.35
DE  Interaction: O15151; IntAct: EBI-750105,EBI-398437; Score: 0.35
DE  Interaction: A2RUC4; IntAct: EBI-750105,EBI-21511702; Score: 0.35
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0007342;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENFSLLSISGPPISSSALSAFPDIMFSRATSLPDIAKTAVPTEASSPAQALPPQYQSIIVRQGIQNTALSPDCSLGDTQ
SQ  HGEKLRRNCTIYRPWFSPYSYFVCADKESQLEAYDFPEVQQDEGKWDNCLSEDMAENICSSSSSPENTCPREATKKSRHG
SQ  LDSITSQDILMASRWHPAQQNGYKCVACCRMYPTLDFLKSHIKRGFREGFSCKVYYRKLKALWSKEQKARLGDRLSSGSC
SQ  QAFNSPAEHLRQIGGEAYLCL
//
ID  Q9UT30;
PN  Nucleus export protein brr6;
GN  brr6;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9UT30;
DR  Pfam: PF10104;
DE  Function: Involved in mRNA and protein export from nucleus. {ECO:0000250|UniProtKB:P38770, ECO:0000269|PubMed:17993570}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:1990578;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSR
SQ  TRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKIL
SQ  QEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLL
SQ  TSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI
//
ID  G0S0E7;
PN  Nucleoporin NUP120;
GN  NUP120;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35729}. Nucleus membrane {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35729}; Cytoplasmic side {ECO:0000250|UniProtKB:P35729}. Nucleus membrane {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35729}; Nucleoplasmic side {ECO:0000250|UniProtKB:P35729}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P35729}.
DR  UNIPROT: G0S0E7;
DR  PROSITE: PS00678;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P35729}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35729};
SQ  MAFDNFEILYKETRLNLEPASPSSVVQLRVAPTNAYGRSSLSSSSSSRPASATADDEKGYRTKNLATASSIYYRKHHSSP
SQ  RGFLWRVLDNNTVLSIRVADVCRQEKVADAPLILNLRFASPLRPACVGFADHEDHDALFVYAIDQSNQLWSIILRPDHFR
SQ  KRSATEGGLGDASRVYSPPGFGFKHPHRLAVVSPDQLIVTMHDGGILKFDRNKNHESHGSPWRESIYNVAGWGQSLRGLV
SQ  PFQRNPTVRYEKINMELTAAASTAVTTMGHAETAFLFTICLDHRMRVWDVRTGQILYTGDILNNTKRDPQEVGKWTVDPS
SQ  QNNLIRILDNGRGQCLVVTYSPVGAGEFKFWKVKANDQGSIHVTDCFPDARLMSPNPTSLDVWTLADFAIAQQPDGPELW
SQ  ALWKNNTSYRVNRLQIIPRNATAPFADGWKAVCVESPGPTPRASGSWNPTDSTEKWLDLIFSPGRFSKSTLETALAMYEK
SQ  GLGTYKETVSRSGKGIAESICSVIGSTTTLDRSSQGGADYDQFRNTSETQWMRFWRLLLELDKQRGEALSLVFDQYDGMV
SQ  WVTCADLLAAVRQCSDLERLYHNLQSPEKKNEDVAALISAGLTFVETFSDSMHQLCKAALRAELYENSALSDRERMQLFL
SQ  DRAGFWVTDEDWAQVLDIVGQNYQMVTSRLYEDLFDLITATSEANSQELREPFTIFGKKVVVRAVQETVELHWQILFSQL
SQ  ILLVNMVDSESEEARPLHTRFDVGSVYRRLIDALRRLEHLRWMTKTELSVSPSKSRSGSSSPTLSKRGQDESYTRTALEE
SQ  LAGHLFGLPESNNMPLLSSITDLVLDLCAPTSTTVLNTWLIQCWLLKEGRPDLALELMPFAEQDPFSTYVQGRVFLALRD
SQ  YDTAAQHFRKAAIGLSIPLKHVDRHSAGLLDDTEWNLLNSGLPNYYAHIVNLYDKQKAYSYVMEFSRLALQFAQTSNQDS
SQ  ASIKTEMLSRLFTASTATSHFEEAHSALLAMDDEALQKSYLRKLLERMCESGQSSELISLPFSGLQNKVDEILAEKCRAT
SQ  RDVLNGVPYHQILYAWRISHNDYRGAAAILLDRLEKLRRSGEGDKLGAEDGENGAGNDALDTQVTRQYLIVINALSCVAP
SQ  QEAYILEDVPPPVPGKGTNDEEYSQTGSKRKLGKLNATSGEEDLDSRIEELARLLDSESAGDKKARPSSSSEEDQQLLER
SQ  MQKFSTAVRQEQGQQTPRRLLRLEDLRKQYQQELDRIVAIQNNQFALTADGEDEDEDMMDIA
//
ID  Q8GYF7;
PN  Nuclear pore complex protein NUP54;
GN  NUP54;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8GYF7;
DR  UNIPROT: O48698;
DR  Pfam: PF13874;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q8W4D8; IntAct: EBI-2015534,EBI-4474560; Score: 0.37
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0005730;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0036228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGTPSSSPSFGTPSSTPAFGTSSPAFGTPSATPAFGTPSNPSFSSGGFGSSLFSSPFSSQQPQQQQQQQQQQQPSSLFQ
SQ  QQPSSNFGFQSPFNNTAQQQQQTPFPNAQLTTQMAPVAPIPYSLADRDVQAIIEAYKEDPTNPKYAFQHLLFSVTEPQYR
SQ  VKPAAVSDIMWAEAMSKLEGMDSTERERLWPQLVQGFKDLSQRLKLQDEVLVSDRDRIKTTQSNVKMLQRHLQASTFPSI
SQ  ERLRQKEQSLQRRMLRVMRIIEGLEGKGFRLPLTKGEAELSEKLTAITRQVKGPGAELSRRVQSLQTISRAQANSIAAGS
SQ  SLYLPGSTKIDEQSLIDMQEVLQQETEAIGRLGNVLKRDMRDMEIMVAEDTEMALDS
//
ID  Q54MI3;
PN  SUN domain-containing protein 2;
GN  sun2;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q54MI3;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005773;
GO  GO:0031154;
GO  GO:0000281;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIINKKYILFILLLLFITSCTIVFSQQQQQQTEQSEQTEQAINNDVNNSINDIFENDSSKQLRQPQQQHTIVDDGNNNNN
SQ  NNNNNNNNNNNNNNNNNNNNNNNNNNNNNNPIDNKDILGLKKLALLKQFEEQKSKSENDINNDIVILNLENDNPNQIIET
SQ  TTTTLNNSNDNKNNIIDDNQDEKLNENIKEDKNEIKNEIKNENQEKDKGIIDVEKDENQPNIEEKGKEKQNLLEKGIENE
SQ  NQNENQIQIEKEKEIEIEIEKEKEKENKELIEESKTEKDNQQKENKENTNEINVTVVEEPEQPQPQQQNQQEQQEQQQQE
SQ  HKEEQQQQEQQQQEQQTQQEQQTHQQQQEHQETQKNSSEETKTQSPIQVNTTDVNNEIELKNEGDNNSQLNDSSIPITSP
SQ  LTNDNDTLKTTKEDSNNNNKNEVINNQTPLIDEKNHQHNYEGNNRNGDDVSIISNIPKTNKAPETQQQQQQQQQQQQQQQ
SQ  QQQQQQQQQQQQQQQQQQQQQQQQQQQHVVLTPNDLPDKFNYASSECGANVLQTNKEAWEVSSILASSRDRYLLNECNKS
SQ  QWFVVELCEEIGVQIIELANFEFFSSMFKDFIVLGSNRYPAQSWHYLGQFTAENSRKQQYFVLKEKAWYKYLKVKILSHY
SQ  GDQLYCPISSFKVYGSTMVDDLKNQVDINISELEKFQRDLSSIPYPMEIGSDTSYSTTTSTTSSSSTSSSYPSSKTKSSN
SQ  SEYPSWERIQSFSEKLRKNVEQQLIQPPSVLNTNDNNNNNNNNNNNNNNNNNNNNNNNNNEEQFIYYETNGNGGPPSTST
SQ  STSSSSSQNHQARTPQSVFKTLADKIKAIEFNQSIGNKFMEKLERYYSEEIKNLKFDVSEFLNDIIKLGNSLDEKLKDHR
SQ  KYDDNKFKETSKEIKILKEKIEKLEEQKSADRNFYLVVTLVSLLIGLLLKPLFTSSSSSSNKSYPNSMPNSPTYLNSGSN
SQ  NYNNNGIINSSGGSGGGGGNLQNSSFIGINGQLNFSDDNISAFLNSSCSNFGLNNNNNNNNGINNNNNNSNSNSNNNSIN
SQ  NGSININSNNSLQQRIHHNKYIHQRRNSSPLVGVQLESFFSPNAIPPTIPIVPQDDNNINYNYNNNNNTNNINNNYNYNN
SQ  NNNNNNNNNNNNNNNNNNNSDNYNNNNNSNNNVNSPSSPTPSSIILSPKFITSIPKNINYYNNGGSGSHLKNRFSRQASE
SQ  SVLSQNHYQINHQNHSLNGVTTNINNNNSNSNGNSNGNSNNMTNGLPPVSMPSSSSHDNLLLHRGNNQSKKYKRRSHL
//
ID  G0S6T0;
PN  Nucleoporin POM33;
GN  POM33;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q12164}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12164}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12164}.
DR  UNIPROT: G0S6T0;
DR  UNIPROT: G0ZGV8;
DR  Pfam: PF03661;
DE  Function: Contributes to proper distribution and/or efficient assembly of nuclear pores. {ECO:0000250|UniProtKB:Q12164}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPPPPSADVPLAERLQRLASTLQFAWFSGHALLLLCVFRYAFSWIRFNYYSGMARFCYRFAFIAAAATYGIVVYKTWRA
SQ  RQKTGVKTSGIKDYLRDENIQYLVLALVWLFMPQYPLALLPYGIYSVFHVATYVRANLIPTLVPPQRINAPAGASPNAKP
SQ  QYTQHPASEAIGVFVKKYYDSSMSMVARLEIMLWLRLILSVILFQRRSWILFAIYTTFLRTRFSQSIHVQNAFALLEARI
SQ  DNLIGAQGTPPQARQVWDNVKTAARQFYAVTDLNKYESGVAAPKKSS
//
ID  G0SB44;
PN  Nucleoporin POM152;
GN  POM152;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P39685}. Nucleus membrane {ECO:0000250|UniProtKB:P39685}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39685}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:P39685}.
DR  UNIPROT: G0SB44;
DR  UNIPROT: G0ZGV5;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs. {ECO:0000250|UniProtKB:P39685}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDAPAVGAFPQTPVAARRGPARPSDSTTSTTIKRTSPLPLAPQAGRQATNISPVIPLHILDAPTQRFYAFAFYLALTAW
SQ  KLYDWTQVLEEDTESFLLFLKWIAIDCVFLFGLPELRIPWLELSQPFVMVAFAIHAMFDWILMFNIGFPWQSWVIGLLKV
SQ  FYDREIAISEHNVKLSSILQNSSLIMGRQIINILPEGSAILNPELQPFCLGGDRKTANIPIFFNSTIPVEVELIRTDFET
SQ  GQQESIKLSKSQLRDIERRAKRESQDGDTVQSIVQFDFPVKKTGAYRLGRVLDEYKLEVQRRNPLTFVVSCPKAWVGPAL
SQ  SAHRCVGDLSDLSMMVEGTPPLKIKYSRMINGKDHSFHFQSLQPEGFVSPLSGLRSNNWGYDEDDISWARAQKVPVGLNE
SQ  SMHSSGDWQYSIDEVQDGFGNIIKYDSLADDPDGKPKPKHLTQSFVVKKRPVIRLEGCDLRHPLKVAKGKSKNLPVSYGL
SQ  SGGSREDSTYQIAWQFSPIDTLTESGDHGDVVTIGTYTAKNNRDRPTISAPGLYTLKSVSASQCEGEIQEPSSCLLLNPL
SQ  EPRLSLRHEEIPDTCAGNSIGLRVDLDLIGTPPFIVRYDVISNGERRSERVSIPGLRYQLDLVPRIAGHHKYIFTHVGDS
SQ  IYDGQKLSGPEYVLEQDVKPAAAALIQHSTGKMSSCLGDQVTVDILLLGDPPFTLEWELIHDGKRKQFKVPNIQENSYQI
SQ  KTAPLTTGGEYTLGLTSVQDKRGCRNFLQEELKISVRRQSPRAAFGQVDGKRKILAVEGSSVKLPLRLTGEGPWKVYYAN
SQ  LHDGSPDKPKVQEKIIKSDNGFLEVRGRGAFAITDVWDSQCHGVVDPKASRFDVDWFPRPELSVALTHGVSKTETGFQLQ
SQ  DVCEGDVSGFEVALKGTPPFTVEYEVRHHPLQGSSSLSKKKIEGVVGKEAIQADTSKAGTYTYKFTALEDDLYSSNRGFQ
SQ  PIIVKQNVNRKPTASFVKPGQTFKYCKSEQDNEDGIPITLTGVPPFFLEVEIKHQSAAVPEIYRTPAIDSHSYELKIPRH
SQ  HLRLGTQHIRIRDIRDGSGCHSTSGILSGPSVQVQLFEAPTIYPLETRTDYCVGERISYTLSGQAPFEVWYTFNGVELKA
SQ  KSPNTNFRRIAESPGEFTITSVSDKASECRAPVSITKTIHPLPAVRISKGKSVRVDIHEGGEVDILFEFFGTPPFEFTYT
SQ  RSTNARKGQKSQVLETRHDISHEHSKVIKASQEGTYEVVAIKDKYCSFSTQAVVGLEGGKKDKTKKLKVY
//
ID  G0S7R3;
PN  Nucleoporin POM34;
GN  POM34;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12445}. Nucleus membrane {ECO:0000250|UniProtKB:Q12445}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12445}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:Q12445}.
DR  UNIPROT: G0S7R3;
DR  UNIPROT: G0ZGV6;
DR  Pfam: PF08058;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:Q12445}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTLSVAKAASTPVKQITSAVGPVKESPGNWKHPRLAEITRRQSRNIFGEKNVRQIVYNVAAIVLLEIFRVFASPSIPS
SQ  QLILPSLRPYSLWIHAVFLVIPLTNIVIALLPLFRPVDDLSDIPLTPAQRKLLGLPPSSKPATPNSVYSTPPRYSRTPSL
SQ  AGSPASIKSYTSSTLPTASSPTPGAAGIGAGSPAAPIYLSPSKFTTSTSSQQFSPSPSGASPLLHRAISNTSTASGVSPY
SQ  GSPNSPSKFGASTNSTLAASTISTSTFSVSTTSSIAHVLNNSRLRESVIEGVPATPTPVGKGASVKANSKWLYQRGRRTS
SQ  SNNWVY
//
ID  P0CP30;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: P0CP30;
DR  UNIPROT: Q55VJ9;
DR  UNIPROT: Q5KKN9;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLF
SQ  LSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRH
SQ  GDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICST
SQ  CQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTV
SQ  ETPWSDESRVQEIAKWCDKGLSVVGMIYTDLTPSPDDITKTLYKRHAQSYTASSLEMLLSAAYQLSHPLSTRMSPTGHYS
SQ  SRFVTCCLTGDKDGGVDILAWQASEHAEAMVKAGIVEASVDPAVVRVRKPGEGEYVPEVFYSYKNEYGLQVKMPAKPTFP
SQ  VEYLYVNITHGFPLAPSPLFLSNAFPTENRPGLHDQSMQVVITQLAAILKTSDAEIGDAGTWPGRIKKDVEKWLSDWHLV
SQ  TFLCMQGLFSLKEQQILCRAATAHAHPNDTHALEELFASGGWQTLLTIVDSEASANARSNPPPTSSFNNLGIDSPAFAGP
SQ  STESSAPPSGPDSVGAGAGAGAGGGRERVCPHCTFVNEHGGSDCEICGLPLDG
//
ID  Q6SW81;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  295027;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q6SW81;
DR  UNIPROT: D2K3L8;
DR  PDB: 5D5N;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCA
SQ  VSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYE
SQ  NLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAG
SQ  PRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHH
SQ  RHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD
//
ID  Q3MHW7;
PN  Sigma intracellular receptor 2;
GN  TMEM97;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q3MHW7;
DR  UNIPROT: A1L510;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000269|PubMed:28559337}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGTLGARRGLEWFLGFYFLSHIPITLLMDLQGVLPRDLYPVELRNLQQWYIEEFKDPLLQTPPAWFKSFLFCELVFQLPF
SQ  FPIAAYAFFKGGCKWIRTPAIIYSVHTMTTLIPILSTLLLDDFSKASHFRGQGPKTFQERLFLISVYIPYFLIPLILLLF
SQ  MVRNPYYKSEEKRKKK
//
ID  G0S0R2;
PN  Nucleoporin NUP57;
GN  NUP57;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P48837}. Nucleus membrane {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48837}; Cytoplasmic side {ECO:0000250|UniProtKB:P48837}. Nucleus membrane {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48837}; Nucleoplasmic side {ECO:0000250|UniProtKB:P48837}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P48837}.
DR  UNIPROT: G0S0R2;
DR  UNIPROT: G0ZGU2;
DR  PDB: 5CWS;
DR  PDB: 5CWT;
DR  Pfam: PF13874;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000250|UniProtKB:P48837}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P48837};
SQ  MFSSLNTRPAGQSLFGANTGGGLFGQSLANQPQQQQQPLQQQQQQAAPALGQSQINQNQQLGGSLWQPGSLTAYQKPIPE
SQ  QIKLIVDKWNPNHPNCAFKTYLYNKVDEHTVPLYGPGPNEDPKEWEEALQRKPAPNFIPVLCSGFPSIVARLMLQRRVIT
SQ  EFNNKLHQINASLDAILSRHDLDHTVRAFNARRRHAELSRRCLHLAARVQVLRNRGYALSGDEDELKQKLQQIDKTLNDP
SQ  AQGSRLEELWSRLIVLRGYAEDLKDQINQAGITESDGLGEEIEAKAKKILEDYDKQLQHLKKQVEEAKKDFEEWEKQHNP
SQ  APAPAR
//
ID  O94464;
PN  Nucleus-vacuole junction protein 2;
GN  nvj2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Single- pass type II membrane protein {ECO:0000305}. Note=Enriched at the nucleus-vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833}.
DR  UNIPROT: O94464;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial- Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000250|UniProtKB:Q06833}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071561;
GO  GO:0008289;
GO  GO:0006869;
GO  GO:1990854;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQ
SQ  DQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELF
SQ  SNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWYYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSP
SQ  DTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADI
SQ  WYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNN
SQ  YLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRH
SQ  ISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASK
SQ  SFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESN
SQ  YSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSR
SQ  NQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL
//
ID  G0SDP9;
PN  Nucleoporin NUP152;
GN  NUP152;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32499}. Nucleus membrane {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side {ECO:0000250|UniProtKB:P32499}.
DR  UNIPROT: G0SDP9;
DR  UNIPROT: G3EQ77;
DR  Pfam: PF13634;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:P32499}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P32499};
SQ  MDPPSKKRSIFGGITSLFRSSTAPPEDRKGKSTNSNSVTANAPSLPPPQPESNGASSPFSPAKRASEAQLSVRKIIPKPQ
SQ  GPSSKLSQSVSASEIAHRPAPSTPAPAAATPVPKRRPGDNPHKLAASTSTPALQNLPNPPAPATSSKATSFSGAPSTPRP
SQ  SIFRNSLYARPAPATTYTQRVSSHPLTQSFPPVTPGRPGRAANVDINNRILSNTASTELFPMKIPEPPRHLTGEMLAKEV
SQ  PEDPNRAGSIYADEYLAHLCPPEFDDLQRRQFFCILDLRRLKYAADEVFLKKDWKINILNFAKEYEKSRSLIMLRYGLYE
SQ  FKTVRASEAVKREWKLKHGIPDSDDESGAPAKTNGGGKRKAEEDLEPSSSTFTHTASPNKRARATEAPATNKRKANDELE
SQ  EESQPSKLQKPGSPSPAKTPSATKSVFESIANKTASPQTAPKSSLFSSSTAAKPNGSIFDNAQKTPATSSNIFGHLSDAS
SQ  KDEDNESDTGSEAEAEDETPAKKKKKTTVNGASSSAPSEGGESTQSRSIFDRITRDANGQPVRQLPEGGLFSGESRKRSL
SQ  SPVKELPANNTWNASAGIKFATPGTSSIFGSSNPKPPATTDTIDFAASTTKKPEEAAAPAEAPKEATPTTNLFGAQTKAT
SQ  EEAPKPAATNIFGSTTNPTETSIPAGSLFSAKPATSTTNSLFGATTSAAGQKKDEESKPTEAAPAPAPATSTLFGAKPAT
SQ  TESPKTNLFQFGTPNKTETAPATQPQFGGLFGKPPSTETPTEKPATTSLFGTDASKPATTSSLFGSATTAADKPAATNLF
SQ  GSTTTPADKPTTTNLFGSTSTQATSGSDEPTAKKFAFGGTTESKPTTSLFGSTTPAPATSTENKGGLFGATTTSATPATN
SQ  TKPLFGSTPAPAQENKPLFGSSTTTAAPVFQFGSTPASTSTEQKPLFGATAATDSKPLFGSTSATSTEQKPLFGSSTTMT
SQ  EQKPLFGSISTTATEQKPLFGSTSTTEAKPLFGAAPASTEQKSLFGITPSTTENNPASIFGNSSTSTEQKPLFGSAPAST
SQ  EQKPLFGSTPSTTENKPAGLFGNTSTTSTSTPLFNFGSQNTTASQPSTTGSIFGSASASFTFTAGGSDGTIKNPFASDGS
SQ  YSAPTSFNFGSGDSQSSSAPFTFGAGGGTPSFTFGASSDSSNASNNASSAPIFSFGASQPSSTPLFGQNNPPAASNIFAS
SQ  SLAPVGGTSTGTSKHVPSFLESENKASAYSSLDSPFTFGGASSLATTPAASTPEPSAANAAAAGEDQGASADADEQPQEQ
SQ  ISLTDGGPGEEDESVVHEVRAKAVKLVTAADSSADSSNGSGEKPAEKKSNSPWKVMGVGPLRLLKHKQTGAVRMLLRAEP
SQ  RGNIALNKLVLPQFTYKPDAATPKFIKFAAARDDGKGLETWMIQVKTPQLAQELAAALEEHKKANEKKDGEKNEESEKKD
SQ  EKQEEKKNEEKKDEKEEKKDEKK
//
ID  Q8CEC0;
PN  Nuclear pore complex protein Nup88;
GN  Nup88;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}.
DR  UNIPROT: Q8CEC0;
DR  UNIPROT: Q80Z13;
DR  UNIPROT: Q8K090;
DR  Pfam: PF10168;
DE  Function: Component of nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}.
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-2553822,EBI-286642; Score: 0.40
DE  Interaction: Q8WYU3; IntAct: EBI-2553822,EBI-2555238; Score: 0.40
DE  Interaction: Q99567; IntAct: EBI-2553822,EBI-726178; Score: 0.40
DE  Interaction: B4DYZ6; IntAct: EBI-2553822,EBI-2562666; Score: 0.40
DE  Interaction: O14980; IntAct: EBI-2553822,EBI-355867; Score: 0.40
DE  Interaction: Q9EPK7; IntAct: EBI-6908541,EBI-2553822; Score: 0.35
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAVGPLGDGELWQSWLPNHVVFLRLREGVRNQSPAEAEKPAASTSPSCPSLPPHLPTRNLVFGLGGELFLWDAEGSAF
SQ  LVVRLRGPSGGGVEPPLSQYQRLLCINPPLFEIHQVLLSPTQHHVALIGSKGLMALELPQRWGKDSEFEGGKATVNCSTI
SQ  PIAERFFTSSTSLTLKHAAWYPSEMLDPHIVLLTSDNVIRIYSLREPQTPTKVIVLSEAEEESLILNKGRAYTASLGETA
SQ  VAFDFGPLVTVSKNIFEQKDRDVVAYPLYILYENGETFLTYVSLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAILCLPC
SQ  VPNILVIATESGMLYHCVVLEGEEEDDQTLEKSWDPRADFIPSLYVFECVELELALKLASGEDDPFASDFSCPIKLHRDP
SQ  KCPSRYHCSHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELTAEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPT
SQ  MICITSTYECLIRPLLSTVHPASPPLLCTQEDAEVAESPLRILAETPDSFEKHIKRILQRSAANPAFLKNCSARSSEKDL
SQ  APPPEECLQLISRATQVFREQYILKQDLAKEEIQRRVKLLCDQKRKQLEDLNYCREERVSHLFRKSLREMAERLADKYEE
SQ  AKEKQEDIMNRMKKVLHSFHAQLPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQRKMEKVLSPQKPTITLSA
SQ  YQRKCIQSILKEEGEHIREMVKQINDIRNHVTF
//
ID  Q05B45;
PN  Transmembrane protein 120A;
GN  TMEM120A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q05B45;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0045444;
GO  GO:0051291;
GO  GO:0051260;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHPPPPGPLGDCLRDWEELQQDFHGIQETHRLYRLKLEELTKLQNSCTSSITRQKKRLQELALVLRKCKPSLPSEAEEAA
SQ  RELENQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVT
SQ  DAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
SQ  QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLG
SQ  NFFTTLRVVHQKFHNQLHGSKKE
//
ID  Q9FWS3;
PN  Zinc finger CCCH domain-containing protein 16;
GN  CG1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9FWS3;
DR  UNIPROT: F4HZ22;
DR  UNIPROT: Q94C30;
DR  Pfam: PF18044;
DR  PROSITE: PS50103;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9XFM0; IntAct: EBI-25527280,EBI-3133404; Score: 0.56
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0003677;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRKELCRNFQRGSCRYGENCRFLHPQQAKPNNPFGFGTQNQQQQQQQQQQNSSNPFGFGVQSGGSSRPNQFQNTWSRTAS
SQ  TPTGGGAAASTQQTGKQTQPADHKCTDPAACKRVMQDDFKNERPMWKLTCYGHWKYFPCDVTGDISYEELRAVAYEEAKR
SQ  GIPLQSIVERERNLQNSKIAEFENFLRNPYKGSVTANQSPFAATTPSIFPQSSQINSPSPAFSGFNQQTAFSNTNAGGLS
SQ  SSGPPNAFASFNQQTTFPNTNAGGVSSSGPPNPFASFTQQSNNQQTAFSNTNAGGLSSSGPPNAFASFNKQPNAFSVNTP
SQ  QPVPSGPSGFQTNPSTTFKPASFGPGPGFATTPQNNNIFGQSTPTPATNTSQNNQTAFNFNVPVASFTAPAINTTNTSSG
SQ  TELQIGGDPVDSSIWLKEKWNPGEIPEQAPPDAFV
//
ID  P0CK47;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P0CK47;
DR  UNIPROT: P03183;
DR  UNIPROT: Q777G9;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-740019,EBI-2620189; Score: 0.37
DE  Interaction: P03185; IntAct: EBI-2620196,EBI-2620189; Score: 0.51
DE  Interaction: Q9UBX5; IntAct: EBI-947897,EBI-2620189; Score: 0.37
DE  Interaction: Q8N2S1; IntAct: EBI-2620189,EBI-947718; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-2620189,EBI-747754; Score: 0.37
DE  Interaction: Q02818; IntAct: EBI-2620189,EBI-2622179; Score: 0.37
DE  Interaction: Q12805; IntAct: EBI-2620189,EBI-536772; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-2620189,EBI-347552; Score: 0.37
DE  Interaction: Q8WXE0; IntAct: EBI-2622376,EBI-2620189; Score: 0.37
DE  Interaction: Q9Y228; IntAct: EBI-2620189,EBI-765817; Score: 0.37
DE  Interaction: B2RCM5; IntAct: EBI-2620189,EBI-2622428; Score: 0.37
DE  Interaction: Q9UEW3; IntAct: EBI-2620189,EBI-2622414; Score: 0.37
DE  Interaction: A1L0V1; IntAct: EBI-2620189,EBI-2622451; Score: 0.37
DE  Interaction: Q86V58; IntAct: EBI-2620189,EBI-2622462; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-2620189,EBI-748420; Score: 0.37
DE  Interaction: P63279; IntAct: EBI-80168,EBI-2620189; Score: 0.37
DE  Interaction: P55268; IntAct: EBI-2529769,EBI-2620189; Score: 0.37
DE  Interaction: Q9UHF1; IntAct: EBI-949532,EBI-2620189; Score: 0.37
DE  Interaction: Q6PKC3; IntAct: EBI-2620189,EBI-749812; Score: 0.37
DE  Interaction: Q9UBP4; IntAct: EBI-2620189,EBI-954409; Score: 0.37
DE  Interaction: Q93062; IntAct: EBI-2620189,EBI-740322; Score: 0.37
DE  Interaction: Q96NA8; IntAct: EBI-2620189,EBI-2622548; Score: 0.37
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRS
SQ  HFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEF
SQ  SSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHI
SQ  PETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ
//
ID  G0S4F3;
PN  Nucleoporin NUP82;
GN  NUP82;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P40368}. Nucleus membrane {ECO:0000250|UniProtKB:P40368}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40368}; Cytoplasmic side {ECO:0000250|UniProtKB:P40368}.
DR  UNIPROT: G0S4F3;
DR  UNIPROT: G0ZGT7;
DR  PDB: 5CWW;
DR  PROSITE: PS00678;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:P40368}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40368};
SQ  MPKIKSFAPAWLNEPAPGHKLFAPAADDGTATVPLAYGKKIKPGPRRTIARRGTEIFVACGKQIRWGDLAQLKESWESRP
SQ  SRSSVGPTSTKKDSSDFDDGAATAGYRIIKTPVADDIRQLVMSPNQDFLAVLTSHTVHICILPDSSHLHIQDTTPFKPKF
SQ  WTLGPTTHVTSRSAVVSAVWHPLGVNGHALVTVTEDAIVRVWELSTADRWTFDAPTLAIDLKKLADATYLDQDFGVSTSA
SQ  TNKGFSPDAFDMEVAAACFPTRDSGGWAPMTLWLAMTSGDVYALCPLLPQRWTPPPTLIPSLSASIVAKVAAAEDNPEST
SQ  PEERLVAQQQLEWMSEIDNQEPKLVEEATGEATIEVYTRPSRPGLVPKLQGPFDFDLNPEDEQDDEVELKDIYVIGEKPR
SQ  VADLMRGEEEELEMMKEDQHNGLSLNIICLLSTSGQVKICLDIDGVEAQWLPPRSKNKRLFAPPPEPPSLLTFQTFDTLK
SQ  PAEVTPDGWPMFSEDATSPYSFYVTHPAGITYISLTPWVFRLESELQSDSEAGTEFRIDLLAKGQGSERDRIFTQTRTQS
SQ  PLAAATSIDDPDLGYFILSATQTDPIALFFETPERPVVPKETSVVIPEHVEERPPSPYWEPRPLFHPAEALDKPSAVPAW
SQ  IDNLRTGRRRPLLTQELRLSMATLEVFHDGHKVVSTEVSDINDAVAELFRKCEALQGELRDQIKKVNEVKNRIHTITGDD
SQ  LSDDPPVSEDQLIKQRIRVARERQEELANRMERLRKKFGRTTTRELSDKEKAWIEEVQNMATSILGPEAGQGALATTPNL
SQ  AKQPWKRLEEIKTLRNALMAEAEQLQKVGDDTEESTPASQMPSLKIPSEIRKAKMAQVMSLLERESALVDAVKARIERLS
SQ  IG
//
ID  Q9W1C5;
PN  Integrator complex subunit 1;
GN  IntS1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:23288851}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9W1C5;
DR  UNIPROT: Q8IGA9;
DR  Pfam: PF12432;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872, PubMed:23097424, PubMed:23288851). Required for the normal expression of the Integrator complex component IntS12 (PubMed:23288851). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q8N201, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:23288851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-175291; Score: 0.35
DE  Interaction: Q9VPR7; IntAct: EBI-181242,EBI-175291; Score: 0.35
DE  Interaction: Q0E8S4; IntAct: EBI-9930148,EBI-175291; Score: 0.46
DE  Interaction: P18431-3; IntAct: EBI-242176,EBI-175291; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9933576,EBI-175291; Score: 0.35
DE  Interaction: O97159; IntAct: EBI-112333,EBI-175291; Score: 0.35
DE  Interaction: P34082; IntAct: EBI-868243,EBI-175291; Score: 0.35
DE  Interaction: Q9VJW9; IntAct: EBI-3410031,EBI-175291; Score: 0.35
DE  Interaction: Q24322; IntAct: EBI-497707,EBI-175291; Score: 0.35
DE  Interaction: Q01083; IntAct: EBI-175291,EBI-91342; Score: 0.37
DE  Interaction: Q9VP27; IntAct: EBI-175291,EBI-192457; Score: 0.37
DE  Interaction: Q7KMQ0; IntAct: EBI-175291,EBI-106192; Score: 0.37
DE  Interaction: Q9V4A1; IntAct: EBI-175291,EBI-137830; Score: 0.37
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0045666;
GO  GO:0034472;
GO  GO:0016180;
GO  GO:0034474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDRGKGSGSNRSQKKVPLGGELFALGKSVRDDSKSKILPIKGMSSSDRKREASTALASSSKRFRGNLKDAGAPDMSSGSS
SQ  QCETWEQFAVDCDLDTVVETIYAALEQNDSETVGRLVCGVIKQTTTSSSRSKVDNIALLALIYVAKVQPSIFCTDIVACA
SQ  LLSFLRREANVKMRYNTNLHILFANLLTRGFMEISQWPEVLLRIYIDDAVNERYWADNELCAPLVKNICAAFKTRTPHIS
SQ  LLRWDVSSSLPSGQAHRDSMTVDDDSGDNSTQSLDASPLNTESEPIPDAMCTTKSRFSDAVVQKHVSDAIRDQLNKRQQQ
SQ  DNYTRNFLKFLCTTSGIAEVRCLSISRLELWIHNGKLVKFAQQLLSYICFNIKGRNTQDNEVLLVLVKMRLKTKPLINHY
SQ  MSCLKEMIFLQPEILSTVMKLVVQNELSNTRNPNNMGMLATMFQTSADQSAATLAEIYQEFLLQRDDCLRTLRVFLRELV
SQ  RMLRFDVNLVKFCKTFLSEREDLTPQIEMFEFKERIFNSMVDIVCLCMFLSATPQAREASLSLKTNRDTKNNHALLKLYN
SQ  QMSQIQLDTVSWMYETVPTLFKIPAAEYHQALHKLLLLDSPEQYSRCDQWPSEPERGAILRIISETPIHEETLLRIILIG
SQ  ITKDIPFSIANTFDVLLLVIKRVSGMKATNIPAVQANKFDIIDFLFSMSEYHHPENIRLPAEYEPPKLAIIAFYWKAWLI
SQ  LLMISAHNPSSFGAFCWDHYPTMKMMMEICITNQFNNSSATKDELQIITMERDHILQFETYLAAQTSPHAVITEETAILI
SQ  TQLMLMDPMGTPRKVPSMVLDQLKFLNQTYKLGHLFCRCRKPDLLLDIIQRQGTTQSMPWLSDLVQNSEGDFSHLPVQCL
SQ  CEFLLFNAHIINEENSRDAELVNFLRNLIFDGNLSHQIVCELLDYIFRRLSSTVKQSRVAALSGLKIIFRHSGDFENEWL
SQ  LKSLQQIPHFYEVKPFIIPQLRAACQVENCPELIMAYIQFITAHTLNDPVNEMLDHVIDMAQLIVERSTMFQHIIISQED
SQ  YDYVPDENRIQTLKCLFVMFNNYIIKLREYHEPYEWTEYPDLLMVQFDDGVQLPLHINIIHAFIILLTYSNSNMPESIPI
SQ  LDYWFPPGRPAPVAFLPSMPQEQVQLLPDWLKLKMIRSSVDRLIEAALNDLTPDQIVLFVQNFGTPVNSMSKLLAMLDTA
SQ  VLEQFDLVKNAILNKAYLAQLIEIQQARGAKNGHYTVQALDLHSHSQTVPDLPKISVVIQEAVEIDDYDSSDSDDRPTNF
SQ  LATKEVAQTILTQPDQLTESRSDCRSLIQKLLDMLASPNSNRADVVNAITEVLAVGCSVTMSRHACTFLRTFFSCMLHSD
SQ  KYHILENALQKNLSMFKHTFADSSLLQKSELYHESLVFMLRNSREIYAQQFKANTALVARKRIVRAIVQSFDQTKDSKTV
SQ  AKSKSDQLFHNGLFIDWLSEMDPEIVSTQLMKERFLFSKSCSEFRFYLLSLINHQTNWDTIERIAEYLFKNFHEDYDYAT
SQ  VLNYFEALTTNPKLWKGRDKYMSKNVRPDAFFMLRTSELEPFSHFILHEGLSEVKLDSKNYDFKLCSRMNLLFKLTEKRR
SQ  DLMVKVMEHVEKSSVSDYLKLQVLQQMYIMYPRIKFLKPGKTGEQAYKLQNLKGCQADKVSNNLITCLGSLVGKKDFETL
SQ  STDTELLLRKLAASHPLLFLRQLGVLSSIMQGRAQLSMKALREEHHFHRFVQILRTLELLQPTIFEEAYKNEIQNTLSCY
SQ  FNFFKHHSNVKEACQMLNKFVQMLQAYINYNPSSALLFIEQYVGILKELAAKYTSLGKLQVLVQAVALLQHKSHSATELD
SQ  DEEVKYEYDLDEHFDVKPSASKPVVTEDPIEVNPQTPIDPSSSRGPLSVLTLGSYSRSNYTDISPHFLDLVKIIKQSNTE
SQ  DVVLGPMQELECLTSKRFVFINELFERLLNLIFSPSAQIRSIAFIILIRHLKHNPGNSDINLCTLNAYIQCLRDENSSVA
SQ  ATAIDNLPEMSVLLQEHAIDILTVAFSLGLKSCLNTGHQIRKVLQTLVIQHGY
//
ID  Q5N941;
PN  Probable ion channel POLLUX;
GN  P0039A07;
OS  39947;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5N941;
DR  UNIPROT: Q0JHD3;
DR  UNIPROT: Q5N940;
DR  Pfam: PF06241;
DE  Function: Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAESDGGEASPSGGGGGEGSPDPRRPPARPQLTKSRTISGSAASAFDRWGTSNSSSSILVRRSSTAPLPPGAAPRGLLTV
SQ  AVDEPSYAAPNGGAAMLDRDWCYPSFLGPHASRPRPPRSQQQTPTTTAAAAADSRSPTPAAPPQTASVSQREEEKSLASV
SQ  VKRPMLLDERRSLSPPPPQQRAPRFDLSPYLVLMLVVTVISFSLAIWQWMKATVLQEKIRSCCSVSTVDCKTTTEAFKIN
SQ  GQHGSDFINSADWNLASCSRMLVFAIPVFLVKYIDQLRRRNTDSIRLRSTEEEVPLKKRIAYKVDVFFSGHPYAKLLALL
SQ  LATIILIASGGIALYVVSGSGFLEALWLSWTFVADSGNHADQVGLGPRIVSVSISSGGMLVFATMLGLVSDAISEKVDSW
SQ  RKGKSEVIEVNHILILGWSDKLGSLLKQLAIANKSIGGGVVVVLAERDKEEMEMDIGKLEFDFMGTSVICRSGSPLILAD
SQ  LKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLM
SQ  IQCALQPGLAQIWEDILGFENAEFYIKRWPELDGMRFGDVLISFPDAVPCGVKIASKAGKILMNPDNDYVLQEGDEVLVI
SQ  AEDDDTYVPASLPQVRKGFLPNIPTPPKYPEKILFCGWRRDIHDMIMVLEAFLAPGSELWMFNEVPEKERERKLTDGGMD
SQ  IYGLTNIKLVHKEGNAVIRRHLESLPLETFDSILILADESVEDSIVHSDSRSLATLLLIRDIQSKRLPSKELKSPLRYNG
SQ  FCHSSWIREMQHASDKSIIISEILDSRTRNLVSVSKISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIRSA
SQ  EFYLYEQEELSFFDIMVRARERDEVVIGYRLANDDQAIINPEQKSEIRKWSLDDVFVVISKAGNATYFVKTTVMRSNPVV
SQ  YSSTF
//
ID  Q8RXH2;
PN  Nuclear pore complex protein NUP85;
GN  NUP85;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RXH2;
DR  UNIPROT: O82634;
DR  UNIPROT: Q9ASW9;
DR  Pfam: PF07575;
DE  Function: Functions as component of the nuclear pore complex (NPC). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0009737;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGMSSESGGGELVLFSTKEKTPVLYPLSYGLKSPVHRLSISWGCGNNLRVTVLRNPELRDDDDGEVGGKVVNVRLSGED
SQ  GEISDPQWRRIAYGSVSPFALLQSRRNSISSLSKMDMSSSLYQTAWWEYVMEYSRDIKSLLSNTISLPAPLIEDPRSVIK
SQ  NAEEPTSLKAAWELMELFYADKTCLSWLPERLVDWLSEYDILLSSSHPTIYSKLQDFQKELVGLQAIEDDPRYWEVMASA
SQ  LSVGWLEIVVKLLHLHGSYQLDQLGHRETENGLVEAVAVLISKMPRMRPQLEDGKFGECSAAKPDFMKTRERWQSQITKL
SQ  ECSAFWVQCAHHQTREGLRNMLKIMIGNADCLRAATCNWMELFVSHLLYLRPFTKGLDGMHSLAQKCVQSKPVNTSHKLL
SQ  RLLIGILGENTEVVLAECSKEFGSWMVAHAMELLTAGSEEGEVLVHEEQRKLGGINMEELHRLVYAQVLSSHALTWQIAP
SQ  IYLASCEKQGLGLLELLFYRQPVQENQMLIKSLEICRLYELSNVSAKLMKISGVHHWKHGRKGSGIFWLQQARDENCLSV
SQ  IAQQLFDSVGKSLSDESLKQWEGLVELLGSESQISGGLDFLHKYRDFKRSLKVVHDGKTIDAAHEAVERLVSLMKSPSTP
SQ  QRFWLPLLHDSLKLLNWPERSLLNVTQTNLMLNKLQELSIARLRPGFIESELSAQAVGSVRLALATNLGRAFLEEC
//
ID  Q8IQV9;
PN  Nuclear pore complex protein Nup205;
GN  Nup205;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q92621}.
DR  UNIPROT: Q8IQV9;
DR  UNIPROT: B6IDH1;
DR  UNIPROT: Q3YMV0;
DR  UNIPROT: Q8MSV6;
DR  UNIPROT: Q9VWB8;
DR  Pfam: PF11894;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and maintenance, but with limited role in NPC permeability. Required for specific nuclear import pathways such as Mad import. {ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: O97159; IntAct: EBI-112333,EBI-499630; Score: 0.35
DE  Interaction: Q960X8; IntAct: EBI-499630,EBI-90175; Score: 0.37
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0042332;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGECLANEQMCVGRQITNATHASTAVIEDMWTPYKHLYNTFQTAVSNRSGFTSDLEQCLKKYKHNFSNLLRNPPRSEKS
SQ  RNLLRNALNEGVPMQGHSRKTKMSQDLADEAVILSDMFDLDEGFAVELLCTAQRQQKHHPGLSRGLVAVLLYYDGRKAIS
SQ  CTLRDMFQVVSGVSWNTELPKEITGLVTNYAESLVDGSGILGRLLQLLEEMDVDKECAMLTTNRAFGSKKHQNQVLGLYE
SQ  DIQQALAMALFNWSAQRGLPRHIAIRLMHQLANRKNHDAGGNMDDVTLIMLMALLYAYDTSMLLVTEEPNEHTTRLPIFS
SQ  DREFAECFLEELYAQSSWQAPRLNAIIAYSFGLTLASLRHAPLQLQATAISIINRDEMLIDEALGAQVFVFFHSLLLEKD
SQ  LVYSTQFFYRRVHLLITDFIDFMNSKVSELRGRADESSHTIISFLNEGLEPPPNLDSNFELLMLCVAKMHGDPRVTIRLC
SQ  NEYWGPGDPNGSTAFKNTSRSVSLFKFISLASDLLPQTLFKAYLKMISGLTRTDFSARCAFNMLRVPQMATGGKYAVSWD
SQ  HFFTTLGNYYTSMRNDFNTNIGMSGETIYRTRSTPKAITQREAEHLVAVMGIIQAVAEHDEVSRIMICDHPNWQTPQVLL
SQ  GLVACATPLFLKAEILHTLAALAKSKETARVIWFHLEASQIIPTVPVSRSYAQCSLLEEMEQIESRSEQYNLTRGILQLL
SQ  YTLMTTNLPKSLGAGQRTPAYEGYLKSMINSVLLKFYNRAYKVPSEKWQVGAQCLKLLYYLLATYRPSAMDFLETVDEPP
SQ  YPGFHVMMQLQLKSEMLQLLLCIVEEVRERLDNYNRFQGKKLLEECSLYALLILEAALAKQNAFFEAHSAANCPILLSGL
SQ  NRMLLDLNPRSRKPDHVLNIIKYVTYNSWLPRHALAAIKILASVTQLPNVSTQILSMYGQGSNEKLEIRQGFVECLEMEV
SQ  CVGKHDDDLLDQLALNNHVPYLGFGDDLDNEREMSGEREYSTIESQLELQAGDGALESKPASIELQLKEAIIKLFEMNLS
SQ  QQLPNFVYFLLGVDVLREFMANGRQHLAIEMQSSCVNSVVLLLEKYMDKQRHSDKYCEHTARIVERIYHLFHGLCANRRT
SQ  AETILRYFRLTCSDFLLRHLRSLPFRQHREDHVLHAMGHLLNCVSIDVKLAAKHGQMTRFNQMCDILLIGNGMERSSHGL
SQ  SMELGHSLISQPSSSFLAMDVLPAGGSISAVAHGAGSASLGAPNTGVKSLKPSLLQETSQGLHVTRLLDILVLEAGTLSQ
SQ  PQLEFFDGHLITQLLRDCEASAEAGANSRANLINVRKLYYILTDELYMVQSIIASGQRKAISTEIMLLLNHAVNINRVRT
SQ  QRCATLAFMAAWGQLVQVLFSNMPDAVLPATQRRQHIIDIVEKVLIKVQPIQPIIEISVQVSETVLLLLANLRYCCYQAE
SQ  DQSPEDLAAEDSLSNGNGNAIGNDSQVNALCLGQRAIGTGSDGGSGGGRDIGSGGNSSNLRFILKNLVQWIMISEVKSQK
SQ  LRINLYSSLLNCLRIAKRLRTDEHLEYQETLISRQESARTYNKEQRRDDRLRLKAMAAEVIGTFGEKLIDTICHDAVTGH
SQ  DVCRMLALACLDMISELQAVSTLCDFVASRGYLKHILESLDQSSTALCGILQPVPDHLRPLYVYESRMAFLTRMANSNVG
SQ  ARLLLTEQALGVLSNMKVYDQQPDLKSSELNRNEPQTFLPSIDDRFRSILLPALSLCDAIVNSLGPRNNSAAVQVLNFLF
SQ  AHIDMVEAMLRSATPYMDLGHLQQVAVISNLFARASTHELTALEDSVQLDLRNRLGRVQQLMIVVFGRFCVSEPTIRRML
SQ  QQDEEQQTNPTDDSKRLRVKYFLDIAANVSLYCRNVVTSHSKDSMTSKYLLTTVINDVTLLTGKMSSKKLTTIMHTILNQ
SQ  LKGSIGYYLSQKSIADNLLQQRASLPNISFGPNGKQSYIELSQRYNEKRSELRQAVFIAEQNLYLLWIHLDFYLRNTIDY
SQ  ANENRNAINESNMDDDNDMSVLNASQEEIVQLKQLLISTFNETFCTQLINASEDYSIKCKGFNGSLLRRIKALVQFAPIT
SQ  ANDVNSSFDS
//
ID  Q9XXN3;
PN  Nuclear envelope phosphatase-regulatory subunit 1 homolog;
GN  nepr;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q8N9A8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N9A8}. Cytoplasm {ECO:0000250|UniProtKB:Q8N9A8}.
DR  UNIPROT: Q9XXN3;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase scpl-2 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May play a role in nuclear membrane dynamics being crucial for early development of the embryo. {ECO:0000269|PubMed:22134922}.
DE  Reference Proteome: Yes;
DE  Interaction: O45734; IntAct: EBI-315958,EBI-328026; Score: 0.37
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0051783;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAIQARRMPEDPSTACEDLKFFEKRLTEVITYMGPTCTRWRIAIVIFAVLVGVIGSKYFANEKIEIFQIPMIDMFLTTHL
SQ  DFTLCFFVGLLLFAVFGVHRRIVAPTIVARRCRDALSPFSLSCDHNGKLIVKPAVRNSAP
//
ID  Q9Y7X6;
PN  Stress response protein ish1;
GN  ish1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11751918}.
DR  UNIPROT: Q9Y7X6;
DR  UNIPROT: Q09149;
DR  Pfam: PF10281;
DE  Function: Has a role in maintaining cell viability during stationary phase induced by stress response. Activated by the spc1 MAPK pathway. {ECO:0000269|PubMed:11751918}.
DE  Reference Proteome: Yes;
DE  Interaction: O13712; IntAct: EBI-1542405,EBI-1559673; Score: 0.37
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRSRSVASLGVLLAIVFYIFTYGFSTYRKNDTSAVKTWLEEHSIPYGSRSSPSDFQQFISESYDSLVPNLDKWSGHNLNS
SQ  WLGKKTESSYLDAISNKIRKTGRKLSGSVEDARDATQEAWESQKASLFESWSDSQLRAFLARHSPQFAAKEKKGILEKLS
SQ  PASLRETAAKEYDALTSKLGNTGDWIYDTWSDNELRTWLHDVGVPISSHESTRSHLLRKLKNYISTKADEAQPSVEAVKG
SQ  KASEKAKQAGEFVSDKAGDAKELVNEKSSEAGQYAGQKMEEGGELLQEISKRRGRFGNWWANSGLKAYFDAHGIPAYQPS
SQ  PIDQFYAHLRRQYYLKTNGYQALKSKAYEEASNVADSASSIASNVASGATEAYQGAASGASRFTEGAKTAAESVTSAFEH
SQ  NKDTATSKAKQMKGKAASLGSTASEKVGEAADYAAETASKVASKAASKVRETIDETIIERWQDSKLKEFLFLRGVPVPQR
SQ  STKDQLLDLVRKHFNKGAVPNWAAYFDTLSSKELSAWIKEYKKHYHGKLHPSKDREHLFQNACNIYRAIAEKADKSVLQS
SQ  IQSKFPKATVPGYDSWSNEDLKSALKEYGDSIGKVFNRKDAIERLKRHDILFYGPVVADKAKSGVSGFLRRVASFMGFGT
SQ  RDVAEIKLGENIQKVKDTASKASSAVSSAGDYVETNVKKAQRVL
//
ID  Q9VX31;
PN  Integrator complex subunit 2;
GN  IntS2;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9H0H0}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9VX31;
DR  Pfam: PF14750;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872, PubMed:23097424). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q9H0H0, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0010628;
GO  GO:0045666;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPVRMYDVSPRVFCAMQNLDITLLASYPEAEIRPVLPSLVRMSLLSPLDNTESSMESRKEILAVLIGIEVVNSIVSYLQV
SQ  NYHELENELKKELQARQKSAFFEGQQHEYGLQSGIALGFERADVARKVRVVLSEIFNLQQQVSEQKPAAHSEMLDDGIYL
SQ  EEVVDILCIALAELPSLLNILELTDALVHVPNGHRIICALVANFPDCYRDVVSHVIANCDEDGSDGKHRLMLLMGLSEMN
SQ  PSQALANRSMCVDMLKVPSFMLKLTLKHPEDLIAFLTGLLLGNDQNLRSWFAAYIRSSQKRKGDALNLVRVELLQKVIQT
SQ  TTNAAELRDFNLQGAVLLRLYCALRGIGGLKFNDDEINALSQLVTSCPQATPSGVRFVTLALCMLIACPSLVSTIPLENK
SQ  AVEWLQWLIREDAFFCKRPGTSTSLGEMLLLLAIHFHSNQISAISEMVCSTLAMKIPIRPNSTNRIKQLFTQDLFTEQVV
SQ  ALHAVRVPVTPNLNGTILCYLPVHCIQQLLKSRTFLKHKVPIKSWIFKQICSSVRPVHPVMPALVEVFVNTLIIPNPTGK
SQ  VNIDHMHRPFTEAEILHVFRTSKLTFFAEELPPMAESQELNQIEVTCPLTAQLLMIYYLMLYEDTRLMNLSALGGRKQKE
SQ  YSNNFLGGLPLKYLLQKAHHYHNDYLSLFHPLLRLIISNYPHLSMVDDWLEEHNLAQGNSTVVVSKHELKPETLDRALAA
SQ  IQTKPHLAIRVFKQLLQMPPETQAQYGQQLVKHLPMVFAKSVPRYVKDLYNDIWLRLNAVLPTTLWIMSLRAITNGSDTM
SQ  DRRTFANESLLEPMEVLSCPRFVFCSPYLLMILLRILKGSLAASKTYLNVHMQMQQKQVLDKNGMMQTDAIWEDLRTTLI
SQ  ASQESAAVHILLEVLDYIASKATDRVSHLELREIQGIIGTYVHQAFISEPSLAKLVHFQTYPKSVIPMMVASVPSMHICI
SQ  DFVHEFLNVTEMEKQIFTIDLTSHLVLNYSIPKSLGVSKFCLNVIQTTLSMLTASTKCRFLRNVMPAMVRFVETFPILAD
SQ  DCVNILMTTGRILHSQSSLGMTTMEMPLTDSDKLCTYRDAQLHIIMIEDAFKALVTAVMKKSDLY
//
ID  Q03760;
PN  Pre-mRNA leakage protein 39;
GN  PML39;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Lumenal side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}. Note=Associated with a subset of nuclear pores opposite to the nucleolus.
DR  UNIPROT: Q03760;
DR  UNIPROT: D6W0H7;
DR  Pfam: PF07967;
DE  Function: Involved in the nuclear retention of improperly spliced pre- mRNAs. {ECO:0000269|PubMed:16162818}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-20589,EBI-27933; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-27933; Score: 0.35
GO  GO:0031965;
GO  GO:0008270;
GO  GO:0051237;
GO  GO:0051028;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MEKDALEVRLKSIRHSLDKNTKLLPGKYRNTLGERLITKWRYKKKSHNGSSMLPEKCKSHVQLYDDLVQESSKHFVGFRL
SQ  HDLRALLKRICSIQNYTRHVLIEWDVRWVNPLTLASKGWEPYQSASQSQVPFKCCCCHAIMTIPLLKNGDDVADYTMKLN
SQ  EKIWNSNIIGNHLQKCPWRENQVDLNKEYYLSSQNLIREIERIHTEIDRIVSGSNEFSLKRNSSRIFHYLSEKEIQKLAF
SQ  FFDCKDYSLVGLLLLGYTKFQKDDLVQCTACFHRASLKKLEYTEFNGHALWCRYYNKELLPTMLLELIGKEDKLITKLGV
SQ  GERLNKLEAVLQTL
//
ID  A6ZTA1;
PN  Nucleus-vacuole junction protein 1;
GN  NVJ1;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A6ZTA1;
DE  Function: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13 (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0006914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVF
SQ  NFISRQSSELDARIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPII
SQ  LSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALSQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEV
SQ  ESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFR
SQ  Y
//
ID  Q9LMK7;
PN  Ran-binding protein 1 homolog a;
GN  RANBP1A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9LMK7;
DR  UNIPROT: O04149;
DR  UNIPROT: Q9XHS1;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P41917; IntAct: EBI-2325844,EBI-2325919; Score: 0.37
DE  Interaction: P41916; IntAct: EBI-2325815,EBI-2325844; Score: 0.37
DE  Interaction: Q8H156; IntAct: EBI-2325844,EBI-2325977; Score: 0.55
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0008536;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0043547;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATNEPEHEHRDEEEAGANEDEDTGAQVAPIVRLEEVAVTTGEEDEDAVLDLKSKLYRFDKDANQWKERGAGTVKFLKHK
SQ  NTGKIRLVMRQSKTLKICANHFVKSGMSVQEHVGNEKSCVWHARDFADGELKDELFCIRFASIENCKTFMQKFKEVAESE
SQ  EEKEESKDAADTAGLLEKLTVEETKTEEKTEAKAVETAKTEVKAEEKKESEAEKSGEAKKTEESGPST
//
ID  P04876;
PN  Matrix protein;
GN  M;
OS  11278;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: P04876;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shut off presumably inhibit interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039657;
GO  GO:0039522;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKSFFTVKMTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEEEASGAWVLDSVRHSKWASLASSF
//
ID  P36137;
PN  Protein UIP5;
GN  UIP5;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass type I membrane protein.
DR  UNIPROT: P36137;
DR  UNIPROT: D6VXA6;
DR  Pfam: PF03388;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P02829; IntAct: EBI-26427,EBI-8659; Score: 0.37
GO  GO:0030134;
GO  GO:0005789;
GO  GO:0005793;
GO  GO:0000324;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005537;
GO  GO:0007029;
GO  GO:0006888;
GO  GO:0007030;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSRDVRAEKLAISLLILSLFLIFQLVAEIYLNNGDQYHTETSPFTRGRSHVTRVPNHDASLSIPFLDKINQFWHVGGATQ
SQ  IRNIQSIKLTQDRDQDKHGLVLSNGIGDNTINDFEIVFTFRISHDPTTQLTGDGMCFAITPENGFLTQNLQSSYAKKQYM
SQ  MNSQGVIADNTDLMGFPKNLPGLFIVLDTYRNQGHDHKEVPFMDVFINVAPESDWYDINSDGELSTSLRLNSRGHIKLKK
SQ  NALWNRVTKLRIIYLESISFLKIDVQYAKEGNYWIELFQTTENLYLPKNMHTGQRYIGCSALNGQLTETVELLDVSTSEF
SQ  HWNDMDASIEDTYDYAKEAELFLEQEFGEVLDREPDEFTKWKMIKAQPNIKTGSQSAEQKTSNNPHSRLFKVVLTIWHYS
SQ  EILLLIMGIYLFSACIRVFQRRFKKIRSRRKRAGSHSVGLLPM
//
ID  Q8R411;
PN  Myc target protein 1;
GN  Myct1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q8R411;
DR  UNIPROT: Q3UQ11;
DR  UNIPROT: Q8C6M8;
DR  UNIPROT: Q9D182;
DR  Pfam: PF15179;
DE  Function: May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability and inhibition of hematopoietic differentiation. {ECO:0000269|PubMed:11909865}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANNTTSLGSPWPENFWEDLIMSFTVSVAIGLAIGGFLWALFVFLSRRRRASAPISQWSPTRRPRSSYNHGLNRTGFYRH
SQ  SGYERRSNLSLASLTFQRQASMELVNSFPRKSSFRASTFHPFLQCPPLPVETESQLMTLSASTTPSTLSTAHSPSRPDFR
SQ  WSSNSLRMGLSTPPPPAYESIIKAFPDS
//
ID  A4FV75;
PN  Trimeric intracellular cation channel type A;
GN  TMEM38A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: A4FV75;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
GO  GO:0071313;
GO  GO:0007029;
GO  GO:0010881;
GO  GO:0014808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRHHPMASWLCAMLHCFGSYILADLLLGEPVIDY
SQ  FSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVT
SQ  LMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVL
SQ  EAYICPVLFGSASGGDHHHNNHGGSQGGSGPGSPHSPLPSKSKEELSEGSRKKKTKKAD
//
ID  P10204;
PN  Protein UL20;
GN  UL20;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000269|PubMed:18596102, ECO:0000269|PubMed:7933124}. Host Golgi apparatus membrane {ECO:0000269|PubMed:15254173}; Multi-pass membrane protein {ECO:0000255}. Host nucleus membrane {ECO:0000269|PubMed:15254173}; Multi-pass membrane protein {ECO:0000255}. Note=During virion morphogenesis, this protein probably accumulates in the trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000269|PubMed:15254173}.
DR  UNIPROT: P10204;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes. {ECO:0000269|PubMed:1719228, ECO:0000269|PubMed:17996071}.
DE  Reference Proteome: Yes;
DE  Interaction: P10221; IntAct: EBI-7906325,EBI-6880600; Score: 0.40
DE  Interaction: P68331; IntAct: EBI-7906325,EBI-7906305; Score: 0.69
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTMRDDLPLVDRDLVDEAAFGGEEGELPLEEQFSLSSYGTSDFFVSSAYSRLPPHTQPVFSKRVILFLWSFLVLKPLEMV
SQ  AAGMYYGLTGRVVAPACILAAIVGYYVTWAVRALLLYVNIKRDRLPLSAPVFWGMSVFLGGTALCALFAAAHETFSPDGL
SQ  FHFIATNQMLPPTDPLRTRALGIACAAGASMWVAAADSFAASANFFLARFWTRAILNAPVAF
//
ID  G0SBS8;
PN  Nucleoporin NUP159;
GN  NUP159;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P40477}. Nucleus membrane {ECO:0000250|UniProtKB:P40477}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40477}; Cytoplasmic side {ECO:0000250|UniProtKB:P40477}.
DR  UNIPROT: G0SBS8;
DR  UNIPROT: G0ZGT8;
DR  PDB: 5CWW;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre- ribosome, and protein export. {ECO:0000250|UniProtKB:P40477}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40477};
SQ  MAFSFGNAGGGGGGVTQGKDLEVIQTEGLGFLALAGDAKVQLTSKWSPPPAPTASLLSIASRKGLVAAAGPDAVHVATTE
SQ  SVRKAFLAEKNGDSEVRPFNPEAKLPLPLRISQLAFTADEQYLVLSAETGGGLRAYDVNSLTQGNTQSAFELATNGETLR
SQ  QLAPNPMPESAAFCAIVTTNGNLYMANLAERTLVSGPNGPTLRSQVSCAAWSTKGKQLVAGMADGSIYQMTPDGTEKAHI
SQ  PKPPNLGDYHVSSVVWLENNVFLTIHNPTNSTNPDDKTVYHVITRQQSSGSPPNFTFQKLNDPVEPFVADKTPHHTVLRL
SQ  KDFPPNLQDLLLVSSTAVETIGLLTRSKTPLATDKPADAITNVFTTTELADDSRRAQLPMSEDMMETYPIGVALDLSSKE
SQ  KVYKPIPTDEEIEYSPGPLPGLWVLNNEGVLASWWVVYNESIRAGTTYSGIGGSSEVIPASPAPALASSTAPVPAFASPV
SQ  SKPTFGSPSPATPAFGGPSALGTKASPWATAGGAASSTPTFGQPSFGKPAAPAFGQASFPGLGQKVSPWATGSTTSAAPA
SQ  FGQSGFASAGTAPGKVFGSSFTAPSSGGFASFATKSGFASLSAPSGGSSIFSSKPGAPLTSAAPEVSMDTDTAFPPPSTK
SQ  TDKPAFGSSPFVLGSTFKADPTAAHDIEKPKEGESKSLFDTGFGLSLEDAAKQPASAAESKDEEMRSTTPPLPPPTETKP
SQ  KSIFESTTPTTTPAPQKFEFKTTTPSGFSTLLGSTKPVASSMPNIFATPKPTSAEKPKSIFDTLKPKEESKENLLKASEP
SQ  PLPPDTTSKAVFQPGSSSSESAESSPGAAAKAAFKVGNDETPKPQKELAPKPEAVPLPPDFVKAKPKTEAKETKAEEPAV
SQ  SPNLPVKPLAKKAEPIPAVPESASEEEQGQAEEEEAESGEEEEEEEEEGEGEEEEEEEEEEEEEEEEGEEGEEQSEAGSE
SQ  GSGVDVAKDLSPTAKFGSMTPGYTPHTSLGGMAESTFSTISRSEVAEQSRPLFGEITKNAPPLFPAAGPLPVSPRSPSPV
SQ  RGVVRSSILRPTETPRPVDTTPVPSRKGLLQKTASFGMSTGQKPAVDPNVKAQRKLAEKLKAEEQVLVDPEDEGIQQILQ
SQ  SKVEPTLRMNEFLAVDTKLAPMKPGRDDVPNACETLWRDINRMIDRLGLNSRSLQSFILGHTSHGKPGGRQKDDLEKPDD
SQ  WVLIEAYDLGDMIDNKLARELEAGRIKDVEGTMAAIHNLGRDLAKLRAKEEDLRKLFNAQVDPDQIALTKALPLSAEQLA
SQ  QQNELRRSYASFSKLLTEAEEALTVLKAKLASANAARGRRGAGAAQVPTVDAIIRTINKMTSMAEKRSGDIDVLESQMRK
SQ  LRIGSLGPAGTPNGNGVGAGTVVPATPGGGGRSRESSPFVTPQSSRRAMFMSPGSVGTATPRGLLAATGTPSPTKKKLSM
SQ  YTAEEKRELRAREAKRKATLRMLRESLARVGPNVVRLRDDD
//
ID  C1BK83;
PN  Nucleoporin SEH1;
GN  seh1l;
OS  8014;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: C1BK83;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: No;
GO  GO:0005623;
GO  GO:0000777;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKSDNGEWNCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKQRGLSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSNTAYSGKVQIYEYVENTRKYAKVETLMTVTDPVHDIAFAPNLGRSFHVLAI
SQ  ATKDVRIFKLIPMRKESSSSGPTKLEVQLQAQFDGHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILRG
SQ  DGSPVNGAAGQAGTPGAAGTPGGPASQNALQAVAGRKKAQLMPG
//
ID  G0SER9;
PN  Nucleoporin NUP84;
GN  NUP84;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52891}. Nucleus membrane {ECO:0000250|UniProtKB:P52891}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52891}; Cytoplasmic side {ECO:0000250|UniProtKB:P52891}. Nucleus membrane {ECO:0000250|UniProtKB:P52891}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52891}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52891}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P52891}.
DR  UNIPROT: G0SER9;
DR  UNIPROT: G0ZGU7;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P52891}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52891};
SQ  MSPAFNIPDSIESSRGSSQSPHHGLNPEEMADIEATSQDNAVRVGEEIDYFAAQLDRYDADQTGSPPERRSRAFQLVDSY
SQ  YTFTRKRLDRLRERQARQRSAQRGSWQRAGSIEMDLDDADEENDDILDEELQQLEDEVQIWDLLRRILPLRYHDATQNQK
SQ  KEHDGSTKSRRQWWNEFMVSDSVARERKVVLEWLQNSASYGPPIDEVVSDLQHNAERGDILAHGWLHTRHKIKLQKSVNA
SQ  YQGVLDPRDAAAAQSHLSSNSLITQLDPDAVTRQARKLEPQDESFERAIWLGCFEMLRRGCSMSEIREWLAVRTELWRAF
SQ  SIAPLPLSNPDDEEQPDFDPVSLILWRRMCYAIATDGGTSDYDRAVYGLLAGDIPSVEKVCKTWDDVLFAHYNALLRTQF
SQ  DLFLIKHGGDAAAKAAQQFPSFNAVAYHGDPATATKRLIDSLETGMKTSAEAFRPAKALQAAIVADDLDKFLFHQGLLLS
SQ  IRANKKEKSKLIPEYPFPHESFSDKKYYDLGDHQGLRILAHVLIIILTLDRLSGVAKDKGPLQARHQAAENSIAAYISYL
SQ  RLVRLEEMIPLYCSKLHGPRVYSTLSRNLIHIVDIDARLHQLTIMRNLGIDVSEFVKSQPLIYLDDVQDELVSCDAKDQF
SQ  KILEDGPATLKYGRLVKPDFFGDDADYVDPEDDALIRSMEWLLLVPGLFVETCAYAVRIYKYFLKRTRLRAARAFSRRVR
SQ  GHEIIRTKFPNLLKDVDENDPAAWFEEFAAAQLPSDLLESCPASQEKLITITRHLWELESLVRALDSIETLTSLAALTRE
SQ  ESVPMTREMWQEVSQTVRIAKACMRPVLKEWLLTTYDGRSVEQDFLDIRQAYIPETILAYISCLHFAGTSLSRDNLLECM
SQ  DLAAIIAEKDSDVAKEFMRCGRMKELVEAFASASKALAIWSGEKKGSQTNSKKLRELGWSRELWSIKS
//
ID  G0S7F3;
PN  Nucleoporin GLE1;
GN  GLE1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12315}; Cytoplasmic side {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12315}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q12315}. Note=Biased towards cytoplasmic side. {ECO:0000250|UniProtKB:Q12315}.
DR  UNIPROT: G0S7F3;
DR  UNIPROT: G0ZGT9;
DR  PDB: 6B4G;
DR  PDB: 6B4H;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:Q12315}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016973;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q12315};
SQ  MAGSSPLNHHLWSSPSRTVEEILAEDRNSEARHRYLLELARKEHERVREEAARIYREQLAREERERLLAERRKEEERIRL
SQ  EQQIAAENARLNALKATRIEIPPLLPDPVPAPSTVNGKPTLPAAVATEAKRCPSEPSLVNGIASNGVVEAPAAASIKTLE
SQ  PAKPAASAFKAAGSATTAAPVAPIASVQPSTNGVVSAVASTPKTAPPAPTETPPDRYVEIHRNLKGLRKYMAEQAKTNLK
SQ  LKQRMGDMRREIRKSVGQLTTGGMAANKDKQQKIKSILTEALSNQVESALVDPNNFVVEPRKPVEGATNNDPLLPSIFVY
SQ  LINIFAKAAISQFINEAGARPETADPVGICVAAILSEPDFLWRGASLIDILIAKFRIVCPVLFGYRGSEKTEQGRQRLGW
SQ  WKESGQWISEQQHMDRMTGLGAGFAAISLRKFALSKKQNPYPPRFYWMAMAKIVNTPPAEISNTQCVVLKAMVQNYEAKF
SQ  IEFYGSAAIAALRTALIDFPARAPHKSAAVNSLEVLAQMLKRDTGLDLG
//
ID  Q5NE24;
PN  Protein NODULATION SIGNALING PATHWAY 2;
GN  NSP2;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane. Endoplasmic reticulum. Note=Mainly localized to the nuclear envelope. Also found in the endoplasmic reticulum. Upon Nod-factor application, the nuclear envelope localization disappears and the protein accumulates in the nucleus.
DR  UNIPROT: Q5NE24;
DR  UNIPROT: G7J334;
DR  Pfam: PF03514;
DR  PROSITE: PS50985;
DE  Function: Transcriptional regulator essential for Nod-factor-induced gene expression (PubMed:15961668). Acts downstream of calcium spiking and DMI3, a calcium/calmodulin-dependent protein kinase (CCaMK) (PubMed:15961668). Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta- carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones (PubMed:22039214, PubMed:26503135). {ECO:0000269|PubMed:15961668, ECO:0000269|PubMed:22039214, ECO:0000269|PubMed:26503135}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0009877;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLMDMDAINDLHFSGHSSLTNTPTSDEDYGCTWNHWSPIVNWDTFTGAPDDFHHLMDTIIEDRTTVLEQLSPSITTTTT
SQ  TTTTTDEEEEEMETTTTTTTTAIKTHEVGDDSKGLKLVHLLMAGAEALTGSTKNRDLARVILIRLKELVSQHANGSNMER
SQ  LAAHFTEALHGLLEGAGGAHNNHHHHNNNKHYLTTNGPHDNQNDTLAAFQLLQDMSPYVKFGHFTANQAIIEAVAHERRV
SQ  HVIDYDIMEGVQWASLIQSLASNNNGPHLRITALSRTGTGRRSIATVQETGRRLTSFAASLGQPFSFHHCRLDSDETFRP
SQ  SALKLVRGEALVFNCMLNLPHLSYRAPESVASFLNGAKTLNPKLVTLVEEEVGSVIGGFVERFMDSLHHYSAVFDSLEAG
SQ  FPMQNRARTLVERVFFGPRIAGSLGRIYRTGGEEERRSWGEWLGEVGFRGVPVSFANHCQAKLLLGLFNDGYRVEEVGVG
SQ  SNKLVLDWKSRRLLSASLWTCSSSDSDL
//
ID  O74446;
PN  Sad1-interacting factor 2;
GN  sif2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localized primarily along the nuclear envelope in a punctate pattern. {ECO:0000269|PubMed:14655046}.
DR  UNIPROT: O74446;
DR  UNIPROT: Q1MTQ4;
DR  Pfam: PF02582;
DE  Function: Required for sporulation where it is believed to have a role in meiotic nuclear division. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0051321;
GO  GO:0140053;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNRIGPQRSTKTAAKLRLLPSTEEFDDFRRQDTGREVYSQIPQIEGSTAKRDAEHLGKRHREFLPRVTAYCTCDTFRVD
SQ  LLFKFFQSRRSSHKTRPKQFDECIYSPYSYNNEETTDLLPDTLESSRGTLNRESSQESLQSIFEESGLDRNQPLFREVFC
SQ  FTYGVVVLWGYTIDEEHRFLRELGRFEIEKLKIEDMEVEEFNYYITTLYQPRIFNDFIALRDASNYMIRLSISHAIAQSV
SQ  KISLFEELVNETIDATKDTPQMIAETGRVNLKREEIMMAVGQLFILRININLQGSVLDSPELMWTEPQLEPIYTAARSYL
SQ  EINQRVALLNQRVEVIGDLLSMLKEQITHTHDESLEWIVVILMGLLVLIALFSIVVDWKLFQ
//
ID  F5HFZ4;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  295027;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: F5HFZ4;
DR  PDB: 5D5N;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSVSGVRTPRERRSALRSLLRKRRQRELASKVASTVNGATSANNHGEPPSPADARPRLTLHDLHDIFREHPELELKYLN
SQ  MMKMAITGKESICLPFNFHSHRQHTCLDISPYGNEQVSRIACTSCEDNRILPTASDAMVAFINQTSNIMKNRNFYYGFCK
SQ  SSELLKLSTNQPPIFQIYYLLHAANHDIVPFMHAENGRLHMHVIFENSDVHIPCDCITQMLTAAREDYSVTLNIVRDHVV
SQ  ISVLCHAVSASSVKIDVTILQRKIDEMDIPNDVSESFERYKELIQELCQSSGNNLYEEATSSYAIRSPLTASPLHVVSTN
SQ  GCGPSSSSQSTPPHLHPPSQATQPHHYSHHQSQSQQHHHRPQSPPPPLFLNSIRAP
//
ID  A6ZMC4;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: A6ZMC4;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy.
DE  Reference Proteome: No;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFAMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAET
SQ  RVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNI
SQ  TELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQ
SQ  IIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKK
SQ  QLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDIS
SQ  EKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIK
SQ  RYYQWAALLLSIYLGAKTGSLIDF
//
ID  Q6NX12;
PN  Nuclear pore complex protein Nup93;
GN  nup93;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q6NX12;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051292;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDGEGFGELLQQAEQLAAETEGVTELPHVERNLQEIQQAGERLRSKTMTRTSQESANVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFVMAEEYHRESMLVEWEQVKQRVLHTLLASGEDALDFTQ
SQ  ESETSYISESGAPGRSSLDNVEMAYARQIYMYNEKVVSGHLQPSLVELCTEAAERLDDKNVSDLWVMVKQMTDVPLIPAS
SQ  DSLKSRCSVQMQMAFLRQALHFLEQSYKNYTLMSVFANLQQAQLGGVPGTYNLVRSFLNIRLPAPIPGLQDGEVEGYPVW
SQ  ALIYYCMRCGDLMAAQQVVNRAQHQLGDFKNCFQEYVHSKDRRLSPTTENKLRLHYRRAVRASTDPYKRVVYCIIGRCDV
SQ  TDNHSEVADKTEDYLWLKLSQVCFEDEANSSPQDRLTLPQFQKQLFEDYGESHFAVNQQPYLYFQVLFLTAQFEAAIAFL
SQ  FRLERTRCHAVHVALALFELKLLLKSTGQSAQLLSLEPGDPQGVRHLNFIRLLMLYTRKFEPTDPREALQYFYFLRNEKD
SQ  SQGESMFLRCVSELVIESREFDMLLGKLEKDGSRKPGAIDKFTRDTKTIINKVASVAENKGLFEEAAKLYDLAKNPDKVL
SQ  ELTNKLLSPVVSQISAPQSNRERLKNMALAIAERYKSQGVSAEKSINSTFYLLLDLITFFDEYHAGHVDLAFDVIERLKL
SQ  VPLSQDSVEERVAAFRNFSDEIRHNLSEILLATMNILFTQYKRLKGSGPNTLGRPQRAQEDKDSVLRSQARALITFAGMI
SQ  PYRMSGDTNARLVQMEVLMN
//
ID  Q66GR8;
PN  Protein NETWORKED 3A;
GN  NET3A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22840520}. Nucleus membrane {ECO:0000269|PubMed:22840520}.
DR  UNIPROT: Q66GR8;
DR  UNIPROT: Q67ZU6;
DR  UNIPROT: Q9LR76;
DR  Pfam: PF07765;
DR  PROSITE: PS51774;
DE  Function: Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex. {ECO:0000305|PubMed:22840520}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005774;
GO  GO:0051015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVMDSSKWWWIGNHNTTNFSPWLHSTLSELDEKTKEMLRVIDEDADSFAARAEMYYKKRPELIAMVEEFYRSHRSLAERY
SQ  DLLRPSSVHKHGSDSESHEKSSTCDESSWSEACETHEEYAESEIDNGESKWVDESEIDGIVEEIEPSEVVYSEGNGNSEM
SQ  MKIEIERLREENKVYSEMVREKDEEKREAIRQMSVAIQMLKEENSELKKRVTNTVVARRNKEGGDSQRKQQMWKPFEFKK
SQ  IKLEGLWGKGFGNWALPNTDSTSKELMTL
//
ID  A0A2R8Q3S9;
PN  Chloride channel CLIC-like protein 1;
GN  clcc1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: A0A2R8Q3S9;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (PubMed:30157172). {ECO:0000250|UniProtKB:Q9WU61, ECO:0000269|PubMed:30157172}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKLSSSSSFGLCILVVFFCFVVIESAKIRIDGYNDEAWIDPYDMLNYDPTTKRMRKSTESESYQNVPTKRREFNSESCDV
SQ  PKCPDEHECIKKLHILQKEFDEQKSKSTATLSKPVCLPVFKRFLSKLLKETSKLGLPDDGITAMHYDAEVKLSKQSLAEI
SQ  QKLLNDEDGWTTGAMDEALSQILVQFKLHDYEAWKWRFEDTFHVDVDTVLKVSLIVLIIVAIICTQLWSVVSWFVQFRRM
SQ  FAVSFFISLIWNWFHLYMLAFAEHKKNIVQVESFNAKCTGLKQLNWQDSLSEWYRRTWTLQDDPCKKYYEVLVVNPILLV
SQ  PPTKAITITITNFITDPLKHIGEGISEFLRALLKDLPVTLQIPVLIIIILAILIFVYGSAQAAIHQVARFPRLGWRQEQP
SQ  PPAVGQRQNPQLRAHEEPWEGGDARQPLPMRQDNRGNHVGNRGDQGFRDANAPENREEDRSMDIRQEFSTKRTPVETLQA
SQ  TGNTFPDDETDSQQRTQELDSGANVEEEVKVEEKEKKESFSVDNKEQKETKSPDRSEPITSEPPSSIDVKTVGADQGNEH
SQ  LMCTKRKWAAQNGFKLQVILCEINSEASADLPEEEECFSFKHPVQETQS
//
ID  Q12144;
PN  Pore and endoplasmic reticulum protein of 33 kDa;
GN  PER33;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex.
DR  UNIPROT: Q12144;
DR  UNIPROT: D6VY65;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P10591; IntAct: EBI-37691,EBI-8591; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-37691,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-37691,EBI-8603; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-37691,EBI-17244; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTVPRNRPMAPFGTIIKSRIKQPQFYWFIGHFLTIFNFIQFHLSITSKQNQLSCYRRSLFYISVTYAIVLYQFFKSDQLK
SQ  FNFTLLRQEMKKLDNLQYFAMLFILFLLSQFNIIISGSLYSPVIFSIFHFLNYFKENLLPFLPLIPLNLKNLLNSKITVF
SQ  IQNYNGFFLQMAQVFEIICGLRVGLFLVPFNFFLLLVRRANVSFEVVGTMLAGLTYVWFFKLRYLQSESMRQIFKQYVLR
SQ  LDAYVSRTLPPYCSRLWNGYKNFVMTVFWKIPV
//
ID  Q9P7M8;
PN  Nucleoporin nup184;
GN  nup184;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10388805}.
DR  UNIPROT: Q9P7M8;
DR  UNIPROT: Q9Y8G4;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Interacts with pom152 in the core structure of the nuclear pore complex (NPC). Involved in the export of mRNA. {ECO:0000269|PubMed:10388805}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006607;
GO  GO:0006606;
GO  GO:0010389;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDYLLSWSWILDAFETSDENLSQNKFEELLDARIAAFQQIESPVTGTLNSNKTTEGEEAKLSIYDSSHSISKSQLESVK
SQ  KISDITGYNEAQVAYVLLVHQYELNTQYFSQLDNDSVLAQEFQRRYYAEIISCWKVLAFLLQACTDADSKWHKMATRLIV
SQ  SIFQTAQRSGENAQSTTPSIFCVRIIDYLSKMTSQAAPASLTFNGEEAISQWYFFHFNLQLQLLRVIFLSTYSLVVCNSE
SQ  MAISWFNCMKKTRYLHDQEFMHLDIDTGFSMCKEITNVAIIISINFISLEKQVLSFKDNPSFFMLSGNTIISLHDMITQL
SQ  SNDSIGAAVSLTWGIALHLLSNSPDNIPLIQNSSVVSSKILQNPQNSFQALIIAALKYDPFTLIHRIISSLEDDPYIDGY
SQ  SKIMATLFSSAVSYVKFSDSTMLCATTLFKTPQVYQLFENNDSVTRLLNFARARFPFEYSQFVLLLIPTFACLTSKQLVS
SQ  SELLHMTTFTQSLPSGFKAYEIIPEPNVTGNALIELQESLHLDSYGFFFPNAERSLPKGTRGRIVSVDTYPPVVMWDLNY
SQ  SLWEAVGISLNYIVRNGLINSHKSFVLTVLSSSVPLFQTDVSGACELVHLASEGLDGELDFINVICDLLDYFLSLSVIED
SQ  ADYQICVSSLRLLREFTRFAATDVWAYVTRSLVCVGSEKGISLEDVIFDYESINGVYDFTLAFFDLYEILLDNCISTSVV
SQ  PDDFSIRLKTDFVKRAMRFLCEVFANYLDWKYARIIQQYQIGHRFASLITKLLNVTFGIEYFNPKTTVNKKTLPLRELSH
SQ  YIVQRFLVQQDSNRYLHPLLSVMDLINLLYTDIFSTISSPRAKAAKMWLISSFCAMKTLICLRGFLNLKPSELERELFSR
SQ  SPDLFNCLPRLLCCIAPILQLLSALILAPWPSETPSLLAYMINSTDIVGRVCIQILTNPIQSTNIEGSVWKFLSSIMKGQ
SQ  QQGLAVLLFSGKKFPLDRMKSLNHNVDVQLTSKSLISLAEKRLDSFSINDILSQVPVFEFIFLSRNFWTASLGNLQQEAN
SQ  FWNRIVDAIKLPLTVKLDGLSSVAQADLYILAAHATRITAIQLHMSKLNKSNSSKKIIIDPLKDSMKDLVQHAFTITAYD
SQ  SNIHNALTRAFKHENGDLHISDLRNTGLFPLRYGDNYFYNIKLAKNMLLNTEDTSFKISMMMSANENLSLLDAQAALLRS
SQ  WSIFICAFVEFVKEDATLSILELKIMKWVLKSLAEDTIDVNVVQELSAERAALVFRISQQTLAIPISNEVKEHLQSILLL
SQ  TWKAITTTKFSIYEDSNGEMAYYRPLLHVLYNTLNRLLSEEKENLSLSVGFVSGLLQLCHRKLSQLFEKAVINPTIEVYG
SQ  DIVLLNSLHKCIVNSHLIRGLQSLYISYINDSFSVDNCLRLFSWSHSLLVDGQPYFADAALSFLLICSSSPAGAEQIVMN
SQ  GFFYSIMESPLSTALSTGGLGLDGSSIQYKIWIRGILPLLFNIVKFLGNRIMNDMREFVLLAFPQIQYALLNWCQPPSSI
SQ  SLASIDESFMIVLLFDLLQQFNPALLQEIRLAELKIEMLEASTI
//
ID  I6V1W0;
PN  Protein brambleberry;
GN  bmb;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22863006}; Multi-pass membrane protein {ECO:0000269|PubMed:22863006}. Note=During metaphase, localizes near the mitotic spindle region, and its localization shifts to the chromosomes as they reach the end of the spindle. During karyomere fusion, detected in prominent puncta, mainly at karyomere-karyomere interfaces corresponding to putative fusion sites.
DR  UNIPROT: I6V1W0;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:22863006}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0061472;
GO  GO:0007344;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALWFVLLWVSSLQYAEVEAFFDWLKKADPAPTPPPAESIVPILLHGEAPAFEMSVVDEKFLAEAKQMELSPLDSCHFRV
SQ  VAQLKATCSGLSEEQLAKLGVALFNCQSEVEGRRTYPCTEEMSIKECTADMDSDTWNAYHIVSNRARSVCYATRQQHFRK
SQ  RAELTVNALISTATSQLDAMKDLKEGQKELRDMTAASLDKLLEGHGALQIQQGALKEGQEQLDASISENLQRLAQEKALI
SQ  STGQQLVAQLIQGITQRMENVSGQLKDQTAEVQEGHQAILEDLAVVRGSAQDIYEKMELNLNGFLQQQNTTAHFYTELMR
SQ  KLELMNGTLGYMLTYLDNMQTRLEDRLHMIQGYLGWAGLSLRALWTCVMHAGYFLLCAVLLSFLQCTTFSRVTLLLSVPI
SQ  NAIAEINQQAALDLISLTLLLFTLSLGRWFVLQLLWALSKIKGRTCSRPPHLSIYPPKEKTPEKQHEFGEKCPASSSTPV
SQ  QSDPVCDLEVESFMMGDPCVLGVSPSRCPPKFSHHHLGGTPNHSTPRLKSRHSIAATELDNIPQRNLGVFLETVNRSRSS
SQ  SPNQSLASSSSFSGRSLCSGITRLGQPCKKRAVVGQDYCRVHEGGHTSYSRL
//
ID  Q8L748;
PN  Nuclear pore complex protein NUP107;
GN  NUP107;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8L748;
DR  UNIPROT: F4JFR3;
DR  UNIPROT: F4JFR5;
DR  UNIPROT: Q84ME0;
DR  UNIPROT: Q9LJH6;
DR  Pfam: PF04121;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P10797; IntAct: EBI-4434139,EBI-4433614; Score: 0.37
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMDMDTSPSYFDPEALSVRDQFRRYRKRHSTSPHEEMLSSNVSENRLLYDGHNIHSPTNTALLLENIKEEVDNFHTDHY
SQ  EGTPTNPISASRRESVGILNDDDEALFRRVESQSLKACKIENDELAESGDTTFALFASLFDSALQGLMSIPNLMLRLEES
SQ  CRNVSQSIRYGSDIRHRAVEDKLMRQKAQLLLGEAASWSLLWNLYGKGTDEVPENLILIPSTSHLEACQFVLNDHTAQLC
SQ  LRIVMWLEELASKSLDLERKVQGSHVGTYLPNAGVWHHTQRYLKKNGSNADTLHHLDFDAPTREHARLLPDDYKQDESVL
SQ  EDVWTLIRAGRIEEACDLCRSAGQSWRAATLCPFSGMDMFPSIEALVKNGENRTLQAIEQESGFGNQLRLWKWASYCASE
SQ  KIAEQDGGKHEVAVFATQCSNLNRMLPICTDWESACWAMAKSWLDVQVDLELAQSKPGLTERFKSCIDESPEATQNGCQA
SQ  SFGPEDWPLHVLNQQPRDLPALLQKLHSGEMVHEAVVRGCKEQHRQIQMNLMLGDISHLLDIIWSWIAPLEDDQSNFRPH
SQ  GDPHMIKFGAHMVLVLRLLFTDEINDSFKEKLNNVGDLILHMYAMFLFSKQHEELVGIYASQLARHRCIELFVHMMELRM
SQ  HSSVHVKYKIFLSAMEYLSFSPVDDLHGNFEEIVDRVLSRSREIKLAKYDPSIDVAEQHRQQSLQKAIAIQWLCFTPPST
SQ  IKDVKDVTSKLLLRSLMHSNILFREFALIAMWRVPATPVGAHTLLSYLAEPLKQLSENPDTLEDYVSENLQEFQDWNEYY
SQ  SCDAKYRNWLKFQLENAEVTELSEEENQKAVVAAKETLDSSLSLLLRQDNPWMTFLEDHVFESEEYLFLELHATAMLCLP
SQ  SGECLRPDATVCAALMSALYSSVSEEVVLDRQLMVNVSISSRDSYCIEVVLRCLAIKGDGLGPHNANDGGILSAVAAAGF
SQ  KGSDIYGTYFSFTYDLPPFSIEIWGCELTRFQAGVTMDISRLDAWYSSKEGSLETPATYIVRGLCRRCCLPELVLRSMQV
SQ  SVSLMESGNPPEDHDELIELVASDETGFLSLFSRQQLQEFMLFEREYRMSQLELQEELSSP
//
ID  Q0P5M9;
PN  Major facilitator superfamily domain-containing protein 10;
GN  MFSD10;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D2V8}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q0P5M9;
DR  Pfam: PF07690;
DR  PROSITE: PS50850;
DE  Function: Confers cellular resistance to apoptosis induced by the non- steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump (By similarity). {ECO:0000250|UniProtKB:Q14728}.
DE  Reference Proteome: Yes;
GO  GO:0031526;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0022857;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCGAGGSCTPRPPIRQQQAPETRVVAVVFLGLLLDLLAFTLLLPLLPGLLESHGRAHDPLYGSWQRGVDWFAAAIGMPA
SQ  EKRYNSVLFGGLIGSVFSLLQFLSAPLTGALSDCLGRRPGMLLSLAGVATSYAVWAASKSFAAFLASRVIGGISKGNVSL
SQ  CTAIVADLGSPSARSKGMAVIGVAFSLGFTLGPTLGAFLPSETVPWLALLFAVSDLLFIWCFLPETLPPEKRAPSVTLGF
SQ  RAAADLLSPLALLRFSAVARGPDPPTGVRLGSLRGLGLVYFLYLFLFSGLEFTLSFLVHQRFRFSRVEQGKMFFFIGLTM
SQ  ATIQGAYARRIRPGREIAAVKQAILLLIPASLFVGWGHTLPILGLGLLLYSWAAAVVVPCLSSVVAGYGSPGQKGTVMGT
SQ  LRSLGALARAVGPVVAASAYWLAGARVCYTVCAALFLLPFSILRTLSPPARTLKAE
//
ID  Q54Z22;
PN  Nuclear pore complex protein nup43;
GN  nup43;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q54Z22;
DR  PROSITE: PS50294;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSVSVHYSTHKINKVRFLNRNFHNDTSLFVTGTNHPVLSKNKISVWGLESRQNSDEIEELASVPIDGIVTELKVIEINN
SQ  KPMIIGSTSKGSIFMYSIFNLPNKFEYIGYDGLLDKKYENYNNINNINDTYDTCNLLKERIWFNSSSNNNNVNSNNINNN
SQ  NYNNNNNNYNNNNNNNNNNNNNNNNNNNNGSCINSFDISYDQHSLVTVGNDGVMNLLSIENLIPIYTNRYIDGLSVNVVK
SQ  SITSNQIITSGELGRYIKFWDIRSNSSQPVKTIKTQCPRIFSLAIHKDEQHIIAAGSSDGQVNLFDIRNDYSIDQNKTHN
SQ  SNVWELSFSKSNPNQLYSCSEDGFIYQYSYNKDNLGGGGMMTLPNQINNTFDIYSKEVSLLQLPTSIGSIDSFDINSNIN
SQ  RLICCSTSSQCLIVKSL
//
ID  Q09877;
PN  Sad1-interacting factor 3;
GN  sif3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q09877;
DR  UNIPROT: O94555;
DR  Pfam: PF02582;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0140053;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHA
SQ  AAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVK
SQ  HFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISE
SQ  IFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAM
SQ  SHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLP
SQ  LYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR
//
ID  A1CS06;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  344612;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A1CS06;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAATRPIILRFESRNGQFRLSVSPQELFPTLKQKILENLPKDVEPSSITLSNKPIGTGGEERSLDGLEGVSIEQVGLKHG
SQ  DKLFVGYQERKGGETTPAKAHAAADSLRRLNGALVPQTETVTFRPPTSSSATVKNPWEVVQQSPLDDKLDKKDGKIQRPR
SQ  DMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKINAATNKAELKSSFMPPLSEPYYRVRHDCPSGHPPWP
SQ  EGICTKCQPSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGSQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDE
SQ  VDGVTLHEWPNEKEVDEVARLCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRLQAQYPKTTKWSRTG
SQ  RFGSNFVTCVLSGDEEGAITISSYQASVSAVEMVRADIVEPSAEPSVMLVQSEDDDSDNKSRYIPEVFYRKINEYGVSAQ
SQ  QNAKPSFPVEFLLVTLTHGFPTESNPLFTKSTFPIENREVIGESQDLRSVAKKLVSHRDSNEVIPEVSDFHLLCYLHSLS
SQ  TFSKTNANRLHSKITRTVTTNLMTPQDEEKLLCRVATSHDPTEGLKLINTPGWATLVTILQESGERPPKRPWLNPADPPR
SQ  PLSQQGKRHLSSRPESPKSESEQLAKRFKGASLE
//
ID  Q99NF8;
PN  Ran-binding protein 17;
GN  Ranbp17;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q99NF8;
DR  UNIPROT: Q9D4E3;
DR  Pfam: PF03810;
DE  Function: May function as a nuclear transport receptor. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005049;
GO  GO:0008536;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALHFQSLAELEVLCTHLYVGTDLTERIEAEKALLELIDSPECLSKCQLLLEQGTTSYAQLLAATCLSKLVTRINPLPIE
SQ  QRIDIRNYILNYVASQPKLAPFVIQALIQVIAKLTKLGWFEVQKDEFVFREIIADVKKFLQGTVEHCIIGVIILCELTQE
SQ  MNLVDYSRPSAKHRKIATSFRDTSLKDILVLACSLLKQVLAKPLNLQDQDQQSLVMQVLKLVLSCLNFDFLGSSADESAD
SQ  DLCTVQIPTTWRTIFLEPETLDLFFNLYHSLPPLLSQLALSCLVQFASTRRSLFSSPERAKYLGNLIKGVKRILENPQGL
SQ  SDPGNYHEFCRFLARLKTNYQLGELVLVKEYAEVIGLIANFTITSLQHWEFAPNSVHYLLTLWQRMVASVPFVKSAEPHL
SQ  LDTYAPEITKAFITSRLESVAIVVRDNLEDPLDDTATVFQQLEQLCTVSRCEYEKTCTLLVQLFDQNAQNYQKLLHAAPG
SQ  LAVDMAIQEGRLAWLIYLVGTVVGGRLTYTSTDEHDAMDGELSCRVFQLISLMDTRLPHCTNEKIELAVLWFLDQFRKTY
SQ  VGDQLQRTSKVYARMSEVLGITDDNHVLETFMTKIVTNLKYWGRCEPVISRTLQFLSDLSVGYILLKKLVKIDAVKFMLK
SQ  NHTSEHFPFLGISETYNVGDFRCRTTFYTALTRLLMVDLGEDEDEFENFMLPLTVSFETVLQIFNNNFKQEEVKRMLIGL
SQ  ARDLRGIAFALNTKTSYTMLFDWIYPAYLPVLQRAIERWYGEPACTTPILKLLAELMQNRSQRLNFDVSSPNGILLFREA
SQ  SKMICTYGNQILSLGSLSKDKIYPMKLKGISICYSALKSALCGNYVSFGVFKLYGDNHFDNVLQAFVKMLLSVSHSDLLQ
SQ  YRKLSQSYYPLLECLTQDHMSFITNLEPPVLLYVLTSLSEGLTTLDTVVSSSCCTSLDYMVTYLFKHIAKEGKKPLRSRE
SQ  AMQAGQRLLHFMQQNPDVLQQMMSVLMNTIVFEDCRNQWSVSRPLLGLILLNEKYFSELRASLINSQPLPKQEVLGQCFR
SQ  NLMEGVEQNLSVKNRDRFTQNLSVFRRDVAEALRSDGHTDLSSLDMMS
//
ID  Q298S5;
PN  Nucleoporin Ndc1;
GN  Ndc1;
OS  46245;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q298S5;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHLSTINACKLLLFRRCLQAVLLTVGIQFLLLTIFLLFVNFQLLRPLHWISVTLSLVCSMYTWFASIPLVGAVVLYGMI
SQ  LCQQHLAERLYCPTRFRWLVHYAPRKLLFLAAHLLVGYLTAWLYTGYMHTDYRHLWYKCYDQECISAYHVYLLGMGIFAG
SQ  CYYFVSVHMRQEVEIEFPIVNHLWGEKLREVLYSSLARSLIKSLLPTLAYTLLFWLFGGVVCHKLSHIFAVDLDERLEGF
SQ  FGVATNGRLLFYGWLLTSQILSNMHLMRCFYSMFLSEEFPLAITKNRAAFVQEKEVTVVAALGLSNVYVVQCLAAKYLYN
SQ  LVTAGDAEKRSELFQLTEPGNRPANWRSLCDQCLSLFGNFTDELIDSMQKISVLKGSPSSPPLTPISENASASLMAERVL
SQ  TRQYNQMHGIRAIVSPRSNAVIDRPVDRIHRVPDWCERTSMQLEQSLQLLINRIPGIVYMFTEPEGAKTAFLLTHSLPLV
SQ  FVIQALSQICVFSLKEDRYGVVQTDLPDIIRSMSRLKGELDKLSSVASNLRGPGSSFSVLRGAVRRSLFHICVAFGEYLS
SQ  ELIPSGEELHQLQTVINQE
//
ID  F4IGA5;
PN  Nuclear pore complex protein NUP133;
GN  NUP133;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4IGA5;
DR  UNIPROT: F4IGA4;
DR  UNIPROT: Q9SJ43;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016020;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0031081;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSPLTKRAKQSSRNEKTPRNRVPPPDSPVTPATQNRNNFISDRPATGTPAPWAPRLSVLARVSPGNNGDKGVDSDQLKP
SQ  VFVGEFPQLLRDEQSYPGDACVSGGMDKETCLSWFITGSKVFVWSHLTTLPSRKCVVLELPVVVLVNEESGSGLQDGKSW
SQ  LVNVVSWDTSAGAATRASRSRSPVGVVMCNRKTRAVVYWSDIFSGQEAAPAEKARHLIKRQSNGIRSSRAENSDLNSLIT
SQ  TAVAAAERLCIAIACSSNGELWQFTCSPTGVKSNQVQLNISSSSVSEGYPRSLIWRFSQGLARESCWEFLMLTDCDIHCF
SQ  TIEPYPDLTVSEVWQHEIVGTDGDSGIKKDIASQKQIWPLDLQVDDQGKVITVLVATICMDRASSSSYTQYSLLTLQHKS
SQ  EMRFADGREEKVLEKQGPIQVIIPKARVEDKDFLFSMRLRVGGRPPGSAIILSGDGTATVCYCHGSSTRLYKFDLPYDAG
SQ  KVLDASVLSSTDEHEYGAWTVLTEKAGVWAIPEKAVVLGGVEPPERSLSRKNSSNERSTRDETRVTPYGVDRTAGRENSD
SQ  IQNIEDKGNPKMGFTRQTARDEESEALLGQLFEGFLLSGKVDGSLEKLSQSGAFDRDGEANVFARKSKSIVDTLAKHWTT
SQ  TRGAEIVAMTVISSQLVEKQQKHENFLHFLALSKCHEELCSKQRHSLQIILENGEKLAAMIQLRELQNMINQNRSARFGS
SQ  PQAGSEDQVSCALWDLIQFVGERARRNTVLLMDRDNAEVFYSKVSELEEVFYCLNRQLEYIIRADQPLGTQLQRACELSN
SQ  ACVTILQTALDYKNEHQMWYPPLEGLIPWHSQTVVCNGLWCIASFMLHLLTEASRIDISAKSDIYTHLEVLTEVLLEACA
SQ  GSTFAKLEREEENKGLLNEYWTRRDTIFDSLYRQAKEFMEAEIQGIRERTEATDEDIFRNRCSNLISIAKRHAGYKIMWK
SQ  ICYDLNDTGLLRNLMHEGVGPQGGFSYFVFQQLYDMKQFSKLLRLGEEFQDELLIFLKRHSDLVWLHQVFLHQFSSASDT
SQ  LHTLALSQDEESMTTVEERTGPEPEDVQPTFADRKRFLNLSKIAYVADKDADSESKVKRIEADLNLLKLQEEITKALPNG
SQ  EARNRLFRPEELIETCLNIQGRWTAIKAFEVFAWTSSSFRENHRSLLEECWRNAADQDDWDRHHQASTNEGWSEEETLQN
SQ  LRNTALFQASKRCYGPTRVNTFDGDFAQVLPLRRENPEDSTSSVEDVLMSHKDFAEAGKLMLTAIMLGCVEEEGIVAEEF
SQ  SSPME
//
ID  G0S9A7;
PN  Nucleoporin NUP133;
GN  NUP133;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P36161}. Nucleus membrane {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36161}; Cytoplasmic side {ECO:0000250|UniProtKB:P36161}. Nucleus membrane {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36161}; Nucleoplasmic side {ECO:0000250|UniProtKB:P36161}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P36161}.
DR  UNIPROT: G0S9A7;
DR  UNIPROT: G3EQ74;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre- ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P36161}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36161};
SQ  MFSSTLHEDGPATRTRSSRRRQRPVASDSSLQTQPKAKRQRVPLTESNTAPTPTPADADAPPEMFEVKPDPVLAKRERDG
SQ  IGIENIENLGPRRELSLRSKKPKSGERTSKGDGSIILTTNNAFTVSKLPALPDRLRAEPTSRQHGAIFSSGYALALTHTH
SQ  AFVWPYTATTASPETFTFALPYPSKHASDPLPLGALVPPSASSDDPGLVVVMPVSGRVVYWESISSAATLDFIRQQRTGI
SQ  EDAISGMYSSEHITQLVSAESAGFVLVFSSGRIAYMSVRDPHGRPGITVQYLRSPFGGASLGFLSTLRHALSGSSRGDIA
SQ  AAHANHGPRVGERVVIAASSKGRLQAWKIHRGGHHEPVAEADVRERLVEAVNEADAKTQAFPSESFEVLDFAFVPRGLEP
SQ  KYVNASRLSEALTHEEDSLQHMLLLVGFSRGHQARYSLVETVLAPEGARIGTVRPITSYTSPVRPGALEKPRLYLPRPAL
SQ  VAFVVFDRAVVVASMVAPPDSPDSQLQEDSHILPPTFEDVVDFRDDDTLQVVGSGSEEPGAGTSSEDVRPHRHKTKNPTA
SQ  VLLLPGVGIVRVAITDIERFASDAPPRVTAKSKLEQAVFFGIKSDNPLVFQGRRALPFSDREVCDAAVELSHEIVNSKTP
SQ  FIPSVPASLEGNMKSRSAYLDALITFLNACKVNMDERTRWMLLYDAEKMAVATWIWQKHEQFLAERPRADKKTLISEAAV
SQ  FINENQKTELNVAAGQVDPVRHWFIHDIFRLDIFVAWAYQIIKYHYTQKLSDEPGLNRLVWEAVTINNGALLEARQFRLD
SQ  KAAQYGVDPAVVPTGNGLPEPWTSTYFITNNLKRLTEFCHQWLAKHDAQPSADPRFDARLLDTVRERLPSLTSQYFTSLS
SQ  EYITWAASSTDPETQDRCRAYQAAYAEDVYKKIVKLKEFDLWEEAVELAREFEAFDALADVVVGQILMLEAAAADPTTTE
SQ  SKAQENAALAQVKKQRLGRLMEEFGEGFASRAYEVLLDAAGVQAVLEFAFDRKGFITKWLRGKPELARISWVNEVLREGD
SQ  VGGAAETLLGLGMSREVQVWNKKVELSLGKLALLAEGGGSDDEAGKGEVGGTIKKIDAELEVVKVQDLLYQWILASVHEA
SQ  VDSSAEVELAVKQFGGLIPRRQKALLQIFEDGIARLLKHEVLDPLTLIDLLTLSSLGPGHYEGMGDQFFLALKVAHYAAL
SQ  ENAEEVRRLIWRRCLVRDDWRQVNETNLKGDEEALEAVGETAAYRTLFACFDEESSTPTFRPHHTLKPSDCLGVYTEPEQ
SQ  LDSRFAAMDDSFRGKLVEAMRAEDRLLRGFVEKAQLDEWWRATRETAERMVGVAAQKGHRRVNSGSVGNGGVNGLSLNGR
SQ  VKMY
//
ID  A2IDD5;
PN  Coiled-coil domain-containing protein 78;
GN  CCDC78;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Cell membrane, sarcolemma. Sarcoplasmic reticulum. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm.
DR  UNIPROT: A2IDD5;
DR  UNIPROT: B4DNY4;
DR  UNIPROT: B4E1U6;
DR  UNIPROT: Q05BY7;
DR  UNIPROT: Q05CA0;
DR  UNIPROT: Q6T2V5;
DR  UNIPROT: Q6ZR33;
DR  UNIPROT: Q8IUR3;
DR  UNIPROT: Q8NAY7;
DR  UNIPROT: Q96S12;
DR  Pfam: PF14739;
DR  OMIM: 614666;
DR  OMIM: 614807;
DR  DisGeNET: 124093;
DE  Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome. {ECO:0000269|PubMed:24075808}.
DE  Disease: Myopathy, centronuclear, 4 (CNM4) [MIM:614807]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:22818856}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NQ75-2; IntAct: EBI-2874003,EBI-12270182; Score: 0.37
DE  Interaction: Q8D194; IntAct: EBI-2874003,EBI-2847851; Score: 0.37
GO  GO:0005814;
GO  GO:0098536;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030030;
GO  GO:0098535;
GO  GO:0003009;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHE
SQ  AEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHR
SQ  LGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLK
SQ  DEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAP
SQ  GNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQ
SQ  SWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS
//
ID  Q15642;
PN  Cdc42-interacting protein 4;
GN  TRIP10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Note=Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. {ECO:0000250}. [Isoform 5]: Cytoplasm, perinuclear region.
DR  UNIPROT: Q15642;
DR  UNIPROT: B2R8A6;
DR  UNIPROT: B7WP22;
DR  UNIPROT: D6W645;
DR  UNIPROT: O15184;
DR  UNIPROT: Q53G22;
DR  UNIPROT: Q5TZN1;
DR  UNIPROT: Q6FI24;
DR  UNIPROT: Q8NFL1;
DR  UNIPROT: Q8TCY1;
DR  UNIPROT: Q8TDX3;
DR  UNIPROT: Q96RJ1;
DR  PDB: 2CT4;
DR  PDB: 2EFK;
DR  PDB: 2KE4;
DR  Pfam: PF00611;
DR  Pfam: PF00018;
DR  PROSITE: PS51741;
DR  PROSITE: PS51860;
DR  PROSITE: PS50002;
DR  OMIM: 604504;
DR  DisGeNET: 9322;
DE  Function: Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5- bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte- derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:11069762, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-739936,EBI-739936; Score: 0.74
DE  Interaction: Q96RU3; IntAct: EBI-1111248,EBI-739936; Score: 0.27
DE  Interaction: Q9H4E5; IntAct: EBI-739936,EBI-6285694; Score: 0.56
DE  Interaction: Q969G3; IntAct: EBI-739936,EBI-455078; Score: 0.56
DE  Interaction: Q92558; IntAct: EBI-739936,EBI-1548747; Score: 0.56
DE  Interaction: Q17R89-2; IntAct: EBI-10238335,EBI-739936; Score: 0.56
DE  Interaction: Q1RLN5; IntAct: EBI-739936,EBI-3959665; Score: 0.56
DE  Interaction: Q68EM7; IntAct: EBI-739936,EBI-1642807; Score: 0.56
DE  Interaction: Q9Y3L3; IntAct: EBI-346869,EBI-739936; Score: 0.56
DE  Interaction: A0A384LA14; IntAct: EBI-2845602,EBI-739936; Score: 0.37
DE  Interaction: A0A0F7RIX9; IntAct: EBI-739936,EBI-2817483; Score: 0.37
DE  Interaction: Q17R89-1; IntAct: EBI-25410514,EBI-739936; Score: 0.35
DE  Interaction: Q9Y2W2; IntAct: EBI-714455,EBI-739936; Score: 0.37
GO  GO:0005938;
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005764;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0042802;
GO  GO:0008289;
GO  GO:0030036;
GO  GO:0007154;
GO  GO:0006897;
GO  GO:0061024;
GO  GO:0051056;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEV
SQ  NDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQ
SQ  DINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELE
SQ  VVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKR
SQ  WPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQR
SQ  KRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRG
SQ  DSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTIS
SQ  MAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN
//
ID  O54946;
PN  DnaJ homolog subfamily B member 6;
GN  Dnajb6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: O54946;
DR  UNIPROT: Q3TE94;
DR  UNIPROT: Q3U6L0;
DR  UNIPROT: Q3UNJ5;
DR  UNIPROT: Q3UYT7;
DR  UNIPROT: Q99LA5;
DR  UNIPROT: Q9QYI9;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8CG73; IntAct: EBI-4281130,EBI-642500; Score: 0.35
DE  Interaction: Q9CQV8; IntAct: EBI-771608,EBI-642500; Score: 0.35
DE  Interaction: Q8BWG8; IntAct: EBI-642500,EBI-641778; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0031072;
GO  GO:0042802;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0030036;
GO  GO:0061077;
GO  GO:0060710;
GO  GO:0060717;
GO  GO:0030198;
GO  GO:0045109;
GO  GO:0043154;
GO  GO:0090084;
GO  GO:0045892;
GO  GO:0006457;
GO  GO:0034504;
GO  GO:0032880;
GO  GO:0060715;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  GIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDT
SQ  GFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALA
SQ  EECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDD
SQ  EQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH
//
ID  O60238;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
GN  BNIP3L;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
DR  UNIPROT: O60238;
DR  UNIPROT: B0AZS9;
DR  UNIPROT: Q5JW63;
DR  UNIPROT: Q8NF87;
DR  Pfam: PF06553;
DR  OMIM: 605368;
DR  DisGeNET: 665;
DE  Function: Induces apoptosis. Interacts with viral and cellular anti- apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-849893,EBI-10171534; Score: 0.56
DE  Interaction: Self; IntAct: EBI-849893,EBI-849893; Score: 0.86
DE  Interaction: Q12983; IntAct: EBI-749464,EBI-849893; Score: 0.96
DE  Interaction: Q5T700; IntAct: EBI-10173166,EBI-849893; Score: 0.67
DE  Interaction: Q969F0; IntAct: EBI-849893,EBI-743099; Score: 0.56
DE  Interaction: Q9BXN2; IntAct: EBI-3939278,EBI-849893; Score: 0.67
DE  Interaction: Q9NRQ5; IntAct: EBI-8640191,EBI-849893; Score: 0.78
DE  Interaction: P17152; IntAct: EBI-723946,EBI-849893; Score: 0.84
DE  Interaction: Q7CIP6; IntAct: EBI-849893,EBI-2852197; Score: 0.37
DE  Interaction: A0A384LD58; IntAct: EBI-2856011,EBI-849893; Score: 0.37
DE  Interaction: P51452; IntAct: EBI-849893,EBI-1049755; Score: 0.37
DE  Interaction: Q16610; IntAct: EBI-947964,EBI-849893; Score: 0.37
DE  Interaction: O14936; IntAct: EBI-849893,EBI-1215506; Score: 0.37
DE  Interaction: Q8IU85; IntAct: EBI-849893,EBI-3911453; Score: 0.37
DE  Interaction: Q8NI37; IntAct: EBI-9089276,EBI-849893; Score: 0.35
DE  Interaction: Q13021; IntAct: EBI-750078,EBI-849893; Score: 0.56
DE  Interaction: Q9NQ11; IntAct: EBI-849893,EBI-6308763; Score: 0.51
DE  Interaction: Q81X61; IntAct: EBI-2817767,EBI-849893; Score: 0.37
DE  Interaction: Q81TT4; IntAct: EBI-849893,EBI-2810319; Score: 0.37
DE  Interaction: A0A384L1C8; IntAct: EBI-2846642,EBI-849893; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-739737,EBI-849893; Score: 0.37
DE  Interaction: Q6NUQ1; IntAct: EBI-849893,EBI-726876; Score: 0.37
DE  Interaction: Q9H2S6-2; IntAct: EBI-849893,EBI-12003398; Score: 0.56
DE  Interaction: P60520; IntAct: EBI-849893,EBI-720116; Score: 0.56
DE  Interaction: Q9H0R8; IntAct: EBI-849893,EBI-746969; Score: 0.56
DE  Interaction: O43169; IntAct: EBI-849893,EBI-1058710; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-849893,EBI-10313040; Score: 0.56
DE  Interaction: Q9BXN2-6; IntAct: EBI-11989440,EBI-849893; Score: 0.56
DE  Interaction: P38182; IntAct: EBI-849893,EBI-2684; Score: 0.67
DE  Interaction: Q15848; IntAct: EBI-849893,EBI-10827839; Score: 0.56
DE  Interaction: Q9Y4P8; IntAct: EBI-719396,EBI-849893; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-849893,EBI-700771; Score: 0.44
DE  Interaction: P10415; IntAct: EBI-77694,EBI-849893; Score: 0.44
DE  Interaction: P03247; IntAct: EBI-849856,EBI-849893; Score: 0.65
DE  Interaction: Q9P104; IntAct: EBI-739600,EBI-849893; Score: 0.37
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031224;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0071456;
GO  GO:0051607;
GO  GO:0097345;
GO  GO:0035694;
GO  GO:0043066;
GO  GO:0060548;
GO  GO:0010917;
GO  GO:0043065;
GO  GO:0016239;
GO  GO:0042981;
GO  GO:1903146;
GO  GO:0043067;
GO  GO:1903214;
GO  GO:0016032;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQH
SQ  ESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRH
SQ  PKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
//
ID  P16278;
PN  Beta-galactosidase;
GN  GLB1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Lysosome {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:3084261}. [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:2511208}. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes. {ECO:0000269|PubMed:2511208}.
DR  UNIPROT: P16278;
DR  UNIPROT: B2R7H8;
DR  UNIPROT: B7Z6B0;
DR  UNIPROT: P16279;
DR  PDB: 3THC;
DR  PDB: 3THD;
DR  PDB: 3WEZ;
DR  PDB: 3WF0;
DR  PDB: 3WF1;
DR  PDB: 3WF2;
DR  PDB: 3WF3;
DR  PDB: 3WF4;
DR  Pfam: PF13364;
DR  Pfam: PF01301;
DR  PROSITE: PS01182;
DR  OMIM: 230500;
DR  OMIM: 230600;
DR  OMIM: 230650;
DR  OMIM: 253010;
DR  OMIM: 611458;
DR  DisGeNET: 2720;
DE  Function: [Isoform 1]: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8200356}. [Isoform 2]: Has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers. {ECO:0000269|PubMed:10841810, ECO:0000269|PubMed:8922281}.
DE  Disease: GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. {ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238, ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816, ECO:0000269|Ref.28, ECO:0000269|Ref.31}. Note=The disease is caused by mutations affecting the gene represented in this entry. GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:12644936, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816}. Note=The disease is caused by mutations affecting the gene represented in this entry. GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8198123, ECO:0000269|Ref.28, ECO:0000269|Ref.30}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02866; IntAct: EBI-2905940,EBI-989638; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-494830,EBI-989638; Score: 0.35
DE  Interaction: P01100; IntAct: EBI-852851,EBI-989638; Score: 0.37
DE  Interaction: P62699; IntAct: EBI-11721624,EBI-989638; Score: 0.51
DE  Interaction: P08670; IntAct: EBI-353844,EBI-989638; Score: 0.51
DE  Interaction: Q9NQH7; IntAct: EBI-989638,EBI-1171467; Score: 0.27
DE  Interaction: P10619; IntAct: EBI-989638,EBI-989654; Score: 0.27
DE  Interaction: Q8NBJ4; IntAct: EBI-712073,EBI-989638; Score: 0.56
DE  Interaction: P04985; IntAct: EBI-989582,EBI-989638; Score: 0.35
DE  Interaction: Q99519; IntAct: EBI-721517,EBI-989638; Score: 0.37
DE  Interaction: Q9NSA3; IntAct: EBI-989638,EBI-747082; Score: 0.40
DE  Interaction: P30825; IntAct: EBI-4289564,EBI-989638; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-18159983,EBI-989638; Score: 0.56
DE  Interaction: Q9BRI3; IntAct: EBI-8644112,EBI-989638; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-989638; Score: 0.35
GO  GO:0035578;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0043202;
GO  GO:0048471;
GO  GO:0005773;
GO  GO:0004565;
GO  GO:0016936;
GO  GO:0042803;
GO  GO:0044262;
GO  GO:0019388;
GO  GO:0006027;
GO  GO:0006687;
GO  GO:0042340;
GO  GO:0043312;
GO  GO:0051413;
GO  GO:1904016;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAI
SQ  QTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDK
SQ  WLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTV
SQ  DFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGA
SQ  NSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKS
SQ  LYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENM
SQ  GRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPS
SQ  GIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVD
SQ  RPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV
//
ID  Q9N3Z3;
PN  Serine/threonine-protein kinase chk-1;
GN  chk;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:26073019}. Nucleus {ECO:0000250|UniProtKB:O61661}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26073019}. Note=The Ser-344 phosphorylated form colocalizes with P granules in a perinuclear manner in embryonic germline precursor cells and in Z2/Z3 primordial germ cells in L1 stage larvae. {ECO:0000269|PubMed:26073019}.
DR  UNIPROT: Q9N3Z3;
DR  UNIPROT: Q17375;
DR  UNIPROT: Q86FM7;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:15326393). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:15326393). Required for checkpoint mediated cell cycle arrest in response to DNA damage in germline cells (PubMed:15326393, PubMed:27956467). Delays cell-cycle reentry of the Z2 and Z3 primordial germ cells in response to transcription-induced DNA damage as they emerge from cell cycle arrest in L1 larvae (PubMed:26073019). Essential for embryogenesis (PubMed:15326393). {ECO:0000269|PubMed:15326393, ECO:0000269|PubMed:26073019, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004674;
GO  GO:0000077;
GO  GO:0009792;
GO  GO:0035556;
GO  GO:0033314;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAASTTSTPAAAAVAPQQPESLYRVVQTLGEGAFGEVLLIVNTKNPEVAAAMKKINIANKSKDFIDNIRKEYLLQKRVS
SQ  AVGHDNVIRMIGMRNDPQFYYLFLEYADGGELFDKIEPDCGMSPVFAQFYFKQLICGLKFIHDNDVVHRDIKPENLLLTG
SQ  THVLKISDFGMATLYRNKGEERLLDLSCGTIPYAAPELCAGKKYRGPPVDVWSSGIVLIAMLTGELPWDRASDASQSYMG
SQ  WISNTSLDERPWKKIDVRALCMLRKIVTDKTDKRATIEQIQADPWYQHNFGQVETPNGRPLKRARNNDENITCTQQAECS
SQ  AKRRHLETPNEKSTLAERQNASFSQPTKTEDLLLTQHIDMSQTNSNLLQRMVCRMTRFCVVTDIRSTYQKVARASEHAGF
SQ  GVRETDDYRLLVTWREVSMMVSLYTMGDIPDKPRVMVDFRRSRGDGIQFKKMFMDVRNRMHEWICTDGNNWLANLGYVPR
SQ  NPQIVNGGGVNVEHSASSINVDV
//
ID  O35864;
PN  COP9 signalosome complex subunit 5;
GN  Cops5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10721695}. Nucleus {ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000250|UniProtKB:Q92905}.
DR  UNIPROT: O35864;
DR  UNIPROT: Q3UA70;
DR  UNIPROT: Q8C1S1;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. {ECO:0000250|UniProtKB:Q92905}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0000785;
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0005667;
GO  GO:0019899;
GO  GO:0035718;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0008237;
GO  GO:0019784;
GO  GO:0004843;
GO  GO:0003713;
GO  GO:1990182;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0045944;
GO  GO:0000338;
GO  GO:0016579;
GO  GO:0051726;
GO  GO:1903894;
GO  GO:0046328;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGL
SQ  MLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQ
SQ  FQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLEL
SQ  LWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS
SQ  QVIKDKLFNQINVA
//
ID  P50613;
PN  Cyclin-dependent kinase 7;
GN  CDK7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides.
DR  UNIPROT: P50613;
DR  UNIPROT: Q9BS60;
DR  UNIPROT: Q9UE19;
DR  PDB: 1LG3;
DR  PDB: 1PA8;
DR  PDB: 1UA2;
DR  PDB: 2HIC;
DR  PDB: 6O9L;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 601955;
DR  DisGeNET: 1022;
DE  Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C- terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261, ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234, ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461, ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:9372954, ECO:0000269|PubMed:9840937}.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-1245958,EBI-357515; Score: 0.35
DE  Interaction: P12270; IntAct: EBI-1245958,EBI-1048528; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-714559,EBI-1245958; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-1245958,EBI-295634; Score: 0.46
DE  Interaction: Q14684; IntAct: EBI-1245958,EBI-372051; Score: 0.35
DE  Interaction: Q14241; IntAct: EBI-1245958,EBI-742350; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-1245958,EBI-6380459; Score: 0.60
DE  Interaction: Q13888; IntAct: EBI-1245958,EBI-1565170; Score: 0.69
DE  Interaction: Q13823; IntAct: EBI-1245958,EBI-1043365; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-1245958,EBI-1050630; Score: 0.35
DE  Interaction: Q13011; IntAct: EBI-1245958,EBI-711968; Score: 0.35
DE  Interaction: P55199; IntAct: EBI-1245958,EBI-1245868; Score: 0.35
DE  Interaction: P51948; IntAct: EBI-1245958,EBI-716139; Score: 0.78
DE  Interaction: P51946; IntAct: EBI-1245958,EBI-741406; Score: 0.86
DE  Interaction: P46013; IntAct: EBI-1245958,EBI-876367; Score: 0.35
DE  Interaction: P32780; IntAct: EBI-1245958,EBI-715539; Score: 0.71
DE  Interaction: P29083; IntAct: EBI-1245958,EBI-5462215; Score: 0.35
DE  Interaction: P28715; IntAct: EBI-1245958,EBI-765885; Score: 0.60
DE  Interaction: P21127; IntAct: EBI-1245958,EBI-1298; Score: 0.35
DE  Interaction: P19447; IntAct: EBI-1245958,EBI-1183307; Score: 0.69
DE  Interaction: P18074; IntAct: EBI-1245958,EBI-6380590; Score: 0.69
DE  Interaction: O75683; IntAct: EBI-1245958,EBI-2691252; Score: 0.35
DE  Interaction: O00541; IntAct: EBI-1245958,EBI-1053271; Score: 0.35
DE  Interaction: Q9Y5Q9; IntAct: EBI-1245958,EBI-1054873; Score: 0.35
DE  Interaction: Q9Y5Q8; IntAct: EBI-1245958,EBI-1045409; Score: 0.35
DE  Interaction: Q9Y4W2; IntAct: EBI-1245958,EBI-1051591; Score: 0.35
DE  Interaction: Q9Y2X9; IntAct: EBI-1245958,EBI-396200; Score: 0.35
DE  Interaction: Q9Y2G7; IntAct: EBI-1245958,EBI-16770406; Score: 0.35
DE  Interaction: Q9H9Y6; IntAct: EBI-1245958,EBI-355441; Score: 0.35
DE  Interaction: Q9H9B1; IntAct: EBI-1245958,EBI-766087; Score: 0.35
DE  Interaction: Q9BYE7; IntAct: EBI-1245958,EBI-1048026; Score: 0.35
DE  Interaction: Q9BTC8; IntAct: EBI-1245958,EBI-2461787; Score: 0.35
DE  Interaction: Q8IWI9; IntAct: EBI-1245958,EBI-2815196; Score: 0.35
DE  Interaction: Q6P1X5; IntAct: EBI-1245958,EBI-1560063; Score: 0.35
DE  Interaction: Q5UIP0; IntAct: EBI-1245958,EBI-711331; Score: 0.35
DE  Interaction: Q15542; IntAct: EBI-1245958,EBI-1560145; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-1245958,EBI-2514399; Score: 0.35
DE  Interaction: Q12789; IntAct: EBI-1245958,EBI-357956; Score: 0.35
DE  Interaction: P62891; IntAct: EBI-1245958,EBI-8830744; Score: 0.35
DE  Interaction: P49848; IntAct: EBI-1245958,EBI-1560206; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-1245958,EBI-726050; Score: 0.35
DE  Interaction: P38432; IntAct: EBI-1245958,EBI-945751; Score: 0.35
DE  Interaction: P29084; IntAct: EBI-1245958,EBI-2853321; Score: 0.35
DE  Interaction: P21675; IntAct: EBI-1245958,EBI-491289; Score: 0.35
DE  Interaction: O95602; IntAct: EBI-1245958,EBI-359472; Score: 0.35
DE  Interaction: O00268; IntAct: EBI-1245958,EBI-1034261; Score: 0.35
DE  Interaction: Q9NXF1; IntAct: EBI-1245958,EBI-2371062; Score: 0.35
DE  Interaction: Q96PZ0; IntAct: EBI-1245958,EBI-1052964; Score: 0.35
DE  Interaction: Q8WUA4; IntAct: EBI-1245958,EBI-1237062; Score: 0.35
DE  Interaction: Q7Z4V5; IntAct: EBI-1245958,EBI-1049136; Score: 0.35
DE  Interaction: O15355; IntAct: EBI-1245958,EBI-725702; Score: 0.35
DE  Interaction: Q13042; IntAct: EBI-1245958,EBI-994830; Score: 0.35
DE  Interaction: Q8N1G0; IntAct: EBI-1245958,EBI-1210558; Score: 0.35
DE  Interaction: P30260; IntAct: EBI-1245958,EBI-994813; Score: 0.35
DE  Interaction: Q96ME7; IntAct: EBI-1245958,EBI-10986895; Score: 0.35
DE  Interaction: Q8TDI0; IntAct: EBI-1245958,EBI-1042816; Score: 0.35
DE  Interaction: Q7Z5K2; IntAct: EBI-1245958,EBI-1022242; Score: 0.35
DE  Interaction: Q9NW82; IntAct: EBI-1245958,EBI-2515581; Score: 0.35
DE  Interaction: Q9Y3C7; IntAct: EBI-1245958,EBI-394707; Score: 0.35
DE  Interaction: Q9Y2R4; IntAct: EBI-1245958,EBI-395458; Score: 0.35
DE  Interaction: Q9UK58; IntAct: EBI-1245958,EBI-2836773; Score: 0.35
DE  Interaction: Q9NY93; IntAct: EBI-1245958,EBI-372376; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-1245958,EBI-713507; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-1245958,EBI-2878099; Score: 0.35
DE  Interaction: Q9NVC6; IntAct: EBI-1245958,EBI-394562; Score: 0.35
DE  Interaction: Q9H0A0; IntAct: EBI-1245958,EBI-876527; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-1245958,EBI-1056249; Score: 0.35
DE  Interaction: Q96S94; IntAct: EBI-1245958,EBI-1045974; Score: 0.35
DE  Interaction: Q92759; IntAct: EBI-1245958,EBI-6380495; Score: 0.60
DE  Interaction: Q92621; IntAct: EBI-1245958,EBI-1045046; Score: 0.35
DE  Interaction: Q8TF01; IntAct: EBI-1245958,EBI-3437793; Score: 0.35
DE  Interaction: Q8IY81; IntAct: EBI-1245958,EBI-744088; Score: 0.35
DE  Interaction: Q8IX01; IntAct: EBI-1245958,EBI-949116; Score: 0.35
DE  Interaction: Q6ZYL4; IntAct: EBI-1245958,EBI-6380438; Score: 0.69
DE  Interaction: Q6PD62; IntAct: EBI-1245958,EBI-1019583; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1245958; Score: 0.35
DE  Interaction: Q01094; IntAct: EBI-448924,EBI-1245958; Score: 0.40
DE  Interaction: A0A0H2W2U3; IntAct: EBI-2845132,EBI-1245958; Score: 0.37
DE  Interaction: P51659; IntAct: EBI-1245958,EBI-358398; Score: 0.37
DE  Interaction: P01909; IntAct: EBI-1245958,EBI-713389; Score: 0.37
DE  Interaction: P15927; IntAct: EBI-1245958,EBI-621404; Score: 0.35
DE  Interaction: P56270; IntAct: EBI-1245958,EBI-1809742; Score: 0.35
DE  Interaction: P0DMV8; IntAct: EBI-1245958,EBI-11052499; Score: 0.35
DE  Interaction: Q7Z739; IntAct: EBI-1245958,EBI-2849837; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-1245958,EBI-2880718; Score: 0.35
DE  Interaction: P62633; IntAct: EBI-1245958,EBI-1047529; Score: 0.35
DE  Interaction: O15235; IntAct: EBI-1245958,EBI-712205; Score: 0.35
DE  Interaction: Q6P1K8; IntAct: EBI-8469755,EBI-1245958; Score: 0.35
DE  Interaction: P14635; IntAct: EBI-1245958,EBI-495332; Score: 0.35
DE  Interaction: Q58FG0; IntAct: EBI-1245958,EBI-11323222; Score: 0.35
DE  Interaction: Q9UBF8-2; IntAct: EBI-1245958,EBI-16107849; Score: 0.35
DE  Interaction: Q96NH3-4; IntAct: EBI-1245958,EBI-21548859; Score: 0.35
DE  Interaction: Q8IZL9; IntAct: EBI-1245958,EBI-6128565; Score: 0.35
DE  Interaction: Q58FG1; IntAct: EBI-1245958,EBI-6916562; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-1245958,EBI-9996483; Score: 0.35
DE  Interaction: Q58FF6; IntAct: EBI-1245958,EBI-6916503; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-1245958,EBI-306914; Score: 0.35
DE  Interaction: Q13137; IntAct: EBI-1245958,EBI-739580; Score: 0.35
DE  Interaction: P46527; IntAct: EBI-1245958,EBI-519280; Score: 0.35
DE  Interaction: P24864; IntAct: EBI-1245958,EBI-519526; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-1245958,EBI-457097; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-1245958,EBI-352572; Score: 0.56
DE  Interaction: P07900-2; IntAct: EBI-1245958,EBI-6190772; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-375096,EBI-1245958; Score: 0.71
DE  Interaction: P01023; IntAct: EBI-1245958,EBI-640741; Score: 0.35
DE  Interaction: P48740; IntAct: EBI-1245958,EBI-6380536; Score: 0.35
DE  Interaction: P23634; IntAct: EBI-1245958,EBI-1174388; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-593303,EBI-1245958; Score: 0.44
DE  Interaction: Q96SB4; IntAct: EBI-539478,EBI-1245958; Score: 0.44
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-1245958; Score: 0.40
DE  Interaction: O96006; IntAct: EBI-740037,EBI-1245958; Score: 0.35
GO  GO:0019907;
GO  GO:0005737;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005675;
GO  GO:0070985;
GO  GO:0050681;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0008094;
GO  GO:0016301;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0008353;
GO  GO:0003713;
GO  GO:0006370;
GO  GO:0030521;
GO  GO:0007050;
GO  GO:0051301;
GO  GO:0000082;
GO  GO:0000086;
GO  GO:0006294;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0000079;
GO  GO:0042795;
GO  GO:0006363;
GO  GO:0006366;
GO  GO:0006362;
GO  GO:0006368;
GO  GO:0006361;
GO  GO:0006367;
GO  GO:0006283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDA
SQ  FGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAK
SQ  SFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDM
SQ  CSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQ
SQ  SNPALAIKRKRTEALEQGGLPKKLIF
//
ID  Q07912;
PN  Activated CDC42 kinase 1;
GN  TNK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane. Nucleus. Endosome. Cell junction, adherens junction {ECO:0000250}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Membrane, clathrin-coated pit. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20110370}. Note=The Tyr-284 phosphorylated form is found both in the membrane and nucleus. Colocalizes with EGFR on endosomes. Nuclear translocation is CDC42- dependent.
DR  UNIPROT: Q07912;
DR  UNIPROT: Q6ZMQ0;
DR  UNIPROT: Q8N6U7;
DR  UNIPROT: Q96H59;
DR  PDB: 1CF4;
DR  PDB: 1U46;
DR  PDB: 1U4D;
DR  PDB: 1U54;
DR  PDB: 3EQP;
DR  PDB: 3EQR;
DR  PDB: 4EWH;
DR  PDB: 4HZR;
DR  PDB: 4HZS;
DR  PDB: 4ID7;
DR  PDB: 5ZXB;
DR  Pfam: PF09027;
DR  Pfam: PF11555;
DR  Pfam: PF07714;
DR  Pfam: PF14604;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50002;
DR  OMIM: 606994;
DR  DisGeNET: 10188;
DE  Function: Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. Phosphorylates WASP (PubMed:20110370). {ECO:0000269|PubMed:10652228, ECO:0000269|PubMed:11278436, ECO:0000269|PubMed:16247015, ECO:0000269|PubMed:16257963, ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:18262180, ECO:0000269|PubMed:18435854, ECO:0000269|PubMed:19815557, ECO:0000269|PubMed:20110370, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20383201}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-714707,EBI-603457; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-297353,EBI-603457; Score: 0.35
DE  Interaction: Self; IntAct: EBI-603457,EBI-603457; Score: 0.59
DE  Interaction: Q12913; IntAct: EBI-2264500,EBI-603457; Score: 0.44
DE  Interaction: Q05209; IntAct: EBI-603457,EBI-2266035; Score: 0.44
DE  Interaction: P08575; IntAct: EBI-1341,EBI-603457; Score: 0.44
DE  Interaction: P60953-1; IntAct: EBI-3625591,EBI-603457; Score: 0.37
DE  Interaction: Q96JZ2; IntAct: EBI-3919324,EBI-603457; Score: 0.37
DE  Interaction: Q8WXH5; IntAct: EBI-603457,EBI-3942425; Score: 0.49
DE  Interaction: Q9HC98; IntAct: EBI-603457,EBI-740364; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-745213,EBI-603457; Score: 0.56
DE  Interaction: O60880; IntAct: EBI-6983382,EBI-603457; Score: 0.56
DE  Interaction: P07902; IntAct: EBI-750827,EBI-603457; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-945833,EBI-603457; Score: 0.56
DE  Interaction: P60953; IntAct: EBI-81752,EBI-603457; Score: 0.37
DE  Interaction: P62993; IntAct: EBI-603457,EBI-401755; Score: 0.66
DE  Interaction: P16333; IntAct: EBI-389883,EBI-603457; Score: 0.59
DE  Interaction: G3X972; IntAct: EBI-11079353,EBI-603457; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-603457; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-354967,EBI-603457; Score: 0.70
DE  Interaction: O95817; IntAct: EBI-747185,EBI-603457; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-603457,EBI-352572; Score: 0.56
DE  Interaction: Q8IUQ4; IntAct: EBI-603457,EBI-747107; Score: 0.37
DE  Interaction: P85968; IntAct: EBI-603457,EBI-22237670; Score: 0.35
DE  Interaction: G3V7X3; IntAct: EBI-603457,EBI-22085594; Score: 0.35
DE  Interaction: D4A3M8; IntAct: EBI-603457,EBI-21231408; Score: 0.35
DE  Interaction: P97573; IntAct: EBI-603457,EBI-8008869; Score: 0.35
DE  Interaction: O35244; IntAct: EBI-603457,EBI-915490; Score: 0.35
DE  Interaction: Q7Z7F7; IntAct: EBI-603457,EBI-7825445; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-603457,EBI-296047; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-603457,EBI-9996483; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-603457,EBI-352528; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-603457,EBI-356553; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-603457,EBI-356687; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-603457,EBI-355710; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-603457,EBI-356876; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-603457,EBI-357407; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-603457,EBI-295634; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-603457,EBI-355133; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-603457,EBI-356673; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-603457,EBI-359097; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-603457,EBI-356507; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-603457,EBI-2961708; Score: 0.35
DE  Interaction: P60953-2; IntAct: EBI-603457,EBI-287394; Score: 0.59
GO  GO:0005912;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0097268;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005768;
GO  GO:0031234;
GO  GO:0070436;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0005154;
GO  GO:0005095;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0004713;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0050699;
GO  GO:0030154;
GO  GO:0007166;
GO  GO:0006897;
GO  GO:0038083;
GO  GO:0016310;
GO  GO:0050731;
GO  GO:0042127;
GO  GO:2000369;
GO  GO:0007264;
GO  GO:0007169;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVF
SQ  SGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCL
SQ  KPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGM
SQ  GYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTL
SQ  WEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFE
SQ  EPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPD
SQ  RIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKA
SQ  SRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQ
SQ  DEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQA
SQ  PAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGS
SQ  SPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQ
SQ  SPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPAD
SQ  KIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR
//
ID  P20749;
PN  B-cell lymphoma 3 protein;
GN  BCL3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Ubiquitination via 'Lys-63'- linked ubiquitin chains is required for nuclear accumulation. {ECO:0000250}.
DR  UNIPROT: P20749;
DR  PDB: 1K1A;
DR  PDB: 1K1B;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  OMIM: 109560;
DR  DisGeNET: 602;
DE  Function: Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity). {ECO:0000250, ECO:0000269|PubMed:8453667}.
DE  Disease: Note=A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions. {ECO:0000269|PubMed:2180580, ECO:0000269|PubMed:7896265}.
DE  Reference Proteome: Yes;
DE  Interaction: O95999; IntAct: EBI-958922,EBI-958997; Score: 0.52
DE  Interaction: Q92598; IntAct: EBI-958997,EBI-356829; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-958997,EBI-307326; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-958997,EBI-300010; Score: 0.35
DE  Interaction: P17066; IntAct: EBI-958997,EBI-355106; Score: 0.35
DE  Interaction: O15084; IntAct: EBI-359567,EBI-958997; Score: 0.37
DE  Interaction: P56545; IntAct: EBI-741533,EBI-958997; Score: 0.51
GO  GO:0032996;
GO  GO:0033257;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0030496;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0003700;
GO  GO:0030674;
GO  GO:0000978;
GO  GO:0008134;
GO  GO:0019730;
GO  GO:0006974;
GO  GO:0042742;
GO  GO:0042832;
GO  GO:0030330;
GO  GO:0030198;
GO  GO:0002268;
GO  GO:0002467;
GO  GO:0002455;
GO  GO:0007249;
GO  GO:0042771;
GO  GO:0051457;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0045415;
GO  GO:0046426;
GO  GO:0045892;
GO  GO:0042536;
GO  GO:0032729;
GO  GO:0045082;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0045727;
GO  GO:0042981;
GO  GO:0051101;
GO  GO:1901222;
GO  GO:0010225;
GO  GO:0009615;
GO  GO:0048536;
GO  GO:0042088;
GO  GO:0045064;
GO  GO:0006351;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRCPAGAMDEGPVDLRTRPKAAGLPGAALPLRKRPLRAPSPEPAAPRGAAGLVVPLDPLRGGCDLPAVPGPPHGLARPE
SQ  ALYYPGALLPLYPTRAMGSPFPLVNLPTPLYPMMCPMEHPLSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQ
SQ  GGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPGTLDLEARNY
SQ  DGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRG
SQ  LLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPASTSQPDPSPDRSANTSPESSSRLSSNGLLSASPS
SQ  SSPSQSPPRDPPGFPMAPPNFFLPSPSPPAFLPFAGVLRGPGRPVPPSPAPGGS
//
ID  Q96A70;
PN  Antizyme inhibitor 2;
GN  AZIN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region. Membrane {ECO:0000250}. Cytoplasmic vesicle. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-Golgi network. Cytoplasmic granule. Cell projection, axon. Cell projection, dendrite. Perikaryon. Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in an antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}.
DR  UNIPROT: Q96A70;
DR  UNIPROT: B2RDU5;
DR  UNIPROT: D3DPQ9;
DR  UNIPROT: Q5TIF4;
DR  UNIPROT: Q5TIF5;
DR  UNIPROT: Q5TIF6;
DR  UNIPROT: Q8TF56;
DR  UNIPROT: Q96L54;
DR  UNIPROT: Q96L55;
DR  UNIPROT: Q96L56;
DR  UNIPROT: Q96L57;
DR  UNIPROT: Q96MD9;
DR  Pfam: PF02784;
DR  Pfam: PF00278;
DR  PROSITE: PS00878;
DR  PROSITE: PS00879;
DR  OMIM: 608353;
DR  DisGeNET: 113451;
DE  Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:17900240). Inhibits antizyme- dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:17900240). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (PubMed:20188728). {ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:20188728}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UMX2; IntAct: EBI-10281601,EBI-10281609; Score: 0.56
DE  Interaction: Q9UMX2-2; IntAct: EBI-12049527,EBI-10281609; Score: 0.56
DE  Interaction: Q9NZC9; IntAct: EBI-10281609,EBI-5457961; Score: 0.35
DE  Interaction: Q96FC9-2; IntAct: EBI-10281609,EBI-21510470; Score: 0.35
DE  Interaction: Q8ND04-2; IntAct: EBI-10281609,EBI-21539621; Score: 0.35
DE  Interaction: Q5T3J3; IntAct: EBI-10281609,EBI-473196; Score: 0.35
DE  Interaction: Q16890-2; IntAct: EBI-10281609,EBI-18777952; Score: 0.35
DE  Interaction: P78395; IntAct: EBI-10281609,EBI-348325; Score: 0.35
DE  Interaction: P57737-2; IntAct: EBI-10281609,EBI-21546130; Score: 0.35
DE  Interaction: P54368; IntAct: EBI-10281609,EBI-948441; Score: 0.35
DE  Interaction: O95190; IntAct: EBI-10281609,EBI-1051861; Score: 0.35
GO  GO:0030424;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033116;
GO  GO:1990005;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030133;
GO  GO:0008792;
GO  GO:0042978;
GO  GO:0097055;
GO  GO:0042177;
GO  GO:0043085;
GO  GO:1902269;
GO  GO:0033387;
GO  GO:0007283;
GO  GO:0098629;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKV
SQ  LAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDD
SQ  SHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
SQ  GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREEENGSTSKTIVYHLD
SQ  EGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWG
SQ  TQACHITYAMSRVAWEALRRQLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
//
ID  O89039;
PN  Atypical chemokine receptor 3;
GN  Ackr3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21655198}; Multi-pass membrane protein {ECO:0000269|PubMed:21655198}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21655198}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin -dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: O89039;
DR  UNIPROT: Q9JLZ0;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein- mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. {ECO:0000269|PubMed:20018651}.
DE  Reference Proteome: Yes;
DE  Interaction: P30560; IntAct: EBI-21299265,EBI-21299313; Score: 0.40
DE  Interaction: O08565; IntAct: EBI-21299265,EBI-11167786; Score: 0.59
GO  GO:0005623;
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0005768;
GO  GO:0009897;
GO  GO:0016021;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0019957;
GO  GO:0016493;
GO  GO:0019958;
GO  GO:0016494;
GO  GO:0019956;
GO  GO:0015026;
GO  GO:0005044;
GO  GO:0001525;
GO  GO:0019722;
GO  GO:0007155;
GO  GO:0060326;
GO  GO:0070098;
GO  GO:0006935;
GO  GO:0006955;
GO  GO:1902230;
GO  GO:0007204;
GO  GO:0070374;
GO  GO:1905322;
GO  GO:0031623;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVHLFDYVEPGNYSDINWPCNSSDCIVVDTVQCPAMPNKNVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTH
SQ  CYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLACMSVDRYLSITYFTSTSSYKKKMV
SQ  RRVVCVLVWLLAFFVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMS
SQ  ASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVTQCLSLVHCCVNPVLYSFINR
SQ  NYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQNTK
//
ID  P54259;
PN  Atrophin-1;
GN  ATN1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Cell junction {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell- cell junctions and leading edges of cells (By similarity). Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Gln (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles. {ECO:0000250}.
DR  UNIPROT: P54259;
DR  UNIPROT: Q99495;
DR  UNIPROT: Q99621;
DR  UNIPROT: Q9UEK7;
DR  Pfam: PF03154;
DR  OMIM: 125370;
DR  OMIM: 607462;
DR  OMIM: 618494;
DR  DisGeNET: 1822;
DE  Function: Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats. {ECO:0000250|UniProtKB:O35126, ECO:0000269|PubMed:10085113, ECO:0000269|PubMed:10973986}.
DE  Disease: Dentatorubral-pallidoluysian atrophy (DRPLA) [MIM:125370]: Autosomal dominant neurodegenerative disorder characterized by a loss of neurons in the dentate nucleus, rubrum, glogus pallidus and Luys'body. Clinical features are myoclonus epilepsy, dementia, and cerebellar ataxia. Onset of the disease occurs usually in the second decade of life and death in the fourth. {ECO:0000269|PubMed:7842016, ECO:0000269|PubMed:8136840}. Note=The disease is caused by mutations affecting the gene represented in this entry. Congenital hypotonia, epilepsy, developmental delay, and digital anomalies (CHEDDA) [MIM:618494]: An autosomal dominant neurodevelopmental syndrome characterized by severe global developmental delay, impaired intellectual development, poor or absent language, significant motor disability with inability to walk, dysmorphic facial features, skeletal anomalies, and variable congenital malformations. Most patients also have seizures and structural brain abnormalities. {ECO:0000269|PubMed:30827498}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-740019,EBI-945980; Score: 0.49
DE  Interaction: Self; IntAct: EBI-945980,EBI-945980; Score: 0.37
DE  Interaction: Q9P2R6; IntAct: EBI-945980,EBI-948076; Score: 0.37
DE  Interaction: Q9HAU0; IntAct: EBI-945934,EBI-945980; Score: 0.51
DE  Interaction: Q15654; IntAct: EBI-742327,EBI-945980; Score: 0.51
DE  Interaction: Q9NWB1; IntAct: EBI-945980,EBI-945906; Score: 0.51
DE  Interaction: Q9UQB8; IntAct: EBI-945980,EBI-525456; Score: 0.63
DE  Interaction: Q06455; IntAct: EBI-945980,EBI-743342; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-945980,EBI-739737; Score: 0.49
DE  Interaction: Q96CN9; IntAct: EBI-945980,EBI-746252; Score: 0.37
DE  Interaction: Q96PV6; IntAct: EBI-739546,EBI-945980; Score: 0.37
DE  Interaction: Q99750; IntAct: EBI-945980,EBI-724076; Score: 0.37
DE  Interaction: Q9BSW2; IntAct: EBI-945980,EBI-739773; Score: 0.37
DE  Interaction: O43639; IntAct: EBI-945980,EBI-713635; Score: 0.37
DE  Interaction: P61964; IntAct: EBI-945980,EBI-540834; Score: 0.66
DE  Interaction: O00308; IntAct: EBI-945980,EBI-743923; Score: 0.37
DE  Interaction: Q9BQ66; IntAct: EBI-739863,EBI-945980; Score: 0.37
DE  Interaction: P61289; IntAct: EBI-355546,EBI-945980; Score: 0.49
DE  Interaction: Q93062; IntAct: EBI-740322,EBI-945980; Score: 0.37
DE  Interaction: O00468; IntAct: EBI-947482,EBI-945980; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-347552,EBI-945980; Score: 0.37
DE  Interaction: Q02641; IntAct: EBI-947514,EBI-945980; Score: 0.37
DE  Interaction: O43439; IntAct: EBI-748628,EBI-945980; Score: 0.37
DE  Interaction: Q9HC77; IntAct: EBI-946194,EBI-945980; Score: 0.37
DE  Interaction: Q9H2X0; IntAct: EBI-947551,EBI-945980; Score: 0.37
DE  Interaction: P52943; IntAct: EBI-947590,EBI-945980; Score: 0.37
DE  Interaction: O14641; IntAct: EBI-740850,EBI-945980; Score: 0.37
DE  Interaction: Q12805; IntAct: EBI-536772,EBI-945980; Score: 0.37
DE  Interaction: O95967; IntAct: EBI-743414,EBI-945980; Score: 0.37
DE  Interaction: O75095; IntAct: EBI-947597,EBI-945980; Score: 0.37
DE  Interaction: Q7Z7M0; IntAct: EBI-947617,EBI-945980; Score: 0.37
DE  Interaction: P23142; IntAct: EBI-726652,EBI-945980; Score: 0.37
DE  Interaction: Q5ZEY4; IntAct: EBI-947655,EBI-945980; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-747754,EBI-945980; Score: 0.37
DE  Interaction: P98160; IntAct: EBI-947664,EBI-945980; Score: 0.37
DE  Interaction: Q9Y219; IntAct: EBI-946223,EBI-945980; Score: 0.37
DE  Interaction: O60290; IntAct: EBI-310635,EBI-945980; Score: 0.37
DE  Interaction: Q14766; IntAct: EBI-947693,EBI-945980; Score: 0.37
DE  Interaction: Q8N2S1; IntAct: EBI-947718,EBI-945980; Score: 0.37
DE  Interaction: P02686; IntAct: EBI-947410,EBI-945980; Score: 0.37
DE  Interaction: A6BM72; IntAct: EBI-947743,EBI-945980; Score: 0.37
DE  Interaction: Q92832; IntAct: EBI-947754,EBI-945980; Score: 0.37
DE  Interaction: Q99435; IntAct: EBI-946274,EBI-945980; Score: 0.37
DE  Interaction: O75420; IntAct: EBI-945980,EBI-947774; Score: 0.37
DE  Interaction: P17858; IntAct: EBI-487243,EBI-945980; Score: 0.37
DE  Interaction: Q96PM5; IntAct: EBI-947779,EBI-945980; Score: 0.37
DE  Interaction: O75093; IntAct: EBI-947791,EBI-945980; Score: 0.37
DE  Interaction: Q6ZWJ1; IntAct: EBI-947833,EBI-945980; Score: 0.37
DE  Interaction: Q86TM6; IntAct: EBI-947849,EBI-945980; Score: 0.37
DE  Interaction: Q99973; IntAct: EBI-947859,EBI-945980; Score: 0.37
DE  Interaction: Q9ULU4; IntAct: EBI-765834,EBI-945980; Score: 0.37
DE  Interaction: P98175; IntAct: EBI-721525,EBI-945980; Score: 0.37
DE  Interaction: Q9NP73; IntAct: EBI-947892,EBI-945980; Score: 0.37
DE  Interaction: Q9UBX5; IntAct: EBI-947897,EBI-945980; Score: 0.37
DE  Interaction: P98164; IntAct: EBI-947916,EBI-945980; Score: 0.37
DE  Interaction: Q92824; IntAct: EBI-945980,EBI-751290; Score: 0.37
DE  Interaction: P25788; IntAct: EBI-348380,EBI-945980; Score: 0.37
DE  Interaction: Q9H0M0; IntAct: EBI-742157,EBI-945980; Score: 0.37
DE  Interaction: Q08117; IntAct: EBI-717810,EBI-945980; Score: 0.37
DE  Interaction: P61204; IntAct: EBI-641535,EBI-945980; Score: 0.37
DE  Interaction: P48634; IntAct: EBI-347545,EBI-945980; Score: 0.37
DE  Interaction: Q9H9J5; IntAct: EBI-947238,EBI-945980; Score: 0.37
DE  Interaction: Q09013; IntAct: EBI-692774,EBI-945980; Score: 0.37
DE  Interaction: Q16610; IntAct: EBI-945980,EBI-947964; Score: 0.37
DE  Interaction: P98095; IntAct: EBI-947973,EBI-945980; Score: 0.37
DE  Interaction: Q3KQU3; IntAct: EBI-713229,EBI-945980; Score: 0.37
DE  Interaction: Q5JSZ5; IntAct: EBI-744891,EBI-945980; Score: 0.37
DE  Interaction: A7E2V4; IntAct: EBI-947995,EBI-945980; Score: 0.37
DE  Interaction: Q15323; IntAct: EBI-948001,EBI-945980; Score: 0.37
DE  Interaction: Q92794; IntAct: EBI-948013,EBI-945980; Score: 0.37
DE  Interaction: Q8WYB5; IntAct: EBI-948029,EBI-945980; Score: 0.37
DE  Interaction: O43251; IntAct: EBI-746056,EBI-945980; Score: 0.37
DE  Interaction: Q96EP0; IntAct: EBI-948111,EBI-945980; Score: 0.37
DE  Interaction: Q8IUQ4; IntAct: EBI-747107,EBI-945980; Score: 0.55
DE  Interaction: O43255; IntAct: EBI-948141,EBI-945980; Score: 0.37
DE  Interaction: Q96R06; IntAct: EBI-413317,EBI-945980; Score: 0.37
DE  Interaction: Q9Y4B4; IntAct: EBI-948156,EBI-945980; Score: 0.37
DE  Interaction: Q70EL1; IntAct: EBI-946185,EBI-945980; Score: 0.37
DE  Interaction: A0A384KST0; IntAct: EBI-2845592,EBI-945980; Score: 0.37
DE  Interaction: A0A2S9PJQ7; IntAct: EBI-2846239,EBI-945980; Score: 0.37
DE  Interaction: A0A384LHY7; IntAct: EBI-2850412,EBI-945980; Score: 0.37
DE  Interaction: Q8ZA76; IntAct: EBI-945980,EBI-2846943; Score: 0.37
DE  Interaction: A0A1Q4M0N4; IntAct: EBI-945980,EBI-2817814; Score: 0.37
DE  Interaction: A0A0F7R9Q0; IntAct: EBI-945980,EBI-2815990; Score: 0.37
DE  Interaction: A0A384LQ43; IntAct: EBI-2848562,EBI-945980; Score: 0.37
DE  Interaction: O75081; IntAct: EBI-1190217,EBI-945980; Score: 0.37
DE  Interaction: Q14457; IntAct: EBI-949378,EBI-945980; Score: 0.35
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0019904;
GO  GO:0001085;
GO  GO:0003714;
GO  GO:0007417;
GO  GO:0000122;
GO  GO:0051402;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESE
SQ  SEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYH
SQ  PPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGA
SQ  ASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGL
SQ  GAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFP
SQ  ASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHH
SQ  HHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQ
SQ  AGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYG
SQ  KRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPP
SQ  LSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLV
SQ  EKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDT
SQ  PALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPL
SQ  HGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLA
SQ  RLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFA
SQ  APYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
//
ID  Q8IWQ3;
PN  Serine/threonine-protein kinase BRSK2;
GN  BRSK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.
DR  UNIPROT: Q8IWQ3;
DR  UNIPROT: B3KVE9;
DR  UNIPROT: E9PLM7;
DR  UNIPROT: O60843;
DR  UNIPROT: O95099;
DR  UNIPROT: Q5J5B4;
DR  UNIPROT: Q6ZMQ4;
DR  UNIPROT: Q8TB60;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 609236;
DR  DisGeNET: 9024;
DE  Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr- 174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8WVZ9; IntAct: EBI-473695,EBI-3232062; Score: 0.40
DE  Interaction: Q99PL5; IntAct: EBI-8361659,EBI-3232062; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0150034;
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0060590;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0004674;
GO  GO:0048156;
GO  GO:0050321;
GO  GO:0031532;
GO  GO:0007409;
GO  GO:0051301;
GO  GO:0036503;
GO  GO:0030010;
GO  GO:0006887;
GO  GO:0000086;
GO  GO:0035556;
GO  GO:0070059;
GO  GO:0090176;
GO  GO:0030182;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0043462;
GO  GO:0050770;
GO  GO:0061178;
GO  GO:0010975;
GO  GO:1904152;
GO  GO:2000807;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLK
SQ  LHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADF
SQ  GMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIP
SQ  PDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQ
SQ  DLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRA
SQ  IEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLN
SQ  SIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSL
SQ  SHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPP
SQ  AAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTG
SQ  KDTAKMGPPTARREQP
//
ID  O75140;
PN  GATOR complex protein DEPDC5;
GN  DEPDC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61460}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61460}. Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000269|PubMed:28199306}.
DR  UNIPROT: O75140;
DR  UNIPROT: A6H8V6;
DR  UNIPROT: A8MPX9;
DR  UNIPROT: B4DH93;
DR  UNIPROT: B9EGN9;
DR  UNIPROT: Q5K3V5;
DR  UNIPROT: Q5THY9;
DR  UNIPROT: Q5THZ0;
DR  UNIPROT: Q5THZ1;
DR  UNIPROT: Q5THZ3;
DR  UNIPROT: Q68DR1;
DR  UNIPROT: Q6MZX3;
DR  UNIPROT: Q6PEZ1;
DR  UNIPROT: Q9UGV8;
DR  UNIPROT: Q9UH13;
DR  PDB: 6CES;
DR  PDB: 6CET;
DR  Pfam: PF00610;
DR  Pfam: PF12257;
DR  PROSITE: PS50186;
DR  OMIM: 604364;
DR  OMIM: 614191;
DR  DisGeNET: 9681;
DE  Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:29769719}.
DE  Disease: Epilepsy, familial focal, with variable foci 1 (FFEVF1) [MIM:604364]: An autosomal dominant form of epilepsy characterized by focal seizures arising from different cortical regions in different family members. Many patients have an aura and show automatisms during the seizures, whereas others may have nocturnal seizures. There is often secondary generalization. Some patients show abnormal interictal EEG, and some patients may have intellectual disability or autism spectrum disorders. Seizure onset usually occurs in the first or second decades, although later onset has been reported, and there is phenotypic variability within families. Penetrance of the disorder is incomplete. {ECO:0000269|PubMed:23542697, ECO:0000269|PubMed:23542701, ECO:0000269|PubMed:24283814, ECO:0000269|PubMed:24591017, ECO:0000269|PubMed:25366275, ECO:0000269|PubMed:26505888, ECO:0000269|PubMed:27173016}. Note=The disease is caused by mutations affecting the gene represented in this entry. Note=Inactivating mutations and truncating deletions in the genes encoding GATOR1 proteins, including DEPDC5, are detected in glioblastoma and ovarian tumors and are associated with loss of heterozygosity events. Inactivation of GATOR1 proteins promotes constitutive localization of mTORC1 to the lysosomal membrane and blocks mTORC1 inactivation following amino acid withdrawal (PubMed:23723238). {ECO:0000269|PubMed:23723238}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5T011; IntAct: EBI-10749411,EBI-11102814; Score: 0.35
DE  Interaction: Q12980; IntAct: EBI-2650314,EBI-11102814; Score: 0.35
DE  Interaction: Q8WTW4; IntAct: EBI-11102814,EBI-1043552; Score: 0.53
DE  Interaction: Q99459; IntAct: EBI-11102814,EBI-374880; Score: 0.37
DE  Interaction: P58043; IntAct: EBI-9638431,EBI-11102814; Score: 0.35
DE  Interaction: Q9Y664; IntAct: EBI-11102814,EBI-1048252; Score: 0.35
DE  Interaction: Q96MD2; IntAct: EBI-11102814,EBI-20840475; Score: 0.35
DE  Interaction: Q969R8; IntAct: EBI-11102814,EBI-723695; Score: 0.35
DE  Interaction: Q5T011-5; IntAct: EBI-11102814,EBI-10245139; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-11102814; Score: 0.40
DE  Interaction: Q1RMZ1; IntAct: EBI-21285976,EBI-11102814; Score: 0.35
GO  GO:0005829;
GO  GO:1990130;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0044877;
GO  GO:0034198;
GO  GO:0035556;
GO  GO:0032007;
GO  GO:1904262;
GO  GO:0010506;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLR
SQ  PYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEDT
SQ  RVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEINRA
SQ  SIRQDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKH
SQ  YINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSAPRDSRLGDDYNIP
SQ  HWINHSFYTSKSQLFCNSFTPRIKLAGKKPASEKAKNGRDTSLGSPKESENALPIQVDYDAYDAQVFRLPGPSRAQCLTT
SQ  CRSVRERESHSRKSASSCDVSSSPSLPSRTLPTEEVRSQASDDSSLGKSANILMIPHPHLHQYEVSSSLGYTSTRDVLEN
SQ  MMEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNM
SQ  AELQGSGQRDPTHSSAELLELAYHEAAGRHSNSRQPGDGMSFLNFSGTEELSVGLLSNSGAGMNPRTQNKDSLEDSVSTS
SQ  PDPILTLSAPPVVPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADIDRRDEDGVQMTAQQVFE
SQ  EFICQRLMQGYQIIVQPKTQKPNPAVPPPLSSSPLYSRGLVSRNRPEEEDQYWLSMGRTFHKVTLKDKMITVTRYLPKYP
SQ  YESAQIHYTYSLCPSHSDSEFVSCWVEFSHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRIT
SQ  EGEAHCDIYGDRPRADEDEWQLLDGFVRFVEGLNRIRRRHRSDRMMRKGTAMKGLQMTGPISTHSLESTAPPVGKKGTSA
SQ  LSALLEMEASQKCLGEQQAAVHGGKSSAQSAESSSVAMTPTYMDSPRKDGAFFMEFVRSPRTASSAFYPQVSVDQTATPM
SQ  LDGTSLGICTGQSMDRGNSQTFGNSQNIGEQGYSSTNSSDSSSQQLVASSLTSSSTLTEILEAMKHPSTGVQLLSEQKGL
SQ  SPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVAMQQPATTWHT
SQ  AGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDV
SQ  NNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLF
SQ  IPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSKRKF
SQ  SGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTSCLEKMHA
SQ  SAP
//
ID  Q13625;
PN  Apoptosis-stimulating of p53 protein 2;
GN  TP53BP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.
DR  UNIPROT: Q13625;
DR  UNIPROT: B4DG66;
DR  UNIPROT: Q12892;
DR  UNIPROT: Q86X75;
DR  UNIPROT: Q96KQ3;
DR  PDB: 1YCS;
DR  PDB: 2UWQ;
DR  PDB: 4A63;
DR  PDB: 4IRV;
DR  PDB: 6GHM;
DR  PDB: 6HKP;
DR  Pfam: PF12796;
DR  Pfam: PF00018;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS50002;
DR  OMIM: 602143;
DR  DisGeNET: 7159;
DE  Function: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (PubMed:12524540). Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}.
DE  Reference Proteome: Yes;
DE  Interaction: P49790; IntAct: EBI-77642,EBI-286779; Score: 0.35
DE  Interaction: P61970; IntAct: EBI-77642,EBI-591778; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-77642,EBI-286642; Score: 0.64
DE  Interaction: Q12840; IntAct: EBI-713468,EBI-77642; Score: 0.37
DE  Interaction: O15265; IntAct: EBI-77642,EBI-708350; Score: 0.37
DE  Interaction: P46108; IntAct: EBI-886,EBI-77642; Score: 0.40
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-77642; Score: 0.64
DE  Interaction: P61981; IntAct: EBI-359832,EBI-77642; Score: 0.35
DE  Interaction: Q05086-2; IntAct: EBI-10175863,EBI-77642; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-366083,EBI-77642; Score: 0.90
DE  Interaction: Q6NSK7; IntAct: EBI-77642,EBI-21369851; Score: 0.37
DE  Interaction: P31946; IntAct: EBI-359815,EBI-77642; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-746752,EBI-77642; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-1044059,EBI-77642; Score: 0.69
DE  Interaction: Q7TSJ6; IntAct: EBI-6305003,EBI-77642; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-2511319,EBI-77642; Score: 0.35
DE  Interaction: P29991; IntAct: EBI-77642,EBI-8826488; Score: 0.37
DE  Interaction: Q14457; IntAct: EBI-949378,EBI-77642; Score: 0.40
DE  Interaction: Q9BYG5; IntAct: EBI-295391,EBI-77642; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-2212028,EBI-77642; Score: 0.35
DE  Interaction: Q9Y2I6; IntAct: EBI-719716,EBI-77642; Score: 0.35
DE  Interaction: O60308; IntAct: EBI-2685240,EBI-77642; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-716327,EBI-77642; Score: 0.35
DE  Interaction: O94986; IntAct: EBI-311012,EBI-77642; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-741421,EBI-77642; Score: 0.35
DE  Interaction: Q5BJF6; IntAct: EBI-8744243,EBI-77642; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11335160,EBI-77642; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-1059012,EBI-77642; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-1046993,EBI-77642; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-77642; Score: 0.35
DE  Interaction: Q8N4C6; IntAct: EBI-1164022,EBI-77642; Score: 0.35
DE  Interaction: Q8TES7; IntAct: EBI-2350063,EBI-77642; Score: 0.35
DE  Interaction: Q96KN7; IntAct: EBI-1050213,EBI-77642; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-2514016,EBI-77642; Score: 0.35
DE  Interaction: Q96ST8; IntAct: EBI-2799206,EBI-77642; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-2873150,EBI-77642; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-2563266,EBI-77642; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-347088,EBI-77642; Score: 0.67
DE  Interaction: Q9NPB6; IntAct: EBI-81876,EBI-77642; Score: 0.35
DE  Interaction: Q9JK83; IntAct: EBI-81861,EBI-77642; Score: 0.35
DE  Interaction: P46938; IntAct: EBI-1211949,EBI-77642; Score: 0.35
DE  Interaction: Q8NHQ8; IntAct: EBI-306805,EBI-77642; Score: 0.53
DE  Interaction: Q96NE9-2; IntAct: EBI-13213391,EBI-77642; Score: 0.35
DE  Interaction: Q15435; IntAct: EBI-77642,EBI-1024281; Score: 0.51
DE  Interaction: P36873-1; IntAct: EBI-77642,EBI-356289; Score: 0.37
DE  Interaction: P36873-2; IntAct: EBI-3964623,EBI-77642; Score: 0.37
DE  Interaction: P62136; IntAct: EBI-357253,EBI-77642; Score: 0.86
DE  Interaction: P36873; IntAct: EBI-77642,EBI-356283; Score: 0.85
DE  Interaction: Q8IUQ4; IntAct: EBI-77642,EBI-747107; Score: 0.37
DE  Interaction: Q81ZG1; IntAct: EBI-2815760,EBI-77642; Score: 0.37
DE  Interaction: Q9BYC9; IntAct: EBI-714361,EBI-77642; Score: 0.37
DE  Interaction: Q13107; IntAct: EBI-723290,EBI-77642; Score: 0.37
DE  Interaction: Q9NU19; IntAct: EBI-8787464,EBI-77642; Score: 0.37
DE  Interaction: P04637-1; IntAct: EBI-3895849,EBI-77642; Score: 0.37
DE  Interaction: Q53HC0; IntAct: EBI-719994,EBI-77642; Score: 0.37
DE  Interaction: P16403; IntAct: EBI-358372,EBI-77642; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-297903,EBI-77642; Score: 0.40
DE  Interaction: Q8TEW0; IntAct: EBI-77642,EBI-81968; Score: 0.53
DE  Interaction: A6NKD9; IntAct: EBI-77642,EBI-2561671; Score: 0.35
DE  Interaction: P41236; IntAct: EBI-77642,EBI-1056517; Score: 0.35
DE  Interaction: O75901; IntAct: EBI-77642,EBI-6871931; Score: 0.35
DE  Interaction: Q9H3G5; IntAct: EBI-77642,EBI-357542; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-77642,EBI-356933; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-77642,EBI-352350; Score: 0.60
DE  Interaction: Q92598; IntAct: EBI-77642,EBI-356829; Score: 0.35
DE  Interaction: Q02833; IntAct: EBI-77642,EBI-929013; Score: 0.35
DE  Interaction: Q15834; IntAct: EBI-77642,EBI-739674; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-77642,EBI-354007; Score: 0.35
DE  Interaction: A6NK89; IntAct: EBI-6912267,EBI-77642; Score: 0.35
DE  Interaction: Q8N137; IntAct: EBI-947360,EBI-77642; Score: 0.35
DE  Interaction: Q8N960; IntAct: EBI-2563015,EBI-77642; Score: 0.35
DE  Interaction: Q8IW35; IntAct: EBI-1566210,EBI-77642; Score: 0.35
DE  Interaction: Q9C0F1; IntAct: EBI-744115,EBI-77642; Score: 0.35
DE  Interaction: Q9HC77; IntAct: EBI-946194,EBI-77642; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-352162,EBI-77642; Score: 0.37
DE  Interaction: P21246; IntAct: EBI-473725,EBI-77642; Score: 0.37
DE  Interaction: Q9BVJ6; IntAct: EBI-473284,EBI-77642; Score: 0.37
DE  Interaction: Q13432; IntAct: EBI-711260,EBI-77642; Score: 0.37
DE  Interaction: P05067; IntAct: EBI-77613,EBI-77642; Score: 0.58
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0051059;
GO  GO:0002039;
GO  GO:0017124;
GO  GO:0005070;
GO  GO:0007049;
GO  GO:0072332;
GO  GO:0045786;
GO  GO:1900119;
GO  GO:1901216;
GO  GO:1900740;
GO  GO:0042981;
GO  GO:1901796;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFL
SQ  RHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLK
SQ  QQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTR
SQ  QLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQ
SQ  QKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQ
SQ  TKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQS
SQ  SEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIP
SQ  SVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPH
SQ  FSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEA
SQ  LRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEV
SQ  VSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPE
SQ  GPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGI
SQ  TALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGY
SQ  TQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRI
SQ  KPRQRSLA
//
ID  Q5RED8;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  CYLD;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DR  UNIPROT: Q5RED8;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Plays an important role in the regulation of pathways leading to NF-kappa-B activation. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Removes 'Lys- 63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0061578;
GO  GO:0004843;
GO  GO:0008270;
GO  GO:0045087;
GO  GO:0090090;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:0010803;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NQC7};
SQ  MSSGLWSQDKVTSPYWEERVFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNRIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKV
SQ  GETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLA
SQ  FMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSP
SQ  PLQPPPVNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKE
SQ  NPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNS
SQ  LAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELL
SQ  RTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFME
SQ  KNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECR
SQ  ECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGK
SQ  DDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q8C0T9;
PN  Adenylate cyclase type 10;
GN  Adcy10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000269|PubMed:12475901}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane- associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}.
DR  UNIPROT: Q8C0T9;
DR  UNIPROT: B2RRJ9;
DR  UNIPROT: Q3V0F8;
DR  Pfam: PF00211;
DR  PROSITE: PS50125;
DE  Function: Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP- responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (PubMed:14976244, PubMed:16054031). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244, ECO:0000269|PubMed:16054031}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0045178;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005576;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0031514;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004016;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0071890;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0006171;
GO  GO:0071241;
GO  GO:0003351;
GO  GO:0035556;
GO  GO:0043065;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96PN6};
SQ  MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYIS
SQ  AIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEAEEGLDIRVKIGLAAGHITMLVFGDE
SQ  TRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFTKCMGFMDYY
SQ  PSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVH
SQ  ITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTV
SQ  RHEYTVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNR
SQ  YEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQI
SQ  LMANVLGLDTCKHYKERQTNLQNRVKTLLDEKFHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILAQTVREERI
SQ  IFIIDEAQFVDGTSWAFIEKLIRSMPIFIVMSLAPFSEVPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIP
SQ  RELDSYLVEGSCGIPYYCEELLKNLDHHRVLLFQQAETEQKTNVTWNNMFKHSVRPTDDMQLFTSISEGQKEVCYLVSGV
SQ  RLNNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFNCFRSSKDLQ
SQ  LALKQNVPTFEVHYRSLALKLKEGLTYGEEEELREMEGEVVECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEES
SQ  AHRCNHCRNVDFIPYHHFIVDIRLNTLDMDTVKRMVTSQGFKIDEEEAIFSKSELPRKYKFPENLSITEIREKILHFFDN
SQ  VILKMKSSPNDIIPLESCQCKELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTN
SQ  EDSWSQTFEYATFYSLKAEVCFNMGQMVLAKKMLRKALKLLNRMFPCNLLTLTFQMHVEKNRLSHFMNQHTQEGSVPGKK
SQ  LAQLYLQASCFSLLWRIYSLNFFFHYKYYGHLAAMMEMNTSLETQNDFQIIKAYLDFSLYHHLAGYQGVWFKYEILVMEQ
SQ  LLNLPLKGEAIEIMAYTADTLGHIKFLMGHLDLAIELGSRAHRMWSLLRNPNKYQMVLCRLSKPLFLKSRYKHLVQVLGW
SQ  LWDLSVTEEDIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFNK
SQ  FSDRAKHLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVEILKALETLVAQNTTGPVFYPRLYHLMAYVC
SQ  ILMGDGHSCDFFLNTALELSETHGNLLEKCWLSMSKEWWYSASELTGDQWLQTVLSLPSWDKIVSGKGGQRKRSWSWFCP
SQ  PNFSMVSWSQPQCA
//
ID  P61809;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  Cdk5r1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
DR  UNIPROT: P61809;
DR  UNIPROT: Q62938;
DR  Pfam: PF03261;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:24235147}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0043292;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0016533;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0045296;
GO  GO:0005509;
GO  GO:0061575;
GO  GO:0008092;
GO  GO:0046875;
GO  GO:0051879;
GO  GO:0035255;
GO  GO:0016301;
GO  GO:0002020;
GO  GO:0019901;
GO  GO:0043539;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0007420;
GO  GO:0021549;
GO  GO:0021799;
GO  GO:0009792;
GO  GO:0048013;
GO  GO:0007213;
GO  GO:0021766;
GO  GO:0035235;
GO  GO:0021819;
GO  GO:0030517;
GO  GO:0045892;
GO  GO:0007158;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0071158;
GO  GO:0045348;
GO  GO:0043525;
GO  GO:0045860;
GO  GO:0090314;
GO  GO:0010870;
GO  GO:0032956;
GO  GO:0061001;
GO  GO:0070507;
GO  GO:0098693;
GO  GO:0048511;
GO  GO:0042501;
GO  GO:0021722;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
//
ID  Q12840;
PN  Kinesin heavy chain isoform 5A;
GN  KIF5A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. {ECO:0000250|UniProtKB:Q6QLM7}.
DR  UNIPROT: Q12840;
DR  UNIPROT: A6H8M5;
DR  UNIPROT: Q4LE26;
DR  PDB: 4UXT;
DR  PDB: 4UXY;
DR  PDB: 4UY0;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DR  OMIM: 602821;
DR  OMIM: 604187;
DR  OMIM: 617235;
DR  OMIM: 617921;
DR  DisGeNET: 3798;
DE  Function: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation. {ECO:0000250|UniProtKB:P33175, ECO:0000250|UniProtKB:Q6QLM7}.
DE  Disease: Spastic paraplegia 10, autosomal dominant (SPG10) [MIM:604187]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:12355402, ECO:0000269|PubMed:15452312, ECO:0000269|PubMed:16476820, ECO:0000269|PubMed:16489470, ECO:0000269|PubMed:18203753, ECO:0000269|PubMed:18245137, ECO:0000269|PubMed:18853458, ECO:0000269|PubMed:21107874}. Note=The disease is caused by mutations affecting the gene represented in this entry. Myoclonus, intractable, neonatal (NEIMY) [MIM:617235]: An autosomal dominant neurologic disorder characterized by severe, infantile-onset myoclonic seizures, hypotonia, optic nerve abnormalities, dysphagia, apnea, and early developmental arrest. Brain imaging shows a progressive leukoencephalopathy. Some patients may die in infancy. {ECO:0000269|PubMed:24215330, ECO:0000269|PubMed:27414745, ECO:0000269|PubMed:27463701}. Note=The disease is caused by mutations affecting the gene represented in this entry. Amyotrophic lateral sclerosis 25 (ALS25) [MIM:617921]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. ALS25 is an autosomal dominant form with variable adult onset and incomplete penetrance. {ECO:0000269|PubMed:29342275, ECO:0000269|PubMed:29566793}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. The mutation NM_004984.2:c.33019A>G encoding the predicted missence variant p.Arg1007Gly, may also affect splicing and induce the skipping of exon 27, resulting in a frameshift and a premature stop codon producing a truncated protein p.Asn999Valfs*39. {ECO:0000269|PubMed:29342275}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-351935,EBI-713468; Score: 0.40
DE  Interaction: Q06787; IntAct: EBI-713468,EBI-366305; Score: 0.37
DE  Interaction: P31946-2; IntAct: EBI-10770173,EBI-713468; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-359832,EBI-713468; Score: 0.35
DE  Interaction: Q9NV70; IntAct: EBI-713468,EBI-1045313; Score: 0.37
DE  Interaction: Q8TDR0-2; IntAct: EBI-713468,EBI-11946508; Score: 0.37
DE  Interaction: P61457; IntAct: EBI-740475,EBI-713468; Score: 0.40
DE  Interaction: O95819; IntAct: EBI-2511133,EBI-713468; Score: 0.37
DE  Interaction: Q9Y4G8; IntAct: EBI-307079,EBI-713468; Score: 0.37
DE  Interaction: Q00987; IntAct: EBI-389668,EBI-713468; Score: 0.40
DE  Interaction: P28702; IntAct: EBI-748576,EBI-713468; Score: 0.40
DE  Interaction: P06213; IntAct: EBI-10818032,EBI-713468; Score: 0.35
DE  Interaction: Q4G0F5; IntAct: EBI-6151831,EBI-713468; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-713468; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-347088,EBI-713468; Score: 0.35
DE  Interaction: O60296; IntAct: EBI-2851680,EBI-713468; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-359854,EBI-713468; Score: 0.35
DE  Interaction: Q96NW4; IntAct: EBI-6125599,EBI-713468; Score: 0.58
DE  Interaction: Q8TDR0; IntAct: EBI-928811,EBI-713468; Score: 0.37
DE  Interaction: Q9BYV6; IntAct: EBI-713468,EBI-2341179; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-713468; Score: 0.35
DE  Interaction: Q96EV8-2; IntAct: EBI-16749183,EBI-713468; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-713468; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-2547514,EBI-713468; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-9008641,EBI-713468; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-742327,EBI-713468; Score: 0.35
DE  Interaction: P13497; IntAct: EBI-489827,EBI-713468; Score: 0.35
DE  Interaction: Q07866-2; IntAct: EBI-11979975,EBI-713468; Score: 0.35
DE  Interaction: P12524-2; IntAct: EBI-18936665,EBI-713468; Score: 0.35
DE  Interaction: Q8N205-2; IntAct: EBI-12099160,EBI-713468; Score: 0.35
DE  Interaction: Q9NV70-2; IntAct: EBI-10961687,EBI-713468; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-713468; Score: 0.35
DE  Interaction: Q15811; IntAct: EBI-713468,EBI-602041; Score: 0.37
DE  Interaction: Q13625; IntAct: EBI-713468,EBI-77642; Score: 0.37
GO  GO:1904115;
GO  GO:0005623;
GO  GO:0035253;
GO  GO:0005829;
GO  GO:0032839;
GO  GO:0005871;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0008574;
GO  GO:0016887;
GO  GO:0019894;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0003774;
GO  GO:0099641;
GO  GO:0098971;
GO  GO:0019886;
GO  GO:0007411;
GO  GO:0007268;
GO  GO:0030705;
GO  GO:0007018;
GO  GO:1990049;
GO  GO:0006890;
GO  GO:0048489;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG
SQ  TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDK
SQ  NRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVS
SQ  KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMF
SQ  GQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVN
SQ  DNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAA
SQ  KDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSE
SQ  FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKI
SQ  RSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDE
SQ  INEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKL
SQ  FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALK
SQ  EAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQ
SQ  ATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS
//
ID  O95996;
PN  Adenomatous polyposis coli protein 2;
GN  APC2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}. Golgi apparatus {ECO:0000269|PubMed:11691822}. Cytoplasm {ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10646860}. Note=Associated with actin filaments (PubMed:11691822, PubMed:25753423). Associated with microtubule network (PubMed:10644998, PubMed:11691822, PubMed:25753423). {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
DR  UNIPROT: O95996;
DR  UNIPROT: Q05BW4;
DR  UNIPROT: Q9UBZ1;
DR  UNIPROT: Q9UEM8;
DR  UNIPROT: Q9UQJ8;
DR  UNIPROT: Q9UQJ9;
DR  UNIPROT: Q9Y632;
DR  Pfam: PF05956;
DR  Pfam: PF16689;
DR  Pfam: PF05923;
DR  Pfam: PF18797;
DR  Pfam: PF00514;
DR  Pfam: PF05924;
DR  OMIM: 612034;
DR  OMIM: 617169;
DR  DisGeNET: 10297;
DE  Function: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases (PubMed:25753423). May also function in Wnt signaling by promoting the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822, PubMed:9823329). {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423, ECO:0000269|PubMed:9823329}.
DE  Disease: Sotos syndrome 3 (SOTOS3) [MIM:617169]: A form of Sotos syndrome, a childhood overgrowth syndrome characterized by prenatal and postnatal overgrowth, developmental delay, mental retardation, advanced bone age, and abnormal craniofacial morphology. SOTOS3 patients do not have advanced bone age, hypotonia, seizures, or autism. SOTOS3 transmission pattern is consistent with autosomal recessive inheritance. {ECO:0000269|PubMed:25753423}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRI5; IntAct: EBI-1053045,EBI-529989; Score: 0.37
DE  Interaction: P16035; IntAct: EBI-1053045,EBI-1033507; Score: 0.40
GO  GO:0005884;
GO  GO:0030877;
GO  GO:0016342;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0045171;
GO  GO:0031258;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0008013;
GO  GO:0045295;
GO  GO:0008017;
GO  GO:0090630;
GO  GO:0001708;
GO  GO:0016477;
GO  GO:0000226;
GO  GO:0090090;
GO  GO:0007026;
GO  GO:0007389;
GO  GO:0045732;
GO  GO:0045595;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQ
SQ  MDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQ
SQ  GLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQA
SQ  LLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQI
SQ  LHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGA
SQ  GSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVAN
SQ  KATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNL
SQ  SAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLT
SQ  IVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYV
SQ  RKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPA
SQ  ALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPG
SQ  QEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCG
SQ  QPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVP
SQ  EKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGAT
SQ  SLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPD
SQ  SPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSA
SQ  LALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVAS
SQ  ALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMG
SQ  HRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPA
SQ  AAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPR
SQ  GREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASD
SQ  LDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVK
SQ  TSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRS
SQ  RSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQ
SQ  HKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKE
SQ  SPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSES
SQ  PSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRS
SQ  TLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPI
SQ  SAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE
//
ID  O75146;
PN  Huntingtin-interacting protein 1-related protein;
GN  HIP1R;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
DR  UNIPROT: O75146;
DR  UNIPROT: A6NHQ6;
DR  UNIPROT: Q6NXG8;
DR  UNIPROT: Q9UED9;
DR  PDB: 1R0D;
DR  Pfam: PF07651;
DR  Pfam: PF16515;
DR  Pfam: PF01608;
DR  PROSITE: PS50942;
DR  PROSITE: PS50945;
DR  OMIM: 605613;
DR  DisGeNET: 9026;
DE  Function: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3- phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:14732715}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-714707,EBI-4402639; Score: 0.53
DE  Interaction: P03372; IntAct: EBI-78473,EBI-4402639; Score: 0.35
DE  Interaction: Q62925; IntAct: EBI-4402639,EBI-636664; Score: 0.44
DE  Interaction: Q13404; IntAct: EBI-4402639,EBI-1050671; Score: 0.44
DE  Interaction: P22314; IntAct: EBI-4402639,EBI-709688; Score: 0.44
DE  Interaction: P61088; IntAct: EBI-4402639,EBI-1052908; Score: 0.44
DE  Interaction: P60033; IntAct: EBI-712921,EBI-4402639; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-353957,EBI-4402639; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-777558,EBI-4402639; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-350338,EBI-4402639; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-762451,EBI-4402639; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-351479,EBI-4402639; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079353,EBI-4402639; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-726598,EBI-4402639; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-4402639; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-2803688,EBI-4402639; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-354967,EBI-4402639; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-2693855,EBI-4402639; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-10983249,EBI-4402639; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-19027521,EBI-4402639; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-2561547,EBI-4402639; Score: 0.35
DE  Interaction: Q8N468; IntAct: EBI-20809966,EBI-4402639; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-4402639; Score: 0.35
DE  Interaction: Q9NZQ7; IntAct: EBI-4314282,EBI-4402639; Score: 0.35
DE  Interaction: Q9NUM3; IntAct: EBI-2823239,EBI-4402639; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12562139,EBI-4402639; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-18539709,EBI-4402639; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-2875891,EBI-4402639; Score: 0.35
DE  Interaction: P46059; IntAct: EBI-21560873,EBI-4402639; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-4320063,EBI-4402639; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-968453,EBI-4402639; Score: 0.35
DE  Interaction: Q86VU5; IntAct: EBI-2836030,EBI-4402639; Score: 0.35
DE  Interaction: Q6PJG9; IntAct: EBI-7910762,EBI-4402639; Score: 0.35
DE  Interaction: Q96FJ0; IntAct: EBI-745021,EBI-4402639; Score: 0.35
DE  Interaction: P35813; IntAct: EBI-4402639,EBI-989143; Score: 0.35
DE  Interaction: Q96D71-2; IntAct: EBI-4402639,EBI-10284498; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-4402639,EBI-749285; Score: 0.35
DE  Interaction: Q10567-2; IntAct: EBI-4402639,EBI-11037749; Score: 0.35
DE  Interaction: P23246; IntAct: EBI-4402639,EBI-355453; Score: 0.35
DE  Interaction: O75688-2; IntAct: EBI-4402639,EBI-21645158; Score: 0.35
DE  Interaction: O00291; IntAct: EBI-4402639,EBI-473886; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671881,EBI-4402639; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-6911574,EBI-4402639; Score: 0.35
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0030665;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0032839;
GO  GO:0043197;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0051015;
GO  GO:0035615;
GO  GO:0030276;
GO  GO:0032051;
GO  GO:0042802;
GO  GO:0035091;
GO  GO:0005547;
GO  GO:0043325;
GO  GO:0080025;
GO  GO:0005546;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0017124;
GO  GO:0007015;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:0048268;
GO  GO:0055123;
GO  GO:0061024;
GO  GO:0030837;
GO  GO:0043066;
GO  GO:0034316;
GO  GO:0043065;
GO  GO:1905445;
GO  GO:0045742;
GO  GO:1901030;
GO  GO:2000588;
GO  GO:0032092;
GO  GO:0048260;
GO  GO:0050821;
GO  GO:0006898;
GO  GO:0032956;
GO  GO:2000369;
GO  GO:0030100;
GO  GO:0060453;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSS
SQ  ILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEV
SQ  LEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSC
SQ  LPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIE
SQ  ISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRK
SQ  QKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQ
SQ  SQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALS
SQ  GAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVS
SQ  KLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADR
SQ  LIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRR
SQ  IEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVG
SQ  WGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQI
SQ  EDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPL
SQ  AQKPSVAPRQDHQLDKKDGIYPAQLVNY
//
ID  Q9UQF2;
PN  C-Jun-amino-terminal kinase-interacting protein 1;
GN  MAPK8IP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane. Mitochondrion membrane. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9UQF2;
DR  UNIPROT: D3DQP4;
DR  UNIPROT: O43407;
DR  PDB: 2G01;
DR  PDB: 2GMX;
DR  PDB: 2H96;
DR  PDB: 3OXI;
DR  PDB: 3PTG;
DR  PDB: 3VUD;
DR  PDB: 3VUG;
DR  PDB: 3VUH;
DR  PDB: 3VUI;
DR  PDB: 3VUK;
DR  PDB: 3VUL;
DR  PDB: 3VUM;
DR  PDB: 4E73;
DR  PDB: 4G1W;
DR  PDB: 4H39;
DR  PDB: 4HYS;
DR  PDB: 4HYU;
DR  PDB: 4IZY;
DR  PDB: 5LW1;
DR  PDB: 6FUZ;
DR  Pfam: PF00640;
DR  Pfam: PF14604;
DR  PROSITE: PS01179;
DR  PROSITE: PS50002;
DR  OMIM: 125853;
DR  OMIM: 604641;
DR  DisGeNET: 9479;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells. {ECO:0000250|UniProtKB:Q9WVI9}.
DE  Disease: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:10700186}. Note=The disease may be caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-78404,EBI-641062; Score: 0.59
DE  Interaction: Q9UPT6; IntAct: EBI-717887,EBI-78404; Score: 0.35
DE  Interaction: Self; IntAct: EBI-78404,EBI-78404; Score: 0.40
DE  Interaction: Q86Y07-2; IntAct: EBI-78404,EBI-1207636; Score: 0.46
DE  Interaction: O43318; IntAct: EBI-78404,EBI-358684; Score: 0.72
DE  Interaction: O14733; IntAct: EBI-78404,EBI-492605; Score: 0.62
DE  Interaction: P45983; IntAct: EBI-78404,EBI-286483; Score: 0.62
DE  Interaction: Q86Y07-1; IntAct: EBI-78404,EBI-1207633; Score: 0.46
DE  Interaction: P27824; IntAct: EBI-78404,EBI-355947; Score: 0.27
DE  Interaction: Q15750; IntAct: EBI-78404,EBI-358643; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-78404,EBI-515315; Score: 0.37
DE  Interaction: P05067; IntAct: EBI-78404,EBI-77613; Score: 0.72
DE  Interaction: Q9UK73; IntAct: EBI-78404,EBI-310482; Score: 0.35
DE  Interaction: Q7Z333-4; IntAct: EBI-78404,EBI-21514402; Score: 0.35
DE  Interaction: Q14679; IntAct: EBI-78404,EBI-11332149; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-78404,EBI-350989; Score: 0.35
DE  Interaction: Q13387-2; IntAct: EBI-78404,EBI-21570214; Score: 0.35
DE  Interaction: Q01484-4; IntAct: EBI-78404,EBI-21549385; Score: 0.35
DE  Interaction: P45984-2; IntAct: EBI-78404,EBI-21529223; Score: 0.35
DE  Interaction: P45983-2; IntAct: EBI-78404,EBI-21562989; Score: 0.35
DE  Interaction: P31273; IntAct: EBI-78404,EBI-1752118; Score: 0.35
DE  Interaction: Q12955; IntAct: EBI-78404,EBI-2691178; Score: 0.35
DE  Interaction: Q96HI0; IntAct: EBI-78404,EBI-3895753; Score: 0.35
DE  Interaction: O94762; IntAct: EBI-78404,EBI-395321; Score: 0.37
GO  GO:0044295;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0044294;
GO  GO:0044302;
GO  GO:0005789;
GO  GO:0031966;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0004860;
GO  GO:0007258;
GO  GO:0090090;
GO  GO:2001243;
GO  GO:0043508;
GO  GO:0045807;
GO  GO:0046330;
GO  GO:0006898;
GO  GO:2000564;
GO  GO:0046328;
GO  GO:0006355;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGG
SQ  GGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKR
SQ  PTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRS
SQ  TATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPS
SQ  TAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCF
SQ  GDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLF
SQ  SCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKN
SQ  SDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQ
SQ  LKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
//
ID  Q8IX03;
PN  Protein KIBRA;
GN  WWC1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Cell projection, ruffle membrane. Note=Colocalizes with PRKCZ in the perinuclear region.
DR  UNIPROT: Q8IX03;
DR  UNIPROT: B4DK05;
DR  UNIPROT: O94946;
DR  UNIPROT: Q6MZX4;
DR  UNIPROT: Q6Y2F8;
DR  UNIPROT: Q7Z4G8;
DR  UNIPROT: Q8WVM4;
DR  UNIPROT: Q9BT29;
DR  PDB: 2Z0U;
DR  PDB: 6FB4;
DR  PDB: 6FD0;
DR  PDB: 6FJC;
DR  PDB: 6FJD;
DR  Pfam: PF00397;
DR  PROSITE: PS50004;
DR  PROSITE: PS01159;
DR  PROSITE: PS50020;
DR  OMIM: 610533;
DR  OMIM: 615602;
DR  DisGeNET: 23286;
DE  Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance. {ECO:0000269|PubMed:15081397, ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:23778582}.
DE  Reference Proteome: Yes;
DE  Interaction: O95831; IntAct: EBI-715828,EBI-356440; Score: 0.37
DE  Interaction: Q2I360; IntAct: EBI-715828,EBI-912397; Score: 0.37
DE  Interaction: P61981; IntAct: EBI-359832,EBI-715828; Score: 0.53
DE  Interaction: Q9UKE5; IntAct: EBI-715828,EBI-1051794; Score: 0.55
DE  Interaction: Q99459; IntAct: EBI-374880,EBI-715828; Score: 0.37
DE  Interaction: Q4VCS5; IntAct: EBI-2511319,EBI-715828; Score: 0.53
DE  Interaction: P29991; IntAct: EBI-8826689,EBI-715828; Score: 0.37
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-715828; Score: 0.53
DE  Interaction: Q8IW50; IntAct: EBI-715828,EBI-718694; Score: 0.37
DE  Interaction: Q05513; IntAct: EBI-295351,EBI-715828; Score: 0.35
DE  Interaction: Q15678; IntAct: EBI-715828,EBI-1237156; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-715828,EBI-356498; Score: 0.35
DE  Interaction: Q9Y2J2; IntAct: EBI-715828,EBI-310986; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-715828,EBI-349105; Score: 0.35
DE  Interaction: O43491; IntAct: EBI-715828,EBI-1052044; Score: 0.35
DE  Interaction: Q96FJ2; IntAct: EBI-715828,EBI-742371; Score: 0.35
DE  Interaction: Q9Y297; IntAct: EBI-715828,EBI-307461; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-715828,EBI-359854; Score: 0.35
DE  Interaction: Q9UKB1; IntAct: EBI-715828,EBI-355189; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-715828,EBI-359815; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-715828,EBI-352007; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-715828; Score: 0.35
DE  Interaction: Q6P1J9; IntAct: EBI-930143,EBI-715828; Score: 0.37
DE  Interaction: Q5UIP0; IntAct: EBI-711331,EBI-715828; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0019900;
GO  GO:0060090;
GO  GO:0003713;
GO  GO:0016477;
GO  GO:0030010;
GO  GO:0035329;
GO  GO:0035331;
GO  GO:0046621;
GO  GO:0000122;
GO  GO:0043410;
GO  GO:0007221;
GO  GO:0035330;
GO  GO:0032386;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRPELPLPEGWEEARDFDGKVYYIDHTNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQ
SQ  IEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEIL
SQ  KAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDKKMSDAQGSYKLDEAQAVLRETKAIKKAITCGEKEKQDLIK
SQ  SLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPLPKQYLDVSSQTDISGSFGINSNNQLAEKVRLRLRYEEAKRRIANLKI
SQ  QLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARKRLEKDLQAARDTQSKALTERLKLNS
SQ  KRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLVASSLDSSTSASFTDLYYDPFEQLDSELQSK
SQ  VEFLLLEGATGFRPSGCITTIHEDEVAKTQKAEGGGRLQALRSLSGTPKSMTSLSPRSSLSSPSPPCSPLMADPLLAGDA
SQ  FLNSLEFEDPELSATLCELSLGNSAQERYRLEEPGTEGKQLGQAVNTAQGCGLKVACVSAAVSDESVAGDSGVYEASVQR
SQ  LGASEAAAFDSDESEAVGATRIQIALKYDEKNKQFAILIIQLSNLSALLQQQDQKVNIRVAVLPCSESTTCLFRTRPLDA
SQ  SDTLVFNEVFWVSMSYPALHQKTLRVDVCTTDRSHLEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQSRELKPVG
SQ  VMAPASGPASTDAVSALLEQTAVELEKRQEGRSSTQTLEDSWRYEETSENEAVAEEEEEEVEEEEGEEDVFTEKASPDMD
SQ  GYPALKVDKETNTETPAPSPTVVRPKDRRVGTPSQGPFLRGSTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVR
SQ  NSLERRSVRMKRPSSVKSLRSERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEQLEQAKSHGEKELPQWLREDERF
SQ  RLLLRMLEKRQMDRAEHKGELQTDKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV
//
ID  O60711;
PN  Leupaxin;
GN  LPXN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.
DR  UNIPROT: O60711;
DR  UNIPROT: B2R8B4;
DR  UNIPROT: B4DV71;
DR  UNIPROT: Q53FW6;
DR  UNIPROT: Q6FI07;
DR  PDB: 1X3H;
DR  PDB: 4XEF;
DR  PDB: 4XEK;
DR  PDB: 4XEV;
DR  Pfam: PF00412;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  OMIM: 605390;
DR  DisGeNET: 9404;
DE  Function: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin- induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}.
DE  Reference Proteome: Yes;
DE  Interaction: Q14289; IntAct: EBI-744222,EBI-298640; Score: 0.37
DE  Interaction: Q8IVE3; IntAct: EBI-744222,EBI-2815745; Score: 0.67
DE  Interaction: P25800; IntAct: EBI-8639312,EBI-744222; Score: 0.74
DE  Interaction: P31274; IntAct: EBI-1779423,EBI-744222; Score: 0.78
DE  Interaction: Q494U1; IntAct: EBI-10241513,EBI-744222; Score: 0.56
DE  Interaction: Q8N3L3; IntAct: EBI-744222,EBI-6116822; Score: 0.56
DE  Interaction: Q06455-4; IntAct: EBI-10224192,EBI-744222; Score: 0.56
DE  Interaction: O14733; IntAct: EBI-744222,EBI-492605; Score: 0.37
DE  Interaction: Q9Y473; IntAct: EBI-3438881,EBI-744222; Score: 0.37
DE  Interaction: Q99608; IntAct: EBI-744222,EBI-718177; Score: 0.37
DE  Interaction: Q7Z3B4-2; IntAct: EBI-21504088,EBI-744222; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-744222,EBI-81279; Score: 0.44
DE  Interaction: P09022; IntAct: EBI-3957603,EBI-744222; Score: 0.57
DE  Interaction: Q8D0I3; IntAct: EBI-744222,EBI-2860455; Score: 0.37
DE  Interaction: Q8ZBT8; IntAct: EBI-744222,EBI-2865235; Score: 0.37
DE  Interaction: Q8CLR7; IntAct: EBI-744222,EBI-2844920; Score: 0.37
DE  Interaction: Q8CZX0; IntAct: EBI-2843256,EBI-744222; Score: 0.37
DE  Interaction: A0A384LCM3; IntAct: EBI-744222,EBI-2860622; Score: 0.37
DE  Interaction: A0A0J1I0J1; IntAct: EBI-744222,EBI-2820004; Score: 0.37
DE  Interaction: Q5NGW8; IntAct: EBI-744222,EBI-2803320; Score: 0.37
DE  Interaction: Q9BUY5; IntAct: EBI-743265,EBI-744222; Score: 0.37
DE  Interaction: Q96BD5; IntAct: EBI-745085,EBI-744222; Score: 0.37
DE  Interaction: P49639; IntAct: EBI-744222,EBI-740785; Score: 0.37
DE  Interaction: Q96HA1; IntAct: EBI-739990,EBI-744222; Score: 0.37
DE  Interaction: Q9NV31; IntAct: EBI-747481,EBI-744222; Score: 0.37
DE  Interaction: P48059; IntAct: EBI-744222,EBI-306928; Score: 0.37
DE  Interaction: Q63HR2; IntAct: EBI-744222,EBI-949753; Score: 0.56
DE  Interaction: Q8TAP4-4; IntAct: EBI-744222,EBI-11742507; Score: 0.56
DE  Interaction: P18206-2; IntAct: EBI-744222,EBI-11027067; Score: 0.56
DE  Interaction: P01137; IntAct: EBI-744222,EBI-779636; Score: 0.56
DE  Interaction: P21549; IntAct: EBI-744222,EBI-727098; Score: 0.56
DE  Interaction: Q96HA1-2; IntAct: EBI-744222,EBI-11956563; Score: 0.56
DE  Interaction: Q06455-2; IntAct: EBI-744222,EBI-11984663; Score: 0.56
DE  Interaction: Q494U1-3; IntAct: EBI-744222,EBI-12014286; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-744222,EBI-745213; Score: 0.56
DE  Interaction: Q9Y2X9; IntAct: EBI-744222,EBI-396200; Score: 0.35
DE  Interaction: Q9Y2X7-3; IntAct: EBI-744222,EBI-11070376; Score: 0.35
DE  Interaction: Q9ULM0; IntAct: EBI-744222,EBI-2803624; Score: 0.35
DE  Interaction: Q9UGP4; IntAct: EBI-744222,EBI-2652871; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-744222,EBI-2515122; Score: 0.35
DE  Interaction: Q9NVD7; IntAct: EBI-744222,EBI-747655; Score: 0.35
DE  Interaction: Q9NR12; IntAct: EBI-744222,EBI-350517; Score: 0.35
DE  Interaction: Q9H939; IntAct: EBI-744222,EBI-2609610; Score: 0.35
DE  Interaction: Q99700-2; IntAct: EBI-744222,EBI-16813710; Score: 0.35
DE  Interaction: Q96SN8-2; IntAct: EBI-744222,EBI-21545131; Score: 0.35
DE  Interaction: Q96F86; IntAct: EBI-744222,EBI-997311; Score: 0.35
DE  Interaction: Q93052; IntAct: EBI-744222,EBI-718388; Score: 0.35
DE  Interaction: Q8IZD4; IntAct: EBI-744222,EBI-521595; Score: 0.35
DE  Interaction: Q86YT6; IntAct: EBI-744222,EBI-2129148; Score: 0.35
DE  Interaction: Q76N32; IntAct: EBI-744222,EBI-9051024; Score: 0.35
DE  Interaction: Q69YQ0; IntAct: EBI-744222,EBI-351113; Score: 0.35
DE  Interaction: Q2TAL8; IntAct: EBI-744222,EBI-2798044; Score: 0.35
DE  Interaction: Q16204; IntAct: EBI-744222,EBI-1045350; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-744222,EBI-742327; Score: 0.35
DE  Interaction: Q15154-2; IntAct: EBI-744222,EBI-16811645; Score: 0.35
DE  Interaction: Q15052-2; IntAct: EBI-744222,EBI-21521235; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-744222,EBI-1046878; Score: 0.35
DE  Interaction: Q14155-1; IntAct: EBI-744222,EBI-717540; Score: 0.35
DE  Interaction: Q13177; IntAct: EBI-744222,EBI-1045887; Score: 0.35
DE  Interaction: Q13153-2; IntAct: EBI-744222,EBI-1019502; Score: 0.35
DE  Interaction: Q05397; IntAct: EBI-744222,EBI-702142; Score: 0.55
DE  Interaction: Q05209; IntAct: EBI-744222,EBI-2266035; Score: 0.35
DE  Interaction: P29558-2; IntAct: EBI-744222,EBI-21554551; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-744222,EBI-530012; Score: 0.35
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0016020;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0046872;
GO  GO:0003712;
GO  GO:0007155;
GO  GO:0050859;
GO  GO:0007162;
GO  GO:0065003;
GO  GO:0033628;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKE
SQ  SPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIA
SQ  GKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHC
SQ  GEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELH
SQ  YHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
//
ID  P25491;
PN  Mitochondrial protein import protein MAS5;
GN  YDJ1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrated in a perinuclear ring as well as in the cytoplasm.
DR  UNIPROT: P25491;
DR  UNIPROT: D6W1B6;
DR  PDB: 1NLT;
DR  PDB: 1XAO;
DR  PDB: 5VSO;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex. {ECO:0000269|PubMed:11689685}.
DE  Reference Proteome: Yes;
DE  Interaction: P06105; IntAct: EBI-10420,EBI-16374; Score: 0.35
DE  Interaction: P06782; IntAct: EBI-10420,EBI-17516; Score: 0.35
DE  Interaction: P12866; IntAct: EBI-18383,EBI-10420; Score: 0.35
DE  Interaction: P40075; IntAct: EBI-16735,EBI-10420; Score: 0.35
DE  Interaction: P04150; IntAct: EBI-493507,EBI-10420; Score: 0.50
DE  Interaction: P10591; IntAct: EBI-8591,EBI-10420; Score: 0.53
DE  Interaction: P31376; IntAct: EBI-20613,EBI-10420; Score: 0.35
DE  Interaction: P08153; IntAct: EBI-10420,EBI-18633; Score: 0.35
DE  Interaction: P40528; IntAct: EBI-18696,EBI-10420; Score: 0.35
DE  Interaction: P40468; IntAct: EBI-10420,EBI-18961; Score: 0.35
DE  Interaction: Q06510; IntAct: EBI-10420,EBI-2094606; Score: 0.35
DE  Interaction: Q12466; IntAct: EBI-10420,EBI-34614; Score: 0.35
DE  Interaction: Q03640; IntAct: EBI-10420,EBI-27872; Score: 0.35
DE  Interaction: P38228; IntAct: EBI-19039,EBI-10420; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-7218,EBI-10420; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-6314,EBI-10420; Score: 0.35
DE  Interaction: P41903; IntAct: EBI-14154,EBI-10420; Score: 0.35
DE  Interaction: P36145; IntAct: EBI-18907,EBI-10420; Score: 0.35
DE  Interaction: Q02939; IntAct: EBI-2345544,EBI-10420; Score: 0.35
DE  Interaction: P32367; IntAct: EBI-10420,EBI-19150; Score: 0.35
DE  Interaction: P14306; IntAct: EBI-5916,EBI-10420; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-10420,EBI-9017; Score: 0.35
DE  Interaction: P34167; IntAct: EBI-10420,EBI-9025; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-8951,EBI-10420; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-10420,EBI-8958; Score: 0.35
DE  Interaction: P38431; IntAct: EBI-10420,EBI-9038; Score: 0.35
DE  Interaction: Q01852; IntAct: EBI-9141,EBI-10420; Score: 0.35
DE  Interaction: Q02208; IntAct: EBI-27048,EBI-10420; Score: 0.35
DE  Interaction: P04786; IntAct: EBI-19338,EBI-10420; Score: 0.35
DE  Interaction: P35169; IntAct: EBI-19374,EBI-10420; Score: 0.35
DE  Interaction: P40032; IntAct: EBI-22536,EBI-10420; Score: 0.35
DE  Interaction: P40414; IntAct: EBI-10420,EBI-19419; Score: 0.35
DE  Interaction: P48561; IntAct: EBI-10420,EBI-19525; Score: 0.35
DE  Interaction: P12685; IntAct: EBI-19530,EBI-10420; Score: 0.35
DE  Interaction: Q04183; IntAct: EBI-10420,EBI-32112; Score: 0.35
DE  Interaction: P40061; IntAct: EBI-22621,EBI-10420; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-10420,EBI-18976; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-10420,EBI-18981; Score: 0.35
DE  Interaction: P52488; IntAct: EBI-19710,EBI-10420; Score: 0.35
DE  Interaction: P25037; IntAct: EBI-10420,EBI-19819; Score: 0.35
DE  Interaction: Q06682; IntAct: EBI-32041,EBI-10420; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-10420,EBI-14372; Score: 0.35
DE  Interaction: P03962; IntAct: EBI-14397,EBI-10420; Score: 0.35
DE  Interaction: P25386; IntAct: EBI-20157,EBI-10420; Score: 0.35
DE  Interaction: P35194; IntAct: EBI-10420,EBI-1871; Score: 0.35
DE  Interaction: P53254; IntAct: EBI-1878,EBI-10420; Score: 0.35
DE  Interaction: Q06679; IntAct: EBI-35712,EBI-10420; Score: 0.35
DE  Interaction: Q07468; IntAct: EBI-20422,EBI-10420; Score: 0.35
DE  Interaction: P40522; IntAct: EBI-10420,EBI-25035; Score: 0.35
DE  Interaction: Q06337; IntAct: EBI-10420,EBI-35867; Score: 0.35
DE  Interaction: P40157; IntAct: EBI-10420,EBI-29136; Score: 0.35
DE  Interaction: P40547; IntAct: EBI-10420,EBI-24957; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-20254,EBI-10420; Score: 0.35
DE  Interaction: P23643; IntAct: EBI-10420,EBI-20469; Score: 0.35
DE  Interaction: Q03433; IntAct: EBI-10420,EBI-27814; Score: 0.35
DE  Interaction: P40438; IntAct: EBI-3662633,EBI-10420; Score: 0.35
DE  Interaction: P40890; IntAct: EBI-10420,EBI-26271; Score: 0.35
DE  Interaction: P33767; IntAct: EBI-12658,EBI-10420; Score: 0.35
DE  Interaction: Q12416; IntAct: EBI-10420,EBI-29963; Score: 0.35
DE  Interaction: P38749; IntAct: EBI-10420,EBI-24313; Score: 0.35
DE  Interaction: O13527; IntAct: EBI-33845,EBI-10420; Score: 0.35
DE  Interaction: P40017; IntAct: EBI-2345299,EBI-10420; Score: 0.35
DE  Interaction: P34220; IntAct: EBI-3759231,EBI-10420; Score: 0.35
DE  Interaction: P34225; IntAct: EBI-10420,EBI-2344464; Score: 0.35
DE  Interaction: Q12491; IntAct: EBI-10420,EBI-3767258; Score: 0.35
DE  Interaction: Q12193; IntAct: EBI-10420,EBI-38876; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-21409,EBI-10420; Score: 0.35
DE  Interaction: P38266; IntAct: EBI-21584,EBI-10420; Score: 0.35
DE  Interaction: P38331; IntAct: EBI-21083,EBI-10420; Score: 0.35
DE  Interaction: P38332; IntAct: EBI-21094,EBI-10420; Score: 0.35
DE  Interaction: P39109; IntAct: EBI-10420,EBI-21779; Score: 0.35
DE  Interaction: P25616; IntAct: EBI-21864,EBI-10420; Score: 0.35
DE  Interaction: Q06156; IntAct: EBI-10420,EBI-4785; Score: 0.35
DE  Interaction: Q07349; IntAct: EBI-10420,EBI-3698596; Score: 0.35
DE  Interaction: Q12516; IntAct: EBI-10420,EBI-38546; Score: 0.35
DE  Interaction: Q06640; IntAct: EBI-34097,EBI-10420; Score: 0.35
DE  Interaction: Q04411; IntAct: EBI-10420,EBI-36153; Score: 0.35
DE  Interaction: Q3E7X8; IntAct: EBI-3763343,EBI-10420; Score: 0.35
DE  Interaction: P40028; IntAct: EBI-22514,EBI-10420; Score: 0.35
DE  Interaction: P40085; IntAct: EBI-10420,EBI-22717; Score: 0.35
DE  Interaction: P43560; IntAct: EBI-22832,EBI-10420; Score: 0.35
DE  Interaction: P43597; IntAct: EBI-10420,EBI-22951; Score: 0.35
DE  Interaction: P53144; IntAct: EBI-10420,EBI-23891; Score: 0.35
DE  Interaction: P53100; IntAct: EBI-24104,EBI-10420; Score: 0.35
DE  Interaction: P53077; IntAct: EBI-24169,EBI-10420; Score: 0.35
DE  Interaction: P53234; IntAct: EBI-10420,EBI-23168; Score: 0.35
DE  Interaction: P53246; IntAct: EBI-10420,EBI-23209; Score: 0.35
DE  Interaction: Q99315; IntAct: EBI-3767461,EBI-10420; Score: 0.35
DE  Interaction: P50089; IntAct: EBI-10420,EBI-23545; Score: 0.35
DE  Interaction: P53321; IntAct: EBI-23598,EBI-10420; Score: 0.35
DE  Interaction: Q05900; IntAct: EBI-10420,EBI-754; Score: 0.35
DE  Interaction: P0C2J7; IntAct: EBI-10420,EBI-3761931; Score: 0.35
DE  Interaction: P38842; IntAct: EBI-10420,EBI-24752; Score: 0.35
DE  Interaction: P47024; IntAct: EBI-26039,EBI-10420; Score: 0.35
DE  Interaction: P47101; IntAct: EBI-10420,EBI-25467; Score: 0.35
DE  Interaction: P28320; IntAct: EBI-10420,EBI-26795; Score: 0.35
DE  Interaction: P34246; IntAct: EBI-10420,EBI-26803; Score: 0.35
DE  Interaction: P34248; IntAct: EBI-26807,EBI-10420; Score: 0.35
DE  Interaction: P28273; IntAct: EBI-27022,EBI-10420; Score: 0.35
DE  Interaction: P36158; IntAct: EBI-2936913,EBI-10420; Score: 0.35
DE  Interaction: Q07799; IntAct: EBI-38901,EBI-10420; Score: 0.35
DE  Interaction: Q12244; IntAct: EBI-10420,EBI-35601; Score: 0.35
DE  Interaction: Q12177; IntAct: EBI-30090,EBI-10420; Score: 0.35
DE  Interaction: Q07897; IntAct: EBI-10420,EBI-37851; Score: 0.35
DE  Interaction: Q12110; IntAct: EBI-33635,EBI-10420; Score: 0.35
DE  Interaction: Q12288; IntAct: EBI-10420,EBI-3767612; Score: 0.35
DE  Interaction: Q06247; IntAct: EBI-10420,EBI-38452; Score: 0.35
DE  Interaction: Q06152; IntAct: EBI-10420,EBI-35313; Score: 0.35
DE  Interaction: Q05867; IntAct: EBI-10420,EBI-36496; Score: 0.35
DE  Interaction: Q06159; IntAct: EBI-33888,EBI-10420; Score: 0.35
DE  Interaction: Q06479; IntAct: EBI-35627,EBI-10420; Score: 0.35
DE  Interaction: Q06409; IntAct: EBI-35964,EBI-10420; Score: 0.35
DE  Interaction: O13577; IntAct: EBI-34501,EBI-10420; Score: 0.35
DE  Interaction: Q04533; IntAct: EBI-10420,EBI-10803; Score: 0.35
DE  Interaction: Q04371; IntAct: EBI-10420,EBI-28049; Score: 0.35
DE  Interaction: P0CF18; IntAct: EBI-3767696,EBI-10420; Score: 0.35
DE  Interaction: Q03153; IntAct: EBI-28199,EBI-10420; Score: 0.35
DE  Interaction: Q04471; IntAct: EBI-10420,EBI-27220; Score: 0.35
DE  Interaction: Q03496; IntAct: EBI-10420,EBI-3654556; Score: 0.35
DE  Interaction: P40168; IntAct: EBI-10420,EBI-3767735; Score: 0.35
DE  Interaction: P53852; IntAct: EBI-10420,EBI-29230; Score: 0.35
DE  Interaction: P53850; IntAct: EBI-3767755,EBI-10420; Score: 0.35
DE  Interaction: P53837; IntAct: EBI-10420,EBI-28271; Score: 0.35
DE  Interaction: P53756; IntAct: EBI-10420,EBI-28581; Score: 0.35
DE  Interaction: P53757; IntAct: EBI-10420,EBI-28586; Score: 0.35
DE  Interaction: Q99247; IntAct: EBI-34003,EBI-10420; Score: 0.53
DE  Interaction: Q12496; IntAct: EBI-29300,EBI-10420; Score: 0.35
DE  Interaction: Q08270; IntAct: EBI-35014,EBI-10420; Score: 0.35
DE  Interaction: Q08457; IntAct: EBI-36267,EBI-10420; Score: 0.35
DE  Interaction: Q12275; IntAct: EBI-10420,EBI-33858; Score: 0.35
DE  Interaction: P53049; IntAct: EBI-29324,EBI-10420; Score: 0.35
DE  Interaction: Q12032; IntAct: EBI-32069,EBI-10420; Score: 0.35
DE  Interaction: Q08748; IntAct: EBI-2050125,EBI-10420; Score: 0.35
DE  Interaction: Q02754; IntAct: EBI-10420,EBI-34779; Score: 0.35
DE  Interaction: Q02895; IntAct: EBI-35030,EBI-10420; Score: 0.35
DE  Interaction: Q08964; IntAct: EBI-38118,EBI-10420; Score: 0.35
DE  Interaction: Q06813; IntAct: EBI-38252,EBI-10420; Score: 0.35
DE  Interaction: Q06108; IntAct: EBI-10420,EBI-38709; Score: 0.35
DE  Interaction: P01123; IntAct: EBI-29496,EBI-10420; Score: 0.35
DE  Interaction: P51996; IntAct: EBI-29384,EBI-10420; Score: 0.35
DE  Interaction: P36019; IntAct: EBI-29415,EBI-10420; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-10420,EBI-29516; Score: 0.35
DE  Interaction: P53819; IntAct: EBI-2103894,EBI-10420; Score: 0.35
DE  Interaction: P40341; IntAct: EBI-14858,EBI-10420; Score: 0.35
DE  Interaction: P40328; IntAct: EBI-19022,EBI-10420; Score: 0.35
DE  Interaction: P40340; IntAct: EBI-10420,EBI-19030; Score: 0.35
DE  Interaction: P31111; IntAct: EBI-29645,EBI-10420; Score: 0.35
DE  Interaction: P22202; IntAct: EBI-10420,EBI-8621; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-8611,EBI-10420; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-10420,EBI-22339; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-10420; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-10420,EBI-8050; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-10420; Score: 0.35
DE  Interaction: P32048; IntAct: EBI-10420,EBI-18739; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-10420,EBI-8973; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-8555,EBI-10420; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-10420; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-10420,EBI-8648; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-10420; Score: 0.35
DE  Interaction: P42884; IntAct: EBI-1994,EBI-10420; Score: 0.35
DE  Interaction: P37898; IntAct: EBI-10420,EBI-1998; Score: 0.35
DE  Interaction: Q03266; IntAct: EBI-27624,EBI-10420; Score: 0.35
DE  Interaction: Q00955; IntAct: EBI-10420,EBI-4814; Score: 0.35
DE  Interaction: P21192; IntAct: EBI-2073,EBI-10420; Score: 0.35
DE  Interaction: Q07622; IntAct: EBI-10420,EBI-38674; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-2169,EBI-10420; Score: 0.35
DE  Interaction: Q07732; IntAct: EBI-33406,EBI-10420; Score: 0.35
DE  Interaction: P22136; IntAct: EBI-3318,EBI-10420; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-37072,EBI-10420; Score: 0.35
DE  Interaction: P03875; IntAct: EBI-10420,EBI-46469; Score: 0.35
DE  Interaction: Q9ZZX1; IntAct: EBI-10420,EBI-3758055; Score: 0.35
DE  Interaction: Q12013; IntAct: EBI-10420,EBI-34438; Score: 0.35
DE  Interaction: P47029; IntAct: EBI-25974,EBI-10420; Score: 0.35
DE  Interaction: P22108; IntAct: EBI-10420,EBI-2635; Score: 0.35
DE  Interaction: Q04601; IntAct: EBI-32842,EBI-10420; Score: 0.35
DE  Interaction: P38281; IntAct: EBI-20838,EBI-10420; Score: 0.35
DE  Interaction: P27351; IntAct: EBI-2202,EBI-10420; Score: 0.35
DE  Interaction: P38065; IntAct: EBI-10420,EBI-2181; Score: 0.35
DE  Interaction: Q08951; IntAct: EBI-10420,EBI-29702; Score: 0.35
DE  Interaction: P11076; IntAct: EBI-2816,EBI-10420; Score: 0.35
DE  Interaction: P04076; IntAct: EBI-10420,EBI-2877; Score: 0.35
DE  Interaction: P38116; IntAct: EBI-2869,EBI-10420; Score: 0.35
DE  Interaction: P08566; IntAct: EBI-2883,EBI-10420; Score: 0.35
DE  Interaction: Q04052; IntAct: EBI-2045173,EBI-10420; Score: 0.35
DE  Interaction: P34233; IntAct: EBI-10420,EBI-3027; Score: 0.35
DE  Interaction: P53983; IntAct: EBI-10420,EBI-28603; Score: 0.35
DE  Interaction: P39945; IntAct: EBI-10420,EBI-3066; Score: 0.35
DE  Interaction: Q12527; IntAct: EBI-10420,EBI-31977; Score: 0.35
DE  Interaction: P53855; IntAct: EBI-29212,EBI-10420; Score: 0.35
DE  Interaction: Q12142; IntAct: EBI-34628,EBI-10420; Score: 0.35
DE  Interaction: P32453; IntAct: EBI-3306,EBI-10420; Score: 0.35
DE  Interaction: Q08236; IntAct: EBI-10420,EBI-29284; Score: 0.35
DE  Interaction: P47068; IntAct: EBI-10420,EBI-3437; Score: 0.35
DE  Interaction: Q01389; IntAct: EBI-10420,EBI-3470; Score: 0.35
DE  Interaction: P46678; IntAct: EBI-10420,EBI-19164; Score: 0.35
DE  Interaction: Q08347; IntAct: EBI-10420,EBI-3763789; Score: 0.35
DE  Interaction: P39960; IntAct: EBI-3517,EBI-10420; Score: 0.35
DE  Interaction: P43583; IntAct: EBI-22761,EBI-10420; Score: 0.35
DE  Interaction: Q08965; IntAct: EBI-10420,EBI-3683; Score: 0.35
DE  Interaction: P47125; IntAct: EBI-10420,EBI-25538; Score: 0.35
DE  Interaction: P41832; IntAct: EBI-10420,EBI-3692; Score: 0.35
DE  Interaction: P40450; IntAct: EBI-3711,EBI-10420; Score: 0.35
DE  Interaction: P38041; IntAct: EBI-10420,EBI-3719; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-3727,EBI-10420; Score: 0.35
DE  Interaction: P25385; IntAct: EBI-10420,EBI-3735; Score: 0.35
DE  Interaction: P25356; IntAct: EBI-10420,EBI-3708933; Score: 0.35
DE  Interaction: P33314; IntAct: EBI-3835,EBI-10420; Score: 0.35
DE  Interaction: P41697; IntAct: EBI-3857,EBI-10420; Score: 0.35
DE  Interaction: P48524; IntAct: EBI-3881,EBI-10420; Score: 0.35
DE  Interaction: P53280; IntAct: EBI-10420,EBI-23322; Score: 0.35
DE  Interaction: P29547; IntAct: EBI-10420,EBI-6323; Score: 0.35
DE  Interaction: P28495; IntAct: EBI-10420,EBI-4003; Score: 0.35
DE  Interaction: P53894; IntAct: EBI-10420,EBI-4110; Score: 0.35
DE  Interaction: P38626; IntAct: EBI-2048224,EBI-10420; Score: 0.35
DE  Interaction: Q03702; IntAct: EBI-4363,EBI-10420; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-10420,EBI-9890; Score: 0.35
DE  Interaction: P26309; IntAct: EBI-4212,EBI-10420; Score: 0.53
DE  Interaction: P06785; IntAct: EBI-10420,EBI-19690; Score: 0.35
DE  Interaction: P25655; IntAct: EBI-12139,EBI-10420; Score: 0.35
DE  Interaction: P07834; IntAct: EBI-4434,EBI-10420; Score: 0.35
DE  Interaction: Q08032; IntAct: EBI-4292,EBI-10420; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-10420,EBI-4308; Score: 0.35
DE  Interaction: P30665; IntAct: EBI-4326,EBI-10420; Score: 0.35
DE  Interaction: P39525; IntAct: EBI-10420,EBI-4467; Score: 0.35
DE  Interaction: O13297; IntAct: EBI-10420,EBI-4473; Score: 0.35
DE  Interaction: Q12453; IntAct: EBI-10420,EBI-31271; Score: 0.35
DE  Interaction: Q06632; IntAct: EBI-10420,EBI-32872; Score: 0.35
DE  Interaction: P32657; IntAct: EBI-10420,EBI-4574; Score: 0.35
DE  Interaction: P22516; IntAct: EBI-10420,EBI-4600; Score: 0.35
DE  Interaction: P29465; IntAct: EBI-4632,EBI-10420; Score: 0.35
DE  Interaction: P38779; IntAct: EBI-10420,EBI-24538; Score: 0.35
DE  Interaction: P40987; IntAct: EBI-10420,EBI-4665; Score: 0.35
DE  Interaction: P27895; IntAct: EBI-4687,EBI-10420; Score: 0.35
DE  Interaction: P20485; IntAct: EBI-9699,EBI-10420; Score: 0.35
DE  Interaction: P48562; IntAct: EBI-10420,EBI-4750; Score: 0.35
DE  Interaction: Q08685; IntAct: EBI-10420,EBI-29732; Score: 0.35
DE  Interaction: Q03690; IntAct: EBI-10420,EBI-8989; Score: 0.35
DE  Interaction: P06787; IntAct: EBI-3976,EBI-10420; Score: 0.35
DE  Interaction: P23287; IntAct: EBI-10420,EBI-12771; Score: 0.53
DE  Interaction: Q04632; IntAct: EBI-6035,EBI-10420; Score: 0.35
DE  Interaction: P53622; IntAct: EBI-10420,EBI-4860; Score: 0.35
DE  Interaction: P49017; IntAct: EBI-4937,EBI-10420; Score: 0.35
DE  Interaction: Q04935; IntAct: EBI-36910,EBI-10420; Score: 0.35
DE  Interaction: P23285; IntAct: EBI-5448,EBI-10420; Score: 0.35
DE  Interaction: P33307; IntAct: EBI-10420,EBI-5168; Score: 0.35
DE  Interaction: Q12734; IntAct: EBI-10420,EBI-32379; Score: 0.35
DE  Interaction: Q01454; IntAct: EBI-10420,EBI-5209; Score: 0.35
DE  Interaction: P89105; IntAct: EBI-5283,EBI-10420; Score: 0.56
DE  Interaction: P53008; IntAct: EBI-10420,EBI-5323; Score: 0.35
DE  Interaction: P32898; IntAct: EBI-10420,EBI-22092; Score: 0.35
DE  Interaction: P08678; IntAct: EBI-10420,EBI-5364; Score: 0.35
DE  Interaction: P32582; IntAct: EBI-10420,EBI-4167; Score: 0.35
DE  Interaction: Q12389; IntAct: EBI-10420,EBI-5644; Score: 0.35
DE  Interaction: Q06151; IntAct: EBI-10420,EBI-38973; Score: 0.35
DE  Interaction: P06634; IntAct: EBI-10420,EBI-5744; Score: 0.35
DE  Interaction: Q08496; IntAct: EBI-31943,EBI-10420; Score: 0.53
DE  Interaction: P25453; IntAct: EBI-10420,EBI-5955; Score: 0.53
DE  Interaction: P38859; IntAct: EBI-5973,EBI-10420; Score: 0.35
DE  Interaction: Q12675; IntAct: EBI-10420,EBI-3114; Score: 0.35
DE  Interaction: Q12674; IntAct: EBI-3142,EBI-10420; Score: 0.35
DE  Interaction: Q08387; IntAct: EBI-10420,EBI-5983; Score: 0.35
DE  Interaction: P54861; IntAct: EBI-6002,EBI-10420; Score: 0.35
DE  Interaction: Q05610; IntAct: EBI-10420,EBI-31191; Score: 0.35
DE  Interaction: Q03921; IntAct: EBI-10420,EBI-34442; Score: 0.35
DE  Interaction: P24482; IntAct: EBI-10420,EBI-6071; Score: 0.35
DE  Interaction: P53847; IntAct: EBI-10420,EBI-29249; Score: 0.35
DE  Interaction: P38149; IntAct: EBI-21176,EBI-10420; Score: 0.35
DE  Interaction: Q12432; IntAct: EBI-10420,EBI-6281; Score: 0.35
DE  Interaction: Q04110; IntAct: EBI-10420,EBI-37150; Score: 0.35
DE  Interaction: Q04217; IntAct: EBI-10420,EBI-1820; Score: 0.35
DE  Interaction: Q05958; IntAct: EBI-38445,EBI-10420; Score: 0.35
DE  Interaction: P32525; IntAct: EBI-10420,EBI-26215; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-10420,EBI-24359; Score: 0.51
DE  Interaction: Q06673; IntAct: EBI-34554,EBI-10420; Score: 0.35
DE  Interaction: Q03214; IntAct: EBI-10420,EBI-27382; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-10420,EBI-6333; Score: 0.35
DE  Interaction: P40557; IntAct: EBI-24929,EBI-10420; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-10420,EBI-5127; Score: 0.35
DE  Interaction: Q03018; IntAct: EBI-10420,EBI-6657; Score: 0.35
DE  Interaction: Q06163; IntAct: EBI-10420,EBI-3764464; Score: 0.35
DE  Interaction: P34756; IntAct: EBI-6754,EBI-10420; Score: 0.35
DE  Interaction: P53971; IntAct: EBI-28638,EBI-10420; Score: 0.35
DE  Interaction: P46671; IntAct: EBI-10420,EBI-6789; Score: 0.35
DE  Interaction: P19097; IntAct: EBI-6806,EBI-10420; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-10420,EBI-2447; Score: 0.35
DE  Interaction: P39521; IntAct: EBI-6897,EBI-10420; Score: 0.35
DE  Interaction: P32785; IntAct: EBI-7033,EBI-10420; Score: 0.35
DE  Interaction: P53848; IntAct: EBI-10420,EBI-6812; Score: 0.35
DE  Interaction: P38911; IntAct: EBI-6951,EBI-10420; Score: 0.35
DE  Interaction: Q12333; IntAct: EBI-7128,EBI-10420; Score: 0.35
DE  Interaction: P31380; IntAct: EBI-20621,EBI-10420; Score: 0.35
DE  Interaction: P46949; IntAct: EBI-23450,EBI-10420; Score: 0.35
DE  Interaction: P38297; IntAct: EBI-10420,EBI-20900; Score: 0.35
DE  Interaction: P09032; IntAct: EBI-10420,EBI-6275; Score: 0.35
DE  Interaction: P32481; IntAct: EBI-8924,EBI-10420; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-6270,EBI-10420; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-10420,EBI-7442; Score: 0.51
DE  Interaction: Q03330; IntAct: EBI-10420,EBI-7458; Score: 0.35
DE  Interaction: Q06625; IntAct: EBI-10420,EBI-37861; Score: 0.35
DE  Interaction: P47102; IntAct: EBI-10420,EBI-7539; Score: 0.35
DE  Interaction: P53192; IntAct: EBI-10420,EBI-23722; Score: 0.35
DE  Interaction: Q03016; IntAct: EBI-10420,EBI-33380; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-10420,EBI-7727; Score: 0.35
DE  Interaction: P08539; IntAct: EBI-7376,EBI-10420; Score: 0.35
DE  Interaction: P41911; IntAct: EBI-7791,EBI-10420; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-13517,EBI-10420; Score: 0.35
DE  Interaction: P25373; IntAct: EBI-7903,EBI-10420; Score: 0.35
DE  Interaction: P32477; IntAct: EBI-10420,EBI-7910; Score: 0.35
DE  Interaction: P48239; IntAct: EBI-10420,EBI-23378; Score: 0.35
DE  Interaction: Q08929; IntAct: EBI-10420,EBI-3764709; Score: 0.35
DE  Interaction: Q05775; IntAct: EBI-8944,EBI-10420; Score: 0.35
DE  Interaction: P40012; IntAct: EBI-3689057,EBI-10420; Score: 0.35
DE  Interaction: P32874; IntAct: EBI-8281,EBI-10420; Score: 0.35
DE  Interaction: P48362; IntAct: EBI-8304,EBI-10420; Score: 0.35
DE  Interaction: P02309; IntAct: EBI-8113,EBI-10420; Score: 0.35
DE  Interaction: P33734; IntAct: EBI-8342,EBI-10420; Score: 0.35
DE  Interaction: Q08702; IntAct: EBI-10420,EBI-30129; Score: 0.35
DE  Interaction: Q05080; IntAct: EBI-10420,EBI-5412; Score: 0.35
DE  Interaction: P40480; IntAct: EBI-8492,EBI-10420; Score: 0.35
DE  Interaction: Q05787; IntAct: EBI-10420,EBI-31647; Score: 0.35
DE  Interaction: Q05549; IntAct: EBI-3671253,EBI-10420; Score: 0.35
DE  Interaction: Q12385; IntAct: EBI-10420,EBI-32624; Score: 0.35
DE  Interaction: P53982; IntAct: EBI-8892,EBI-10420; Score: 0.35
DE  Interaction: P25038; IntAct: EBI-10420,EBI-2067334; Score: 0.35
DE  Interaction: P53897; IntAct: EBI-10420,EBI-28967; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-9068,EBI-10420; Score: 0.35
DE  Interaction: P25605; IntAct: EBI-9087,EBI-10420; Score: 0.35
DE  Interaction: P25642; IntAct: EBI-9217,EBI-10420; Score: 0.35
DE  Interaction: Q06704; IntAct: EBI-10420,EBI-33343; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-25710,EBI-10420; Score: 0.35
DE  Interaction: P50942; IntAct: EBI-28834,EBI-10420; Score: 0.35
DE  Interaction: Q12271; IntAct: EBI-36688,EBI-10420; Score: 0.35
DE  Interaction: Q08227; IntAct: EBI-10420,EBI-38678; Score: 0.35
DE  Interaction: P47056; IntAct: EBI-10420,EBI-3764906; Score: 0.35
DE  Interaction: Q07843; IntAct: EBI-10420,EBI-32747; Score: 0.35
DE  Interaction: Q06554; IntAct: EBI-10420,EBI-31528; Score: 0.35
DE  Interaction: P40541; IntAct: EBI-10420,EBI-16667; Score: 0.35
DE  Interaction: P38250; IntAct: EBI-10420,EBI-21520; Score: 0.35
DE  Interaction: P38144; IntAct: EBI-21087,EBI-10420; Score: 0.35
DE  Interaction: P53125; IntAct: EBI-23967,EBI-10420; Score: 0.35
DE  Interaction: Q12358; IntAct: EBI-10420,EBI-27164; Score: 0.35
DE  Interaction: P32767; IntAct: EBI-10420,EBI-13044; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-9619,EBI-10420; Score: 0.35
DE  Interaction: P28742; IntAct: EBI-9740,EBI-10420; Score: 0.35
DE  Interaction: P32350; IntAct: EBI-10420,EBI-9834; Score: 0.35
DE  Interaction: P38873; IntAct: EBI-10420,EBI-24864; Score: 0.35
DE  Interaction: P27810; IntAct: EBI-10420,EBI-2069227; Score: 0.35
DE  Interaction: P38130; IntAct: EBI-9987,EBI-10420; Score: 0.35
DE  Interaction: Q08963; IntAct: EBI-594,EBI-10420; Score: 0.35
DE  Interaction: P53598; IntAct: EBI-18506,EBI-10420; Score: 0.35
DE  Interaction: P53312; IntAct: EBI-10420,EBI-18513; Score: 0.35
DE  Interaction: P07866; IntAct: EBI-10420,EBI-10243; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-25128,EBI-10420; Score: 0.35
DE  Interaction: P40957; IntAct: EBI-10420,EBI-10354; Score: 0.35
DE  Interaction: P29469; IntAct: EBI-10420,EBI-10533; Score: 0.35
DE  Interaction: P24279; IntAct: EBI-10420,EBI-10541; Score: 0.35
DE  Interaction: Q01846; IntAct: EBI-10420,EBI-10626; Score: 0.35
DE  Interaction: P38111; IntAct: EBI-10420,EBI-6668; Score: 0.35
DE  Interaction: P05694; IntAct: EBI-10782,EBI-10420; Score: 0.35
DE  Interaction: P43638; IntAct: EBI-10420,EBI-10880; Score: 0.35
DE  Interaction: P36046; IntAct: EBI-10420,EBI-26978; Score: 0.53
DE  Interaction: P38760; IntAct: EBI-24454,EBI-10420; Score: 0.35
DE  Interaction: P40850; IntAct: EBI-10983,EBI-10420; Score: 0.35
DE  Interaction: Q07980; IntAct: EBI-10420,EBI-33369; Score: 0.35
DE  Interaction: Q12083; IntAct: EBI-31634,EBI-10420; Score: 0.35
DE  Interaction: Q02455; IntAct: EBI-10420,EBI-11009; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-25261,EBI-10420; Score: 0.35
DE  Interaction: P36044; IntAct: EBI-11072,EBI-10420; Score: 0.35
DE  Interaction: P07884; IntAct: EBI-11135,EBI-10420; Score: 0.35
DE  Interaction: P32333; IntAct: EBI-11152,EBI-10420; Score: 0.35
DE  Interaction: Q12404; IntAct: EBI-10420,EBI-11184; Score: 0.35
DE  Interaction: P53159; IntAct: EBI-10420,EBI-23834; Score: 0.35
DE  Interaction: P32829; IntAct: EBI-11255,EBI-10420; Score: 0.35
DE  Interaction: Q06815; IntAct: EBI-10420,EBI-33784; Score: 0.35
DE  Interaction: P38175; IntAct: EBI-21331,EBI-10420; Score: 0.35
DE  Interaction: P36525; IntAct: EBI-15545,EBI-10420; Score: 0.35
DE  Interaction: P36534; IntAct: EBI-15595,EBI-10420; Score: 0.35
DE  Interaction: P21771; IntAct: EBI-16288,EBI-10420; Score: 0.35
DE  Interaction: P48525; IntAct: EBI-18669,EBI-10420; Score: 0.35
DE  Interaction: P25846; IntAct: EBI-10420,EBI-11347; Score: 0.53
DE  Interaction: Q03834; IntAct: EBI-11383,EBI-10420; Score: 0.35
DE  Interaction: P22438; IntAct: EBI-10420,EBI-18768; Score: 0.35
DE  Interaction: P52918; IntAct: EBI-10420,EBI-11420; Score: 0.35
DE  Interaction: P38714; IntAct: EBI-18800,EBI-10420; Score: 0.35
DE  Interaction: P38994; IntAct: EBI-11460,EBI-10420; Score: 0.35
DE  Interaction: Q03151; IntAct: EBI-10420,EBI-28195; Score: 0.35
DE  Interaction: Q03920; IntAct: EBI-10420,EBI-31378; Score: 0.35
DE  Interaction: P40959; IntAct: EBI-10420,EBI-11636; Score: 0.35
DE  Interaction: P08964; IntAct: EBI-10420,EBI-11650; Score: 0.35
DE  Interaction: P36006; IntAct: EBI-10420,EBI-11670; Score: 0.35
DE  Interaction: P27929; IntAct: EBI-11843,EBI-10420; Score: 0.35
DE  Interaction: P25293; IntAct: EBI-11850,EBI-10420; Score: 0.35
DE  Interaction: Q07500; IntAct: EBI-10420,EBI-38178; Score: 0.35
DE  Interaction: P40527; IntAct: EBI-3137,EBI-10420; Score: 0.35
DE  Interaction: P32497; IntAct: EBI-10420,EBI-8965; Score: 0.35
DE  Interaction: P33420; IntAct: EBI-10420,EBI-12049; Score: 0.35
DE  Interaction: P38798; IntAct: EBI-12071,EBI-10420; Score: 0.35
DE  Interaction: Q99207; IntAct: EBI-35157,EBI-10420; Score: 0.35
DE  Interaction: P39683; IntAct: EBI-12218,EBI-10420; Score: 0.35
DE  Interaction: P43124; IntAct: EBI-14410,EBI-10420; Score: 0.35
DE  Interaction: P40064; IntAct: EBI-11740,EBI-10420; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-10420,EBI-11756; Score: 0.35
DE  Interaction: Q00684; IntAct: EBI-10420,EBI-4192; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-28814,EBI-10420; Score: 0.35
DE  Interaction: P53397; IntAct: EBI-10420,EBI-12494; Score: 0.35
DE  Interaction: P16547; IntAct: EBI-12546,EBI-10420; Score: 0.35
DE  Interaction: P21375; IntAct: EBI-10420,EBI-12646; Score: 0.35
DE  Interaction: P40512; IntAct: EBI-10420,EBI-25069; Score: 0.35
DE  Interaction: P40186; IntAct: EBI-10420,EBI-25021; Score: 0.35
DE  Interaction: Q12477; IntAct: EBI-10420,EBI-38090; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-10420,EBI-5687; Score: 0.35
DE  Interaction: P27801; IntAct: EBI-13130,EBI-10420; Score: 0.35
DE  Interaction: P12868; IntAct: EBI-10420,EBI-6450; Score: 0.35
DE  Interaction: P08468; IntAct: EBI-10420,EBI-14086; Score: 0.35
DE  Interaction: P32606; IntAct: EBI-10420,EBI-14109; Score: 0.35
DE  Interaction: P53112; IntAct: EBI-10420,EBI-13212; Score: 0.35
DE  Interaction: P35056; IntAct: EBI-10420,EBI-13170; Score: 0.35
DE  Interaction: P53248; IntAct: EBI-13187,EBI-10420; Score: 0.35
DE  Interaction: P40433; IntAct: EBI-10420,EBI-1956; Score: 0.35
DE  Interaction: P36093; IntAct: EBI-13366,EBI-10420; Score: 0.35
DE  Interaction: Q12252; IntAct: EBI-34575,EBI-10420; Score: 0.35
DE  Interaction: P19881; IntAct: EBI-35376,EBI-10420; Score: 0.35
DE  Interaction: P20052; IntAct: EBI-10420,EBI-13310; Score: 0.35
DE  Interaction: P38264; IntAct: EBI-13350,EBI-10420; Score: 0.35
DE  Interaction: P07271; IntAct: EBI-13404,EBI-10420; Score: 0.35
DE  Interaction: P24583; IntAct: EBI-9860,EBI-10420; Score: 0.35
DE  Interaction: Q03306; IntAct: EBI-10420,EBI-37683; Score: 0.35
DE  Interaction: P32634; IntAct: EBI-10420,EBI-22695; Score: 0.35
DE  Interaction: P33775; IntAct: EBI-10420,EBI-13567; Score: 0.35
DE  Interaction: P21951; IntAct: EBI-10420,EBI-6140; Score: 0.35
DE  Interaction: P39008; IntAct: EBI-10420,EBI-13629; Score: 0.35
DE  Interaction: P40478; IntAct: EBI-3765704,EBI-10420; Score: 0.35
DE  Interaction: P27796; IntAct: EBI-19236,EBI-10420; Score: 0.35
DE  Interaction: P07272; IntAct: EBI-10420,EBI-13792; Score: 0.35
DE  Interaction: P09232; IntAct: EBI-10420,EBI-13925; Score: 0.35
DE  Interaction: P21242; IntAct: EBI-10420,EBI-13963; Score: 0.35
DE  Interaction: P23638; IntAct: EBI-13967,EBI-10420; Score: 0.35
DE  Interaction: P54885; IntAct: EBI-10420,EBI-13872; Score: 0.35
DE  Interaction: P24384; IntAct: EBI-13853,EBI-10420; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-465,EBI-10420; Score: 0.35
DE  Interaction: P31374; IntAct: EBI-10420,EBI-9442; Score: 0.35
DE  Interaction: Q08217; IntAct: EBI-10420,EBI-9839; Score: 0.35
DE  Interaction: P36082; IntAct: EBI-10420,EBI-26754; Score: 0.35
DE  Interaction: P40164; IntAct: EBI-29107,EBI-10420; Score: 0.35
DE  Interaction: Q04373; IntAct: EBI-10420,EBI-33208; Score: 0.35
DE  Interaction: Q08647; IntAct: EBI-29265,EBI-10420; Score: 0.35
DE  Interaction: P52489; IntAct: EBI-10420,EBI-9895; Score: 0.35
DE  Interaction: P40352; IntAct: EBI-10420,EBI-14687; Score: 0.35
DE  Interaction: P14736; IntAct: EBI-10420,EBI-14766; Score: 0.35
DE  Interaction: P32849; IntAct: EBI-10420,EBI-14773; Score: 0.35
DE  Interaction: P12753; IntAct: EBI-10420,EBI-14700; Score: 0.53
DE  Interaction: P53063; IntAct: EBI-24206,EBI-10420; Score: 0.35
DE  Interaction: Q02792; IntAct: EBI-14845,EBI-10420; Score: 0.35
DE  Interaction: P47104; IntAct: EBI-10420,EBI-25471; Score: 0.35
DE  Interaction: P25332; IntAct: EBI-10420,EBI-14854; Score: 0.35
DE  Interaction: P39531; IntAct: EBI-10420,EBI-26224; Score: 0.35
DE  Interaction: P12689; IntAct: EBI-14951,EBI-10420; Score: 0.35
DE  Interaction: P14284; IntAct: EBI-6155,EBI-10420; Score: 0.35
DE  Interaction: Q12090; IntAct: EBI-2083048,EBI-10420; Score: 0.35
DE  Interaction: P38629; IntAct: EBI-15000,EBI-10420; Score: 0.35
DE  Interaction: Q06407; IntAct: EBI-15060,EBI-10420; Score: 0.35
DE  Interaction: P19263; IntAct: EBI-15087,EBI-10420; Score: 0.35
DE  Interaction: P40395; IntAct: EBI-15183,EBI-10420; Score: 0.35
DE  Interaction: P29539; IntAct: EBI-10420,EBI-2083307; Score: 0.35
DE  Interaction: P32445; IntAct: EBI-10420,EBI-15206; Score: 0.35
DE  Interaction: P43565; IntAct: EBI-10420,EBI-15150; Score: 0.35
DE  Interaction: Q08562; IntAct: EBI-36902,EBI-10420; Score: 0.35
DE  Interaction: Q08961; IntAct: EBI-30703,EBI-10420; Score: 0.35
DE  Interaction: Q03942; IntAct: EBI-10420,EBI-32816; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-15475,EBI-10420; Score: 0.35
DE  Interaction: P39975; IntAct: EBI-10420,EBI-22419; Score: 0.35
DE  Interaction: P32611; IntAct: EBI-10420,EBI-22374; Score: 0.35
DE  Interaction: Q04740; IntAct: EBI-15658,EBI-10420; Score: 0.35
DE  Interaction: P21672; IntAct: EBI-10420,EBI-15246; Score: 0.53
DE  Interaction: P49723; IntAct: EBI-10420,EBI-15251; Score: 0.35
DE  Interaction: P51862; IntAct: EBI-10420,EBI-15702; Score: 0.35
DE  Interaction: P08518; IntAct: EBI-15767,EBI-10420; Score: 0.35
DE  Interaction: P32910; IntAct: EBI-15835,EBI-10420; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-15881,EBI-10420; Score: 0.35
DE  Interaction: P38249; IntAct: EBI-10420,EBI-8981; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-14480,EBI-10420; Score: 0.35
DE  Interaction: P54780; IntAct: EBI-10420,EBI-14485; Score: 0.35
DE  Interaction: P14126; IntAct: EBI-15364,EBI-10420; Score: 0.35
DE  Interaction: P49166; IntAct: EBI-10420,EBI-14629; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-10420,EBI-15409; Score: 0.35
DE  Interaction: P05737; IntAct: EBI-10420,EBI-15422; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-15427,EBI-10420; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-15913,EBI-10420; Score: 0.35
DE  Interaction: P38886; IntAct: EBI-10420,EBI-15949; Score: 0.35
DE  Interaction: P53196; IntAct: EBI-23691,EBI-10420; Score: 0.35
DE  Interaction: P04050; IntAct: EBI-10420,EBI-15760; Score: 0.35
DE  Interaction: P38786; IntAct: EBI-15968,EBI-10420; Score: 0.35
DE  Interaction: P33442; IntAct: EBI-16132,EBI-10420; Score: 0.35
DE  Interaction: P38701; IntAct: EBI-10420,EBI-16081; Score: 0.35
DE  Interaction: P26786; IntAct: EBI-10420,EBI-16161; Score: 0.35
DE  Interaction: P53549; IntAct: EBI-18520,EBI-10420; Score: 0.35
DE  Interaction: P33297; IntAct: EBI-10420,EBI-13920; Score: 0.35
DE  Interaction: Q01939; IntAct: EBI-10420,EBI-13914; Score: 0.35
DE  Interaction: Q12348; IntAct: EBI-10420,EBI-32238; Score: 0.35
DE  Interaction: P25359; IntAct: EBI-1773,EBI-10420; Score: 0.35
DE  Interaction: Q05022; IntAct: EBI-10420,EBI-16011; Score: 0.35
DE  Interaction: Q02206; IntAct: EBI-16204,EBI-10420; Score: 0.35
DE  Interaction: P13856; IntAct: EBI-16228,EBI-10420; Score: 0.35
DE  Interaction: P38903; IntAct: EBI-10420,EBI-1931; Score: 0.35
DE  Interaction: P40962; IntAct: EBI-10420,EBI-16348; Score: 0.35
DE  Interaction: P53289; IntAct: EBI-23393,EBI-10420; Score: 0.35
DE  Interaction: P46674; IntAct: EBI-16425,EBI-10420; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-10789,EBI-10420; Score: 0.35
DE  Interaction: P50110; IntAct: EBI-10420,EBI-2347180; Score: 0.35
DE  Interaction: P53036; IntAct: EBI-10420,EBI-16467; Score: 0.35
DE  Interaction: P53324; IntAct: EBI-23602,EBI-10420; Score: 0.35
DE  Interaction: Q04002; IntAct: EBI-10420,EBI-16662; Score: 0.35
DE  Interaction: Q12334; IntAct: EBI-10420,EBI-31788; Score: 0.35
DE  Interaction: P38072; IntAct: EBI-10420,EBI-16730; Score: 0.35
DE  Interaction: P48415; IntAct: EBI-10420,EBI-16551; Score: 0.35
DE  Interaction: P18759; IntAct: EBI-16565,EBI-10420; Score: 0.35
DE  Interaction: P32844; IntAct: EBI-10420,EBI-16874; Score: 0.35
DE  Interaction: P32855; IntAct: EBI-10420,EBI-16896; Score: 0.35
DE  Interaction: Q04228; IntAct: EBI-27730,EBI-10420; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-16945,EBI-10420; Score: 0.35
DE  Interaction: P33330; IntAct: EBI-16970,EBI-10420; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-10420,EBI-16993; Score: 0.35
DE  Interaction: Q12369; IntAct: EBI-2213082,EBI-10420; Score: 0.35
DE  Interaction: Q12118; IntAct: EBI-10420,EBI-31784; Score: 0.64
DE  Interaction: P34223; IntAct: EBI-10420,EBI-17093; Score: 0.35
DE  Interaction: Q07657; IntAct: EBI-10420,EBI-22083; Score: 0.35
DE  Interaction: P53266; IntAct: EBI-10420,EBI-17111; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-17148,EBI-10420; Score: 0.35
DE  Interaction: P22579; IntAct: EBI-10420,EBI-17160; Score: 0.35
DE  Interaction: P53965; IntAct: EBI-28668,EBI-10420; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-34508,EBI-10420; Score: 0.35
DE  Interaction: P35207; IntAct: EBI-10420,EBI-1851; Score: 0.35
DE  Interaction: P42843; IntAct: EBI-10420,EBI-28370; Score: 0.35
DE  Interaction: Q02775; IntAct: EBI-17379,EBI-10420; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-17402,EBI-10420; Score: 0.35
DE  Interaction: P12904; IntAct: EBI-17537,EBI-10420; Score: 0.35
DE  Interaction: P32568; IntAct: EBI-10420,EBI-17590; Score: 0.35
DE  Interaction: P25357; IntAct: EBI-17596,EBI-10420; Score: 0.35
DE  Interaction: P53127; IntAct: EBI-10420,EBI-23958; Score: 0.35
DE  Interaction: Q04748; IntAct: EBI-28123,EBI-10420; Score: 0.35
DE  Interaction: P23201; IntAct: EBI-10420,EBI-17803; Score: 0.35
DE  Interaction: P25808; IntAct: EBI-17819,EBI-10420; Score: 0.35
DE  Interaction: P32380; IntAct: EBI-12369,EBI-10420; Score: 0.35
DE  Interaction: P36126; IntAct: EBI-17726,EBI-10420; Score: 0.35
DE  Interaction: Q03868; IntAct: EBI-35189,EBI-10420; Score: 0.35
DE  Interaction: Q03012; IntAct: EBI-10420,EBI-32540; Score: 0.35
DE  Interaction: P08458; IntAct: EBI-17889,EBI-10420; Score: 0.53
DE  Interaction: P32558; IntAct: EBI-4334,EBI-10420; Score: 0.35
DE  Interaction: Q03707; IntAct: EBI-18064,EBI-10420; Score: 0.35
DE  Interaction: Q12020; IntAct: EBI-38714,EBI-10420; Score: 0.35
DE  Interaction: P38688; IntAct: EBI-18011,EBI-10420; Score: 0.35
DE  Interaction: P53599; IntAct: EBI-10420,EBI-18191; Score: 0.53
DE  Interaction: P47821; IntAct: EBI-10420,EBI-20078; Score: 0.35
DE  Interaction: P11972; IntAct: EBI-18232,EBI-10420; Score: 0.35
DE  Interaction: P46679; IntAct: EBI-18321,EBI-10420; Score: 0.35
DE  Interaction: P18851; IntAct: EBI-7390,EBI-10420; Score: 0.53
DE  Interaction: P32597; IntAct: EBI-18410,EBI-10420; Score: 0.35
DE  Interaction: P53101; IntAct: EBI-10420,EBI-24097; Score: 0.35
DE  Interaction: P37297; IntAct: EBI-10420,EBI-18454; Score: 0.35
DE  Interaction: P38198; IntAct: EBI-10420,EBI-18463; Score: 0.35
DE  Interaction: P09064; IntAct: EBI-10420,EBI-8920; Score: 0.35
DE  Interaction: P46676; IntAct: EBI-10420,EBI-18547; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-6533,EBI-10420; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-10420; Score: 0.62
DE  Interaction: A0A023PZA9; IntAct: EBI-3862844,EBI-10420; Score: 0.35
DE  Interaction: P47171; IntAct: EBI-10420,EBI-25715; Score: 0.35
DE  Interaction: Q03973; IntAct: EBI-10420,EBI-33047; Score: 0.35
DE  Interaction: P32478; IntAct: EBI-10420,EBI-4405; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-10420,EBI-8076; Score: 0.35
DE  Interaction: P07263; IntAct: EBI-10420,EBI-18711; Score: 0.35
DE  Interaction: Q12692; IntAct: EBI-8080,EBI-10420; Score: 0.35
DE  Interaction: P04807; IntAct: EBI-10420,EBI-8738; Score: 0.35
DE  Interaction: P43579; IntAct: EBI-10420,EBI-22775; Score: 0.35
DE  Interaction: P38286; IntAct: EBI-10420,EBI-20857; Score: 0.35
DE  Interaction: P09436; IntAct: EBI-18718,EBI-10420; Score: 0.35
DE  Interaction: P00927; IntAct: EBI-19200,EBI-10420; Score: 0.35
DE  Interaction: P50095; IntAct: EBI-10420,EBI-9190; Score: 0.35
DE  Interaction: P53115; IntAct: EBI-24019,EBI-10420; Score: 0.35
DE  Interaction: P40006; IntAct: EBI-2050819,EBI-10420; Score: 0.35
DE  Interaction: Q07821; IntAct: EBI-10420,EBI-27136; Score: 0.35
DE  Interaction: P36132; IntAct: EBI-10420,EBI-26411; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-9152,EBI-10420; Score: 0.35
DE  Interaction: Q08979; IntAct: EBI-10420,EBI-9638; Score: 0.35
DE  Interaction: P22209; IntAct: EBI-9730,EBI-10420; Score: 0.35
DE  Interaction: P40540; IntAct: EBI-24977,EBI-10420; Score: 0.35
DE  Interaction: Q3E840; IntAct: EBI-2055307,EBI-10420; Score: 0.35
DE  Interaction: P12695; IntAct: EBI-10420,EBI-12469; Score: 0.35
DE  Interaction: P57743; IntAct: EBI-10420,EBI-10227; Score: 0.35
DE  Interaction: P53905; IntAct: EBI-10420,EBI-141; Score: 0.35
DE  Interaction: P48570; IntAct: EBI-8502,EBI-10420; Score: 0.35
DE  Interaction: P49367; IntAct: EBI-10276,EBI-10420; Score: 0.35
DE  Interaction: P11914; IntAct: EBI-11205,EBI-10420; Score: 0.35
DE  Interaction: P39677; IntAct: EBI-6361,EBI-10420; Score: 0.35
DE  Interaction: P24719; IntAct: EBI-10690,EBI-10420; Score: 0.35
DE  Interaction: P00958; IntAct: EBI-10420,EBI-18762; Score: 0.35
DE  Interaction: P53128; IntAct: EBI-11572,EBI-10420; Score: 0.35
DE  Interaction: P33441; IntAct: EBI-10841,EBI-10420; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-3903,EBI-10420; Score: 0.35
DE  Interaction: P53141; IntAct: EBI-10988,EBI-10420; Score: 0.35
DE  Interaction: P25847; IntAct: EBI-10420,EBI-11352; Score: 0.35
DE  Interaction: P32335; IntAct: EBI-10420,EBI-11318; Score: 0.35
DE  Interaction: P47047; IntAct: EBI-11592,EBI-10420; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-10420,EBI-11659; Score: 0.35
DE  Interaction: P38205; IntAct: EBI-10420,EBI-11933; Score: 0.35
DE  Interaction: Q08972; IntAct: EBI-10420,EBI-32014; Score: 0.35
DE  Interaction: P53081; IntAct: EBI-12063,EBI-10420; Score: 0.35
DE  Interaction: P06102; IntAct: EBI-10420,EBI-12165; Score: 0.35
DE  Interaction: P53164; IntAct: EBI-10420,EBI-11856; Score: 0.35
DE  Interaction: P31378; IntAct: EBI-10420,EBI-12294; Score: 0.35
DE  Interaction: P35172; IntAct: EBI-10420,EBI-19513; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-20731,EBI-10420; Score: 0.35
DE  Interaction: P54784; IntAct: EBI-12568,EBI-10420; Score: 0.35
DE  Interaction: P50874; IntAct: EBI-12584,EBI-10420; Score: 0.35
DE  Interaction: P38826; IntAct: EBI-12588,EBI-10420; Score: 0.35
DE  Interaction: Q12451; IntAct: EBI-12621,EBI-10420; Score: 0.35
DE  Interaction: Q12447; IntAct: EBI-10420,EBI-33397; Score: 0.35
DE  Interaction: P38254; IntAct: EBI-10420,EBI-21533; Score: 0.35
DE  Interaction: Q04264; IntAct: EBI-13077,EBI-10420; Score: 0.35
DE  Interaction: P42841; IntAct: EBI-28378,EBI-10420; Score: 0.53
DE  Interaction: P47110; IntAct: EBI-6084,EBI-10420; Score: 0.35
DE  Interaction: P39985; IntAct: EBI-6120,EBI-10420; Score: 0.35
DE  Interaction: P23595; IntAct: EBI-10420,EBI-12752; Score: 0.53
DE  Interaction: P32345; IntAct: EBI-12759,EBI-10420; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-505,EBI-10420; Score: 0.35
DE  Interaction: P28708; IntAct: EBI-9782,EBI-10420; Score: 0.35
DE  Interaction: Q12265; IntAct: EBI-9886,EBI-10420; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-11191,EBI-10420; Score: 0.35
DE  Interaction: Q12335; IntAct: EBI-10420,EBI-14064; Score: 0.35
DE  Interaction: Q12318; IntAct: EBI-10420,EBI-37340; Score: 0.35
DE  Interaction: P09368; IntAct: EBI-10420,EBI-14299; Score: 0.35
DE  Interaction: P06777; IntAct: EBI-10420,EBI-14752; Score: 0.35
DE  Interaction: P32628; IntAct: EBI-10420,EBI-14668; Score: 0.35
DE  Interaction: P32641; IntAct: EBI-14675,EBI-10420; Score: 0.53
DE  Interaction: P06839; IntAct: EBI-10420,EBI-14762; Score: 0.64
DE  Interaction: Q04231; IntAct: EBI-10420,EBI-27726; Score: 0.35
DE  Interaction: P25454; IntAct: EBI-10420,EBI-14709; Score: 0.35
DE  Interaction: P21538; IntAct: EBI-10420,EBI-14905; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-10420,EBI-14971; Score: 0.35
DE  Interaction: P39083; IntAct: EBI-10420,EBI-15044; Score: 0.35
DE  Interaction: Q00453; IntAct: EBI-15073,EBI-10420; Score: 0.35
DE  Interaction: P16664; IntAct: EBI-15080,EBI-10420; Score: 0.35
DE  Interaction: P48565; IntAct: EBI-3664151,EBI-10420; Score: 0.35
DE  Interaction: Q07844; IntAct: EBI-10420,EBI-27142; Score: 0.35
DE  Interaction: P21524; IntAct: EBI-15234,EBI-10420; Score: 0.35
DE  Interaction: P32561; IntAct: EBI-15864,EBI-10420; Score: 0.35
DE  Interaction: P32565; IntAct: EBI-15919,EBI-10420; Score: 0.35
DE  Interaction: P40016; IntAct: EBI-10420,EBI-15927; Score: 0.35
DE  Interaction: P40327; IntAct: EBI-10420,EBI-13901; Score: 0.35
DE  Interaction: Q12754; IntAct: EBI-10420,EBI-30678; Score: 0.35
DE  Interaction: P53236; IntAct: EBI-16192,EBI-10420; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-35018,EBI-10420; Score: 0.35
DE  Interaction: Q03940; IntAct: EBI-10420,EBI-30712; Score: 0.35
DE  Interaction: P32368; IntAct: EBI-10420,EBI-16210; Score: 0.35
DE  Interaction: Q08873; IntAct: EBI-33137,EBI-10420; Score: 0.35
DE  Interaction: P40509; IntAct: EBI-4884,EBI-10420; Score: 0.35
DE  Interaction: P38968; IntAct: EBI-10420,EBI-20524; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-10420,EBI-31337; Score: 0.35
DE  Interaction: P46995; IntAct: EBI-16985,EBI-10420; Score: 0.35
DE  Interaction: P53953; IntAct: EBI-17006,EBI-10420; Score: 0.35
DE  Interaction: P23293; IntAct: EBI-10420,EBI-17078; Score: 0.35
DE  Interaction: P51534; IntAct: EBI-10420,EBI-17086; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-17237,EBI-10420; Score: 0.35
DE  Interaction: Q04195; IntAct: EBI-10420,EBI-32913; Score: 0.35
DE  Interaction: P53327; IntAct: EBI-10420,EBI-23623; Score: 0.35
DE  Interaction: P38989; IntAct: EBI-10420,EBI-17412; Score: 0.35
DE  Interaction: P47037; IntAct: EBI-17423,EBI-10420; Score: 0.35
DE  Interaction: P36048; IntAct: EBI-243,EBI-10420; Score: 0.35
DE  Interaction: Q04053; IntAct: EBI-10420,EBI-30464; Score: 0.35
DE  Interaction: P38633; IntAct: EBI-10420,EBI-17658; Score: 0.35
DE  Interaction: P38863; IntAct: EBI-17786,EBI-10420; Score: 0.35
DE  Interaction: P23561; IntAct: EBI-18259,EBI-10420; Score: 0.35
DE  Interaction: P05453; IntAct: EBI-6540,EBI-10420; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-10420,EBI-23061; Score: 0.35
DE  Interaction: P09959; IntAct: EBI-18641,EBI-10420; Score: 0.35
DE  Interaction: Q05471; IntAct: EBI-22102,EBI-10420; Score: 0.35
DE  Interaction: Q04175; IntAct: EBI-10420,EBI-35508; Score: 0.35
DE  Interaction: Q12297; IntAct: EBI-10420,EBI-36697; Score: 0.35
DE  Interaction: P33339; IntAct: EBI-10420,EBI-19159; Score: 0.35
DE  Interaction: Q06339; IntAct: EBI-29851,EBI-10420; Score: 0.35
DE  Interaction: P17423; IntAct: EBI-9685,EBI-10420; Score: 0.35
DE  Interaction: P23254; IntAct: EBI-19291,EBI-10420; Score: 0.35
DE  Interaction: P40462; IntAct: EBI-25239,EBI-10420; Score: 0.35
DE  Interaction: P53840; IntAct: EBI-10420,EBI-28257; Score: 0.35
DE  Interaction: Q03280; IntAct: EBI-10420,EBI-36817; Score: 0.35
DE  Interaction: P06786; IntAct: EBI-19352,EBI-10420; Score: 0.35
DE  Interaction: P43637; IntAct: EBI-10420,EBI-9668; Score: 0.35
DE  Interaction: P06244; IntAct: EBI-10420,EBI-9458; Score: 0.35
DE  Interaction: Q00764; IntAct: EBI-10420,EBI-19430; Score: 0.35
DE  Interaction: P38426; IntAct: EBI-19448,EBI-10420; Score: 0.35
DE  Interaction: P38811; IntAct: EBI-24638,EBI-10420; Score: 0.35
DE  Interaction: Q07527; IntAct: EBI-10420,EBI-36284; Score: 0.35
DE  Interaction: P00937; IntAct: EBI-10420,EBI-19585; Score: 0.35
DE  Interaction: P38427; IntAct: EBI-10420,EBI-19638; Score: 0.35
DE  Interaction: Q07381; IntAct: EBI-10420,EBI-35023; Score: 0.35
DE  Interaction: P53378; IntAct: EBI-19013,EBI-10420; Score: 0.35
DE  Interaction: P36164; IntAct: EBI-10420,EBI-26527; Score: 0.35
DE  Interaction: Q08960; IntAct: EBI-10420,EBI-29349; Score: 0.35
DE  Interaction: Q01476; IntAct: EBI-19826,EBI-10420; Score: 0.35
DE  Interaction: P43593; IntAct: EBI-19852,EBI-10420; Score: 0.35
DE  Interaction: P54860; IntAct: EBI-10420,EBI-20003; Score: 0.35
DE  Interaction: P33202; IntAct: EBI-20010,EBI-10420; Score: 0.35
DE  Interaction: P38067; IntAct: EBI-10420,EBI-20027; Score: 0.35
DE  Interaction: P28274; IntAct: EBI-20128,EBI-10420; Score: 0.35
DE  Interaction: P42945; IntAct: EBI-10420,EBI-1884; Score: 0.35
DE  Interaction: Q05946; IntAct: EBI-34702,EBI-10420; Score: 0.35
DE  Interaction: Q06078; IntAct: EBI-359,EBI-10420; Score: 0.35
DE  Interaction: P53276; IntAct: EBI-23301,EBI-10420; Score: 0.35
DE  Interaction: P32623; IntAct: EBI-2098544,EBI-10420; Score: 0.35
DE  Interaction: P53076; IntAct: EBI-24173,EBI-10420; Score: 0.35
DE  Interaction: Q12045; IntAct: EBI-38784,EBI-10420; Score: 0.35
DE  Interaction: Q06685; IntAct: EBI-35034,EBI-10420; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-10420,EBI-20415; Score: 0.35
DE  Interaction: Q12109; IntAct: EBI-18832,EBI-10420; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-10420,EBI-20627; Score: 0.35
DE  Interaction: P46683; IntAct: EBI-20829,EBI-10420; Score: 0.35
DE  Interaction: P38222; IntAct: EBI-21417,EBI-10420; Score: 0.35
DE  Interaction: P38317; IntAct: EBI-20989,EBI-10420; Score: 0.35
DE  Interaction: P25361; IntAct: EBI-10420,EBI-21909; Score: 0.35
DE  Interaction: Q04093; IntAct: EBI-30943,EBI-10420; Score: 0.35
DE  Interaction: Q04431; IntAct: EBI-10420,EBI-32446; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-10420,EBI-6338; Score: 0.35
DE  Interaction: P43594; IntAct: EBI-22936,EBI-10420; Score: 0.35
DE  Interaction: P53262; IntAct: EBI-2061527,EBI-10420; Score: 0.35
DE  Interaction: P38829; IntAct: EBI-10420,EBI-24704; Score: 0.35
DE  Interaction: P38833; IntAct: EBI-24716,EBI-10420; Score: 0.35
DE  Interaction: P40533; IntAct: EBI-24998,EBI-10420; Score: 0.35
DE  Interaction: P36114; IntAct: EBI-10420,EBI-27086; Score: 0.35
DE  Interaction: Q05778; IntAct: EBI-10420,EBI-33792; Score: 0.35
DE  Interaction: Q06188; IntAct: EBI-35613,EBI-10420; Score: 0.35
DE  Interaction: Q04847; IntAct: EBI-10420,EBI-27556; Score: 0.35
DE  Interaction: P53970; IntAct: EBI-28642,EBI-10420; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-10420,EBI-28374; Score: 0.35
DE  Interaction: Q08206; IntAct: EBI-38207,EBI-10420; Score: 0.35
DE  Interaction: Q08548; IntAct: EBI-10420,EBI-38058; Score: 0.35
DE  Interaction: Q08822; IntAct: EBI-10420,EBI-6705; Score: 0.35
DE  Interaction: P12688; IntAct: EBI-29473,EBI-10420; Score: 0.35
DE  Interaction: Q08924; IntAct: EBI-38332,EBI-10420; Score: 0.35
DE  Interaction: O13585; IntAct: EBI-10420,EBI-33008; Score: 0.35
DE  Interaction: Q06109; IntAct: EBI-10420,EBI-38369; Score: 0.35
DE  Interaction: Q08245; IntAct: EBI-10420,EBI-32089; Score: 0.35
DE  Interaction: P53303; IntAct: EBI-29657,EBI-10420; Score: 0.35
DE  Interaction: P11412; IntAct: EBI-10420,EBI-7233; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-8666,EBI-10420; Score: 0.35
DE  Interaction: P47138; IntAct: EBI-10420,EBI-25576; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-3949,EBI-10420; Score: 0.35
DE  Interaction: P46997; IntAct: EBI-10420,EBI-26138; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-17244,EBI-10420; Score: 0.35
DE  Interaction: P38009; IntAct: EBI-14223,EBI-10420; Score: 0.35
DE  Interaction: P07244; IntAct: EBI-10420,EBI-323; Score: 0.35
DE  Interaction: P38972; IntAct: EBI-10420,EBI-14246; Score: 0.35
DE  Interaction: P25376; IntAct: EBI-2357,EBI-10420; Score: 0.35
DE  Interaction: P47019; IntAct: EBI-10420,EBI-26061; Score: 0.35
DE  Interaction: P47771; IntAct: EBI-10420,EBI-5772; Score: 0.35
DE  Interaction: P54115; IntAct: EBI-10420,EBI-5798; Score: 0.35
DE  Interaction: P46682; IntAct: EBI-2213,EBI-10420; Score: 0.35
DE  Interaction: P38328; IntAct: EBI-2777,EBI-10420; Score: 0.35
DE  Interaction: Q12500; IntAct: EBI-10420,EBI-38577; Score: 0.35
DE  Interaction: Q05029; IntAct: EBI-27508,EBI-10420; Score: 0.35
DE  Interaction: P34730; IntAct: EBI-3672,EBI-10420; Score: 0.35
DE  Interaction: P47039; IntAct: EBI-25893,EBI-10420; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-10420,EBI-31563; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-10420,EBI-861; Score: 0.35
DE  Interaction: P40096; IntAct: EBI-10420,EBI-11908; Score: 0.35
DE  Interaction: P00812; IntAct: EBI-10420,EBI-2856; Score: 0.35
DE  Interaction: P33322; IntAct: EBI-10420,EBI-4105; Score: 0.35
DE  Interaction: P31384; IntAct: EBI-4396,EBI-10420; Score: 0.53
DE  Interaction: Q03705; IntAct: EBI-912262,EBI-10420; Score: 0.35
DE  Interaction: P19454; IntAct: EBI-9548,EBI-10420; Score: 0.35
DE  Interaction: P53195; IntAct: EBI-4847,EBI-10420; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-10420,EBI-20589; Score: 0.35
DE  Interaction: Q06440; IntAct: EBI-4950,EBI-10420; Score: 0.35
DE  Interaction: P14922; IntAct: EBI-18215,EBI-10420; Score: 0.35
DE  Interaction: P36009; IntAct: EBI-5844,EBI-10420; Score: 0.53
DE  Interaction: Q04216; IntAct: EBI-10420,EBI-27260; Score: 0.35
DE  Interaction: P54858; IntAct: EBI-10420,EBI-6042; Score: 0.35
DE  Interaction: P32461; IntAct: EBI-6090,EBI-10420; Score: 0.35
DE  Interaction: P53911; IntAct: EBI-10420,EBI-28927; Score: 0.35
DE  Interaction: P47169; IntAct: EBI-10420,EBI-25702; Score: 0.35
DE  Interaction: P38241; IntAct: EBI-780,EBI-10420; Score: 0.35
DE  Interaction: Q04409; IntAct: EBI-38225,EBI-10420; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-6468,EBI-10420; Score: 0.35
DE  Interaction: P38333; IntAct: EBI-6482,EBI-10420; Score: 0.35
DE  Interaction: P43572; IntAct: EBI-22792,EBI-10420; Score: 0.35
DE  Interaction: P32353; IntAct: EBI-10420,EBI-6554; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-10420,EBI-6587; Score: 0.35
DE  Interaction: P38819; IntAct: EBI-6603,EBI-10420; Score: 0.35
DE  Interaction: Q08649; IntAct: EBI-10420,EBI-6648; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-10420,EBI-28537; Score: 0.35
DE  Interaction: Q12178; IntAct: EBI-10420,EBI-6851; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-10420,EBI-8936; Score: 0.35
DE  Interaction: Q08193; IntAct: EBI-29273,EBI-10420; Score: 0.35
DE  Interaction: P41814; IntAct: EBI-8995,EBI-10420; Score: 0.35
DE  Interaction: P12754; IntAct: EBI-6265,EBI-10420; Score: 0.35
DE  Interaction: P43535; IntAct: EBI-10420,EBI-7423; Score: 0.35
DE  Interaction: Q05584; IntAct: EBI-7672,EBI-10420; Score: 0.35
DE  Interaction: Q08220; IntAct: EBI-7915,EBI-10420; Score: 0.35
DE  Interaction: P27472; IntAct: EBI-8036,EBI-10420; Score: 0.35
DE  Interaction: P32190; IntAct: EBI-7694,EBI-10420; Score: 0.35
DE  Interaction: Q12180; IntAct: EBI-10420,EBI-37549; Score: 0.35
DE  Interaction: Q12341; IntAct: EBI-8176,EBI-10420; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-10420,EBI-5612; Score: 0.35
DE  Interaction: P11353; IntAct: EBI-8257,EBI-10420; Score: 0.35
DE  Interaction: Q04458; IntAct: EBI-10420,EBI-27205; Score: 0.35
DE  Interaction: P61830; IntAct: EBI-8098,EBI-10420; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-10420,EBI-18084; Score: 0.35
DE  Interaction: P0CS82; IntAct: EBI-10420,EBI-5419; Score: 0.35
DE  Interaction: Q08273; IntAct: EBI-31686,EBI-10420; Score: 0.53
DE  Interaction: P22146; IntAct: EBI-10420,EBI-7327; Score: 0.27
DE  Interaction: P38085; IntAct: EBI-20222,EBI-10420; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-2098,EBI-10420; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-3242,EBI-10420; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-2293,EBI-10420; Score: 0.27
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0072380;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0031072;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0006458;
GO  GO:0071470;
GO  GO:0051131;
GO  GO:0042026;
GO  GO:0045047;
GO  GO:0006626;
GO  GO:0009408;
GO  GO:0035719;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1527016};
SQ  MVKETKFYDILGVPVTATDVEIKKAYRKCALKYHPDKNPSEEAAEKFKEASAAYEILSDPEKRDIYDQFGEDGLSGAGGA
SQ  GGFPGGGFGFGDDIFSQFFGAGGAQRPRGPQRGKDIKHEISASLEELYKGRTAKLALNKQILCKECEGRGGKKGAVKKCT
SQ  SCNGQGIKFVTRQMGPMIQRFQTECDVCHGTGDIIDPKDRCKSCNGKKVENERKILEVHVEPGMKDGQRIVFKGEADQAP
SQ  DVIPGDVVFIVSERPHKSFKRDGDDLVYEAEIDLLTAIAGGEFALEHVSGDWLKVGIVPGEVIAPGMRKVIEGKGMPIPK
SQ  YGGYGNLIIKFTIKFPENHFTSEENLKKLEEILPPRIVPAIPKKATVDECVLADFDPAKYNRTRASRGGANYDSDEEEQG
SQ  GEGVQCASQ
//
ID  P34160;
PN  Nuclear cap-binding protein complex subunit 1;
GN  STO1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:8858145}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10823828}. Note=Predominantly nuclear, is able to exit the nucleus in an RNA-dependent manner. {ECO:0000269|PubMed:10823828}.
DR  UNIPROT: P34160;
DR  UNIPROT: D6VZU8;
DR  PDB: 3UKY;
DR  PDB: 6N7P;
DR  Pfam: PF02854;
DR  Pfam: PF09088;
DR  Pfam: PF09090;
DE  Function: Component of the CBC complex, which binds co- transcriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive- strand RNA virus BMV. {ECO:0000269|PubMed:10490594, ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:12756324, ECO:0000269|PubMed:12897126, ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:1512188, ECO:0000269|PubMed:15753296, ECO:0000269|PubMed:16166263, ECO:0000269|PubMed:8811086, ECO:0000269|PubMed:8846890, ECO:0000269|PubMed:8858145, ECO:0000269|PubMed:9499403}.
DE  Reference Proteome: Yes;
DE  Interaction: P06105; IntAct: EBI-745,EBI-16374; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-745; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-745,EBI-22339; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-7876,EBI-745; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-8637,EBI-745; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-10154,EBI-745; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-745,EBI-8680; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-745,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-745; Score: 0.53
DE  Interaction: P39076; IntAct: EBI-745,EBI-19049; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-3949,EBI-745; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-745,EBI-30084; Score: 0.35
DE  Interaction: P53207; IntAct: EBI-736,EBI-745; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-11835,EBI-745; Score: 0.35
DE  Interaction: Q02554; IntAct: EBI-654,EBI-745; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-724,EBI-745; Score: 0.35
DE  Interaction: P39935; IntAct: EBI-9002,EBI-745; Score: 0.35
DE  Interaction: P32588; IntAct: EBI-14231,EBI-745; Score: 0.35
DE  Interaction: P38996; IntAct: EBI-11776,EBI-745; Score: 0.35
DE  Interaction: Q07508; IntAct: EBI-673,EBI-745; Score: 0.35
DE  Interaction: P38199; IntAct: EBI-21217,EBI-745; Score: 0.35
DE  Interaction: P32605; IntAct: EBI-680,EBI-745; Score: 0.35
DE  Interaction: P54999; IntAct: EBI-770,EBI-745; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-18146,EBI-745; Score: 0.35
DE  Interaction: P40204; IntAct: EBI-637,EBI-745; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-861,EBI-745; Score: 0.35
DE  Interaction: Q03782; IntAct: EBI-627,EBI-745; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-12228,EBI-745; Score: 0.53
DE  Interaction: P28320; IntAct: EBI-26795,EBI-745; Score: 0.35
DE  Interaction: P07260; IntAct: EBI-150,EBI-745; Score: 0.53
DE  Interaction: Q03776; IntAct: EBI-802,EBI-745; Score: 0.35
DE  Interaction: Q04493; IntAct: EBI-13253,EBI-745; Score: 0.35
DE  Interaction: P32561; IntAct: EBI-15864,EBI-745; Score: 0.35
DE  Interaction: P11633; IntAct: EBI-12028,EBI-745; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-33556,EBI-745; Score: 0.82
DE  Interaction: Q12046; IntAct: EBI-553,EBI-745; Score: 0.35
DE  Interaction: P36036; IntAct: EBI-745,EBI-27015; Score: 0.56
DE  Interaction: P39936; IntAct: EBI-745,EBI-9006; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-745,EBI-6314; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-745,EBI-1797; Score: 0.69
DE  Interaction: P25567; IntAct: EBI-745,EBI-18084; Score: 0.35
DE  Interaction: P43321; IntAct: EBI-745,EBI-529; Score: 0.35
DE  Interaction: Q06217; IntAct: EBI-745,EBI-235; Score: 0.35
DE  Interaction: Q02260; IntAct: EBI-745,EBI-585; Score: 0.35
DE  Interaction: P23293; IntAct: EBI-745,EBI-17078; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-745,EBI-16945; Score: 0.35
DE  Interaction: Q04693; IntAct: EBI-745,EBI-519; Score: 0.35
DE  Interaction: P0C0W1; IntAct: EBI-745,EBI-16090; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-745,EBI-15475; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-745,EBI-465; Score: 0.35
DE  Interaction: P33203; IntAct: EBI-745,EBI-701; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-745,EBI-12823; Score: 0.35
DE  Interaction: P40965; IntAct: EBI-745,EBI-11371; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-745,EBI-9145; Score: 0.35
DE  Interaction: P38697; IntAct: EBI-745,EBI-9186; Score: 0.35
DE  Interaction: P04911; IntAct: EBI-745,EBI-8072; Score: 0.35
DE  Interaction: Q05949; IntAct: EBI-745,EBI-30948; Score: 0.35
DE  Interaction: Q12492; IntAct: EBI-745,EBI-32227; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-745,EBI-31475; Score: 0.44
DE  Interaction: Q05900; IntAct: EBI-754,EBI-745; Score: 0.56
DE  Interaction: P32357; IntAct: EBI-340,EBI-745; Score: 0.27
DE  Interaction: P33322; IntAct: EBI-4105,EBI-745; Score: 0.27
DE  Interaction: P47130; IntAct: EBI-763,EBI-745; Score: 0.27
DE  Interaction: P40018; IntAct: EBI-432,EBI-745; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-745,EBI-19749; Score: 0.37
DE  Interaction: P53854; IntAct: EBI-29221,EBI-745; Score: 0.35
GO  GO:0000243;
GO  GO:0005845;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003729;
GO  GO:0000339;
GO  GO:0006370;
GO  GO:0045292;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006970;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFNRKRRGDFDEDENYRDFRPRMPKRQRIPPVVQLCKEMMPDIRTIGESVKAFEDDIKFLSEAIMNEYGHEDYFNNALLS
SQ  TLNAVVVEQPQKQAAIALLTMVVNSKNNVAGKSIINYFFEELQKWCKQTYNDEFKSTSNETGPWNKIKLILRFLSILSPM
SQ  FLVDELINIYKSLFELSIELNNLDPGNRVPLSEAIYTNTLLNIPYLFFFNRNNDGLRTKVEELLAYVEQNYLVKTTDINL
SQ  LREYNGEPPYEMVELVRVVLPNVKKALINNLEQLNELFPDWNHLLTPQTGDEGFNDALTLPSVDDLKSFVRLNKNFGSVD
SQ  SMWKTPRYAFHVYLPNSAGNFETVVPISTYAGQLFNDIIIDLVESLEFNRKEVARQVITLDLFFKAGIFTEPGESIAQLI
SQ  ATYEENPLAPTFKIEDLAIETILGLIFKLPSVSQPFAYFYTLLVDICQNSPKAIAPVFGRAFRFFYSHLDSLDFELKLRY
SQ  LDWFSIQMSNFNFSWKWNEWEDDSIKFGKYFYNPKVNFAKNLIQKELRLTSNFSEVEDSLPQEFTKYLDTSYIPRDQLIN
SQ  YYQSLFTGYTVEEDSVRKNDLYFRQEGVPMENTVRKILDYTHKANNSREVTELESILGELKNEYGSIISDFNRFVIILLV
SQ  QAVTDSGSRSLSHANKYINDLKEDLKTIFAKIELDIETKEYIIIEAVLTFWNANPQTGFLVADAFKYAGLLTSRTIFTFI
SQ  FNETGLKNNGLIEATAIEAVFRNLSQQISEENESGNNFEFVFERLCTIANSTIDLLDVNADEDIEIPKVNGEMDIDDIED
SQ  DKLDLKWKYFTVIGFIKSILRRYSHEYRELADKFIANIDNAIPHESTRRTISNWIQETKEV
//
ID  P50995;
PN  Annexin A11;
GN  ANXA11;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:28469040}. Melanosome. Nucleus envelope. Nucleus, nucleoplasm {ECO:0000269|PubMed:28469040}. Cytoplasm, cytoskeleton, spindle. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus (By similarity). Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
DR  UNIPROT: P50995;
DR  UNIPROT: B4DVE7;
DR  Pfam: PF00191;
DR  PROSITE: PS00223;
DR  PROSITE: PS51897;
DR  OMIM: 602572;
DR  OMIM: 617839;
DR  DisGeNET: 311;
DE  Function: Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250, ECO:0000269|PubMed:15197175}.
DE  Disease: Amyotrophic lateral sclerosis 23 (ALS23) [MIM:617839]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. ALS23 is an autosomal dominant form with incomplete penetrance. {ECO:0000269|PubMed:28469040}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-715243,EBI-740019; Score: 0.55
DE  Interaction: O75340; IntAct: EBI-352915,EBI-715243; Score: 0.75
DE  Interaction: Q8IUH5; IntAct: EBI-715243,EBI-524753; Score: 0.37
DE  Interaction: Q9WVM1; IntAct: EBI-2552104,EBI-715243; Score: 0.35
DE  Interaction: Q80UG5; IntAct: EBI-772170,EBI-715243; Score: 0.35
DE  Interaction: Q91ZJ0; IntAct: EBI-11131709,EBI-715243; Score: 0.35
DE  Interaction: Q15828; IntAct: EBI-7163527,EBI-715243; Score: 0.40
DE  Interaction: Q93034; IntAct: EBI-1057139,EBI-715243; Score: 0.35
DE  Interaction: Q81ZA2; IntAct: EBI-2811440,EBI-715243; Score: 0.37
DE  Interaction: Q0WDP0; IntAct: EBI-715243,EBI-2843240; Score: 0.37
DE  Interaction: Q5NHS4; IntAct: EBI-2798955,EBI-715243; Score: 0.37
DE  Interaction: P31942; IntAct: EBI-715243,EBI-711437; Score: 0.37
DE  Interaction: Q53EZ4; IntAct: EBI-747776,EBI-715243; Score: 0.78
DE  Interaction: Q92734; IntAct: EBI-715243,EBI-357061; Score: 0.67
DE  Interaction: P60033; IntAct: EBI-712921,EBI-715243; Score: 0.35
DE  Interaction: Q96AE4-2; IntAct: EBI-12121668,EBI-715243; Score: 0.56
DE  Interaction: Q8NI38; IntAct: EBI-10271199,EBI-715243; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-11953846,EBI-715243; Score: 0.56
DE  Interaction: P15289; IntAct: EBI-2117357,EBI-715243; Score: 0.56
DE  Interaction: Q9NZC7-5; IntAct: EBI-12040603,EBI-715243; Score: 0.56
DE  Interaction: Q3LI66; IntAct: EBI-11962084,EBI-715243; Score: 0.56
DE  Interaction: P09104; IntAct: EBI-715243,EBI-713154; Score: 0.37
GO  GO:0042582;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0042470;
GO  GO:0016020;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0045335;
GO  GO:0042581;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0005544;
GO  GO:0048306;
GO  GO:0023026;
GO  GO:0008429;
GO  GO:0003723;
GO  GO:0044548;
GO  GO:0032506;
GO  GO:0006909;
GO  GO:0051592;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDYLSGMAANMSGTFGGANMPNLYPGAPGA
SQ  GYPPVPPGGFGQPPSAQQPVPPYGMYPPPGGNPPSRMPSYPPYPGAPVPGQPMPPPGQQPPGAYPGQPPVTYPGQPPVPL
SQ  PGQQQPVPSYPGYPGSGTVTPAVPPTQFGSRGTITDAPGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILL
SQ  SFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDIYEIKEAIKGVGTDEACLIEILASRSNEHIRELNRAYKAEFKK
SQ  TLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLAQRDAQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQR
SQ  MTGRDIEKSICREMSGDLEEGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSETDLLDIRSEYKRMYGKS
SQ  LYHDISGDTSGDYRKILLKICGGND
//
ID  P58546;
PN  Myotrophin;
GN  MTPN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P58546;
DR  PDB: 3AAA;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  OMIM: 606484;
DR  DisGeNET: 136319;
DE  Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:10329199, ECO:0000269|PubMed:16895918, ECO:0000269|PubMed:20625546}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H8T0; IntAct: EBI-711399,EBI-1051736; Score: 0.37
DE  Interaction: P00441; IntAct: EBI-990792,EBI-1051736; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-1051736; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-1051736; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-1051736,EBI-959949; Score: 0.37
DE  Interaction: Q9UPV0; IntAct: EBI-3937015,EBI-1051736; Score: 0.35
DE  Interaction: Q14203; IntAct: EBI-724352,EBI-1051736; Score: 0.35
DE  Interaction: O15078; IntAct: EBI-1811944,EBI-1051736; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-1104799,EBI-1051736; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-1046993,EBI-1051736; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-1051736; Score: 0.35
DE  Interaction: Q6XUX3; IntAct: EBI-1051736,EBI-1049520; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-1051736,EBI-307369; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-1051736,EBI-359276; Score: 0.40
DE  Interaction: P01889; IntAct: EBI-1051736,EBI-1046513; Score: 0.40
DE  Interaction: P11171; IntAct: EBI-1051736,EBI-1050906; Score: 0.40
DE  Interaction: Q9Y478; IntAct: EBI-1051736,EBI-719769; Score: 0.40
DE  Interaction: Q9UBN6; IntAct: EBI-1051736,EBI-1044859; Score: 0.40
DE  Interaction: Q9UET6; IntAct: EBI-1051736,EBI-1055987; Score: 0.40
DE  Interaction: P40337; IntAct: EBI-1051736,EBI-301246; Score: 0.40
DE  Interaction: Q9NRY4; IntAct: EBI-766200,EBI-1051736; Score: 0.35
DE  Interaction: Q3KRB8; IntAct: EBI-25411786,EBI-1051736; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-2361917,EBI-1051736; Score: 0.35
DE  Interaction: Q8N137; IntAct: EBI-947360,EBI-1051736; Score: 0.35
DE  Interaction: Q96Q45; IntAct: EBI-2602465,EBI-1051736; Score: 0.35
DE  Interaction: Q6UVJ0; IntAct: EBI-1570153,EBI-1051736; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-2563266,EBI-1051736; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-1051736; Score: 0.35
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043565;
GO  GO:0006584;
GO  GO:0071260;
GO  GO:0021707;
GO  GO:0030182;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
GO  GO:0016202;
GO  GO:0006417;
GO  GO:0043403;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ
//
ID  Q9BV73;
PN  Centrosome-associated protein CEP250;
GN  CEP250;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:9647649}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q60952}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q60952}. Note=Component of the core centrosome. In interphase cells, it specifically associates with the proximal ends of both mother and daughter centrioles. Associates with the centrosome in interphase cells. In mitotic cells, it dissociates from the mitotic spindle poles. At the end of cell division, it reaccumulates at centrosomes.
DR  UNIPROT: Q9BV73;
DR  UNIPROT: E1P5Q3;
DR  UNIPROT: O14812;
DR  UNIPROT: O60588;
DR  UNIPROT: Q9H450;
DR  OMIM: 609689;
DR  OMIM: 618358;
DR  DisGeNET: 11190;
DE  Function: May be involved in ciliogenesis (PubMed:28005958). Probably plays an important role in centrosome cohesion during interphase. {ECO:0000269|PubMed:28005958}.
DE  Disease: Cone-rod dystrophy and hearing loss 2 (CRDHL2) [MIM:618358]: An autosomal recessive disease defined by the association of progressive cone-rod dystrophy with sensorineural hearing loss. Cone- rod dystrophy is characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors. {ECO:0000269|PubMed:24780881, ECO:0000269|PubMed:29718797, ECO:0000269|PubMed:30459346, ECO:0000269|PubMed:30998843}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-1053100; Score: 0.35
DE  Interaction: O08788; IntAct: EBI-776180,EBI-1053100; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-1053100; Score: 0.35
DE  Interaction: Q9H0K1; IntAct: EBI-1053100,EBI-1181664; Score: 0.62
DE  Interaction: Q9HAU0; IntAct: EBI-1053100,EBI-945934; Score: 0.37
DE  Interaction: Q8ZGW9; IntAct: EBI-2856781,EBI-1053100; Score: 0.37
DE  Interaction: P35579; IntAct: EBI-350338,EBI-1053100; Score: 0.35
DE  Interaction: Q15008; IntAct: EBI-1053100,EBI-359701; Score: 0.40
DE  Interaction: Q9UII2; IntAct: EBI-718459,EBI-1053100; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1053100; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475888,EBI-1053100; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-356231,EBI-1053100; Score: 0.40
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0032991;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0010457;
GO  GO:0097711;
GO  GO:0060271;
GO  GO:0050908;
GO  GO:0000086;
GO  GO:0000278;
GO  GO:1905515;
GO  GO:1904781;
GO  GO:0008104;
GO  GO:0033365;
GO  GO:0030997;
GO  GO:0010389;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METRSPGLNNMKPQSLQLVLEEQVLALQQQMAENQAASWRKLKNSQEAQQRQATLVRKLQAKVLQYRSWCQELEKRLEAT
SQ  GGPIPQRWENVEEPNLDELLVRLEEEQQRCESLAEVNTQLRLHMEKADVVNKALREDVEKLTVDWSRARDELMRKESQWQ
SQ  MEQEFFKGYLKGEHGRLLSLWREVVTFRRHFLEMKSATDRDLMELKAEHVRLSGSLLTCCLRLTVGAQSREPNGSGRMDG
SQ  REPAQLLLLLAKTQELEKEAHERSQELIQLKSQGDLEKAELQDRVTELSALLTQSQKQNEDYEKMIKALRETVEILETNH
SQ  TELMEHEASLSRNAQEEKLSLQQVIKDITQVMVEEGDNIAQGSGHENSLELDSSIFSQFDYQDADKALTLVRSVLTRRRQ
SQ  AVQDLRQQLAGCQEAVNLLQQQHDQWEEEGKALRQRLQKLTGERDTLAGQTVDLQGEVDSLSKERELLQKAREELRQQLE
SQ  VLEQEAWRLRRVNVELQLQGDSAQGQKEEQQEELHLAVRERERLQEMLMGLEAKQSESLSELITLREALESSHLEGELLR
SQ  QEQTEVTAALARAEQSIAELSSSENTLKTEVADLRAAAVKLSALNEALALDKVGLNQQLLQLEEENQSVCSRMEAAEQAR
SQ  NALQVDLAEAEKRREALWEKNTHLEAQLQKAEEAGAELQADLRDIQEEKEEIQKKLSESRHQQEAATTQLEQLHQEAKRQ
SQ  EEVLARAVQEKEALVREKAALEVRLQAVERDRQDLAEQLQGLSSAKELLESSLFEAQQQNSVIEVTKGQLEVQIQTVTQA
SQ  KEVIQGEVRCLKLELDTERSQAEQERDAAARQLAQAEQEGKTALEQQKAAHEKEVNQLREKWEKERSWHQQELAKALESL
SQ  EREKMELEMRLKEQQTEMEAIQAQREEERTQAESALCQMQLETEKERVSLLETLLQTQKELADASQQLERLRQDMKVQKL
SQ  KEQETTGILQTQLQEAQRELKEAARQHRDDLAALQEESSSLLQDKMDLQKQVEDLKSQLVAQDDSQRLVEQEVQEKLRET
SQ  QEYNRIQKELEREKASLTLSLMEKEQRLLVLQEADSIRQQELSALRQDMQEAQGEQKELSAQMELLRQEVKEKEADFLAQ
SQ  EAQLLEELEASHITEQQLRASLWAQEAKAAQLQLRLRSTESQLEALAAEQQPGNQAQAQAQLASLYSALQQALGSVCESR
SQ  PELSGGGDSAPSVWGLEPDQNGARSLFKRGPLLTALSAEAVASALHKLHQDLWKTQQTRDVLRDQVQKLEERLTDTEAEK
SQ  SQVHTELQDLQRQLSQNQEEKSKWEGKQNSLESELMELHETMASLQSRLRRAELQRMEAQGERELLQAAKENLTAQVEHL
SQ  QAAVVEARAQASAAGILEEDLRTARSALKLKNEEVESERERAQALQEQGELKVAQGKALQENLALLTQTLAEREEEVETL
SQ  RGQIQELEKQREMQKAALELLSLDLKKRNQEVDLQQEQIQELEKCRSVLEHLPMAVQEREQKLTVQREQIRELEKDRETQ
SQ  RNVLEHQLLELEKKDQMIESQRGQVQDLKKQLVTLECLALELEENHHKMECQQKLIKELEGQRETQRVALTHLTLDLEER
SQ  SQELQAQSSQIHDLESHSTVLARELQERDQEVKSQREQIEELQRQKEHLTQDLERRDQELMLQKERIQVLEDQRTRQTKI
SQ  LEEDLEQIKLSLRERGRELTTQRQLMQERAEEGKGPSKAQRGSLEHMKLILRDKEKEVECQQEHIHELQELKDQLEQQLQ
SQ  GLHRKVGETSLLLSQREQEIVVLQQQLQEAREQGELKEQSLQSQLDEAQRALAQRDQELEALQQEQQQAQGQEERVKEKA
SQ  DALQGALEQAHMTLKERHGELQDHKEQARRLEEELAVEGRRVQALEEVLGDLRAESREQEKALLALQQQCAEQAQEHEVE
SQ  TRALQDSWLQAQAVLKERDQELEALRAESQSSRHQEEAARARAEALQEALGKAHAALQGKEQHLLEQAELSRSLEASTAT
SQ  LQASLDACQAHSRQLEEALRIQEGEIQDQDLRYQEDVQQLQQALAQRDEELRHQQEREQLLEKSLAQRVQENMIQEKQNL
SQ  GQEREEEEIRGLHQSVRELQLTLAQKEQEILELRETQQRNNLEALPHSHKTSPMEEQSLKLDSLEPRLQRELERLQAALR
SQ  QTEAREIEWREKAQDLALSLAQTKASVSSLQEVAMFLQASVLERDSEQQRLQDELELTRRALEKERLHSPGATSTAELGS
SQ  RGEQGVQLGEVSGVEAEPSPDGMEKQSWRQRLEHLQQAVARLEIDRSRLQRHNVQLRSTLEQVERERRKLKREAMRAAQA
SQ  GSLEISKATASSPTQQDGRGQKNSDAKCVAELQKEVVLLQAQLTLERKQKQDYITRSAQTSRELAGLHHSLSHSLLAVAQ
SQ  APEATVLEAETRRLDESLTQSLTSPGPVLLHPSPSTTQAASR
//
ID  P70245;
PN  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
GN  Ebp;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
DR  UNIPROT: P70245;
DR  UNIPROT: Q9CSP4;
DR  Pfam: PF05241;
DR  PROSITE: PS51751;
DE  Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}.
DE  Disease: Note=Defects in Ebp are a cause of 'Tattered' (Td) which is an X-linked, semidominant mouse mutation associated with prenatal male lethality. Heterozygous females are small and at 4 to 5 days of age develop patches of hyperkeratotic skin where no hair grows, resulting in a striping of the coat in adults. Craniofacial anomalies and twisted toes have also been observed in some affected females.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0000247;
GO  GO:0047750;
GO  GO:0004769;
GO  GO:0006695;
GO  GO:0030097;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTTNTVPLHPYWPRHLKLDNFVPNDLPTSHILVGLFSISGGLIVITWLLSSRASVVPLGAGRRLALCWFAVCTFIHLVIE
SQ  GWFSLYNGILLEDQAFLSQLWKEYSKGDSRYILSDSFVVCMETVTACLWGPLSLWVVIAFLRQQPFRFVLQLVVSMGQIY
SQ  GDVLYFLTELHEGLQHGEIGHPVYFWFYFVFLNAVWLVIPSILVLDAIKHLTSAQSVLDSKVMKIKSKHN
//
ID  Q15056;
PN  Eukaryotic translation initiation factor 4H;
GN  EIF4H;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q15056;
DR  UNIPROT: A8K3R1;
DR  UNIPROT: D3DXF6;
DR  UNIPROT: D3DXF8;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DR  OMIM: 603431;
DR  DisGeNET: 7458;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.
DE  Disease: Note=EIF4H is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of EIF4H may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000269|PubMed:8812460}.
DE  Reference Proteome: Yes;
DE  Interaction: P60842; IntAct: EBI-73449,EBI-748492; Score: 0.54
DE  Interaction: Q6MZP7; IntAct: EBI-1389411,EBI-748492; Score: 0.35
DE  Interaction: Q9H3H3; IntAct: EBI-721765,EBI-748492; Score: 0.74
DE  Interaction: Q8TBB1; IntAct: EBI-739832,EBI-748492; Score: 0.67
DE  Interaction: Q91W50; IntAct: EBI-8318466,EBI-748492; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-748492; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-748492; Score: 0.35
DE  Interaction: P10225; IntAct: EBI-6148417,EBI-748492; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-748492; Score: 0.35
DE  Interaction: A0A384LA14; IntAct: EBI-748492,EBI-2845602; Score: 0.37
DE  Interaction: A0A1S0QL17; IntAct: EBI-2814598,EBI-748492; Score: 0.37
DE  Interaction: Q14164; IntAct: EBI-748492,EBI-307369; Score: 0.40
DE  Interaction: O60739; IntAct: EBI-748492,EBI-1043343; Score: 0.40
DE  Interaction: P23508; IntAct: EBI-307531,EBI-748492; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475877,EBI-748492; Score: 0.35
GO  GO:0005829;
GO  GO:0016281;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0045296;
GO  GO:0003723;
GO  GO:0008135;
GO  GO:0003743;
GO  GO:0048589;
GO  GO:0006446;
GO  GO:0019953;
GO  GO:0006413;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRD
SQ  DFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPRE
SQ  EVVQKEQE
//
ID  Q96HJ5;
PN  Membrane-spanning 4-domains subfamily A member 3;
GN  MS4A3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Located in the perinuclear area.
DR  UNIPROT: Q96HJ5;
DR  UNIPROT: A8MTP8;
DR  UNIPROT: Q8NHW2;
DR  Pfam: PF04103;
DR  OMIM: 606498;
DR  DisGeNET: 932;
DE  Function: Hematopoietic modulator for the G1-S cell cycle transition. Modulates the level of phosphorylation of cyclin-dependent kinase 2 (CDK2) through its direct binding to cyclin-dependent kinase inhibitor 3 (CDKN3/KAP). {ECO:0000269|PubMed:11781350}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y6I9; IntAct: EBI-10329860,EBI-12806656; Score: 0.60
DE  Interaction: Q9Y267; IntAct: EBI-12824155,EBI-12806656; Score: 0.60
DE  Interaction: Q99437; IntAct: EBI-12806656,EBI-3904417; Score: 0.56
DE  Interaction: A2RU14; IntAct: EBI-12806656,EBI-10173151; Score: 0.56
DE  Interaction: Q6ZP80; IntAct: EBI-12806656,EBI-10255122; Score: 0.56
DE  Interaction: P56747; IntAct: EBI-12806656,EBI-12955011; Score: 0.56
DE  Interaction: O95393; IntAct: EBI-12806656,EBI-3922513; Score: 0.56
DE  Interaction: Q01628; IntAct: EBI-7932862,EBI-12806656; Score: 0.56
DE  Interaction: P21854; IntAct: EBI-12806656,EBI-307924; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-12806656,EBI-10827839; Score: 0.56
DE  Interaction: Q8IY26; IntAct: EBI-12806656,EBI-11721828; Score: 0.56
DE  Interaction: Q9BZL3; IntAct: EBI-12806656,EBI-741850; Score: 0.56
DE  Interaction: O43765; IntAct: EBI-12806656,EBI-347996; Score: 0.56
DE  Interaction: Q9NY91; IntAct: EBI-12806656,EBI-12409133; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-12806656,EBI-2844246; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-12806656,EBI-718439; Score: 0.56
DE  Interaction: P52803; IntAct: EBI-12806656,EBI-1753674; Score: 0.56
DE  Interaction: P54852; IntAct: EBI-12806656,EBI-3907816; Score: 0.56
DE  Interaction: Q96EC8; IntAct: EBI-12806656,EBI-751210; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-8652744,EBI-12806656; Score: 0.56
DE  Interaction: O95832; IntAct: EBI-12806656,EBI-723889; Score: 0.56
DE  Interaction: Q8N0U8; IntAct: EBI-12806656,EBI-11337915; Score: 0.56
DE  Interaction: Q96CE8; IntAct: EBI-12806656,EBI-13351685; Score: 0.56
DE  Interaction: Q6UX40; IntAct: EBI-12806656,EBI-12845616; Score: 0.56
DE  Interaction: Q8WW34-2; IntAct: EBI-12806656,EBI-11528917; Score: 0.56
DE  Interaction: Q12983; IntAct: EBI-12806656,EBI-749464; Score: 0.56
DE  Interaction: P19397; IntAct: EBI-12806656,EBI-6657396; Score: 0.56
DE  Interaction: Q5J8X5; IntAct: EBI-12806656,EBI-12070086; Score: 0.56
DE  Interaction: Q9UNK0; IntAct: EBI-12806656,EBI-727240; Score: 0.56
DE  Interaction: Q8WVX3-2; IntAct: EBI-12806656,EBI-12003442; Score: 0.56
DE  Interaction: Q9P0B6; IntAct: EBI-12806656,EBI-9083477; Score: 0.56
DE  Interaction: Q9UKR5; IntAct: EBI-12806656,EBI-711490; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-8640191,EBI-12806656; Score: 0.56
DE  Interaction: P55061; IntAct: EBI-12806656,EBI-1045825; Score: 0.56
DE  Interaction: Q16617; IntAct: EBI-12806656,EBI-3919611; Score: 0.56
DE  Interaction: P24593; IntAct: EBI-12806656,EBI-720480; Score: 0.56
DE  Interaction: P60201-2; IntAct: EBI-12806656,EBI-12188331; Score: 0.56
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035579;
GO  GO:0043312;
GO  GO:0051726;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASHEVDNAELGSASAHGTPGSEAGPEELNTSVYQPIDGSPDYQKAKLQVLGAIQILNAAMILALGVFLGSLQYPYHFQK
SQ  HFFFFTFYTGYPIWGAVFFCSSGTLSVVAGIKPTRTWIQNSFGMNIASATIALVGTAFLSLNIAVNIQSLRSCHSSSESP
SQ  DLCNYMGSISNGMVSLLLILTLLELCVTISTIAMWCNANCCNSREEISSPPNSV
//
ID  Q24568;
PN  Netrin-B;
GN  NetB;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29513217}. Note=Expressed in the perinuclear region of the oldest most anterior lamina neurons at 24 hours after puparium formation. {ECO:0000269|PubMed:29513217}.
DR  UNIPROT: Q24568;
DR  UNIPROT: Q9VY23;
DR  Pfam: PF00053;
DR  Pfam: PF00055;
DR  Pfam: PF01759;
DR  PROSITE: PS00022;
DR  PROSITE: PS01248;
DR  PROSITE: PS50027;
DR  PROSITE: PS51117;
DR  PROSITE: PS50189;
DE  Function: Netrins control guidance of CNS commissural axons and peripheral motor axons (PubMed:8780645, PubMed:8780646, PubMed:11719202). Its association with either fra or unc-5 receptors will lead to axon attraction or repulsion, respectively (PubMed:11719202). While short-range repulsion requires both fra and unc-5 receptors, long-range repulsion only requires unc-5 (PubMed:11719202). {ECO:0000269|PubMed:11719202, ECO:0000269|PubMed:8780645, ECO:0000269|PubMed:8780646}.
DE  Reference Proteome: Yes;
DE  Interaction: P20240; IntAct: EBI-3406532,EBI-115143; Score: 0.35
DE  Interaction: P49021; IntAct: EBI-3406532,EBI-266295; Score: 0.35
DE  Interaction: P31368; IntAct: EBI-3406532,EBI-150557; Score: 0.35
DE  Interaction: Q9VJA9; IntAct: EBI-3406532,EBI-175637; Score: 0.35
DE  Interaction: Q9V3E7; IntAct: EBI-3406532,EBI-109769; Score: 0.46
DE  Interaction: Q9VL48; IntAct: EBI-3406532,EBI-174402; Score: 0.46
DE  Interaction: P05130-2; IntAct: EBI-3406532,EBI-3406439; Score: 0.46
DE  Interaction: Q8IML5; IntAct: EBI-3406532,EBI-3406340; Score: 0.35
DE  Interaction: Q9W263; IntAct: EBI-3406532,EBI-106473; Score: 0.35
DE  Interaction: A1Z7K2; IntAct: EBI-3406532,EBI-136170; Score: 0.35
DE  Interaction: Q9VA23; IntAct: EBI-3406532,EBI-3406529; Score: 0.46
DE  Interaction: Q9VK08; IntAct: EBI-3406532,EBI-3407972; Score: 0.35
DE  Interaction: Q960V3-2; IntAct: EBI-3406532,EBI-3406327; Score: 0.46
DE  Interaction: Q7KML4; IntAct: EBI-3406532,EBI-119435; Score: 0.35
DE  Interaction: M9NE38; IntAct: EBI-3406532,EBI-2509181; Score: 0.35
DE  Interaction: Q9W4Z9; IntAct: EBI-3406532,EBI-174129; Score: 0.35
DE  Interaction: Q00174; IntAct: EBI-3406532,EBI-138476; Score: 0.46
DE  Interaction: P17672-1; IntAct: EBI-3406532,EBI-3407667; Score: 0.35
DE  Interaction: Q9VH64; IntAct: EBI-3406532,EBI-88845; Score: 0.35
DE  Interaction: Q9VLC0; IntAct: EBI-3406532,EBI-124019; Score: 0.35
DE  Interaction: Q9VYS3; IntAct: EBI-3406532,EBI-3404907; Score: 0.35
DE  Interaction: Q7K2X1; IntAct: EBI-3406532,EBI-185330; Score: 0.35
DE  Interaction: Q9VH20; IntAct: EBI-3406532,EBI-104191; Score: 0.35
DE  Interaction: Q95R34; IntAct: EBI-3406532,EBI-3406662; Score: 0.35
DE  Interaction: Q9VF72; IntAct: EBI-3406532,EBI-119219; Score: 0.35
DE  Interaction: Q9VGI8; IntAct: EBI-3406532,EBI-128453; Score: 0.35
DE  Interaction: Q9VGW4; IntAct: EBI-3406532,EBI-143134; Score: 0.46
DE  Interaction: Q9W3E1; IntAct: EBI-3406532,EBI-96015; Score: 0.35
DE  Interaction: Q7KVD1; IntAct: EBI-3406532,EBI-164173; Score: 0.46
DE  Interaction: Q8SX76; IntAct: EBI-3406532,EBI-195876; Score: 0.35
DE  Interaction: P48608; IntAct: EBI-3406532,EBI-135200; Score: 0.46
DE  Interaction: Q9VE94; IntAct: EBI-3406532,EBI-3407489; Score: 0.35
DE  Interaction: Q9VEX6; IntAct: EBI-3406532,EBI-3407343; Score: 0.35
DE  Interaction: P39770; IntAct: EBI-3406532,EBI-146567; Score: 0.35
DE  Interaction: Q86B49; IntAct: EBI-3406532,EBI-3407544; Score: 0.35
DE  Interaction: Q9VY43; IntAct: EBI-3406532,EBI-123786; Score: 0.46
DE  Interaction: Q9VZF5; IntAct: EBI-3406532,EBI-140069; Score: 0.46
DE  Interaction: Q8IQ71; IntAct: EBI-3406532,EBI-3404397; Score: 0.35
DE  Interaction: Q9VK35; IntAct: EBI-3406532,EBI-2507613; Score: 0.35
DE  Interaction: Q9U969-1; IntAct: EBI-3406532,EBI-3407869; Score: 0.35
DE  Interaction: Q8IQI2; IntAct: EBI-3406532,EBI-3407397; Score: 0.35
DE  Interaction: Q9VPG1; IntAct: EBI-3406532,EBI-117581; Score: 0.35
DE  Interaction: Q9VZI3; IntAct: EBI-3406532,EBI-142656; Score: 0.35
DE  Interaction: Q8SWT2; IntAct: EBI-3406532,EBI-183314; Score: 0.35
DE  Interaction: P11046; IntAct: EBI-3406532,EBI-176205; Score: 0.35
DE  Interaction: Q9V3H9; IntAct: EBI-3406532,EBI-189139; Score: 0.35
DE  Interaction: A1ZBL7; IntAct: EBI-3406532,EBI-189834; Score: 0.35
DE  Interaction: Q9VSA4; IntAct: EBI-3406532,EBI-158642; Score: 0.35
DE  Interaction: Q9U5L1; IntAct: EBI-3406532,EBI-121637; Score: 0.35
DE  Interaction: Q9W0T1-3; IntAct: EBI-3406532,EBI-3407673; Score: 0.46
DE  Interaction: Q8T4D6; IntAct: EBI-3406532,EBI-3406872; Score: 0.35
DE  Interaction: Q9VLY7; IntAct: EBI-3406532,EBI-163846; Score: 0.35
DE  Interaction: Q9VZY3; IntAct: EBI-3406532,EBI-3406541; Score: 0.35
DE  Interaction: Q8IP51; IntAct: EBI-3406532,EBI-498443; Score: 0.46
DE  Interaction: P07207; IntAct: EBI-3406532,EBI-103438; Score: 0.35
DE  Interaction: Q9VQI9; IntAct: EBI-3406532,EBI-141144; Score: 0.46
DE  Interaction: Q9I7M8; IntAct: EBI-3406532,EBI-166721; Score: 0.35
DE  Interaction: Q9VCP0-1; IntAct: EBI-3406532,EBI-3407072; Score: 0.35
DE  Interaction: P24014-2; IntAct: EBI-3406532,EBI-3408048; Score: 0.35
DE  Interaction: A1Z8N1; IntAct: EBI-3406532,EBI-101212; Score: 0.35
DE  Interaction: P48610-2; IntAct: EBI-3406532,EBI-1443832; Score: 0.35
DE  Interaction: Q7KTL4; IntAct: EBI-3406532,EBI-870738; Score: 0.35
DE  Interaction: Q9VXM5; IntAct: EBI-3406532,EBI-3406320; Score: 0.35
DE  Interaction: Q9XZ21; IntAct: EBI-3406532,EBI-143278; Score: 0.35
DE  Interaction: Q9VQ08; IntAct: EBI-3406532,EBI-153643; Score: 0.35
DE  Interaction: Q9VPL5; IntAct: EBI-3406532,EBI-165122; Score: 0.35
DE  Interaction: Q9VIJ0; IntAct: EBI-3406532,EBI-94912; Score: 0.35
DE  Interaction: Q86BB1; IntAct: EBI-3406532,EBI-84258; Score: 0.35
DE  Interaction: Q9VGI6; IntAct: EBI-3406532,EBI-162613; Score: 0.35
DE  Interaction: Q9V3R1; IntAct: EBI-3406532,EBI-143174; Score: 0.35
DE  Interaction: P00522; IntAct: EBI-3406532,EBI-534090; Score: 0.35
DE  Interaction: Q9VBF5; IntAct: EBI-3406532,EBI-3406899; Score: 0.35
DE  Interaction: P13217-1; IntAct: EBI-3406532,EBI-3406224; Score: 0.35
DE  Interaction: Q7KTT0; IntAct: EBI-3406532,EBI-107806; Score: 0.35
DE  Interaction: Q9VBL3; IntAct: EBI-3406532,EBI-115399; Score: 0.35
DE  Interaction: A1Z9G1; IntAct: EBI-3406532,EBI-2508424; Score: 0.35
DE  Interaction: Q8IMA6; IntAct: EBI-3406532,EBI-3408021; Score: 0.35
DE  Interaction: Q9VN57; IntAct: EBI-3406532,EBI-169772; Score: 0.46
DE  Interaction: Q9VS62; IntAct: EBI-3406532,EBI-108483; Score: 0.35
DE  Interaction: O16102; IntAct: EBI-3406532,EBI-188287; Score: 0.35
DE  Interaction: O61366; IntAct: EBI-3406532,EBI-193211; Score: 0.35
DE  Interaction: Q9NFV8; IntAct: EBI-3406532,EBI-3406211; Score: 0.35
DE  Interaction: P42787-5; IntAct: EBI-3406532,EBI-3407781; Score: 0.35
DE  Interaction: P18490; IntAct: EBI-3406532,EBI-114125; Score: 0.46
DE  Interaction: Q9V769; IntAct: EBI-3406532,EBI-170059; Score: 0.35
DE  Interaction: O18475; IntAct: EBI-3406532,EBI-3407560; Score: 0.46
DE  Interaction: Q9VSK9; IntAct: EBI-3406532,EBI-151143; Score: 0.46
DE  Interaction: Q7JR82; IntAct: EBI-3406532,EBI-3403437; Score: 0.35
DE  Interaction: Q9W391-1; IntAct: EBI-3406532,EBI-3407103; Score: 0.46
DE  Interaction: Q8T421; IntAct: EBI-3406532,EBI-3407249; Score: 0.35
DE  Interaction: Q9V3Y8; IntAct: EBI-3406532,EBI-139574; Score: 0.46
DE  Interaction: A1ZAE2; IntAct: EBI-3406532,EBI-105655; Score: 0.35
DE  Interaction: Q8INT5; IntAct: EBI-3406532,EBI-3407121; Score: 0.46
DE  Interaction: Q4V4S9; IntAct: EBI-3406532,EBI-3407372; Score: 0.35
DE  Interaction: Q9VG73; IntAct: EBI-3406532,EBI-151485; Score: 0.35
DE  Interaction: Q86B91; IntAct: EBI-3406532,EBI-188776; Score: 0.35
DE  Interaction: Q9VZS7; IntAct: EBI-3406532,EBI-2508827; Score: 0.35
DE  Interaction: Q8IR22; IntAct: EBI-3406532,EBI-3404086; Score: 0.35
DE  Interaction: P26019; IntAct: EBI-3406532,EBI-419315; Score: 0.35
DE  Interaction: Q9VPW5; IntAct: EBI-3406532,EBI-143897; Score: 0.35
DE  Interaction: Q9VJX4; IntAct: EBI-3406532,EBI-117739; Score: 0.35
DE  Interaction: Q9VKG0; IntAct: EBI-3406532,EBI-3403315; Score: 0.35
DE  Interaction: P20659-1; IntAct: EBI-3406532,EBI-3406352; Score: 0.46
DE  Interaction: Q9VVQ9; IntAct: EBI-3406532,EBI-3404281; Score: 0.35
DE  Interaction: Q8IPN1; IntAct: EBI-3406532,EBI-95123; Score: 0.35
DE  Interaction: Q7KNQ9; IntAct: EBI-3406532,EBI-111569; Score: 0.35
DE  Interaction: Q9VS41; IntAct: EBI-3406532,EBI-165294; Score: 0.35
DE  Interaction: Q9VSG7; IntAct: EBI-3406532,EBI-3406689; Score: 0.35
DE  Interaction: Q9VXY2; IntAct: EBI-3406532,EBI-159039; Score: 0.46
DE  Interaction: P05084; IntAct: EBI-3406532,EBI-176716; Score: 0.35
DE  Interaction: Q7KT06; IntAct: EBI-3406532,EBI-140557; Score: 0.35
DE  Interaction: O76464; IntAct: EBI-3406532,EBI-133873; Score: 0.35
DE  Interaction: O97159; IntAct: EBI-3406532,EBI-112333; Score: 0.35
DE  Interaction: Q9W5E0-1; IntAct: EBI-3406532,EBI-3407711; Score: 0.35
DE  Interaction: Q9VY05; IntAct: EBI-3406532,EBI-3407862; Score: 0.35
DE  Interaction: Q9VB11; IntAct: EBI-3406532,EBI-2507853; Score: 0.46
DE  Interaction: A1ZBH5; IntAct: EBI-3406532,EBI-3406614; Score: 0.35
DE  Interaction: Q9VWR5; IntAct: EBI-3406532,EBI-118095; Score: 0.35
DE  Interaction: Q9VD51; IntAct: EBI-3406532,EBI-139183; Score: 0.46
DE  Interaction: P18171-1; IntAct: EBI-3406532,EBI-3406906; Score: 0.46
DE  Interaction: Q9W5E8; IntAct: EBI-3406532,EBI-229586; Score: 0.35
DE  Interaction: O18388; IntAct: EBI-3406532,EBI-155558; Score: 0.35
DE  Interaction: Q8IQ27; IntAct: EBI-3406532,EBI-86319; Score: 0.46
DE  Interaction: Q9VCN1; IntAct: EBI-3406532,EBI-173478; Score: 0.46
DE  Interaction: Q8IR12; IntAct: EBI-3406532,EBI-3406795; Score: 0.35
DE  Interaction: P13496; IntAct: EBI-3406532,EBI-157742; Score: 0.35
DE  Interaction: Q9VZK8; IntAct: EBI-3406532,EBI-151496; Score: 0.35
DE  Interaction: Q1EBX4; IntAct: EBI-3406532,EBI-3406950; Score: 0.35
DE  Interaction: Q0E8J0; IntAct: EBI-3406532,EBI-91014; Score: 0.35
DE  Interaction: Q8MSU4; IntAct: EBI-3406532,EBI-167328; Score: 0.35
DE  Interaction: Q9VNA1; IntAct: EBI-3406532,EBI-2509088; Score: 0.46
DE  Interaction: Q9W1G0; IntAct: EBI-3406532,EBI-2108630; Score: 0.35
DE  Interaction: P16568; IntAct: EBI-3406532,EBI-112159; Score: 0.46
DE  Interaction: Q9VM67; IntAct: EBI-3406532,EBI-147466; Score: 0.46
DE  Interaction: Q01820; IntAct: EBI-3406532,EBI-176400; Score: 0.35
DE  Interaction: Q9VRX7; IntAct: EBI-3406532,EBI-108965; Score: 0.35
DE  Interaction: Q9Y105; IntAct: EBI-3406532,EBI-109039; Score: 0.35
DE  Interaction: Q9VJ14; IntAct: EBI-3406532,EBI-75248; Score: 0.35
DE  Interaction: Q9VUS0; IntAct: EBI-3406532,EBI-3407515; Score: 0.35
DE  Interaction: A1Z8S6; IntAct: EBI-3406532,EBI-2890470; Score: 0.35
DE  Interaction: Q9W2I5; IntAct: EBI-3406532,EBI-3407976; Score: 0.35
DE  Interaction: Q9VAT1; IntAct: EBI-3406532,EBI-102630; Score: 0.46
DE  Interaction: Q9V3E9; IntAct: EBI-3406532,EBI-100795; Score: 0.46
DE  Interaction: Q9VQV3; IntAct: EBI-3406532,EBI-3403380; Score: 0.35
DE  Interaction: Q7JQ32; IntAct: EBI-3406532,EBI-83327; Score: 0.35
DE  Interaction: Q9W4X4; IntAct: EBI-3406532,EBI-2508843; Score: 0.35
DE  Interaction: P04197; IntAct: EBI-3406532,EBI-75933; Score: 0.35
DE  Interaction: Q9VD22; IntAct: EBI-3406532,EBI-164569; Score: 0.35
DE  Interaction: Q967S0; IntAct: EBI-3406532,EBI-145750; Score: 0.35
DE  Interaction: Q9VWH5; IntAct: EBI-3406532,EBI-3407956; Score: 0.35
DE  Interaction: Q9VUH9; IntAct: EBI-3406532,EBI-127625; Score: 0.46
DE  Interaction: Q9VWC0; IntAct: EBI-3406532,EBI-152269; Score: 0.46
DE  Interaction: Q9VIP9; IntAct: EBI-3406532,EBI-147085; Score: 0.35
DE  Interaction: Q9W3J0; IntAct: EBI-3406532,EBI-175576; Score: 0.35
DE  Interaction: Q9VSE8; IntAct: EBI-3406532,EBI-3408175; Score: 0.35
DE  Interaction: Q9W021; IntAct: EBI-3406532,EBI-3407002; Score: 0.35
DE  Interaction: Q9VDA0; IntAct: EBI-3406532,EBI-90318; Score: 0.35
DE  Interaction: Q9VZ81; IntAct: EBI-3406532,EBI-193349; Score: 0.35
DE  Interaction: Q9VQ54; IntAct: EBI-3406532,EBI-3402096; Score: 0.35
DE  Interaction: Q8IRL2; IntAct: EBI-3406532,EBI-3406987; Score: 0.46
DE  Interaction: Q8INH7; IntAct: EBI-3406532,EBI-112263; Score: 0.35
DE  Interaction: Q8IRR2; IntAct: EBI-3406532,EBI-3407903; Score: 0.35
DE  Interaction: Q9I7F7; IntAct: EBI-3406532,EBI-3406602; Score: 0.35
DE  Interaction: Q9VK58; IntAct: EBI-3406532,EBI-472027; Score: 0.35
DE  Interaction: Q9I7R5; IntAct: EBI-3406532,EBI-3406979; Score: 0.35
DE  Interaction: Q9VVB5; IntAct: EBI-3406532,EBI-97513; Score: 0.35
DE  Interaction: A1ZAH1; IntAct: EBI-3406532,EBI-195942; Score: 0.46
DE  Interaction: Q9W0D3; IntAct: EBI-3406532,EBI-182108; Score: 0.46
DE  Interaction: Q9VES5; IntAct: EBI-3406532,EBI-3407743; Score: 0.35
DE  Interaction: Q9VMS3; IntAct: EBI-3406532,EBI-93318; Score: 0.35
DE  Interaction: Q9W1N6; IntAct: EBI-3406532,EBI-2508519; Score: 0.35
DE  Interaction: Q86NK9; IntAct: EBI-3406532,EBI-131980; Score: 0.35
DE  Interaction: Q8IR23; IntAct: EBI-3406532,EBI-868068; Score: 0.35
DE  Interaction: A1Z700; IntAct: EBI-3406532,EBI-501095; Score: 0.35
DE  Interaction: Q9VUH5; IntAct: EBI-3406532,EBI-3406436; Score: 0.35
DE  Interaction: Q9W3H8; IntAct: EBI-3406532,EBI-3407451; Score: 0.35
DE  Interaction: P12428; IntAct: EBI-3406532,EBI-122973; Score: 0.35
DE  Interaction: Q8IRV8; IntAct: EBI-3406532,EBI-2509100; Score: 0.35
DE  Interaction: Q8IN06; IntAct: EBI-3406532,EBI-3406720; Score: 0.35
DE  Interaction: Q9VSM1; IntAct: EBI-3406532,EBI-499790; Score: 0.46
DE  Interaction: Q9VA45; IntAct: EBI-3406532,EBI-191164; Score: 0.46
DE  Interaction: Q9W0X7; IntAct: EBI-3406532,EBI-3404030; Score: 0.35
DE  Interaction: Q9VPI9; IntAct: EBI-3406532,EBI-108869; Score: 0.35
DE  Interaction: Q9VC62; IntAct: EBI-3406532,EBI-3407579; Score: 0.35
DE  Interaction: Q9VP22; IntAct: EBI-3406532,EBI-1627953; Score: 0.46
DE  Interaction: Q9VCJ9; IntAct: EBI-3406532,EBI-3407541; Score: 0.35
DE  Interaction: Q9VXQ2; IntAct: EBI-3406532,EBI-127096; Score: 0.46
DE  Interaction: Q86B80; IntAct: EBI-3406532,EBI-158531; Score: 0.35
DE  Interaction: Q9V4C8-1; IntAct: EBI-3406532,EBI-3408191; Score: 0.35
DE  Interaction: Q9VL65; IntAct: EBI-3406532,EBI-83201; Score: 0.35
DE  Interaction: Q27237-2; IntAct: EBI-3406532,EBI-3406766; Score: 0.35
DE  Interaction: Q9VPS7; IntAct: EBI-3406532,EBI-3406692; Score: 0.35
DE  Interaction: Q86B52; IntAct: EBI-3406532,EBI-3407261; Score: 0.46
DE  Interaction: P22814; IntAct: EBI-3406532,EBI-868309; Score: 0.35
DE  Interaction: Q8IRD5; IntAct: EBI-3406532,EBI-3407384; Score: 0.35
DE  Interaction: P25439-1; IntAct: EBI-3406532,EBI-3408079; Score: 0.35
DE  Interaction: P20354-1; IntAct: EBI-3406532,EBI-3408005; Score: 0.35
DE  Interaction: Q9VN82; IntAct: EBI-3406532,EBI-3406505; Score: 0.35
DE  Interaction: Q9VYW3; IntAct: EBI-3406532,EBI-90835; Score: 0.35
DE  Interaction: Q8SYD9; IntAct: EBI-3406532,EBI-98461; Score: 0.35
DE  Interaction: Q9VPX3; IntAct: EBI-3406532,EBI-84444; Score: 0.35
DE  Interaction: Q9VEX0; IntAct: EBI-3406532,EBI-107137; Score: 0.35
DE  Interaction: Q9XYA7; IntAct: EBI-3406532,EBI-3407409; Score: 0.35
DE  Interaction: Q7KSD3; IntAct: EBI-3406532,EBI-3407171; Score: 0.35
DE  Interaction: A1ZAJ8; IntAct: EBI-3406532,EBI-158400; Score: 0.35
DE  Interaction: Q9VKM1; IntAct: EBI-3406532,EBI-3406276; Score: 0.35
DE  Interaction: Q9XYU0; IntAct: EBI-3406532,EBI-496657; Score: 0.35
DE  Interaction: Q9VZT7; IntAct: EBI-3406532,EBI-153240; Score: 0.35
DE  Interaction: Q9VAG2; IntAct: EBI-3406532,EBI-3406728; Score: 0.35
DE  Interaction: Q8MT77; IntAct: EBI-3406532,EBI-3406391; Score: 0.35
DE  Interaction: Q9VJ30; IntAct: EBI-3406532,EBI-154050; Score: 0.35
DE  Interaction: Q9VB72; IntAct: EBI-3406532,EBI-96596; Score: 0.46
DE  Interaction: Q9W350; IntAct: EBI-3406532,EBI-132638; Score: 0.35
DE  Interaction: Q9VRM7; IntAct: EBI-3406532,EBI-154881; Score: 0.35
DE  Interaction: Q9VT19; IntAct: EBI-3406532,EBI-188920; Score: 0.35
DE  Interaction: Q9W002; IntAct: EBI-3406532,EBI-173708; Score: 0.35
DE  Interaction: Q9W2N0; IntAct: EBI-3406532,EBI-173404; Score: 0.35
DE  Interaction: Q9VXW9; IntAct: EBI-3406532,EBI-181668; Score: 0.35
DE  Interaction: Q9VQ76; IntAct: EBI-3406532,EBI-3407478; Score: 0.35
DE  Interaction: Q9W0T7; IntAct: EBI-3406532,EBI-3404132; Score: 0.35
DE  Interaction: Q9W1H0; IntAct: EBI-3406532,EBI-181659; Score: 0.46
DE  Interaction: Q7KV92; IntAct: EBI-3406532,EBI-3407153; Score: 0.35
DE  Interaction: Q9VU16; IntAct: EBI-3406532,EBI-99531; Score: 0.35
DE  Interaction: P28750; IntAct: EBI-3406532,EBI-191747; Score: 0.46
DE  Interaction: Q9VQ79-1; IntAct: EBI-3406532,EBI-3407803; Score: 0.35
DE  Interaction: Q9VWF2; IntAct: EBI-3406532,EBI-131186; Score: 0.46
DE  Interaction: P26675; IntAct: EBI-3406532,EBI-82070; Score: 0.35
DE  Interaction: Q9W484; IntAct: EBI-3406532,EBI-156280; Score: 0.46
DE  Interaction: Q86LG9; IntAct: EBI-3406532,EBI-3407109; Score: 0.35
DE  Interaction: Q9W2P0; IntAct: EBI-3406532,EBI-1628748; Score: 0.35
DE  Interaction: Q95V55-2; IntAct: EBI-3406532,EBI-3406421; Score: 0.35
DE  Interaction: A1Z7J0; IntAct: EBI-3406532,EBI-132882; Score: 0.35
DE  Interaction: Q9VI17; IntAct: EBI-3406532,EBI-3406937; Score: 0.35
DE  Interaction: Q7KTX4; IntAct: EBI-3406532,EBI-3406840; Score: 0.35
DE  Interaction: Q9VXA3; IntAct: EBI-3406532,EBI-102203; Score: 0.35
DE  Interaction: Q8MS59; IntAct: EBI-3406532,EBI-3407751; Score: 0.35
DE  Interaction: Q9VW51; IntAct: EBI-3406532,EBI-148823; Score: 0.35
DE  Interaction: P34739; IntAct: EBI-3406532,EBI-190656; Score: 0.35
DE  Interaction: Q9VA73-2; IntAct: EBI-3406532,EBI-3406703; Score: 0.46
DE  Interaction: A1Z7Z9; IntAct: EBI-3406532,EBI-3406448; Score: 0.46
DE  Interaction: P52034-2; IntAct: EBI-3406532,EBI-3406511; Score: 0.35
DE  Interaction: Q9VW97; IntAct: EBI-3406532,EBI-3407058; Score: 0.35
DE  Interaction: Q9V9Q2; IntAct: EBI-3406532,EBI-114989; Score: 0.35
DE  Interaction: Q9W4H1; IntAct: EBI-3406532,EBI-107424; Score: 0.35
DE  Interaction: Q9W0L7; IntAct: EBI-3406532,EBI-108609; Score: 0.35
DE  Interaction: Q8I0P1; IntAct: EBI-3406532,EBI-154500; Score: 0.35
DE  Interaction: A1Z9W4; IntAct: EBI-3406532,EBI-2508484; Score: 0.35
DE  Interaction: Q9VPR0; IntAct: EBI-3406532,EBI-2508802; Score: 0.35
DE  Interaction: Q9VFE4; IntAct: EBI-3406532,EBI-108627; Score: 0.35
DE  Interaction: P13677; IntAct: EBI-3406532,EBI-130595; Score: 0.35
DE  Interaction: Q9VYK6; IntAct: EBI-3406532,EBI-3405162; Score: 0.35
DE  Interaction: Q9VP76; IntAct: EBI-3406532,EBI-3407915; Score: 0.35
DE  Interaction: P18502; IntAct: EBI-3406532,EBI-140029; Score: 0.46
DE  Interaction: Q7JQY8; IntAct: EBI-3406532,EBI-157064; Score: 0.35
DE  Interaction: Q8IN10; IntAct: EBI-3406532,EBI-3407747; Score: 0.35
DE  Interaction: Q9VEP3; IntAct: EBI-3406532,EBI-3406732; Score: 0.35
DE  Interaction: Q9VG60; IntAct: EBI-3406532,EBI-3406685; Score: 0.35
DE  Interaction: Q9XZ22; IntAct: EBI-3406532,EBI-189603; Score: 0.46
DE  Interaction: P25159-1; IntAct: EBI-3406532,EBI-3406255; Score: 0.35
DE  Interaction: Q8IPV3; IntAct: EBI-3406532,EBI-100728; Score: 0.35
DE  Interaction: Q9U6R9; IntAct: EBI-3406532,EBI-122434; Score: 0.46
DE  Interaction: Q00449; IntAct: EBI-3406532,EBI-121715; Score: 0.46
DE  Interaction: Q9VAW1; IntAct: EBI-3406532,EBI-2507864; Score: 0.35
DE  Interaction: Q9W4A9; IntAct: EBI-3406532,EBI-3407506; Score: 0.35
DE  Interaction: Q9VN28; IntAct: EBI-3406532,EBI-3406583; Score: 0.35
DE  Interaction: Q0E9C5; IntAct: EBI-3406532,EBI-2890300; Score: 0.35
DE  Interaction: Q9VP05; IntAct: EBI-3406532,EBI-92171; Score: 0.35
DE  Interaction: P15215; IntAct: EBI-3406532,EBI-150670; Score: 0.35
DE  Interaction: Q9VUA0; IntAct: EBI-3406532,EBI-125261; Score: 0.35
DE  Interaction: Q9VRV9; IntAct: EBI-3406532,EBI-181097; Score: 0.35
DE  Interaction: Q7KTW9; IntAct: EBI-3406532,EBI-2890386; Score: 0.35
DE  Interaction: P22813; IntAct: EBI-3406532,EBI-130048; Score: 0.35
DE  Interaction: Q9W3B8; IntAct: EBI-3406532,EBI-170708; Score: 0.35
DE  Interaction: P26016-1; IntAct: EBI-3406532,EBI-3407640; Score: 0.35
DE  Interaction: Q95TY8; IntAct: EBI-3406532,EBI-3407656; Score: 0.35
DE  Interaction: Q9V9N5; IntAct: EBI-3406532,EBI-3403972; Score: 0.35
DE  Interaction: Q9VXD6; IntAct: EBI-3406532,EBI-143815; Score: 0.35
DE  Interaction: Q9VWE6; IntAct: EBI-3406532,EBI-91923; Score: 0.35
DE  Interaction: A1ZBA1; IntAct: EBI-3406532,EBI-3407609; Score: 0.35
DE  Interaction: Q9W345; IntAct: EBI-3406532,EBI-85123; Score: 0.35
DE  Interaction: Q9W3D1; IntAct: EBI-3406532,EBI-130352; Score: 0.35
DE  Interaction: Q9W0E8; IntAct: EBI-3406532,EBI-155632; Score: 0.46
DE  Interaction: Q9VPH4; IntAct: EBI-3406532,EBI-193999; Score: 0.46
DE  Interaction: Q9VZ60; IntAct: EBI-3406532,EBI-114012; Score: 0.35
DE  Interaction: Q24113; IntAct: EBI-3406532,EBI-89058; Score: 0.35
DE  Interaction: M9PIS3; IntAct: EBI-3406532,EBI-3405597; Score: 0.35
DE  Interaction: Q9V410; IntAct: EBI-3406532,EBI-156792; Score: 0.46
DE  Interaction: Q9VU94; IntAct: EBI-3406532,EBI-3407096; Score: 0.35
DE  Interaction: Q9VBJ2; IntAct: EBI-3406532,EBI-2509129; Score: 0.35
DE  Interaction: P28466; IntAct: EBI-3406532,EBI-127508; Score: 0.35
DE  Interaction: Q9VV61; IntAct: EBI-3406532,EBI-2890575; Score: 0.35
DE  Interaction: Q86BR6; IntAct: EBI-3406532,EBI-105321; Score: 0.35
DE  Interaction: Q24325; IntAct: EBI-3406532,EBI-141415; Score: 0.35
DE  Interaction: C0PUW9; IntAct: EBI-3406532,EBI-3406830; Score: 0.35
DE  Interaction: A8WHJ2; IntAct: EBI-3406532,EBI-3407821; Score: 0.35
DE  Interaction: Q86NV3; IntAct: EBI-3406532,EBI-124919; Score: 0.35
DE  Interaction: A1ZAU8-2; IntAct: EBI-3406532,EBI-3407157; Score: 0.46
DE  Interaction: Q9W106; IntAct: EBI-3406532,EBI-187617; Score: 0.35
DE  Interaction: Q9VJ03; IntAct: EBI-3406532,EBI-185684; Score: 0.35
DE  Interaction: Q9VJJ8; IntAct: EBI-3406532,EBI-500699; Score: 0.35
DE  Interaction: Q9W4F6; IntAct: EBI-3406532,EBI-149664; Score: 0.35
DE  Interaction: Q9VVK6; IntAct: EBI-3406532,EBI-3407810; Score: 0.35
DE  Interaction: Q9W4E4; IntAct: EBI-3406532,EBI-121808; Score: 0.46
DE  Interaction: O15943-3; IntAct: EBI-3406532,EBI-496920; Score: 0.35
DE  Interaction: Q9VXL9; IntAct: EBI-3406532,EBI-3403531; Score: 0.35
DE  Interaction: Q9VK06; IntAct: EBI-3406532,EBI-123819; Score: 0.35
DE  Interaction: Q9VC89; IntAct: EBI-3406532,EBI-111843; Score: 0.35
DE  Interaction: Q59DV6; IntAct: EBI-3406532,EBI-3407933; Score: 0.35
DE  Interaction: Q8IPG1; IntAct: EBI-3406532,EBI-3408063; Score: 0.35
DE  Interaction: Q9W1L7; IntAct: EBI-3406532,EBI-95471; Score: 0.35
DE  Interaction: Q9VM93; IntAct: EBI-3406532,EBI-113116; Score: 0.35
DE  Interaction: P54398; IntAct: EBI-3406532,EBI-188496; Score: 0.35
DE  Interaction: P18106-4; IntAct: EBI-3406532,EBI-3406778; Score: 0.46
DE  Interaction: Q9VF33; IntAct: EBI-3406532,EBI-3406335; Score: 0.35
DE  Interaction: A1Z7D2; IntAct: EBI-3406532,EBI-3406366; Score: 0.35
DE  Interaction: A1Z8J5; IntAct: EBI-3406532,EBI-109496; Score: 0.46
DE  Interaction: Q9VXW2; IntAct: EBI-3406532,EBI-2508890; Score: 0.46
DE  Interaction: Q9V4B2; IntAct: EBI-3406532,EBI-158430; Score: 0.35
DE  Interaction: Q9VTU0; IntAct: EBI-3406532,EBI-149723; Score: 0.35
DE  Interaction: Q9VPA1; IntAct: EBI-3406532,EBI-90086; Score: 0.35
DE  Interaction: P00967; IntAct: EBI-3406532,EBI-89487; Score: 0.35
DE  Interaction: Q7KVY9; IntAct: EBI-3406532,EBI-3407635; Score: 0.35
DE  Interaction: Q9W1C5; IntAct: EBI-3406532,EBI-175291; Score: 0.35
DE  Interaction: Q9W3J6; IntAct: EBI-3406532,EBI-137021; Score: 0.35
DE  Interaction: Q9VXV3; IntAct: EBI-3406532,EBI-99850; Score: 0.35
DE  Interaction: Q9VC66; IntAct: EBI-3406532,EBI-166765; Score: 0.35
DE  Interaction: Q9NB04; IntAct: EBI-3406532,EBI-442573; Score: 0.35
DE  Interaction: Q9V430; IntAct: EBI-3406532,EBI-97579; Score: 0.35
DE  Interaction: Q9I7L9; IntAct: EBI-3406532,EBI-195985; Score: 0.35
DE  Interaction: Q9VHD0; IntAct: EBI-3406532,EBI-126669; Score: 0.35
DE  Interaction: Q9VU43; IntAct: EBI-3406532,EBI-109972; Score: 0.35
DE  Interaction: Q9VEZ5; IntAct: EBI-3406532,EBI-148871; Score: 0.35
DE  Interaction: Q9VPL3; IntAct: EBI-3406532,EBI-3406912; Score: 0.35
DE  Interaction: A1ZAL4; IntAct: EBI-3406532,EBI-187807; Score: 0.35
DE  Interaction: Q9VSZ4; IntAct: EBI-3406532,EBI-3407265; Score: 0.35
DE  Interaction: Q9VGN4; IntAct: EBI-3406532,EBI-191064; Score: 0.35
DE  Interaction: Q8WTI8; IntAct: EBI-3406532,EBI-123112; Score: 0.35
DE  Interaction: Q9VF03; IntAct: EBI-3406532,EBI-132623; Score: 0.46
DE  Interaction: Q9VZM9; IntAct: EBI-3406532,EBI-158602; Score: 0.35
DE  Interaction: P18167; IntAct: EBI-3406532,EBI-3407042; Score: 0.35
DE  Interaction: Q6AWJ9; IntAct: EBI-3406532,EBI-870398; Score: 0.35
DE  Interaction: A1ZAN6; IntAct: EBI-3406532,EBI-2508872; Score: 0.35
DE  Interaction: Q9W2D5; IntAct: EBI-3406532,EBI-3406680; Score: 0.35
DE  Interaction: Q9VK89; IntAct: EBI-3406532,EBI-3407465; Score: 0.35
DE  Interaction: Q9VAQ1; IntAct: EBI-3406532,EBI-151474; Score: 0.35
DE  Interaction: Q9VZX7; IntAct: EBI-3406532,EBI-2508459; Score: 0.46
DE  Interaction: Q9W457; IntAct: EBI-3406532,EBI-157731; Score: 0.35
DE  Interaction: Q9VT40; IntAct: EBI-3406532,EBI-190718; Score: 0.35
DE  Interaction: Q9VVK7; IntAct: EBI-3406532,EBI-98134; Score: 0.35
DE  Interaction: Q9VXG1; IntAct: EBI-3406532,EBI-151096; Score: 0.35
DE  Interaction: Q59DP9; IntAct: EBI-3406532,EBI-3407240; Score: 0.35
DE  Interaction: Q8IR50; IntAct: EBI-3406532,EBI-120243; Score: 0.35
DE  Interaction: A1Z9J1; IntAct: EBI-3406532,EBI-2890352; Score: 0.35
DE  Interaction: Q9VDQ7; IntAct: EBI-3406532,EBI-188148; Score: 0.35
DE  Interaction: Q9W420; IntAct: EBI-3406532,EBI-3406848; Score: 0.35
DE  Interaction: Q9VL71; IntAct: EBI-3406532,EBI-186545; Score: 0.35
DE  Interaction: Q9VH96; IntAct: EBI-3406532,EBI-3406967; Score: 0.35
DE  Interaction: Q9V3J1-2; IntAct: EBI-3406532,EBI-3407617; Score: 0.35
DE  Interaction: Q9VH71; IntAct: EBI-3406532,EBI-3406960; Score: 0.35
DE  Interaction: Q9VXE6; IntAct: EBI-3406532,EBI-178209; Score: 0.35
DE  Interaction: Q9VW37; IntAct: EBI-3406532,EBI-172301; Score: 0.35
DE  Interaction: Q9W3R8; IntAct: EBI-3406532,EBI-118274; Score: 0.35
DE  Interaction: Q9VSM7; IntAct: EBI-3406532,EBI-3407217; Score: 0.35
DE  Interaction: O61602; IntAct: EBI-3406532,EBI-3407034; Score: 0.35
DE  Interaction: Q9VTV9; IntAct: EBI-3406532,EBI-179443; Score: 0.35
DE  Interaction: Q9VCH5; IntAct: EBI-3406532,EBI-139789; Score: 0.35
DE  Interaction: Q9VYY4; IntAct: EBI-3406532,EBI-3406267; Score: 0.35
DE  Interaction: Q9VZ00; IntAct: EBI-3406532,EBI-129187; Score: 0.46
DE  Interaction: Q9VE08; IntAct: EBI-3406532,EBI-3406522; Score: 0.35
DE  Interaction: Q7JUN3; IntAct: EBI-3406532,EBI-196569; Score: 0.35
DE  Interaction: Q9W2Y5; IntAct: EBI-3406532,EBI-90956; Score: 0.35
DE  Interaction: Q59DP4; IntAct: EBI-3406532,EBI-3403924; Score: 0.35
DE  Interaction: Q9VAQ5; IntAct: EBI-3406532,EBI-2108336; Score: 0.35
DE  Interaction: Q9VU84; IntAct: EBI-3406532,EBI-147955; Score: 0.35
DE  Interaction: Q9VQS0; IntAct: EBI-3406532,EBI-117667; Score: 0.35
DE  Interaction: Q9VY54; IntAct: EBI-3406532,EBI-173542; Score: 0.46
DE  Interaction: Q9W425; IntAct: EBI-3406532,EBI-194118; Score: 0.35
DE  Interaction: P25455-1; IntAct: EBI-3406532,EBI-3404050; Score: 0.35
DE  Interaction: Q0E996; IntAct: EBI-3406532,EBI-194406; Score: 0.46
DE  Interaction: Q95U58; IntAct: EBI-3406532,EBI-3408178; Score: 0.35
DE  Interaction: Q9W3R9; IntAct: EBI-3406532,EBI-144663; Score: 0.35
DE  Interaction: O46072; IntAct: EBI-3406532,EBI-3406876; Score: 0.35
DE  Interaction: Q8INC1; IntAct: EBI-3406532,EBI-3407456; Score: 0.35
DE  Interaction: Q8SX24; IntAct: EBI-3406532,EBI-3406579; Score: 0.35
DE  Interaction: A1ZA87; IntAct: EBI-3406532,EBI-3407022; Score: 0.35
DE  Interaction: P54367; IntAct: EBI-3406532,EBI-129996; Score: 0.35
DE  Interaction: Q9V3Z3; IntAct: EBI-3406532,EBI-107179; Score: 0.35
DE  Interaction: A1ZAV3; IntAct: EBI-3406532,EBI-2508761; Score: 0.35
DE  Interaction: Q9VIF5; IntAct: EBI-3406532,EBI-151790; Score: 0.46
DE  Interaction: P54351; IntAct: EBI-3406532,EBI-189984; Score: 0.35
DE  Interaction: Q24270-3; IntAct: EBI-3406532,EBI-3407722; Score: 0.35
DE  Interaction: Q9VY10; IntAct: EBI-3406532,EBI-3407347; Score: 0.35
DE  Interaction: Q9W3X0; IntAct: EBI-3406532,EBI-102177; Score: 0.35
DE  Interaction: Q9W1A9; IntAct: EBI-3406532,EBI-194800; Score: 0.35
DE  Interaction: Q9V463; IntAct: EBI-3406532,EBI-118619; Score: 0.35
DE  Interaction: Q9VQV6; IntAct: EBI-3406532,EBI-3406837; Score: 0.35
DE  Interaction: Q9VMN5; IntAct: EBI-3406532,EBI-139765; Score: 0.35
DE  Interaction: Q9VMG8; IntAct: EBI-3406532,EBI-156218; Score: 0.46
DE  Interaction: Q9VZE8; IntAct: EBI-3406532,EBI-167134; Score: 0.35
DE  Interaction: Q86BH1; IntAct: EBI-3406532,EBI-3407733; Score: 0.46
DE  Interaction: Q7KV70; IntAct: EBI-3406532,EBI-3407195; Score: 0.35
DE  Interaction: Q8T3J1; IntAct: EBI-3406532,EBI-190355; Score: 0.35
DE  Interaction: Q9VI07; IntAct: EBI-3406532,EBI-3407376; Score: 0.35
DE  Interaction: Q7JXU4; IntAct: EBI-3406532,EBI-3407354; Score: 0.35
DE  Interaction: Q24595-1; IntAct: EBI-3406532,EBI-3406735; Score: 0.46
DE  Interaction: Q95SK9; IntAct: EBI-3406532,EBI-3407814; Score: 0.35
DE  Interaction: Q9VCX2; IntAct: EBI-3406532,EBI-497621; Score: 0.35
DE  Interaction: Q9VE80; IntAct: EBI-3406532,EBI-235134; Score: 0.35
DE  Interaction: Q04691-1; IntAct: EBI-3406532,EBI-3406372; Score: 0.35
DE  Interaction: Q9VV79; IntAct: EBI-3406532,EBI-111118; Score: 0.35
DE  Interaction: Q9VCB7; IntAct: EBI-3406532,EBI-3407221; Score: 0.35
DE  Interaction: Q9VPC7; IntAct: EBI-3406532,EBI-3406922; Score: 0.35
DE  Interaction: Q9XZ32; IntAct: EBI-3406532,EBI-94453; Score: 0.35
DE  Interaction: A1ZBN5; IntAct: EBI-3406532,EBI-3406940; Score: 0.35
DE  Interaction: Q9VCJ3; IntAct: EBI-3406532,EBI-179284; Score: 0.35
DE  Interaction: A1Z8Q9; IntAct: EBI-3406532,EBI-3406629; Score: 0.35
DE  Interaction: Q9W0J2; IntAct: EBI-3406532,EBI-160429; Score: 0.35
DE  Interaction: Q5U154; IntAct: EBI-3406532,EBI-164412; Score: 0.35
DE  Interaction: A1ZAW3; IntAct: EBI-3406532,EBI-145169; Score: 0.35
DE  Interaction: A1Z773; IntAct: EBI-3406532,EBI-3407930; Score: 0.35
DE  Interaction: Q9VLW7; IntAct: EBI-3406532,EBI-114696; Score: 0.35
DE  Interaction: Q9W378; IntAct: EBI-3406532,EBI-187428; Score: 0.35
DE  Interaction: Q8IPJ5; IntAct: EBI-3406532,EBI-3407831; Score: 0.35
DE  Interaction: Q9VWV5; IntAct: EBI-3406532,EBI-3403836; Score: 0.46
DE  Interaction: Q9V853; IntAct: EBI-3406532,EBI-133520; Score: 0.35
DE  Interaction: Q9W289; IntAct: EBI-3406532,EBI-3406488; Score: 0.35
DE  Interaction: Q9W2W2; IntAct: EBI-3406532,EBI-182976; Score: 0.35
DE  Interaction: Q9VRJ1; IntAct: EBI-3406532,EBI-3407834; Score: 0.46
DE  Interaction: Q9W0R3; IntAct: EBI-3406532,EBI-117182; Score: 0.46
DE  Interaction: Q9VX18; IntAct: EBI-3406532,EBI-96241; Score: 0.35
DE  Interaction: A1ZAC7; IntAct: EBI-3406532,EBI-142941; Score: 0.35
DE  Interaction: Q26307; IntAct: EBI-3406532,EBI-145644; Score: 0.35
DE  Interaction: Q9VU88; IntAct: EBI-3406532,EBI-106257; Score: 0.35
DE  Interaction: Q0E9G3; IntAct: EBI-3406532,EBI-150380; Score: 0.35
DE  Interaction: Q9W198; IntAct: EBI-3406532,EBI-169270; Score: 0.35
DE  Interaction: Q9VX80; IntAct: EBI-3406532,EBI-128251; Score: 0.46
DE  Interaction: Q7KN85; IntAct: EBI-3406532,EBI-3407796; Score: 0.35
DE  Interaction: Q9W433; IntAct: EBI-3406532,EBI-155123; Score: 0.35
DE  Interaction: Q9VPH9; IntAct: EBI-3406532,EBI-3407421; Score: 0.35
DE  Interaction: Q9VU91; IntAct: EBI-3406532,EBI-181929; Score: 0.35
DE  Interaction: Q6WV17-1; IntAct: EBI-3406532,EBI-3406622; Score: 0.35
DE  Interaction: Q03042; IntAct: EBI-3406532,EBI-3408169; Score: 0.35
DE  Interaction: Q86BY9; IntAct: EBI-3406532,EBI-422757; Score: 0.35
DE  Interaction: P55824-1; IntAct: EBI-3406532,EBI-3408117; Score: 0.46
DE  Interaction: Q9TVP3-1; IntAct: EBI-3406532,EBI-3407737; Score: 0.35
DE  Interaction: Q9VQR0; IntAct: EBI-3406532,EBI-3406220; Score: 0.35
DE  Interaction: Q9VYK0; IntAct: EBI-3406532,EBI-2508136; Score: 0.35
DE  Interaction: Q9I7T2; IntAct: EBI-3406532,EBI-3407886; Score: 0.35
DE  Interaction: Q9VWN1; IntAct: EBI-3406532,EBI-3407528; Score: 0.35
DE  Interaction: Q1EC46; IntAct: EBI-3406532,EBI-3407601; Score: 0.35
DE  Interaction: Q9VX91; IntAct: EBI-3406532,EBI-143532; Score: 0.35
DE  Interaction: Q86B47-2; IntAct: EBI-3406532,EBI-3406856; Score: 0.35
DE  Interaction: Q9VIU8; IntAct: EBI-3406532,EBI-146037; Score: 0.35
DE  Interaction: Q9VE86; IntAct: EBI-3406532,EBI-166260; Score: 0.35
DE  Interaction: Q9VGH5; IntAct: EBI-3406532,EBI-132496; Score: 0.35
DE  Interaction: Q9W1J9; IntAct: EBI-3406532,EBI-161024; Score: 0.35
DE  Interaction: Q9VX63; IntAct: EBI-3406532,EBI-99157; Score: 0.35
DE  Interaction: P16620-1; IntAct: EBI-3406532,EBI-3406572; Score: 0.35
DE  Interaction: O76462; IntAct: EBI-3406532,EBI-135829; Score: 0.35
DE  Interaction: Q9VSS2; IntAct: EBI-3406532,EBI-189424; Score: 0.35
DE  Interaction: Q9VFJ2; IntAct: EBI-3406532,EBI-86141; Score: 0.35
DE  Interaction: Q8SWU7-1; IntAct: EBI-3406532,EBI-3406997; Score: 0.35
DE  Interaction: Q7KUG5; IntAct: EBI-3406532,EBI-3404257; Score: 0.35
DE  Interaction: P22769; IntAct: EBI-3406532,EBI-93148; Score: 0.35
DE  Interaction: Q9VEN2; IntAct: EBI-3406532,EBI-85718; Score: 0.35
DE  Interaction: Q9VGG5; IntAct: EBI-3406532,EBI-2110530; Score: 0.35
DE  Interaction: Q9V3I5; IntAct: EBI-3406532,EBI-84939; Score: 0.35
DE  Interaction: Q9VJB6; IntAct: EBI-3406532,EBI-2508884; Score: 0.46
DE  Interaction: Q9VQP5; IntAct: EBI-3406532,EBI-3404042; Score: 0.35
DE  Interaction: P13607-1; IntAct: EBI-3406532,EBI-213208; Score: 0.35
DE  Interaction: Q8MSX1-3; IntAct: EBI-3406532,EBI-3406819; Score: 0.35
DE  Interaction: O96433-1; IntAct: EBI-3406532,EBI-3406553; Score: 0.35
DE  Interaction: Q9VZX9; IntAct: EBI-3406532,EBI-88701; Score: 0.35
DE  Interaction: Q9VCE0; IntAct: EBI-3406532,EBI-103248; Score: 0.35
DE  Interaction: Q23976; IntAct: EBI-3406532,EBI-137596; Score: 0.35
DE  Interaction: Q9VIU5; IntAct: EBI-3406532,EBI-98558; Score: 0.35
DE  Interaction: Q9VM08-5; IntAct: EBI-3406532,EBI-3408032; Score: 0.35
DE  Interaction: Q23983; IntAct: EBI-3406532,EBI-195132; Score: 0.35
DE  Interaction: Q7JVY0; IntAct: EBI-3406532,EBI-102727; Score: 0.35
DE  Interaction: Q9XZ25; IntAct: EBI-3406532,EBI-3407214; Score: 0.35
DE  Interaction: Q8INM3-1; IntAct: EBI-3406532,EBI-3407078; Score: 0.35
DE  Interaction: Q9NII1-3; IntAct: EBI-3406532,EBI-3403843; Score: 0.35
DE  Interaction: P20028; IntAct: EBI-3406532,EBI-3403932; Score: 0.46
DE  Interaction: Q9VMP4; IntAct: EBI-3406532,EBI-3407941; Score: 0.35
DE  Interaction: A8JUV0-3; IntAct: EBI-3406532,EBI-3408159; Score: 0.35
DE  Interaction: Q9W018; IntAct: EBI-3406532,EBI-3406658; Score: 0.35
DE  Interaction: Q8SX83-1; IntAct: EBI-3406532,EBI-3407844; Score: 0.46
DE  Interaction: Q9V3K3; IntAct: EBI-3406532,EBI-192924; Score: 0.35
DE  Interaction: Q9VLB3; IntAct: EBI-3406532,EBI-96512; Score: 0.46
DE  Interaction: Q8MT36; IntAct: EBI-3406532,EBI-148375; Score: 0.35
DE  Interaction: P05990; IntAct: EBI-3406532,EBI-466976; Score: 0.46
DE  Interaction: P51406; IntAct: EBI-3406532,EBI-117198; Score: 0.35
DE  Interaction: Q9V9V7; IntAct: EBI-3406532,EBI-168994; Score: 0.35
DE  Interaction: Q9VE00; IntAct: EBI-3406532,EBI-152246; Score: 0.35
DE  Interaction: Q9VGY2; IntAct: EBI-3406532,EBI-3408102; Score: 0.35
DE  Interaction: Q9U1H0-2; IntAct: EBI-3406532,EBI-3407127; Score: 0.35
DE  Interaction: A1Z6S0; IntAct: EBI-3406532,EBI-3407629; Score: 0.46
DE  Interaction: Q9W490; IntAct: EBI-3406532,EBI-3403464; Score: 0.35
DE  Interaction: Q9VRB3; IntAct: EBI-3406532,EBI-186042; Score: 0.35
DE  Interaction: Q9VUZ2; IntAct: EBI-3406532,EBI-3407590; Score: 0.35
DE  Interaction: Q24573-2; IntAct: EBI-3406532,EBI-3406294; Score: 0.35
DE  Interaction: Q9VQE5; IntAct: EBI-3406532,EBI-86891; Score: 0.35
DE  Interaction: Q9VYT8; IntAct: EBI-3406532,EBI-3403554; Score: 0.35
DE  Interaction: A1Z8W1; IntAct: EBI-3406532,EBI-3406712; Score: 0.46
DE  Interaction: Q9V460-1; IntAct: EBI-3406532,EBI-3407980; Score: 0.46
DE  Interaction: Q24298; IntAct: EBI-3406532,EBI-112930; Score: 0.35
DE  Interaction: Q59E61; IntAct: EBI-3406532,EBI-3407279; Score: 0.46
DE  Interaction: Q0E9C6; IntAct: EBI-3406532,EBI-3406101; Score: 0.46
DE  Interaction: Q7KVP6; IntAct: EBI-3406532,EBI-3403350; Score: 0.35
DE  Interaction: Q9W2P1; IntAct: EBI-3406532,EBI-3408001; Score: 0.35
DE  Interaction: Q9VCD1; IntAct: EBI-3406532,EBI-3407549; Score: 0.35
DE  Interaction: Q9VB25; IntAct: EBI-3406532,EBI-499959; Score: 0.35
DE  Interaction: Q9VTZ1; IntAct: EBI-3406532,EBI-139086; Score: 0.46
DE  Interaction: P91660; IntAct: EBI-3406532,EBI-123933; Score: 0.35
DE  Interaction: Q8IGR0; IntAct: EBI-3406532,EBI-3405191; Score: 0.35
DE  Interaction: Q7JUX9; IntAct: EBI-3406532,EBI-192122; Score: 0.35
DE  Interaction: Q9V3D6; IntAct: EBI-3406532,EBI-91480; Score: 0.35
DE  Interaction: Q9VC54; IntAct: EBI-3406532,EBI-146045; Score: 0.35
DE  Interaction: Q59DW9; IntAct: EBI-3406532,EBI-3406757; Score: 0.46
DE  Interaction: Q9VNT3; IntAct: EBI-3406532,EBI-3408040; Score: 0.35
DE  Interaction: Q7K3W4; IntAct: EBI-3406532,EBI-112670; Score: 0.35
DE  Interaction: Q7KSF4; IntAct: EBI-3406532,EBI-3406697; Score: 0.35
DE  Interaction: Q9V9P7; IntAct: EBI-3406532,EBI-2890598; Score: 0.35
DE  Interaction: Q9VGL0; IntAct: EBI-3406532,EBI-148838; Score: 0.35
DE  Interaction: Q9VRJ0; IntAct: EBI-3406532,EBI-3406666; Score: 0.35
DE  Interaction: Q8IQQ7; IntAct: EBI-3406532,EBI-176269; Score: 0.35
DE  Interaction: Q7KV35; IntAct: EBI-3406532,EBI-3403520; Score: 0.35
DE  Interaction: Q9VTK2; IntAct: EBI-3406532,EBI-3407704; Score: 0.35
DE  Interaction: Q9VBE1; IntAct: EBI-3406532,EBI-3405786; Score: 0.35
DE  Interaction: Q9VUX7; IntAct: EBI-3406532,EBI-3403487; Score: 0.35
DE  Interaction: Q9V9E3; IntAct: EBI-3406532,EBI-195343; Score: 0.35
DE  Interaction: Q9NBD7; IntAct: EBI-3406532,EBI-171079; Score: 0.35
DE  Interaction: P46863; IntAct: EBI-3406532,EBI-95528; Score: 0.35
DE  Interaction: Q9VDU0; IntAct: EBI-3406532,EBI-3407272; Score: 0.35
DE  Interaction: Q24246-2; IntAct: EBI-3406532,EBI-213425; Score: 0.35
DE  Interaction: Q8SWR8-1; IntAct: EBI-3406532,EBI-3407693; Score: 0.35
DE  Interaction: Q9I7J1; IntAct: EBI-3406532,EBI-3408016; Score: 0.35
DE  Interaction: Q9VNP5; IntAct: EBI-3406532,EBI-132890; Score: 0.35
DE  Interaction: Q9VR89; IntAct: EBI-3406532,EBI-185486; Score: 0.35
DE  Interaction: Q9W0B8; IntAct: EBI-3406532,EBI-171121; Score: 0.35
DE  Interaction: Q9VQZ3; IntAct: EBI-3406532,EBI-127938; Score: 0.35
DE  Interaction: Q9VXG0; IntAct: EBI-3406532,EBI-3428380; Score: 0.35
DE  Interaction: Q9VHG1; IntAct: EBI-3406532,EBI-187940; Score: 0.35
DE  Interaction: Q24180; IntAct: EBI-3406532,EBI-149832; Score: 0.35
DE  Interaction: P46150-4; IntAct: EBI-3406532,EBI-3408125; Score: 0.35
DE  Interaction: A4UZL2; IntAct: EBI-3406532,EBI-3407252; Score: 0.35
DE  Interaction: Q9VJE5-3; IntAct: EBI-3406532,EBI-3407364; Score: 0.35
DE  Interaction: Q9V3C5; IntAct: EBI-3406532,EBI-153404; Score: 0.35
DE  Interaction: Q7KNF1; IntAct: EBI-3406532,EBI-159398; Score: 0.35
DE  Interaction: Q9VJ07; IntAct: EBI-3406532,EBI-3407092; Score: 0.35
DE  Interaction: Q9VI63; IntAct: EBI-3406532,EBI-124051; Score: 0.35
DE  Interaction: A1Z6E0; IntAct: EBI-3406532,EBI-75338; Score: 0.35
DE  Interaction: Q9VU30; IntAct: EBI-3406532,EBI-3407237; Score: 0.35
DE  Interaction: Q8T3L6; IntAct: EBI-3406532,EBI-3407492; Score: 0.35
DE  Interaction: Q9VNA0; IntAct: EBI-3406532,EBI-3407906; Score: 0.35
DE  Interaction: Q9VEK8; IntAct: EBI-3406532,EBI-86436; Score: 0.35
DE  Interaction: Q9VDK5; IntAct: EBI-3406532,EBI-3406250; Score: 0.35
DE  Interaction: Q8MRL0; IntAct: EBI-3406532,EBI-149556; Score: 0.35
DE  Interaction: Q9XTP7; IntAct: EBI-3406532,EBI-176893; Score: 0.35
DE  Interaction: Q9VJS8; IntAct: EBI-3406532,EBI-498806; Score: 0.35
DE  Interaction: B9A0M4; IntAct: EBI-3406532,EBI-3410226; Score: 0.35
DE  Interaction: Q9VM04; IntAct: EBI-3406532,EBI-90210; Score: 0.35
DE  Interaction: Q9VXU6; IntAct: EBI-3406532,EBI-3406569; Score: 0.35
DE  Interaction: P40657; IntAct: EBI-3406532,EBI-112718; Score: 0.35
DE  Interaction: Q8IRG5; IntAct: EBI-3406532,EBI-3407054; Score: 0.35
DE  Interaction: Q9VE34-1; IntAct: EBI-3406532,EBI-3407358; Score: 0.35
DE  Interaction: Q9VMC6; IntAct: EBI-3406532,EBI-91117; Score: 0.35
DE  Interaction: Q9VY98; IntAct: EBI-3406532,EBI-181816; Score: 0.35
DE  Interaction: Q9VBE6; IntAct: EBI-3406532,EBI-184661; Score: 0.35
DE  Interaction: Q9VIE8; IntAct: EBI-3406532,EBI-413174; Score: 0.35
DE  Interaction: Q9VCV8; IntAct: EBI-3406532,EBI-3406834; Score: 0.35
DE  Interaction: Q9VCE7; IntAct: EBI-3406532,EBI-148224; Score: 0.35
DE  Interaction: Q9VEH0; IntAct: EBI-3406532,EBI-109689; Score: 0.35
DE  Interaction: Q9VVU5; IntAct: EBI-3406532,EBI-3406597; Score: 0.35
DE  Interaction: P54358; IntAct: EBI-3406532,EBI-131791; Score: 0.35
DE  Interaction: Q27297-1; IntAct: EBI-3406532,EBI-3406287; Score: 0.35
DE  Interaction: Q9V6Y3; IntAct: EBI-3406532,EBI-3406399; Score: 0.35
DE  Interaction: P30432-2; IntAct: EBI-3406532,EBI-3404319; Score: 0.35
DE  Interaction: Q9VJZ6; IntAct: EBI-3406532,EBI-191805; Score: 0.35
DE  Interaction: Q9VYR9; IntAct: EBI-3406532,EBI-3406865; Score: 0.35
DE  Interaction: Q9W2N6; IntAct: EBI-3406532,EBI-175605; Score: 0.35
DE  Interaction: Q00168-4; IntAct: EBI-3406532,EBI-3406380; Score: 0.35
DE  Interaction: Q0E919; IntAct: EBI-3406532,EBI-132309; Score: 0.35
DE  Interaction: Q8INH6; IntAct: EBI-3406532,EBI-3406492; Score: 0.35
DE  Interaction: P54397; IntAct: EBI-3406532,EBI-167608; Score: 0.35
DE  Interaction: Q9V8Y7; IntAct: EBI-3406532,EBI-89272; Score: 0.35
DE  Interaction: P07666; IntAct: EBI-3406532,EBI-98421; Score: 0.35
DE  Interaction: Q9VNG2; IntAct: EBI-3406532,EBI-3408012; Score: 0.35
DE  Interaction: Q8SZ63; IntAct: EBI-3406532,EBI-161229; Score: 0.35
DE  Interaction: P17671-1; IntAct: EBI-3406532,EBI-3407522; Score: 0.35
DE  Interaction: Q9W117; IntAct: EBI-3406532,EBI-3406476; Score: 0.35
DE  Interaction: Q8IH56; IntAct: EBI-3406532,EBI-219184; Score: 0.35
DE  Interaction: Q7KV88; IntAct: EBI-3406532,EBI-868359; Score: 0.35
DE  Interaction: P04052; IntAct: EBI-3406532,EBI-173525; Score: 0.35
DE  Interaction: Q9VQB6; IntAct: EBI-3406532,EBI-3407418; Score: 0.35
DE  Interaction: A1Z945; IntAct: EBI-3406532,EBI-3407474; Score: 0.35
DE  Interaction: O76904; IntAct: EBI-3406532,EBI-133828; Score: 0.35
DE  Interaction: Q0KI87; IntAct: EBI-3406532,EBI-93158; Score: 0.35
DE  Interaction: Q9VKJ1; IntAct: EBI-3406532,EBI-168534; Score: 0.35
DE  Interaction: P10676-2; IntAct: EBI-3406532,EBI-3403371; Score: 0.35
DE  Interaction: Q9W201; IntAct: EBI-3406532,EBI-97867; Score: 0.35
DE  Interaction: Q9I7S4; IntAct: EBI-3406532,EBI-129467; Score: 0.35
DE  Interaction: Q8INC0; IntAct: EBI-3406532,EBI-3402350; Score: 0.35
DE  Interaction: Q9VFK2; IntAct: EBI-3406532,EBI-121566; Score: 0.35
DE  Interaction: Q24478; IntAct: EBI-3406532,EBI-868840; Score: 0.35
DE  Interaction: Q9VKL9; IntAct: EBI-3406532,EBI-3406885; Score: 0.35
DE  Interaction: Q9W0D9; IntAct: EBI-3406532,EBI-3408028; Score: 0.35
DE  Interaction: Q494G8; IntAct: EBI-3406532,EBI-3407038; Score: 0.35
DE  Interaction: Q27268; IntAct: EBI-3406532,EBI-176504; Score: 0.35
DE  Interaction: Q7KMH9; IntAct: EBI-3406532,EBI-75206; Score: 0.35
DE  Interaction: Q9VWE7; IntAct: EBI-3406532,EBI-125059; Score: 0.35
DE  Interaction: Q9VXK9; IntAct: EBI-3406532,EBI-175990; Score: 0.35
DE  Interaction: P13368; IntAct: EBI-3406532,EBI-522166; Score: 0.35
DE  Interaction: Q9VP47; IntAct: EBI-3406532,EBI-138303; Score: 0.35
DE  Interaction: Q9VAD3; IntAct: EBI-3406532,EBI-106333; Score: 0.35
DE  Interaction: Q9VNH6; IntAct: EBI-3406532,EBI-86247; Score: 0.35
DE  Interaction: Q9V6B9; IntAct: EBI-3406532,EBI-179307; Score: 0.35
DE  Interaction: Q9W4W4; IntAct: EBI-3406532,EBI-189577; Score: 0.35
DE  Interaction: Q9VM15; IntAct: EBI-3406532,EBI-118580; Score: 0.35
DE  Interaction: Q9VMN9; IntAct: EBI-3406532,EBI-3407175; Score: 0.35
DE  Interaction: Q9VIQ9; IntAct: EBI-3406532,EBI-98817; Score: 0.35
DE  Interaction: Q9XTN4; IntAct: EBI-3406532,EBI-159245; Score: 0.35
DE  Interaction: A1Z7A6; IntAct: EBI-3406532,EBI-2507868; Score: 0.35
DE  Interaction: P41073; IntAct: EBI-3406532,EBI-522331; Score: 0.35
DE  Interaction: Q9VEN1; IntAct: EBI-3406532,EBI-133626; Score: 0.35
DE  Interaction: Q8IPV2; IntAct: EBI-3406532,EBI-3406762; Score: 0.35
DE  Interaction: Q9VC81; IntAct: EBI-3406532,EBI-101680; Score: 0.35
DE  Interaction: Q9VVL7; IntAct: EBI-3406532,EBI-110434; Score: 0.35
DE  Interaction: Q8I0G5; IntAct: EBI-3406532,EBI-146110; Score: 0.35
DE  Interaction: Q9VA60; IntAct: EBI-3406532,EBI-3407483; Score: 0.35
DE  Interaction: Q9VZ97; IntAct: EBI-3406532,EBI-134041; Score: 0.35
DE  Interaction: Q7KU82; IntAct: EBI-3406532,EBI-3406525; Score: 0.35
DE  Interaction: Q9W058; IntAct: EBI-3406532,EBI-184518; Score: 0.35
DE  Interaction: P81923; IntAct: EBI-3406532,EBI-134371; Score: 0.35
DE  Interaction: Q9VA02; IntAct: EBI-3406532,EBI-166909; Score: 0.35
DE  Interaction: Q9V466; IntAct: EBI-3406532,EBI-89961; Score: 0.35
DE  Interaction: Q9VC08; IntAct: EBI-3406532,EBI-134140; Score: 0.35
DE  Interaction: Q7K4H4; IntAct: EBI-3406532,EBI-119369; Score: 0.35
DE  Interaction: Q9W2U4; IntAct: EBI-3406532,EBI-3406931; Score: 0.35
DE  Interaction: Q8MLV8; IntAct: EBI-3406532,EBI-2508405; Score: 0.35
DE  Interaction: Q02748; IntAct: EBI-3406532,EBI-85570; Score: 0.35
DE  Interaction: Q9VJY4; IntAct: EBI-3406532,EBI-3407572; Score: 0.35
DE  Interaction: Q9V9W7; IntAct: EBI-3406532,EBI-3407063; Score: 0.35
DE  Interaction: Q9VD37; IntAct: EBI-3406532,EBI-2110665; Score: 0.35
DE  Interaction: Q9VK52; IntAct: EBI-3406532,EBI-3406592; Score: 0.35
DE  Interaction: P27864; IntAct: EBI-3406532,EBI-3406944; Score: 0.35
DE  Interaction: Q9VA30; IntAct: EBI-3406532,EBI-92362; Score: 0.35
DE  Interaction: Q86B55; IntAct: EBI-3406532,EBI-136747; Score: 0.35
DE  Interaction: Q9VM77; IntAct: EBI-3406532,EBI-2508306; Score: 0.35
DE  Interaction: Q9VVC9; IntAct: EBI-3406532,EBI-3407840; Score: 0.35
DE  Interaction: Q0KIB3; IntAct: EBI-3406532,EBI-118590; Score: 0.35
DE  Interaction: Q8IQW4; IntAct: EBI-3406532,EBI-2508395; Score: 0.35
DE  Interaction: Q9XZ06; IntAct: EBI-3406532,EBI-179313; Score: 0.35
DE  Interaction: Q9VVW2; IntAct: EBI-3406532,EBI-151410; Score: 0.35
DE  Interaction: Q9VH97; IntAct: EBI-3406532,EBI-3402637; Score: 0.35
DE  Interaction: Q9VJ35; IntAct: EBI-3406532,EBI-176850; Score: 0.35
DE  Interaction: P91645-2; IntAct: EBI-3406532,EBI-3402394; Score: 0.35
DE  Interaction: A1Z6Z8; IntAct: EBI-3406532,EBI-3406344; Score: 0.35
DE  Interaction: Q9VQJ6; IntAct: EBI-3406532,EBI-153683; Score: 0.35
DE  Interaction: Q9VC90; IntAct: EBI-3406532,EBI-141072; Score: 0.35
DE  Interaction: Q9VB58; IntAct: EBI-3406532,EBI-189408; Score: 0.35
DE  Interaction: Q9VRK6; IntAct: EBI-3406532,EBI-3407147; Score: 0.35
DE  Interaction: Q9VB05; IntAct: EBI-3406532,EBI-167636; Score: 0.35
DE  Interaction: Q9W397; IntAct: EBI-3406532,EBI-3407311; Score: 0.35
DE  Interaction: Q9VW85; IntAct: EBI-3406532,EBI-189867; Score: 0.35
DE  Interaction: Q9VCW7; IntAct: EBI-3406532,EBI-175483; Score: 0.35
DE  Interaction: P10040-1; IntAct: EBI-3406532,EBI-3407388; Score: 0.35
DE  Interaction: Q9VQ73; IntAct: EBI-3406532,EBI-147445; Score: 0.35
DE  Interaction: Q9VF10; IntAct: EBI-3406532,EBI-98449; Score: 0.35
DE  Interaction: Q8MLN2; IntAct: EBI-3406532,EBI-107897; Score: 0.35
DE  Interaction: Q961H1; IntAct: EBI-3406532,EBI-167433; Score: 0.35
DE  Interaction: Q9VKV3; IntAct: EBI-3406532,EBI-115843; Score: 0.35
DE  Interaction: Q9VTE2; IntAct: EBI-3406532,EBI-184907; Score: 0.35
DE  Interaction: Q9VJ47; IntAct: EBI-3406532,EBI-3429732; Score: 0.35
DE  Interaction: A1Z6M0; IntAct: EBI-3406532,EBI-126851; Score: 0.35
DE  Interaction: Q9V4P1-2; IntAct: EBI-3406532,EBI-3407895; Score: 0.35
DE  Interaction: Q9VS82; IntAct: EBI-3406532,EBI-83931; Score: 0.35
DE  Interaction: P45437; IntAct: EBI-3406532,EBI-122274; Score: 0.35
DE  Interaction: P26308; IntAct: EBI-3406532,EBI-160827; Score: 0.35
DE  Interaction: Q9VID4; IntAct: EBI-3406532,EBI-84837; Score: 0.35
DE  Interaction: Q9VRY4; IntAct: EBI-3406532,EBI-186345; Score: 0.35
DE  Interaction: Q9VJY3; IntAct: EBI-3406532,EBI-194825; Score: 0.35
DE  Interaction: Q9VSM9; IntAct: EBI-3406532,EBI-151519; Score: 0.35
DE  Interaction: O16810; IntAct: EBI-3406532,EBI-90907; Score: 0.35
DE  Interaction: Q9W283; IntAct: EBI-3406532,EBI-158972; Score: 0.35
DE  Interaction: Q8IMA8; IntAct: EBI-3406532,EBI-3406303; Score: 0.35
DE  Interaction: Q9V3C0; IntAct: EBI-3406532,EBI-134927; Score: 0.35
DE  Interaction: Q8SYS8; IntAct: EBI-3406532,EBI-3407826; Score: 0.35
DE  Interaction: Q9V3L1; IntAct: EBI-3406532,EBI-183090; Score: 0.35
DE  Interaction: Q8IN16; IntAct: EBI-3406532,EBI-2890319; Score: 0.35
DE  Interaction: Q7K7E6; IntAct: EBI-3406532,EBI-3408074; Score: 0.35
DE  Interaction: Q9VGG9; IntAct: EBI-3406532,EBI-153300; Score: 0.35
DE  Interaction: A1Z8J4; IntAct: EBI-3406532,EBI-3406428; Score: 0.35
DE  Interaction: Q9VYN8; IntAct: EBI-3406532,EBI-99551; Score: 0.35
DE  Interaction: Q9VM45; IntAct: EBI-3406532,EBI-168789; Score: 0.35
DE  Interaction: Q9VPB2; IntAct: EBI-3406532,EBI-119347; Score: 0.35
DE  Interaction: Q0E940; IntAct: EBI-3406532,EBI-151120; Score: 0.35
DE  Interaction: Q8T4F7-2; IntAct: EBI-3406532,EBI-3407178; Score: 0.35
DE  Interaction: Q0E993; IntAct: EBI-3406532,EBI-86215; Score: 0.35
DE  Interaction: Q9W3H0; IntAct: EBI-3406532,EBI-166815; Score: 0.35
DE  Interaction: Q9VKZ6; IntAct: EBI-3406532,EBI-3406954; Score: 0.35
DE  Interaction: Q7JX95; IntAct: EBI-3406532,EBI-3406964; Score: 0.35
DE  Interaction: Q29R10; IntAct: EBI-3406532,EBI-84773; Score: 0.35
DE  Interaction: Q8IQA6; IntAct: EBI-3406532,EBI-153156; Score: 0.35
DE  Interaction: Q7K284; IntAct: EBI-3406532,EBI-3406316; Score: 0.35
DE  Interaction: Q967D7-2; IntAct: EBI-3406532,EBI-3408139; Score: 0.35
DE  Interaction: Q9VNL6; IntAct: EBI-3406532,EBI-154139; Score: 0.35
DE  Interaction: Q9VUL5; IntAct: EBI-3406532,EBI-3406671; Score: 0.35
DE  Interaction: Q7K4C7; IntAct: EBI-3406532,EBI-185283; Score: 0.35
DE  Interaction: Q9V414; IntAct: EBI-3406532,EBI-3406410; Score: 0.35
DE  Interaction: O02372; IntAct: EBI-3406532,EBI-182453; Score: 0.35
DE  Interaction: Q9W594; IntAct: EBI-3406532,EBI-128604; Score: 0.35
DE  Interaction: Q8MS38; IntAct: EBI-3406532,EBI-3406800; Score: 0.35
DE  Interaction: Q0KHQ1; IntAct: EBI-3406532,EBI-3407775; Score: 0.35
DE  Interaction: O61735-2; IntAct: EBI-3406532,EBI-440389; Score: 0.35
DE  Interaction: Q9VBW3; IntAct: EBI-3406532,EBI-3404264; Score: 0.35
DE  Interaction: Q7K4B4; IntAct: EBI-3406532,EBI-3407113; Score: 0.35
DE  Interaction: Q9VZP5; IntAct: EBI-3406532,EBI-171044; Score: 0.35
DE  Interaction: A1ZBB4; IntAct: EBI-3406532,EBI-170192; Score: 0.35
DE  Interaction: Q8MV48; IntAct: EBI-3406532,EBI-106149; Score: 0.35
DE  Interaction: Q9W1G7; IntAct: EBI-3406532,EBI-180893; Score: 0.35
DE  Interaction: Q9VHX9; IntAct: EBI-3406532,EBI-149978; Score: 0.35
DE  Interaction: Q9Y1T2; IntAct: EBI-3406532,EBI-114593; Score: 0.35
DE  Interaction: Q9VG29; IntAct: EBI-3406532,EBI-3406349; Score: 0.35
DE  Interaction: Q95TU2; IntAct: EBI-3406532,EBI-139966; Score: 0.35
DE  Interaction: Q9VPP2; IntAct: EBI-3406532,EBI-195064; Score: 0.35
DE  Interaction: Q9W1D3; IntAct: EBI-3406532,EBI-3407150; Score: 0.35
DE  Interaction: A1ZAK1; IntAct: EBI-3406532,EBI-148930; Score: 0.35
DE  Interaction: Q9VA35; IntAct: EBI-3406532,EBI-2890306; Score: 0.35
DE  Interaction: Q24141; IntAct: EBI-3406532,EBI-183986; Score: 0.35
DE  Interaction: Q9V6U9; IntAct: EBI-3406532,EBI-177823; Score: 0.35
DE  Interaction: Q9VEF7; IntAct: EBI-3406532,EBI-3406312; Score: 0.35
DE  Interaction: Q9VUM0; IntAct: EBI-3406532,EBI-169029; Score: 0.35
DE  Interaction: Q9VNC3; IntAct: EBI-3406532,EBI-3406471; Score: 0.35
DE  Interaction: Q7K0F7; IntAct: EBI-3406532,EBI-179939; Score: 0.35
DE  Interaction: Q9VBR7; IntAct: EBI-3406532,EBI-3408097; Score: 0.35
DE  Interaction: Q961D3; IntAct: EBI-3406532,EBI-180605; Score: 0.35
DE  Interaction: Q7KRY7-2; IntAct: EBI-3406532,EBI-3404221; Score: 0.35
DE  Interaction: Q9VF20; IntAct: EBI-3406532,EBI-104505; Score: 0.35
DE  Interaction: Q8SX64; IntAct: EBI-3406532,EBI-3406194; Score: 0.35
DE  Interaction: Q9VP43; IntAct: EBI-3406532,EBI-3406500; Score: 0.35
DE  Interaction: Q9VS54; IntAct: EBI-3406532,EBI-86020; Score: 0.35
DE  Interaction: Q9VXU8; IntAct: EBI-3406532,EBI-188191; Score: 0.35
DE  Interaction: Q9VZK2; IntAct: EBI-3406532,EBI-163256; Score: 0.35
DE  Interaction: A1Z9I9; IntAct: EBI-3406532,EBI-171485; Score: 0.35
DE  Interaction: Q9V9X8; IntAct: EBI-3406532,EBI-137454; Score: 0.35
DE  Interaction: Q8MSQ4; IntAct: EBI-3406532,EBI-870203; Score: 0.35
DE  Interaction: Q0KHR4; IntAct: EBI-3406532,EBI-99044; Score: 0.35
DE  Interaction: Q9W1S1; IntAct: EBI-3406532,EBI-3407772; Score: 0.35
DE  Interaction: Q9U3W7; IntAct: EBI-3406532,EBI-9944840; Score: 0.35
DE  Interaction: Q9VWJ0; IntAct: EBI-3406532,EBI-3406496; Score: 0.35
DE  Interaction: Q9W4X1; IntAct: EBI-3406532,EBI-143242; Score: 0.35
DE  Interaction: Q9W205; IntAct: EBI-3406532,EBI-112086; Score: 0.35
DE  Interaction: Q9VRC8; IntAct: EBI-3406532,EBI-128793; Score: 0.35
DE  Interaction: Q9VVG4; IntAct: EBI-3406532,EBI-168923; Score: 0.35
DE  Interaction: Q9VT32; IntAct: EBI-3406532,EBI-146688; Score: 0.35
DE  Interaction: O61307; IntAct: EBI-3406532,EBI-118556; Score: 0.35
DE  Interaction: Q9VGW1; IntAct: EBI-3406532,EBI-139913; Score: 0.35
DE  Interaction: Q9W3Y7; IntAct: EBI-3406532,EBI-115606; Score: 0.35
DE  Interaction: Q9VU76; IntAct: EBI-3406532,EBI-156334; Score: 0.35
DE  Interaction: Q9W1A0; IntAct: EBI-3406532,EBI-161680; Score: 0.35
DE  Interaction: Q9VG43; IntAct: EBI-3406532,EBI-2890546; Score: 0.35
DE  Interaction: Q9VS63; IntAct: EBI-3406532,EBI-3404012; Score: 0.35
DE  Interaction: Q9W1U2; IntAct: EBI-3406532,EBI-91105; Score: 0.35
DE  Interaction: Q9W472; IntAct: EBI-3406532,EBI-3406460; Score: 0.35
DE  Interaction: Q9VFG4; IntAct: EBI-3406532,EBI-3406481; Score: 0.35
DE  Interaction: Q8SWW4; IntAct: EBI-3406532,EBI-98746; Score: 0.35
DE  Interaction: Q9W1W0; IntAct: EBI-3406532,EBI-116547; Score: 0.35
DE  Interaction: Q9VHB5; IntAct: EBI-3406532,EBI-169701; Score: 0.35
DE  Interaction: Q9W1A4; IntAct: EBI-3406532,EBI-91385; Score: 0.35
DE  Interaction: Q9VM62; IntAct: EBI-3406532,EBI-2507813; Score: 0.35
DE  Interaction: Q9VRF2; IntAct: EBI-3406532,EBI-3406415; Score: 0.35
DE  Interaction: Q9VLN6; IntAct: EBI-3406532,EBI-3407882; Score: 0.35
DE  Interaction: Q9VGI5; IntAct: EBI-3406532,EBI-3406455; Score: 0.35
DE  Interaction: Q9VN58; IntAct: EBI-3406532,EBI-3407755; Score: 0.35
DE  Interaction: Q7JR75; IntAct: EBI-3406532,EBI-3406647; Score: 0.35
DE  Interaction: O46067; IntAct: EBI-3406532,EBI-3406881; Score: 0.35
DE  Interaction: Q9VAE4; IntAct: EBI-3406532,EBI-153347; Score: 0.35
DE  Interaction: P40301; IntAct: EBI-3406532,EBI-98978; Score: 0.35
DE  Interaction: Q9W0Z5; IntAct: EBI-3406532,EBI-94769; Score: 0.35
DE  Interaction: Q8IPL3; IntAct: EBI-3406532,EBI-3407968; Score: 0.35
DE  Interaction: Q9VAU5; IntAct: EBI-3406532,EBI-153806; Score: 0.35
DE  Interaction: Q7KU30; IntAct: EBI-3406532,EBI-130703; Score: 0.35
DE  Interaction: Q9VCH1; IntAct: EBI-3406532,EBI-136479; Score: 0.35
DE  Interaction: Q9VW47; IntAct: EBI-3406532,EBI-139710; Score: 0.35
DE  Interaction: Q9W278; IntAct: EBI-3406532,EBI-3406916; Score: 0.35
DE  Interaction: Q9V9W5; IntAct: EBI-3406532,EBI-108326; Score: 0.35
DE  Interaction: Q9VUC7; IntAct: EBI-3406532,EBI-177260; Score: 0.35
DE  Interaction: Q9VLI2; IntAct: EBI-3406532,EBI-109911; Score: 0.35
DE  Interaction: Q86B79; IntAct: EBI-3406532,EBI-90517; Score: 0.35
DE  Interaction: Q7Z020; IntAct: EBI-3406532,EBI-3433727; Score: 0.35
DE  Interaction: Q8IM95; IntAct: EBI-3406532,EBI-3407269; Score: 0.35
DE  Interaction: Q9VHD1; IntAct: EBI-3406532,EBI-148163; Score: 0.35
DE  Interaction: Q7JV09; IntAct: EBI-3406532,EBI-141560; Score: 0.35
DE  Interaction: Q9U3V5; IntAct: EBI-3406532,EBI-3407583; Score: 0.35
DE  Interaction: Q9VQ61; IntAct: EBI-3406532,EBI-129434; Score: 0.35
DE  Interaction: Q9VFI3; IntAct: EBI-3406532,EBI-152984; Score: 0.35
DE  Interaction: O77410; IntAct: EBI-3406532,EBI-111126; Score: 0.35
DE  Interaction: Q7KQM6-2; IntAct: EBI-3406532,EBI-3406403; Score: 0.35
DE  Interaction: Q9VL96; IntAct: EBI-3406532,EBI-157240; Score: 0.35
DE  Interaction: Q9VSM6; IntAct: EBI-3406532,EBI-86489; Score: 0.35
DE  Interaction: Q9VP16; IntAct: EBI-3406532,EBI-111934; Score: 0.35
DE  Interaction: Q9W0E3; IntAct: EBI-3406532,EBI-3407605; Score: 0.35
DE  Interaction: Q9VW80; IntAct: EBI-3406532,EBI-3407048; Score: 0.35
DE  Interaction: Q07886; IntAct: EBI-3406532,EBI-3406559; Score: 0.35
DE  Interaction: Q9VJF6; IntAct: EBI-3406532,EBI-126430; Score: 0.35
DE  Interaction: Q9VAW3; IntAct: EBI-3406532,EBI-171618; Score: 0.35
DE  Interaction: Q9V7P1; IntAct: EBI-3406532,EBI-138088; Score: 0.35
DE  Interaction: Q9VHH2; IntAct: EBI-3406532,EBI-3406245; Score: 0.35
DE  Interaction: Q9VY63; IntAct: EBI-3406532,EBI-3408068; Score: 0.35
DE  Interaction: Q9VUE8; IntAct: EBI-3406532,EBI-2507788; Score: 0.35
DE  Interaction: Q9W093; IntAct: EBI-3406532,EBI-3406537; Score: 0.35
DE  Interaction: Q9W0S9; IntAct: EBI-3406532,EBI-94338; Score: 0.35
DE  Interaction: Q9VMQ4; IntAct: EBI-3406532,EBI-3406282; Score: 0.35
DE  Interaction: Q9VAS7; IntAct: EBI-3406532,EBI-82460; Score: 0.35
DE  Interaction: Q9VLM8; IntAct: EBI-3406532,EBI-3402873; Score: 0.35
DE  Interaction: Q9NFV7; IntAct: EBI-3406532,EBI-3403514; Score: 0.35
DE  Interaction: Q7KTX8; IntAct: EBI-3406532,EBI-110730; Score: 0.35
DE  Interaction: Q9VWI5; IntAct: EBI-3406532,EBI-3407255; Score: 0.35
DE  Interaction: Q9VAH7; IntAct: EBI-3406532,EBI-2509120; Score: 0.35
DE  Interaction: Q9XZS9; IntAct: EBI-3406532,EBI-3403938; Score: 0.35
DE  Interaction: Q9VTC1; IntAct: EBI-3406532,EBI-90688; Score: 0.35
DE  Interaction: Q9VPM5; IntAct: EBI-3406532,EBI-178893; Score: 0.35
DE  Interaction: Q9W592; IntAct: EBI-3406532,EBI-122425; Score: 0.35
DE  Interaction: Q27294; IntAct: EBI-3406532,EBI-2890847; Score: 0.35
DE  Interaction: Q5BI50; IntAct: EBI-3406532,EBI-191142; Score: 0.35
DE  Interaction: Q9VNX1; IntAct: EBI-3406532,EBI-115702; Score: 0.35
DE  Interaction: Q0KIF4; IntAct: EBI-3406532,EBI-146233; Score: 0.35
DE  Interaction: Q9V9Z9; IntAct: EBI-3406532,EBI-243148; Score: 0.35
DE  Interaction: A1ZAJ2-1; IntAct: EBI-3406532,EBI-3406636; Score: 0.35
DE  Interaction: A1Z6W6; IntAct: EBI-3406532,EBI-155731; Score: 0.35
DE  Interaction: Q9VDY9; IntAct: EBI-3406532,EBI-178694; Score: 0.35
DE  Interaction: Q7KTW3; IntAct: EBI-3406532,EBI-2509116; Score: 0.35
DE  Interaction: Q9V3X4; IntAct: EBI-3406532,EBI-3408088; Score: 0.35
DE  Interaction: Q9VW64; IntAct: EBI-3406532,EBI-3407961; Score: 0.35
DE  Interaction: Q9VPH6; IntAct: EBI-3406532,EBI-164999; Score: 0.35
DE  Interaction: Q7JVN6; IntAct: EBI-3406532,EBI-84801; Score: 0.35
DE  Interaction: Q9VJ21; IntAct: EBI-3406532,EBI-160882; Score: 0.35
DE  Interaction: A1Z9I3; IntAct: EBI-3406532,EBI-3406677; Score: 0.35
DE  Interaction: Q9V9K7; IntAct: EBI-3406532,EBI-283668; Score: 0.35
DE  Interaction: Q9V9T2; IntAct: EBI-3406532,EBI-3407405; Score: 0.35
DE  Interaction: Q4V5M2; IntAct: EBI-3406532,EBI-193476; Score: 0.35
DE  Interaction: Q9V895-1; IntAct: EBI-3406532,EBI-3407136; Score: 0.35
DE  Interaction: Q9VK72; IntAct: EBI-3406532,EBI-3407031; Score: 0.35
DE  Interaction: Q9W1S3; IntAct: EBI-3406532,EBI-2509178; Score: 0.35
DE  Interaction: I0DHL3; IntAct: EBI-3406532,EBI-9944848; Score: 0.35
DE  Interaction: Q9VAY6; IntAct: EBI-3406532,EBI-162110; Score: 0.35
DE  Interaction: Q9VTG7-2; IntAct: EBI-3406532,EBI-3407949; Score: 0.35
DE  Interaction: P08155-2; IntAct: EBI-3406532,EBI-3407648; Score: 0.35
DE  Interaction: O46040-1; IntAct: EBI-3406532,EBI-3406861; Score: 0.35
DE  Interaction: Q9VY78; IntAct: EBI-3406532,EBI-3406749; Score: 0.35
DE  Interaction: Q9VWQ3; IntAct: EBI-3406532,EBI-3407660; Score: 0.35
DE  Interaction: Q9VL52; IntAct: EBI-3406532,EBI-2508552; Score: 0.35
DE  Interaction: Q9VX34; IntAct: EBI-3406532,EBI-3407051; Score: 0.35
DE  Interaction: Q9VHB4; IntAct: EBI-3406532,EBI-3406586; Score: 0.35
DE  Interaction: Q9VLP5; IntAct: EBI-3406532,EBI-191609; Score: 0.35
DE  Interaction: Q8IPP9; IntAct: EBI-3406532,EBI-3407937; Score: 0.35
DE  Interaction: Q9VIK0; IntAct: EBI-3406532,EBI-102051; Score: 0.35
DE  Interaction: Q9VU11; IntAct: EBI-3406532,EBI-3407566; Score: 0.35
DE  Interaction: Q9VR59; IntAct: EBI-3406532,EBI-153960; Score: 0.35
DE  Interaction: Q9VQ36; IntAct: EBI-3406532,EBI-164303; Score: 0.35
DE  Interaction: A1ZB09; IntAct: EBI-3406532,EBI-3404157; Score: 0.35
DE  Interaction: Q9N6D8; IntAct: EBI-3406532,EBI-122286; Score: 0.35
DE  Interaction: Q9VGU5; IntAct: EBI-3406532,EBI-88232; Score: 0.35
DE  Interaction: Q86BS3; IntAct: EBI-3406532,EBI-109513; Score: 0.35
DE  Interaction: Q9VUK7; IntAct: EBI-3406532,EBI-164419; Score: 0.35
DE  Interaction: A1Z7L8; IntAct: EBI-3406532,EBI-103891; Score: 0.35
DE  Interaction: Q9W213; IntAct: EBI-3406532,EBI-151958; Score: 0.35
DE  Interaction: Q9VKU2; IntAct: EBI-3406532,EBI-3407461; Score: 0.35
DE  Interaction: Q8IN81; IntAct: EBI-3406532,EBI-196787; Score: 0.35
DE  Interaction: Q7KNA0; IntAct: EBI-3406532,EBI-131459; Score: 0.35
DE  Interaction: Q7K2B0; IntAct: EBI-3406532,EBI-2507846; Score: 0.35
DE  Interaction: A1Z8R2; IntAct: EBI-3406532,EBI-2508444; Score: 0.35
DE  Interaction: Q9W3K5; IntAct: EBI-3406532,EBI-3406992; Score: 0.35
DE  Interaction: A1ZAD3; IntAct: EBI-3406532,EBI-2890523; Score: 0.35
DE  Interaction: Q9VU57; IntAct: EBI-3406532,EBI-3406724; Score: 0.35
DE  Interaction: Q9W0S2; IntAct: EBI-3406532,EBI-3406974; Score: 0.35
DE  Interaction: Q9VD46; IntAct: EBI-3406532,EBI-86484; Score: 0.35
DE  Interaction: Q7K3L1; IntAct: EBI-3406532,EBI-191301; Score: 0.35
DE  Interaction: Q8MRN4; IntAct: EBI-3406532,EBI-1109586; Score: 0.35
DE  Interaction: Q9VNH1; IntAct: EBI-3406532,EBI-1629458; Score: 0.35
DE  Interaction: Q9W0S7; IntAct: EBI-3406532,EBI-131216; Score: 0.35
DE  Interaction: Q9VPT4; IntAct: EBI-3406532,EBI-3406206; Score: 0.35
DE  Interaction: Q9W3E2; IntAct: EBI-3406532,EBI-3407921; Score: 0.35
DE  Interaction: Q86B72; IntAct: EBI-3406532,EBI-3407501; Score: 0.35
DE  Interaction: Q9VX14; IntAct: EBI-3406532,EBI-3407350; Score: 0.35
DE  Interaction: Q9NGK5; IntAct: EBI-3406532,EBI-3407445; Score: 0.35
DE  Interaction: A1ZBF7; IntAct: EBI-3406532,EBI-3407533; Score: 0.35
DE  Interaction: Q9VHL1; IntAct: EBI-3406532,EBI-176306; Score: 0.35
DE  Interaction: Q94538; IntAct: EBI-3406532,EBI-6895101; Score: 0.40
GO  GO:0044295;
GO  GO:0005604;
GO  GO:0031012;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0009887;
GO  GO:0007411;
GO  GO:0048749;
GO  GO:0016358;
GO  GO:0070983;
GO  GO:0008347;
GO  GO:0008045;
GO  GO:2000289;
GO  GO:0007432;
GO  GO:0016200;
GO  GO:0008039;
GO  GO:0009888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRATGTRMGLLLPIILALAIGSSAAGISSNDPCYFEGKPRKCLPSFVNAAYGNPVQASSVCGAQQPERYCELLRDGNAG
SQ  ECRSCEQQRYGPAALTDLNNPSNVTCWRSGAVNVPHDPDSAPPDNVTLTLSLGKKYELTYISLSFCPRSPRPDSLAIFKS
SQ  SDFGQTWQPFQFYSSQCQKFYGRPDRAKISKFNEQEARCINSQHDTGGAAQRFAFNTLEGRPSANDLDSSLVLQDWVTAT
SQ  DIRVVFHRLELPPQLLKVKNANAFSDEMGGSREEDEDDDADLELDGEQDEYDYNLQDNDSADAGYDEYEEPKKHLELDDD
SQ  HLHLDYASDGESVVKRQGKHKGSAYEKHYQSKLAATTPPQQPPKVTPPGKVTPPSTAAPSAAASAVTLPISQHYAVSDFA
SQ  VGGRCKCNGHASECVATVSSGSGTALSDQDDGQDEDTPSAPSLANHFGRSTQMSAKLTMTCACKHNTAGPECERCKPFYF
SQ  DRPWGRATDNDANECKMCQCNGHARRCRFNLELYKLSGRVSGGVCYNCQHDTTGRYCHYCREGYYRDATKPPNHRKVCKR
SQ  CDCHPVGSTGKTCNHLSGQCPCKEGVTGLTCNRCARGYQQTRSHVAPCIKVPTNANMIQAESAGGGGGGGTGDYKDGGGS
SQ  QVEEMKKYCGKCKASPKKLNLNKFCMEDYAILAKVIGHDRASQDISTEKFSIERQNEIYKYEINIQTIFKRNPMSGTTSS
SQ  LLGRGNMMLLVPRKSIECQCPKIKLNKSYLILGRDSEAAPGYLAIGPSSVVLEWKDEWSLRMKRFQRRARKCS
//
ID  Q6ZMQ8;
PN  Serine/threonine-protein kinase LMTK1;
GN  AATK;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10837911}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10837911}. Note=Predominantly perinuclear.
DR  UNIPROT: Q6ZMQ8;
DR  UNIPROT: O75136;
DR  UNIPROT: Q6ZN31;
DR  UNIPROT: Q86X28;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 605276;
DR  DisGeNET: 9625;
DE  Function: May be involved in neuronal differentiation. {ECO:0000269|PubMed:10837911}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-2008380,EBI-641062; Score: 0.37
DE  Interaction: P31689; IntAct: EBI-2008380,EBI-347834; Score: 0.35
DE  Interaction: Q15078; IntAct: EBI-746189,EBI-2008380; Score: 0.44
DE  Interaction: P51571; IntAct: EBI-2008380,EBI-1054539; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-2008380,EBI-1222503; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-2008380,EBI-357253; Score: 0.67
DE  Interaction: P36873; IntAct: EBI-2008380,EBI-356283; Score: 0.55
DE  Interaction: Q15293; IntAct: EBI-2008380,EBI-948278; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-2008380,EBI-352007; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-2008380,EBI-352682; Score: 0.35
DE  Interaction: P68032; IntAct: EBI-2008380,EBI-352273; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-2008380,EBI-1047585; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-2008380,EBI-1050588; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-2008380,EBI-356767; Score: 0.35
DE  Interaction: P13674; IntAct: EBI-2008380,EBI-1237386; Score: 0.35
DE  Interaction: O60762; IntAct: EBI-2008380,EBI-719526; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-2008380,EBI-359174; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-2008380,EBI-359163; Score: 0.35
DE  Interaction: Q96N21; IntAct: EBI-11139477,EBI-2008380; Score: 0.56
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004674;
GO  GO:0004713;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSSFFNPSFAFSSHFDPDGAPLSELSWPSSLAVVAVSFSGLFAVIVLMLACLCCKKGGIGFKEFENAEGDEYAADLAQG
SQ  SPATAAQNGPDVYVLPLTEVSLPMAKQPGRSVQLLKSTDVGRHSLLYLKEIGRGWFGKVFLGEVNSGISSAQVVVKELQA
SQ  SASVQEQMQFLEEVQPYRALKHSNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLRSCRVAESMAPDPRTLQRMACEVACG
SQ  VLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLAHCKYREDYFVTADQLWVPLRWIAPELVDEVHSNLLVVDQTKSGNV
SQ  WSLGVTIWELFELGTQPYPQHSDQQVLAYTVREQQLKLPKPQLQLTLSDRWYEVMQFCWLQPEQRPTAEEVHLLLSYLCA
SQ  KGATEAEEEFERRWRSLRPGGGGVGPGPGAAGPMLGGVVELAAASSFPLLEQFAGDGFHADGDDVLTVTETSRGLNFEYK
SQ  WEAGRGAEAFPATLSPGRTARLQELCAPDGAPPGVVPVLSAHSPSLGSEYFIRLEEAAPAAGHDPDCAGCAPSPPATADQ
SQ  DDDSDGSTAASLAMEPLLGHGPPVDVPWGRGDHYPRRSLARDPLCPSRSPSPSAGPLSLAEGGAEDADWGVAAFCPAFFE
SQ  DPLGTSPLGSSGAPPLPLTGEDELEEVGARRAAQRGHWRSNVSANNNSGSRCPESWDPVSAGGHAEGCPSPKQTPRASPE
SQ  PGYPGEPLLGLQAASAQEPGCCPGLPHLCSAQGLAPAPCLVTPSWTETASSGGDHPQAEPKLATEAEGTTGPRLPLPSVP
SQ  SPSQEGAPLPSEEASAPDAPDALPDSPTPATGGEVSAIKLASALNGSSSSPEVEAPSSEDEDTAEATSGIFTDTSSDGLQ
SQ  ARRPDVVPAFRSLQKQVGTPDSLDSLDIPSSASDGGYEVFSPSATGPSGGQPRALDSGYDTENYESPEFVLKEAQEGCEP
SQ  QAFAELASEGEGPGPETRLSTSLSGLNEKNPYRDSAYFSDLEAEAEATSGPEKKCGGDRAPGPELGLPSTGQPSEQVCLR
SQ  PGVSGEAQGSGPGEVLPPLLQLEGSSPEPSTCPSGLVPEPPEPQGPAKVRPGPSPSCSQFFLLTPVPLRSEGNSSEFQGP
SQ  PGLLSGPAPQKRMGGPGTPRAPLRLALPGLPAALEGRPEEEEEDSEDSDESDEELRCYSVQEPSEDSEEEAPAVPVVVAE
SQ  SQSARNLRSLLKMPSLLSETFCEDLERKKKAVSFFDDVTVYLFDQESPTRELGEPFPGAKESPPTFLRGSPGSPSAPNRP
SQ  QQADGSPNGSTAEEGGGFAWDDDFPLMTAKAAFAMALDPAAPAPAAPTPTPAPFSRFTVSPAPTSRFSITHVSDSDAESK
SQ  RGPEAGAGGESKEA
//
ID  Q9NXE4;
PN  Sphingomyelin phosphodiesterase 4;
GN  SMPD4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16517606, ECO:0000269|PubMed:18505924}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16517606}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZPR5}.
DR  UNIPROT: Q9NXE4;
DR  UNIPROT: B1PBA3;
DR  UNIPROT: B4DM23;
DR  UNIPROT: B4DQ31;
DR  UNIPROT: B4DRB8;
DR  UNIPROT: B4DWK7;
DR  UNIPROT: B4E0L6;
DR  UNIPROT: E7ESA2;
DR  UNIPROT: E9PCE6;
DR  UNIPROT: Q6FI76;
DR  UNIPROT: Q6P1P7;
DR  UNIPROT: Q6ZT43;
DR  UNIPROT: Q9H0M2;
DR  UNIPROT: Q9NW20;
DR  UNIPROT: Q9NWL2;
DR  UNIPROT: Q9P2C9;
DR  Pfam: PF14724;
DR  OMIM: 610457;
DR  DisGeNET: 55627;
DE  Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide (PubMed:16517606). May sensitize cells to DNA damage-induced apoptosis (PubMed:18505924). {ECO:0000269|PubMed:16517606, ECO:0000269|PubMed:18505924}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-372102; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-372102; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-372102,EBI-641062; Score: 0.37
DE  Interaction: P05161; IntAct: EBI-746466,EBI-372102; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-372102; Score: 0.35
DE  Interaction: Q9NWW5; IntAct: EBI-6165897,EBI-372102; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-372102; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-372102; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-372102; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-372102; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-372102; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-372102; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-372102; Score: 0.35
DE  Interaction: Q9HAW0; IntAct: EBI-372102,EBI-1055224; Score: 0.40
DE  Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-372102; Score: 0.35
DE  Interaction: Q9NPD3; IntAct: EBI-372102,EBI-371823; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005802;
GO  GO:0046872;
GO  GO:0004767;
GO  GO:0050290;
GO  GO:0071356;
GO  GO:0046513;
GO  GO:0046475;
GO  GO:0006687;
GO  GO:0001701;
GO  GO:0006685;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MTTFGAVAEWRLPSLRRATLWIPQWFAKKAIFNSPLEAAMAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPA
SQ  KELHTIFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKAS
SQ  IQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTSDCAYFILVDRYLSWFLPTEGS
SQ  VPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRHISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQK
SQ  MQSPHAKLEVLHYRLSVSSALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSPL
SQ  EEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSDSQPRCVSEKWAPFVQENLLMY
SQ  TKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAEMIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAV
SQ  TDASFKVKSHVYSLEGQDCKYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYTA
SQ  NDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCIVGEDGLILTPLGRYQIINGLR
SQ  RFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFAGQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVA
SQ  GHTRGPRLSLRFLGSYRTLVSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
//
ID  Q22799;
PN  Dynein light chain 1, cytoplasmic;
GN  dlc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63170}. Nucleus envelope {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}. Cytoplasmic granule {ECO:0000269|PubMed:27864381}. Note=Probably recruited to the nuclear envelope by unc-83 (PubMed:20005871). Localizes to perinuclear patches in the transition zone (PubMed:27864381). Localizes to P- granules in the mitotic region and transition zone (PubMed:27864381). {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}.
DR  UNIPROT: Q22799;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as a non-catalytic accessory component of a dynein complex (By similarity). Part of a complex with bicd-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migrations in hypodermal precursor cells (PubMed:20005871). Probably within a dynein motor complex, plays a role in the cell fate specification of the germline and oogenesis (PubMed:19752194, PubMed:27864381). In particular, it inhibits germ cell proliferation (PubMed:19752194). Regulates the function and localization of the RNA-binding protein fbf- 2 in the germline (PubMed:27864381). Plays a role in mitotic and meiotic processes (PubMed:19752194, PubMed:26483555). Involved in the pairing of homologous chromosomes (PubMed:26483555). Independently of its dynein-mediated functions, plays a role in germ cell apoptosis (PubMed:24030151). {ECO:0000250|UniProtKB:Q24117, ECO:0000269|PubMed:19752194, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:24030151, ECO:0000269|PubMed:26483555, ECO:0000269|PubMed:27864381}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17902; IntAct: EBI-328330,EBI-328324; Score: 0.75
DE  Interaction: Self; IntAct: EBI-328324,EBI-328324; Score: 0.37
DE  Interaction: Q23064; IntAct: EBI-2902228,EBI-328324; Score: 0.37
DE  Interaction: Q23064-3; IntAct: EBI-328324,EBI-2902257; Score: 0.53
DE  Interaction: G5ECT7; IntAct: EBI-328382,EBI-328324; Score: 0.62
DE  Interaction: C6KRN1; IntAct: EBI-328324,EBI-323135; Score: 0.71
DE  Interaction: Q9XUM8; IntAct: EBI-328324,EBI-328132; Score: 0.49
DE  Interaction: Q19207; IntAct: EBI-323336,EBI-328324; Score: 0.37
DE  Interaction: Q7K714; IntAct: EBI-328324,EBI-2005487; Score: 0.37
DE  Interaction: Q19816; IntAct: EBI-328324,EBI-328360; Score: 0.55
DE  Interaction: Q18529; IntAct: EBI-328324,EBI-314884; Score: 0.55
DE  Interaction: Q17902-2; IntAct: EBI-17158122,EBI-328324; Score: 0.37
DE  Interaction: O45599; IntAct: EBI-328324,EBI-319105; Score: 0.37
DE  Interaction: P30642; IntAct: EBI-311981,EBI-328324; Score: 0.37
DE  Interaction: Q18194; IntAct: EBI-2002421,EBI-328324; Score: 0.37
DE  Interaction: P46502; IntAct: EBI-312846,EBI-328324; Score: 0.37
DE  Interaction: G5EFV3; IntAct: EBI-1187461,EBI-328324; Score: 0.37
DE  Interaction: O45087; IntAct: EBI-313406,EBI-328324; Score: 0.37
DE  Interaction: G5EBL8; IntAct: EBI-328324,EBI-2003045; Score: 0.37
DE  Interaction: P34766; IntAct: EBI-311911,EBI-328324; Score: 0.37
DE  Interaction: P91249; IntAct: EBI-313893,EBI-328324; Score: 0.37
DE  Interaction: O45335; IntAct: EBI-324368,EBI-328324; Score: 0.37
DE  Interaction: G5EG76; IntAct: EBI-322231,EBI-328324; Score: 0.37
DE  Interaction: Q9XVX4; IntAct: EBI-328324,EBI-328356; Score: 0.37
DE  Interaction: Q93572; IntAct: EBI-319283,EBI-328324; Score: 0.37
DE  Interaction: P48150; IntAct: EBI-328370,EBI-328324; Score: 0.37
DE  Interaction: O45436; IntAct: EBI-313048,EBI-328324; Score: 0.37
DE  Interaction: Q19988; IntAct: EBI-328365,EBI-328324; Score: 0.37
DE  Interaction: Q20805; IntAct: EBI-328376,EBI-328324; Score: 0.37
DE  Interaction: P48154; IntAct: EBI-321394,EBI-328324; Score: 0.37
DE  Interaction: G5EBX2; IntAct: EBI-316840,EBI-328324; Score: 0.37
DE  Interaction: P55853; IntAct: EBI-313647,EBI-328324; Score: 0.37
DE  Interaction: P34574; IntAct: EBI-319001,EBI-328324; Score: 0.37
DE  Interaction: Q22696; IntAct: EBI-328387,EBI-328324; Score: 0.37
DE  Interaction: G5EDQ5; IntAct: EBI-320979,EBI-328324; Score: 0.37
DE  Interaction: Q9U2M6; IntAct: EBI-328406,EBI-328324; Score: 0.37
DE  Interaction: P55954; IntAct: EBI-328392,EBI-328324; Score: 0.37
DE  Interaction: Q9N432; IntAct: EBI-328399,EBI-328324; Score: 0.37
DE  Interaction: H2L0C9; IntAct: EBI-328416,EBI-328324; Score: 0.37
DE  Interaction: G5EBV6; IntAct: EBI-328338,EBI-328324; Score: 0.37
DE  Interaction: Q18192; IntAct: EBI-319458,EBI-328324; Score: 0.37
DE  Interaction: O16474; IntAct: EBI-328348,EBI-328324; Score: 0.37
DE  Interaction: O17641; IntAct: EBI-328342,EBI-328324; Score: 0.37
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0030286;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0045505;
GO  GO:0051959;
GO  GO:0003774;
GO  GO:0006915;
GO  GO:0051301;
GO  GO:0051321;
GO  GO:0007017;
GO  GO:2000582;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDRKAVIKNADMSDDMQQDAIDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQ
SQ  VAILLFKSG
//
ID  O75821;
PN  Eukaryotic translation initiation factor 3 subunit G;
GN  EIF3G;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
DR  UNIPROT: O75821;
DR  UNIPROT: O14801;
DR  UNIPROT: Q969U5;
DR  PDB: 2CQ0;
DR  PDB: 2MJC;
DR  PDB: 5K0Y;
DR  Pfam: PF12353;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DR  OMIM: 603913;
DR  DisGeNET: 8666;
DE  Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF- 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem- loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP- Rule:MF_03006, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-366632; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-353366,EBI-366632; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-1058922,EBI-366632; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-366632; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-366632; Score: 0.56
DE  Interaction: Q8IZU0; IntAct: EBI-10175124,EBI-366632; Score: 0.56
DE  Interaction: Q9P2Y5; IntAct: EBI-2952704,EBI-366632; Score: 0.35
DE  Interaction: Q9Y6I4; IntAct: EBI-2512643,EBI-366632; Score: 0.40
DE  Interaction: Q9Z0R6; IntAct: EBI-2551755,EBI-366632; Score: 0.40
DE  Interaction: P23116; IntAct: EBI-2552342,EBI-366632; Score: 0.56
DE  Interaction: O15372; IntAct: EBI-709735,EBI-366632; Score: 0.56
DE  Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-366632; Score: 0.35
DE  Interaction: E9QNG1; IntAct: EBI-11017012,EBI-366632; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-366632; Score: 0.35
DE  Interaction: P60229; IntAct: EBI-2678912,EBI-366632; Score: 0.35
DE  Interaction: Q9QZD9; IntAct: EBI-7466616,EBI-366632; Score: 0.35
DE  Interaction: Q49MI3-2; IntAct: EBI-21731382,EBI-366632; Score: 0.35
DE  Interaction: A9UHW6-2; IntAct: EBI-366632,EBI-9118295; Score: 0.56
DE  Interaction: P03366; IntAct: EBI-6164084,EBI-366632; Score: 0.46
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-366632; Score: 0.35
DE  Interaction: A0A384L807; IntAct: EBI-366632,EBI-2844797; Score: 0.37
DE  Interaction: Q5NEC0; IntAct: EBI-366632,EBI-2796355; Score: 0.37
DE  Interaction: P62330; IntAct: EBI-366632,EBI-638181; Score: 0.40
DE  Interaction: O60739; IntAct: EBI-366632,EBI-1043343; Score: 0.40
DE  Interaction: P20339; IntAct: EBI-399437,EBI-366632; Score: 0.35
DE  Interaction: P55884; IntAct: EBI-366632,EBI-366696; Score: 0.86
DE  Interaction: Q9UMQ6; IntAct: EBI-366632,EBI-3915726; Score: 0.40
DE  Interaction: Q8K337-1; IntAct: EBI-25409743,EBI-366632; Score: 0.35
DE  Interaction: Q6ZR37; IntAct: EBI-20845503,EBI-366632; Score: 0.35
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-366632; Score: 0.56
DE  Interaction: P40217; IntAct: EBI-366632,EBI-8951; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-366632; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-366632,EBI-373519; Score: 0.35
DE  Interaction: Q99613; IntAct: EBI-366632,EBI-353741; Score: 0.67
DE  Interaction: Q7L2H7; IntAct: EBI-366632,EBI-353901; Score: 0.35
DE  Interaction: Q14152; IntAct: EBI-366632,EBI-366617; Score: 0.67
DE  Interaction: Q13347; IntAct: EBI-366632,EBI-354047; Score: 0.69
DE  Interaction: P60228; IntAct: EBI-366632,EBI-347740; Score: 0.35
DE  Interaction: P55884-2; IntAct: EBI-366632,EBI-16399439; Score: 0.35
DE  Interaction: O15371; IntAct: EBI-366632,EBI-353818; Score: 0.35
DE  Interaction: O00303; IntAct: EBI-366632,EBI-711990; Score: 0.35
DE  Interaction: O75822; IntAct: EBI-366647,EBI-366632; Score: 0.35
DE  Interaction: Q99547; IntAct: EBI-366632,EBI-373187; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016282;
GO  GO:0033290;
GO  GO:0005852;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
GO  GO:0001732;
GO  GO:0006413;
GO  GO:0075525;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFK
SQ  IVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRIC
SQ  KGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNAT
SQ  IRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
//
ID  Q969L2;
PN  Protein MAL2;
GN  MAL2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Endomembrane system. Cytoplasm, perinuclear region. Note=Associated with lipid rafts. In polarized epithelial cells, restricted to the apical surface. In hepatocytes, as well as in polarized hepatoma Hep-G2 cells, found in the canalicular membrane, equivalent to the apical surface, beneath the canalicular actin cytoskeleton. In non-polarized Hep-G2 cells, distributed to the perinuclear region.
DR  UNIPROT: Q969L2;
DR  UNIPROT: B2R520;
DR  UNIPROT: Q6ZMD9;
DR  Pfam: PF01284;
DR  PROSITE: PS51225;
DR  OMIM: 609684;
DR  DisGeNET: 114569;
DE  Function: Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway. {ECO:0000269|PubMed:12370246}.
DE  Reference Proteome: Yes;
DE  Interaction: P55327; IntAct: EBI-944295,EBI-782581; Score: 0.37
DE  Interaction: P53365; IntAct: EBI-638194,EBI-944295; Score: 0.72
DE  Interaction: Q9BU27; IntAct: EBI-944295,EBI-10298603; Score: 0.56
DE  Interaction: Q969Z0; IntAct: EBI-702328,EBI-944295; Score: 0.56
DE  Interaction: Q96AX2; IntAct: EBI-944295,EBI-748121; Score: 0.56
DE  Interaction: P43378; IntAct: EBI-944295,EBI-742898; Score: 0.67
DE  Interaction: Q5JS98; IntAct: EBI-10244393,EBI-944295; Score: 0.56
DE  Interaction: Q5ST30-3; IntAct: EBI-944295,EBI-10244969; Score: 0.56
DE  Interaction: Q5SU16; IntAct: EBI-944295,EBI-10245038; Score: 0.56
DE  Interaction: Q6FGM0; IntAct: EBI-944295,EBI-10173690; Score: 0.56
DE  Interaction: Q6IQ43; IntAct: EBI-10250413,EBI-944295; Score: 0.56
DE  Interaction: Q05329; IntAct: EBI-9304251,EBI-944295; Score: 0.72
DE  Interaction: Q9NQG6; IntAct: EBI-740987,EBI-944295; Score: 0.56
DE  Interaction: Q9ULP0-2; IntAct: EBI-11978907,EBI-944295; Score: 0.72
DE  Interaction: Q9BW92; IntAct: EBI-1045099,EBI-944295; Score: 0.56
DE  Interaction: Q9HB07; IntAct: EBI-709754,EBI-944295; Score: 0.56
DE  Interaction: Q9P2R7; IntAct: EBI-944295,EBI-2269898; Score: 0.56
DE  Interaction: Q99961; IntAct: EBI-697911,EBI-944295; Score: 0.56
DE  Interaction: Q9UGP5-2; IntAct: EBI-10320765,EBI-944295; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-944295,EBI-13059134; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-17247926,EBI-944295; Score: 0.56
DE  Interaction: P62136; IntAct: EBI-944295,EBI-357253; Score: 0.37
DE  Interaction: Q9H221; IntAct: EBI-3908684,EBI-944295; Score: 0.37
DE  Interaction: P49638; IntAct: EBI-944295,EBI-10210710; Score: 0.56
DE  Interaction: Q5VYK3; IntAct: EBI-944295,EBI-521451; Score: 0.56
DE  Interaction: Q9UKF7-2; IntAct: EBI-944295,EBI-14223623; Score: 0.56
DE  Interaction: Q9UBD0; IntAct: EBI-944295,EBI-947253; Score: 0.56
DE  Interaction: Q8WY91; IntAct: EBI-944295,EBI-726691; Score: 0.56
DE  Interaction: Q96AL5; IntAct: EBI-944295,EBI-741171; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-944295,EBI-2623095; Score: 0.56
DE  Interaction: A0A0S2Z4D9; IntAct: EBI-944295,EBI-16430771; Score: 0.56
DE  Interaction: Q9BSJ6; IntAct: EBI-944295,EBI-2568609; Score: 0.56
DE  Interaction: Q99259; IntAct: EBI-944295,EBI-743184; Score: 0.72
DE  Interaction: P34897; IntAct: EBI-944295,EBI-352908; Score: 0.56
DE  Interaction: A8MRB1; IntAct: EBI-944295,EBI-16432654; Score: 0.56
DE  Interaction: Q8NI60; IntAct: EBI-944295,EBI-745535; Score: 0.56
DE  Interaction: O95971; IntAct: EBI-944295,EBI-4314390; Score: 0.56
DE  Interaction: O00141; IntAct: EBI-944295,EBI-1042854; Score: 0.56
DE  Interaction: Q8NET5; IntAct: EBI-11990542,EBI-944295; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-7545592,EBI-944295; Score: 0.56
DE  Interaction: P34810; IntAct: EBI-2826276,EBI-944295; Score: 0.56
DE  Interaction: O15342; IntAct: EBI-12935759,EBI-944295; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-13345167,EBI-944295; Score: 0.56
DE  Interaction: P08034; IntAct: EBI-17565645,EBI-944295; Score: 0.56
DE  Interaction: Q9NQQ7-3; IntAct: EBI-17295964,EBI-944295; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-10192441,EBI-944295; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-8638294,EBI-944295; Score: 0.56
DE  Interaction: P15941-11; IntAct: EBI-17263240,EBI-944295; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-11343438,EBI-944295; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-6942903,EBI-944295; Score: 0.56
DE  Interaction: Q6IN84; IntAct: EBI-944295,EBI-5454865; Score: 0.56
DE  Interaction: Q96E29; IntAct: EBI-7825321,EBI-944295; Score: 0.56
DE  Interaction: P00431; IntAct: EBI-4389,EBI-944295; Score: 0.56
DE  Interaction: P04819; IntAct: EBI-944295,EBI-5991; Score: 0.56
DE  Interaction: P32453; IntAct: EBI-944295,EBI-3306; Score: 0.56
GO  GO:0016324;
GO  GO:0012505;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0019911;
GO  GO:0042552;
GO  GO:0045056;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAGGASVPPPPNPAVSFPPPRVTLPAGPDILRTYSGAFVCLEILFGGLVWILVASSNVPLPLLQGWVMFVSVTAFFFSL
SQ  LFLGMFLSGMVAQIDANWNFLDFAYHFTVFVFYFGAFLLEAAATSLHDLHCNTTITGQPLLSDNQYNINVAASIFAFMTT
SQ  ACYGCSLGLALRRWRP
//
ID  Q9NZU7;
PN  Calcium-binding protein 1;
GN  CABP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14685260}. Cell membrane {ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side. Golgi apparatus {ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}. Cell junction, synapse, postsynaptic density {ECO:0000305}. Note=L- CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane. {ECO:0000269|PubMed:10625670}. [Isoform L-CaBP1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures. {ECO:0000269|PubMed:10625670}. [Isoform S-CaBP1]: Cytoplasm, cell cortex. Cell membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor {ECO:0000305}. Note=S-CaBP1 is localized at or near the plasma membrane.
DR  UNIPROT: Q9NZU7;
DR  UNIPROT: O95663;
DR  UNIPROT: Q8N6H5;
DR  UNIPROT: Q9NZU8;
DR  PDB: 2K7B;
DR  PDB: 2K7C;
DR  PDB: 2K7D;
DR  PDB: 2LAN;
DR  PDB: 2LAP;
DR  PDB: 3OX5;
DR  PDB: 3OX6;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 605563;
DR  DisGeNET: 9478;
DE  Function: Modulates calcium-dependent activity of inositol 1,4,5- triphosphate receptors (ITPRs)(PubMed:14570872). Inhibits agonist- induced intracellular calcium signaling (PubMed:15980432). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C- terminal domain of CACNA1C, but has an opposite effect on channel function (PubMed:15140941). Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels (PubMed:15895247). Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity). {ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7, ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
DE  Reference Proteome: Yes;
DE  Interaction: P06623; IntAct: EBI-907934,EBI-907894; Score: 0.40
DE  Interaction: P08047; IntAct: EBI-298336,EBI-907894; Score: 0.40
DE  Interaction: P01100; IntAct: EBI-907894,EBI-852851; Score: 0.40
DE  Interaction: Q13936; IntAct: EBI-1038838,EBI-907894; Score: 0.52
GO  GO:0005938;
GO  GO:0030054;
GO  GO:0005856;
GO  GO:0005615;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0004857;
GO  GO:0008139;
GO  GO:0042308;
GO  GO:0050896;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAAS
SQ  GGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSS
SQ  PLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKD
SQ  KDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDG
SQ  EISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
//
ID  Q9UII4;
PN  E3 ISG15--protein ligase HERC5;
GN  HERC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20542004}. Note=Associated with the polyribosomes, probably via the 60S subunit.
DR  UNIPROT: Q9UII4;
DR  UNIPROT: B2RTQ1;
DR  UNIPROT: Q69G20;
DR  Pfam: PF00632;
DR  Pfam: PF00415;
DR  PROSITE: PS50237;
DR  PROSITE: PS00626;
DR  PROSITE: PS50012;
DR  OMIM: 608242;
DR  DisGeNET: 51191;
DE  Function: Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15. {ECO:0000269|PubMed:16407192, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:16884686, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20385878, ECO:0000269|PubMed:20542004}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8K4B0; IntAct: EBI-1216353,EBI-2339540; Score: 0.35
DE  Interaction: Q969T4; IntAct: EBI-348496,EBI-2339540; Score: 0.37
DE  Interaction: P51965; IntAct: EBI-348546,EBI-2339540; Score: 0.37
DE  Interaction: Q96LR5; IntAct: EBI-2129763,EBI-2339540; Score: 0.37
DE  Interaction: Q99558; IntAct: EBI-358011,EBI-2339540; Score: 0.35
DE  Interaction: Q8WVJ2; IntAct: EBI-2339540,EBI-1052153; Score: 0.40
DE  Interaction: P33981; IntAct: EBI-1645856,EBI-2339540; Score: 0.35
DE  Interaction: Q9JJR9; IntAct: EBI-2553399,EBI-2339540; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-2339540; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-985879,EBI-2339540; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-351126,EBI-2339540; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-8361659,EBI-2339540; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054761,EBI-2339540; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-1237328,EBI-2339540; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-2008793,EBI-2339540; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-5453434,EBI-2339540; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-356746,EBI-2339540; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-444173,EBI-2339540; Score: 0.35
DE  Interaction: Q9BSG1; IntAct: EBI-8489229,EBI-2339540; Score: 0.35
DE  Interaction: Q8WYQ5-3; IntAct: EBI-10980537,EBI-2339540; Score: 0.35
DE  Interaction: Q5T3I0-3; IntAct: EBI-21605187,EBI-2339540; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-352694,EBI-2339540; Score: 0.35
DE  Interaction: Q9P031; IntAct: EBI-1047110,EBI-2339540; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-443446,EBI-2339540; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-6911574,EBI-2339540; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0042296;
GO  GO:0003723;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032020;
GO  GO:0032480;
GO  GO:0000209;
GO  GO:0016567;
GO  GO:0000079;
GO  GO:0050688;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERRSRRKSRRNGRSTAGKAAATQPAKSPGAQLWLFPSAAGLHRALLRRVEVTRQLCCSPGRLAVLERGGAGVQVHQLLA
SQ  GSGGARTPKCIKLGKNMKIHSVDQGAEHMLILSSDGKPFEYDNYSMKHLRFESILQEKKIIQITCGDYHSLALSKGGELF
SQ  AWGQNLHGQLGVGRKFPSTTTPQIVEHLAGVPLAQISAGEAHSMALSMSGNIYSWGKNECGQLGLGHTESKDDPSLIEGL
SQ  DNQKVEFVACGGSHSALLTQDGLLFTFGAGKHGQLGHNSTQNELRPCLVAELVGYRVTQIACGRWHTLAYVSDLGKVFSF
SQ  GSGKDGQLGNGGTRDQLMPLPVKVSSSEELKLESHTSEKELIMIAGGNQSILLWIKKENSYVNLKRTIPTLNEGTVKRWI
SQ  ADVETKRWQSTKREIQEIFSSPACLTGSFLRKRRTTEMMPVYLDLNKARNIFKELTQKDWITNMITTCLKDNLLKRLPFH
SQ  SPPQEALEIFFLLPECPMMHISNNWESLVVPFAKVVCKMSDQSSLVLEEYWATLQESTFSKLVQMFKTAVICQLDYWDES
SQ  AEENGNVQALLEMLKKLHRVNQVKCQLPESIFQVDELLHRLNFFVEVCRRYLWKMTVDASENVQCCVIFSHFPFIFNNLS
SQ  KIKLLHTDTLLKIESKKHKAYLRSAAIEEERESEFALRPTFDLTVRRNHLIEDVLNQLSQFENEDLRKELWVSFSGEIGY
SQ  DLGGVKKEFFYCLFAEMIQPEYGMFMYPEGASCMWFPVKPKFEKKRYFFFGVLCGLSLFNCNVANLPFPLALFKKLLDQM
SQ  PSLEDLKELSPDLGKNLQTLLDDEGDNFEEVFYIHFNVHWDRNDTNLIPNGSSITVNQTNKRDYVSKYINYIFNDSVKAV
SQ  YEEFRRGFYKMCDEDIIKLFHPEELKDVIVGNTDYDWKTFEKNARYEPGYNSSHPTIVMFWKAFHKLTLEEKKKFLVFLT
SQ  GTDRLQMKDLNNMKITFCCPESWNERDPIRALTCFSVLFLPKYSTMETVEEALQEAINNNRGFG
//
ID  P12683;
PN  3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
GN  HMG1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope.
DR  UNIPROT: P12683;
DR  UNIPROT: D6W0K8;
DR  Pfam: PF00368;
DR  Pfam: PF13323;
DR  Pfam: PF12349;
DR  PROSITE: PS00066;
DR  PROSITE: PS00318;
DR  PROSITE: PS01192;
DR  PROSITE: PS50065;
DR  PROSITE: PS50156;
DE  Function: One of 2 isozymes that catalyze the conversion of HMG-CoA to mevalonate. It is the rate-limiting enzyme of the sterol biosynthesis pathway. Involved in ergosterol biosynthesis. {ECO:0000269|PubMed:3526336, ECO:0000269|PubMed:9292983}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-8377,EBI-8377; Score: 0.37
DE  Interaction: P12684; IntAct: EBI-8377,EBI-8384; Score: 0.67
DE  Interaction: Q12329; IntAct: EBI-8571,EBI-8377; Score: 0.35
DE  Interaction: Q08421; IntAct: EBI-8377,EBI-762498; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-8377,EBI-24471; Score: 0.35
DE  Interaction: Q12447; IntAct: EBI-8377,EBI-33397; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-8377,EBI-21409; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-8377,EBI-20254; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-8377,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-8377,EBI-18976; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-8377,EBI-6314; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8377,EBI-8603; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-8377,EBI-10789; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-8377,EBI-13910; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-8377,EBI-15913; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-8377,EBI-11191; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-8377,EBI-11178; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-8377,EBI-9166; Score: 0.35
DE  Interaction: P39993; IntAct: EBI-8377,EBI-7547; Score: 0.35
DE  Interaction: P43535; IntAct: EBI-8377,EBI-7423; Score: 0.35
DE  Interaction: P47912; IntAct: EBI-8377,EBI-10095; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-8377,EBI-20589; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-8377,EBI-2218; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8377,EBI-8627; Score: 0.35
DE  Interaction: P16370; IntAct: EBI-8377,EBI-15773; Score: 0.35
DE  Interaction: P25454; IntAct: EBI-8377,EBI-14709; Score: 0.44
DE  Interaction: P46985; IntAct: EBI-8377,EBI-11052; Score: 0.35
DE  Interaction: P39925; IntAct: EBI-2317,EBI-8377; Score: 0.27
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005778;
GO  GO:0050662;
GO  GO:0004420;
GO  GO:0042282;
GO  GO:0015936;
GO  GO:0006696;
GO  GO:0019287;
GO  GO:0008299;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYR
SQ  DSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSD
SQ  RKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQ
SQ  CILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCS
SQ  MYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLN
SQ  LSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRI
SQ  EDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTV
SQ  ISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLG
SQ  DTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVAS
SQ  AMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFM
SQ  RFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKS
SQ  DVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIG
SQ  GGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATD
SQ  INRLKDGSVTCIKS
//
ID  P35508;
PN  Casein kinase I isoform delta;
GN  CSNK1D;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
DR  UNIPROT: P35508;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000139;
GO  GO:0005815;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005876;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0032922;
GO  GO:1905515;
GO  GO:0018105;
GO  GO:0090263;
GO  GO:0032436;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  P63243;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  RACK1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: P63243;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  UNIPROT: Q3T0R8;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (By similarity). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration (By similarity). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0022627;
GO  GO:0030425;
GO  GO:1990630;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0051434;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0019899;
GO  GO:0008200;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0030178;
GO  GO:0043473;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0072344;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P0C6W4;
PN  2'-O-methyltransferase;
GN  rep;
OS  694008;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W4;
DR  UNIPROT: A3EXC9;
DR  Pfam: PF13087;
DR  Pfam: PF16348;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF11633;
DR  Pfam: PF08715;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016896;
GO  GO:0008168;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0032259;
GO  GO:0039648;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVAGVAPQGARGKYRAELNTEKRTDHVSLKASLCDAGDLVLKISPWFMDGESAYKHVSEQLSKGSKLLFVPQTLKGFI
SQ  RHLPGPRVYLVERLTGGTYSDPFMVNQLAYQNAAGEGVIGTTLQGKRVGMFFPFDADLVTGEFQFLLRKKGFGGNRFRDA
SQ  PWDYNWTPYSDLMDALEADPCGKYSQSLLKKLVGGDFTPIDQYMCGKNGKPIAEFAALMASEGITKLADVEAEVKSRTDS
SQ  DRYIVFKNKLYRIVWNVQRKDVAYSKQSAFTMNSIVQLDTMEDVPRHSFTIGSEIQVIAPSTAVQANGHLNLKQRLLYAF
SQ  YGKQAVSEPNYIYHSAYVDCTSCGKGSWLTGNAVQGFACDCGAHYCANDVDLQSSGLVRKNAVLLTTCPCNKDGECKHTL
SQ  PQLVSMMTDKCDVEVVGKTFILTYGGVIYAYMGCSGGTMHFIPRAKSCVSKIGDAIFTGCTGTWSKVCETANLFLERAQH
SQ  AINFVNEFVLTETVVALLSGTTSSIEELRDLCRNATFEKVRDYLTPRGWIVTMGSYIEGVINVGAAGVCNAALNAPFIVL
SQ  SGLGESFKKVAATPWKLCSSLRETLDHYADSITYRVFPYDIPCDVTDYTALLLDCAVLTGASAYFVARYVDEKVEQLTNL
SQ  VFSSCQSAVAAFVQACMSTYKATAKFISDMFTLIKVVSERLYVYTSVGFVVVGDYSSQLLKQFMHILSKAMQLLHTTVSW
SQ  AGSKLPSVVYNGRDSLVFPSGTYYCVSTQGRSLQDQFDLVIPGDLSKKQIGILEPTPNSTTVDKKINTNVVEVVVGQLEP
SQ  TKEHSPELVVGDYVIISNKIFVRSVEDSETVFYPLCTDGKIVPTLFRLKGGAPPKGVKFGGEQTKEITAVRSVSVDYDVH
SQ  PVLDALLAGSELATFTVEKDLPVKDFVDVVKDEVIELLSKLLRGYNVDGFDLEDFADTPCYVYNAEGDLAWSSTMTFSVN
SQ  PVEEVEEECDDDYVEDEYLSEEMLVEEDENSWAAAVEAVIPMEDVQLDTLVAEIDVSEPADDVAEQASTEEVEVPSACVL
SQ  EASQVANAAEVESCEAEVSSSIPLHEDANAAKANDCAEGMPALDSTETVSKLSVDTPVGDVTQDDATSSNATVISEDVHT
SQ  ATHSKGLVAVPEVVPEKALGTSVERMRSTSEWTVVETSLKQETAVIVKNDSSAKPQRVKKPKAENPLKNFKHIVLNNDVT
SQ  LVFGDAIAVARATEDCILVNAANTHLKHGGGIAAAIDRASGGLVQAESDDYVNFYGPLNVGDSTLLKGHGLATGILHVVG
SQ  PDARANQDIQLLKRCYKAFNKYPLVVSPLISAGIFCVEPRVSLEYLLSVVHTKTYVVVNSEKVYNDLAAPKPPTGLTYSH
SQ  EGWRGIIRNAKSFGFTCFICTDQSANAKLLKGRGVDLTKKTQTVDGVKYYLYSSKDPLTDIITAANACKGICAMPIGYVT
SQ  HGLDLAQAGQQVKKITVPYVCLLASKDQVPILNSDVAVQTPEQSFINTVIANGGYHCWHLVTGELIVKGVSYRKLLNWSD
SQ  QTICYADNKFYVVKGQIALPFDSLEKCRTYLTSRAAQQKNVDVLVTIDGVNFRTVVLNNTTTYRVQLGSVFYKGSDISDT
SQ  IPTEKMSGEAVYLADNLSEAEKAVLSEVYGTADTAFLHRYYSLLALVKKWKYTVHDGVKSLKLNSNNCYVNVTMLMLDML
SQ  KEIKFIVPALQAAYLKHKGGDSTEFIALIMAYGDCTYGEPDDASRLLHTILSKAELTTQAKMVWRQWCNVCGVQDTTTTG
SQ  LKACIYVGMNSLDELHATHEECCQCGDVRKRQLVEHNAPWLLLSGLNEAKVMTPTSQSAGPDYTAFNVFQGVETSVGHYL
SQ  HVRVKDNLLYKYDSGSLSKTSDMKCKMTDVYYPKQRYSADCNVVVYSLDGNTWADVDPDLSAFYMKDGKYFTKKPVIEYS
SQ  PATILSGSVYTNSCLVGHDGTIGSDAISSSFNNLLGFDNSKPVSKKLTYSFFPDFEGDVILTEYSTYDPIYKNGAMLHGK
SQ  PILWVNNSKFDSALNKFNRATLRQVYDIAPVTLENKYTVLQDNQIQQVEVEAPKEDAKPQSPVQVAEDIDNKLPIIKCKG
SQ  LKKPFVKDGYSFVNDPQGVNVIDTLGIDDLRALYVDRNLRLIVLKENNWSALFNIHTVEKGDLSVIAASGSITRRVKILL
SQ  GASSLFAQFASVTVNVTTAMGKALGRMTRNVITNTGIIGQGFALLKMLLILPFTFWKSKNQSTVKVEVGALRTAGIVTTN
SQ  VVKQCASAAYDVLVVKFKRIDWKSTLRLLFLICTTGLLLSSLYYLFLFHQVLTSDVMLDGAEGMLATYRELRSYLGIHSL
SQ  CDGMVEAYRNVSYDVNDFCSNRSALCNWCLIGQDSLTRYSAFQMIQTHVTSYVINIDWVWFVMEFALAYVLYTSTFNVLL
SQ  LVVSSQYFFSYTGAFVNWRSYNYLVSGYFFCVTHIPLLGLVRIYNFLACLWFLRRFYNHVINGCKDTACLLCYKRNRLTR
SQ  VEASTVVCGSKRTFYIVANGGTSFCCRHNWNCVDCDTAGIGNTFICEEVANDLTTSLRRLVKPTDKSHYYVESVTVKDSV
SQ  VQLHYSREGASCYERYPLCYFTNLDKLKFKEVCKTPTGIPEHNFLIYDSSDRGQENLARSACVYYSQVLSKPMLLVDSNM
SQ  VTTVGDSREIASKMLDSYVNSFISLFGVNRDKLDKLVATARDCVKRGDDFQTVIKTFTDAARGPAGVESDVETSSIVDAL
SQ  QYAYKHDLQLTTEGFNNYVPSYIKPDSVATADLGCLIDLNAASVNQTSIRNANGACIWNSSDYMKLSDSLKRQIRIACRK
SQ  CNIPFRLTTSRLRSADNILSVKFSATKLSGGAPKWLLKLRDFTWKSYCVVTLVVFAMAVLSYLCLPAFNMSQVSFHEDRI
SQ  LTYKVVENGIIRDITPSDTCFANKYQSFSKWFNEHYGGLFNNDISCPVTVAVIAGVAGARVPNLPANVAWVGRQIVLFVS
SQ  RVFASSNNVCYTPTAEIPYERFSDSGCVLASECTLFRDAEGKINPYCYDPTVLPGASAYDQMKPHVRYDMYDSDMYIKFP
SQ  EVVFESTLRITKTLATRYCRFGSCEDANEGVCITTNGSWAIYNDHYANKPGVYCGDNYFDIVRRLGLSLFQPVTYFQLST
SQ  SLALGVMLCIFLTIAFYYVNKVKRALADYTQCAVVAVAAALLNSLCLCFVVSNPLLVLPYTALYYYATFYLTGEPAFVMH
SQ  VSWFVMFGTVVPIWMVFAYIVGVCLRHLLWVMAYFSKKHVEVFTDGKLNCSFQDAAANIFVINKDTYVALRNSITQDSYN
SQ  RYLSMFNKYKYYSGAMDTASYREASAAHLCKALQVYSETGSDVLFQPPNCSVTSSVLQSGLVKMAAPSGVVENCMVQVTC
SQ  GSMTLNGLWLDNYVWCPRHVMCPADQLSDPNYDALLVSKTNLSFIVQKNVGAPANLRVVGHTMVGTLLKLTVESANPQTP
SQ  AYTFTTVKPGASFSVLACYNGRPTGVFMVNMRQNSTIKGSFLCGSCGSVGYTQEGNVINFCYMHQMELSNGTHTGCAFDG
SQ  VMYGAFEDRQVHQVQLSDKYCTINIVAWLYAAILNGCNWFVKPNKTGIATFNEWAMSNQFTEFIGTQSVDMLAHKTGVSV
SQ  EQLLYAIQTLHKGFQGKTILGNSMLEDEFTPDDVNMQVMGVVMQSGVKRISYGLVHWLFTTLLLAYVATLQLTKFTIWNY
SQ  LFEVIPLQLTPLVLCVMACVMLTVKHKHTFLTLFLLPTAICLTYANIVYEPQTPVSSALIAVANWLNPASVYMRTTHTDL
SQ  GVYLSLCFALAVVVRRLYRPNASNLALALGSAMVWFYTYTTGDCSSPLTYLMFLTTLTSDYTVTVFLAVNVAKFFARVVF
SQ  LYAPHAGFIFPEVKLVLLMYLAVGYFCTVYFGVFSLLNLKLRVPLGVYDYTVSTQEFRYLTGNGLHAPRNSWEALRLNMK
SQ  LIGIGGTPCIKIASVQSKLTDLKCTSVVLLSVLQQLHLEANSKAWAHCVKLHNDILAATDPTEAFDNFVCLFATLMSFSA
SQ  NVDLEALASDLLDHPSVLQATLSEFSHLASYAELEAAQSSYQKALNSGDASPQVLKALQKAVNIAKNAYEKDKAVARKLE
SQ  RMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVISNARNGCVPLSVVPLCASNKLRVVIPDITIWNK
SQ  VVTWPSLSYAGALWDISLINNVDGEVVKSSDVTETNESLTWPLVLECTRAASSAVTLQNNEIRPSGLKTMVVSAGIDHAN
SQ  CNTSSLAYYEPVEGRKMLMGILSENAHLKWAKVEGRDGFVNIELQPPCKFLIAGPKGPEVRYLYFVKNLNNLHRGQLLGH
SQ  IAATVRLQAGSNTEFAINSSVLSAVTFSVDPGKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAVSVKPEANADQDTYGGAS
SQ  VCLYCRAHIEHPDVTGVCKFKGKFVQVPLHIRDPVGFCLQNTPCNVCQFWIGHGCNCDALRGTTIPQSKDSNFLNRVRGS
SQ  IVNARIEPCASGLTTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVEVDDEGHRLDSFFVVKRHTMENYELEKRCYDLVK
SQ  DCDAVAVHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNNCEVLKSILVKYGCCDASYFDNKLWFDFVENPNV
SQ  ISVYHKLGERIRQAVLNTVKFCDQMVKSGLVGVLTLDNQDLNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCL
SQ  AAETHRDCDLTKPLIEWPLLEYDYTDYKIGLFEKYFKXWDQQYHPNCVNCTDDRCVLHCANFNVLFSMTLPGTSFGPIVR
SQ  KIFVDGVPFVISCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVR
SQ  PGNFNKDFYDFVVSKGFFKEGSSVTLRHFFFAQDGHAAITDYSYYAYNLPTMCDIKQMLFCMEVVDRYFEIYDGGCLNAS
SQ  EVIVNNLDKSAGHPFNKFGKARVYYESLSYQEQDELFAMTKRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQY
SQ  HQKMLKSMAATRGSTCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHSTCCTNTDR
SQ  FYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNTIVDEEVKDMQFELYVNV
SQ  YRKSQPDPKFVDRYYAFLNKHFSMMILSDDGVVCYNSDYATKGYIASIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHE
SQ  FCSQHTLFIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHDDPEYQNVFWVYLQYIEKL
SQ  YKDLTGHMLDSYSVMLCGDNSAKFWEESFYRDLYTAPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPH
SQ  KMVLSVSPYVCNAPGCDVADVTKLYLGGMSYFCIDHRPVCSFPLCANGLVFGLYKNMCTGSPSVTEFNRLATCDWTESGD
SQ  YTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERELLLVWEAGKAKPPLNRNYVFTGYHITKNSKVQLGEYV
SQ  FERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLQAPTIVNQERYVKITGLYPTLTVPEEFANHVANFQKAGFSKFVT
SQ  VQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDQFKVNETNSQYLFST
SQ  INALPETSADILVVDEVSMCTNYDLSVINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLS
SQ  VCYRCPEEIVNTVSALVYNNKLVAKKPASGQCFKILYKGSVTHDASSAINRPQLNFVKSFIAANPNWSKAVFISPYNSQN
SQ  AVARSVLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNINRFNVAVTRAQKGILCVMTSQALFDSLEFAEVSLNNYKLQS
SQ  QIVTGLYKDCSRESSGLHPAYAPTYVSVDDKYKTSDELCVNLNVPANVPYSRVISRMGFKLDASIPNYPKLFITRDEAIR
SQ  QVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGSMLTSIAARPPPGEQFKHLVPLMNKGAAWPI
SQ  VRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQRCCMCNRRASTYSSPLHSYACWSHSSGYDYVYNPFF
SQ  VDVQQWGYIGNLATNHDRYCSVHQGAHVASNDAVMTRCLAIHDCFIERVEWDITYPYISHEKRLNSCCRAVERNVVRAAL
SQ  LAGRFERVYDIGNPKGIPIVDDPVVDWHYYDAQPLSKKVQQLFYTEDCAKNFSDGLCLFWNCNVPRYPNNAIVCRFDTRV
SQ  HSEFNLPGCDGGSLYVNKHAFHTPAYDASAFRDLKPLPFFYYSTTPCEVHGNGNMLEDIDYVPLKSAVCITACNLGGAVC
SQ  RKHAAEYRDYMEAYNLVSASGFRLWCYKTFDVYNLWSTFTKIQGLENIAYNVIKQGHFTGVEGELPVAVVNDKIYTKSDV
SQ  NDVCIFENKTTLPTNIAFELYAKRAVRSHPDFNLLRNLEVDVCYKFVLWDYERSNIYGSATIGVCKYTDIDVNSALNICF
SQ  DIRDNGSLERFMSLPNGILISDRKVKNYPCIVSSNYAYFNGTLIRDNTGNSQSSDGEVKQPVTFYIYKKVNNEFVQFTDT
SQ  YYTLGRTVSDFTPVSEMEKDFLALDSDVFIKKYKLEAYAFEHVVYGDFSRTTLGGLHLLIGLYKKHQEGHIIMEEMLKER
SQ  ATVHNYFVTESNTASFKAVCSVIDLKLDDFVDIIKAMDLSVVSKVVKIPIDLTMIEFMLWCKDGQVQTFYPRLQAINDWK
SQ  PGLAMPSLFKVQNSNLEPCMLPNYKQSIPMPQGVHMNIAKYMQLCQYLNTCTIAVPANMRVMHFGAGSDKGVAPGSSVLR
SQ  QWLPTDAILIDNDLNEYVSDADITLFGDCVTVRVGQQVDLLISDMYDPSTKVVGETNEAKALFFVYLCNFIKNNLALGGS
SQ  VAIKITEHSWSAELYELMGRFAWWTVFCTNANASSSEGFLIGINYLGELKEVIDGNVMHANYIFWRNTTLMNLSTYSLFD
SQ  LSRFPLKLKGTPVLQLKESQINELVISLLSQGKLIIRDNDTLSVSTDVLVNFYRKPHKRSKC
//
ID  P0C6V2;
PN  Non-structural protein 11;
GN  1a;
OS  11151;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6V2;
DR  UNIPROT: Q9IW06;
DR  PDB: 1LVO;
DR  PDB: 1P9U;
DR  PDB: 2AMP;
DR  PDB: 3MP2;
DR  PDB: 3ZBD;
DR  PDB: 4F49;
DR  Pfam: PF16688;
DR  Pfam: PF16348;
DR  Pfam: PF01661;
DR  Pfam: PF09401;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF05409;
DR  Pfam: PF08715;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003968;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEP
SQ  SVMLQGFIVRANCNGVLEDFDLKIARTGRGAIYVDQYMCGADGKPVIEGDFKDYFGDEDIIEFEGEEYHCAWTTVRDEKP
SQ  LNQQTLFTIQEIQYNLDIPHKLPNCATRHVAPPVKKNSKIVLSEDYKKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRC
SQ  PCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDIKPGDAVVTSMSAGKGVKFFANCVLQYAGDVEGVSIWKVIKTFTVDE
SQ  TVCTPGFEGELNDFIKPESKSLVACSVKRAFITGDIDDAVHDCIITGKLDLSTNLFGNVGLLFKKTPWFVQKCGALFVDA
SQ  WKVVEELCGSLTLTYKQIYEVVASLCTSAFTIVNYKPTFVVPDNRVKDLVDKCVKVLVKAFDVFTQIITIAGIEAKCFVL
SQ  GAKYLLFNNALVKLVSVKILGKKQKGLECAFFATSLVGATVNVTPKRTETATISLNKVDDVVAPGEGYIVIVGDMAFYKS
SQ  GEYYFMMSSPNFVLTNNVFKAVKVPSYDIVYDVDNDTKSKMIAKLGSSFEYDGDIDAAIVKVNELLIEFRQQSLCFRAFK
SQ  DDKSIFVEAYFKKYKMPACLAKHIGLWNIIKKDSCKRGFLNLFNHLNELEDIKETNIQAIKNILCPDPLLDLDYGAIWYN
SQ  CMPGCSDPSVLGSVQLLIGNGVKVVCDGCKGFANQLSKGYNKLCNAARNDIEIGGIPFSTFKTPTNTFIEMTDAIYSVIE
SQ  QGKALSFRDADVPVVDNGTISTADWSEPILLEPAEYVKPKNNGNVIVIAGYTFYKDEDEHFYPYGFGKIVQRMYNKMGGG
SQ  DKTVSFSEEVDVQEIAPVTRVKLEFEFDNEIVTGVLERAIGTRYKFTGTTWEEFEESISEELDAIFDTLANQGVELEGYF
SQ  IYDTCGGFDIKNPDGIMISQYDINITADEKSEVSASSEEEEVESVEEDPENEIVEASEGAEGTSSQEEVETVEVADITST
SQ  EEDVDIVEVSAKDDPWAAAVDVQEAEQFNPSLPPFKTTNLNGKIILKQGDNNCWINACCYQLQAFDFFNNEAWEKFKKGD
SQ  VMDFVNLCYAATTLARGHSGDAEYLLELMLNDYSTAKIVLAAKCGCGEKEIVLERAVFKLTPLKESFNYGVCGDCMQVNT
SQ  CRFLSVEGSGVFVHDILSKQTPEAMFVVKPVMHAVYTGTTQNGHYMVDDIEHGYCVDGMGIKPLKKRCYTSTLFINANVM
SQ  TRAEKPKQEFKVEKVEQQPIVEENKSSIEKEEIQSPKNDDLILPFYKAGKLSFYQGALDVLINFLEPDVIVNAANGDLKH
SQ  MGGVARAIDVFTGGKLTERSKDYLKKNKSIAPGNAVFFENVIEHLSVLNAVGPRNGDSRVEAKLCNVYKAIAKCEGKILT
SQ  PLISVGIFNVRLETSLQCLLKTVNDRGLNVFVYTDQERQTIENFFSCSIPVNVTEDNVNHERVSVSFDKTYGEQLKGTVV
SQ  IKDKDVTNQLPSAFDVGQKVIKAIDIDWQAHYGFRDAAAFSASSHDAYKFEVVTHSNFIVHKQTDNNCWINAICLALQRL
SQ  KPQWKFPGVRGLWNEFLERKTQGFVHMLYHISGVKKGEPGDAELMLHKLGDLMDNDCEIIVTHTTACDKCAKVEKFVGPV
SQ  VAAPLAIHGTDETCVHGVSVNVKVTQIKGTVAITSLIGPIIGEVLEATGYICYSGSNRNGHYTYYDNRNGLVVDAEKAYH
SQ  FNRDLLQVTTAIASNFVVKKPQAEERPKNCAFNKVAASPKIVQEQKLLAIESGANYALTEFGRYADMFFMAGDKILRLLL
SQ  EVFKYLLVLFMCLRSTKMPKVKVKPPLAFKDFGAKVRTLNYMRQLNKPSVWRYAKLVLLLIAIYNFFYLFVSIPVVHKLT
SQ  CNGAVQAYKNSSFIKSAVCGNSILCKACLASYDELADFQHLQVTWDFKSDPLWNRLVQLSYFAFLAVFGNNYVRCFLMYF
SQ  VSQYLNLWLSYFGYVEYSWFLHVVNFESISAEFVIVVIVVKAVLALKHIVFACSNPSCKTCSRTARQTRIPIQVVVNGSM
SQ  KTVYVHANGTGKFCKKHNFYCKNCDSYGFENTFICDEIVRDLSNSVKQTVYATDRSHQEVTKVECSDGFYRFYVGDEFTS
SQ  YDYDVKHKKYSSQEVLKSMLLLDDFIVYSPSGSALANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVI
SQ  KNSFNVDVSECKNLDECYRACNLNVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIV
SQ  NAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVSPKSGSGFFDVITQLKQ
SQ  IVILVFVFIFICGLCSVYSVATQSYIESAEGYDYMVIKNGIVQPFDDTISCVHNTYKGFGDWFKAKYGFIPTFGKSCPIV
SQ  VGTVFDLENMRPIPDVPAYVSIVGRSLVFAINAAFGVTNMCYDHTGNAVSKDSYFDTCVFNTACTTLTGLGGTIVYCAKQ
SQ  GLVEGAKLYSDLMPDYYYEHASGNMVKLPAIIRGLGLRFVKTQATTYCRVGECIDSKAGFCFGGDNWFVYDNEFGNGYIC
SQ  GNSVLGFFKNVFKLFNSNMSVVATSGAMLVNIIIACLAIAMCYGVLKFKKIFGDCTFLIVMIIVTLVVNNVSYFVTQNTF
SQ  FMIIYAIVYYFITRKLAYPGILDAGFIIAYINMAPWYVITAYILVFLYDSLPSLFKLKVSTNLFEGDKFVGNFESAAMGT
SQ  FVIDMRSYETIVNSTSIARIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVNRTDMLYTPPTVSVNSTLQSG
SQ  LRKMAQPSGLVEPCIVRVSYGNNVLNGLWLGDEVICPRHVIASDTTRVINYENEMSSVRLHNFSVSKNNVFLGVVSARYK
SQ  GVNLVLKVNQVNPNTPEHKFKSIKAGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGILYFVYMH
SQ  HLELGNGSHVGSNFEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMSLESYNTWAKTNSFTELS
SQ  STDAFSMLAAKTGQSVEKLLDSIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQAGKVKSFFYPIMTAMTILFA
SQ  FWLEFFMYTPFTWINPTFVSIVLAVTTLISTVFVSGIKHKMLFFMSFVLPSVILVTAHNLFWDFSYYESLQSIVENTNTM
SQ  FLPVDMQGVMLTVFCFIVFVTYSVRFFTCKQSWFSLAVTTILVIFNMVKIFGTSDEPWTENQIAFCFVNMLTMIVSLTTK
SQ  DWMVVIASYRIAYYIVVCVMPSAFVSDFGFMKCISIVYMACGYLFCCYYGILYWVNRFTCMTCGVYQFTVSAAELKYMTA
SQ  NNLSAPKNAYDAMILSAKLIGVGGKRNIKISTVQSKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPE
SQ  IVLEKLLALIAFFLSKHNTCDLSELIESYFENTTILQSVASAYAALPSWIALEKARADLEEAKKNDVSPQILKQLTKAFN
SQ  IAKSDFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKLDMSSVNTIIDQARNGVLPLSIIPAA
SQ  SATRLVVITPSLEVFSKIRQENNVHYAGAIWTIVEVKDANGSHVHLKEVTAANELNLTWPLSITCERTTKLQNNEIMPGK
SQ  LKERAVRASATLDGEAFGSGKALMASESGKSFMYAFIASDNNLKYVKWESNNDIIPIELEAPLRFYVDGANGPEVKYLYF
SQ  VKNLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSSLLTLCAFSPDPAKAYVDAVKRGMQPVNNCVKMLSNGAGNGMAVTN
SQ  GVEANTQQDSYGGASVCIYCRCHVEHPAIDGLCRYKGKFVQIPTGTQDPIRFCIENEVCVVCGCWLNNGCMCDRTSMQSF
SQ  TVDQSYLNECGVLVQLD
//
ID  O75716;
PN  Serine/threonine-protein kinase 16;
GN  STK16;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
DR  UNIPROT: O75716;
DR  UNIPROT: A8K9H9;
DR  UNIPROT: Q5U0F8;
DR  UNIPROT: Q96KI2;
DR  UNIPROT: Q9BUH4;
DR  UNIPROT: Q9UEN3;
DR  UNIPROT: Q9UP78;
DR  PDB: 2BUJ;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 604719;
DR  DisGeNET: 8576;
DE  Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000269|PubMed:10364453}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-740019,EBI-749295; Score: 0.56
DE  Interaction: Q6UY14; IntAct: EBI-742002,EBI-749295; Score: 0.62
DE  Interaction: Q8IWZ5; IntAct: EBI-749295,EBI-5235829; Score: 0.72
DE  Interaction: P50222; IntAct: EBI-748397,EBI-749295; Score: 0.56
DE  Interaction: Q8IYX7; IntAct: EBI-749295,EBI-3957636; Score: 0.72
DE  Interaction: O43186; IntAct: EBI-748171,EBI-749295; Score: 0.56
DE  Interaction: O43597; IntAct: EBI-742487,EBI-749295; Score: 0.56
DE  Interaction: O43734; IntAct: EBI-749295,EBI-744798; Score: 0.56
DE  Interaction: O95967; IntAct: EBI-749295,EBI-743414; Score: 0.72
DE  Interaction: P12757; IntAct: EBI-2902468,EBI-749295; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-719493,EBI-749295; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-749295,EBI-533224; Score: 0.56
DE  Interaction: P49247; IntAct: EBI-749295,EBI-744831; Score: 0.67
DE  Interaction: P60370; IntAct: EBI-749295,EBI-10172150; Score: 0.56
DE  Interaction: P60409; IntAct: EBI-10172290,EBI-749295; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-749295,EBI-10171774; Score: 0.72
DE  Interaction: P60411; IntAct: EBI-749295,EBI-10172052; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-307352,EBI-749295; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-717810,EBI-749295; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-749295,EBI-6509505; Score: 0.72
DE  Interaction: Q13137; IntAct: EBI-739580,EBI-749295; Score: 0.56
DE  Interaction: Q13829; IntAct: EBI-2505861,EBI-749295; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-742327,EBI-749295; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-742948,EBI-749295; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-749295,EBI-2349927; Score: 0.56
DE  Interaction: Q5JXC2; IntAct: EBI-749295,EBI-2801965; Score: 0.67
DE  Interaction: Q6PEX3; IntAct: EBI-749295,EBI-3957672; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-749295,EBI-945833; Score: 0.56
DE  Interaction: Q8HWS3; IntAct: EBI-749295,EBI-746118; Score: 0.56
DE  Interaction: Q8N5Z5-2; IntAct: EBI-749295,EBI-10189368; Score: 0.56
DE  Interaction: Q8N5Z5; IntAct: EBI-743960,EBI-749295; Score: 0.78
DE  Interaction: Q92824; IntAct: EBI-751290,EBI-749295; Score: 0.56
DE  Interaction: Q96EY1-2; IntAct: EBI-749295,EBI-3952284; Score: 0.56
DE  Interaction: Q96Q35; IntAct: EBI-749295,EBI-750451; Score: 0.56
DE  Interaction: Q99081; IntAct: EBI-749295,EBI-722877; Score: 0.56
DE  Interaction: Q9BQ13; IntAct: EBI-749295,EBI-10189448; Score: 0.67
DE  Interaction: Q9GZT8; IntAct: EBI-749295,EBI-740897; Score: 0.56
DE  Interaction: Q9NRY6; IntAct: EBI-750734,EBI-749295; Score: 0.72
DE  Interaction: Q9UKT9; IntAct: EBI-749295,EBI-747204; Score: 0.56
DE  Interaction: Q9Y295; IntAct: EBI-749295,EBI-719554; Score: 0.56
DE  Interaction: Q8XC86; IntAct: EBI-749295,EBI-10038594; Score: 0.37
DE  Interaction: Q7DB77; IntAct: EBI-749295,EBI-6480811; Score: 0.51
DE  Interaction: B7UM99; IntAct: EBI-2504426,EBI-749295; Score: 0.37
DE  Interaction: Q9Y4P1-2; IntAct: EBI-749295,EBI-21856470; Score: 0.35
DE  Interaction: Q96GV9; IntAct: EBI-749295,EBI-2350695; Score: 0.35
DE  Interaction: Q8WVV4-1; IntAct: EBI-749295,EBI-11986735; Score: 0.35
DE  Interaction: Q6ZVX7; IntAct: EBI-749295,EBI-2877737; Score: 0.35
DE  Interaction: Q6BDS2; IntAct: EBI-749295,EBI-11028496; Score: 0.35
DE  Interaction: Q5QP82-2; IntAct: EBI-749295,EBI-10983996; Score: 0.35
DE  Interaction: Q3ZCM7; IntAct: EBI-749295,EBI-302558; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-749295,EBI-350989; Score: 0.35
DE  Interaction: P20930; IntAct: EBI-749295,EBI-1058782; Score: 0.35
DE  Interaction: Q96KN3; IntAct: EBI-2692890,EBI-749295; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-10251462,EBI-749295; Score: 0.56
DE  Interaction: Q9HB66; IntAct: EBI-1054754,EBI-749295; Score: 0.40
DE  Interaction: Q6P2I7; IntAct: EBI-1047027,EBI-749295; Score: 0.40
DE  Interaction: Q14680; IntAct: EBI-749295,EBI-1046702; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-749295,EBI-307369; Score: 0.40
DE  Interaction: P40337; IntAct: EBI-749295,EBI-301246; Score: 0.40
DE  Interaction: O75116; IntAct: EBI-749295,EBI-366288; Score: 0.40
DE  Interaction: P26441; IntAct: EBI-749295,EBI-1050897; Score: 0.40
DE  Interaction: Q96RG2; IntAct: EBI-749295,EBI-1042651; Score: 0.40
DE  Interaction: P63162; IntAct: EBI-749295,EBI-712493; Score: 0.40
DE  Interaction: Q93063; IntAct: EBI-749295,EBI-1047761; Score: 0.40
DE  Interaction: P41235; IntAct: EBI-749295,EBI-1049011; Score: 0.40
DE  Interaction: Q15583; IntAct: EBI-749295,EBI-714215; Score: 0.40
DE  Interaction: Q05084; IntAct: EBI-749295,EBI-1046751; Score: 0.40
DE  Interaction: Q9NRH2; IntAct: EBI-1053132,EBI-749295; Score: 0.40
DE  Interaction: Q13185; IntAct: EBI-78176,EBI-749295; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-3867333,EBI-749295; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-22310682,EBI-749295; Score: 0.56
DE  Interaction: Q7Z3K6-2; IntAct: EBI-12224671,EBI-749295; Score: 0.56
DE  Interaction: Q70EL1-9; IntAct: EBI-11975223,EBI-749295; Score: 0.56
DE  Interaction: Q9BQ13-2; IntAct: EBI-12278688,EBI-749295; Score: 0.56
DE  Interaction: Q04864-2; IntAct: EBI-10829018,EBI-749295; Score: 0.56
DE  Interaction: Q07627; IntAct: EBI-11959885,EBI-749295; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-11953846,EBI-749295; Score: 0.56
DE  Interaction: O14508; IntAct: EBI-617737,EBI-749295; Score: 0.56
DE  Interaction: Q9Y3S2; IntAct: EBI-749295,EBI-373456; Score: 0.56
DE  Interaction: Q93015-2; IntAct: EBI-749295,EBI-12126220; Score: 0.56
DE  Interaction: Q06546; IntAct: EBI-749295,EBI-638925; Score: 0.56
DE  Interaction: Q9NQX0; IntAct: EBI-11320284,EBI-749295; Score: 0.56
DE  Interaction: Q7RTU4; IntAct: EBI-17508719,EBI-749295; Score: 0.56
DE  Interaction: Q6P1L6; IntAct: EBI-10252492,EBI-749295; Score: 0.56
DE  Interaction: Q9BS75; IntAct: EBI-10693436,EBI-749295; Score: 0.56
DE  Interaction: P27918; IntAct: EBI-9038570,EBI-749295; Score: 0.56
DE  Interaction: Q9Y6H3; IntAct: EBI-12811889,EBI-749295; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-948001,EBI-749295; Score: 0.56
DE  Interaction: Q5T749; IntAct: EBI-10981970,EBI-749295; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-712648,EBI-749295; Score: 0.56
DE  Interaction: Q6UY14-3; IntAct: EBI-10173507,EBI-749295; Score: 0.56
DE  Interaction: P51114-2; IntAct: EBI-11022345,EBI-749295; Score: 0.56
DE  Interaction: Q2I0M5; IntAct: EBI-12821217,EBI-749295; Score: 0.56
DE  Interaction: P31321; IntAct: EBI-2805516,EBI-749295; Score: 0.56
DE  Interaction: A8MUP2; IntAct: EBI-749295,EBI-12842046; Score: 0.56
DE  Interaction: O15496; IntAct: EBI-726466,EBI-749295; Score: 0.56
DE  Interaction: Q96D03; IntAct: EBI-742054,EBI-749295; Score: 0.56
DE  Interaction: A0A087WVE9; IntAct: EBI-12808086,EBI-749295; Score: 0.56
DE  Interaction: Q8IUC1; IntAct: EBI-1052037,EBI-749295; Score: 0.56
DE  Interaction: Q03431; IntAct: EBI-2860297,EBI-749295; Score: 0.56
DE  Interaction: O43559; IntAct: EBI-725515,EBI-749295; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005798;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004715;
GO  GO:0004674;
GO  GO:0000978;
GO  GO:0071560;
GO  GO:0045944;
GO  GO:0046777;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:10364453};
SQ  MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRL
SQ  VAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG
SQ  QPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ
SQ  KGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
//
ID  O18158;
PN  UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase;
GN  ogt;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9083068}.
DR  UNIPROT: O18158;
DR  UNIPROT: Q21232;
DR  Pfam: PF13844;
DR  Pfam: PF00515;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. {ECO:0000250|UniProtKB:O15294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17446; IntAct: EBI-313084,EBI-312987; Score: 0.37
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016262;
GO  GO:0097363;
GO  GO:0004722;
GO  GO:0040024;
GO  GO:0006112;
GO  GO:0005977;
GO  GO:0009100;
GO  GO:0019915;
GO  GO:0006470;
GO  GO:0006493;
GO  GO:0000003;
GO  GO:0009266;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAV
SQ  NQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLP
SQ  TLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSG
SQ  GDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEK
SQ  AVTLDPNFLDAYINLGNVLKEARIFDRAVSAYLRALNLSGNHAVVHGNLACVYYEQGLIDLAIDTYKKAIDLQPHFPDAY
SQ  CNLANALKEKGSVVEAEQMYMKALELCPTHADSQNNLANIKREQGKIEDATRLYLKALEIYPEFAAAHSNLASILQQQGK
SQ  LNDAILHYKEAIRIAPTFADAYSNMGNTLKEMGDSSAAIACYNRAIQINPAFADAHSNLASIHKDAGNMAEAIQSYSTAL
SQ  KLKPDFPDAYCNLAHCHQIICDWNDYDKRVRKLVQIVEDQLCKKRLPSVHPHHSMLYPLSHAARIAIAAKHASLCFDKVH
SQ  VQMLGKTPLIHADRFSVQNGQRLRIGYVSSDFGNHPTSHLMQSIPGMHDRSRVEVFCYALSVNDGTNFRSKLMNESEHFV
SQ  DLSQIPCNGKAAEKIAQDGIHILINMNGYTKGARNEIFALRPAPIQVMWLGYPSTSGATFMDYIITDAVTSPLRLANAFT
SQ  EKLAYMPHTFFIGDHAQMLRHLTDKVVVKDKETTERDSCLIMNTANMDPILAKSEIKEQVLDTEVVSGPNKELVRAEMVL
SQ  PVLEVPTEPIKQMIMTGQMTMNVMEDMNVQNGLGQSQMHHKAATGEEIPNSVLLTSRAQYQLPDDAIVFCNFNQLYKIDP
SQ  STLDMWIKILENVPKSILWLLRFPYQGEEHIRKYCVERGLDPSRIVFSNVAAKEEHVRRGQLADVCLDTPLCNGHTTGMD
SQ  ILWTGTPMVTMPLESLASRVATSQLYALGVPELVAKTRQEYVSIAVRLGTDADHLANMRAKVWMARTSSTLFDVKQYCHD
SQ  MEDLLGQMWKRYESGMPIDHITNNTETPHGL
//
ID  E7F4N7;
PN  Stimulator of interferon genes protein;
GN  sting1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23091644}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase tbk1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: E7F4N7;
DR  UNIPROT: K4Q6R6;
DR  PDB: 6MYD;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:23091644). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:23091644). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and irf3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842662). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30842662). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation. Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:23091644, ECO:0000269|PubMed:30842662}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0035438;
GO  GO:0061507;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0039528;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0038061;
GO  GO:0002230;
GO  GO:0016239;
GO  GO:0032481;
GO  GO:0010506;
GO  GO:0009615;
GO  GO:0061709;
GO  GO:0032606;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRM
SQ  SEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSF
SQ  YIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKIT
SQ  HNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSREL
SQ  FQNLKQQDGEIFMDPTNEVHPVPEEGPVGNCNGALQATFHEEPMSDEPTLMFSRPQSLRSEPVETTDYFNPSSAMKQN
//
ID  O40955;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  11044;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: O40955;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006396;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWGAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAEHRALRCREWDFEVLRARADTAAAPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQSAAT
SQ  SSPPGDPPPPRCARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPVPPTSAGPADRARDAELEVAYEPSGPPTST
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWARVACPLLGAGVYGWSAAESLRAALAATRTEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGVPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPRCAYGRALSEARTHKDFAALSQRW
SQ  SASHADASSDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIEIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  P05769;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  301478;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P05769;
DR  UNIPROT: Q9Q9F7;
DR  PDB: 2PX2;
DR  PDB: 2PX4;
DR  PDB: 2PX5;
DR  PDB: 2PX8;
DR  PDB: 2PXA;
DR  PDB: 2PXC;
DR  PDB: 2V8O;
DR  PDB: 2WV9;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860, ECO:0000269|PubMed:19793813}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKH
SQ  LTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCW
SQ  IRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDST
SQ  KATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGD
SQ  SCITIMAADKPTLDIRMMNIEATNLALVRNYCYAATVSDVSTVSNCPTTGESHNTKRADHNYLCKRGVTDRGWGNGCGLF
SQ  GKGSIDTCAKFTCSNSAAGRLILPEDIKYEVGVFVHGSTDSTSHGNYSTQIGANQAVRFTISPNAPAITAKMGDYGEVTV
SQ  ECEPRSGLNTEAYYVMTIGTKHFLVHREWFNDLLLPWTSPASTEWRNREILVEFEEPHATKQSVVALGSQEGALHQALAG
SQ  AIPVEFSSSTLKLTSGHLKCRVKMEKLKLKGTTYGMCTEKFTFSKNPADTGHGTVVLELQYTGSDGPCKIPISSVASLND
SQ  MTPVGRMVTANPYVASSTANAKVLVEIEPPFGDSYIVVGRGDKQINHHWHKEGSSIGKAFSTTLKGAQRLAALGDTAWDF
SQ  GSVGGVFNSIGKAVHQVFGGAFRTLFGGMSWISPGLLGALLLWMGVNARDKSIALAFLATGGVLLFLATNVHADTGCAID
SQ  ITRRELKCGSGIFIHNDVEAWIDRYKYLPETPKQLAKVVENAHKSGICGIRSVNRFEHQMWESVRDELNALLKENAIDLS
SQ  VVVEKQKGMYRAAPNRLRLTVEELDIGWKAWGKSLLFAAELANSTFVVDGPETAECPNSKRAWNSFEIEDFGFGITSTRG
SQ  WLKLREENTSECDSTIIGTAVKGNHAVHSDLSYWIESGLNGTWKLERAIFGEVKSCTWPETHTLWGDAVEETELIIPVTL
SQ  AGPRSKHNRREGYKVQVQGPWDEEDIKLDFDYCPGTTVTVSEHCGKRGPSVRTTTDSGKLVTDWCCRSCTLPPLRFTTAS
SQ  GCWYGMEIRPMKHDESTLVKSRVQAFNGDMIDPFQLGLLVMFLATQEVLRKRWTARLTLPAAVGALLVLLLGGITYTDLV
SQ  RYLILVGSAFAESNNGGDVIHLALIAVFKVQPAFLVASLTRSRWTNQENLVLVLGAAFFQMAASDLELTIPGLLNSAATA
SQ  WMVLRAMAFPSTSAIAMPMLAMLAPGMRMLHLDTYRIVLLLIGICSLLNERRRSVEKKKGAVLIGLALTSTGYFSPTIMA
SQ  AGLMICNPNKKRGWPATEVLTAVGLMFAIVGGLAELDIDSMSVPFTIAGLMLVSYVISGKATDMWLERAADVSWEAGAAI
SQ  TGTSERLDVQLDDDGDFHLLNDPGVPWKIWVLRMTCLSVAAITPRAILPSAFGYWLTLKYTKRGGVFWDTPSPKVYPKGD
SQ  TTPGVYRIMARGILGRYQAGVGVMHEGVFHTLWHTTRGAAIMSGEGRLTPYWGNVKEDRVTYGGPWKLDQKWNGVDDVQM
SQ  IVVEPGKPAINVQTKPGIFKTAHGEIGAVSLDYPIGTSGSPIVNSNGEIIGLYGNGVILGNGAYVSAIVQGERVEEPVPE
SQ  AYNPEMLKKRQLTVLDLHPGAGKTRRILPQIIKDAIQKRLRTAVLAPTRVVAAEMAEALRGLPVRYLTPAVQREHSGNEI
SQ  VDVMCHATLTHRLMSPLRVPNYNLFVMDEAHFTDPASIAARGYIATRVEAGEAAAIFMTATPPGTSDPFPDTNSPVHDVS
SQ  SEIPDRAWSSGFEWITDYAGKTVWFVASVKMSNEIAQCLQRAGKRVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGAN
SQ  FGASRVIDCRKSVKPTILDEGEGRVILSVPSAITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTMLAHWTEAKILLD
SQ  NIHLPNGLVAQLYGPERDKTYTMDGEYRLRGEERKTFLELIKTADLPVWLAYKVASNGIQYNDRKWCFDGPRSNIILEDN
SQ  NEVEIITRIGERKVLKPRWLDARVYSDHQSLKWFKDFAAGKRSAIGFFEVLGRMPEHFAGKTREALDTMYLVATSEKGGK
SQ  AHRMALEELPDALETITLIAALGVMTAGFFLLMMQRKGIGKLGLGALVLVVATFFLWMSDVSGTKIAGVLLLALLMMVVL
SQ  IPEPEKQRSQTDNQLAVFLICVLLVVGLVAANEYGMLERTKTDIRNLFGKSLIEENEVHIPPFDFFTLDLKPATAWALYG
SQ  GSTVVLTPLIKHLVTSQYVTTSLASINAQAGSLFTLPKGIPFTDFDLSVALVFLGCWGQVTLTTLIMATILVTLHYGYLL
SQ  PGWQAEALRAAQKRTAAGIMKNAVVDGIVATDVPELERTTPQMQKRLGQILLVLASVAAVCVNPRITTIREAGILCTAAA
SQ  LTLWDNNASAAWNSTTATGLCHVMRGSWIAGASIAWTLIKNAEKPAFKRGRAGGRTLGEQWKEKLNAMGKEEFFSYRKEA
SQ  ILEVDRTEARRARREGNKVGGHPVSRGTAKLRWLVERRFVQPIGKVVDLGCGRGGWSYYAATMKNVQEVRGYTKGGPGHE
SQ  EPMLMQSYGWNIVTMKSGVDVFYKPSEISDTLLCDIGESSPSAEIEEQRTLRILEMVSDWLSRGPKEFCIKILCPYMPKV
SQ  IEKLESLQRRFGGGLVRVPLSRNSNHEMYWVSGASGNIVHAVNMTSQVLIGRMDKKIWKGPKYEEDVNLGSGTRAVGKGV
SQ  QHTDYKRIKSRIEKLKEEYAATWHTDDNHPYRTWTYHGSYEVKPSGSASTLVNGVVRLLSKPWDAITGVTTMAMTDTTPF
SQ  GQQRVFKEKVDTKAPEPPQGVKTVMDETTNWLWAYLARNKKARLCTREEFVKKVNSHAALGAMFEEQNQWKNAREAVEDP
SQ  KFWEMVDEERECHLRGECRTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWMSRENSGGGVEG
SQ  AGIQKLGYILRDVAQKPGGKIYADDTAGWDTRITQADLENEAKVLELMEGEQRTLARAIIELTYRHKVVKVMRPAAGGKT
SQ  VMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEAVIGPDDIESIERKKKFAVRTWLFENAEERVQRMAVSGDDCV
SQ  VKPLDDRFSTALHFLNAMSKVRKDIQEWKPSQGWYDWQQVPFCSNHFQEVIMKDGRTLVVPCRGQDELIGRARISPGSGW
SQ  NVRDTACLAKAYAQMWLVLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWILENEWMED
SQ  KTTVSDWTEVPYVGKREDIWCGSLIGTRTRATWAENIYAAINQVRSVIGKEKYVDYVQSLRRYEETHVSEDRVL
//
ID  P01112;
PN  GTPase HRas, N-terminally processed;
GN  HRAS;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}. [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
DR  UNIPROT: P01112;
DR  UNIPROT: B5BUA0;
DR  UNIPROT: Q14080;
DR  UNIPROT: Q6FHV9;
DR  UNIPROT: Q9BR65;
DR  UNIPROT: Q9UCE2;
DR  PDB: 121P;
DR  PDB: 1AA9;
DR  PDB: 1AGP;
DR  PDB: 1BKD;
DR  PDB: 1CLU;
DR  PDB: 1CRP;
DR  PDB: 1CRQ;
DR  PDB: 1CRR;
DR  PDB: 1CTQ;
DR  PDB: 1GNP;
DR  PDB: 1GNQ;
DR  PDB: 1GNR;
DR  PDB: 1HE8;
DR  PDB: 1IAQ;
DR  PDB: 1IOZ;
DR  PDB: 1JAH;
DR  PDB: 1JAI;
DR  PDB: 1K8R;
DR  PDB: 1LF0;
DR  PDB: 1LF5;
DR  PDB: 1LFD;
DR  PDB: 1NVU;
DR  PDB: 1NVV;
DR  PDB: 1NVW;
DR  PDB: 1NVX;
DR  PDB: 1P2S;
DR  PDB: 1P2T;
DR  PDB: 1P2U;
DR  PDB: 1P2V;
DR  PDB: 1PLJ;
DR  PDB: 1PLK;
DR  PDB: 1PLL;
DR  PDB: 1Q21;
DR  PDB: 1QRA;
DR  PDB: 1RVD;
DR  PDB: 1WQ1;
DR  PDB: 1XCM;
DR  PDB: 1XD2;
DR  PDB: 1XJ0;
DR  PDB: 1ZVQ;
DR  PDB: 1ZW6;
DR  PDB: 221P;
DR  PDB: 2C5L;
DR  PDB: 2CE2;
DR  PDB: 2CL0;
DR  PDB: 2CL6;
DR  PDB: 2CL7;
DR  PDB: 2CLC;
DR  PDB: 2CLD;
DR  PDB: 2EVW;
DR  PDB: 2GDP;
DR  PDB: 2LCF;
DR  PDB: 2LWI;
DR  PDB: 2N42;
DR  PDB: 2N46;
DR  PDB: 2Q21;
DR  PDB: 2QUZ;
DR  PDB: 2RGA;
DR  PDB: 2RGB;
DR  PDB: 2RGC;
DR  PDB: 2RGD;
DR  PDB: 2RGE;
DR  PDB: 2RGG;
DR  PDB: 2UZI;
DR  PDB: 2VH5;
DR  PDB: 2X1V;
DR  PDB: 3DDC;
DR  PDB: 3I3S;
DR  PDB: 3K8Y;
DR  PDB: 3K9L;
DR  PDB: 3K9N;
DR  PDB: 3KKM;
DR  PDB: 3KKN;
DR  PDB: 3KUD;
DR  PDB: 3L8Y;
DR  PDB: 3L8Z;
DR  PDB: 3LBH;
DR  PDB: 3LBI;
DR  PDB: 3LBN;
DR  PDB: 3LO5;
DR  PDB: 3OIU;
DR  PDB: 3OIV;
DR  PDB: 3OIW;
DR  PDB: 3RRY;
DR  PDB: 3RRZ;
DR  PDB: 3RS0;
DR  PDB: 3RS2;
DR  PDB: 3RS3;
DR  PDB: 3RS4;
DR  PDB: 3RS5;
DR  PDB: 3RS7;
DR  PDB: 3RSL;
DR  PDB: 3RSO;
DR  PDB: 3TGP;
DR  PDB: 421P;
DR  PDB: 4DLR;
DR  PDB: 4DLS;
DR  PDB: 4DLT;
DR  PDB: 4DLU;
DR  PDB: 4DLV;
DR  PDB: 4DLW;
DR  PDB: 4DLX;
DR  PDB: 4DLY;
DR  PDB: 4DLZ;
DR  PDB: 4DST;
DR  PDB: 4DSU;
DR  PDB: 4EFL;
DR  PDB: 4EFM;
DR  PDB: 4EFN;
DR  PDB: 4G0N;
DR  PDB: 4G3X;
DR  PDB: 4K81;
DR  PDB: 4L9S;
DR  PDB: 4L9W;
DR  PDB: 4NYI;
DR  PDB: 4NYJ;
DR  PDB: 4NYM;
DR  PDB: 4Q21;
DR  PDB: 4RSG;
DR  PDB: 4URU;
DR  PDB: 4URV;
DR  PDB: 4URW;
DR  PDB: 4URX;
DR  PDB: 4URY;
DR  PDB: 4URZ;
DR  PDB: 4US0;
DR  PDB: 4US1;
DR  PDB: 4US2;
DR  PDB: 4XVQ;
DR  PDB: 4XVR;
DR  PDB: 521P;
DR  PDB: 5B2Z;
DR  PDB: 5B30;
DR  PDB: 5E95;
DR  PDB: 5P21;
DR  PDB: 5VBE;
DR  PDB: 5VBZ;
DR  PDB: 5WDO;
DR  PDB: 5WDP;
DR  PDB: 5WDQ;
DR  PDB: 5WFO;
DR  PDB: 5WFP;
DR  PDB: 5WFQ;
DR  PDB: 5WFR;
DR  PDB: 5WPL;
DR  PDB: 5X9S;
DR  PDB: 5ZC6;
DR  PDB: 621P;
DR  PDB: 6AMB;
DR  PDB: 6AXG;
DR  PDB: 6BVI;
DR  PDB: 6BVJ;
DR  PDB: 6BVK;
DR  PDB: 6BVL;
DR  PDB: 6BVM;
DR  PDB: 6CUO;
DR  PDB: 6CUP;
DR  PDB: 6CUR;
DR  PDB: 6D55;
DR  PDB: 6D56;
DR  PDB: 6D59;
DR  PDB: 6D5E;
DR  PDB: 6D5G;
DR  PDB: 6D5H;
DR  PDB: 6D5J;
DR  PDB: 6D5L;
DR  PDB: 6D5M;
DR  PDB: 6D5V;
DR  PDB: 6D5W;
DR  PDB: 6DZH;
DR  PDB: 6E6C;
DR  PDB: 6E6P;
DR  PDB: 6Q21;
DR  PDB: 721P;
DR  PDB: 821P;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DR  OMIM: 109800;
DR  OMIM: 163200;
DR  OMIM: 188470;
DR  OMIM: 190020;
DR  OMIM: 218040;
DR  DisGeNET: 3265;
DE  Function: Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:22821884, ECO:0000269|PubMed:9020151}.
DE  Disease: Costello syndrome (CSTLO) [MIM:218040]: A rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities. {ECO:0000269|PubMed:16170316, ECO:0000269|PubMed:16329078, ECO:0000269|PubMed:16443854, ECO:0000269|PubMed:17054105, ECO:0000269|PubMed:18039947, ECO:0000269|PubMed:18247425, ECO:0000269|PubMed:19995790}. Note=The disease is caused by mutations affecting the gene represented in this entry. Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome. {ECO:0000269|PubMed:17412879}. Note=The disease is caused by mutations affecting the gene represented in this entry. Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12727991}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Note=Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors. {ECO:0000269|PubMed:3670300}. Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. {ECO:0000269|PubMed:6298635, ECO:0000269|PubMed:6844927}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:22683711}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P42337; IntAct: EBI-641748,EBI-350145; Score: 0.59
DE  Interaction: P27986; IntAct: EBI-79464,EBI-350145; Score: 0.40
DE  Interaction: Q12967; IntAct: EBI-350145,EBI-365861; Score: 0.70
DE  Interaction: O15211; IntAct: EBI-350145,EBI-712355; Score: 0.37
DE  Interaction: Q9NZL6; IntAct: EBI-350145,EBI-365926; Score: 0.67
DE  Interaction: Q8WWW0-2; IntAct: EBI-960502,EBI-350145; Score: 0.37
DE  Interaction: Q9NT62-2; IntAct: EBI-21549195,EBI-350145; Score: 0.35
DE  Interaction: Q96SQ9-2; IntAct: EBI-21537560,EBI-350145; Score: 0.35
DE  Interaction: P18827; IntAct: EBI-2855248,EBI-350145; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-365996,EBI-350145; Score: 0.97
DE  Interaction: P05783; IntAct: EBI-297888,EBI-350145; Score: 0.37
DE  Interaction: P42684; IntAct: EBI-1102694,EBI-350145; Score: 0.46
DE  Interaction: Q13671; IntAct: EBI-350145,EBI-366017; Score: 0.75
DE  Interaction: Q03385; IntAct: EBI-923705,EBI-350145; Score: 0.37
DE  Interaction: Q13671-1; IntAct: EBI-366030,EBI-350145; Score: 0.61
DE  Interaction: Q9EQZ6; IntAct: EBI-772212,EBI-350145; Score: 0.56
DE  Interaction: Q9UQ13; IntAct: EBI-993879,EBI-350145; Score: 0.35
DE  Interaction: P20936; IntAct: EBI-1026476,EBI-350145; Score: 0.44
DE  Interaction: Q03386; IntAct: EBI-1026899,EBI-350145; Score: 0.44
DE  Interaction: Q07889; IntAct: EBI-297487,EBI-350145; Score: 0.94
DE  Interaction: P21359; IntAct: EBI-1172917,EBI-350145; Score: 0.50
DE  Interaction: Q86Z23; IntAct: EBI-12062109,EBI-350145; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-3893317,EBI-350145; Score: 0.35
DE  Interaction: P08678; IntAct: EBI-5364,EBI-350145; Score: 0.44
DE  Interaction: Q13503; IntAct: EBI-394678,EBI-350145; Score: 0.35
DE  Interaction: P53611; IntAct: EBI-536715,EBI-350145; Score: 0.35
DE  Interaction: Q53EQ6; IntAct: EBI-10748977,EBI-350145; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587304,EBI-350145; Score: 0.35
DE  Interaction: Q16288-2; IntAct: EBI-21583219,EBI-350145; Score: 0.35
DE  Interaction: Q6PEY0; IntAct: EBI-21551278,EBI-350145; Score: 0.35
DE  Interaction: P26842; IntAct: EBI-520729,EBI-350145; Score: 0.35
DE  Interaction: P21453; IntAct: EBI-2681920,EBI-350145; Score: 0.35
DE  Interaction: Q9NRW4-2; IntAct: EBI-21542510,EBI-350145; Score: 0.35
DE  Interaction: Q8TBF2; IntAct: EBI-7280826,EBI-350145; Score: 0.35
DE  Interaction: O00141; IntAct: EBI-1042854,EBI-350145; Score: 0.35
DE  Interaction: O95620-2; IntAct: EBI-21824577,EBI-350145; Score: 0.35
DE  Interaction: P13995; IntAct: EBI-1058895,EBI-350145; Score: 0.35
DE  Interaction: P15056; IntAct: EBI-365980,EBI-350145; Score: 0.78
DE  Interaction: P54277; IntAct: EBI-2893308,EBI-350145; Score: 0.35
DE  Interaction: Q0VAA5; IntAct: EBI-350145,EBI-21824821; Score: 0.40
DE  Interaction: Q15392; IntAct: EBI-5457558,EBI-350145; Score: 0.35
DE  Interaction: Q16850; IntAct: EBI-2680495,EBI-350145; Score: 0.35
DE  Interaction: Q9H0R4-2; IntAct: EBI-21692182,EBI-350145; Score: 0.35
DE  Interaction: Q9Y277-2; IntAct: EBI-21506455,EBI-350145; Score: 0.35
DE  Interaction: Q8WTQ1; IntAct: EBI-21825134,EBI-350145; Score: 0.35
DE  Interaction: Q9UN70; IntAct: EBI-2681692,EBI-350145; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757569,EBI-350145; Score: 0.35
DE  Interaction: O14880; IntAct: EBI-724754,EBI-350145; Score: 0.35
DE  Interaction: Q04631; IntAct: EBI-602447,EBI-350145; Score: 0.40
DE  Interaction: Q7Z569; IntAct: EBI-350145,EBI-349900; Score: 0.52
DE  Interaction: Q9Z0S9; IntAct: EBI-476965,EBI-350145; Score: 0.51
DE  Interaction: P10398; IntAct: EBI-350145,EBI-365961; Score: 0.67
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008022;
GO  GO:0044877;
GO  GO:0009887;
GO  GO:0007050;
GO  GO:0007166;
GO  GO:0071480;
GO  GO:0090398;
GO  GO:0006935;
GO  GO:0042832;
GO  GO:0006897;
GO  GO:0048013;
GO  GO:0097193;
GO  GO:0001889;
GO  GO:0000165;
GO  GO:0007093;
GO  GO:0008285;
GO  GO:0010629;
GO  GO:0034260;
GO  GO:0043524;
GO  GO:2000251;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0045740;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:0032729;
GO  GO:0046330;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:2000630;
GO  GO:0010863;
GO  GO:0001934;
GO  GO:0090314;
GO  GO:0046579;
GO  GO:1900029;
GO  GO:0045944;
GO  GO:0090303;
GO  GO:0007265;
GO  GO:0048169;
GO  GO:0098696;
GO  GO:0035900;
GO  GO:0007165;
GO  GO:0002223;
GO  GO:0050852;
GO  GO:0042088;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8626715};
SQ  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
SQ  VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV
SQ  REIRQHKLRKLNPPDESGPGCMSCKCVLS
//
ID  Q6AZZ1;
PN  E3 ubiquitin-protein ligase TRIM68;
GN  TRIM68;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Colocalized with AR in nucleus.
DR  UNIPROT: Q6AZZ1;
DR  UNIPROT: A6NI19;
DR  UNIPROT: A8K551;
DR  UNIPROT: B3KPM5;
DR  UNIPROT: B4DVK4;
DR  UNIPROT: Q8WZ70;
DR  UNIPROT: Q96LE5;
DR  UNIPROT: Q96PF7;
DR  UNIPROT: Q9H9C2;
DR  UNIPROT: Q9NW18;
DR  Pfam: PF13765;
DR  Pfam: PF00622;
DR  Pfam: PF00643;
DR  PROSITE: PS50188;
DR  PROSITE: PS50119;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  OMIM: 613184;
DR  DisGeNET: 55128;
DE  Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000269|PubMed:18451177}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-2130449,EBI-2130449; Score: 0.56
DE  Interaction: Q5VVX9; IntAct: EBI-2130449,EBI-2130181; Score: 0.37
DE  Interaction: O76076; IntAct: EBI-2850068,EBI-2130449; Score: 0.35
DE  Interaction: P29279; IntAct: EBI-2835375,EBI-2130449; Score: 0.35
DE  Interaction: Q8IV31; IntAct: EBI-7238458,EBI-2130449; Score: 0.35
DE  Interaction: O95081; IntAct: EBI-2847286,EBI-2130449; Score: 0.35
DE  Interaction: Q99954; IntAct: EBI-12067698,EBI-2130449; Score: 0.35
DE  Interaction: Q9BWP8-4; IntAct: EBI-21848899,EBI-2130449; Score: 0.35
DE  Interaction: P49765-2; IntAct: EBI-21717775,EBI-2130449; Score: 0.35
DE  Interaction: P51888; IntAct: EBI-2827057,EBI-2130449; Score: 0.35
DE  Interaction: Q9H7T9; IntAct: EBI-2130449,EBI-10693257; Score: 0.40
DE  Interaction: Q9H239; IntAct: EBI-2130449,EBI-20858485; Score: 0.40
DE  Interaction: Q96BZ8; IntAct: EBI-726510,EBI-2130449; Score: 0.35
DE  Interaction: Q7RTY5; IntAct: EBI-2130449,EBI-21891692; Score: 0.40
DE  Interaction: Q5TGY3; IntAct: EBI-948813,EBI-2130449; Score: 0.35
DE  Interaction: P34130; IntAct: EBI-2130449,EBI-3907456; Score: 0.40
DE  Interaction: O95561; IntAct: EBI-10191951,EBI-2130449; Score: 0.35
DE  Interaction: O14494-2; IntAct: EBI-2130449,EBI-21891618; Score: 0.40
DE  Interaction: Q9NQ48; IntAct: EBI-2824799,EBI-2130449; Score: 0.56
DE  Interaction: P15884-3; IntAct: EBI-13636688,EBI-2130449; Score: 0.56
DE  Interaction: Q9NRI5-2; IntAct: EBI-11988027,EBI-2130449; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-11139477,EBI-2130449; Score: 0.56
DE  Interaction: P62487; IntAct: EBI-347928,EBI-2130449; Score: 0.56
DE  Interaction: Q9BRJ7; IntAct: EBI-2949792,EBI-2130449; Score: 0.56
DE  Interaction: Q04864-2; IntAct: EBI-10829018,EBI-2130449; Score: 0.56
DE  Interaction: Q3SY46; IntAct: EBI-10241252,EBI-2130449; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-6509505,EBI-2130449; Score: 0.56
DE  Interaction: B2RXF5; IntAct: EBI-12287587,EBI-2130449; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-11953846,EBI-2130449; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-739832,EBI-2130449; Score: 0.56
DE  Interaction: B9A064; IntAct: EBI-6677229,EBI-2130449; Score: 0.35
DE  Interaction: Q8N0V5; IntAct: EBI-21492685,EBI-2130449; Score: 0.35
DE  Interaction: P01148; IntAct: EBI-21753351,EBI-2130449; Score: 0.35
DE  Interaction: P13284; IntAct: EBI-2868897,EBI-2130449; Score: 0.35
DE  Interaction: O75791; IntAct: EBI-740418,EBI-2130449; Score: 0.35
DE  Interaction: C9JJ79; IntAct: EBI-12117156,EBI-2130449; Score: 0.35
DE  Interaction: Q13227; IntAct: EBI-713355,EBI-2130449; Score: 0.35
DE  Interaction: Q9Y215-2; IntAct: EBI-21671462,EBI-2130449; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0050681;
GO  GO:0035035;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0060333;
GO  GO:0051865;
GO  GO:0060765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVE
SQ  KVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAW
SQ  KLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQV
SQ  LWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSE
SQ  DRKRVHYGDTNQKLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCKQNVDRKEVVYLSPHYGFWVIRLRK
SQ  GNEYRAGTDEYPILSLPVPPRRVGIFVDYEAHDISFYNVTDCGSHIFTFPRYPFPGRLLPYFSPCYSIGTNNTAPLAICS
SQ  LDGED
//
ID  Q9LR44;
PN  UDP-glycosyltransferase 75B1;
GN  UGT75B1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11283335}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:11283335}. Note=During interphase, distributed in a punctate pattern in the perinuclear region. Localized in the forming cell plate during cytokinesis.
DR  UNIPROT: Q9LR44;
DR  Pfam: PF00201;
DR  PROSITE: PS00375;
DE  Function: Possesses low catalytic activity on indole-3-acetic acid (IAA) in vitro. May transfer UDP-glucose from sucrose synthase to callose synthase for the synthesis of callose at the forming cell plate during cytokinesis. Has high affinity for 4-aminobenzoate. Catalyzes the formation of 4-aminobenzoate glucose ester which represents a storage form of 4-aminobenzoate in the vacuole. Is the major source of this activity in the plant. Also active in vitro on benzoates and benzoate derivatives. {ECO:0000269|PubMed:11042207, ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:18385129}.
DE  Reference Proteome: Yes;
DE  Interaction: Q39821; IntAct: EBI-1765815,EBI-1765823; Score: 0.53
DE  Interaction: P92978; IntAct: EBI-1553104,EBI-1765823; Score: 0.44
DE  Interaction: Q9AUE0; IntAct: EBI-1765999,EBI-1765823; Score: 0.37
GO  GO:0005856;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0047215;
GO  GO:0080043;
GO  GO:0080044;
GO  GO:0080002;
GO  GO:0035251;
GO  GO:0008194;
GO  GO:0046482;
GO  GO:0009751;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPPHFLLVTFPAQGHVNPSLRFARRLIKRTGARVTFVTCVSVFHNSMIANHNKVENLSFLTFSDGFDDGGISTYEDRQK
SQ  RSVNLKVNGDKALSDFIEATKNGDSPVTCLIYTILLNWAPKVARRFQLPSALLWIQPALVFNIYYTHFMGNKSVFELPNL
SQ  SSLEIRDLPSFLTPSNTNKGAYDAFQEMMEFLIKETKPKILINTFDSLEPEALTAFPNIDMVAVGPLLPTEIFSGSTNKS
SQ  VKDQSSSYTLWLDSKTESSVIYVSFGTMVELSKKQIEELARALIEGKRPFLWVITDKSNRETKTEGEEETEIEKIAGFRH
SQ  ELEEVGMIVSWCSQIEVLSHRAVGCFVTHCGWSSTLESLVLGVPVVAFPMWSDQPTNAKLLEESWKTGVRVRENKDGLVE
SQ  RGEIRRCLEAVMEEKSVELRENAKKWKRLAMEAGREGGSSDKNMEAFVEDICGESLIQNLCEAEEVKVK
//
ID  Q5RA57;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
GN  AGPAT3;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NRZ7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRZ7}.
DR  UNIPROT: Q5RA57;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. Has a preference for arachidonoyl-CoA as a donor (By similarity). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:Q9D517, ECO:0000250|UniProtKB:Q9NRZ7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0003841;
GO  GO:0016024;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLLAFLKTQFVLHPLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQA
SQ  TVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLR
SQ  RLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
SQ  LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLS
SQ  PLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
//
ID  Q3U827;
PN  E3 ubiquitin-protein ligase RNF180;
GN  Rnf180;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18363970}; Single-pass membrane protein {ECO:0000269|PubMed:18363970}. Nucleus envelope {ECO:0000269|PubMed:18363970}.
DR  UNIPROT: Q3U827;
DR  UNIPROT: Q3UW39;
DR  UNIPROT: Q80ZX1;
DR  UNIPROT: Q8CCR1;
DR  UNIPROT: Q9CXV6;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000269|PubMed:18363970}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031227;
GO  GO:0005635;
GO  GO:0046872;
GO  GO:0031624;
GO  GO:0061630;
GO  GO:0030534;
GO  GO:0042415;
GO  GO:1901360;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0000209;
GO  GO:0050790;
GO  GO:0042428;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRSEESTSTQSPEEQTGTLHCWRCRKCIASSGCFMTPLETQVVEQDRHESVDAQNTCHLWHMNVDALPEWISCLLQKAQ
SQ  WTVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLCKSRTDHQAAQGGRLMRPALKHLPHPGVPSGCDKETLLTGGGSK
SQ  TRNHWLLSMARNSNGLGRLTEALCLEVRATYFEMKNEKLLFKASDPKCQPFVPQPDTGRCPSRASHRKSHSLDLNISEKL
SQ  ILLPTLYEIHRKPTAYPRLNETGPIDLSGLALPCSNSSCSFQSPPSFDPNMLLHRLSVAPHETQAQRGRECQCGLEASSV
SQ  YSDHANANSLPFLMDLPSAGRSVLEASDQEEHLSQLDFLRSASFPLGTINHRLNNRERSKLRTLRRQQRRERWLQKQGKY
SQ  SGVGLLDHMTVSNEMSTDEETEFPEEKDSYMCAVCLDVYFNPYMCYPCHHIFCEPCLRTLAKDNPASTPCPLCRTIISRV
SQ  FLQTELNNATKTFFTKEYLKIKQSFQKSSSAKWPLPSCRKGFHLFGGFHRRAAPVTRRQFPHGAHRMDYLHFEDDSRGWW
SQ  FDMDMVIIYIYSVNWVIGFVVFCFLCYFFFPF
//
ID  Q8B912;
PN  Non-structural protein 12;
GN  rep;
OS  300563;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-beta papain-like cysteine proteinase]: Host cytoplasm {ECO:0000250}. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q8B912;
DR  UNIPROT: Q8B911;
DR  Pfam: PF16749;
DR  Pfam: PF14757;
DR  Pfam: PF14756;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. Nsp1-alpha inhibits IFN-beta production. Counteracts the action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-alpha is suppressed. This leads to the blockage of NF-kappaB nuclear translocation and thus interference of NF-kappaB activation. Also seems to inhibit IRF3-dependent pathways (By similarity). {ECO:0000250}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. Deubiquitinates host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation (By similarity). {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039648;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039563;
GO  GO:0039502;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVPELGVLGLFYRPEEPLRWTLPRAFPTVECSPTGACWLSA
SQ  IFPIARMTSGNLNFQQRMVRVAGEIYRAGQLTPTVLKTIQVYERGCRWYPIVGPVPGVGVYANSLHVSDKPFPGATHVLT
SQ  NLPLPQRPKPEDFCPFECAMADVYDIGRGAVMYVAGGKVSWAPRGGDEVKFEPVPKELKLVANRLHTSFPPHHVVDMSKF
SQ  TFMTPGSGVSMRVEYQYGCLPADTVPEGNCWWRLFDLLPPEVQNKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTD
SQ  THGPIVIQYFSVKESWIRHLKPVEEPSLPGFEDLLRIRVEPNTSPLAGKNEKIFRFGSHKWYGAGKRARKARSGATTMVA
SQ  HRASSAHETRQATKHEGAGANKAEHLKLYSPPAEGNCGWHCISAIVNRMVNSNFETTLPERVRPPDDWATDEDLVNTIQI
SQ  LRLPAALDRNGACGGAKYVLKLEGEHWTVSVNPGMSPSLLPLECVQGCCEHKGGLGSPDAVEVSGFDPACLDRLLQVMHL
SQ  PSSTIPAALAELSDDSNRPVSPAAATWTVSQSYARHRGGNHHDQVCLGKIISLCQVIEDCCCHQNKTNRATPEEVAAKID
SQ  QYLRGATSLEECLAKLERVSPPGAADTSFDWNVVLPGVEAAHQTTEQLHVNPCRTLVPPVTQEPLGKDSVPLTAFSLSNC
SQ  YYPAQGNEVRHRERLNSVLSKLEEVVLEEYGLMSTGLGPRPVLPSGLDELKDQMEEDLLKLANTQATSEMMAWAAEQVDL
SQ  KAWVKSYPRWTPPPPPPRVQPRKTKSVKSLPEDKPVPAPRRKVRSGCGSPVLMGDNVPNGSEDLTVGGPLNFPTPSEPMT
SQ  PMSEPVLTPALQRVPKLMTPLDGSAPVPAPRRTVSRPMTPLSEPIFLSAPRHKFQQVEEANPATTTLTHQNEPLDLSASS
SQ  QTEYEASPLASSQNMSILEAGGQEAEEVLSEISDILNDTSPAPVSSSSSLSSVKITRPKYSAQAIIDSGGPCSGHLQKEK
SQ  EACLSIMREACDASKLSDPATQEWLSRMWDRVDMLTWRNTSAYQAFRTLNGRFEFLPKMILETPPPHPCGFVMLPHTPAP
SQ  SVSAESDLTIGSVATEDVPRILGKIGDTGELLNQGPSAPFKGGPVCDQPAKNSRMSPRESDESIIAPPADTGGAGSFTDL
SQ  PSSDSVDANGGGPLRTVKTKAGRLLDQLSCQVFSLVSHLPVFFSHLFKSDSGYSPGDWGFAAFTLFCLFLCYSYPFFGFA
SQ  PLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGTACEFDSPECRNVLHSFELLKPWDPVRSLVVGPVGLGLAILGR
SQ  LLGGARYVWHFLLRFGIVADCILAGAYVLSQGRCKKCWGSCVRTAPNEIAFNVFPFTRATRSSLIDLCDRFCAPKGMDPI
SQ  FLATVWRGCWTGRSPIEQPSEKPIAFAQLDEKRITARTVVAQPYDPNQAVKCLRVLQAGGAMVAEAVPKVVKVSAIPFRA
SQ  PFFPAGVKVDPECRIVVDPDTFTTALRSGYSTTNLVLGMGDFAQLNGLKIRQISKPSGGGSHLVAALHVACSMALHMLAG
SQ  VYVTAVGSCGTGTNDPWCTNPFAAPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGLQEIALVVLIFVSMGGMAHRLSCK
SQ  ADMLCILLAIASYVWVPLTWLLCVFPCWLRWFSLHPLTILWLVFFLISVNIPSGILAVVLLVSLWLLGRYTNIAGLVTPY
SQ  DIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTQKPSLNTVNVVGSSMGSGGVFTIDGK
SQ  IKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKAQFCEDGWTGRAYWLTSSGVEPGVIGNGFAFC
SQ  FTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVTPIKLSELSEFFAGPKVPLGDVKIGSHIIKDTCEVPS
SQ  DLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVGFFILNEILPAVLVRSVFSFGMFVLSWLTPWSAQVLMI
SQ  RLLTAALNRNRLSLGFYSLGAVTSFVADLAVTQGHPLQVVMNLSTYAFLPRMMVVTSPVPVIACGVVHLLAIILYLFKYR
SQ  CLHYVLVGDGVFSSAFFLRYFAEGKLREGVSQSCGMSHESLTGALAMRLTDEDLDFLTKWTDFKCFVSASNMRNAAGQFI
SQ  EAAYAKALRIELAQLVQVDKVRGTLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSK
SQ  MTVARVVDPTPAPPPVPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEAVGIFVMDGKKYQKFWDKNSGDVFYEEVHNS
SQ  TDEWECLRAGDPADFDPETGVQCGHITIEDRVYNVFTSPSGRKFLVPANPENRRAQWEAAKLSVEQALGMMNVDGELTAK
SQ  ELEKLKGIIDKLQGLTKEQCLNCLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHP
SQ  VARPVDGGVVLLRSAVPSLIDVLISGADASPKLLARHGPGNTGIDGTLWDFEAEATKEEVALSAQIIQACDIRRGDAPEI
SQ  GLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPSGFELYVPTIPASVL
SQ  DYLDSRPDCPKQLTEHGCEDAALRDLSKYDLVTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFP
SQ  TKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAALSGVTQGFMKKAFNSPIALGKNK
SQ  FKELQTPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSV
SQ  SNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPSMPNYHWWVEHLNLMLGFQTD
SQ  PKKTAITDSPTFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCAR
SQ  KDGYSFPGPPFFLSMWEKLRSNHEGKKSRMCGYCMAPAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCGECEPP
SQ  LGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVDLPDGDYASTALLPTCKEINMVA
SQ  VAPNVLRSRFIIGPPGAGKTHWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPAPSRTGPWVRILAGGW
SQ  CPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLV
SQ  SMVNTTRVTYVEKPVRYGQVLTPYHRDREDGAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQ
SQ  LQSMFDLPAKGTPVNLAVHRDEQLIVLDRNNKEITVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGF
SQ  YFSPDLTQFAKLPAELAPHWPVVTTQNNERWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVRGEA
SQ  QVLPETVFSTGRIEVDCREYLDDREREVAESLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGEAAKAF
SQ  CTLTDVYLPDLEAYLHPETQSKCWKVMLDFKEVRLMVWKGKTAYFQLEGRHFTWYQLASYTSYIRVPVNSTVYLDPCMGP
SQ  ALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGED
SQ  WEDYNGAFRARQKGKIYKATATSMKFHFPPGPVIEPTLGLN
//
ID  Q96FS4;
PN  Signal-induced proliferation-associated protein 1;
GN  SIPA1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9346962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9346962}. Endomembrane system; Peripheral membrane protein {ECO:0000269|PubMed:9346962}. Note=Mostly localized in the perinuclear membraneous region. {ECO:0000269|PubMed:9346962}.
DR  UNIPROT: Q96FS4;
DR  UNIPROT: O14518;
DR  UNIPROT: O60484;
DR  UNIPROT: O60618;
DR  UNIPROT: Q2YD83;
DR  Pfam: PF00595;
DR  Pfam: PF02145;
DR  PROSITE: PS50106;
DR  PROSITE: PS50085;
DR  OMIM: 602180;
DR  DisGeNET: 6494;
DE  Function: GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting them to the putatively inactive GDP-bound state (PubMed:9346962). Affects cell cycle progression (By similarity). {ECO:0000250|UniProtKB:P46062, ECO:0000269|PubMed:9346962}.
DE  Reference Proteome: Yes;
DE  Interaction: O00159; IntAct: EBI-350423,EBI-1054981; Score: 0.35
DE  Interaction: P31946-2; IntAct: EBI-10770173,EBI-1054981; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-359832,EBI-1054981; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-1054981; Score: 0.35
DE  Interaction: Q8R034; IntAct: EBI-10976681,EBI-1054981; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-353957,EBI-1054981; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-2553589,EBI-1054981; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-400906,EBI-1054981; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-350338,EBI-1054981; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-762451,EBI-1054981; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-351479,EBI-1054981; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-351394,EBI-1054981; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-1054981; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-10983249,EBI-1054981; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-352350,EBI-1054981; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-297509,EBI-1054981; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-347088,EBI-1054981; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-359854,EBI-1054981; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-1054981; Score: 0.35
DE  Interaction: P38936; IntAct: EBI-1054981,EBI-375077; Score: 0.51
DE  Interaction: O14640; IntAct: EBI-1054981,EBI-723489; Score: 0.37
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0030133;
GO  GO:0005096;
GO  GO:0008022;
GO  GO:0042631;
GO  GO:0007010;
GO  GO:0035556;
GO  GO:0007162;
GO  GO:0045786;
GO  GO:0030308;
GO  GO:0051056;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9346962};
SQ  MPMWAGGVGSPRRGMAPASTDDLFARKLRQPARPPLTPHTFEPRPVRGPLLRSGSDAGEARPPTPASPRARAHSHEEASR
SQ  PAATSTRLFTDPLALLGLPAEEPEPAFPPVLEPRWFAHYDVQSLLFDWAPRSQGMGSHSEASSGTLASAEDQAASSDLLH
SQ  GAPGFVCELGGEGELGLGGPASPPVPPALPNAAVSILEEPQNRTSAYSLEHADLGAGYYRKYFYGKEHQNFFGMDESLGP
SQ  VAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPQLSPSCLRLGSASPKVPRT
SQ  LLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGPAFMQFLTLLGDVVRLKGFESYRAQLDTKTDSTGTHSLYTTYQ
SQ  DHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHTPCTPHTTYRVAVSRT
SQ  QDTPAFGPALPAGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSL
SQ  GGRRRAAPRGPGAELQAAGSLVWGVRAAPGARVAAGAQASGPEGIEVPCLLGISAEALVLVAPRDGRVVFNCACRDVLAW
SQ  TFSEQQLDLYHGRGEAITLRFDGSPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFVTHVERFTFAETA
SQ  GLRPGARLLRVCGQTLPSLRPEAAAQLLRSAPKVCVTVLPPDESGRPRRSFSELYTLSLQEPSRRGAPDPVQDEVQGVTL
SQ  LPTTKQLLHLCLQDGGSPPGPGDLAEERTEFLHSQNSLSPRSSLSDEAPVLPNTTPDLLLATTAKPSVPSADSETPLTQD
SQ  RPGSPSGSEDKGNPAPELRASFLPRTLSLRNSISRIMSEAGSGTLEDEWQAISEIASTCNTILESLSREGQPIPESGDPK
SQ  GTPKSDAEPEPGNLSEKVSHLESMLRKLQEDLQKEKADRAALEEEVRSLRHNNRRLQAESESAATRLLLASKQLGSPTAD
SQ  LA
//
ID  O45717;
PN  Protein nud-2;
GN  nud;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:20005871}. Note=Recruited to the nuclear envelope by unc-83. {ECO:0000269|PubMed:20005871}.
DR  UNIPROT: O45717;
DE  Function: Part of a complex with lis-1, which is recruited to the nuclear envelope by unc-83, where, in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871, PubMed:27697906). Plays a role in GABAergic synaptic vesicle localization in the ventral nerve cord (PubMed:16996038). {ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: Q23064-3; IntAct: EBI-326083,EBI-2902257; Score: 0.60
DE  Interaction: O01738; IntAct: EBI-326083,EBI-2416420; Score: 0.49
DE  Interaction: Q20398; IntAct: EBI-326083,EBI-322716; Score: 0.49
DE  Interaction: Q94420; IntAct: EBI-320790,EBI-326083; Score: 0.49
DE  Interaction: O44139; IntAct: EBI-2414979,EBI-326083; Score: 0.49
DE  Interaction: O76447; IntAct: EBI-314341,EBI-326083; Score: 0.37
GO  GO:0005623;
GO  GO:0005813;
GO  GO:0005871;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0016477;
GO  GO:0051642;
GO  GO:0007059;
GO  GO:0051303;
GO  GO:0000132;
GO  GO:0007020;
GO  GO:0007100;
GO  GO:0007097;
GO  GO:2000574;
GO  GO:0051932;
GO  GO:0048489;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLSEDQIRGLPHHELLGHFLQMREEFNEFQTSSAEIEKMMDSELDDLKTQLKKAETRVQQMTTEQIRNKDRQDDSRVQF
SQ  AQVEEQLRRENSHLHEQCESQRERIRKLEQRNDVLETSERNKEYLASDLGSKLDHAIEKIAMLESELYERQVAAEEMHRL
SQ  REEQLRTTERPRLIVEPLRNDPEILPDEPSPGPSKEEFKMSSEDVFMEDVQHHEDVRMEETIAKIDEVRIDDNKNIQEKS
SQ  QRVSTGTGAGACINRIVKDLMTKVERLDSILSTIRVSNNSSNNNSSHLTTTRA
//
ID  Q8TB68;
PN  Proline-rich protein 7;
GN  PRR7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21460222}; Single-pass type III membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic density membrane {ECO:0000250|UniProtKB:P0C6T3}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21460222}. Cell junction, synapse {ECO:0000269|PubMed:27458189}. Cell projection, dendrite {ECO:0000269|PubMed:27458189}. Nucleus {ECO:0000269|PubMed:27458189}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern. Translocates from synapses to nuclei following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}.
DR  UNIPROT: Q8TB68;
DR  UNIPROT: Q8WU53;
DR  UNIPROT: Q9BTA7;
DR  OMIM: 618306;
DR  DisGeNET: 80758;
DE  Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (By similarity). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (PubMed:27458189). Might play a redundant role in the regulation of T cell receptor signaling (PubMed:21460222). Might promote apoptosis in T cells (PubMed:21460222). {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q3V0I2, ECO:0000269|PubMed:21460222, ECO:0000269|PubMed:27458189}.
DE  Reference Proteome: Yes;
DE  Interaction: A8K8V0; IntAct: EBI-3925410,EBI-3925400; Score: 0.37
GO  GO:0030054;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0016021;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0099092;
GO  GO:0036041;
GO  GO:1990782;
GO  GO:0044877;
GO  GO:0044389;
GO  GO:0002250;
GO  GO:0046632;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0010942;
GO  GO:2001269;
GO  GO:0099527;
GO  GO:0033077;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPQPPPH
SQ  RSRLEAPAHAHSHPHVHVHPLLHHGPAQPHAHAHPHPHHHALPHPPPTHLSVPPRPWSYPRQAESDMSKPPCYEEAVLMA
SQ  EPPPPYSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAPPCPALCLQADRGRRVF
SQ  PSWTDSELSSREPLEHGAWRLPVSIPLFGRTTAV
//
ID  E9QAT4;
PN  Protein transport protein Sec16A;
GN  Sec16a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15027}. Microsome membrane {ECO:0000250|UniProtKB:O15027}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882). Recruited to microsomal membrane in SAR1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:25201882}.
DR  UNIPROT: E9QAT4;
DR  UNIPROT: A2AIX1;
DR  UNIPROT: Q80U43;
DR  UNIPROT: Q811L5;
DR  Pfam: PF12932;
DR  Pfam: PF12931;
DE  Function: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17428803). Mediates the recruitment of MIA3/TANGO to ERES. Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (By similarity). Acts as a RAB10 effector in the regulation of insulin- induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in adipocytes (PubMed:27354378). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:27354378}.
DE  Reference Proteome: Yes;
DE  Interaction: Q61584; IntAct: EBI-8350418,EBI-647676; Score: 0.35
DE  Interaction: Q5S006; IntAct: EBI-647676,EBI-2693710; Score: 0.46
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-647676; Score: 0.27
DE  Interaction: P39428; IntAct: EBI-647676,EBI-520123; Score: 0.37
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070971;
GO  GO:0005789;
GO  GO:0012507;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0031090;
GO  GO:0048471;
GO  GO:0048208;
GO  GO:0007029;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0043000;
GO  GO:0070863;
GO  GO:0032527;
GO  GO:0070973;
GO  GO:0072659;
GO  GO:0050821;
GO  GO:0034976;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15027};
SQ  MQPPPQAVPSGVAGPPPAGNPRSMFWANSPYRKPANNAPVAPITRPLQPVTDPFAFNRQTLQNTPVGSSSKSSLPNLPGP
SQ  ALSVFSQWPGLPVTPTNAGDSSTGLHEPLSGTLSQPRADASLFPPASTPSSLPGLEVSRNAEADPSSGHEVQMLPHSAHY
SQ  IPGVGPEQPLGGQMNDSGSGPDQPMNRHAPHDGAVTHAASPFLPQPQMPGQWGPAQGGPQPSYQHHSPYLEGPVQNMGLQ
SQ  AASLPHFPPPSSLHQGPGHESHAPQTFTPASLASGEGNEIVHQQSKNHPLSSFPPKHTFEQNSRIGNMWASPELKQNPGV
SQ  NKEHLLDPAHVNPFTQGNSPENQAHHPPVAATNHALQEAASGALSMFFQGEETENEENLSSEKAGLDKRLNLDSFSSTSR
SQ  LGHPPPPGASGVYQAFPRGPSSEAAQEGDAQPYFSQSVGVRLDKQSTVPPANDAWGDVPGTGTRCASGPQCENVENLEFV
SQ  QNQEVLPRETLSVDPFPLSDQIRYGPLPGPAASRPATVGLTRGGGLNLEAPDTPLHPTRPDSVSSSYSSHSHRSPPGSAR
SQ  PQELVGTFIQQEVGKLEDDTSGSFFKQIDSSPVGGETDEVTGSQNCCSSLSQPSTPSPPKPTGVFQTSANSSFEPVKSHL
SQ  VGVKPVEADRANMVVEVRGTQYCPKKRRAAVAPPDATSGNLEQPPDNMETPCAPQACPLPLSTTGEAGQLVSNTAGTPLD
SQ  TVRPVPDKRPSARAQGPVKCESPATTLWAQNELPDFGGNVLLAPAAPALYVPVKPKPSEVVHHPEKGMSGQKAWKQGSVP
SQ  PLQNQDPPGASENLENPPKVGEEEALPVQASSGYASLLSSPPTESLHNQPVLIAQPDQSYNLAQPINFSVSLLNPNEKNQ
SQ  SWGDAVVGERSIVSNNWALGGDPEERAALSGVPASAVTGASLPSSIPQNCAPQGSGSSEMIASQSASWLVQQLSPQTPQS
SQ  PHPNAEKGPSEFVSSPAGNTSVMLVPPASSTLVPNSNKAKHSSNQEEAVGALDFTLNRTLENPVRMYSPSPSDGPASQQP
SQ  LPNHPRQSGPGLHNQDHFYQQVTKDAQDQHRLERAQPELVPPRPQNSPQVPQASCPEPSNPESPPTQGQSESLAQPPASP
SQ  ASVNTGQLLPQPPQASSASVTSTNSSQAAVRSEQLWLHPPPPNTFGPAPQDLASYYYYRPLYDAYQSQYPSPYPSDPGTA
SQ  SLYYQDMYGLYEPRYRPYDSSASAYAENHRYSEPERPSSRASHYSDQLAPRQGYPEGYYNSKSGWSSHSDYYANYYSGQY
SQ  DYGDPSRWDRYYGSRLRDPRTWDRRYWYDSEHDPYRKDHYAYSDRPEKCDDHWRYDPRFTGSFDDDAEIHRDPYGEEADR
SQ  RSIHSEHSARSLRSTHSLPSRRSSLSSHSHQSQIYRSHHVTGGSFEAPHAPGSFHGDYAYGTYASNFSGAHGFPEYSYPA
SQ  DTSWPAVEQVPSRPTSPEKFTVPHVCARFGPGGQLLKVIPNLPSEGQPALVEIHSLETLLQHTPEQEEMRSFPGPLGKDD
SQ  THKVDVINFAQNKATKCLQNESLIDKESASLLWKFIILLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNE
SQ  AVEQVEEEESGEAQLSFLTDSQTVTTSVLEKETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRF
SQ  ANSLPINDPLQTVYQLMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASKGLLDAAHFCYLM
SQ  AQVGFGVYTKKTTKLVLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAHTCSLPNFQVFKFIYLCRLAEMGLATQAFHY
SQ  CEVIAKSVLTQPGAYSPVLISQLTQMASQLRLFDPQLKEKPEEESFVEPAWLVQLQHVERQIQEGTVLWSQDGTEPQQCR
SQ  ITSGSEVEQSDGPGLNQQAGPQADNPLLMPSTEPLMHGVQLLPTAPQTLPDGQPAHLSRVPMFPVPMSRGPLELSPAYGP
SQ  PGSALGFPESSRSDPAVLHPGQALPPTTLSLQESGLPPQEAKSPDPEMVPRGSPVRHSPPELSQEEFGESFADPGSSRTA
SQ  QDLETSPVWDLGSSSLTRAPSLTSDSEGKKPAQAVKKEPKEPKKTESWFSRWLPGKKRTEAYLPDDKNKSIVWDEKKNQW
SQ  VNLNEPEEEKKAPPPPPTSFPRVPQVAPTGPAGPPTASVNVFSRKAGGSRARYVDVLNPSGTQRSEPALAPADFFAPLAP
SQ  LPIPSNLFVPNPDAEEPQPADGTGCRGQAPAGTQSKAESTLEPKVGSSTVSAPGPELLPSKPDGSQGGEAPGDHCPTGAP
SQ  HGGSVPFYNPAQLVQASVTSGNSRPGRIGQRKYAALN
//
ID  O76050;
PN  E3 ubiquitin-protein ligase NEURL1;
GN  NEURL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11585928, ECO:0000269|PubMed:20847082}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Note=Localized in the cell bodies of the pyramidal neurons and distributed along their apical dendrites. Colocalized with PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites of CA1 neurons (By similarity). Colocalized with JAG1 at the cell surface. {ECO:0000250}.
DR  UNIPROT: O76050;
DR  UNIPROT: Q5TDR2;
DR  UNIPROT: Q5TDR3;
DR  UNIPROT: Q8TAN0;
DR  UNIPROT: Q9H463;
DR  Pfam: PF07177;
DR  PROSITE: PS51065;
DR  PROSITE: PS50089;
DR  OMIM: 603804;
DR  DisGeNET: 9148;
DE  Function: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:20847082}.
DE  Reference Proteome: Yes;
DE  Interaction: P62256; IntAct: EBI-2129909,EBI-2129917; Score: 0.37
DE  Interaction: P61088; IntAct: EBI-2129917,EBI-1052908; Score: 0.37
DE  Interaction: Q07065; IntAct: EBI-702400,EBI-2129917; Score: 0.40
GO  GO:0097440;
GO  GO:0030054;
GO  GO:0043197;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0046872;
GO  GO:0045183;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0007420;
GO  GO:0071230;
GO  GO:0007595;
GO  GO:0008285;
GO  GO:0045746;
GO  GO:0007399;
GO  GO:0007219;
GO  GO:0043065;
GO  GO:0060999;
GO  GO:0045741;
GO  GO:0051491;
GO  GO:0048170;
GO  GO:0090129;
GO  GO:0006513;
GO  GO:0007519;
GO  GO:0007288;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSH
SQ  KAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEE
SQ  FANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLR
SQ  READDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGR
SQ  DERALVFTSRPVRVAETIFVKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILG
SQ  LVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFGLHGTITQIRILGSTILAERGIPSLPCSPASTPTSPSALGSRLSDP
SQ  LLSTCSSGPLGSSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYACGLRLKKALHACCPIC
SQ  RRPIKDIIKTYRSS
//
ID  Q9UBF8;
PN  Phosphatidylinositol 4-kinase beta;
GN  PI4KB;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus {ECO:0000269|PubMed:22124328}. Golgi apparatus membrane {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:28289207}. Cytoplasm, perinuclear region. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5- bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3 (PubMed:24672044, PubMed:27009356, PubMed:28289207). GGA2 is also involved in the recruitment (PubMed:28289207). {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:28289207}.
DR  UNIPROT: Q9UBF8;
DR  UNIPROT: B4DGI2;
DR  UNIPROT: O15096;
DR  UNIPROT: P78405;
DR  UNIPROT: Q5VWB9;
DR  UNIPROT: Q5VWC0;
DR  UNIPROT: Q5VWC1;
DR  UNIPROT: Q9BWR6;
DR  PDB: 2N73;
DR  PDB: 4D0L;
DR  PDB: 4D0M;
DR  PDB: 4WAE;
DR  PDB: 4WAG;
DR  PDB: 5C46;
DR  PDB: 5C4G;
DR  PDB: 5EUQ;
DR  PDB: 5FBL;
DR  PDB: 5FBQ;
DR  PDB: 5FBR;
DR  PDB: 5FBV;
DR  PDB: 5FBW;
DR  PDB: 5LX2;
DR  PDB: 5NAS;
DR  PDB: 6GL3;
DR  Pfam: PF00454;
DR  PROSITE: PS00915;
DR  PROSITE: PS00916;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DR  OMIM: 602758;
DR  DisGeNET: 5298;
DE  Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250, ECO:0000269|PubMed:10559940, ECO:0000269|PubMed:12749687, ECO:0000269|PubMed:9405935}. (Microbial infection) Plays an essential role in Aichi virus RNA replication (PubMed:22124328, PubMed:27989622, PubMed:22258260). Recruited by ACBD3 at the viral replication sites (PubMed:22124328, PubMed:27989622). {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:27989622}.
DE  Reference Proteome: Yes;
DE  Interaction: P31946-2; IntAct: EBI-10770173,EBI-1053214; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-359832,EBI-1053214; Score: 0.69
DE  Interaction: P03300; IntAct: EBI-21242141,EBI-1053214; Score: 0.50
DE  Interaction: P31946; IntAct: EBI-359815,EBI-1053214; Score: 0.69
DE  Interaction: Q8WVZ9; IntAct: EBI-473695,EBI-1053214; Score: 0.40
DE  Interaction: P46939; IntAct: EBI-1053214,EBI-295856; Score: 0.40
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-1053214; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-347088,EBI-1053214; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-359854,EBI-1053214; Score: 0.76
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-1053214; Score: 0.35
DE  Interaction: Q9Y3M2; IntAct: EBI-1053214,EBI-947308; Score: 0.27
DE  Interaction: Q96QF0; IntAct: EBI-1053214,EBI-747844; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0030867;
GO  GO:0004430;
GO  GO:0071889;
GO  GO:0005524;
GO  GO:0052742;
GO  GO:0006661;
GO  GO:0046854;
GO  GO:0048015;
GO  GO:0006898;
GO  GO:0007165;
GO  GO:0016032;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNG
SQ  DGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYI
SQ  GNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLI
SQ  LSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPV
SQ  RLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIY
SQ  VEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCD
SQ  NISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLS
SQ  VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGS
SQ  YTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGG
SQ  LDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSI
SQ  TTKLYDGFQYLTNGIM
//
ID  P90897;
PN  DEAD-box ATP-dependent RNA helicase rde-12;
GN  rde;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:24684931}. Cytoplasmic granule {ECO:0000269|PubMed:24684930, ECO:0000269|PubMed:24684931}. Cytoplasm {ECO:0000269|PubMed:24684931}. Cytoplasm, P-body {ECO:0000269|PubMed:24684930}. Note=Colocalizes with pgl-1 in perinuclear P granules. Colocalizes with rsd-6 in a subset of germline and embryonic foci. {ECO:0000269|PubMed:24684930}.
DR  UNIPROT: P90897;
DR  UNIPROT: G3MU56;
DR  UNIPROT: G3MU57;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: Probable ATP-dependent RNA helicase involved in RNAi-mediated gene silencing (PubMed:24684930, PubMed:24684931). Specifically required in the endogenous siRNA pathway for biogenesis of secondary endogenous small interfering RNA (siRNA) intermediates called 22G-RNAs (PubMed:24684930, PubMed:24684931). May associate with and recruit rde- 10 to primary siRNA-targeted mRNA for secondary siRNA synthesis (PubMed:24684930). May be recruited to target mRNAs by rde-1 and/or ergo-1 (PubMed:24684930, PubMed:24684931). {ECO:0000269|PubMed:24684930, ECO:0000269|PubMed:24684931}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0043186;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0031332;
GO  GO:0005524;
GO  GO:0019899;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030422;
GO  GO:0006417;
GO  GO:0043330;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHS
SQ  RDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSY
SQ  QGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYR
SQ  GQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHR
SQ  SDGSNSEGVNAPVRAPRDWVPVTRDIDELVRETADRLADCDVGQDRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKY
SQ  NNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRT
SQ  YCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPLGHLGAII
SQ  KDAGFMESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVNLEFFECKGLAEKNAKLREILKQN
SQ  VNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINF
SQ  DLPDGDPDQGADTFIHRAGRTGRTGRKENGLCVSFVDPQSDRDSLLAPKLVELIISQNLPDLKVPDFLDAMAKSSRGKSG
SQ  TSGFGQRGGYGGRGGGFGGTGRGRGGGVFGGGGRGGDFGGSGNFGGSGGGGSFGGSGGGGGFGGVKPSGFGGSRNNAEPT
SQ  SSGGGFGAPKAPTGFPSDNNDASEDAPAAGGFGFSTKAAQDAKKAEESATLGSSTFGTANNADEEPTETGADGNDDDEW
//
ID  P53816;
PN  Phospholipase A and acyltransferase 3;
GN  PLAAT3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:17374643}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}.
DR  UNIPROT: P53816;
DR  UNIPROT: B2R7Q4;
DR  UNIPROT: B7XAK5;
DR  UNIPROT: Q3SYI3;
DR  UNIPROT: Q9HDD1;
DR  PDB: 2KYT;
DR  PDB: 4DOT;
DR  PDB: 4FA0;
DR  PDB: 4Q95;
DR  Pfam: PF04970;
DR  OMIM: 613867;
DR  DisGeNET: 11145;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N- acylphosphatidylethanolamine (NAPE), which serves as precursor for N- acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616, ECO:0000303|PubMed:26503625}. (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid- modifying enzyme activity is required for this process (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRR5; IntAct: EBI-711226,EBI-746318; Score: 0.37
DE  Interaction: Q9UMX0-2; IntAct: EBI-10173939,EBI-746318; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-746318,EBI-741480; Score: 0.78
DE  Interaction: P30153; IntAct: EBI-746318,EBI-302388; Score: 0.64
DE  Interaction: Q9UHD9; IntAct: EBI-947187,EBI-746318; Score: 0.56
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0102567;
GO  GO:0102568;
GO  GO:0046485;
GO  GO:0016042;
GO  GO:0070292;
GO  GO:0045786;
GO  GO:0007031;
GO  GO:0036151;
GO  GO:0036152;
GO  GO:0036149;
GO  GO:0036150;
GO  GO:0008654;
GO  GO:0006644;
GO  GO:1904177;
GO  GO:0009617;
GO  GO:0006641;
GO  GO:0016032;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKH
SQ  DDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQ
SQ  KQ
//
ID  Q9Y4G8;
PN  Rap guanine nucleotide exchange factor 2;
GN  RAPGEF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Late endosome. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. Colocalized with CTNNB1 at cell-cell contacts (By similarity). Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. {ECO:0000250}.
DR  UNIPROT: Q9Y4G8;
DR  UNIPROT: D3DP27;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DR  OMIM: 609530;
DR  OMIM: 618075;
DR  DisGeNET: 9693;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10608844, PubMed:10548487, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP- independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:10608883, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:10934204, ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:23800469}.
DE  Disease: Epilepsy, familial adult myoclonic, 7 (FAME7) [MIM:618075]: A form of familial myoclonic epilepsy, a neurologic disorder characterized by cortical hand tremors, myoclonic jerks and occasional generalized or focal seizures with a non-progressive or very slowly progressive disease course. Usually, myoclonic tremor is the presenting symptom, characterized by tremulous finger movements and myoclonic jerks of the limbs increased by action and posture. In a minority of patients, seizures are the presenting symptom. Some patients exhibit mild cognitive impairment. FAME7 inheritance is autosomal dominant. {ECO:0000269|PubMed:29507423}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q12840; IntAct: EBI-307079,EBI-713468; Score: 0.37
DE  Interaction: Q9Y3A3; IntAct: EBI-713935,EBI-307079; Score: 0.37
DE  Interaction: P46937; IntAct: EBI-1044059,EBI-307079; Score: 0.53
DE  Interaction: P03928; IntAct: EBI-307079,EBI-3439833; Score: 0.37
DE  Interaction: P33176; IntAct: EBI-307079,EBI-355878; Score: 0.37
DE  Interaction: Q9H0H5; IntAct: EBI-717233,EBI-307079; Score: 0.35
DE  Interaction: Q9UJA5; IntAct: EBI-307079,EBI-934061; Score: 0.35
DE  Interaction: Q14696; IntAct: EBI-307079,EBI-6165891; Score: 0.35
DE  Interaction: Q6BDS2; IntAct: EBI-307079,EBI-11028496; Score: 0.35
DE  Interaction: Q96L50; IntAct: EBI-307079,EBI-2510106; Score: 0.35
DE  Interaction: Q96KM6; IntAct: EBI-307079,EBI-1049952; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-307079,EBI-466029; Score: 0.35
DE  Interaction: Q8N9Q2; IntAct: EBI-307079,EBI-10268630; Score: 0.35
DE  Interaction: A6H8Y1-7; IntAct: EBI-307079,EBI-10963103; Score: 0.35
DE  Interaction: C9J1X0; IntAct: EBI-307079,EBI-11033553; Score: 0.35
DE  Interaction: Q9BYT9; IntAct: EBI-307079,EBI-10987814; Score: 0.35
DE  Interaction: Q99442; IntAct: EBI-307079,EBI-949221; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-307079,EBI-954033; Score: 0.35
DE  Interaction: O43414; IntAct: EBI-307079,EBI-9679612; Score: 0.35
DE  Interaction: P20674; IntAct: EBI-307079,EBI-715032; Score: 0.35
DE  Interaction: P98170; IntAct: EBI-307079,EBI-517127; Score: 0.35
DE  Interaction: G5E9A6; IntAct: EBI-307079,EBI-10976685; Score: 0.35
DE  Interaction: Q9H930-2; IntAct: EBI-307079,EBI-10968048; Score: 0.35
DE  Interaction: Q14558-2; IntAct: EBI-307079,EBI-11037566; Score: 0.35
DE  Interaction: P26041; IntAct: EBI-8322611,EBI-307079; Score: 0.35
DE  Interaction: Q96JG6; IntAct: EBI-11044388,EBI-307079; Score: 0.35
DE  Interaction: Q96QZ7-2; IntAct: EBI-21619854,EBI-307079; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-307079,EBI-358348; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-358900,EBI-307079; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-5327611,EBI-307079; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-307079; Score: 0.35
DE  Interaction: P41743; IntAct: EBI-286199,EBI-307079; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0005887;
GO  GO:0005770;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0005509;
GO  GO:0030552;
GO  GO:0019992;
GO  GO:0005096;
GO  GO:0030165;
GO  GO:0070300;
GO  GO:0017034;
GO  GO:0005088;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0090557;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0035556;
GO  GO:0000165;
GO  GO:0030033;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:1901888;
GO  GO:0048167;
GO  GO:0007264;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIRE
SQ  FAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQP
SQ  QQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTS
SQ  PQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SQ  SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFD
SQ  YSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSS
SQ  LTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SQ  SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
//
ID  P0C6W0;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  693999;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W0;
DR  UNIPROT: Q0Q467;
DR  Pfam: PF13087;
DR  Pfam: PF16348;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF09401;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF05409;
DR  Pfam: PF08715;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016896;
GO  GO:0008168;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0032259;
GO  GO:0039648;
GO  GO:0039548;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASNHISLAFANDEEISAIGFGSVEEAVSYYSDAAVNGFDQCRFVSLGLQDAVVGVEDDDVVMLITGVTQLRAYLGTFGD
SQ  RPLNLRGWLLFSNCNYFLEELDLVFGRCGGTTIPVDQFMCGADGAPVIQEGDWTFMDYFQDSNQFTLNGITYVKAWDVDR
SQ  KPNDYAKQNVTCIRRITYITDHRHVLADGTTMKTARHPKVNKSVVLDSPFDQIYKEVGSPFMGNGSTFVEMLKDPAFFHA
SQ  LITCECGRSEWTVGDWKGYNSLCCNIKCKPITIVTPKAVPGAVVITKAGIGAGLKCYNNVFLKHIIDLVVPGTNLGWGVW
SQ  RIAKVQSKDDVATSGNVLVDDPEDRLDPCYFGNDGPFATKFKFQLLANSFDDEVKGAIVQGVVHVNTAICDVVKDILGLP
SQ  WFVKKLGSLVTVMWDQFVAGVQSMKICTLKVVQLAKALSCATMSVVKGVITLVAEVPEIFKRLFYTLTSALKSLCTSSCD
SQ  ALVVAGKSFAKIGDYVLLPSALVRLVSSKVKGKAQSGIKQLQFATVVLGDTHKVESDRVEFSSVNLKMVDEEFPLNPVGH
SQ  TVAVGNQAFFCSDGLYRFMADRDLVITSPIFKPELELEPIFECDAIPGFPKVAASNVAELCVKVDTLLFNYDKIYKKYST
SQ  IIKGDRCYIQCTHTFKAPSYYFDDDEFVELCTKYYKLPDFDAFYNAVHAATDMDQFCALCTSGFEVFIPRVPDCPPILND
SQ  IDGGSIWTSFILSVRSATDFIKTLKIDLGLNGVVVFVTKKFRKAGALLQKLYNAFLDTVTSFIKVAGVAFKYCATCVPKI
SQ  VINGCYHTVTRLFAKDLQIPTEDGVADFNTFNHCVFPVNPTRIETDSLELEEVDFVEPGVDGKLVILDDYSFYSDGTNYY
SQ  PSDGKGVVASCFKKKGGGVVTISDEVQVRTIDPVYKVRLEYEFEDETLVKVCEKAIGTKLKVTGDWSNLLETLEKAMDVV
SQ  RQHLDVPDYFVYDEEGGTDLNLTIMVSQWPLSSDSEDDFKAVDDEPNANTDETVDTFAEDVAETQNVQQDVTQDEVEAVC
SQ  DLVVKATEEGPIEHEELSEDQKEVQQALAFIEDKPVVVKPDVFAFSYASYGGLKVLNQSSNNCWVSSALVQLQLTGLLDS
SQ  DEMQLFNAGRVSPMVKRCYESQRAIFGSLGDVSACLESLLKDRDGMSITCTIDCGCGPGVRVYENAIFRFTPLKTAFPMG
SQ  RCLICSKTLMHTITQMKGTGIFCRDATALDVDTLVVKPLCAAVYVGAQDGGHYLTNMYDANMAVDGHGRHPIKFNTINTL
SQ  CYKDVDWEVSNGSCDVKPFLTYKNIEFYQGELSALLSVNHDFVVNAANEQLSHGGGIAKALDDLTKGELQVLSNQYVSRN
SQ  GSIKVGSGVLIKCKEHSILNVVGPRKGKHAAELLTKAYTFVFKQKGVPLMPLLSVGIFKVPITESLAAFLACVGDRVCKC
SQ  FCYTDKERLAIQNFVTSFQTEQPVEPLPVIQEVKGVQLEKPVPDVKVENPCEPFRIEGDAKFYDLTPSMVQSLQVTRLVS
SQ  FTNSDLCLGSFVRDCDGYVQGSLGGAIANYKKSNPVLPAGNCVTLKCDGFISFTFVILPKEGDTNYEKNFNRAIAKFLKL
SQ  KGSLLVVVEDSSVFNKISHASVAGYVAKPALVDTLFEAKPVQVVVTQDQRSFHTVELSTSQTYGQQLGDCVVEDKKVTNL
SQ  KPVSKDKVVSVVPNVDWDKHYGFVDAGIFHTLDHTMFVFDNNVVNGKRVLRTSDNNCWINAVCLQLQFANAKFKPKGLQQ
SQ  LWESYCTGDVAMFVHWLYWITGVEKGEPSDAENTLNIISRFLKPQGSVEMLRATSTTCDGTCSTKRVVSTPVVNASVLKV
SQ  GLDDGNCVHGLPLVDRVVSVNGTVIITNVGDTPGKPVVATENLLLDGVSYTVFQDSTTGVGHYTVFDKEAKLMFDGDVLK
SQ  PCDLNVSPVTSVVVCNNKKIVVQDPVKRVELDASKFLDTMNVASEKFFTFGDFVSRNIIVLIVYLFSLLAICFRALKKRD
SQ  MKVMAGVPERTGIILKRSVKYNYKALKFFFRLKFQYIKVFLKFSLVLYTLYALMFMFIRFTPVGTPICKRYTDGYANSTF
SQ  DKNDYCGNVLCKICLYGYEELSDFTHTRVIWQHLKDPLIGNILPLFYLVFLIIFGGFFVRIGITYFIMQYINAAGVALGY
SQ  QDNVWLLHLLPFNSMGNIIVVAFIVTRILLFLKHVLFGCDKPSCIACSKSAKLTRVPLQTILQGVTKSFYVNANGGKKFC
SQ  KKHNFFCVDCDSYGYGCTFINDVIAPELSNVTKLNVIPTGPATIIIDKVEFSNGFYYLYSGSTFWKYNFDITEAKYACKD
SQ  VLKNCNILTDFVVFNNSGSNVTQVKNACVYFSQLLCKPIKLVDSALLASLNVDFSANLHKAFVEVLSNSFGKDLSNCSNM
SQ  NECRESLGLSDVPEEEFSAAVSEAHRYDVLISDVSFNNLIVSYAKPEEKLAVHDIANCMRVGAKVVNHNVLTKDNVPVVW
SQ  LAKDFIALSEEARKYIVRTTKTKGINFMLTFNDRRMHLTIPTISVANKKGAGLPSLFTRLYSFFWHLCVLIVVLFVATSL
SQ  LDFSAQVTSDTQYDFKYIENGVLKVFEKPLDCVHNAFVNFNEWHNAKFGSIPTNSRRCPIVVGTSDEVRYIPGVPAGVFL
SQ  YGKSLIFAMSTIFGTSGLCFDDRGLTDPDSCIFNSACTTLSGIGGRNVYCYREGVVDNAKLYSSLLPHSYYRLMDGNHIV
SQ  LPEIITRGFGIRTIKTQAMTYCRTGECIDSQAGVCVGLDRFFVYSKTPGSDYVCGTGFFSLLFNVIGMFSNSIPVTVMSG
SQ  QILLNCVVAFTAVMACFAFTKFKRLFGDMSFGVLSVGLCTVVNNLSYVVTQNSIGMLAYATLYFLCTKGVRYSWVWHVGF
SQ  AISYCFLAPWWVVLAYLICALLEFLPNLFKLKVSTQLFEGDKFVGSFESAASGTFVLDMHSYQKLANSISTEKLKQYCAS
SQ  YNRYKYYSGSASEADYRLACFAHLAKAMSDFANDHMDKLYTPPTVSYNSTLQAGLRKMAQPSGIVEGCIVRVSYGNLTLN
SQ  GLWLGDTVICPRHVIASNTTNVIDYDHAMSLVRLHNFSISSGNMFLGVISASMRGTLLHIKVNQSNVNTPNYTYKVLKPG
SQ  DSFNILACYDGSAAGVYGVNMRTNYTIRGSFISGACGSPGYNINNGVVEFCYMHHLELGSGCHVGSDMDGTMYGKYEDQP
SQ  TLQIEGASNLVTENVCSWLYGALINGDRWWLSSVSVGVDTYNEWALRNGMTALKNVDCFSLLVAKTGVDVGRLLASIQKL
SQ  HGNFGGKSILGCTSLCDEFTLSEVVKQMYGVTLQSGKVSRAFRNASIVCCLLFLFLSEMLNHSKLFWINPGYITPVFLAI
SQ  IVASSALMLLVKHKLLFLQLYLLPSLCIVSGYNIFKDYHFYTYMLEEFDYKVPFGGFNVTGVLNISLCCFVMGLHTFRFL
SQ  QTPNKIFSYVVAVLTVLYTYYYSTDVLGLILTSMSGFTNYWFIGTATYKLATYVLPHTSLLDSFDAIKAVVFLYLLLGYC
SQ  NCVYYGSLYWINRFCKLTLGCYEFKVSAAEFKYMVANGLRAPTGVFDALILSLKLIGVGGRKTIKISSVQSKLTDLKCTN
SQ  VVLLGCLSNMNIAANSREWAYCVDLHNKINLCNDAEAAQEMLLALLAFFLSKNSAFGVDELLDSYFNDSSVLQSVAATYV
SQ  NLPSYLAYETARQSYEDALANGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAASQMYKEARAVNRKSKVVSAM
SQ  HSLLFGMLRRLDMSSVDTILSLAKDGVVPLSIIPAVSATKLNIVVSDIESYSKIQREGCVHYAGVIWSVVDIKDNDGKPV
SQ  HAKEVVTSNVESLAWPLFLNCERIIKLQNNEIIPSKIKQRPIKAEGEGVVADGNALYSNEGGRTFMYAFISDKPDLKVVK
SQ  WEFDGGSNAIELEPPCKFLVEAPSGPVVKYLYFVRNLNNLRRGAVLGFIGATVRLQAGKQTEQATNSSLLTLCAFAVDPP
SQ  KTYLDAVKSGHRPVGNCVKMLANGSGNGQAITNGVEASTNQDSYGGASVCLYCRAHVEHPDMDGFCKLRGKYVQVPLGTL
SQ  DPIRFVLENTVCKVCGCWQANGCTCDRAVIQSVDSGYLNRVRGSSAARLEPLNGSDTHHVFRAFDVYNRDVACISKFLKV
SQ  NCVRLKNLDKHDAFWIVKKCTKSVMEHEQSIYNLISDCGAVAKHDFFTWKEGRSVYGNVCRQDLTEYTMMDLCYALRNFD
SQ  ENNCETLKKILVVVGACDESYFDNKLWFDPVENEDVHRVYAKLGTIVARAMLKCVKYCDAMVEQGIVGVITLDNQDLNGD
SQ  FYDFGDFVTSVKGMGVPICTSYYSYMMPVMGMTNCLASECFIKSDIFGEDFRTFDLLAYDFTEHKVNLFNKYFKHWGQTY
SQ  HPNCEDCHDESCIVHCANFNTLFATTIPITAFGPLCRKCWIDGVPLVTTAGYHFKQLGIVWNKDLNLHSSRLTINELLQF
SQ  CADPSLLIASSPALVDKRTVCFSVAALGTGMTNQTVKPGHFNREFYDFLRSQGFFEEGSELTLKHFFFAQKGDAAVRDFD
SQ  YYRYNRTTVLDICQARVVYQIVQCYFGMYEGGCITAKEVIVNNLNKSAGYPFNKFGKAGLYYDSLSYEEQDDLYAYTKRN
SQ  IIPTMTQLNLKYAISGKDRARTVGGVSLLSTMTTRQYHQKHLKSIVNTRGASVVIGTTKFYGGWDNMLKTLIKDVENPHL
SQ  MGWDYPKCDRALPNMIRMISAMILGSKHVNCCSSSDRYYRLCNELAQVLTEMVYSNGGFYVKPGGTTSGDATTAYANSVF
SQ  NIFQATSANVNRLLSVDSNTCNNIEVKQLQRKLYDCCYRSSSVDQSFVEEYFGYLRKHFSMMILSDDGVVCYNSEYAALG
SQ  YVADLNAFKAVLYYQNNVFMSASKCWIEPDINKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGVFVDDIVKTDPVI
SQ  LLERYVSLAIDAYPLSKHDNPEYRRVFTVMLDWVKHLYKTLNQGVLDSFSVTLLEDATAKFWDESFYASMYEQSSVLQSA
SQ  GLCVVCSSQTVLRCGDCIRRPMLCTKCAYDHVVSTSHKFILAITPYVCCSSGCGVSDVTKLYLGGLSYWCVDHKPRLSFP
SQ  LCSSGNVFGLYKNSATGSPDVDDFNTLATSDWTDVKDYKLANDVKDSLRLFAAETIKAKEESVKSSYACATIHEVVGPKE
SQ  LVLKWEVGKPRPPLSRNSVFTCYHITKNTKFQVGEFTFEKLDYDNDAVSYKSTATTKLVPGMVFVLTSHNVQPLRAPTII
SQ  NQERYSTLHKLRPAFNIHEDYSNLIPYYQLIGKQKLTTIQGPPGSGKSHCVIGLGLYFPGARIVFTACSHAAVDSLCVKA
SQ  ATAYSSDRCSRIIPQKARIECYDGFKSNNTSAQYLFSTVNALPEVNADICVVDEVSMCTNYDLSVINQRVNYRHIVYVGD
SQ  PQQLPAPRVMITRGVLVPEDYNVVTRRMCVLKPDIFLHKCYRCPAEIVNTVSEMVYENQFVPVKSESKECFKIYCRGNVQ
SQ  VDNGSSINRRQLEVVRMFLAKNPKWAKAVFISPYNSQNYVAGRVLGLQIQTVDSSQGSEYDYVIYTQTSDTAHASNVNRF
SQ  NVAITRAKKGILCIMCDRELFDILKFYELKLSDLQVGDGCGLFKDCYKGEDNLPPSHAPTFMSLSDNFKTDKDLAVQIGV
SQ  NGPVKYEHVISFMGFRFDINVPNQHTLFCTRDFAMRNARGWLGFDVEGAHVIGSNVGTNVPLQLGFSNGVDFVVRPEGCV
SQ  STEVGDVIQPVRARAPPGDQFTHLLPLLRKGQPWSVIRRRIVQMCSDYLANLSDTLIFVLWSGGLELTTMRYFVKLGPVQ
SQ  TCDCGKRATCYNSTNHTFSCFRHALGSDYIYNCYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAAMTRCLAIHDCF
SQ  VKNVDWSITYPFIANEQAINKSGRLVQSHVMRAVLKLYNPKAIHDVGNPKGIRCVVTDASWYCYDKNPTNTNVKMLEYDY
SQ  ITHGQLDGLCLFWNCNVDMYPEFSVVCRFDTRMRSTLNLEGCNGGSLYVNNHAFHTPAYDKRAFAKLKAMPFFFYDDSEC
SQ  EKLQDAVNYVPLRASNCITRCNVGGAVCSKHCALYHNYVMAYNTFTTAGFTIWVPNSFDMFNLWQTFKNSNVQGLENIAY
SQ  NVVKKGSFVGVEGELPVAVVNDKVMVRDGVSDNVVFVNNTSLPTNVAFELYAKRKVGLTPPLTILKNLGVVCTSKCVLWD
SQ  YEASRPLTTFTKDVCKYTDFDGDVCTLFDNSVPGAFERFTVTKNAVLISLTAVKKLTAIKLTYGYLNGVPVFTHEDKPFT
SQ  WYIYTRKDGAFVEYPDGYFTQGRVISDFQPRSNMEEDFLNMDMGLFISKYGLEDYGFEHVVFGDVSKTTLGGLHLLISQI
SQ  RLSKIGVLKVEDFVSSSDSTLKSCTVTYVDNPSSKMVCTYVDLLLDDFVNILKSVDLSVVSKVHEVVIDCKVWRWMLWCK
SQ  DHKVQTFYPQLQSAEWKCGYSMPSIYKIQRMCLEPCNLYNYGSGLKLPDGIMFNVVKYTQLCQYLNSTTMCVPHHMRVLH
SQ  LGAGSDKGVAPGTAVLRRWLPLDAVIVDNDVNDYVSDADFSYTGDCASMYLTDKFDLVISDMYDGRTKSCDGDNVSKEGF
SQ  FPYINGVITEKLALGGTVAIKITEFSWNKKLYELIQKFEYWTLFCTSVNTSSSEAFLIGVHFLGDFSTNAIIDGNIMHAN
SQ  YIFWRNSTIMTMSYNSVLDLSKFSCKHKATVVVNLKDSSVTDLVLGLLKNGKLLIRNNGVVCGFSNHLVNSTK
//
ID  Q06502;
PN  Non-structural protein 12;
GN  rep;
OS  300015;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q06502;
DR  UNIPROT: Q06503;
DR  Pfam: PF16749;
DR  Pfam: PF12581;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The Nsp1 chain is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0070008;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSGFDRCLCTPNARVFWERGQVYCTRCLAARPLLPLSQQHPRLGALGLFYRPASPLSWEAPVTYPTKECRPGGMCWLSS
SQ  IYPIARMTSGNHNFQARLNFIASVVYRDGKLTSKHLEEDFEVYSRGCRWYPITGPVPGIALYANAVHVSDESFPGATHVL
SQ  SNLPLPQQPLRKGLCPFADARANVWRYKGNTVFVSPQGYLWTTGSNDSVPEPWGEDRRLCEKIISSLPADHLVKINFSNY
SQ  PFDYSFTGGDGAGFVVFPCKERDTKFSKCWEKIFEDHSGWMAACEEADLADRMGYRTPAGVAGPYLARRLQVRGLRAVVK
SQ  PENNDYIVWALGVPESYIRHVSRAGEPVEEFFVKVGEFSIVSNCVVTPHPKFRFQTRKYYGYSPPGDGACGLHCISAMLN
SQ  DIFGDSFTTRLGKCSRDSSEWLSDQDLYQLVMTANLPATIGHCPSAIYKLDCVNQHWTVTKRKGDRAVGRLAPDCLRGVC
SQ  GECEMGIHIGADTDLSPIVELQLAQDVSPRPGALLWFLELHELCVVDDDFAHAIARAGEEYRRAMGIPRDDWVILAELMT
SQ  ENCRTRHQVLEKLQRGLQLQASSRPSSPASVSPASSVDLSAAGLLLSGTESDKEAVVAVNDGCYTVLGFDKNEATKSEQD
SQ  LATDLFCDLVKPMETSTTKLESRKILEAAAKALESCKPKRKRSRKKKTRTPSPTCSVDAAVAEPTSVNSLGNQDTRETCA
SQ  SEKKAEKCPTPTPPPRPKRAALKNSNSGCVLKDIIWNQTGPGVKCLTIVEDVRAFLKGITPPGGVLSTRSRITKHIVDHF
SQ  HSICEQTPELVLAHAEHQAKNLHELLASETAKLILGIGEDPLKKLVGSQRSLPRRLGFGAWLGGQQKTSGGCGEREFKDV
SQ  GRKSGAERTPSKRDLGVSLGDQLSQDGARRLSSSTACEIKESVPPIIDSGGGLSQKFMAWLNHQVFVLSSHLLAVWSFIF
SQ  GSRQVLGVFDYVYTLFCLCCVLLCFYLPAIGFMTLVGCVFGSPWRVRLSVFSVWLCVAVVVFQEVLPEPGAVCTSASAER
SQ  AAALERYTSNGVHRPVNHLSVGLVGTVAGFVARSVGGPRRYWFYFLRLMVLLDLGLVFLAVALRGSCKKCFCKCVRTASH
SQ  EVQLRVFPSTKVARTTLEAICDMYSAPRVDPIFIATGVRGCWTGSVSPHQVTEKPVSYSNLDDKKISNKTVVPPPTDPQQ
SQ  AVRCLKVLQCGGSIQDVSVPEVKKVTKVPFKAPFFPNVTIDPECYIVVDPVTYSAAMRGGYGVSHLIVGLGDFAEVNGLR
SQ  FVSGGQIADFVCLGLYVLLNFLLSAWLSSPVSCGRGTNDPWCRNPFSYPVVGQGVMCNSHLCVAEDGLTSPMTLSYSLID
SQ  WALMVAIMATVAIFFAKISLLVDVVCVFCCLLMYAFPSLSIAAFGFPFVLCKVSLHPITLVWVQFFLLAVNVWAGVASVV
SQ  VLISSWFLARATSSLGLITPYDVHMITATPRGASSLASAPEGTYLAAVRRSALTGRCCMFVPTNFGSVLEGSLRTRGCAK
SQ  NVVSVFGSASGSGGVFTINGNPVVVTASHLLSDGKARVSCVGFSQCLDFKCAGDYAFARVANWKGDAPKAELSHRRGRAY
SQ  CSPLVGLSLDLLGKNSAFCFTKCGDSGSPVVDEDGNLLGIHTGSNKRGSGMVTTHGGKTLGMANVKLSEMCPHYSGPGVP
SQ  VSTVKLPKHLVVDVETVSSDLVAVVESLPALEGALSSMQLLCVFFFLWRLIHVPDVPVIRIAFFFLNEILPVMLARLMFS
SQ  FALSLFFCVHWLFCSSVAVAFGDCCSKSVTGYSVQVLLLRLVIAALNRPCGPFGFSLLGQLSQCCLMLCLLDIELQLLGC
SQ  LYLGQLLMWPPKEIFFHPTGQFMFLPLFLSLFKRNALADMLVGNGCFDAAFFLKYFAEGNLRDGVSDSCNMTPEGLTAAL
SQ  AITLSDDDLEFLQRHSEFKCFVSASNMRNGAKEFIESAYARALRAQLAATDKIKASKSILAKLESFAGGVVTQVEPGDVV
SQ  VVLGKKVIGDLVEVVINDAKHVIRVIETRTMAGTQFSVGTICGDLENACEDPSGLVKTSKKQARRQKRTGLGTEVVGTVV
SQ  IDGVSYNKVWHIATGDVTYEGCLVTENPQLRPLGMTTIGRFQEFIRKHGEKVKTSVEKYPVGKKKSVEFNITTYLLDGEE
SQ  YDVPDHEPLEWTITIGESDLEAERLTVDQALRHMGHDSLLTAKEKEKLARIIESLNGLQQASALNCLATSGLDRCTRGGL
SQ  TVSGDAVKLVRYHSRTFSIGDVNLKVMGREEYGRTVGKQGHCLVANLVDGVVVMRKHEPSLVDVLLTGEDADLISPTHGP
SQ  GNTGVHGFTWDFEAPPTDLELELSEQIITACSIRRGDAPSLDLPYKLHPVRGNPYRDRGVLYNTRFGDIKYLTPQKTKEP
SQ  LHAAACFNPKGVPVSDSETLVATTLPHGFELYVPTIPQSVLEYLDSRPMHRKCCVRAVVRGLAECDLQKFDLSRQGFVLP
SQ  GVLYMVRRYLCRLVGIRRRLFLPSTYPAKNSMAGINGNRFPTHVVQSHPDIDALCERACKEHWQTVTPCTLKKQYCSKAK
SQ  TRTILGTNNFVALGLRSALSGVTQGFMRKGIGSPICLGKNKFTPLPTKVSGRCLEADLASCDRSTPAIIRWFTTNLLFEL
SQ  AGPEEWIPSYVLNCCHDAVSTMSGCFDKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSAFRCGHKVGGLFLRDSLEMEQL
SQ  FELQPLLVYSDDVVLYDESSELPNYHFFVDHLDLMLGFKTDRSKTVITSDPQFPGCRIAAGRVLVPQRDRILAALAYHMK
SQ  ASCVSDYFASAAAILMDACACCDYDEDWYFDLVCGIADCARKEGFRFPGPSFYVDMWKRLSVEEKKKCRTCAHCGAPSTL
SQ  VSSCGLNLCDYHGHGHPHCPVVLPCGHAVGSGVCDGCSSPVMSLNTELDKLLACVPYHPPKVELLSVNDGVSSLPPGRYQ
SQ  ARGGVVSVRRDILGNVVDLPDGDYQVMKVAQTCADICMVSINSHILRSQFITGAPGTGKTTYLLSVVRDDDVIYTPTHRT
SQ  MLDVVKALGTCRFDPPKDTPLEFPVPSRTGPCVRLIRAGFIPGRVSYLDEAAYCNPLDVLKILSKTPLVCVGDLNQLPPV
SQ  DFIGPCYAFALMLGRQLIEVFRFGPSIVNPIKKFYREELVSRGPDTGVKFLKSYQPYGQVLTPYHRDRVDGAITIDSSQG
SQ  CTYDVITVYLPTPKSLNSARALVAITRARFYVFVYDPHNQLEQYLNMSEHEPAGAVAFWCGEQPMMISEGRVQRLSGPAQ
SQ  TTDPKLQQLMGLEGTASPLPQVAHNLGFYYSPDLVQFARIPSELCKHWPVVTAQNRTDWPDRLVCSMSKIDKCSRAIFCA
SQ  GYHVGPSVFLGVPGVVSYYLTKFLKGKPVPLPDSLMSTGRIALNVREYLDEKEMEFSSRCPHAFIGEVKGSNVGGCHHVT
SQ  SRYLPPVLVPGSVVKIGVSCPGKAAKELCTVTDVYLPELDPYLNPPTKSMDYKLLVDFQPVKLMVWKDATAYFHEGIRPM
SQ  ESMSRFLKVPQEEGVFFDLDEFVTNAKVSKLPCKYSVSANQFLTDVVLSMTHPSLAPPDYELLFARAYCVPGLDVGTLNA
SQ  YIYRRGPSTYTTSNIARLVKDICCPVGCKGSGYMFPK
//
ID  Q80UM3;
PN  N-alpha-acetyltransferase 15, NatA auxiliary subunit;
GN  Naa15;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton- bound polysomes, but not in the membrane-bound polysomes. {ECO:0000250}.
DR  UNIPROT: Q80UM3;
DR  UNIPROT: Q811Z9;
DR  UNIPROT: Q9JID5;
DR  Pfam: PF12569;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:10842358, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564, ECO:0000269|PubMed:15452080}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9GZZ1; IntAct: EBI-2554211,EBI-1052523; Score: 0.40
DE  Interaction: Q9BXJ9; IntAct: EBI-2554211,EBI-1042540; Score: 0.40
DE  Interaction: Q9NX55; IntAct: EBI-2554211,EBI-1048743; Score: 0.40
DE  Interaction: P41227; IntAct: EBI-2554211,EBI-747693; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031415;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005667;
GO  GO:0008080;
GO  GO:0043022;
GO  GO:0001525;
GO  GO:0030154;
GO  GO:0017196;
GO  GO:0006474;
GO  GO:0043066;
GO  GO:0045893;
GO  GO:0050821;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSH
SQ  VCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHL
SQ  LEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRL
SQ  EDAADVYRGLQERNPGNWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDRFLRMNFSK
SQ  GCPPVFNTLRSLYRDKEKVAIVEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTA
SQ  IESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYVLKANLIKEAEEMCSKFTREGTSAVENLN
SQ  EMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARI
SQ  AIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKE
SQ  ELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSGHPWLHECMIRLFHSVC
SQ  ESKDLPETVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDSSSQKRAIELATTLDGSLTNRNLQT
SQ  CMEVLEALCDGSLGDCKEAAEAYRASCHKLFPYALAFMPPGYEEDMKITVNGDSSAETEELANEI
//
ID  Q66T02;
PN  Pleckstrin homology domain-containing family G member 5;
GN  Plekhg5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16467373}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell membrane {ECO:0000269|PubMed:16467373}. Cell junction {ECO:0000269|PubMed:21543326}. Cell projection, lamellipodium {ECO:0000269|PubMed:21543326}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane (PubMed:16467373). Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells (PubMed:21543326). {ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:21543326}.
DR  UNIPROT: Q66T02;
DR  UNIPROT: A2A8B6;
DR  UNIPROT: A2A8B7;
DR  UNIPROT: Q66T00;
DR  UNIPROT: Q6P3B1;
DR  UNIPROT: Q6ZQ62;
DR  UNIPROT: Q8R571;
DR  Pfam: PF00621;
DR  PROSITE: PS50010;
DR  PROSITE: PS50003;
DE  Function: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (PubMed:29084947). Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis (PubMed:21543326). Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (By similarity). {ECO:0000250|UniProtKB:O94827, ECO:0000269|PubMed:21543326, ECO:0000269|PubMed:29084947}.
DE  Reference Proteome: Yes;
DE  Interaction: P35294; IntAct: EBI-6552478,EBI-9079953; Score: 0.35
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005089;
GO  GO:0035767;
GO  GO:0043542;
GO  GO:0099575;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGTGPGVSGRRAAARPSSELPSPDSQLLWVGGHAHSSDSQVCHHADCQQLHHRGPLNLCETCDSKFHSTLHYDGHVRFDL
SQ  PPQGSVLARNVSTRSCPPRTSPAADLEEEEEGCTDGKGDRKSAGLKISKKKARRRHTDDPSKECFTLKFDLNVDIETEIV
SQ  PAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAKPGDEGKVEQGVKDSKSLSLPALRP
SQ  SGAGPPVSERVDPQSRRESSLDILAPGRRRKNMSEFLGEAGIPGHEPPAPSSCSLPVGSSGGTSSGINESWKNRAASRFS
SQ  GFFSSSPSTSAFSREVDKMEQLESKLHAYSLFGLPRMPRRLRFDHDSWEEEEEDDEEDEESSGLRLEDSWRELTDGHEKL
SQ  TRRQCHQQEAVWELLHTEVSYIRKLRVITNLFLCCLLNLQESGLLCEVEAERLFSNIPEIAKLHRGLWGSVMVPVLEKAR
SQ  RTRALLQPSDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYVTWAEKHQQCQRLKLSDMLAKPHQRLTK
SQ  YPLLLKSVLRKTDDPRTKEAIVTMISSVERFIHHVNTCMRQRQERQRLAGVVSRIDAYEVVEGSNDEVDKLLKEFLHLDL
SQ  TAPMPGTSPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTKVIRPPLLVDKIVCRELRDPGSFLLI
SQ  YLNEFHSAVGAYTFQASSQALCRSWVDTIYNAQNQLQQLRAQLSAQEHPGSQHLQSLEEEEDEQEEEGEESGTSAASSPT
SQ  ILRKSSNSLDSEHCTSDGSTETLAMVVVEPGATLSSPEFEGGPVSSQSDESSLSNTASSVTPTSELLPLGPVDGRSCSMD
SQ  SAYGTLSPTSLQDFVAPHPVVEPAPVPQTPSPQPSPRLRRRTPVQLLPRPPRLLKSKSEASLLQLLSGTPAARGVPPAPS
SQ  RSLSELCLISVAPGVRTQRPLQEGGPGWNGPGMCDPCHGPQLSESENRPSHMTGGPADSARRRCREMPSGTMSRVQSEPP
SQ  SGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV
//
ID  P10909;
PN  Clusterin alpha chain;
GN  CLU;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Secreted {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:24073260, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8328966}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. {ECO:0000269|PubMed:17451556}. [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:24073260}. Note=Keeps cytoplasmic localization in stressed and unstressed cell. {ECO:0000269|PubMed:24073260}. [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:24073260}. Note=Keeps cytoplasmic localization in stressed and unstressed cell. {ECO:0000269|PubMed:24073260}. Nucleus {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:19137541}. Cytoplasm {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:17689225}. Cytoplasm, cytosol {ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}. Microsome {ECO:0000269|PubMed:22689054}. Endoplasmic reticulum {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:22689054}. Mitochondrion {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:22689054}. Mitochondrion membrane {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17689225}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250}. Note=Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress (PubMed:17451556). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (PubMed:20068069). Detected at the mitochondrion membrane upon induction of apoptosis (PubMed:17689225). Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction (PubMed:22689054). ER stress reduces secretion (PubMed:22689054). Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm (PubMed:24073260, PubMed:22689054, PubMed:17451556). Non-secreted forms emerge mainly from failed translocation, alternative splicing or non-canonical initiation start codon (PubMed:24073260, PubMed:12551933). {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}.
DR  UNIPROT: P10909;
DR  UNIPROT: B2R9Q1;
DR  UNIPROT: B3KSE6;
DR  UNIPROT: P11380;
DR  UNIPROT: P11381;
DR  UNIPROT: Q2TU75;
DR  UNIPROT: Q5HYC1;
DR  UNIPROT: Q7Z5B9;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DR  OMIM: 185430;
DR  DisGeNET: 1191;
DE  Function: [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17412999, PubMed:17407782). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX- dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12882985, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:19996109, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:21505792, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260, ECO:0000269|PubMed:2780565}. [Isoform 6]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. {ECO:0000269|PubMed:24073260}. [Isoform 4]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405). {ECO:0000269|PubMed:21567405, ECO:0000269|PubMed:24073260}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-1104674,EBI-1104674; Score: 0.37
DE  Interaction: P62993; IntAct: EBI-1104674,EBI-401755; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1104674; Score: 0.35
DE  Interaction: Q9H4B6; IntAct: EBI-1104674,EBI-1017775; Score: 0.37
DE  Interaction: Q92610; IntAct: EBI-1210420,EBI-1104674; Score: 0.37
DE  Interaction: Q9Y2B5; IntAct: EBI-9031083,EBI-1104674; Score: 0.37
DE  Interaction: P31321; IntAct: EBI-2805516,EBI-1104674; Score: 0.37
DE  Interaction: Q9NPF5; IntAct: EBI-399105,EBI-1104674; Score: 0.37
DE  Interaction: Q58WW2; IntAct: EBI-2559044,EBI-1104674; Score: 0.37
DE  Interaction: Q6NUQ1; IntAct: EBI-726876,EBI-1104674; Score: 0.37
DE  Interaction: Q9BXM7; IntAct: EBI-2846068,EBI-1104674; Score: 0.37
DE  Interaction: Q07890; IntAct: EBI-298181,EBI-1104674; Score: 0.37
DE  Interaction: Q99615; IntAct: EBI-357552,EBI-1104674; Score: 0.37
DE  Interaction: P26640; IntAct: EBI-355765,EBI-1104674; Score: 0.37
DE  Interaction: Q15059; IntAct: EBI-1383460,EBI-1104674; Score: 0.37
DE  Interaction: Q9C093; IntAct: EBI-1220460,EBI-1104674; Score: 0.37
DE  Interaction: Q9H974; IntAct: EBI-1221028,EBI-1104674; Score: 0.37
DE  Interaction: Q96MT8; IntAct: EBI-741977,EBI-1104674; Score: 0.37
DE  Interaction: Q14515; IntAct: EBI-2682673,EBI-1104674; Score: 0.37
DE  Interaction: Q96K75; IntAct: EBI-6660752,EBI-1104674; Score: 0.37
DE  Interaction: Q9Y6D5; IntAct: EBI-2837511,EBI-1104674; Score: 0.37
DE  Interaction: Q15185; IntAct: EBI-1049387,EBI-1104674; Score: 0.37
DE  Interaction: Q9UBU8; IntAct: EBI-399246,EBI-1104674; Score: 0.37
DE  Interaction: Q96PY5; IntAct: EBI-3438448,EBI-1104674; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-1104674,EBI-529989; Score: 0.55
DE  Interaction: Q06787; IntAct: EBI-1104674,EBI-366305; Score: 0.37
DE  Interaction: Q9UKE5; IntAct: EBI-1104674,EBI-1051794; Score: 0.55
DE  Interaction: P11766; IntAct: EBI-717798,EBI-1104674; Score: 0.37
DE  Interaction: Q7Z699; IntAct: EBI-5235340,EBI-1104674; Score: 0.37
DE  Interaction: P14868; IntAct: EBI-358730,EBI-1104674; Score: 0.37
DE  Interaction: P36957; IntAct: EBI-351007,EBI-1104674; Score: 0.37
DE  Interaction: Q7Z698; IntAct: EBI-7082156,EBI-1104674; Score: 0.37
DE  Interaction: Q9UL68; IntAct: EBI-1105008,EBI-1104674; Score: 0.37
DE  Interaction: O75592; IntAct: EBI-1043774,EBI-1104674; Score: 0.37
DE  Interaction: Q86TG7; IntAct: EBI-2858265,EBI-1104674; Score: 0.37
DE  Interaction: P02794; IntAct: EBI-713259,EBI-1104674; Score: 0.37
DE  Interaction: Q6AI39; IntAct: EBI-1012434,EBI-1104674; Score: 0.37
DE  Interaction: Q6GYQ0; IntAct: EBI-3957100,EBI-1104674; Score: 0.37
DE  Interaction: Q96EK5; IntAct: EBI-744150,EBI-1104674; Score: 0.37
DE  Interaction: Q00994; IntAct: EBI-741753,EBI-1104674; Score: 0.37
DE  Interaction: F8VWT9; IntAct: EBI-21378194,EBI-1104674; Score: 0.37
DE  Interaction: Q13439; IntAct: EBI-1037845,EBI-1104674; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-352572,EBI-1104674; Score: 0.37
DE  Interaction: P07900; IntAct: EBI-296047,EBI-1104674; Score: 0.37
DE  Interaction: Q6ZMI3; IntAct: EBI-21379491,EBI-1104674; Score: 0.37
DE  Interaction: Q5SZL2; IntAct: EBI-2514702,EBI-1104674; Score: 0.37
DE  Interaction: P26367; IntAct: EBI-747278,EBI-1104674; Score: 0.37
DE  Interaction: Q9NR80; IntAct: EBI-3389984,EBI-1104674; Score: 0.37
DE  Interaction: Q9UBW8; IntAct: EBI-712982,EBI-1104674; Score: 0.37
DE  Interaction: Q9Y575; IntAct: EBI-2875625,EBI-1104674; Score: 0.37
DE  Interaction: P48426; IntAct: EBI-3924422,EBI-1104674; Score: 0.37
DE  Interaction: Q9BZ95; IntAct: EBI-3390132,EBI-1104674; Score: 0.37
DE  Interaction: Q9NVR2; IntAct: EBI-536703,EBI-1104674; Score: 0.37
DE  Interaction: Q9NWB6; IntAct: EBI-2808785,EBI-1104674; Score: 0.37
DE  Interaction: Q5VTB9; IntAct: EBI-949963,EBI-1104674; Score: 0.37
DE  Interaction: P53041; IntAct: EBI-716663,EBI-1104674; Score: 0.37
DE  Interaction: Q9Y275; IntAct: EBI-519169,EBI-1104674; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-1564650,EBI-1104674; Score: 0.35
DE  Interaction: Q9NRD1; IntAct: EBI-3938499,EBI-1104674; Score: 0.35
DE  Interaction: P17028; IntAct: EBI-1104674,EBI-707773; Score: 0.40
DE  Interaction: P01100; IntAct: EBI-852851,EBI-1104674; Score: 0.52
DE  Interaction: P37231; IntAct: EBI-781384,EBI-1104674; Score: 0.52
DE  Interaction: P02866; IntAct: EBI-2905940,EBI-1104674; Score: 0.35
DE  Interaction: P22736; IntAct: EBI-1104674,EBI-721550; Score: 0.40
DE  Interaction: Q00987; IntAct: EBI-1104674,EBI-389668; Score: 0.40
DE  Interaction: P04150; IntAct: EBI-493507,EBI-1104674; Score: 0.40
DE  Interaction: O35638; IntAct: EBI-2552452,EBI-1104674; Score: 0.40
DE  Interaction: P16104; IntAct: EBI-494830,EBI-1104674; Score: 0.35
DE  Interaction: O15160; IntAct: EBI-1104674,EBI-1055079; Score: 0.37
DE  Interaction: P05181; IntAct: EBI-1104674,EBI-3907388; Score: 0.37
DE  Interaction: Q99708; IntAct: EBI-1104674,EBI-745715; Score: 0.37
DE  Interaction: O14901; IntAct: EBI-948266,EBI-1104674; Score: 0.37
DE  Interaction: Q14145; IntAct: EBI-1104674,EBI-751001; Score: 0.37
DE  Interaction: Q9Y3Q8; IntAct: EBI-739485,EBI-1104674; Score: 0.37
DE  Interaction: P51114-2; IntAct: EBI-1104674,EBI-11022345; Score: 0.35
DE  Interaction: P30101; IntAct: EBI-1104674,EBI-979862; Score: 0.59
DE  Interaction: Q96HP0; IntAct: EBI-1104674,EBI-4401295; Score: 0.35
DE  Interaction: Q7Z333-3; IntAct: EBI-1104674,EBI-11025482; Score: 0.35
DE  Interaction: Q5VW52; IntAct: EBI-1104674,EBI-10973822; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-1104674,EBI-355947; Score: 0.35
DE  Interaction: Q07817-1; IntAct: EBI-1104674,EBI-287195; Score: 0.40
DE  Interaction: Q9BWU1; IntAct: EBI-394593,EBI-1104674; Score: 0.35
DE  Interaction: P45984; IntAct: EBI-1104674,EBI-713568; Score: 0.37
DE  Interaction: P62829; IntAct: EBI-1104674,EBI-353303; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-1104674,EBI-347552; Score: 0.37
DE  Interaction: P02647; IntAct: EBI-701692,EBI-1104674; Score: 0.35
DE  Interaction: P01876; IntAct: EBI-727651,EBI-1104674; Score: 0.35
DE  Interaction: P01857; IntAct: EBI-356114,EBI-1104674; Score: 0.35
DE  Interaction: P27918; IntAct: EBI-9038570,EBI-1104674; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-985879,EBI-1104674; Score: 0.66
DE  Interaction: A0A1J9WIU5; IntAct: EBI-1104674,EBI-2811961; Score: 0.37
DE  Interaction: P03428; IntAct: EBI-2547475,EBI-1104674; Score: 0.35
GO  GO:0097440;
GO  GO:0072562;
GO  GO:0009986;
GO  GO:0042583;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0097418;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0031093;
GO  GO:0032991;
GO  GO:0034366;
GO  GO:0045202;
GO  GO:0001540;
GO  GO:0051087;
GO  GO:0050750;
GO  GO:0051787;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0048156;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0019730;
GO  GO:0000902;
GO  GO:0032286;
GO  GO:0051131;
GO  GO:0061077;
GO  GO:0061741;
GO  GO:0006956;
GO  GO:0006958;
GO  GO:0002434;
GO  GO:0045087;
GO  GO:0097193;
GO  GO:0006629;
GO  GO:0001774;
GO  GO:0061518;
GO  GO:1905907;
GO  GO:1902430;
GO  GO:0060548;
GO  GO:1905892;
GO  GO:1905895;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0090201;
GO  GO:1903573;
GO  GO:0002576;
GO  GO:1905908;
GO  GO:1902004;
GO  GO:0043065;
GO  GO:0010628;
GO  GO:2001244;
GO  GO:1902998;
GO  GO:1901216;
GO  GO:0051092;
GO  GO:0045429;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0048260;
GO  GO:1902949;
GO  GO:0032760;
GO  GO:2000060;
GO  GO:0017038;
GO  GO:0050821;
GO  GO:0061740;
GO  GO:1900221;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:0030449;
GO  GO:1901214;
GO  GO:1902847;
GO  GO:0001836;
GO  GO:0051788;
GO  GO:0009615;
GO  GO:0043691;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKK
SQ  KEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRID
SQ  SLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNF
SQ  HAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQ
SQ  AKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPS
SQ  GVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE
//
ID  Q9LH52;
PN  Leucine-rich repeat protein FLOR 1;
GN  FLR1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|Ref.7}. Nucleus {ECO:0000269|Ref.7}. Cytoplasm, perinuclear region {ECO:0000269|Ref.7}. Cell membrane {ECO:0000269|Ref.7}. Note=In carpels, observed both in cytoplasm and nucleus, as well as in the perinuclear and cell membrane in a vesicle-like pattern. In style cells, present in cytoplasm as well as in nucleus possibly in the perinuclear membrane. In leaf tissue, observed in the plasma membrane and in the perinuclear membrane. In roots and tapetum cells, restricted to the cytoplasm. {ECO:0000269|Ref.7}.
DR  UNIPROT: Q9LH52;
DR  UNIPROT: Q93ZC1;
DR  UNIPROT: Q9C7D9;
DR  UNIPROT: Q9M7E7;
DR  Pfam: PF13516;
DR  Pfam: PF08263;
DE  Function: Promotes flowering transition in long days (LD). {ECO:0000269|PubMed:22319055}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0008134;
GO  GO:0048574;
GO  GO:0048510;
GO  GO:0010228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLFVHLSIFFSILFITLPSSYSCTENDKNALLQIKKALGNPPLLSSWNPRTDCCTGWTGVECTNRRVTGLSVTSGEVSG
SQ  QISYQIGDLVDLRTLDFSYLPHLTGNIPRTITKLKNLNTLYLKHTSLSGPIPDYISELKSLTFLDLSFNQFTGPIPGSLS
SQ  QMPKLEAIQINDNKLTGSIPNSFGSFVGNVPNLYLSNNKLSGKIPESLSKYDFNAVDLSGNGFEGDAFMFFGRNKTTVRV
SQ  DLSRNMFNFDLVKVKFARSIVSLDLSQNHIYGKIPPALTKLHLEHFNVSDNHLCGKIPSGGLLQTFEPSAFAHNICLCGT
SQ  PLKAC
//
ID  Q9H7Z7;
PN  Prostaglandin E synthase 2 truncated form;
GN  PTGES2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:12835322}; Single-pass membrane protein {ECO:0000255}. [Prostaglandin E synthase 2 truncated form]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12835322}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region. {ECO:0000269|PubMed:12835322}.
DR  UNIPROT: Q9H7Z7;
DR  UNIPROT: Q53EW9;
DR  UNIPROT: Q5SYV6;
DR  UNIPROT: Q96GI0;
DR  UNIPROT: Q96GL2;
DR  Pfam: PF13417;
DR  PROSITE: PS00195;
DR  PROSITE: PS51354;
DR  PROSITE: PS50405;
DR  OMIM: 608152;
DR  DisGeNET: 80142;
DE  Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2). {ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:18198127}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5VU69; IntAct: EBI-10247920,EBI-681645; Score: 0.56
DE  Interaction: P16104; IntAct: EBI-494830,EBI-681645; Score: 0.35
DE  Interaction: O75208; IntAct: EBI-724524,EBI-681645; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-1049381,EBI-681645; Score: 0.35
DE  Interaction: Q9C002; IntAct: EBI-3905285,EBI-681645; Score: 0.35
DE  Interaction: E9PK12; IntAct: EBI-21644263,EBI-681645; Score: 0.35
DE  Interaction: Q8N140; IntAct: EBI-744483,EBI-681645; Score: 0.35
DE  Interaction: Q6UWI4; IntAct: EBI-11343474,EBI-681645; Score: 0.35
DE  Interaction: Q0VDI3; IntAct: EBI-17555467,EBI-681645; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-681645; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-466029,EBI-681645; Score: 0.40
DE  Interaction: Q5NFN4; IntAct: EBI-681645,EBI-2796796; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-447544,EBI-681645; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25475871,EBI-681645; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-681645; Score: 0.35
DE  Interaction: Q13296-2; IntAct: EBI-21513440,EBI-681645; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-954063,EBI-681645; Score: 0.35
DE  Interaction: P80370; IntAct: EBI-21555397,EBI-681645; Score: 0.35
DE  Interaction: Q9UG63; IntAct: EBI-2959697,EBI-681645; Score: 0.35
DE  Interaction: O60518; IntAct: EBI-1055771,EBI-681645; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-1046087,EBI-681645; Score: 0.35
DE  Interaction: O14949; IntAct: EBI-720294,EBI-681645; Score: 0.35
DE  Interaction: Q01780; IntAct: EBI-681645,EBI-358236; Score: 0.37
GO  GO:0035578;
GO  GO:0005623;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0009055;
GO  GO:0043295;
GO  GO:0020037;
GO  GO:0016829;
GO  GO:0050220;
GO  GO:0015035;
GO  GO:0045454;
GO  GO:0019371;
GO  GO:0043312;
GO  GO:0045893;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHL
SQ  RAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQ
SQ  QLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
SQ  WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGK
SQ  DRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
//
ID  P05783;
PN  Keratin, type I cytoskeletal 18;
GN  KRT18;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus, nucleolus.
DR  UNIPROT: P05783;
DR  UNIPROT: Q53G38;
DR  UNIPROT: Q5U0N8;
DR  UNIPROT: Q9BW26;
DR  Pfam: PF00038;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  OMIM: 148070;
DR  OMIM: 215600;
DR  DisGeNET: 3875;
DE  Function: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.
DE  Disease: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension. {ECO:0000269|PubMed:12724528, ECO:0000269|PubMed:9011570}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-357515,EBI-297888; Score: 0.35
DE  Interaction: O75190; IntAct: EBI-297888,EBI-1053164; Score: 0.62
DE  Interaction: P01112; IntAct: EBI-297888,EBI-350145; Score: 0.37
DE  Interaction: Self; IntAct: EBI-297888,EBI-297888; Score: 0.37
DE  Interaction: Q8NFJ9; IntAct: EBI-297888,EBI-1805484; Score: 0.44
DE  Interaction: Q96RK4; IntAct: EBI-297888,EBI-1805814; Score: 0.44
DE  Interaction: Q9BXC9; IntAct: EBI-297888,EBI-748297; Score: 0.44
DE  Interaction: Q8IWZ6; IntAct: EBI-1806001,EBI-297888; Score: 0.44
DE  Interaction: Q15628; IntAct: EBI-359215,EBI-297888; Score: 0.60
DE  Interaction: P05787; IntAct: EBI-297888,EBI-297852; Score: 0.94
DE  Interaction: Q99816; IntAct: EBI-297888,EBI-346882; Score: 0.67
DE  Interaction: Q9BQ69; IntAct: EBI-297888,EBI-5324932; Score: 0.65
DE  Interaction: P13569; IntAct: EBI-349854,EBI-297888; Score: 0.53
DE  Interaction: Q14108; IntAct: EBI-1564650,EBI-297888; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-297888,EBI-352682; Score: 0.37
DE  Interaction: Q96CS2; IntAct: EBI-297888,EBI-2514791; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-297888; Score: 0.78
DE  Interaction: P61981; IntAct: EBI-297888,EBI-359832; Score: 0.37
DE  Interaction: Q8NFA0; IntAct: EBI-2511075,EBI-297888; Score: 0.40
DE  Interaction: P28799; IntAct: EBI-297888,EBI-747754; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-297888,EBI-81279; Score: 0.57
DE  Interaction: Q14094; IntAct: EBI-297888,EBI-1104653; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-297888,EBI-752420; Score: 0.49
DE  Interaction: Q9D7I8; IntAct: EBI-11048238,EBI-297888; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-349105,EBI-297888; Score: 0.35
DE  Interaction: Q8IYE0-2; IntAct: EBI-10247802,EBI-297888; Score: 0.56
DE  Interaction: P15336; IntAct: EBI-1170906,EBI-297888; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-297888; Score: 0.53
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-297888; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-1046878,EBI-297888; Score: 0.44
DE  Interaction: Q5VU43; IntAct: EBI-297888,EBI-1105124; Score: 0.44
DE  Interaction: P52292; IntAct: EBI-349938,EBI-297888; Score: 0.37
DE  Interaction: O43913; IntAct: EBI-374928,EBI-297888; Score: 0.37
DE  Interaction: Q96GM5; IntAct: EBI-297888,EBI-358489; Score: 0.37
DE  Interaction: Q92837; IntAct: EBI-3934879,EBI-297888; Score: 0.37
DE  Interaction: Q99757; IntAct: EBI-2932492,EBI-297888; Score: 0.37
DE  Interaction: Q6PKC3; IntAct: EBI-749812,EBI-297888; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-297888,EBI-473160; Score: 0.37
DE  Interaction: Q96MU7; IntAct: EBI-2849854,EBI-297888; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-297888,EBI-447295; Score: 0.37
DE  Interaction: Q99459; IntAct: EBI-297888,EBI-374880; Score: 0.37
DE  Interaction: P02671; IntAct: EBI-348571,EBI-297888; Score: 0.37
DE  Interaction: P27348; IntAct: EBI-359854,EBI-297888; Score: 0.37
DE  Interaction: P05452; IntAct: EBI-297888,EBI-1047626; Score: 0.40
DE  Interaction: P23508; IntAct: EBI-297888,EBI-307531; Score: 0.40
DE  Interaction: O75688; IntAct: EBI-297888,EBI-1047039; Score: 0.40
DE  Interaction: Q9BVR6; IntAct: EBI-741889,EBI-297888; Score: 0.37
DE  Interaction: P19012; IntAct: EBI-297888,EBI-739566; Score: 0.55
DE  Interaction: O14964; IntAct: EBI-740220,EBI-297888; Score: 0.78
DE  Interaction: Q9Y5B8; IntAct: EBI-744782,EBI-297888; Score: 0.67
DE  Interaction: O95751; IntAct: EBI-740738,EBI-297888; Score: 0.37
DE  Interaction: Q8IYI6; IntAct: EBI-742102,EBI-297888; Score: 0.37
DE  Interaction: Q15834; IntAct: EBI-739674,EBI-297888; Score: 0.37
DE  Interaction: A0A087WXM9; IntAct: EBI-297888,EBI-20740139; Score: 0.40
DE  Interaction: P08670; IntAct: EBI-297888,EBI-353844; Score: 0.40
DE  Interaction: Q5HYC2; IntAct: EBI-297888,EBI-948754; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-297888,EBI-297903; Score: 0.40
DE  Interaction: Q96M95; IntAct: EBI-297888,EBI-747041; Score: 0.40
DE  Interaction: Q12860; IntAct: EBI-297888,EBI-5564336; Score: 0.40
DE  Interaction: Q8WWL7; IntAct: EBI-297888,EBI-767764; Score: 0.40
DE  Interaction: P48668; IntAct: EBI-2564105,EBI-297888; Score: 0.68
DE  Interaction: Q9NY99; IntAct: EBI-8556870,EBI-297888; Score: 0.40
DE  Interaction: Q66PJ3; IntAct: EBI-297888,EBI-2683099; Score: 0.40
DE  Interaction: Q8WYP5; IntAct: EBI-297888,EBI-396018; Score: 0.40
DE  Interaction: Q8IYB4; IntAct: EBI-297888,EBI-15749355; Score: 0.40
DE  Interaction: P01730; IntAct: EBI-297888,EBI-353826; Score: 0.40
DE  Interaction: Q9Y616; IntAct: EBI-297888,EBI-447690; Score: 0.40
DE  Interaction: Q5JVL4; IntAct: EBI-297888,EBI-743105; Score: 0.56
DE  Interaction: A0A0S2Z505; IntAct: EBI-297888,EBI-16437709; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-297888,EBI-475646; Score: 0.56
DE  Interaction: A0A0S2Z4Q4; IntAct: EBI-297888,EBI-16429135; Score: 0.56
DE  Interaction: Q9NX04; IntAct: EBI-8643161,EBI-297888; Score: 0.56
DE  Interaction: P02538; IntAct: EBI-297888,EBI-702198; Score: 0.56
DE  Interaction: Q3SY84; IntAct: EBI-297888,EBI-2952676; Score: 0.56
DE  Interaction: Q14533; IntAct: EBI-297888,EBI-739648; Score: 0.56
DE  Interaction: Q8TD31-3; IntAct: EBI-297888,EBI-10175300; Score: 0.56
DE  Interaction: Q9P2K3-2; IntAct: EBI-297888,EBI-1504830; Score: 0.56
DE  Interaction: Q9BVG8-5; IntAct: EBI-297888,EBI-14069005; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-297888,EBI-750487; Score: 0.56
DE  Interaction: Q5XKE5; IntAct: EBI-297888,EBI-2514135; Score: 0.56
DE  Interaction: O75022; IntAct: EBI-2830524,EBI-297888; Score: 0.43
DE  Interaction: Q8N0S2; IntAct: EBI-6872807,EBI-297888; Score: 0.56
DE  Interaction: P62993; IntAct: EBI-401755,EBI-297888; Score: 0.35
DE  Interaction: P29353; IntAct: EBI-297888,EBI-78835; Score: 0.27
GO  GO:0005912;
GO  GO:0071944;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005882;
GO  GO:0045095;
GO  GO:0005815;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0098641;
GO  GO:0003723;
GO  GO:0097110;
GO  GO:0005198;
GO  GO:0009653;
GO  GO:0007049;
GO  GO:0070268;
GO  GO:0097191;
GO  GO:0043000;
GO  GO:0097284;
GO  GO:0045104;
GO  GO:0031424;
GO  GO:0043066;
GO  GO:0033209;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNE
SQ  KETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLA
SQ  ADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAP
SQ  KSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASL
SQ  ENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSN
SQ  SMQTIQKTTTRRIVDGKVVSETNDTKVLRH
//
ID  P32336;
PN  Protein NUD1;
GN  NUD1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10330408}. Nucleus envelope {ECO:0000269|PubMed:10330408}. Note=Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
DR  UNIPROT: P32336;
DR  UNIPROT: D6W366;
DR  UNIPROT: Q08895;
DR  PROSITE: PS51450;
DE  Function: Involved in astral microtubule organization by binding SCP72 to the outer plaque in a cell-cycle dependent manner. Required for the mitotic exit by facilitating the binding of TEMP1 to CDC15. Also involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. {ECO:0000269|PubMed:11101520}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-20589,EBI-12361; Score: 0.35
DE  Interaction: Q12411; IntAct: EBI-36275,EBI-12361; Score: 0.55
DE  Interaction: Q08550; IntAct: EBI-34513,EBI-12361; Score: 0.51
DE  Interaction: Q00684; IntAct: EBI-4192,EBI-12361; Score: 0.35
DE  Interaction: P14832; IntAct: EBI-5463,EBI-12361; Score: 0.35
DE  Interaction: P53865; IntAct: EBI-29172,EBI-12361; Score: 0.35
DE  Interaction: P32472; IntAct: EBI-2883297,EBI-12361; Score: 0.35
DE  Interaction: Q02796; IntAct: EBI-30514,EBI-12361; Score: 0.35
DE  Interaction: P38265; IntAct: EBI-21579,EBI-12361; Score: 0.35
DE  Interaction: P38890; IntAct: EBI-24263,EBI-12361; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-12361; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-12361,EBI-8603; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-12361,EBI-8627; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-17244,EBI-12361; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-12361,EBI-3949; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-12361; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-31563,EBI-12361; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-3824,EBI-12361; Score: 0.35
DE  Interaction: P39723; IntAct: EBI-20675,EBI-12361; Score: 0.35
DE  Interaction: Q04477; IntAct: EBI-27228,EBI-12361; Score: 0.35
DE  Interaction: P32337; IntAct: EBI-9159,EBI-12361; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-12361,EBI-19749; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0061499;
GO  GO:0043014;
GO  GO:0045504;
GO  GO:0003774;
GO  GO:0035591;
GO  GO:0030953;
GO  GO:0051301;
GO  GO:0051293;
GO  GO:0000073;
GO  GO:0045132;
GO  GO:0031536;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMDTQEAELSSQLENLTINSPRKLRSNAHSNSGKVFKEYESNHDFQDSNFTSQVVEPAISDSVKKPPTMTVLNNYSTVH
SQ  QKVPSGFSGTTATSHQEAQWKQYFPGIGSGGGTNFGGAVGTANKVPESDLIVSDLVKDLSGVLETNTFKRHLDMKNKTTT
SQ  MQTHENHDTISISHSKDFFNAEKVSSSFSDDSDSGPAAEAHDVFDGILQKQKSNYLVGSYPSNSNNKNNNNNNNNNNNNS
SQ  ININNKDNARTKEEDEEDTSNSFEFSSSSSMSSSQTQSGRKSKVLKKPPLNTISPGQLGYQFNHTHGAWDPPLNQGLDVS
SQ  SSHSLDNTSSNQSQFATMVPTGDNHTNGKAPSILDKKAYELTSTKPGDVGYRQKKIQEEENLANSDDTPLDTPKFNDLFT
SQ  KNGTRAKVKGQMRTSRSISNSNLLEAHKKLKTFPAERVEDITSISEVNTSFNETEKQLISILTSKLSGSPSYDSDWEKIL
SQ  KVDLSRGKLKNMFGMQRLLPNVLVLNLSDNEMNTLEGIPSNVVQLFCSNNKITSAHCSLAGFHDLECLDLSYNLLNTSLK
SQ  FLSLCHHLQEVNLSYNSIQSLEGIGSSRMKKLNLSNNEINGIIDFEQLILTNNSVVGGWLTVEVLDLSNNNIIGVRNINC
SQ  LPRLKVLNLNGNPLVSIVESSKMENGTLRALSIKNTGGALSKLQNYKLDDQFTFPYQNLKILKLDGFAQLSKWQKWPATL
SQ  QILEINGGLASSLPRFSSLKSTNLYSLTIANVRDFTHLPVDLSKELPFLQELHLPGNNLQNAHKLTKTLPRQSVKFLDLR
SQ  NNPITTPRHDRASTSLHYRQLLQLAGLCQQQCPALATLWLDDTPAPTATNL
//
ID  Q9SXA1;
PN  Phosphatidylinositol 4-kinase alpha 1;
GN  PI4KA1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:12805633}; Peripheral membrane protein {ECO:0000269|PubMed:12805633}; Cytoplasmic side {ECO:0000269|PubMed:12805633}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12805633}.
DR  UNIPROT: Q9SXA1;
DR  UNIPROT: O81129;
DR  Pfam: PF00454;
DR  Pfam: PF00613;
DR  PROSITE: PS00915;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DE  Function: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,- trisphosphate. Can bind to phosphatidylinositol 4-monophosphate (PI-4-P or PtdIns4P), phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2 or PtdIns4,5P2), and phosphatidic acid (PtdOH), but not to 3- phosphoinositides. May function upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway. {ECO:0000269|PubMed:22318862, ECO:0000269|PubMed:9712908}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0004430;
GO  GO:0051015;
GO  GO:0070300;
GO  GO:0052742;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0046854;
GO  GO:0048015;
GO  GO:0006468;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12805633};
SQ  MEALTELCDIIAKNPKQFSEKLAWICGRCPQTEWLLAESPRVSRSHLNAVLAVARIISKNPESIDNRAKSVVNEFLSAIP
SQ  ASFRRSFWPHSFPSQLISSFYCDFLSYLSCAADLSPEFGTEVARFTGEVVIAAIAPSSGDSDGDPAISKAFLVALSQHFP
SQ  SILQSDGDKLITMLLDQFVLNRAPASPKEQRQQNSANSETDTSSSQGSPISTNRYPSGKTEMASPGDEVASHGSNLSSKS
SQ  SSSVVMNGGSIVWKSGVDQLSFGFSEGSGGANPVFRQQVASFEDESIESLEKQEIAFRLITHILDKVKIDSKLQDQVRFI
SQ  AKRQLQSMSAFLKSRKRDWNEQGQVLKTRVNAKLSVYQAAAKMKIKSLVSLETDGKTSKRLVLETLALLLDAADACLTSV
SQ  WRKMKACEELFDSLLSGIAKIAVARGGQPLRVLLIRLKPLVLAVCALPDQGAMLESIFKTSCVIIESAWAKDRAPVDNFI
SQ  MGLASSIRERNDYEEQVDREKQVPAVQLNVIRLLADLNVAVKKPEVADMILPLFIESLEEGDASTPSFLRLQLLDAVSRI
SQ  ATLGFDKSYRETVVLMTRSYLSKLSSVGSVESKTSAPEATTERVETLPAGFLTIASGLMDTKLRSDYRHRLLSLCSDVGL
SQ  AAESKSGGSGVDFLGPLLPAVAEICSDFDPTMDVEPSLLKLFRNLWFYIALFGLAPPIVKTPTPPLKSTSNSVNSVGSMS
SQ  ATALQAVGGPYMWDNQWALAVQRIAQGTPPLVVSSVKWLEDELELNALHNPGSRRGNGNEKVASTQRLALSTALGGRVDV
SQ  AAMNTISGVKATYLLAVAFLEIIRFISNGGILNGESSVSASRSAFSCVFEYLKTPNLTPAVSQCLTAIVHRAFETAVSWL
SQ  EDRISLTGKDARNRELTTYAHACFLIKSMSQRDEHVRDISVNLLTQLRDKFPQVLWHSSCLDSLLFSVHDNTPSTVVNDP
SQ  AWTAAVRSLYQKVVREWIIISLSYAPCTSQGLLQDKLCKANTWQRAQTTTDVVSLLSEIKIGTGKNELWSGIRTANIPAV
SQ  MAAAAAASGANLKVSEAFNLEVLGTGVVSATVKCNHAGEIAGMRRLYNSIGGFQSGSTPSGFGGGLQRLISGAFSQAPQP
SQ  EDDSFNEMLIARFVRLLQQFVNTAEKGGEVEKSQFRETCSQATALLLSNLGGESKTNVEGFSQLLRLLCWCPAYISTPDA
SQ  METGIFIWTWLVSAAPQLVSLVLAELVDAWIWTIDTKRGLFASDVRYSGPAAKLRPHLSPGEPEDPPESDPVDQIVAHRL
SQ  WLGFLIDRFEVVRHNSAEQLLLLGRMLQRSTDLEWCFTRHPAAAGTFFSLMLLGLKFCSCQTQGNMQKFRSGLQLLEDRI
SQ  YRTSLGWFAHQPEWYDVNIPNFCHSEALSVSVFVHFLSNELSESSQSDSKGKPRESGNLIDVTDQYHPVWGEMDNYTLGK
SQ  EKRKQLLLMLCQHEADRLDVWAQPISSKDSPYSRLKISSEKWTEYAKTAFSVDPRIALSVASRFPANASVKSEVTQLVQT
SQ  NIVDLRTIPEALPYFVTPKNVEENSVLLQQLPHWAACSITQALEFLTPAYKGHPRVMAYVLRVLESYPPERVTFFMPQLV
SQ  QSLRYDDGRLVEGYLLRATQRSDIFAHILIWHLQGEDVQETPKDGSIDKNAAFQEILPQVRQHIIDGFSPNALDMFTREF
SQ  DFFDKVTSISGVLFPLPKEERRAGIRRELEKIEMQGDDLYLPTAPNKLVRGIRVDSGIPLQSAAKVPIMITFNVIDRDGD
SQ  HSDVKPQACIFKVGDDCRQDVLALQVISLLRDIFQAAGLNLYLFPYGVLPTGAERGIIEVVPNTRSRSQMGETTDGGLYE
SQ  IFQQDYGPVGSTTFETARENFLISSAGYAVASLLLQPKDRHNGNLLFDDVGRLVHIDFGFILETSPGGNMRFESAHFKLS
SQ  HEMTQLLDPSGVMKSKTWHQFVSLCVKGYLAARRQMDGIISTVQMMLESGLPCFSRGDPIGNLRKRFHPEMSEREAAHFM
SQ  IHVCTDAYNKWTTAGYDLIQYLQQGIEK
//
ID  P11147;
PN  Heat shock 70 kDa protein cognate 4;
GN  Hsc70;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress.
DR  UNIPROT: P11147;
DR  UNIPROT: Q3KN45;
DR  UNIPROT: Q8SXQ4;
DR  UNIPROT: Q9VFB0;
DR  Pfam: PF00012;
DR  PROSITE: PS00297;
DR  PROSITE: PS00329;
DR  PROSITE: PS01036;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q24133; IntAct: EBI-75181,EBI-87640; Score: 0.37
DE  Interaction: P83949; IntAct: EBI-75181,EBI-202590; Score: 0.48
DE  Interaction: P25439; IntAct: EBI-868480,EBI-75181; Score: 0.40
DE  Interaction: Q9VRQ2; IntAct: EBI-75181,EBI-169350; Score: 0.37
DE  Interaction: Q03751; IntAct: EBI-75181,EBI-604931; Score: 0.27
DE  Interaction: Q9XZC2; IntAct: EBI-75181,EBI-458892; Score: 0.37
DE  Interaction: Q24570; IntAct: EBI-75181,EBI-167445; Score: 0.37
DE  Interaction: Q9VZF4; IntAct: EBI-75181,EBI-138334; Score: 0.37
DE  Interaction: Q9VWE4; IntAct: EBI-75181,EBI-122539; Score: 0.37
DE  Interaction: Q9VML8; IntAct: EBI-75181,EBI-152952; Score: 0.37
DE  Interaction: Q9VU81; IntAct: EBI-75181,EBI-179238; Score: 0.37
DE  Interaction: Q8IRH9; IntAct: EBI-75181,EBI-162060; Score: 0.37
DE  Interaction: Q9VLG9; IntAct: EBI-75181,EBI-86290; Score: 0.37
DE  Interaction: Q24216; IntAct: EBI-139668,EBI-75181; Score: 0.37
DE  Interaction: Q9VNE0; IntAct: EBI-75181,EBI-159712; Score: 0.37
DE  Interaction: Q9I7H9; IntAct: EBI-139392,EBI-75181; Score: 0.37
DE  Interaction: Q9VRQ6; IntAct: EBI-75181,EBI-194555; Score: 0.37
DE  Interaction: Q9VC50; IntAct: EBI-75181,EBI-85761; Score: 0.37
DE  Interaction: Q9W5G1; IntAct: EBI-75181,EBI-103112; Score: 0.37
DE  Interaction: Q9V3F2; IntAct: EBI-75181,EBI-90755; Score: 0.37
DE  Interaction: Q9XYW6; IntAct: EBI-75181,EBI-135209; Score: 0.37
DE  Interaction: P40301; IntAct: EBI-98978,EBI-75181; Score: 0.37
DE  Interaction: Q7JXC4; IntAct: EBI-75181,EBI-151216; Score: 0.37
DE  Interaction: Q9VUQ1; IntAct: EBI-75181,EBI-162539; Score: 0.37
DE  Interaction: Q9W0B2; IntAct: EBI-75181,EBI-89242; Score: 0.37
DE  Interaction: Q5BI03; IntAct: EBI-102987,EBI-75181; Score: 0.37
DE  Interaction: Q9VRV9; IntAct: EBI-181097,EBI-75181; Score: 0.37
DE  Interaction: Q9VIJ0; IntAct: EBI-75181,EBI-94912; Score: 0.37
DE  Interaction: P29413; IntAct: EBI-75181,EBI-192552; Score: 0.37
DE  Interaction: Q8IR79; IntAct: EBI-149780,EBI-75181; Score: 0.37
DE  Interaction: Q9W3N7; IntAct: EBI-75181,EBI-95849; Score: 0.37
DE  Interaction: Q9VIY9; IntAct: EBI-75181,EBI-82519; Score: 0.37
DE  Interaction: Q9VJB0; IntAct: EBI-75181,EBI-152945; Score: 0.37
DE  Interaction: Q9VMA3; IntAct: EBI-75181,EBI-95398; Score: 0.37
DE  Interaction: Q9VNV2; IntAct: EBI-75181,EBI-172319; Score: 0.37
DE  Interaction: Q9VI55; IntAct: EBI-75181,EBI-172922; Score: 0.37
DE  Interaction: O96757; IntAct: EBI-74922,EBI-75181; Score: 0.37
DE  Interaction: Q9VLI5; IntAct: EBI-75181,EBI-154623; Score: 0.37
DE  Interaction: Q9VVC2; IntAct: EBI-75181,EBI-141024; Score: 0.37
GO  GO:0071013;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0005726;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0071011;
GO  GO:0098793;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042623;
GO  GO:0051087;
GO  GO:0031072;
GO  GO:0051787;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0035967;
GO  GO:0034620;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0070868;
GO  GO:0061738;
GO  GO:0097753;
GO  GO:0000398;
GO  GO:0007399;
GO  GO:0007269;
GO  GO:0030707;
GO  GO:0106161;
GO  GO:0006457;
GO  GO:0042026;
GO  GO:0006986;
GO  GO:0016246;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDD
SQ  AAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKD
SQ  AGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTH
SQ  FVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKA
SQ  LRDAKLDKSVIHDIVLVGGSTRIPKVQRLLQDLFNGKELNKSINPDEAVAYGAAVQAAILHGDKSQEVQDLLLLDVTPLS
SQ  LGIETAGGVMSVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDI
SQ  DANGILNVTALERSTNKENKITITNDKGRLSKEDIERMVNEAEKYRNEDEKQKETIAAKNGLESYCFNMKATLDEDNLKT
SQ  KISDSDRTTILDKCNETIKWLDANQLADKEEYEHRQKELEGVCNPIITKLYQGAGFPPGGMPGGPGGMPGAAGAAGAAGA
SQ  GGAGPTIEEVD
//
ID  Q9N1F0;
PN  Protein MRVI1;
GN  MRVI1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Sarcoplasmic reticulum {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10724174}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9N1F0;
DR  UNIPROT: Q9N1E9;
DR  Pfam: PF05781;
DE  Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO- dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:10724174, ECO:0000269|PubMed:16166082}.
DE  Reference Proteome: Yes;
DE  Interaction: P00516-2; IntAct: EBI-10094470,EBI-10094531; Score: 0.44
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKAPQSEERLAGGGKGNNSVLACGAQASWSIFGADAAEVPGTRSHSRQEAAMPHIPEDEEPPGEPQAAQSPAGQDPATT
SQ  GISCSPPTIILTGDASSPEGETDKNPVNRAHSPHRRLSHRHLKVSTASLTSVDPAGHVIDLVNDQLPDISISEEDKKKNL
SQ  ALLEEAKLVSERFLTRRGRKSRSSPGESSPAVSPNLSPGASPASSQSNSLTVPTPPGLDVCSGPPSPLPGAPPQKGDEAE
SQ  VPSPHLGESNVLKGLADRKQNDQRTLSQGRLTARSPTVEKSKEITIEQKENFDPLQRPEAIPKGPASGPGSGGKMALNSP
SQ  QPGPVESELGKPLAKTAKEGNPLPRGPTQGSGGVAPQASQGKSTVGEPAGSKVGSKAELWPPTSRPPLLRGVSWDSGPEE
SQ  PGPRLQKVLAKLPLAEEEKRFTGKAGSKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILLRNQNLVGLKLPELSEAAEQE
SQ  KGHPSELSSAIEEEESKGGLDVMPNISDVLLRKLRVHKSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERE
SQ  RNLTEENTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEMVGAVRQEKRMSKATEVMMQYVE
SQ  NLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLSLGKNMPRRRVSVAVVPKFNILNLPGQSPSSSPIPS
SQ  LPALSESSNGKGNPPVSSALPALLENGKTNGDPDCEASASVPTPSCLEGISQEAKARMEEEAYNKGYQEGLKKTKELQGL
SQ  REEEEEQKSESPEEPEEVAETEEEEKEQRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAAMLVLTVVLGLYGSHNSCVEQ
SQ  ADGSLGKSTCSAAQRDSWWSSGLQHEQPTEQ
//
ID  P80303;
PN  Nesfatin-1;
GN  NUCB2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:11749975}. Membrane {ECO:0000269|PubMed:11749975}; Peripheral membrane protein {ECO:0000269|PubMed:11749975}. Cytoplasm {ECO:0000269|PubMed:11749975}. Secreted {ECO:0000269|PubMed:11749975}. Endoplasmic reticulum {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Golgi retention is mediated by its N-terminal region. [Nesfatin-1]: Secreted.
DR  UNIPROT: P80303;
DR  UNIPROT: A8K642;
DR  UNIPROT: D3DQX5;
DR  UNIPROT: Q8NFT5;
DR  UNIPROT: V9HW75;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 608020;
DR  DisGeNET: 4925;
DE  Function: Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity). {ECO:0000250|UniProtKB:P81117, ECO:0000250|UniProtKB:Q9JI85}. [Nesfatin-1]: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance. {ECO:0000250|UniProtKB:Q9JI85}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99IB8; IntAct: EBI-6927928,EBI-2296670; Score: 0.37
DE  Interaction: Q3KSU8; IntAct: EBI-2621128,EBI-2296670; Score: 0.37
DE  Interaction: Q2MV58; IntAct: EBI-11333674,EBI-2296670; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-2296670; Score: 0.35
DE  Interaction: Q9NQH7; IntAct: EBI-1171467,EBI-2296670; Score: 0.35
DE  Interaction: O75489; IntAct: EBI-1224896,EBI-2296670; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-2296670; Score: 0.35
DE  Interaction: Q96GM5; IntAct: EBI-358489,EBI-2296670; Score: 0.37
DE  Interaction: O14980; IntAct: EBI-2296670,EBI-355867; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-448167,EBI-2296670; Score: 0.51
DE  Interaction: P08754; IntAct: EBI-2296670,EBI-357563; Score: 0.37
DE  Interaction: P84996; IntAct: EBI-2680244,EBI-2296670; Score: 0.37
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0070062;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0003677;
GO  GO:0001965;
GO  GO:0005085;
GO  GO:0032099;
GO  GO:0007264;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11749975};
SQ  MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADI
SQ  EEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIK
SQ  AATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLD
SQ  PNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLK
SQ  ATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK
SQ  LQQGIPPSGPAGELKFEPHI
//
ID  Q9NUU6;
PN  Inactive ubiquitin thioesterase OTULINL;
GN  OTULINL;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:31056421}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31056421}; Peripheral membrane protein {ECO:0000269|PubMed:31056421}. Nucleus envelope {ECO:0000269|PubMed:31056421}.
DR  UNIPROT: Q9NUU6;
DR  UNIPROT: Q53H50;
DR  UNIPROT: Q9H037;
DR  PDB: 6DRM;
DR  Pfam: PF16218;
DR  DisGeNET: 54491;
DE  Function: Lacks deubiquitinase activity. {ECO:0000269|PubMed:31056421}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NUH8; IntAct: EBI-8638294,EBI-6916492; Score: 0.56
DE  Interaction: Q6ZVE7; IntAct: EBI-6916492,EBI-17231387; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-10262251,EBI-6916492; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-6447886,EBI-6916492; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-2548832,EBI-6916492; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-10266796,EBI-6916492; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-13059134,EBI-6916492; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-1052304,EBI-6916492; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-10192441,EBI-6916492; Score: 0.56
DE  Interaction: Q02223; IntAct: EBI-519945,EBI-6916492; Score: 0.35
GO  GO:0005737;
GO  GO:0042406;
GO  GO:0005635;
GO  GO:0006508;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:31056421};
SQ  MAATRSPTRARERERSGAPAAGSDQVHSWMLATSQALDTVWRMAKGFVMLAVSFLVAAICYFRRLHLYSGHKLKWWIGYL
SQ  QRKFKRNLSVEAEVDLLSYCAREWKGETPRNKLMRKAYEELFWRHHIKCVRQVRRDNYDALRSVLFQIFSQGISFPSWMK
SQ  EKDIVKLPEKLLFSQGCNWIQQYSFGPEKYTGSNVFGKLRKYVELLKTQWTEFNGIRDYHKRGSMCNTLFSDAILEYKLY
SQ  EALKFIMLYQVTEVYEQMKTKKVIPSLFRLLFSRETSSDPLSFMMNHLNSVGDTCGLEQIDMFILGYSLEVKIKVFRLFK
SQ  FNSRDFEVCYPEEPLRDWPEISLLTENDRHYHIPVF
//
ID  F7EQ49;
PN  G-protein coupled estrogen receptor 1;
GN  GPER1;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Endocytosed in a agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer- associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes (By similarity). {ECO:0000250}.
DR  UNIPROT: F7EQ49;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells (By similarity). Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. {ECO:0000250, ECO:0000269|PubMed:19131510}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0016323;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0030425;
GO  GO:0043198;
GO  GO:0044327;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0098686;
GO  GO:0099055;
GO  GO:0099056;
GO  GO:0045095;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0048786;
GO  GO:0042734;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0003682;
GO  GO:0030284;
GO  GO:0004930;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0003707;
GO  GO:0007189;
GO  GO:0030263;
GO  GO:0007049;
GO  GO:0071392;
GO  GO:0071333;
GO  GO:0071389;
GO  GO:0071375;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0030518;
GO  GO:0071157;
GO  GO:0008285;
GO  GO:0051053;
GO  GO:0070373;
GO  GO:0045599;
GO  GO:0010629;
GO  GO:0050728;
GO  GO:0002695;
GO  GO:0051055;
GO  GO:0051898;
GO  GO:1904706;
GO  GO:0019228;
GO  GO:0030264;
GO  GO:0043065;
GO  GO:0097755;
GO  GO:2000724;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0043280;
GO  GO:0007204;
GO  GO:2000353;
GO  GO:0045742;
GO  GO:0070374;
GO  GO:2001238;
GO  GO:0045745;
GO  GO:0010628;
GO  GO:0032962;
GO  GO:0032024;
GO  GO:0043410;
GO  GO:0050769;
GO  GO:0001956;
GO  GO:0014068;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0090200;
GO  GO:0051281;
GO  GO:0045944;
GO  GO:0070474;
GO  GO:0051480;
GO  GO:0043401;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILI
SQ  LVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALA
SQ  RAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRV
SQ  LVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLN
SQ  PLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV
//
ID  Q8BLR9;
PN  Hypoxia-inducible factor 1-alpha inhibitor;
GN  Hif1an;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}.
DR  UNIPROT: Q8BLR9;
DR  UNIPROT: A1L3B7;
DR  UNIPROT: Q3U3G4;
DR  Pfam: PF13621;
DR  PROSITE: PS51184;
DE  Function: Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000250|UniProtKB:Q9NWT6, ECO:0000269|PubMed:17636018}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016706;
GO  GO:0071532;
GO  GO:0031406;
GO  GO:0048037;
GO  GO:0102113;
GO  GO:0005506;
GO  GO:0051059;
GO  GO:0005112;
GO  GO:0036140;
GO  GO:0036139;
GO  GO:0042803;
GO  GO:0008270;
GO  GO:0045746;
GO  GO:0061428;
GO  GO:0055114;
GO  GO:0042265;
GO  GO:0042264;
GO  GO:0036138;
GO  GO:0045663;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
SQ  LQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVM
SQ  DFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQS
SQ  QVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMR
SQ  NIEKMLGEALGNPQEVGPLLNTMIKGRYN
//
ID  O14770;
PN  Homeobox protein Meis2;
GN  MEIS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}.
DR  UNIPROT: O14770;
DR  UNIPROT: A6NJI5;
DR  UNIPROT: A8MWD5;
DR  UNIPROT: B3KP98;
DR  UNIPROT: B3KPQ6;
DR  UNIPROT: Q96DI2;
DR  UNIPROT: Q96KI4;
DR  UNIPROT: Q96KI5;
DR  UNIPROT: Q9NRS1;
DR  UNIPROT: Q9NRS2;
DR  UNIPROT: Q9NRS3;
DR  PDB: 3K2A;
DR  PDB: 4XRM;
DR  PDB: 5BNG;
DR  PDB: 5EG0;
DR  Pfam: PF05920;
DR  Pfam: PF16493;
DR  PROSITE: PS50071;
DR  OMIM: 600987;
DR  OMIM: 601740;
DR  DisGeNET: 4212;
DE  Function: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription. {ECO:0000269|PubMed:10764806, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:21746878}.
DE  Disease: Cleft palate, cardiac defects, and mental retardation (CPCMR) [MIM:600987]: An autosomal dominant disease characterized by multiple congenital malformations, mild-to-severe intellectual disability with poor speech, and delayed psychomotor development. Congenital malformations include heart defects, cleft lip/palate, distally-placed thumbs and toes, and cutaneous syndactyly between the second and third toes. {ECO:0000269|PubMed:24678003, ECO:0000269|PubMed:25712757, ECO:0000269|PubMed:27225850}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-2804934,EBI-2804934; Score: 0.37
DE  Interaction: A0A1B0GWI1; IntAct: EBI-2804934,EBI-10181422; Score: 0.56
DE  Interaction: Q5TZZ9; IntAct: EBI-2804934,EBI-10181435; Score: 0.56
DE  Interaction: Q6P1W5; IntAct: EBI-2804934,EBI-946029; Score: 0.56
DE  Interaction: Q9UJX0; IntAct: EBI-9057006,EBI-2804934; Score: 0.67
DE  Interaction: Q5NG24; IntAct: EBI-2804934,EBI-2803358; Score: 0.37
GO  GO:0000790;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0043565;
GO  GO:0003712;
GO  GO:0003714;
GO  GO:0008134;
GO  GO:0001654;
GO  GO:0045638;
GO  GO:0000122;
GO  GO:0031016;
GO  GO:0110024;
GO  GO:0045931;
GO  GO:0045944;
GO  GO:0070848;
GO  GO:0009612;
GO  GO:0006366;
GO  GO:0008542;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAI
SQ  YGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLE
SQ  LEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGH
SQ  ASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTI
SQ  LQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGM
SQ  SMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMMMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
//
ID  Q9ESN9;
PN  C-Jun-amino-terminal kinase-interacting protein 3;
GN  Mapk8ip3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10629060}. Golgi apparatus {ECO:0000269|PubMed:11106729}. Cytoplasmic vesicle {ECO:0000269|PubMed:11106729}. Cell projection, growth cone {ECO:0000269|PubMed:10629060}. Cell projection, axon {ECO:0000269|PubMed:25944905}. Cell projection, dendrite {ECO:0000250|UniProtKB:E9PSK7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PSK7}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells (PubMed:10629060, PubMed:11106729). KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation (By similarity). {ECO:0000250|UniProtKB:E9PSK7, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729}.
DR  UNIPROT: Q9ESN9;
DR  UNIPROT: Q5D062;
DR  UNIPROT: Q99KU7;
DR  UNIPROT: Q9EQD8;
DR  UNIPROT: Q9ESN7;
DR  UNIPROT: Q9ESN8;
DR  UNIPROT: Q9ESP0;
DR  UNIPROT: Q9JLH2;
DR  UNIPROT: Q9JLH3;
DR  UNIPROT: Q9R0U7;
DR  PDB: 6EJN;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (PubMed:10523642, PubMed:10629060). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner (PubMed:23576431, PubMed:25944905, PubMed:28259553). Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation (PubMed:23576431, PubMed:25944905, PubMed:28259553). Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration (PubMed:23576431, PubMed:25944905, PubMed:28259553). Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development (PubMed:23576431, PubMed:25944905, PubMed:28259553). Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation (PubMed:23576431, PubMed:25944905, PubMed:28259553). {ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905, ECO:0000269|PubMed:28259553}.
DE  Reference Proteome: Yes;
DE  Interaction: P63101; IntAct: EBI-354751,EBI-301496; Score: 0.35
DE  Interaction: O88704; IntAct: EBI-8766347,EBI-301496; Score: 0.35
DE  Interaction: Q80VP2; IntAct: EBI-20567308,EBI-301496; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-301496,EBI-5323863; Score: 0.40
DE  Interaction: O88448; IntAct: EBI-301496,EBI-301558; Score: 0.68
DE  Interaction: O88447; IntAct: EBI-301496,EBI-301550; Score: 0.72
GO  GO:0030673;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0000139;
GO  GO:0030426;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005790;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0030159;
GO  GO:0007257;
GO  GO:0099641;
GO  GO:0061564;
GO  GO:0007411;
GO  GO:0031103;
GO  GO:0030900;
GO  GO:0001701;
GO  GO:0007254;
GO  GO:0048286;
GO  GO:0060425;
GO  GO:0043507;
GO  GO:0045666;
GO  GO:2001224;
GO  GO:0009791;
GO  GO:0008104;
GO  GO:0010468;
GO  GO:0046328;
GO  GO:0007585;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVEL
SQ  ELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKE
SQ  YNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLG
SQ  QLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEV
SQ  QVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDE
SQ  GADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKEL
SQ  EEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASR
SQ  EHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSAR
SQ  REQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWK
SQ  PHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQ
SQ  FTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVA
SQ  TTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGE
SQ  LSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHL
SQ  MDLGHPHHSIRCMAVVNDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTH
SQ  QHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTR
SQ  PGGIIHVYGDDSSDKAASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKL
SQ  KNALVLSGGEGYIDFRIGDGEDDETEECAGDVNQTKPSLSKAERSHIIVWQVSYTPE
//
ID  Q769K2;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  Napepld;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
DR  UNIPROT: Q769K2;
DR  Pfam: PF12706;
DE  Function: Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of these bioactive fatty acid ethanolamides (FAEs), including anandamide (N-arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (PubMed:14634025, PubMed:16527816). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (By similarity). {ECO:0000250|UniProtKB:Q8BH82, ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043227;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0004620;
GO  GO:0008270;
GO  GO:0007568;
GO  GO:0048874;
GO  GO:0070291;
GO  GO:0070292;
GO  GO:1903999;
GO  GO:0009395;
GO  GO:0006644;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0035900;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q6IQ20};
SQ  MDENENSQSPAPSHQYPKETLRKRQNSVQNSGGSESSRLSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNVSIPNV
SQ  LRWLIMEKDHSSVPGSKEELDKELPVLKPYFISDPEEAGVREAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPSQYM
SQ  GPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
SQ  HDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ
SQ  HADPEDAVRIHIDVQAKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLKSEDFFILKHGESRYLNTDDKAFEET
//
ID  Q02821;
PN  Importin subunit alpha;
GN  SRP1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Mainly localized at the periphery of the nucleus.
DR  UNIPROT: Q02821;
DR  UNIPROT: D6W0Z8;
DR  PDB: 1BK5;
DR  PDB: 1BK6;
DR  PDB: 1EE4;
DR  PDB: 1EE5;
DR  PDB: 1UN0;
DR  PDB: 1WA5;
DR  PDB: 2C1T;
DR  PDB: 4PVZ;
DR  PDB: 4XZR;
DR  PDB: 5H2W;
DR  PDB: 5H2X;
DR  PDB: 5T94;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity). {ECO:0000250, ECO:0000269|PubMed:10913188, ECO:0000269|PubMed:21075847, ECO:0000269|PubMed:7565597}.
DE  Reference Proteome: Yes;
DE  Interaction: P20591; IntAct: EBI-1797,EBI-929476; Score: 0.56
DE  Interaction: P20676; IntAct: EBI-12392,EBI-1797; Score: 0.69
DE  Interaction: P32499; IntAct: EBI-1797,EBI-12401; Score: 0.78
DE  Interaction: P34160; IntAct: EBI-745,EBI-1797; Score: 0.69
DE  Interaction: P39705; IntAct: EBI-20731,EBI-1797; Score: 0.69
DE  Interaction: P40069; IntAct: EBI-1797,EBI-9166; Score: 0.53
DE  Interaction: P32562; IntAct: EBI-4440,EBI-1797; Score: 0.53
DE  Interaction: Q08904; IntAct: EBI-32829,EBI-1797; Score: 0.37
DE  Interaction: P53184; IntAct: EBI-1797,EBI-23741; Score: 0.37
DE  Interaction: P51601; IntAct: EBI-1797,EBI-7429; Score: 0.37
DE  Interaction: P25367; IntAct: EBI-21708,EBI-1797; Score: 0.37
DE  Interaction: P08536; IntAct: EBI-10753,EBI-1797; Score: 0.37
DE  Interaction: Q03063; IntAct: EBI-29752,EBI-1797; Score: 0.37
DE  Interaction: P17423; IntAct: EBI-9685,EBI-1797; Score: 0.37
DE  Interaction: P60010; IntAct: EBI-1797,EBI-2169; Score: 0.37
DE  Interaction: P38821; IntAct: EBI-6008,EBI-1797; Score: 0.37
DE  Interaction: Q02895; IntAct: EBI-1797,EBI-35030; Score: 0.37
DE  Interaction: Q12306; IntAct: EBI-17490,EBI-1797; Score: 0.37
DE  Interaction: Q06549; IntAct: EBI-1797,EBI-4455; Score: 0.37
DE  Interaction: P32318; IntAct: EBI-1797,EBI-19215; Score: 0.37
DE  Interaction: P43619; IntAct: EBI-11793,EBI-1797; Score: 0.37
DE  Interaction: Q03373; IntAct: EBI-34019,EBI-1797; Score: 0.55
DE  Interaction: P09201; IntAct: EBI-1797,EBI-6744; Score: 0.37
DE  Interaction: Q12189; IntAct: EBI-15898,EBI-1797; Score: 0.37
DE  Interaction: P15202; IntAct: EBI-4061,EBI-1797; Score: 0.37
DE  Interaction: P18759; IntAct: EBI-1797,EBI-16565; Score: 0.37
DE  Interaction: P38716; IntAct: EBI-24682,EBI-1797; Score: 0.37
DE  Interaction: Q12206; IntAct: EBI-1797,EBI-20571; Score: 0.37
DE  Interaction: P33307; IntAct: EBI-5168,EBI-1797; Score: 0.57
DE  Interaction: Q02796; IntAct: EBI-30514,EBI-1797; Score: 0.35
DE  Interaction: P22216; IntAct: EBI-17843,EBI-1797; Score: 0.69
DE  Interaction: P36124; IntAct: EBI-16993,EBI-1797; Score: 0.53
DE  Interaction: Q04116; IntAct: EBI-2889005,EBI-1797; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-1797; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-1797,EBI-8627; Score: 0.35
DE  Interaction: P25303; IntAct: EBI-1797,EBI-16711; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-3003,EBI-1797; Score: 0.35
DE  Interaction: Q12495; IntAct: EBI-3913,EBI-1797; Score: 0.53
DE  Interaction: P53131; IntAct: EBI-505,EBI-1797; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-17751,EBI-1797; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-27500,EBI-1797; Score: 0.35
DE  Interaction: P22579; IntAct: EBI-17160,EBI-1797; Score: 0.67
DE  Interaction: P50102; IntAct: EBI-19863,EBI-1797; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-18868,EBI-1797; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-17958,EBI-1797; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-1797; Score: 0.35
DE  Interaction: Q9HAN9; IntAct: EBI-1797,EBI-3917542; Score: 0.56
DE  Interaction: Q9NS73; IntAct: EBI-1797,EBI-741953; Score: 0.56
DE  Interaction: Q9NS73-5; IntAct: EBI-10182361,EBI-1797; Score: 0.56
DE  Interaction: Q9NVV9; IntAct: EBI-741515,EBI-1797; Score: 0.56
DE  Interaction: P22234; IntAct: EBI-1797,EBI-712261; Score: 0.56
DE  Interaction: O00635; IntAct: EBI-1797,EBI-2130415; Score: 0.56
DE  Interaction: P35520; IntAct: EBI-740135,EBI-1797; Score: 0.56
DE  Interaction: P63261; IntAct: EBI-1797,EBI-351292; Score: 0.56
DE  Interaction: A0A0C4DGF1; IntAct: EBI-10188476,EBI-1797; Score: 0.56
DE  Interaction: Q7Z6G3-2; IntAct: EBI-1797,EBI-10172876; Score: 0.56
DE  Interaction: Q96A10; IntAct: EBI-1797,EBI-10486892; Score: 0.56
DE  Interaction: P13196; IntAct: EBI-3905054,EBI-1797; Score: 0.56
DE  Interaction: P60709; IntAct: EBI-1797,EBI-353944; Score: 0.56
DE  Interaction: Q13137; IntAct: EBI-739580,EBI-1797; Score: 0.56
DE  Interaction: Q13557-8; IntAct: EBI-1797,EBI-11534483; Score: 0.56
DE  Interaction: Q13867; IntAct: EBI-1797,EBI-718504; Score: 0.56
DE  Interaction: Q15038; IntAct: EBI-1797,EBI-724310; Score: 0.56
DE  Interaction: Q15041; IntAct: EBI-1797,EBI-714543; Score: 0.56
DE  Interaction: Q8WVF5; IntAct: EBI-1797,EBI-741463; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-1797,EBI-286758; Score: 0.44
DE  Interaction: Q12449; IntAct: EBI-37072,EBI-1797; Score: 0.35
DE  Interaction: P27466; IntAct: EBI-9592,EBI-1797; Score: 0.35
DE  Interaction: P46948; IntAct: EBI-1788,EBI-1797; Score: 0.35
DE  Interaction: Q12149; IntAct: EBI-1782,EBI-1797; Score: 0.67
DE  Interaction: Q02724; IntAct: EBI-20050,EBI-1797; Score: 0.59
DE  Interaction: Q12124; IntAct: EBI-37542,EBI-1797; Score: 0.35
DE  Interaction: P13259; IntAct: EBI-5254,EBI-1797; Score: 0.69
DE  Interaction: P53256; IntAct: EBI-1842,EBI-1797; Score: 0.35
DE  Interaction: P53881; IntAct: EBI-29042,EBI-1797; Score: 0.35
DE  Interaction: Q08278; IntAct: EBI-10674,EBI-1797; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-13638,EBI-1797; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-29626,EBI-1797; Score: 0.35
DE  Interaction: P22215; IntAct: EBI-17397,EBI-1797; Score: 0.35
DE  Interaction: P53866; IntAct: EBI-1797,EBI-29168; Score: 0.35
DE  Interaction: P32337; IntAct: EBI-1797,EBI-9159; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-1797,EBI-11191; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-1797,EBI-9145; Score: 0.94
DE  Interaction: P00330; IntAct: EBI-1797,EBI-2218; Score: 0.35
DE  Interaction: P38792; IntAct: EBI-1757,EBI-1797; Score: 0.53
DE  Interaction: P32799; IntAct: EBI-5070,EBI-1797; Score: 0.35
DE  Interaction: P53859; IntAct: EBI-1731,EBI-1797; Score: 0.35
DE  Interaction: Q08285; IntAct: EBI-1831,EBI-1797; Score: 0.35
DE  Interaction: Q05636; IntAct: EBI-1810,EBI-1797; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-33556,EBI-1797; Score: 0.77
DE  Interaction: Q12464; IntAct: EBI-31814,EBI-1797; Score: 0.53
DE  Interaction: Q06218; IntAct: EBI-5640,EBI-1797; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-1797; Score: 0.27
DE  Interaction: P15108; IntAct: EBI-8666,EBI-1797; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042564;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0097718;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0006607;
GO  GO:0031144;
GO  GO:0006612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQ
SQ  FYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIAS
SQ  GTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLS
SQ  NLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPAL
SQ  RAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTK
SQ  KEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKA
SQ  GGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN
//
ID  Q8WY41;
PN  Nanos homolog 1;
GN  NANOS1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:19168546}. Cytoplasm {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:19168546}. Note=Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ cells. {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:19168546}.
DR  UNIPROT: Q8WY41;
DR  PDB: 4CQO;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DR  OMIM: 608226;
DR  OMIM: 615413;
DR  DisGeNET: 340719;
DE  Function: May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion. {ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680}.
DE  Disease: Spermatogenic failure 12 (SPGF12) [MIM:615413]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. Non-obstructive azoospermia, oligozoospermia and oligo-astheno- teratozoospermia are features observed in SPGF12 patients. {ECO:0000269|PubMed:23315541}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0016477;
GO  GO:0098749;
GO  GO:0010631;
GO  GO:0017148;
GO  GO:1900153;
GO  GO:0010608;
GO  GO:0001558;
GO  GO:0001894;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAFPWAPRSPRRGRAPPPMALVPSARYVSAPGPAHPQPFSSWNDYLGLATLITKAVDGEPRFGCARGGNGGGGSPPSSS
SQ  SSSCCSPHTGAGPGALGPALGPPDYDEDDDDDSDEPGSRGRYLGSALELRALELCAGPAEAGLLEERFAELSPFAGRAAA
SQ  VLLGCAPAAAAAATTTSEATPREERAPAWAAEPRLHAASGAAAARLLKPELQVCVFCRNNKEAMALYTTHILKGPDGRVL
SQ  CPVLRRYTCPLCGASGDNAHTIKYCPLSKVPPPPARPPPRSARDGPPGKKLR
//
ID  Q9M0N8;
PN  Mitotic-spindle organizing protein 1B;
GN  GIP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q08AG7}. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, phragmoplast. Nucleus envelope. Note=Reorganized from the nucleus to the prospindle and the preprophase band in late G2. After nuclear envelope breakdown, localized on spindle and phragmoplast microtubules (MTs) and on the reforming nuclear envelope of daughter cells. Present in mitotic microtubule arrays. In interphase cortical arrays, gamma-tubulin complexes are preferentially recruited to existing microtubules, from which new microtubules are efficiently nucleated.
DR  UNIPROT: Q9M0N8;
DR  Pfam: PF12554;
DE  Function: Required for gamma-tubulin complex recruitment to the microtubule organizing centers (MTOCs) (By similarity). During mitosis, modulates gamma-tubulin complex localization, spindle stability and chromosomal segregation. Necessary for gametophyte development and embryogenesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000930;
GO  GO:0008274;
GO  GO:0031021;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0009524;
GO  GO:0009574;
GO  GO:0005819;
GO  GO:0042393;
GO  GO:0034080;
GO  GO:0034508;
GO  GO:0033566;
GO  GO:0000226;
GO  GO:0051415;
GO  GO:0051418;
GO  GO:0090307;
GO  GO:0007052;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDEEASRTARESLELVFRMSNILDTGLDRHTLSVLIALCDLGVNPEALATVVKELRRESIPDSVTTTPSIH
//
ID  Q9UK39;
PN  Nocturnin;
GN  NOCT;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O35710}. Mitochondrion {ECO:0000269|PubMed:31147539}.
DR  UNIPROT: Q9UK39;
DR  UNIPROT: D3DNY5;
DR  UNIPROT: Q14D51;
DR  UNIPROT: Q9HD93;
DR  UNIPROT: Q9HD94;
DR  UNIPROT: Q9HD95;
DR  PDB: 6BT1;
DR  PDB: 6BT2;
DR  PDB: 6MAL;
DR  PDB: 6NF0;
DR  Pfam: PF03372;
DR  OMIM: 608468;
DR  DisGeNET: 25819;
DE  Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference for NADPH over NADP(+) (PubMed:31147539). Represses translation and promotes degradation of target mRNA molecules (PubMed:29860338). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (By similarity). Exerts a rhythmic post- transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (By similarity). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (By similarity). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (By similarity). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (By similarity). Critical for proper development of early embryos (By similarity). {ECO:0000250|UniProtKB:O35710, ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:31147539}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TEM1; IntAct: EBI-5655962,EBI-372826; Score: 0.40
DE  Interaction: Q92614; IntAct: EBI-949059,EBI-5655962; Score: 0.35
DE  Interaction: P02746; IntAct: EBI-2813376,EBI-5655962; Score: 0.35
DE  Interaction: Q8NBA8; IntAct: EBI-20218988,EBI-5655962; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-1056930,EBI-5655962; Score: 0.35
DE  Interaction: O75953; IntAct: EBI-5655937,EBI-5655962; Score: 0.37
DE  Interaction: Q15116; IntAct: EBI-4314328,EBI-5655962; Score: 0.35
DE  Interaction: Q86UE6; IntAct: EBI-9028422,EBI-5655962; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-18636064,EBI-5655962; Score: 0.35
DE  Interaction: Q92930; IntAct: EBI-1760095,EBI-5655962; Score: 0.35
DE  Interaction: Q13432; IntAct: EBI-711260,EBI-5655962; Score: 0.35
DE  Interaction: P11912; IntAct: EBI-7797864,EBI-5655962; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-4320063,EBI-5655962; Score: 0.35
DE  Interaction: P20309; IntAct: EBI-2687785,EBI-5655962; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-1753048,EBI-5655962; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-11472922,EBI-5655962; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-6655721,EBI-5655962; Score: 0.35
DE  Interaction: Q03405; IntAct: EBI-716505,EBI-5655962; Score: 0.35
DE  Interaction: Q9NXH9-2; IntAct: EBI-21531900,EBI-5655962; Score: 0.35
DE  Interaction: Q86VW1; IntAct: EBI-21721937,EBI-5655962; Score: 0.35
DE  Interaction: P40967-2; IntAct: EBI-15894236,EBI-5655962; Score: 0.35
DE  Interaction: Q9NQ79-2; IntAct: EBI-21534707,EBI-5655962; Score: 0.35
DE  Interaction: Q9Y6Y0; IntAct: EBI-5655962,EBI-715774; Score: 0.35
DE  Interaction: Q9HBU6; IntAct: EBI-5655962,EBI-2834493; Score: 0.35
DE  Interaction: Q96BK5; IntAct: EBI-5655962,EBI-721782; Score: 0.35
DE  Interaction: P11182; IntAct: EBI-5655962,EBI-359002; Score: 0.35
DE  Interaction: O75414; IntAct: EBI-5655962,EBI-3941531; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-1046087,EBI-5655962; Score: 0.35
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0000175;
GO  GO:0046872;
GO  GO:0003729;
GO  GO:0019178;
GO  GO:0102757;
GO  GO:0004535;
GO  GO:0032922;
GO  GO:0007623;
GO  GO:0033962;
GO  GO:0000290;
GO  GO:0048255;
GO  GO:0006739;
GO  GO:0010629;
GO  GO:0045668;
GO  GO:0045600;
GO  GO:0042752;
GO  GO:0045995;
GO  GO:0009991;
GO  GO:0032496;
GO  GO:0006366;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFHSPRRLCSALLQRDAPGLRRLPAPGLRRPLSPPAAVPRPASPRLLAAASAASGAARSCSRTVCSMGTGTSRLYSALAK
SQ  TLNSSAASQHPEYLVSPDPEHLEPIDPKELLEECRAVLHTRPPRFQRDFVDLRTDCPSTHPPIRVMQWNILAQALGEGKD
SQ  NFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFF
SQ  LQNRFKLVNSANIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLI
SQ  VCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSADGQSEPPYTTWKIRTSGECRHTLDYIWYSKHALNVRSALDLLTEEQI
SQ  GPNRLPSFNYPSDHLSLVCDFSFTEESDGLS
//
ID  Q15256;
PN  Receptor-type tyrosine-protein phosphatase R;
GN  PTPRR;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. [Isoform Delta]: Cytoplasm, perinuclear region. Note=Locates to the perinuclear areas within the cytoplasm. [Isoform Gamma]: Cytoplasm, perinuclear region. Note=Locates to the perinuclear areas within the cytoplasm.
DR  UNIPROT: Q15256;
DR  UNIPROT: B2R5Z7;
DR  UNIPROT: B7Z3J1;
DR  UNIPROT: F5GXR7;
DR  UNIPROT: O00342;
DR  UNIPROT: Q92682;
DR  UNIPROT: Q9UE65;
DR  PDB: 2A8B;
DR  Pfam: PF00102;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DR  PROSITE: PS50055;
DR  OMIM: 602853;
DR  DisGeNET: 5801;
DE  Function: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-2265659,EBI-351935; Score: 0.35
DE  Interaction: P42704; IntAct: EBI-2265659,EBI-1050853; Score: 0.35
DE  Interaction: P19022; IntAct: EBI-2265659,EBI-2256711; Score: 0.44
DE  Interaction: P09619; IntAct: EBI-641237,EBI-2265659; Score: 0.44
DE  Interaction: P28482; IntAct: EBI-2265659,EBI-959949; Score: 0.62
DE  Interaction: O60783; IntAct: EBI-2265659,EBI-1045956; Score: 0.35
DE  Interaction: O75688; IntAct: EBI-2265659,EBI-1047039; Score: 0.35
DE  Interaction: P07237; IntAct: EBI-2265659,EBI-395883; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-2265659,EBI-352528; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-2265659,EBI-359129; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-2265659,EBI-356553; Score: 0.35
DE  Interaction: P23528; IntAct: EBI-2265659,EBI-352733; Score: 0.35
DE  Interaction: P31153; IntAct: EBI-2265659,EBI-1050743; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-2265659,EBI-356687; Score: 0.35
DE  Interaction: P42166; IntAct: EBI-2265659,EBI-395393; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-2265659,EBI-355710; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-2265659,EBI-356673; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-2265659,EBI-356507; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-2265659,EBI-356876; Score: 0.35
DE  Interaction: P56134; IntAct: EBI-2265659,EBI-712794; Score: 0.35
DE  Interaction: P63261; IntAct: EBI-2265659,EBI-351292; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-2265659,EBI-357407; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-2265659,EBI-1050752; Score: 0.35
DE  Interaction: P82673; IntAct: EBI-2265659,EBI-2513649; Score: 0.35
DE  Interaction: P82675; IntAct: EBI-2265659,EBI-1054287; Score: 0.35
DE  Interaction: P82914; IntAct: EBI-2265659,EBI-2880040; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-2265659,EBI-1048516; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-2265659,EBI-359174; Score: 0.35
DE  Interaction: Q15149; IntAct: EBI-2265659,EBI-297903; Score: 0.35
DE  Interaction: Q16875; IntAct: EBI-2265659,EBI-764464; Score: 0.35
DE  Interaction: Q7L014; IntAct: EBI-2265659,EBI-2555356; Score: 0.35
DE  Interaction: Q8NCE2; IntAct: EBI-2265659,EBI-5658424; Score: 0.35
DE  Interaction: Q92552; IntAct: EBI-2265659,EBI-2211879; Score: 0.35
DE  Interaction: Q92665; IntAct: EBI-2265659,EBI-720602; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-2265659,EBI-356767; Score: 0.35
DE  Interaction: Q96EY7; IntAct: EBI-2265659,EBI-721110; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-2265659,EBI-357046; Score: 0.35
DE  Interaction: Q9BU76; IntAct: EBI-2265659,EBI-742459; Score: 0.35
DE  Interaction: Q9GZT3; IntAct: EBI-2265659,EBI-1050793; Score: 0.35
DE  Interaction: Q9H3K6; IntAct: EBI-2265659,EBI-1642537; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-2265659,EBI-352007; Score: 0.35
DE  Interaction: Q9NWB6; IntAct: EBI-2265659,EBI-2808785; Score: 0.35
DE  Interaction: Q9NXV2; IntAct: EBI-2265659,EBI-1056857; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-2265659,EBI-351384; Score: 0.35
DE  Interaction: Q9Y291; IntAct: EBI-2265659,EBI-2688704; Score: 0.35
DE  Interaction: Q9Y2Q9; IntAct: EBI-2265659,EBI-5325249; Score: 0.35
DE  Interaction: Q9Y2R9; IntAct: EBI-2265659,EBI-1054973; Score: 0.35
DE  Interaction: Q9Y399; IntAct: EBI-2265659,EBI-2880048; Score: 0.35
DE  Interaction: Q9Y3D9; IntAct: EBI-2265659,EBI-1054270; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-2265659,EBI-346967; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-2265659,EBI-358318; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-2265659,EBI-1050630; Score: 0.35
DE  Interaction: Q5VZ46; IntAct: EBI-2265659,EBI-20895075; Score: 0.35
DE  Interaction: Q6P5R6; IntAct: EBI-2265659,EBI-2512545; Score: 0.35
DE  Interaction: Q9BQ67; IntAct: EBI-2265659,EBI-351000; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-2265659,EBI-353803; Score: 0.35
DE  Interaction: Q9NUL7; IntAct: EBI-2265659,EBI-2560229; Score: 0.35
GO  GO:0030054;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0019901;
GO  GO:0004725;
GO  GO:0005001;
GO  GO:0038128;
GO  GO:0001701;
GO  GO:0010633;
GO  GO:0070373;
GO  GO:0006470;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQI
SQ  VNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKK
SQ  NSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVI
SQ  IVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATS
SQ  VCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEI
SQ  PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMV
SQ  WQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDS
SQ  AQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFV
SQ  HHALCLYESRLSAETVQ
//
ID  Q80U58;
PN  Pumilio homolog 2;
GN  Pum2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305|PubMed:19861488}. Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm, perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity). Colocalizes with NANOS3 in the stress granules (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72, ECO:0000269|PubMed:19861488}.
DR  UNIPROT: Q80U58;
DR  UNIPROT: Q80UZ9;
DR  UNIPROT: Q91YW4;
DR  UNIPROT: Q925A0;
DR  UNIPROT: Q9ERC7;
DR  PDB: 3GVO;
DR  PDB: 3GVT;
DR  Pfam: PF00806;
DR  PROSITE: PS50302;
DR  PROSITE: PS50303;
DE  Function: Sequence-specific RNA-binding protein that acts as a post- transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'- UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q8TB72}.
DE  Reference Proteome: Yes;
DE  Interaction: P35637; IntAct: EBI-400434,EBI-998056; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:2000637;
GO  GO:1900246;
GO  GO:0010608;
GO  GO:0035196;
GO  GO:0051983;
GO  GO:0043488;
GO  GO:0006417;
GO  GO:0034063;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAI
SQ  LSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGL
SQ  PNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPG
SQ  NQVPMDSSGATVGLFDYNSQQQLFQRTSALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGT
SQ  DPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAASNTANQQAASQAQPGQQQVLRPGAGQRPITPSQGQ
SQ  QGQQAESLAAAANPTLAFGQSLAAGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSTAAQAAAAAA
SQ  AAGGTANSLTGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASLGFGSGSSLG
SQ  AAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPS
SQ  LSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFP
SQ  NLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIR
SQ  GHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVL
SQ  STHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASN
SQ  VVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHI
SQ  LAKLEKYYLKNSPDLGPIGGPPNGML
//
ID  Q960X8;
PN  Hepatocyte growth factor-regulated tyrosine kinase substrate;
GN  Hrs;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000269|PubMed:11832215}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11832215}. Note=Locates to vesicles present in the perinuclear regions of muscle cells and in the periphery of Garland cells of third-instar larvae.
DR  UNIPROT: Q960X8;
DR  UNIPROT: A4V018;
DR  UNIPROT: Q8IGU6;
DR  UNIPROT: Q9VQF2;
DR  UNIPROT: Q9VQF3;
DR  PDB: 1DVP;
DR  Pfam: PF01363;
DR  Pfam: PF12210;
DR  Pfam: PF00790;
DR  PROSITE: PS50330;
DR  PROSITE: PS50179;
DR  PROSITE: PS50178;
DE  Function: Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Required during gastrulation and appears to regulate early embryonic signaling pathways. Inhibits tyrosine kinase receptor signaling by promoting degradation of the tyrosine-phosphorylated, active receptor, potentially by sorting activated receptors into MVBs. The MVBs are then trafficked to the lysosome where their contents are degraded. {ECO:0000269|PubMed:11832215}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8IQV9; IntAct: EBI-499630,EBI-90175; Score: 0.37
DE  Interaction: Q9VVT5; IntAct: EBI-179987,EBI-90175; Score: 0.37
DE  Interaction: Q9Y103; IntAct: EBI-90175,EBI-174432; Score: 0.37
DE  Interaction: P18091; IntAct: EBI-244744,EBI-90175; Score: 0.37
DE  Interaction: Q8SXD4; IntAct: EBI-130342,EBI-90175; Score: 0.37
DE  Interaction: Q7KLE5; IntAct: EBI-177679,EBI-90175; Score: 0.37
DE  Interaction: Q9V595; IntAct: EBI-164088,EBI-90175; Score: 0.37
DE  Interaction: Q03017; IntAct: EBI-200600,EBI-90175; Score: 0.37
DE  Interaction: Q9VH60; IntAct: EBI-161705,EBI-90175; Score: 0.37
DE  Interaction: Q95RP4; IntAct: EBI-90175,EBI-497971; Score: 0.37
DE  Interaction: Q9VCB8; IntAct: EBI-107457,EBI-90175; Score: 0.37
DE  Interaction: Q23983; IntAct: EBI-195132,EBI-90175; Score: 0.37
DE  Interaction: Q9VEN1; IntAct: EBI-133626,EBI-90175; Score: 0.37
DE  Interaction: Q00963; IntAct: EBI-75025,EBI-90175; Score: 0.37
DE  Interaction: A1Z9J3; IntAct: EBI-498304,EBI-90175; Score: 0.37
DE  Interaction: Q9VN68; IntAct: EBI-499329,EBI-90175; Score: 0.37
DE  Interaction: Q9VXG4; IntAct: EBI-93056,EBI-90175; Score: 0.37
DE  Interaction: Q7YU91; IntAct: EBI-500268,EBI-90175; Score: 0.37
DE  Interaction: Q8SXA8; IntAct: EBI-498965,EBI-90175; Score: 0.37
DE  Interaction: Q9VW47; IntAct: EBI-139710,EBI-90175; Score: 0.37
DE  Interaction: P29742; IntAct: EBI-160368,EBI-90175; Score: 0.37
DE  Interaction: Q9VC36; IntAct: EBI-184086,EBI-90175; Score: 0.37
DE  Interaction: Q9XTL2; IntAct: EBI-87548,EBI-90175; Score: 0.55
DE  Interaction: O44381; IntAct: EBI-497423,EBI-90175; Score: 0.37
DE  Interaction: Q9VPL5; IntAct: EBI-165122,EBI-90175; Score: 0.37
DE  Interaction: P54360; IntAct: EBI-499647,EBI-90175; Score: 0.37
DE  Interaction: P48608; IntAct: EBI-135200,EBI-90175; Score: 0.37
DE  Interaction: P07666; IntAct: EBI-98421,EBI-90175; Score: 0.37
DE  Interaction: Q8T987; IntAct: EBI-500835,EBI-90175; Score: 0.37
DE  Interaction: Q7KN74; IntAct: EBI-84709,EBI-90175; Score: 0.37
DE  Interaction: O02373; IntAct: EBI-185832,EBI-90175; Score: 0.37
DE  Interaction: Q9VM75; IntAct: EBI-157271,EBI-90175; Score: 0.37
DE  Interaction: Q9W4P5; IntAct: EBI-179683,EBI-90175; Score: 0.37
DE  Interaction: Q9VAD6; IntAct: EBI-105290,EBI-90175; Score: 0.37
DE  Interaction: Q9V397; IntAct: EBI-164075,EBI-90175; Score: 0.37
DE  Interaction: O46036; IntAct: EBI-159330,EBI-90175; Score: 0.37
DE  Interaction: Q9VNS1; IntAct: EBI-169089,EBI-90175; Score: 0.37
DE  Interaction: O46339; IntAct: EBI-137488,EBI-90175; Score: 0.37
DE  Interaction: Q9VLJ5; IntAct: EBI-130492,EBI-90175; Score: 0.37
DE  Interaction: P23573; IntAct: EBI-95916,EBI-90175; Score: 0.37
GO  GO:0005938;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0043130;
GO  GO:0045022;
GO  GO:0032456;
GO  GO:0006897;
GO  GO:0016197;
GO  GO:0032509;
GO  GO:1990182;
GO  GO:0006886;
GO  GO:0001933;
GO  GO:0120177;
GO  GO:0016322;
GO  GO:1903688;
GO  GO:0031398;
GO  GO:0045752;
GO  GO:0061357;
GO  GO:0031623;
GO  GO:0051726;
GO  GO:2000274;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRSSFDKNLENATSHLRLEPDWPSILLICDEINQKDVTPKNAFAAIKKKMNSPNPHSSCYSLLVLESIVKNCGAPVHEE
SQ  VFTKENCEMFSSFLESTPHENVRQKMLELVQTWAYAFRSSDKYQAIKDTMTILKAKGHTFPELREADAMFTADTAPNWAD
SQ  GRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQRPTSGSGGAKSGPRPADSELPA
SQ  EYLNSTLAQQVQTPARKTEQELKEEEELQLALALSQSEAEQQKPKLQSLPPAAYRMQQRSPSPEAPPEPKEYHQQPEEAT
SQ  NPELAKYLNRSYWEQRKISESSSMASPSAPSPMPPTPQPQQIMPLQVKSADEVQIDEFAANMRTQVEIFVNRMKSNSSRG
SQ  RSISNDSSVQTLFMTLTSLHSQQLSYIKEMDDKRMWYEQLQDKLTQIKDSRAALDQLRQEHVEKLRRIAEEQERQRQMQM
SQ  AQKLDIMRKKKQEYLQYQRQLALQRIQEQEREMQLRQEQQKAQYLMGQSAPPFPYMPPSAVPQHGSPSHQLNNVYNPYAA
SQ  GVPGYLPQGPAPAPNGHGQFQAIPPGMYNPAIQQPMPPNLQPGGLMQQPAPPGNPQMMPPMPENQFANNPAAILQLPQQH
SQ  SIAQPPQIPFQPQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPVQQPQPQPQMGHVMLQQHQAPPAAQAPPVT
SQ  EIANNQVQAVAAAPAPPQNEPGPAPVKAEEPATAELISFD
//
ID  Q70IA6;
PN  MOB kinase activator 2;
GN  MOB2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15067004}.
DR  UNIPROT: Q70IA6;
DR  UNIPROT: B4DKP3;
DR  UNIPROT: Q96M67;
DR  Pfam: PF03637;
DR  OMIM: 611969;
DR  DisGeNET: 81532;
DE  Function: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000269|PubMed:15067004}.
DE  Reference Proteome: Yes;
DE  Interaction: P35610; IntAct: EBI-6621955,EBI-2558739; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-2558739; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-444308,EBI-2558739; Score: 0.35
DE  Interaction: Q96H96; IntAct: EBI-20304109,EBI-2558739; Score: 0.35
DE  Interaction: Q9Y2H1; IntAct: EBI-991501,EBI-2558739; Score: 0.84
DE  Interaction: Q9H8S9; IntAct: EBI-748229,EBI-2558739; Score: 0.35
DE  Interaction: Q7L9L4; IntAct: EBI-2558745,EBI-2558739; Score: 0.35
DE  Interaction: P05549-1; IntAct: EBI-2558739,EBI-9678982; Score: 0.37
DE  Interaction: Q91VJ4; IntAct: EBI-2527046,EBI-2558739; Score: 0.40
DE  Interaction: Q15208; IntAct: EBI-458376,EBI-2558739; Score: 0.35
DE  Interaction: O95562; IntAct: EBI-4402330,EBI-2558739; Score: 0.56
DE  Interaction: P10644; IntAct: EBI-476431,EBI-2558739; Score: 0.35
DE  Interaction: Q8K0Q5; IntAct: EBI-8586076,EBI-2558739; Score: 0.35
DE  Interaction: Q9NRY4; IntAct: EBI-766200,EBI-2558739; Score: 0.35
DE  Interaction: Q3KRB8; IntAct: EBI-25411786,EBI-2558739; Score: 0.35
DE  Interaction: A0A024R136; IntAct: EBI-25411891,EBI-2558739; Score: 0.35
DE  Interaction: A6NKK0; IntAct: EBI-23725364,EBI-2558739; Score: 0.56
DE  Interaction: Q6NZ36-4; IntAct: EBI-12013806,EBI-2558739; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-10192441,EBI-2558739; Score: 0.56
DE  Interaction: Q5JXC2; IntAct: EBI-2801965,EBI-2558739; Score: 0.56
DE  Interaction: Q9GZT6; IntAct: EBI-713148,EBI-2558739; Score: 0.56
DE  Interaction: Q70Z53; IntAct: EBI-710176,EBI-2558739; Score: 0.56
DE  Interaction: Q9NT62; IntAct: EBI-988094,EBI-2558739; Score: 0.56
DE  Interaction: Q96ST8; IntAct: EBI-2799206,EBI-2558739; Score: 0.35
DE  Interaction: Q96HA8; IntAct: EBI-2558739,EBI-741158; Score: 0.56
GO  GO:0005829;
GO  GO:0044306;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0030036;
GO  GO:0010976;
GO  GO:0001934;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLMGKSKAKPNGKKPAAEERKAYLEPEHTKARITDFQFKELVVLPREIDLNEWLASNTTTFFHHINLQYSTISEFCTG
SQ  ETCQTMAVCNTQYYWYDERGKKVKCTAPQYVDFVMSSVQKLVTDEDVFPTKYGREFPSSFESLVRKICRHLFHVLAHIYW
SQ  AHFKETLALELHGHLNTLYVHFILFAREFNLLDPKETAIMDDLTEVLCSGAGGVHSGGSGDGAGSGGPGAQNHVKER
//
ID  E9PXF8;
PN  Myotubularin-related protein 13;
GN  Sbf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:16750429, ECO:0000269|PubMed:23297362}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16750429}. Membrane {ECO:0000250|UniProtKB:Q86WG5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q86WG5}. Endosome membrane {ECO:0000269|PubMed:23297362}; Peripheral membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23297362}. Note=Associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (PubMed:16399794). Membrane localization is likely to be mediated via its interaction with MTMR2 (PubMed:23297362). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
DR  UNIPROT: E9PXF8;
DR  UNIPROT: E9Q305;
DR  UNIPROT: Q8BJ67;
DR  UNIPROT: Q8BJD2;
DR  UNIPROT: Q8BJP4;
DR  UNIPROT: Q91VH0;
DR  Pfam: PF02141;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  Pfam: PF00169;
DR  Pfam: PF12335;
DR  Pfam: PF03456;
DR  PROSITE: PS50211;
DR  PROSITE: PS50003;
DR  PROSITE: PS51339;
DE  Function: Guanine nucleotide exchange factor (GEF) which activates RAB21 and possibly RAB28 (By similarity). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). In response to starvation-induced autophagy, activates RAB21 which in turn binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Acts as an adapter for the phosphatase MTMR2 (PubMed:16399794). Increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate (PubMed:16399794). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DP23; IntAct: EBI-397435,EBI-911785; Score: 0.35
GO  GO:0030424;
GO  GO:0010008;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005774;
GO  GO:0019902;
GO  GO:0019208;
GO  GO:0035091;
GO  GO:0017112;
GO  GO:0006914;
GO  GO:0043087;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHY
SQ  CSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLC
SQ  ACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRA
SQ  LESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQ
SQ  SALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVE
SQ  NDFLTKVLNGMAFAGFVSERGPPYRACDLFDELVAFEVERIKVEEKNPLKMIKHIRELAEQLFKNENPNPHMAFQKVPRP
SQ  TEGSHLRVHILPFPKINEARVQELIQENLAKNQNAPPATRIEKKCVVPAGPPVVSIMEKVITVFNSAQRLEVVRNCISFI
SQ  FENKTLETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSA
SQ  FYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKDDNHIPHLKQKLPDGQHQEKTAMDLAAEQLR
SQ  LWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRASAPGDWESGSNSIVTNSIAGSVAESYDTESG
SQ  FEDSENSDVANSVVRFIARFIDKVCTESGVTQDHIRSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLPGE
SQ  EIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQL
SQ  QQSVQEGLQITSASFQLIKVAFDEEVSPEVVDIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFSKT
SQ  IVKGAKKAGKMTIGRQYLLKKRTGTIVEERVNRPGWNEEDDISVSDDSELPTSTTLKASEKSTMEQLVEKACFRDYQRLG
SQ  LGTISGNSSRSKPEYFRVTASNRLYSLCRSYPGLLVIPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGFHG
SQ  KGVVGLFKSQNSPQAVSTSSLESSSSIEQEKYLQALLTAVIVHQKLRGSSTLTVRPALALSPVHGYRDKSFTQSNPKSSA
SQ  KEPVHNQGVWASLRSSTRLISSPTSFIDVGARLAGKDHSASFSNSTYLQNQLLKRQAALYIFGEKSQLRSSKVEFAFNCE
SQ  FVPVEFHEIRQVKASFKKLMRACIPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVWVCLEEGWDIT
SQ  TQVTSLAQLLSDPFYRTIAGFRTLVEKEWLSFGHKFSQRSSLALNSQGGGFAPIFLQFLDCVHQVHNQYPTEFEFNLYYL
SQ  KFLAFHYVSNRFKTFLLDSDYERLEHGTLFDDKGDKHAKKGVCIWECIDKMHTRSPIFFNYLYSPVEVEALKPNVNVSSL
SQ  KKWDYYTEETLSAGPSYDWMMLTPKHFPYEESDVAGGAGPQSQRKTVWPCYDDVTCSQPDALTRLFSEIEKLEHKLNQTP
SQ  ERWHQLWEKVTTDLKEEPRTAHSLRHSAGSPGIASTNVPSYQKRPALHPLHRGLGEDQSTTTAPSNGVEHRAATLYSQYT
SQ  SKNDENRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKYTSDKAFFD
SQ  LKTSKRVYNFCAQDGQSAQQWMDRIQSCISDA
//
ID  Q9D1E8;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon;
GN  Agpat5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUQ2}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NUQ2}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUQ2}.
DR  UNIPROT: Q9D1E8;
DR  UNIPROT: Q3U702;
DR  UNIPROT: Q8BG61;
DR  UNIPROT: Q8CGN6;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:15367102). Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl- CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA (By similarity). Activity toward lysophosphatidylglycerol not detectable (By similarity). {ECO:0000250|UniProtKB:Q9NUQ2, ECO:0000269|PubMed:15367102}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-912574,EBI-773051; Score: 0.35
DE  Interaction: Q9CQV8; IntAct: EBI-771608,EBI-773051; Score: 0.35
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0003841;
GO  GO:0016746;
GO  GO:0006639;
GO  GO:0016024;
GO  GO:0002244;
GO  GO:0036149;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSLVLHTYSMRYLLPSVLLLGSAPTYLLAWTLWRVLSALMPARLYQRVDDRLYCVYQNMVLFFFENYTGVQILLYGDL
SQ  PKNKENVIYLANHQSTVDWIVADMLAARQDALGHVRYVLKDKLKWLPLYGFYFAQHGGIYVKRSAKFNDKEMRSKLQSYV
SQ  NAGTPMYLVIFPEGTRYNATYTKLLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDSMKSHLDAIYDVTVVYEGNEKGSG
SQ  KYSNPPSMTEFLCKQCPKLHIHFDRIDRNEVPEEQEHMKKWLHERFEIKDRLLIEFYDSPDPERRNKFPGKSVHSRLSVK
SQ  KTLPSVLILGSLTAVMLMTESGRKLYMGTWLYGTLLGCLWFVIKA
//
ID  Q8IZ41;
PN  Ras and EF-hand domain-containing protein;
GN  RASEF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17448446}.
DR  UNIPROT: Q8IZ41;
DR  UNIPROT: A6NC29;
DR  UNIPROT: Q96N04;
DR  PDB: 2P5S;
DR  PDB: 2PMY;
DR  Pfam: PF13499;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DR  OMIM: 611344;
DR  DisGeNET: 158158;
DE  Function: Binds predominantly GDP, and also GTP. {ECO:0000269|PubMed:17448446}.
DE  Reference Proteome: Yes;
DE  Interaction: P13569; IntAct: EBI-349854,EBI-21855855; Score: 0.35
DE  Interaction: P31150; IntAct: EBI-946999,EBI-21855855; Score: 0.35
DE  Interaction: Q9UNT1-2; IntAct: EBI-12256104,EBI-21855855; Score: 0.35
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEADGDGEELARLRSVFAACDANRSGRLEREEFRALCTELRVRPADAEAVFQRLDADRDGAITFQEFARGFLGSLRGGRR
SQ  RDWGPLDPAPAVSEAGPETHDSEEDEGDEDAAAALATSCGPASPGRAWQDFQARLGDEAKFIPREEQVSTLYQNINLVEP
SQ  RLIQPYEHVIKNFIREIRLQSTEMENLAIAVKRAQDKAAMQLSELEEEMDQRIQAAEHKTRKDEKRKAEEALSDLRRQYE
SQ  TEVGDLQVTIKKLRKLEEQSKRVSQKEDVAALKKQIYDLSMENQKVKKDLLEAQTNIAFLQSELDALKSDYADQSLNTER
SQ  DLEIIRAYTEDRNSLERQIEILQTANRKLHDSNDGLRSALENSYSKFNRSLHINNISPGNTISRSSPKFIGHSPQPLGYD
SQ  RSSRSSYVDEDCDSLALCDPLQRTNCEVDSLPESCFDSGLSTLRDPNEYDSEVEYKHQRGFQRSHGVQESFGGDASDTDV
SQ  PDIRDEETFGLEDVASVLDWKPQGSVSEGSIVSSSRKPISALSPQTDLVDDNAKSFSSQKAYKIVLAGDAAVGKSSFLMR
SQ  LCKNEFRENISATLGVDFQMKTLIVDGERTVLQLWDTAGQERFRSIAKSYFRKADGVLLLYDVTCEKSFLNIREWVDMIE
SQ  DAAHETVPIMLVGNKADIRDTAATEGQKCVPGHFGEKLAMTYGALFCETSAKDGSNIVEAVLHLAREVKKRTDKDDSRSI
SQ  TNLTGTNSKKSPQMKNCCNG
//
ID  Q9Y6R4;
PN  Mitogen-activated protein kinase kinase kinase 4;
GN  MAP3K4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles. {ECO:0000250}.
DR  UNIPROT: Q9Y6R4;
DR  UNIPROT: A6H8W0;
DR  UNIPROT: B7ZLD3;
DR  UNIPROT: B9EG75;
DR  UNIPROT: Q5VTT8;
DR  UNIPROT: Q5VTT9;
DR  UNIPROT: Q92612;
DR  UNIPROT: Q9H408;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602425;
DR  DisGeNET: 4216;
DE  Function: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:12052864, ECO:0000269|PubMed:9305639}.
DE  Reference Proteome: Yes;
DE  Interaction: P12270; IntAct: EBI-448104,EBI-1048528; Score: 0.37
DE  Interaction: Q9NRD5; IntAct: EBI-448104,EBI-79165; Score: 0.37
DE  Interaction: Self; IntAct: EBI-448104,EBI-448104; Score: 0.37
DE  Interaction: P60953; IntAct: EBI-81752,EBI-448104; Score: 0.40
DE  Interaction: P52564; IntAct: EBI-448104,EBI-448135; Score: 0.57
DE  Interaction: P46734; IntAct: EBI-448104,EBI-602462; Score: 0.40
DE  Interaction: O15264; IntAct: EBI-2116951,EBI-448104; Score: 0.40
DE  Interaction: Q7Z7A1; IntAct: EBI-448104,EBI-2563266; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-448104,EBI-347088; Score: 0.37
DE  Interaction: Q9Y4C4; IntAct: EBI-2864441,EBI-448104; Score: 0.44
DE  Interaction: Q9UHD2; IntAct: EBI-356402,EBI-448104; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-1050828,EBI-448104; Score: 0.40
DE  Interaction: P62851; IntAct: EBI-353054,EBI-448104; Score: 0.40
DE  Interaction: P24522; IntAct: EBI-448167,EBI-448104; Score: 0.37
DE  Interaction: O75293; IntAct: EBI-448187,EBI-448104; Score: 0.57
DE  Interaction: O95257; IntAct: EBI-448202,EBI-448104; Score: 0.37
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004709;
GO  GO:0046872;
GO  GO:0004674;
GO  GO:0000186;
GO  GO:0032147;
GO  GO:0060718;
GO  GO:0035556;
GO  GO:0019100;
GO  GO:0001890;
GO  GO:0043507;
GO  GO:1900745;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0010468;
GO  GO:0007346;
GO  GO:0010225;
GO  GO:0023014;
GO  GO:0031098;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MREAAAALVPPPAFAVTPAAAMEEPPPPPPPPPPPPEPETESEPECCLAARQEGTLGDSACKSPESDLEDFSDETNTENL
SQ  YGTSPPSTPRQMKRMSTKHQRNNVGRPASRSNLKEKMNAPNQPPHKDTGKTVENVEEYSYKQEKKIRAALRTTERDRKKN
SQ  VQCSFMLDSVGGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSVPMPIARPARQTSRTDCPADRLKFFETLRLLLKLTSVSK
SQ  KKDREQRGQENTSGFWLNRSNELIWLELQAWHAGRTINDQDFFLYTARQAIPDIINEILTFKVDYGSFAFVRDRAGFNGT
SQ  SVEGQCKATPGTKIVGYSTHHEHLQRQRVSFEQVKRIMELLEYIEALYPSLQALQKDYEKYAAKDFQDRVQALCLWLNIT
SQ  KDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKGNEPEYEGDDTEGELKELESSTDESEEEQISDPRVPEIRQPIDN
SQ  SFDIQSRDCISKKLERLESEDDSLGWGAPDWSTEAGFSRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMDGSLQRARIA
SQ  LVKNDRPVEFSEFPDPMWGSDYVQLSRTPPSSEEKCSAVSWEELKAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPA
SQ  GEPSLLSIKQLVRECKEVLKGGLLMKQYYQFMLQEVLEDLEKPDCNIDAFEEDLHKMLMVYFDYMRSWIQMLQQLPQASH
SQ  SLKNLLEEEWNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLEFGLQESCAEFWTSADDSSASDEIRRSVIEISRA
SQ  LKELFHEARERASKALGFAKMLRKDLEIAAEFRLSAPVRDLLDVLKSKQYVKVQIPGLENLQMFVPDTLAEEKSIILQLL
SQ  NAAAGKDCSKDSDDVLIDAYLLLTKHGDRARDSEDSWGTWEAQPVKVVPQVETVDTLRSMQVDNLLLVVMQSAHLTIQRK
SQ  AFQQSIEGLMTLCQEQTSSQPVIAKALQQLKNDALELCNRISNAIDRVDHMFTSEFDAEVDESESVTLQQYYREAMIQGY
SQ  NFGFEYHKEVVRLMSGEFRQKIGDKYISFARKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQA
SQ  LMNECIGHVIGKPHSPVTGLYLAIHRNSPRPMKVPRCHSDPPNPHLIIPTPEGFSTRSMPSDARSHGSPAAAAAAAAAAV
SQ  AASRPSPSGGDSVLPKSISSAHDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRGDSSGSTRRSWELRTL
SQ  ISQSKDTASKLGPIEAIQKSVRLFEEKRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTC
SQ  ISVDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVI
SQ  RLYSKQITIAINVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGE
SQ  GHGRAADIWSLGCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKDFLSHCLESDPKMRWTASQLLDHSF
SQ  VKVCTDEE
//
ID  Q6P5Z2;
PN  Serine/threonine-protein kinase N3;
GN  PKN3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10441506}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10441506}. Note=Nuclear and perinuclear Golgi region.
DR  UNIPROT: Q6P5Z2;
DR  UNIPROT: Q9UM03;
DR  Pfam: PF02185;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS51860;
DR  OMIM: 610714;
DR  DisGeNET: 29941;
DE  Function: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}.
DE  Reference Proteome: Yes;
DE  Interaction: O96018; IntAct: EBI-6115839,EBI-1384335; Score: 0.35
DE  Interaction: Q8IVD9; IntAct: EBI-744342,EBI-1384335; Score: 0.35
DE  Interaction: P17918; IntAct: EBI-1173716,EBI-1384335; Score: 0.35
DE  Interaction: Q96BD8; IntAct: EBI-741854,EBI-1384335; Score: 0.35
DE  Interaction: Q9UKF6; IntAct: EBI-1044699,EBI-1384335; Score: 0.35
DE  Interaction: O95235; IntAct: EBI-2551319,EBI-1384335; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-2551470,EBI-1384335; Score: 0.35
DE  Interaction: Q62376; IntAct: EBI-6665659,EBI-1384335; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-743488,EBI-1384335; Score: 0.35
DE  Interaction: Q8BQ46; IntAct: EBI-645898,EBI-1384335; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-301697,EBI-1384335; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-351126,EBI-1384335; Score: 0.35
DE  Interaction: Q91YI4; IntAct: EBI-994161,EBI-1384335; Score: 0.35
DE  Interaction: D3Z482; IntAct: EBI-11073196,EBI-1384335; Score: 0.35
DE  Interaction: Q9EQU5; IntAct: EBI-1543689,EBI-1384335; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-298478,EBI-1384335; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-4283704,EBI-1384335; Score: 0.35
DE  Interaction: P62714; IntAct: EBI-1044367,EBI-1384335; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-712311,EBI-1384335; Score: 0.35
DE  Interaction: Q13033; IntAct: EBI-1053857,EBI-1384335; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-302589,EBI-1384335; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-8322817,EBI-1384335; Score: 0.35
DE  Interaction: P19788; IntAct: EBI-11032993,EBI-1384335; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-299674,EBI-1384335; Score: 0.35
DE  Interaction: Q13352; IntAct: EBI-712105,EBI-1384335; Score: 0.35
DE  Interaction: Q9P2B7; IntAct: EBI-2558932,EBI-1384335; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-1103245,EBI-1384335; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-437708,EBI-1384335; Score: 0.35
DE  Interaction: P55795; IntAct: EBI-352823,EBI-1384335; Score: 0.35
DE  Interaction: Q14134; IntAct: EBI-702370,EBI-1384335; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-741415,EBI-1384335; Score: 0.35
DE  Interaction: Q86WV1-2; IntAct: EBI-11995314,EBI-1384335; Score: 0.35
DE  Interaction: A8K8V0-2; IntAct: EBI-21612038,EBI-1384335; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-2903122,EBI-1384335; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-15009894,EBI-1384335; Score: 0.35
DE  Interaction: Q9UNA1-1; IntAct: EBI-25412129,EBI-1384335; Score: 0.35
DE  Interaction: Q5JR59-3; IntAct: EBI-11522433,EBI-1384335; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-1105213,EBI-1384335; Score: 0.56
DE  Interaction: Q8N1B4; IntAct: EBI-2799833,EBI-1384335; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-1384335; Score: 0.56
DE  Interaction: Q8ND90; IntAct: EBI-302345,EBI-1384335; Score: 0.56
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-1384335; Score: 0.35
DE  Interaction: Q15323; IntAct: EBI-1384335,EBI-948001; Score: 0.56
DE  Interaction: O95619; IntAct: EBI-1384335,EBI-399269; Score: 0.27
DE  Interaction: Q6NZI2; IntAct: EBI-2559016,EBI-1384335; Score: 0.27
DE  Interaction: O43482; IntAct: EBI-1384335,EBI-536879; Score: 0.27
DE  Interaction: O15516; IntAct: EBI-1384335,EBI-1794265; Score: 0.27
DE  Interaction: O00327; IntAct: EBI-1384335,EBI-1794206; Score: 0.27
DE  Interaction: O00233; IntAct: EBI-1384335,EBI-750973; Score: 0.27
DE  Interaction: Q5R372; IntAct: EBI-1384335,EBI-2810417; Score: 0.27
DE  Interaction: O43815; IntAct: EBI-1384335,EBI-1046642; Score: 0.27
DE  Interaction: Q8TBA6; IntAct: EBI-1384335,EBI-11278147; Score: 0.27
DE  Interaction: Q8TD31; IntAct: EBI-1384335,EBI-949834; Score: 0.27
DE  Interaction: Q7Z4H7; IntAct: EBI-1384335,EBI-2558196; Score: 0.27
DE  Interaction: Q6NSJ2; IntAct: EBI-1384335,EBI-6148204; Score: 0.27
DE  Interaction: Q5VIR6; IntAct: EBI-1384335,EBI-2850511; Score: 0.27
DE  Interaction: Q5T0U0; IntAct: EBI-1384335,EBI-2836961; Score: 0.27
DE  Interaction: Q567U6; IntAct: EBI-1384335,EBI-1104769; Score: 0.27
DE  Interaction: Q53HC9; IntAct: EBI-1384335,EBI-1055422; Score: 0.27
DE  Interaction: Q4V328; IntAct: EBI-1384335,EBI-717919; Score: 0.27
DE  Interaction: Q15276; IntAct: EBI-1384335,EBI-447043; Score: 0.27
DE  Interaction: Q14161; IntAct: EBI-1384335,EBI-1046878; Score: 0.27
DE  Interaction: P61244; IntAct: EBI-1384335,EBI-751711; Score: 0.27
DE  Interaction: P0C1Z6; IntAct: EBI-1384335,EBI-1245626; Score: 0.27
DE  Interaction: Q9BZD4; IntAct: EBI-1384335,EBI-724102; Score: 0.27
DE  Interaction: Q96P16; IntAct: EBI-1384335,EBI-1053506; Score: 0.27
DE  Interaction: Q96JG6; IntAct: EBI-1384335,EBI-11044388; Score: 0.27
DE  Interaction: Q96EK4; IntAct: EBI-1384335,EBI-1790529; Score: 0.27
DE  Interaction: Q96BD5; IntAct: EBI-1384335,EBI-745085; Score: 0.27
DE  Interaction: Q86Y13; IntAct: EBI-1384335,EBI-948630; Score: 0.27
DE  Interaction: Q9Y3A3; IntAct: EBI-1384335,EBI-713935; Score: 0.27
DE  Interaction: Q9Y2X7; IntAct: EBI-1384335,EBI-466061; Score: 0.27
DE  Interaction: Q9UKL0; IntAct: EBI-1384335,EBI-926563; Score: 0.27
DE  Interaction: Q9UJ41; IntAct: EBI-1384335,EBI-913954; Score: 0.27
DE  Interaction: Q9UID3; IntAct: EBI-1384335,EBI-2932923; Score: 0.27
DE  Interaction: Q9NP66; IntAct: EBI-1384335,EBI-740641; Score: 0.27
DE  Interaction: Q9NNX1; IntAct: EBI-1384335,EBI-2557363; Score: 0.27
DE  Interaction: Q9HCH0; IntAct: EBI-1384335,EBI-3437824; Score: 0.27
DE  Interaction: O15460-2; IntAct: EBI-10182841,EBI-1384335; Score: 0.35
DE  Interaction: Q96F46; IntAct: EBI-5591258,EBI-1384335; Score: 0.35
DE  Interaction: P52799; IntAct: EBI-7532268,EBI-1384335; Score: 0.35
DE  Interaction: Q9Y5G3-2; IntAct: EBI-21584477,EBI-1384335; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-11472922,EBI-1384335; Score: 0.35
DE  Interaction: Q9Y279; IntAct: EBI-903131,EBI-1384335; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-2830042,EBI-1384335; Score: 0.35
DE  Interaction: Q15768; IntAct: EBI-3908475,EBI-1384335; Score: 0.35
DE  Interaction: P04201; IntAct: EBI-21274133,EBI-1384335; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-446668,EBI-1384335; Score: 0.35
DE  Interaction: Q8N831; IntAct: EBI-12023322,EBI-1384335; Score: 0.35
DE  Interaction: Q6ZN54-2; IntAct: EBI-12346463,EBI-1384335; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-296151,EBI-1384335; Score: 0.35
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0017049;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0010631;
GO  GO:0035556;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILL
SQ  PGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLR
SQ  MKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLL
SQ  EQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQ
SQ  RGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLS
SQ  LSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRT
SQ  PTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFR
SQ  CLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTE
SQ  FVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFC
SQ  GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEK
SQ  RLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFD
SQ  FVSERFLEP
//
ID  P50393;
PN  Lysophospholipase;
GN  Pla2g4a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: P50393;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042588;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0035035;
GO  GO:0004622;
GO  GO:0004623;
GO  GO:0102567;
GO  GO:0102568;
GO  GO:0007568;
GO  GO:0019369;
GO  GO:0050482;
GO  GO:0071236;
GO  GO:0046697;
GO  GO:0046475;
GO  GO:0046456;
GO  GO:0001554;
GO  GO:0001542;
GO  GO:0043065;
GO  GO:0030501;
GO  GO:0008284;
GO  GO:0031622;
GO  GO:0050729;
GO  GO:0031394;
GO  GO:0031340;
GO  GO:0042127;
GO  GO:0051592;
GO  GO:0051384;
GO  GO:0009408;
GO  GO:0009725;
GO  GO:0042542;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0051597;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0033280;
GO  GO:0043129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRRQ
SQ  RKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSTTLSSLKEKVS
SQ  AARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEDAEREYQNDNQASWVHRMLMALVSDSALFN
SQ  TREGRAGKEHNFMLGLNLNTSYPLSPLRDFSPQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHF
SQ  VLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRR
SQ  QNPSRCSVSLSNVEARKFFNKEFLSKPTAESI
//
ID  Q9BX97;
PN  Plasmalemma vesicle-associated protein;
GN  PLVAP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of caveolae. Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels. Also colocalized with CAV1 in perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}.
DR  UNIPROT: Q9BX97;
DR  UNIPROT: Q86VP0;
DR  UNIPROT: Q8N8Y0;
DR  UNIPROT: Q8ND68;
DR  UNIPROT: Q8TER8;
DR  UNIPROT: Q9BZD5;
DR  Pfam: PF06637;
DR  OMIM: 607647;
DR  OMIM: 618183;
DR  DisGeNET: 83483;
DE  Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development. {ECO:0000250|UniProtKB:Q91VC4}.
DE  Disease: Diarrhea 10, protein-losing enteropathy type (DIAR10) [MIM:618183]: An autosomal recessive, congenital diarrheal disorder characterized by intractable secretory diarrhea with massive protein loss due to leaky fenestrated capillaries, severe hypoalbuminemia, hypogammaglobulinemia, hypertriglyceridemia, and electrolyte abnormalities. Disease severity is variable and death in infancy may occur in severe cases. Some patients show facial dysmorphic features, and cardiac and renal abnormalities. {ECO:0000269|PubMed:26207260, ECO:0000269|PubMed:29661969, ECO:0000269|PubMed:29875123}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H6R6-2; IntAct: EBI-2803560,EBI-21511418; Score: 0.35
DE  Interaction: Q9H0V9-2; IntAct: EBI-2803560,EBI-21511115; Score: 0.35
DE  Interaction: Q9BYC5; IntAct: EBI-2803560,EBI-2869363; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-2803560,EBI-2514786; Score: 0.35
DE  Interaction: O60906; IntAct: EBI-2803560,EBI-12828299; Score: 0.35
DE  Interaction: P07306; IntAct: EBI-1172335,EBI-2803560; Score: 0.35
DE  Interaction: Q56974; IntAct: EBI-2861069,EBI-2803560; Score: 0.37
DE  Interaction: Q8CL86; IntAct: EBI-2803560,EBI-2846580; Score: 0.37
DE  Interaction: Q8ZDG9; IntAct: EBI-2803560,EBI-2846543; Score: 0.37
DE  Interaction: Q8ZED8; IntAct: EBI-2840186,EBI-2803560; Score: 0.37
DE  Interaction: A0A0H2W5A2; IntAct: EBI-2841456,EBI-2803560; Score: 0.37
DE  Interaction: Q5NHQ9; IntAct: EBI-2803560,EBI-2803576; Score: 0.37
DE  Interaction: Q5NGF1; IntAct: EBI-2797546,EBI-2803560; Score: 0.37
DE  Interaction: A0A384KIG3; IntAct: EBI-2842935,EBI-2803560; Score: 0.37
DE  Interaction: A0A1U9X8X8; IntAct: EBI-2803560,EBI-17234977; Score: 0.56
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0032502;
GO  GO:0000165;
GO  GO:0002693;
GO  GO:0033209;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLAMEHGGSYARAGGSSRGCWYYLRYFFLFVSLIQFLIILGLVLFMVYGNVHVSTESNLQATERRAEGLYSQLLGLTAS
SQ  QSNLTKELNFTTRAKDAIMQMWLNARRDLDRINASFRQCQGDRVIYTNNQRYMAAIILSEKQCRDQFKDMNKSCDALLFM
SQ  LNQKVKTLEVEIAKEKTICTKDKESVLLNKRVAEEQLVECVKTRELQHQERQLAKEQLQKVQALCLPLDKDKFEMDLRNL
SQ  WRDSIIPRSLDNLGYNLYHPLGSELASIRRACDHMPSLMSSKVEELARSLRADIERVARENSDLQRQKLEAQQGLRASQE
SQ  AKQKVEKEAQAREAKLQAECSRQTQLALEEKAVLRKERDNLAKELEEKKREAEQLRMELAIRNSALDTCIKTKSQPMMPV
SQ  SRPMGPVPNPQPIDPASLEEFKRKILESQRPPAGIPVAPSSG
//
ID  Q68749;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356413;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein p21]: Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host mitochondrion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host lipid droplet {ECO:0000250}. Note=The C- terminal transmembrane domain of core protein p21 contains an ER signal leading the nascent polyprotein to the ER membrane. Only a minor proportion of core protein is present in the nucleus and an unknown proportion is secreted. [Core protein p19]: Virion {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Secreted {ECO:0000250}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane. [p7]: Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}. Note=The C-terminus of p7 membrane domain acts as a signal sequence. After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. Only a fraction localizes to the plasma membrane. [Protease NS2-3]: Host endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=NS3 is associated to the ER membrane through its binding to NS4A. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Host membrane insertion occurs after processing by the NS3 protease. [RNA-directed RNA polymerase]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease.
DR  UNIPROT: Q68749;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor- induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T- cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up- regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250}. E1 and E2 glycoproteins form a heterodimer that is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, but this binding is not sufficient for infection, some additional liver specific cofactors may be needed. The fusion function may possibly be carried by E1. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC- SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage- like cells of lymph node sinuses. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection (By similarity). {ECO:0000250}. P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity (By similarity). {ECO:0000250}. Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity). {ECO:0000250}. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS (By similarity). {ECO:0000250}. NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). {ECO:0000250}. NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). {ECO:0000250}. NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0039545;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRAARKTSERSQPRGRRQPIPKDRRSTGKSWGRPG
SQ  YPWPLYRNEGLGWAGWLLSPRGSRPSWGPSDPRHKSRNLGKVIDTLTCGFADLMGYIPVVGAPVGGVARALAHGVRVLED
SQ  GINYATGNLPGCSFSIFLLALLSCISVPVSAVEVRNTSSSYMATNDCSNSSIVWQLEGAVLHTPGCVPCEKTGNKSRCWV
SQ  PVTPNIAINQPGALTKGLRAHIDVIVMSATLCSALYVGDVCGALMIAAQVVVVSPQHHHFVQECNCSIYPGKITGHRMAW
SQ  DMMMNWSPTTTMLLAYLVRIPEVVLDIITGGHWGVMFGLAYFSMQGAWAKVVVILLLTAGVEASTYTTGAVVGRSTHLFT
SQ  SMFSLGSQQRVQLIHTNGSWHINRTALNCNDSLETGFLAALFYTSSFNSSGCPERLAACRSIESFRIGWGSLEYEESVTN
SQ  DADMRPYCWHYPPRPCGIVPARTVCGPVYCFTPSPVVVGTTDRAGAPTYNWGENETDVFLLNSTRPPKGAWFGCTWMNGT
SQ  GFTKTCGAPPCRIRKDFNASEDLLCPTDCFRKHPGATYIKCGAGPWLTPRCLVDYPYRLWHYPCTVNYTIYKVRMFVGGI
SQ  EHRLQAACNFTRGDRCNLEDRDRSQLSPLLHSTTEWAILPCSYTDLPALSTGLLHLHQNIVDVQYLYGLSPAITKYVVKW
SQ  EWVVLLFLLLADARVCACLWMLLLLGQAEAALEKLVILHAASAASSNGLLYFILFFVAAWCIKGRAVPMVTYTLLGCWSF
SQ  VLLLMALPHQAYALDAAEQGQIGMALLIAITAFTITPAYKILLSRCLWWTCYMLVLAEALIQDWIPPLQARGGRDGVIWA
SQ  MTMFYPGVVFDITKWLLAILGPGYLFRAAVMRTPYFVRANALLRMCALVKQLAGGKYVQVALITLGKWTGTYIYDHLSPM
SQ  SDWAADGLRDLAVAVEPIVFSPMERKVIVWGAETTACGDIIHGLPVSARLGQEVLLGPADGYTSKGWRLLAPITAYAQQT
SQ  RGLLSAIVVSMTGRDKTDQAGEIQVLSTVTQSFLGTSISGVLWTVFHGAGNKTLAGSRGPVTQMYSSAEGDLVGWPSPPG
SQ  TRSLEPCTCGAVDLYLVTRNADVIPARRRGDRRGALLSPRPLSSLKGSSGGPVLCPRGHAVGIFRAAVCSRGVAKSIDFI
SQ  PVESLDVVTRSPNFTDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAYGINP
SQ  NIRTGVRTVTTGDAITYSTYGKFLADGGCSGGAYDVIICDECHSVDSTTILGIGTVLDQAETAGVRLTVLATATPPGSVT
SQ  TPHPNIEEVALGHEGEIPFYGKAIPLSAIKGGRHLIFCHSKKKCDELAVALRGMGLNAVAYYRGLDVSIIPTQGDVVVVA
SQ  TDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFTITTQTVPQDSVSRSQRRGRTGRGRLGIYRYVSSGERASGMFDTVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGEGFPYLVAYQATVCAR
SQ  AKAPPPSWDVMWKCLIRLKPTLVGPTPLLYRLGSVTNEVTLTHPVTKYIATCMQADLEIMTSTWVLAGGVLAAVAAYCLA
SQ  TGCVSIIGRIHVNQKTIIAPDKEVLYEAFDEMEECASRTALIEEGHRIAEMLKSKIQGLMQQASKQAQGVQPAVQATWPK
SQ  LEQFWAKHMWNFISGIQYLAGLSTLPGNPAVASMMSFSAALTSPLSTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPSVEDVVNLLPAILSPGALVVGVICAAILRRHVGQGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVAESDASQRVTQLLGSLTITSLLRRLHQWITEDCPVPCSGSWLRDVWDWVCSILIDFKNWLS
SQ  AKLFPRLPGIPFISCQKGYRGTWAGTGIMTTRCPCGANITGNVRLGTMRISGPKTCLNTWQGTFPINCYTEGSCVPKPAP
SQ  NFKTAIWRVAASEYAEVTQHDSHAYVTGLTADNLKVPCQLPCPEFFSWVDGVQIHRFAPTPKAFMRDEVSFSVGLNSYVV
SQ  GSQLPCEPEPDTEVLASMLTDPSHITAEAAARRLARGSPPSAASSSASQLSAPSLRATCTTHAKCPDIDMVDANLFCWCT
SQ  MGGNMTRIESESKVLMVDSFDPVVDKEDEREPSIPSEYLLPKSRFPPALPPWARPDYNPPLLETWKRPDYQPPVVAGCAL
SQ  PPPGTTPVPPPRRRRAVVLDQSNVGEALKELAIKSFGCPPPSGDPGHSTGGGTTGETSKSPPDEPDDSEAGSVSSMPPLE
SQ  GEPGDPDLEPEQVEHPAPPQEGGAAPGSDSGSWSTCSDVDDSVVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYH
SQ  NKVYCTTSRSASQRAKKVTFDRVQLLDSHYESVLKDVKQAATKVSAKLLSIEEACALTPPHSARSKYGFGAKEVRSLSRR
SQ  AVDHIKSVWEDLLEDHCSPIDTTIMAKNEVFCVDPTKGGKKPARLIVYPDLGVRVCEKMALYDITQKLPVAVMGQSYGFQ
SQ  YSPAQRVDFLLQAWKEKKTPMGFSYDTRCFDSTVTERDIRTEESIYLSCSLPEEARTAIHSLTERLYVGGPMTNSKGQSC
SQ  GYRRCRASGVLTTSMGNTLTCYVKAKAACNAAGIVAPTMLVCGDDLVVISESQGVEEDERNLRVFTEAMTRYSAPPGDPP
SQ  KAEYDLELITSCSSNVSVALDPRGRRRYYLTRDPTTPLARAAWETARHSPVNSWLGNIIQYAPTVWVRMVLMTHFFSVLM
SQ  AQDTLDQDLNFEMYGAVYSVSPLDLPAIIERLHGLEAFSLHSYSPHELTRVAAALRKLGAPPLRAWKSRARAVRASLISR
SQ  GGSAATCGRYLFNWAVRTKLKLTPLPAARLLDLSSWFTVSAGGGDIYHSVSRARPRLLLLGLLLLCVGVGIFLLPAR
//
ID  Q7Z3Z2;
PN  Protein RD3;
GN  RD3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q8BRE0}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8BRE0}. Endosome {ECO:0000250|UniProtKB:Q8BRE0}. Nucleus {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29030614}. Note=Colocalizes with GUCY2E and GUCY2F in rods and cones photoreceptors. Colocalizes with GUK1 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer (By similarity). Strong dot-like perinuclear staining in the epithelial cells (PubMed:29030614). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:29030614}.
DR  UNIPROT: Q7Z3Z2;
DR  UNIPROT: A8K595;
DR  PDB: 6DRF;
DR  Pfam: PF14473;
DR  OMIM: 180040;
DR  OMIM: 610612;
DR  DisGeNET: 343035;
DE  Function: Plays a critical role in the regulation of enzymes involved in nucleotide cycle in photoreceptors (PubMed:29515371, PubMed:21928830, PubMed:21078983, PubMed:27471269, PubMed:30559291). Inhibits the basal catalytic activity and the GCAP-stimulated activity of GUCY2D and GUCY2F, two retinal guanylyl cyclases involved in the production of cGMP in photoreceptors (PubMed:21928830, PubMed:27471269, PubMed:29515371, PubMed:30559291). Involved in the transport of GUCY2D and GUCY2F to their target sites in the photoreceptor outer segment (PubMed:21078983). Up-regulates the activity of GUK1, a kinase that plays also an essential role for recycling GMP and indirectly, cGMP (PubMed:29515371). Plays an important role for the survival of rods and cones in the retina (By similarity). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:21928830, ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:29515371, ECO:0000269|PubMed:30559291}.
DE  Disease: Leber congenital amaurosis 12 (LCA12) [MIM:610612]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:17186464}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A2ABF9; IntAct: EBI-10257497,EBI-10174566; Score: 0.56
DE  Interaction: Q14232; IntAct: EBI-491065,EBI-10257497; Score: 0.78
DE  Interaction: Q8NFP9; IntAct: EBI-10257497,EBI-723014; Score: 0.35
DE  Interaction: Q7L592-2; IntAct: EBI-10257497,EBI-21502380; Score: 0.35
DE  Interaction: P50851-2; IntAct: EBI-10257497,EBI-4403233; Score: 0.35
DE  Interaction: P19086; IntAct: EBI-10257497,EBI-9071731; Score: 0.35
DE  Interaction: Q96HA8; IntAct: EBI-10257497,EBI-741158; Score: 0.56
DE  Interaction: Q9NPB3; IntAct: EBI-10257497,EBI-12011224; Score: 0.56
DE  Interaction: Q96KQ7; IntAct: EBI-744366,EBI-10257497; Score: 0.56
GO  GO:0120199;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0120200;
GO  GO:0031283;
GO  GO:0015031;
GO  GO:0050896;
GO  GO:0060041;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLISWLRWNEAPSRLSTRSPAEMVLETLMMELTGQMREAERQQRERSNAVRKVCTGVDYSWLASTPRSTYDLSPIERLQ
SQ  LEDVCVKIHPSYCGPAILRFRQLLAEQEPEVQEVSQLFRSVLQEVLERMKQEEEAHKLTRQWSLRPRGSLATFKTRARIS
SQ  PFASDIRTISEDVERDTPPPLRSWSMPEFRAPKAD
//
ID  O95295;
PN  SNARE-associated protein Snapin;
GN  SNAPIN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q9Z266}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane {ECO:0000305|PubMed:25898167}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:21102408}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000269|PubMed:19168546}.
DR  UNIPROT: O95295;
DR  UNIPROT: D3DV56;
DR  UNIPROT: Q5SXU8;
DR  Pfam: PF14712;
DR  OMIM: 607007;
DR  DisGeNET: 23557;
DE  Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE- mediated membrane fusion in non-neuronal cells (PubMed:17182842, PubMed:18167355). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}.
DE  Reference Proteome: Yes;
DE  Interaction: A1L4K1; IntAct: EBI-5661036,EBI-296723; Score: 0.56
DE  Interaction: Q16539; IntAct: EBI-73946,EBI-296723; Score: 0.37
DE  Interaction: Q15849-1; IntAct: EBI-1633392,EBI-296723; Score: 0.60
DE  Interaction: Q62668-1; IntAct: EBI-1635608,EBI-296723; Score: 0.62
DE  Interaction: Q08850; IntAct: EBI-296723,EBI-918243; Score: 0.35
DE  Interaction: O70377; IntAct: EBI-296723,EBI-1573765; Score: 0.35
DE  Interaction: Q62668; IntAct: EBI-296723,EBI-1573598; Score: 0.35
DE  Interaction: Q9NV70; IntAct: EBI-296723,EBI-1045313; Score: 0.55
DE  Interaction: Q5S007; IntAct: EBI-296723,EBI-5323863; Score: 0.66
DE  Interaction: P60881; IntAct: EBI-1027214,EBI-296723; Score: 0.40
DE  Interaction: Q9D0F1; IntAct: EBI-309872,EBI-296723; Score: 0.40
DE  Interaction: Q96L14; IntAct: EBI-743488,EBI-296723; Score: 0.56
DE  Interaction: Q6A065; IntAct: EBI-2554140,EBI-296723; Score: 0.40
DE  Interaction: H7BX26; IntAct: EBI-11022011,EBI-296723; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-296723; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-296723; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-3923210,EBI-296723; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-1104799,EBI-296723; Score: 0.55
DE  Interaction: A5D8V7; IntAct: EBI-8466445,EBI-296723; Score: 0.35
DE  Interaction: Q8N7C3; IntAct: EBI-11059915,EBI-296723; Score: 0.35
DE  Interaction: O60296; IntAct: EBI-2851680,EBI-296723; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-346882,EBI-296723; Score: 0.56
DE  Interaction: Q9UPT5-1; IntAct: EBI-6251402,EBI-296723; Score: 0.56
DE  Interaction: P78537; IntAct: EBI-348630,EBI-296723; Score: 0.76
DE  Interaction: Q2M2I5; IntAct: EBI-2952736,EBI-296723; Score: 0.60
DE  Interaction: Q96EV8; IntAct: EBI-465804,EBI-296723; Score: 0.82
DE  Interaction: Q5JTB6; IntAct: EBI-3923605,EBI-296723; Score: 0.56
DE  Interaction: Q6QNY1; IntAct: EBI-465872,EBI-296723; Score: 0.83
DE  Interaction: P35609; IntAct: EBI-296723,EBI-77797; Score: 0.37
DE  Interaction: P05023; IntAct: EBI-296723,EBI-358778; Score: 0.37
DE  Interaction: O00499; IntAct: EBI-719094,EBI-296723; Score: 0.37
DE  Interaction: Q5VT25; IntAct: EBI-296723,EBI-689171; Score: 0.37
DE  Interaction: Q8N3K9; IntAct: EBI-2323272,EBI-296723; Score: 0.37
DE  Interaction: P17661; IntAct: EBI-1055572,EBI-296723; Score: 0.37
DE  Interaction: P50570; IntAct: EBI-346547,EBI-296723; Score: 0.37
DE  Interaction: Q03001; IntAct: EBI-296723,EBI-310758; Score: 0.37
DE  Interaction: Q8IWE2; IntAct: EBI-296723,EBI-2686288; Score: 0.37
DE  Interaction: Q9H6L5; IntAct: EBI-5664372,EBI-296723; Score: 0.37
DE  Interaction: O95163; IntAct: EBI-296723,EBI-347559; Score: 0.55
DE  Interaction: Q14974; IntAct: EBI-286758,EBI-296723; Score: 0.37
DE  Interaction: Q04695; IntAct: EBI-296723,EBI-297873; Score: 0.37
DE  Interaction: P24043; IntAct: EBI-2529730,EBI-296723; Score: 0.37
DE  Interaction: P11047; IntAct: EBI-296723,EBI-714904; Score: 0.55
DE  Interaction: Q9UPN3-5; IntAct: EBI-6131019,EBI-296723; Score: 0.37
DE  Interaction: Q7Z406; IntAct: EBI-296723,EBI-355595; Score: 0.37
DE  Interaction: P11055; IntAct: EBI-296723,EBI-5654298; Score: 0.37
DE  Interaction: P12883; IntAct: EBI-519141,EBI-296723; Score: 0.37
DE  Interaction: Q14511; IntAct: EBI-2108053,EBI-296723; Score: 0.37
DE  Interaction: Q15149; IntAct: EBI-297903,EBI-296723; Score: 0.37
DE  Interaction: Q15276; IntAct: EBI-447043,EBI-296723; Score: 0.37
DE  Interaction: Q9UJ41; IntAct: EBI-913954,EBI-296723; Score: 0.37
DE  Interaction: Q96Q15; IntAct: EBI-296723,EBI-1049832; Score: 0.37
DE  Interaction: P11277; IntAct: EBI-514908,EBI-296723; Score: 0.37
DE  Interaction: Q01082; IntAct: EBI-296723,EBI-351561; Score: 0.37
DE  Interaction: O94826; IntAct: EBI-2800236,EBI-296723; Score: 0.37
DE  Interaction: P09493; IntAct: EBI-296723,EBI-351158; Score: 0.37
DE  Interaction: P07951; IntAct: EBI-296723,EBI-352633; Score: 0.37
DE  Interaction: Q969Q1; IntAct: EBI-5661333,EBI-296723; Score: 0.37
DE  Interaction: P62258; IntAct: EBI-296723,EBI-356498; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-347088,EBI-296723; Score: 0.37
DE  Interaction: O75923; IntAct: EBI-296723,EBI-2799016; Score: 0.54
DE  Interaction: Q9BZ29; IntAct: EBI-2695893,EBI-296723; Score: 0.37
DE  Interaction: P13929; IntAct: EBI-4287222,EBI-296723; Score: 0.37
DE  Interaction: Q9UL45; IntAct: EBI-465781,EBI-296723; Score: 0.53
DE  Interaction: Q7Z465; IntAct: EBI-3942634,EBI-296723; Score: 0.37
DE  Interaction: Q8CZZ7; IntAct: EBI-296723,EBI-2842831; Score: 0.37
DE  Interaction: Q96AW1; IntAct: EBI-715058,EBI-296723; Score: 0.37
DE  Interaction: O60282; IntAct: EBI-717170,EBI-296723; Score: 0.37
DE  Interaction: Q96R06; IntAct: EBI-413317,EBI-296723; Score: 0.37
DE  Interaction: Q9Y561; IntAct: EBI-296693,EBI-296723; Score: 0.37
DE  Interaction: Q5T0J7-2; IntAct: EBI-12833746,EBI-296723; Score: 0.35
DE  Interaction: Q70UQ0-4; IntAct: EBI-12190633,EBI-296723; Score: 0.67
DE  Interaction: Q8TDM0-3; IntAct: EBI-13025473,EBI-296723; Score: 0.35
DE  Interaction: Q9UBB9; IntAct: EBI-1105213,EBI-296723; Score: 0.56
DE  Interaction: P08779; IntAct: EBI-356410,EBI-296723; Score: 0.56
DE  Interaction: Q9NYB9-2; IntAct: EBI-296723,EBI-11096309; Score: 0.56
DE  Interaction: P67936; IntAct: EBI-296723,EBI-1642100; Score: 0.56
DE  Interaction: P35900; IntAct: EBI-296723,EBI-742094; Score: 0.56
DE  Interaction: Q13515; IntAct: EBI-296723,EBI-10229433; Score: 0.56
DE  Interaction: Q68D86; IntAct: EBI-296723,EBI-10171570; Score: 0.56
DE  Interaction: Q7Z6G3-2; IntAct: EBI-296723,EBI-10172876; Score: 0.56
DE  Interaction: P49585; IntAct: EBI-296723,EBI-2563309; Score: 0.56
DE  Interaction: Q8N9N5-2; IntAct: EBI-296723,EBI-11524452; Score: 0.56
DE  Interaction: P20700; IntAct: EBI-296723,EBI-968218; Score: 0.56
DE  Interaction: Q8IV53; IntAct: EBI-296723,EBI-2871584; Score: 0.56
DE  Interaction: P06753; IntAct: EBI-296723,EBI-355607; Score: 0.56
DE  Interaction: Q7Z3Y9; IntAct: EBI-296723,EBI-12084444; Score: 0.56
DE  Interaction: Q9UJ41-4; IntAct: EBI-296723,EBI-14093916; Score: 0.56
DE  Interaction: P51946; IntAct: EBI-296723,EBI-741406; Score: 0.56
DE  Interaction: P08727; IntAct: EBI-742756,EBI-296723; Score: 0.56
DE  Interaction: Q96BD8; IntAct: EBI-296723,EBI-741854; Score: 0.56
DE  Interaction: P07951-2; IntAct: EBI-296723,EBI-10977815; Score: 0.56
DE  Interaction: A1L168; IntAct: EBI-18396958,EBI-296723; Score: 0.56
DE  Interaction: Q9Y5B8; IntAct: EBI-296723,EBI-744782; Score: 0.56
DE  Interaction: Q8IYW4; IntAct: EBI-296723,EBI-20842218; Score: 0.56
DE  Interaction: Q2T9L4; IntAct: EBI-4311436,EBI-296723; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-3044087,EBI-296723; Score: 0.56
DE  Interaction: P19012; IntAct: EBI-739566,EBI-296723; Score: 0.56
DE  Interaction: Q96NL6; IntAct: EBI-2514016,EBI-296723; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-296723,EBI-1188238; Score: 0.37
DE  Interaction: Q12934-2; IntAct: EBI-296723,EBI-12123320; Score: 0.56
DE  Interaction: Q9Y3C0; IntAct: EBI-296723,EBI-712969; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-296723,EBI-2556193; Score: 0.56
DE  Interaction: Q9H1M0; IntAct: EBI-296723,EBI-751933; Score: 0.56
DE  Interaction: Q96EV8-2; IntAct: EBI-16749183,EBI-296723; Score: 0.35
DE  Interaction: Q86WT6-2; IntAct: EBI-11525489,EBI-296723; Score: 0.35
DE  Interaction: Q9UIL1-2; IntAct: EBI-21638756,EBI-296723; Score: 0.35
DE  Interaction: Q9NX95-3; IntAct: EBI-21651984,EBI-296723; Score: 0.35
DE  Interaction: Q07866-2; IntAct: EBI-11979975,EBI-296723; Score: 0.35
DE  Interaction: Q8WVE6; IntAct: EBI-10264837,EBI-296723; Score: 0.35
DE  Interaction: Q96GS4; IntAct: EBI-10193358,EBI-296723; Score: 0.35
DE  Interaction: Q9NV70-2; IntAct: EBI-10961687,EBI-296723; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-296723; Score: 0.35
DE  Interaction: Q9UJT2; IntAct: EBI-852101,EBI-296723; Score: 0.35
DE  Interaction: Q08345; IntAct: EBI-296723,EBI-711879; Score: 0.37
DE  Interaction: P26641; IntAct: EBI-351467,EBI-296723; Score: 0.37
DE  Interaction: P54257; IntAct: EBI-712814,EBI-296723; Score: 0.37
DE  Interaction: Q92993; IntAct: EBI-399080,EBI-296723; Score: 0.37
DE  Interaction: Q16891; IntAct: EBI-473801,EBI-296723; Score: 0.37
DE  Interaction: O95251; IntAct: EBI-473199,EBI-296723; Score: 0.37
DE  Interaction: Q9NUP1; IntAct: EBI-296723,EBI-465852; Score: 0.37
DE  Interaction: Q6QNY0; IntAct: EBI-465930,EBI-296723; Score: 0.35
GO  GO:1904115;
GO  GO:0031083;
GO  GO:0099078;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0000139;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0030141;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0030672;
GO  GO:0000149;
GO  GO:0008089;
GO  GO:0048490;
GO  GO:0097352;
GO  GO:0034629;
GO  GO:0008333;
GO  GO:0006886;
GO  GO:1902774;
GO  GO:0007042;
GO  GO:0032418;
GO  GO:0007040;
GO  GO:0032438;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0007269;
GO  GO:1902824;
GO  GO:0051604;
GO  GO:0043393;
GO  GO:2000300;
GO  GO:0008090;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016188;
GO  GO:0048489;
GO  GO:0072553;
GO  GO:0016032;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z266};
SQ  MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDP
SQ  YVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK
//
ID  Q8NC51;
PN  Plasminogen activator inhibitor 1 RNA-binding protein;
GN  SERBP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:28695742}. Nucleus {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:28695742}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12505151}.
DR  UNIPROT: Q8NC51;
DR  UNIPROT: Q5VU19;
DR  UNIPROT: Q5VU20;
DR  UNIPROT: Q5VU22;
DR  UNIPROT: Q8WUH0;
DR  UNIPROT: Q96SE2;
DR  UNIPROT: Q9BTY3;
DR  UNIPROT: Q9BUM4;
DR  UNIPROT: Q9Y367;
DR  UNIPROT: Q9Y4S3;
DR  PDB: 4V6X;
DR  Pfam: PF04774;
DR  Pfam: PF16174;
DR  OMIM: 607378;
DR  DisGeNET: 26135;
DE  Function: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). {ECO:0000269|PubMed:11001948, ECO:0000269|PubMed:28695742}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-523558; Score: 0.35
DE  Interaction: Self; IntAct: EBI-523558,EBI-523558; Score: 0.37
DE  Interaction: P32121; IntAct: EBI-714559,EBI-523558; Score: 0.35
DE  Interaction: O15264; IntAct: EBI-2116951,EBI-523558; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-523558; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-353366,EBI-523558; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-79964,EBI-523558; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-715747,EBI-523558; Score: 0.35
DE  Interaction: Q99497; IntAct: EBI-1164361,EBI-523558; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-6621955,EBI-523558; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-1057265,EBI-523558; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-724571,EBI-523558; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-2862306,EBI-523558; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-523558; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-523558; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-10191195,EBI-523558; Score: 0.35
DE  Interaction: F5H7Q8; IntAct: EBI-21261518,EBI-523558; Score: 0.35
DE  Interaction: Q4VGL6; IntAct: EBI-2366263,EBI-523558; Score: 0.35
DE  Interaction: P0C090; IntAct: EBI-8759965,EBI-523558; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-523558; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-712001,EBI-523558; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-523558; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-523558; Score: 0.35
DE  Interaction: P52735; IntAct: EBI-297549,EBI-523558; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-523558; Score: 0.35
DE  Interaction: P01100; IntAct: EBI-523558,EBI-852851; Score: 0.40
DE  Interaction: P14921; IntAct: EBI-913209,EBI-523558; Score: 0.40
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-523558; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-523558; Score: 0.35
DE  Interaction: Q9D287; IntAct: EBI-8338824,EBI-523558; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-523558; Score: 0.35
DE  Interaction: P23116; IntAct: EBI-2552342,EBI-523558; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-351126,EBI-523558; Score: 0.35
DE  Interaction: Q16666-2; IntAct: EBI-6273540,EBI-523558; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-8361659,EBI-523558; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-78579,EBI-523558; Score: 0.35
DE  Interaction: Q0HD54; IntAct: EBI-6147978,EBI-523558; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-716247,EBI-523558; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-523558; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-359390,EBI-523558; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-523558; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-523558; Score: 0.35
DE  Interaction: A0A384LAN6; IntAct: EBI-523558,EBI-2840998; Score: 0.37
DE  Interaction: A0A0F7R3R0; IntAct: EBI-2814126,EBI-523558; Score: 0.37
DE  Interaction: Q14164; IntAct: EBI-523558,EBI-307369; Score: 0.40
DE  Interaction: O75815; IntAct: EBI-523558,EBI-702336; Score: 0.40
DE  Interaction: P01889; IntAct: EBI-523558,EBI-1046513; Score: 0.40
DE  Interaction: O94817; IntAct: EBI-523558,EBI-746742; Score: 0.40
DE  Interaction: P62330; IntAct: EBI-523558,EBI-638181; Score: 0.40
DE  Interaction: Q15654; IntAct: EBI-523558,EBI-742327; Score: 0.40
DE  Interaction: Q53HC9; IntAct: EBI-523558,EBI-1055422; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-515315,EBI-523558; Score: 0.35
DE  Interaction: Q16828; IntAct: EBI-746870,EBI-523558; Score: 0.35
DE  Interaction: P15918; IntAct: EBI-523558,EBI-1755109; Score: 0.40
DE  Interaction: Q5VT25; IntAct: EBI-523558,EBI-689171; Score: 0.40
DE  Interaction: Q969X2; IntAct: EBI-523558,EBI-949146; Score: 0.40
DE  Interaction: P46783; IntAct: EBI-354442,EBI-523558; Score: 0.40
DE  Interaction: P30622; IntAct: EBI-523558,EBI-2683569; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475864,EBI-523558; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-464729,EBI-523558; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-79165,EBI-523558; Score: 0.56
DE  Interaction: Q9NZI8; IntAct: EBI-1053892,EBI-523558; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-523590,EBI-523558; Score: 0.58
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045296;
GO  GO:0003730;
GO  GO:0003723;
GO  GO:0032183;
GO  GO:0030578;
GO  GO:0042981;
GO  GO:0043488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKN
SQ  PLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDR
SQ  PIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQK
SQ  QISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWK
SQ  KGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDD
SQ  PEAFPALA
//
ID  Q8NDT2;
PN  Putative RNA-binding protein 15B;
GN  RBM15B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:16129689}. Nucleus speckle {ECO:0000269|PubMed:19586903}. Nucleus envelope {ECO:0000269|PubMed:19586903}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000269|PubMed:16129689}.
DR  UNIPROT: Q8NDT2;
DR  UNIPROT: A4QPG7;
DR  UNIPROT: Q6QE19;
DR  UNIPROT: Q9BV96;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DR  OMIM: 612602;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6- methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:27602518). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA splicing (PubMed:21044963). Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1 (PubMed:19586903). {ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:21044963, ECO:0000269|PubMed:27602518, ECO:0000305|PubMed:16129689}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-726721,EBI-641062; Score: 0.37
DE  Interaction: P61981; IntAct: EBI-359832,EBI-726721; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-726721; Score: 0.35
DE  Interaction: Q8IVL1; IntAct: EBI-741200,EBI-726721; Score: 0.56
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-726721; Score: 0.35
DE  Interaction: P11161; IntAct: EBI-625282,EBI-726721; Score: 0.37
DE  Interaction: P63316; IntAct: EBI-726721,EBI-3906339; Score: 0.37
DE  Interaction: Q15003; IntAct: EBI-1046410,EBI-726721; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-743488,EBI-726721; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-1765605,EBI-726721; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-352602,EBI-726721; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-11105430,EBI-726721; Score: 0.35
DE  Interaction: Q9BRX9; IntAct: EBI-7705033,EBI-726721; Score: 0.35
DE  Interaction: P36406; IntAct: EBI-740098,EBI-726721; Score: 0.35
DE  Interaction: Q9BWE0; IntAct: EBI-5458270,EBI-726721; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-726721; Score: 0.35
DE  Interaction: Q96T37-2; IntAct: EBI-726721,EBI-21508071; Score: 0.35
DE  Interaction: Q53GT1; IntAct: EBI-726721,EBI-1996072; Score: 0.35
DE  Interaction: Q8N8Y2; IntAct: EBI-726721,EBI-3923949; Score: 0.37
DE  Interaction: O00487; IntAct: EBI-726721,EBI-722193; Score: 0.37
DE  Interaction: Q14627; IntAct: EBI-4320063,EBI-726721; Score: 0.35
DE  Interaction: Q7Z4N8; IntAct: EBI-10181968,EBI-726721; Score: 0.35
DE  Interaction: Q86VM9; IntAct: EBI-1045965,EBI-726721; Score: 0.35
DE  Interaction: Q9NZQ3-2; IntAct: EBI-21676167,EBI-726721; Score: 0.35
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0036396;
GO  GO:0003723;
GO  GO:0009048;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0000381;
GO  GO:0001510;
GO  GO:0008380;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGAKHPVPARARDKPRGSGSGGGGHRDGRGTGDANHRA
SQ  SSGRSSGSGAGGGGRGGKASGDPGASGMSPRASPLPPPPPPPGAEPACPGSSAAAPEYKTLLISSLSPALPAEHLEDRLF
SQ  HQFKRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGGSSRRSSSSSAAASTPP
SQ  PGPPAPADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYP
SQ  AVCEEDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGR
SQ  VIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGG
SQ  PDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLVRDRTPPHLLYSDRDRTFLEGDWTSPSKSSDRR
SQ  NSLEGYSRSVRSRSGERWGADGDRGLPKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGSGQQSERGSDRTPERSRKENH
SQ  SSEGTKESSSNSLSNSRHGAEERGHHHHHHEAADSSHGKKARDSERNHRTTEAEPKPLEEPKHETKKLKNLSEYAQTLQL
SQ  GWNGLLVLKNSCFPTSMHILEGDQGVISSLLKDHTSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLATQAT
SQ  PSGLGTEGMPTVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDGTGMLYAFPPCDFSQQYLQSALRTLGKLEEEH
SQ  MVIVIVRDTA
//
ID  Q63481;
PN  Ras-related protein Rab-7L1;
GN  Rab29;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000269|PubMed:23395371}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23395371}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). Colocalized with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:23395371). {ECO:0000250|UniProtKB:O14966, ECO:0000269|PubMed:23395371}.
DR  UNIPROT: Q63481;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:23395371). Essential for maintaining the integrity of endosome-trans-Golgi network structure (PubMed:23395371). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (PubMed:23395371). {ECO:0000250|UniProtKB:O14966, ECO:0000269|PubMed:23395371}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-6513837,EBI-5323863; Score: 0.46
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0012505;
GO  GO:0005794;
GO  GO:0097708;
GO  GO:0042470;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0020003;
GO  GO:0005802;
GO  GO:0031982;
GO  GO:0070840;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019894;
GO  GO:0017137;
GO  GO:0060271;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:0032438;
GO  GO:0007005;
GO  GO:0010977;
GO  GO:0090316;
GO  GO:0001921;
GO  GO:0050862;
GO  GO:1903441;
GO  GO:0072657;
GO  GO:0032482;
GO  GO:1901214;
GO  GO:1905279;
GO  GO:0009617;
GO  GO:0042147;
GO  GO:0007416;
GO  GO:0042110;
GO  GO:1901998;
GO  GO:0039694;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDSEMVRLQLWDIAGQERFTSMTRLYYRD
SQ  ASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPSGEPVPCLLLANKSDLSPWAVSRDQIDRFSKENGFTGWTETSVKENK
SQ  NINEAMRVLVEKMMNNSREDIMSSSTQGNYINLQTKPSPGWTCC
//
ID  Q71F54;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  Sh3rf1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16571722}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DR  UNIPROT: Q71F54;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF00097;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway (PubMed:12514131). Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:12514131}.
DE  Reference Proteome: Yes;
DE  Interaction: Q920M9; IntAct: EBI-957514,EBI-957526; Score: 0.40
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0006915;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0051865;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRP
SQ  WKPGPGGGGSTTCTNVLRAQGSTVVNCGSKDLQSPQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IILRRQVDENWYHGEVNGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAAQSSSASKHSDTKKNTRKRHSFTSLTMANKSSQASQ
SQ  NRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPTDVPYQAALGTMNPPL
SQ  PPPPLLATTVLASTPSGATAAAVAAAAAAVAAGVGPRPAVGSTEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMF
SQ  LVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQASRGVTMVSPSTAGGPAQKPQGNGVAGNP
SQ  SVVPTAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAACIGPASVGLPHHSLASQP
SQ  LPPMVGPAAHIAAVNINRTSVPLACAAGASSLASPNMTTAALETEPSGRTVTILPGLPTSPESAASACGNSSAVKPDKDS
SQ  KKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGSGEVPLQGAVGPELPLGGVHGRVGSCPTDGDGPVAAGTAALAQDA
SQ  FHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRN
SQ  GKTGLFPGSFVENI
//
ID  E1C7U0;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: E1C7U0;
DR  UNIPROT: A0A1D5P7Q9;
DR  PDB: 6NT6;
DR  PDB: 6NT7;
DR  PDB: 6NT8;
DR  PDB: 6NT9;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:30842659). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842659). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842659}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0035438;
GO  GO:0061507;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032608;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0051259;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:30842659};
SQ  MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLH
SQ  SRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNV
SQ  AHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGI
SQ  KRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYE
SQ  EPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP
//
ID  Q9D5V6;
PN  Synapse-associated protein 1;
GN  Syap1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:27344443}. Golgi apparatus {ECO:0000269|PubMed:27344443}. Perikaryon {ECO:0000269|PubMed:27344443}. Cell projection, axon {ECO:0000269|PubMed:27344443}. Cell projection, dendrite {ECO:0000269|PubMed:27344443}. Cell projection, growth cone {ECO:0000269|PubMed:27344443}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:27344443}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:27344443}. Membrane {ECO:0000250|UniProtKB:Q96A49}. Note=Localizes to cholinergic neuromuscular junctions and in actin-rich growth cone regions (PubMed:27344443). Membrane-associated in a epidermal growth factor (EGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q96A49, ECO:0000269|PubMed:27344443}.
DR  UNIPROT: Q9D5V6;
DR  UNIPROT: Q3UI67;
DR  UNIPROT: Q9D870;
DR  Pfam: PF03909;
DR  PROSITE: PS50858;
DE  Function: Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0030054;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0031234;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0042734;
GO  GO:0030154;
GO  GO:0071364;
GO  GO:0032869;
GO  GO:1990314;
GO  GO:0036120;
GO  GO:0045600;
GO  GO:0071902;
GO  GO:0038203;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGGLSSWLGLKPPEGAAAEGEEPPSRDGDKLSAGAAPSEESPERPVEPTEEQQQQPPTEDPQFLHQAKGLGNYLYNFAS
SQ  AATKKITESVTETAQTIKKSVEEGKIDDILDKTILGDFQKEQKKFVEEQNTKKSEAAVPPWVESHDEETIQQQILALSAD
SQ  KRNFLRDPPAGVQFNFDFDQMYPVALVMLQEDELLSKMRFALVPKLVKEEVFWRNYFYRISLIKQSAQLTALAAQQQASG
SQ  KEEKSSNRDDNLPLTEAVRPKTPPVVIKSQLKSQEDEEEISTSPGVSEFVSDAFDTCSLNQEDLRKEMEQLVLDKKQEEA
SQ  TALEEDSTDWEKELQQELQEYEVVAESEKRDENWDKEIEKMLQES
//
ID  P62166;
PN  Neuronal calcium sensor 1;
GN  NCS1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cell junction, synapse, postsynaptic density {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11092894, ECO:0000269|PubMed:17555535}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000269|PubMed:17555535}; Peripheral membrane protein. Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000305}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000305, ECO:0000305|PubMed:17555535}.
DR  UNIPROT: P62166;
DR  UNIPROT: E9PAY3;
DR  UNIPROT: P36610;
DR  UNIPROT: Q9UK26;
DR  PDB: 1G8I;
DR  PDB: 2LCP;
DR  PDB: 4GUK;
DR  PDB: 5O9S;
DR  PDB: 6QI4;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 603315;
DR  DisGeNET: 23413;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage- gated calcium channel (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BYM8; IntAct: EBI-2340624,EBI-746987; Score: 0.35
DE  Interaction: Q9H0F6; IntAct: EBI-3942966,EBI-746987; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-356349,EBI-746987; Score: 0.35
DE  Interaction: Q12933; IntAct: EBI-355744,EBI-746987; Score: 0.35
DE  Interaction: Q8NFZ5; IntAct: EBI-359372,EBI-746987; Score: 0.35
DE  Interaction: P21554; IntAct: EBI-746987,EBI-2909859; Score: 0.46
DE  Interaction: Q9BXU9; IntAct: EBI-12187137,EBI-746987; Score: 0.40
DE  Interaction: Q86UW9; IntAct: EBI-746987,EBI-740376; Score: 0.83
DE  Interaction: P41271; IntAct: EBI-746987,EBI-10208650; Score: 0.56
DE  Interaction: Q96ST8; IntAct: EBI-2799206,EBI-746987; Score: 0.35
DE  Interaction: P37058; IntAct: EBI-2932988,EBI-746987; Score: 0.35
DE  Interaction: P08637; IntAct: EBI-2833956,EBI-746987; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-746987,EBI-1642365; Score: 0.35
DE  Interaction: Q9BV23; IntAct: EBI-746987,EBI-3916106; Score: 0.35
DE  Interaction: Q5W0U4; IntAct: EBI-746987,EBI-5884190; Score: 0.35
DE  Interaction: P30419-2; IntAct: EBI-746987,EBI-21690011; Score: 0.35
DE  Interaction: P04183; IntAct: EBI-746987,EBI-712550; Score: 0.35
DE  Interaction: O75175; IntAct: EBI-746987,EBI-743073; Score: 0.35
DE  Interaction: O60551; IntAct: EBI-746987,EBI-3920273; Score: 0.35
DE  Interaction: Q96ST8-3; IntAct: EBI-11144046,EBI-746987; Score: 0.60
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-746987; Score: 0.56
DE  Interaction: Q9UKN5; IntAct: EBI-2803427,EBI-746987; Score: 0.56
DE  Interaction: P78358; IntAct: EBI-1188472,EBI-746987; Score: 0.56
DE  Interaction: P10451; IntAct: EBI-723648,EBI-746987; Score: 0.56
DE  Interaction: O60930; IntAct: EBI-2372399,EBI-746987; Score: 0.56
DE  Interaction: O95868; IntAct: EBI-12382527,EBI-746987; Score: 0.56
DE  Interaction: Q8IWL1; IntAct: EBI-12350685,EBI-746987; Score: 0.56
DE  Interaction: Q9BXJ5; IntAct: EBI-2817707,EBI-746987; Score: 0.56
DE  Interaction: Q03060-25; IntAct: EBI-12884642,EBI-746987; Score: 0.56
DE  Interaction: A0A1U9X8X8; IntAct: EBI-17234977,EBI-746987; Score: 0.56
DE  Interaction: Q8TDS5; IntAct: EBI-12813389,EBI-746987; Score: 0.56
DE  Interaction: Q9Y336; IntAct: EBI-746987,EBI-12857926; Score: 0.56
DE  Interaction: O75084; IntAct: EBI-746987,EBI-746917; Score: 0.56
DE  Interaction: Q96C03-3; IntAct: EBI-746987,EBI-11988931; Score: 0.56
DE  Interaction: Q7Z698; IntAct: EBI-7082156,EBI-746987; Score: 0.56
DE  Interaction: Q96K80; IntAct: EBI-746987,EBI-742550; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-746987; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587304,EBI-746987; Score: 0.35
DE  Interaction: P05362; IntAct: EBI-1035358,EBI-746987; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757569,EBI-746987; Score: 0.35
GO  GO:0044305;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0031045;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0005509;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0005245;
GO  GO:0099626;
GO  GO:0048015;
GO  GO:0045921;
GO  GO:0010975;
GO  GO:2000300;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:25255805};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  P60763;
PN  Ras-related C3 botulinum toxin substrate 3;
GN  RAC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Endomembrane system. Cell projection, lamellipodium. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery.
DR  UNIPROT: P60763;
DR  UNIPROT: O14658;
DR  UNIPROT: Q5U0M8;
DR  PDB: 2C2H;
DR  PDB: 2G0N;
DR  PDB: 2IC5;
DR  PDB: 2OV2;
DR  PDB: 2QME;
DR  PDB: 6TM1;
DR  Pfam: PF00071;
DR  PROSITE: PS51420;
DR  OMIM: 602050;
DR  OMIM: 618577;
DR  DisGeNET: 5881;
DE  Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}.
DE  Disease: Neurodevelopmental disorder with structural brain anomalies and dysmorphic facies (NEDBAF) [MIM:618577]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, severe intellectual disability, poor language, seizures, dysmorphic features, and thin corpus callosum. {ECO:0000269|PubMed:29276006, ECO:0000269|PubMed:30293988}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P013; IntAct: EBI-767084,EBI-2371709; Score: 0.40
DE  Interaction: Q9Y5V0; IntAct: EBI-2690918,EBI-767084; Score: 0.40
DE  Interaction: Q7L014; IntAct: EBI-767084,EBI-2555356; Score: 0.40
DE  Interaction: P19338; IntAct: EBI-767084,EBI-346967; Score: 0.40
DE  Interaction: Q96IZ7; IntAct: EBI-767084,EBI-712189; Score: 0.40
DE  Interaction: Q9HB71; IntAct: EBI-1047302,EBI-767084; Score: 0.40
DE  Interaction: P55209; IntAct: EBI-767084,EBI-356392; Score: 0.40
DE  Interaction: P07197; IntAct: EBI-767084,EBI-1105035; Score: 0.40
DE  Interaction: Q9H446; IntAct: EBI-767084,EBI-748952; Score: 0.40
DE  Interaction: P07195; IntAct: EBI-767084,EBI-358748; Score: 0.40
DE  Interaction: P31629; IntAct: EBI-2514157,EBI-767084; Score: 0.40
DE  Interaction: Q96IZ5; IntAct: EBI-767084,EBI-740773; Score: 0.40
DE  Interaction: Q92581; IntAct: EBI-21492614,EBI-767084; Score: 0.35
DE  Interaction: P63000-2; IntAct: EBI-11049550,EBI-767084; Score: 0.35
DE  Interaction: P15153; IntAct: EBI-489652,EBI-767084; Score: 0.35
DE  Interaction: Q9BYG5; IntAct: EBI-767084,EBI-295391; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-767084,EBI-638194; Score: 0.56
DE  Interaction: Q8WUI4-6; IntAct: EBI-767084,EBI-12094670; Score: 0.56
DE  Interaction: P30825; IntAct: EBI-4289564,EBI-767084; Score: 0.35
DE  Interaction: P52306; IntAct: EBI-746389,EBI-767084; Score: 0.35
DE  Interaction: Q9UHY1; IntAct: EBI-767084,EBI-749731; Score: 0.56
GO  GO:0005938;
GO  GO:0071944;
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0070062;
GO  GO:0031941;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019901;
GO  GO:0030036;
GO  GO:0007015;
GO  GO:0030031;
GO  GO:0021894;
GO  GO:0030865;
GO  GO:0007163;
GO  GO:0048873;
GO  GO:0035556;
GO  GO:0050885;
GO  GO:0031175;
GO  GO:0033630;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0014041;
GO  GO:0051056;
GO  GO:0007266;
GO  GO:0051932;
GO  GO:0016055;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLI
SQ  CFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSAL
SQ  TQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
//
ID  P0C6Y3;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  11127;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6Y3;
DR  UNIPROT: Q0GNB9;
DR  UNIPROT: Q0GNC0;
DR  UNIPROT: Q5I5Y0;
DR  UNIPROT: Q5I5Y1;
DR  PDB: 2Q6D;
DR  PDB: 2Q6F;
DR  PDB: 5C94;
DR  Pfam: PF16348;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF09401;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF17896;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  Pfam: PF08715;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. Activity of PL-PRO is dependent on zinc (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The peptide p16 might be involved in the EGF signaling pathway. {ECO:0000250}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016896;
GO  GO:0008168;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0032259;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMR
SQ  RLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAG
SQ  TCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  AEIPVESEGWSAILGGHLCYVFKSGDRFYAAPLSGNFALHDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVAELVAA
SQ  IKRGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLKLFQSARVKVEDVWSSLTEKSFEFWRLAYGKVRNLEEFVKTCFC
SQ  KAQMAIVILATVLGEGIWHLVSQVIYKVGGLFTKVVDFCEKYWKGFCAQLKRAKLIVTETLCVLKGVAQHCFQLLLDAIQ
SQ  FMYKSFKKCALGRIHGDLLFWKGGVHKIIQEGDEIWFDAIDSIDVEDLGVVQEKLIDFDVCDNVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVFIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  ETDLTVEQLLSVVYEKMCDDLKLFPEAPEPPPFENVTLVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGDA
SQ  EECDTNLECEEEDEDTKVLALIQDPASNKYPLPLDDDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKALPQKV
SQ  IDVLGDWGEAVDAQEQLCQQESTRVISEKSVEGFTGSCDAMAEQAIVEEQEIVPVVEQSQDVVVFTPADLEVVKETAEEV
SQ  DEFILISAVPKEEVVSQEKEEPQVEQEPTLVVKAQREKKAKKFKVKPATCEKPKFLEYKTCVGDLAVVIAKALDEFKEFC
SQ  IVNAANEHMSHGGGVAKAIADFCGPDFVEYCADYVKKHGPQQKLVTPSFVKGIQCVNNVVGPRHGDSNLREKLVAAYKSV
SQ  LVGGVVNYVVPVLSSGIFGVDFKISIDAMREAFKGCAIRVLLFSLSQEHIDYFDATCKQKTIYLTEDGVKYRSVVLKPGD
SQ  SLGQFGQVFARNKVVFSADDVEDKEILFIPTTDKTILEYYGLDAQKYVTYLQTLAQKWDVQYRDNFVILEWRDGNCWISS
SQ  AIVLLQAAKIRFKGFLAEAWAKLLGGDPTDFVAWCYASCNAKVGDFSDANWLLANLAEHFDADYTNALLKKCVSCNCGVK
SQ  SYELRGLEACIQPVRAPNLLHFKTQYSNCPTCGASSTDEVIEASLPYLLLFATDGPATVDCDENAVGTVVFIGSTNSGHC
SQ  YTQADGKAFDNLAKDRKFGRKSPYITAMYTRFSLRSENPLLVVEHSKGKAKVVKEDVSNLATSSKASFDDLTDFEQWYDS
SQ  NIYESLKVQETPDNLDEYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFTYKLTPDTDENSKTPVYYPVLDSISLRAIW
SQ  VEGSANFVVGHPNYYSKSLRIPTFWENAESFVKMGYKIDGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKI
SQ  LVKAATYVADKVGDGVVRNITDRIKGLCGFTRGHFEKKMSLQFLKTLVFFFFYFLKASSKSLVSSYKIVLCKVVFATLLI
SQ  VWFIYTSNPVVFTGIRVLDFLFEGSLCGPYNDYGKDSFDVLRYCAGDFTCRVCLHDRDSLHLYKHAYSVEQIYKDAASGI
SQ  NFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLSSTVLQTGVGFLDWFVKTVFTHFNFMGAGFYFWLFYKIYVQVHHIL
SQ  YCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVK
SQ  PTAYAYHVVYEACVVDDFVNLKYKAAIPGKDNASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEA
SQ  KNAAVYYAQYLCKPILILDQALYEQLIVEPVSKSVIDKVCSILSNIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIF
SQ  CHNHEVEYTGDGFTNVIPSYGMDTDKLTPRDRGFLINADASIANLRVKNAPPVVWKFSDLIKLSDSCLKYLISATVKSGG
SQ  RFFITKSGAKQVISCHTQKLLVEKKAGGVINNTFKWFMSCFKWLFVFYILFTACCLGYYYMEMNKSFVHPMYDVNSTLHV
SQ  EGFKVIDKGVIREIVSEDNCFSNKFVNFDAFWGKSYENNKNCPIVTVVIDGDGTVAVGVPGFVSWVMDGVMFVHMTQTDR
SQ  RPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVR
SQ  LIVPQQILHTPYIVKFVSDSYCRGSVCEYTKPGYCVSLDSQWVLFNDEYISKPGVFCGSTVRELMFNMVSTFFTGVNPNI
SQ  YIQLATMFLILVVIVLIFAMVIKFQGVFKAYATIVFTIMLVWVINAFVLCVHSYNSVLAVILLVLYCYASMVTSRNTAII
SQ  MHCWLVFTFGLIVPTWLACCYLGFILYMYTPLVFWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGTEFVKLTNEIGD
SQ  KFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEVVYTPPRYSIGVSRLQAGFKKLVSPSSAVEKCIVS
SQ  VSYRGNNLNGLWLGDSIYCPRHVLGKFSGDQWGDVLNLANNHEFEVVTQNGVTLNVVSRRLKGAVLILQTAVANAETPKY
SQ  KFVKANCGDSFTIACSYGGTVIGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEF
SQ  YGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSQPKWLESTTVSIEDYNRWASDNGFTPFSTSTAITKLSAIT
SQ  GVDVCKLLRTIMVKSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTA
SQ  VPLKFYVHAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPW
SQ  MLLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFMKLGFVIYTSSNTLTAYTEGNWELFFELVHTIVLANVSSNSLIGLIVF
SQ  KCAKWMLYYCNATYFNNYVLMAVMVNGIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKVNPPKTVWEVF
SQ  TTNILIQGIGGDRVLPIATVQSKLSDVKCTTVVLMQLLTKLNVEANSKMHAYLVELHNKILASDDVGECMDNLLGMLITL
SQ  FCIDSTIDLGEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKSIYEKVLADSKNGGVTQQELAAYRKAANIAKSVFDRD
SQ  LAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQANSGVVPLATVPIVCSNKLTLVI
SQ  PDPETWVKCVEGVHVTYSTVVWNIDCVTDADGTELHPTSTGSGLTYCISGDNIAWPLKVNLTRNGHNKVDVALQNNELMP
SQ  HGVKTKACVAGVDQAHCSVESKCYYTSISGSSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGDKVEVVYL
SQ  YFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFA
SQ  ITSKPSPTPDQDSYGGASVCLYCRAHIAHPGGAGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCD
SQ  SLRQPKPSVQSVAVASGFDKNYLNRVRGSSEARLIPLANGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQEVRDTEDG
SQ  NLEYCDSYFVVKQTTPSNYEHEKACYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEI
SQ  LVTYGCIEDYHPKWFEENKDWYDPIENPKYYAMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGD
SQ  FQKTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQDLFQKYFKYWDQEYHPNCRDC
SQ  SDDRCLIHCANFNILFSTLVPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALL
SQ  VGTSNKLVDLRTSCFSVCALASGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRP
SQ  TMFDIRQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFESTKKNVLPTITQM
SQ  NLKYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNAPVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKC
SQ  DRAMPNLLRIAASLVLARKHTNCCTWSERVYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSA
SQ  NVARLLSVITRDIVYDDIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGF
SQ  REVLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPRYLPYPDPSRILCACVFVDDLDKTESVAVMERYIAL
SQ  AIDAYPLVHHENEEYKKVFFVLLSYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNS
SQ  QTILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQPGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVF
SQ  GIYRANCAGSENVDDFNQLATTNWSTVEPYILANRCVDSLRRFAAETVKATEELHKQQFASAEVREVLSDRELILSWEPG
SQ  KTRPPLNRNYVFTGFHFTRTSKVQLGDFTFEKGEGKDVVYYRATSTAKLSVGDIFVLTSHNVVSLIAPTLCPQQTFSRFV
SQ  NLRPNVMVPACFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAAYFSNARVVFTACSHAAVDALCEKAFKFLKVDDC
SQ  TRIVPQRTTIDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRT
SQ  LLNGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRQCFKVIVNNGNSDVGHESGSAY
SQ  NITQLEFVKDFVCRNKEWREATFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRA
SQ  KRGILVVMRQRDELYSALKFIELDSVASLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITY
SQ  KHLISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGN
SQ  NFEPVNSKAPPGEQFNHLRALFKSAKPWHVVRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKDQVCSCGS
SQ  RATTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASADAIMTRCLAINNAFCQDVNW
SQ  DLTYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDLNFRFYDKNPIVPNVKQFEYDYNQHKD
SQ  KFADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFHTPKFDRTSFRNLKAMPFFFYDSSPCETI
SQ  QLDGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYADFVTSYNAAVTAGFTFWVTNNFNPYNLWKSFSALQSIDNIAYNM
SQ  YKGGHYDAIAGEMPTIVTGDKVFVIDQGVEKAVFFNQTILPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYT
SQ  NQTPLYRNTVKVCAYTDIEPNGLIVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGIPLKDGANLYVY
SQ  KRVNGAFVTLPNTLNTQGRSYETFEPRSDVERDFLDMSEESFVEKYGKELGLQHILYGEVDKPQLGGLHTVIGMCRLLRA
SQ  NKLNAKSVTNSDSDVMQNYFVLADNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMAWFEDGI
SQ  IKTCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGIALPSGIMMNVAKYTQLCQYLSKTTMCVPHNMRVMHFGAG
SQ  SDKGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYKTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDV
SQ  FIYLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLVGVNYLGASEKVKVSGKTLHANY
SQ  IFWRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM
//
ID  O35413;
PN  Sorbin and SH3 domain-containing protein 2;
GN  Sorbs2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873, ECO:0000269|PubMed:15659545, ECO:0000269|PubMed:16125169}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Note=Detected in the stress fibers, synaptosomal cytosol, postsynaptic density fraction, Z-disks and intercalated. The CBL/PTK2B/ARGBP2 complex is recruited to lipid rafts following growth factor stimulation. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250|UniProtKB:O94875}.
DR  UNIPROT: O35413;
DR  UNIPROT: Q923T8;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF02208;
DR  PROSITE: PS50002;
DR  PROSITE: PS50831;
DE  Function: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000250, ECO:0000250|UniProtKB:O94875, ECO:0000269|PubMed:10521485}.
DE  Reference Proteome: Yes;
DE  Interaction: P49286; IntAct: EBI-7458031,EBI-1188341; Score: 0.37
GO  GO:0016324;
GO  GO:0030425;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0003676;
GO  GO:0019904;
GO  GO:0095500;
GO  GO:0007015;
GO  GO:0061049;
GO  GO:0007219;
GO  GO:1904393;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDK
SQ  KSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEE
SQ  EKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPA
SQ  AKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQH
SQ  ERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSR
SQ  AQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCD
SQ  DLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLM
SQ  NSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCP
SQ  KRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFD
SQ  HFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPF
SQ  RRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQP
SQ  FHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEV
SQ  KLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAI
SQ  AKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSL
SQ  SSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
//
ID  O75147;
PN  Obscurin-like protein 1;
GN  OBSL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24793695}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons (PubMed:21572988).
DR  UNIPROT: O75147;
DR  UNIPROT: A4KVA4;
DR  UNIPROT: A4KVA5;
DR  UNIPROT: Q96IW3;
DR  UNIPROT: S4R3M6;
DR  PDB: 2CPC;
DR  PDB: 2E6P;
DR  PDB: 2E6Q;
DR  PDB: 2LU7;
DR  PDB: 2LVC;
DR  PDB: 2WP3;
DR  PDB: 2WWK;
DR  PDB: 2WWM;
DR  PDB: 3KNB;
DR  PDB: 5FM5;
DR  Pfam: PF07679;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DR  OMIM: 610991;
DR  OMIM: 612921;
DR  DisGeNET: 23363;
DE  Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.
DE  Disease: 3M syndrome 2 (3M2) [MIM:612921]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies. {ECO:0000269|PubMed:19481195, ECO:0000269|PubMed:23018678}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q92844; IntAct: EBI-356349,EBI-1223896; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-1223896,EBI-352682; Score: 0.37
DE  Interaction: Q8IYT8; IntAct: EBI-714340,EBI-1223896; Score: 0.35
DE  Interaction: Q8WVZ9; IntAct: EBI-473695,EBI-1223896; Score: 0.40
DE  Interaction: Q96RR4; IntAct: EBI-1104575,EBI-1223896; Score: 0.40
DE  Interaction: Q8IYM1; IntAct: EBI-2585067,EBI-1223896; Score: 0.37
DE  Interaction: A7MCY6; IntAct: EBI-359969,EBI-1223896; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-73946,EBI-1223896; Score: 0.53
DE  Interaction: Q15759; IntAct: EBI-298304,EBI-1223896; Score: 0.35
DE  Interaction: P02768; IntAct: EBI-714423,EBI-1223896; Score: 0.35
DE  Interaction: Q8NEP3; IntAct: EBI-11906667,EBI-1223896; Score: 0.51
DE  Interaction: C5E524; IntAct: EBI-12561527,EBI-1223896; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-6050648,EBI-1223896; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-1223896; Score: 0.35
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0014704;
GO  GO:0031430;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0008093;
GO  GO:0055003;
GO  GO:0007010;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0050775;
GO  GO:0043687;
GO  GO:0034067;
GO  GO:0007088;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPVVVWEKGGQQLAASERLSFPADGAEHGLLLTAALPTDAG
SQ  VYVCRARNAAGEAYAAAAVTVLEPPASDPELQPAERPLPSPGSGEGAPVFLTGPRSQWVLRGAEVVLTCRAGGLPEPTLY
SQ  WEKDGMALDEVWDSSHFALQPGRAEDGPGASLALRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPPESPPADPDEA
SQ  PAPVVEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHWEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCA
SQ  ARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIAVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLIIH
SQ  RLKADDDGIYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETLEAGVEGRWSRDGEELPVICQSSSGHMH
SQ  ALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPILAEMFKGHKNTVLLTWKPPEPAPETPFIYRLERQEVGS
SQ  EDWIQCFSIEKAGAVEVPGDCVPSEGDYRFRICTVSGHGRSPHVVFHGSAHLVPTARLVAGLEDVQVYDGEDAVFSLDLS
SQ  TIIQGTWFLNGEELKSNEPEGQVEPGALRYRIEQKGLQHRLILHAVKHQDSGALVGFSCPGVQDSAALTIQESPVHILSP
SQ  QDRVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESELLVVKMDGRKHRLILPEAKVQDSGEFECRTEGVSAFFGVT
SQ  VQDPPVHIVDPREHVFVHAITSECVMLACEVDREDAPVRWYKDGQEVEESDFVVLENEGPHRRLVLPATQPSDGGEFQCV
SQ  AGDECAYFTVTITDVSSWIVYPSGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLQKEDTVRRLVLPAV
SQ  QLEDSGEYLCEIDDESASFTVTVTEPPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKDGLEVEESEALVLERD
SQ  GPRCRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLHFGAPGRVELRCEVAPAGSQVRWYKDGLE
SQ  VEASDALQLGAEGPTRTLTLPHAQPEDAGEYVCETRHEAITFNVILAEPPVQFLALETTPSPLCVAPGEPVVLSCELSRA
SQ  GAPVVWSHNGRPVQEGEGLELHAEGPRRVLCIQAAGPAHAGLYTCQSGAAPGAPSLSFTVQVAEPPVRVVAPEAAQTRVR
SQ  STPGGDLELVVHLSGPGGPVRWYKDGERLASQGRVQLEQAGARQVLRVQGARSGDAGEYLCDAPQDSRIFLVSVEEPLLV
SQ  KLVSELTPLTVHEGDDATFRCEVSPPDADVTWLRNGAVVTPGPQVEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSA
SQ  RLHVRETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHDSRLSMAQDGHIHRLFIHGVILADQGTY
SQ  GCESHHDRTLARLSVRPRQLRVLRPLEDVTISEGGSATFQLELSQEGVTGEWARGGVQLYPGPKCHIHSDGHRHRLVLNG
SQ  LGLADSGCVSFTADSLRCAARLIVREVPVTIVRGPHDLEVTEGDTATFECELSQALADVTWEKDGNALTPSPRLRLQALG
SQ  TRRLLQLRRCGPSDAGTYSCAVGTARAGPVRLTVRERTVAVLSELRSVSAREGDGATFECTVSEVETTGRWELGGRPLRP
SQ  GARVRIRQEGKKHILVLSELRAEDAGEVRFQAGPAQSLALLEVEALPLQMCRHPPREKTVLVGRRAVLEVTVSRSGGHVC
SQ  WLREGAELCPGDKYEMRSHGPTHSLVIHDVRPEDQGTYCCQAGQDSTHTRLLVEGN
//
ID  Q5NCP0;
PN  E3 ubiquitin-protein ligase RNF43;
GN  Rnf43;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Note=May be secreted. {ECO:0000250}.
DR  UNIPROT: Q5NCP0;
DR  UNIPROT: B2KGH3;
DR  UNIPROT: Q6DI76;
DR  UNIPROT: Q8BME0;
DR  UNIPROT: Q8C191;
DR  UNIPROT: Q8K0X4;
DR  Pfam: PF13639;
DR  Pfam: PF18212;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (PubMed:22895187). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity). {ECO:0000250|UniProtKB:P0DPR2, ECO:0000269|PubMed:22895187}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005109;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0007275;
GO  GO:0030178;
GO  GO:0016567;
GO  GO:0072089;
GO  GO:0006511;
GO  GO:0038018;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGGHQLQLAVLWPWLLMATLHAGFGHTGRVLAAAVESERSAEQKAVIRVIPLKMDPTGKLNLTLEGVFAGVAEVTPAEG
SQ  KLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGANAVLFDITEDRSAAEQLQQPLGLTKP
SQ  VVLIWGSDAAKLMEFVYKNRKAYVWIELKEPPAGANYDVWILLTVVGTVFVIILASVLRIRCRPHHSRPDPLQQRTARAI
SQ  SQLATRRYQAGCRRARAEWPDSGSSCSSTPVCAICLEEFSEGQELRVISCLHEFHRTCVDPWLYQHRTCPLCMFNIVEGD
SQ  SFSQAPAASPSYQEPGRRLHLIRQHPGHAHYHLPSAYLLGPSRTSVARTPRPRPFLPSQEPSMGSRHQRLPRTSHLRAPE
SQ  EQQHLAVSPHPYAQGWGLNRLRCTSQHPAACPVALRRARPHESSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVV
SQ  NCTDVSLQGIHGSSSTFRSSLSSDFDPLVYCSPEGDLQGKGIQPSVTSRPRSLDSVVPRGETQVSSHIHYHRHRHHHYKR
SQ  QFQWHGRKPGPETGIPQSMPAASHTQLEPSLPDQQLITPNPTASSMLPNPQRPRALTEPAPGLAEASSPSPSPKPNPSGL
SQ  LNLQKSSLTVRHPHRKRRGGPSEPLPTSLPPDLTVHTACPVFPHYSPRLAYPWPPEVHPLMFRPPGPDRRLLHEVPGPCY
SQ  SSSQPVWLYLNPCQPLGPCLPGEGHSKWTFDSPEGRRCPYSHCQVLPAQPGSEEELEELCEQAV
//
ID  P41933;
PN  Nuclear hormone receptor family member odr-7;
GN  odr;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region.
DR  UNIPROT: P41933;
DR  UNIPROT: C3U4U8;
DR  UNIPROT: C3U4U9;
DR  UNIPROT: C3U4V2;
DR  Pfam: PF00105;
DR  PROSITE: PS00031;
DR  PROSITE: PS51030;
DE  Function: Required for the function of one pair of chemosensory neurons called AWA neurons that are involved in chemotaxis to volatile odorants. Acts in a pathway that specifies olfactory neuronal fate. Regulates the transcription of olfactory signaling molecules such as odr-10 that specify AWA neuron identity and function. Represses the expression in AWA neurons of factors such as str-2 which specify AWC neuron identity. {ECO:0000269|PubMed:10421632, ECO:0000269|PubMed:11018015, ECO:0000269|PubMed:11546744, ECO:0000269|PubMed:14704165, ECO:0000269|PubMed:8601313}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EFI7; IntAct: EBI-6731836,EBI-6731843; Score: 0.37
DE  Interaction: O45291; IntAct: EBI-6736645,EBI-6731836; Score: 0.37
DE  Interaction: Q19418; IntAct: EBI-2315670,EBI-6731836; Score: 0.37
DE  Interaction: Q22289; IntAct: EBI-6731836,EBI-6726526; Score: 0.37
DE  Interaction: Q9NAE4; IntAct: EBI-332523,EBI-6731836; Score: 0.37
DE  Interaction: Q9TXN8; IntAct: EBI-6726742,EBI-6731836; Score: 0.37
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0043565;
GO  GO:0008270;
GO  GO:0022401;
GO  GO:0050918;
GO  GO:0045944;
GO  GO:0006357;
GO  GO:0007608;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MIVPDTEGLLIYSYGLMYGSYCMACQMLIPHFQCIPGIFPNFRISTELIKTMTDKLEQPNNNVPQQPWGPFPPAFGGRPS
SQ  GEQTDGNPGEFDNDAAHQQTAPFMTHFFPRIGLQFPDFTEYQRFNGFQRNAFFPNPFGSQFTGQAFAQSFPLHNSMTTMD
SQ  GFNLTHAPHPFSTNTNSTKPKDIENTVQSTIKHSSENIQDKPPVLSVEYPVKYDSELKFDANVDFTAVPKQESSDDSTLK
SQ  NLKKSDQQLQQPQQFTFPPPLLAEKSFEQPRMREDVLPFHPQFYPAPLDMGTNFKQEMRTPPIDGHIDYRKFDASGKRME
SQ  FQPPGALHDCQVCLSTHANGLHFGARTCAACAAFFRRTISDDKRYVCKRNQRCNNASRDGTGYRKICRSCRMKRCLEIGM
SQ  LPENVQHKRNRRDSGSPPRKTPFDTFFNGFYPSFQPSGSAAQPITVSSSESPRHTTN
//
ID  O43502;
PN  DNA repair protein RAD51 homolog 3;
GN  RAD51C;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA.
DR  UNIPROT: O43502;
DR  UNIPROT: O43503;
DR  UNIPROT: Q3B783;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  OMIM: 602774;
DR  OMIM: 613390;
DR  OMIM: 613399;
DR  DisGeNET: 5889;
DE  Function: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD21 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1- BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA- dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross- link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:19451272, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
DE  Disease: Fanconi anemia complementation group O (FANCO) [MIM:613390]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:20400963, ECO:0000269|PubMed:24141787}. Note=The disease is caused by mutations affecting the gene represented in this entry. Breast-ovarian cancer, familial, 3 (BROVCA3) [MIM:613399]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:20400964, ECO:0000269|PubMed:21990120, ECO:0000269|PubMed:24141787}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-2849976,EBI-2267048; Score: 0.93
DE  Interaction: O75173; IntAct: EBI-3934482,EBI-2267048; Score: 0.35
DE  Interaction: Q6JEL2; IntAct: EBI-2267048,EBI-6426253; Score: 0.35
DE  Interaction: Q96MF4; IntAct: EBI-2267048,EBI-21802615; Score: 0.35
DE  Interaction: P43378; IntAct: EBI-2267048,EBI-742898; Score: 0.35
DE  Interaction: O43543; IntAct: EBI-3918457,EBI-2267048; Score: 0.67
DE  Interaction: Q86YZ3; IntAct: EBI-2267048,EBI-1047017; Score: 0.40
DE  Interaction: Q8IZS8; IntAct: EBI-2267048,EBI-2267087; Score: 0.40
DE  Interaction: O00571; IntAct: EBI-2267048,EBI-353779; Score: 0.40
DE  Interaction: O15315; IntAct: EBI-2267048,EBI-2824089; Score: 0.87
DE  Interaction: Q8TBP5; IntAct: EBI-18636064,EBI-2267048; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-1753048,EBI-2267048; Score: 0.35
DE  Interaction: Q15768; IntAct: EBI-3908475,EBI-2267048; Score: 0.35
DE  Interaction: Q5T8I9; IntAct: EBI-9675710,EBI-2267048; Score: 0.35
DE  Interaction: Q9HBV2; IntAct: EBI-17498703,EBI-2267048; Score: 0.35
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033063;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0008821;
GO  GO:0003677;
GO  GO:0008094;
GO  GO:0007596;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0007066;
GO  GO:0007141;
GO  GO:0010971;
GO  GO:0007131;
GO  GO:0007062;
GO  GO:0007283;
GO  GO:0000722;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSE
SQ  SHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDT
SQ  EGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVI
SQ  VDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRK
SQ  QRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL
//
ID  Q14244;
PN  Ensconsin;
GN  MAP7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Basolateral cell membrane. Cytoplasm, cytoskeleton. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike- like bundles facing intercellular contacts.
DR  UNIPROT: Q14244;
DR  UNIPROT: B7Z290;
DR  UNIPROT: B7Z400;
DR  UNIPROT: B7Z5S7;
DR  UNIPROT: B7Z9U7;
DR  UNIPROT: C9JPS0;
DR  UNIPROT: E9PCP3;
DR  UNIPROT: F5H1E2;
DR  UNIPROT: Q7Z6S0;
DR  UNIPROT: Q8TAU5;
DR  UNIPROT: Q9NY82;
DR  UNIPROT: Q9NY83;
DR  Pfam: PF05672;
DR  OMIM: 604108;
DR  DisGeNET: 9053;
DE  Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:11719555, ECO:0000269|PubMed:8408219, ECO:0000269|PubMed:9989799}.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-357515,EBI-2211064; Score: 0.35
DE  Interaction: Q14203; IntAct: EBI-724352,EBI-2211064; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-359832,EBI-2211064; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-2211064; Score: 0.35
DE  Interaction: Q86V81; IntAct: EBI-347640,EBI-2211064; Score: 0.35
DE  Interaction: P61457; IntAct: EBI-740475,EBI-2211064; Score: 0.40
DE  Interaction: E9QKK1; IntAct: EBI-10967445,EBI-2211064; Score: 0.35
DE  Interaction: Q2KHM9; IntAct: EBI-2805604,EBI-2211064; Score: 0.35
DE  Interaction: Q86VQ0; IntAct: EBI-6658186,EBI-2211064; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-4283704,EBI-2211064; Score: 0.35
DE  Interaction: P62714; IntAct: EBI-1044367,EBI-2211064; Score: 0.35
DE  Interaction: Q8TF05; IntAct: EBI-1056262,EBI-2211064; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079353,EBI-2211064; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-8322817,EBI-2211064; Score: 0.35
DE  Interaction: Q9Y3M2; IntAct: EBI-2211064,EBI-947308; Score: 0.51
DE  Interaction: O95273; IntAct: EBI-748961,EBI-2211064; Score: 0.37
DE  Interaction: Q6NSX1; IntAct: EBI-6873045,EBI-2211064; Score: 0.56
DE  Interaction: Q8N3C7; IntAct: EBI-2211064,EBI-5655540; Score: 0.56
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-2211064; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-2361917,EBI-2211064; Score: 0.35
DE  Interaction: Q8NC26; IntAct: EBI-2211064,EBI-10265237; Score: 0.56
GO  GO:0030424;
GO  GO:0016323;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0005102;
GO  GO:0005198;
GO  GO:0007163;
GO  GO:0000226;
GO  GO:0072659;
GO  GO:0006970;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELGAGGDGHRGGDGAVRSETAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQ
SQ  LAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRW
SQ  SWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARS
SQ  KSTAALSGEAASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPK
SQ  ARQPARSRLWLPSKSLPHLPGTPRPTSSLPPGSVKAAPAQVRPPSPGNIRPVKREVKVEPEKKDPEKEPQKVANEPSLKG
SQ  RAPLVKVEEATVEERTPAEPEVGPAAPAMAPAPASAPAPASAPAPAPVPTPAMVSAPSSTVNASASVKTSAGTTDPEEAT
SQ  RLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQRQAEERALREREE
SQ  AERAQRQKEEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATDKKTSDQRNGDIAKGALTGGTEVS
SQ  ALPCTTNAPGNGKPVGSPHVVTSHQSKVTVESTPDLEKQPNENGVSVQNENFEEIINLPIGSKPSRLDVTNSESPEIPLN
SQ  PILAFDDEGTLGPLPQVDGVQTQQTAEVI
//
ID  Q13330;
PN  Metastasis-associated protein MTA1;
GN  MTA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform Short]: Cytoplasm. [Isoform Long]: Nucleus. Nucleus envelope. Cytoplasm. Cytoplasm, cytoskeleton. Note=Associated with microtubules. Localization at the nuclear envelope is TPR-dependent.
DR  UNIPROT: Q13330;
DR  UNIPROT: A5PLK4;
DR  UNIPROT: Q86SW2;
DR  UNIPROT: Q8NFI8;
DR  UNIPROT: Q96GI8;
DR  PDB: 4BKX;
DR  PDB: 4PBY;
DR  PDB: 4PBZ;
DR  PDB: 4PC0;
DR  PDB: 5FXY;
DR  PDB: 5ICN;
DR  PDB: 6G16;
DR  Pfam: PF01426;
DR  Pfam: PF01448;
DR  Pfam: PF00320;
DR  Pfam: PF17226;
DR  Pfam: PF00249;
DR  PROSITE: PS51038;
DR  PROSITE: PS51156;
DR  PROSITE: PS51293;
DR  OMIM: 603526;
DR  DisGeNET: 9112;
DE  Function: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone- deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK- ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity). {ECO:0000250|UniProtKB:Q8K4B0, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24413532}.
DE  Reference Proteome: Yes;
DE  Interaction: P36957; IntAct: EBI-351007,EBI-714236; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-523590,EBI-714236; Score: 0.35
DE  Interaction: Q14839; IntAct: EBI-372916,EBI-714236; Score: 0.53
DE  Interaction: P03372; IntAct: EBI-78473,EBI-714236; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-301834,EBI-714236; Score: 0.90
DE  Interaction: Q09028; IntAct: EBI-620823,EBI-714236; Score: 0.78
DE  Interaction: Q16576; IntAct: EBI-352227,EBI-714236; Score: 0.53
DE  Interaction: Q5S007; IntAct: EBI-714236,EBI-5323863; Score: 0.44
DE  Interaction: Q92769; IntAct: EBI-301821,EBI-714236; Score: 0.80
DE  Interaction: P43364-2; IntAct: EBI-714236,EBI-10178634; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-714236,EBI-10171774; Score: 0.56
DE  Interaction: Q13422; IntAct: EBI-714236,EBI-745305; Score: 0.56
DE  Interaction: Q5VWX1; IntAct: EBI-714236,EBI-742808; Score: 0.56
DE  Interaction: Q6A162; IntAct: EBI-10171697,EBI-714236; Score: 0.67
DE  Interaction: Q6FGM0; IntAct: EBI-10173690,EBI-714236; Score: 0.56
DE  Interaction: P21673; IntAct: EBI-714236,EBI-711613; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-945833,EBI-714236; Score: 0.56
DE  Interaction: O00505; IntAct: EBI-358297,EBI-714236; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-714236,EBI-741037; Score: 0.56
DE  Interaction: Q99497; IntAct: EBI-1164361,EBI-714236; Score: 0.35
DE  Interaction: Q9BTC8; IntAct: EBI-2461787,EBI-714236; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-710124,EBI-714236; Score: 0.53
DE  Interaction: Q96KQ7; IntAct: EBI-744366,EBI-714236; Score: 0.58
DE  Interaction: Q92560; IntAct: EBI-714236,EBI-1791447; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-714236,EBI-302023; Score: 0.35
DE  Interaction: Q86YP4; IntAct: EBI-714236,EBI-726224; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-714236,EBI-351896; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-714236,EBI-456067; Score: 0.35
DE  Interaction: P52732; IntAct: EBI-714236,EBI-355697; Score: 0.35
DE  Interaction: O60315; IntAct: EBI-714236,EBI-717614; Score: 0.61
DE  Interaction: P04004; IntAct: EBI-714236,EBI-1036653; Score: 0.35
DE  Interaction: O14744; IntAct: EBI-714236,EBI-351098; Score: 0.35
DE  Interaction: Q8WXI9; IntAct: EBI-714236,EBI-923440; Score: 0.35
DE  Interaction: O95983; IntAct: EBI-714236,EBI-1783068; Score: 0.60
DE  Interaction: O35207; IntAct: EBI-11100491,EBI-714236; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-6253193,EBI-714236; Score: 0.35
DE  Interaction: O14519; IntAct: EBI-1052532,EBI-714236; Score: 0.53
DE  Interaction: P04040; IntAct: EBI-2432181,EBI-714236; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-618309,EBI-714236; Score: 0.35
DE  Interaction: P68431; IntAct: EBI-79722,EBI-714236; Score: 0.35
DE  Interaction: P0DPK4; IntAct: EBI-714236,EBI-22310682; Score: 0.56
DE  Interaction: A8E1C4; IntAct: EBI-6148716,EBI-714236; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-714236; Score: 0.35
DE  Interaction: Q9NVP1; IntAct: EBI-714236,EBI-724378; Score: 0.37
DE  Interaction: O15530; IntAct: EBI-717097,EBI-714236; Score: 0.35
DE  Interaction: P46734; IntAct: EBI-602462,EBI-714236; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-396343,EBI-714236; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-948001,EBI-714236; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-3867333,EBI-714236; Score: 0.56
DE  Interaction: Q99961; IntAct: EBI-697911,EBI-714236; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-79165,EBI-714236; Score: 0.56
DE  Interaction: Q58EX7; IntAct: EBI-949255,EBI-714236; Score: 0.56
DE  Interaction: P26358; IntAct: EBI-719459,EBI-714236; Score: 0.35
DE  Interaction: Q8IXH7; IntAct: EBI-714236,EBI-536725; Score: 0.37
DE  Interaction: P32249; IntAct: EBI-714236,EBI-715171; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016581;
GO  GO:0003682;
GO  GO:0042826;
GO  GO:0000978;
GO  GO:0001103;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0008270;
GO  GO:0032922;
GO  GO:0006302;
GO  GO:0043153;
GO  GO:0016575;
GO  GO:0045475;
GO  GO:0000122;
GO  GO:1902499;
GO  GO:0043161;
GO  GO:0040029;
GO  GO:0010212;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEE
SQ  GEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTL
SQ  LADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHM
SQ  SAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSL
SQ  TSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQ
SQ  SYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTR
SQ  IARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVL
SQ  SSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSL
SQ  PPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
//
ID  Q9U1H9;
PN  Nuclear RNA export factor 1;
GN  sbr;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:14729961}. Cytoplasm {ECO:0000269|PubMed:14729961}. Nucleus envelope {ECO:0000269|PubMed:14729961}. Note=Localized in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:14729961}.
DR  UNIPROT: Q9U1H9;
DR  UNIPROT: Q9NFQ2;
DR  UNIPROT: Q9NFQ3;
DR  UNIPROT: Q9VZ65;
DR  UNIPROT: Q9VZ68;
DR  PDB: 6IHJ;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DE  Function: Mediates the export of the majority of mRNAs from the nucleus to the cytoplasm. {ECO:0000269|PubMed:11779805, ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:11780634}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9V813; IntAct: EBI-124076,EBI-144932; Score: 0.37
DE  Interaction: Q24114; IntAct: EBI-86112,EBI-144932; Score: 0.35
DE  Interaction: Q9V3H8; IntAct: EBI-144932,EBI-160435; Score: 0.27
DE  Interaction: Q9UKK6; IntAct: EBI-301889,EBI-144932; Score: 0.35
DE  Interaction: Q9VFS4; IntAct: EBI-144932,EBI-134023; Score: 0.37
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0047485;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0051168;
GO  GO:0016973;
GO  GO:0046833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKRGGGSSQRYNNNVGNGGGRYNAPEDFDDFDVEDRQRRKDRNKRRVSFKPSQCLHNKKDIKLRPEDLRRWDEDDDMSD
SQ  MTTAVKDRPTSRRRGSPIPRGKFGKLMPNSFGWYQVTLQNAQIYEKETLLSALLAAMSPHVFIPQYWRVERNCVIFFTDD
SQ  YEAAERIQHLGKNGHLPDGYRLMPRVRSGIPLVAIDDAFKEKMKVTMAKRYNIQTKALDLSRFHADPDLKQVFCPLFRQN
SQ  VMGAAIDIMCDNIPDLEALNLNDNSISSMEAFKGVEKRLPNLKILYLGDNKIPSLAHLVVLRNLSILELVLKNNPCRSRY
SQ  KDSQQFISEVRRKFPKLVKLDGETLEPQITFDLSEQGRLLETKASYLCDVAGAEVVRQFLDQYFRIFDSGNRQALLDAYH
SQ  EKAMLSISMPSASQAGRLNSFWKFNRNLRRLLNGEENRTRNLKYGRLACVSTLDEWPKTQHDRRTFTVDLTIYNTSMMVF
SQ  TVTGLFKELNDETNNPASMELYDVRHFARTYVVVPQNNGFCIRNETIFITNATHEQVREFKRSQHQPAPGAMPSTSSAVT
SQ  SPQAGAAAGLQGRLNALGVATGPVAILSGDPLAATAPVNSGSAAISTTAVAPGAQDESTKMQMIEAMSAQSQMNVIWSRK
SQ  CLEETNWDFNHAAFVFEKLFKENKIPPEAFMK
//
ID  P70496;
PN  Phospholipase D1;
GN  Pld1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Membrane-associated.
DR  UNIPROT: P70496;
DR  UNIPROT: O08959;
DR  UNIPROT: O35856;
DR  UNIPROT: O54765;
DR  UNIPROT: P70497;
DR  UNIPROT: Q9QWJ6;
DR  Pfam: PF00169;
DR  Pfam: PF00614;
DR  Pfam: PF13091;
DR  Pfam: PF00787;
DR  PROSITE: PS50003;
DR  PROSITE: PS50035;
DR  PROSITE: PS50195;
DE  Function: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0098981;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0031985;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0031902;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0031982;
GO  GO:0070290;
GO  GO:0035091;
GO  GO:0004630;
GO  GO:0048870;
GO  GO:0050830;
GO  GO:0048017;
GO  GO:0006654;
GO  GO:0008654;
GO  GO:0009395;
GO  GO:0030335;
GO  GO:0032534;
GO  GO:0098693;
GO  GO:0043434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:11121416};
SQ  MSLRSEARVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPTAQEACIPFSSIYNTQGFKEPNIQIYLSGCP
SQ  VKAQVLEVERFTSTSRMPSVNLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREM
SQ  PSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNC
SQ  CGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWG
SQ  GAIEEFIQKHGTDFLKDHRFGSYAAVHENILAKWYVNAKGYFEDIANAMEGATEEIFITDWWLSPEIFLKRPVVEGNRWR
SQ  LDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGI
SQ  DLAYGRWDDNEHRLTDVGSVKRVTSGQSLGSLTAASVESMESLSLKDKHQSHKNEPVLKSVNDTDMKLKGIGKSRKFSKF
SQ  SLYRQLHRRNLHNSDSISSVDSASSYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSADTGSIRSVQTGVGELHGE
SQ  TRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLL
SQ  PKSQATAHELRYQVPGAVHAKAQLLRSAADWSAGIKHHEESIHAAYTHVIENSKHYIYIENQFFISCADDKVVFNKVGNA
SQ  IAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRT
SQ  HAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFAQGLRLECF
SQ  RLVLGYLSDPSEDIQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDRLRAEEELRKI
SQ  RGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT
//
ID  Q13875;
PN  Myelin-associated oligodendrocyte basic protein;
GN  MOBP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Present in the major dense line of CNS myelin. {ECO:0000250}.
DR  UNIPROT: Q13875;
DR  UNIPROT: A8K2C2;
DR  UNIPROT: G5E945;
DR  UNIPROT: Q13874;
DR  UNIPROT: Q6DHZ6;
DR  UNIPROT: Q8TBJ1;
DR  Pfam: PF02318;
DR  OMIM: 600948;
DR  DisGeNET: 4336;
DE  Function: May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P60370; IntAct: EBI-10230628,EBI-10172150; Score: 0.56
DE  Interaction: P60409; IntAct: EBI-10172290,EBI-10230628; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-10172052,EBI-10230628; Score: 0.72
DE  Interaction: P36957; IntAct: EBI-351007,EBI-10230628; Score: 0.40
DE  Interaction: Q6A162; IntAct: EBI-10171697,EBI-10230628; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10171774,EBI-10230628; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-10230628; Score: 0.56
GO  GO:0030864;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0017137;
GO  GO:0019911;
GO  GO:0007399;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRP
SQ  KQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQP
SQ  RSSPLRGPGASRGGSPVKASRFW
//
ID  B3H5K9;
PN  Protein NEDD1;
GN  NEDD1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:25438942}. Note=First detected in prophase on the nuclear envelope, where it appeared to cap the future spindle poles. Later detected along kinetochore microtubules (MTs) of the metaphase spindle, with more prominent signals toward the poles. In anaphase, detected with the shortening kinetochore fibers. In the developing phragmoplast, localized mainly toward the minus end of MTs. {ECO:0000269|PubMed:19383896}.
DR  UNIPROT: B3H5K9;
DR  UNIPROT: B6EUA6;
DR  UNIPROT: Q9FI89;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulates microtubules organization in a centrosome- independent manner. Required for the spindle to be positioned correctly and for the function of gamma-tubulin in organizing phragmoplast microtubules (PubMed:19383896). Component of active gamma-tubulin ring complexes (gamma-TuRCs) associated with cortical microtubules in interphase cells (PubMed:25438942). Mediates gamma-TuRC recruitment to the nucleation sites and is important for determining the ratio of branched to parallel nucleation (PubMed:25438942). May mediate the localization of GCP2 and GCP3 to the nuclear envelope (PubMed:19383896). {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005828;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0000919;
GO  GO:0009553;
GO  GO:0009555;
GO  GO:0032467;
GO  GO:0060236;
GO  GO:2000694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMSNLVEPSWRLLAASGGDTVKLFDVSADSGDPCVLSYTPSPGCAVNSVKWNHTNLVVASTGEDKKISLWRKNGQSLGTV
SQ  PVTGKDGGDSAEECLSAISFSKKGSRYICSGGTGQIVKIWDLQRKLCIKKLKGHTSTITGVMYNCKDEHLASVSVGGDLI
SQ  VHNLASGARATELKDPNGQVLRLLDYSRSSRHLLVTAGDDGTVHLWDTTGRSPKMSWLKQHSAPTAGVCFSPSNEKIIAS
SQ  VGMDKKLYTYDSGSRRSSSCIAYEAPFSSLAFGDNGYILVAGTSNGRVVFYDIRGKPQPVTVLHAFSNSEDVTSLSWQTS
SQ  KPVIVNEKNYTSEMALLGSTVEDSVVIPDPLPSTTPSASQSAMAPGSRGVSASTVNASSVEQTPNRNHLWPSGPLGRLHA
SQ  LRANDSYNDDMGVFSPIIDVSSVEKWADSEGYNNKDHLVVDNKPSSLLFPSSSKGYSFGDNGSKEHPIFDWKPSSTSKQD
SQ  DPRAAFSSFGSITPTASSKSEDSALTPPEAWGGDKFSEKFNQLANEKFSDKFSHLHAPSRLAVSSTGASTSGSMFSSSRD
SQ  FPLSHGQTNFANASLEFPRIRDFSSTFETSSTQTDNNLPSSPLFTKGITAPGNIDSLRLSPNFTRRFSTYAERISTTSSF
SQ  SDGASLSLGGSPKIKKTGSETREEVLNHLLARPETVVATEAGAMPLMNQGGLKQSQTDQQQVMGSSNFTLQLFQRTLEGT
SQ  LDSFQNSIHDDVRNLHIEILRQFHMHEMEMSKVLSSILENQAEQMKELKLLRKENQELRQRL
//
ID  P27815;
PN  cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
GN  PDE4A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm, perinuclear region. [Isoform 2]: Cytoplasm, perinuclear region. Cell projection, ruffle membrane. [Isoform 4]: Membrane; Peripheral membrane protein. Note=Isoform 4 has propensity for association with membranes. [Isoform 6]: Cytoplasm, perinuclear region. [Isoform 7]: Cytoplasm. Membrane. Note=Predominantly cytoplasmic.
DR  UNIPROT: P27815;
DR  UNIPROT: O75522;
DR  UNIPROT: O76092;
DR  UNIPROT: Q16255;
DR  UNIPROT: Q16691;
DR  UNIPROT: Q5DM53;
DR  UNIPROT: Q6PMT2;
DR  UNIPROT: Q8IVA7;
DR  UNIPROT: Q8WUQ3;
DR  UNIPROT: Q9H3H2;
DR  PDB: 2QYK;
DR  PDB: 3I8V;
DR  PDB: 3TVX;
DR  Pfam: PF18100;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DR  OMIM: 600126;
DR  DisGeNET: 5141;
DE  Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:11566027, ECO:0000269|PubMed:17727341}.
DE  Reference Proteome: Yes;
DE  Interaction: P27987; IntAct: EBI-751388,EBI-1384345; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-299649,EBI-1384345; Score: 0.40
DE  Interaction: O75344; IntAct: EBI-744771,EBI-1384345; Score: 0.35
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0004115;
GO  GO:0030552;
GO  GO:0046872;
GO  GO:0006198;
GO  GO:0035690;
GO  GO:0007186;
GO  GO:0043949;
GO  GO:0010738;
GO  GO:0007608;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQPHRPIERADAMDTSDRPGLR
SQ  TTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGRSPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKT
SQ  MSRNSSVTSEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
SQ  CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEIPSPTMKEREKQQAPRPRPSQ
SQ  PPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTDQEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQ
SQ  ERDLLKKFRIPVDTMVTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SQ  SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMV
SQ  ETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEK
SQ  SQVGFIDYIVHPLWETWADLVHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
SQ  ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLTQQAQSTGSAPVAPDEFSSRE
SQ  EFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLPSTAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGG
SQ  SGGDPT
//
ID  P03600;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  928299;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000269|PubMed:10864669}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.
DR  UNIPROT: P03600;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000269|PubMed:16453750, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000269|PubMed:11883002, ECO:0000269|PubMed:16453534}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins (PubMed:1413528). The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis (PubMed:12021362). {ECO:0000269|PubMed:12021362, ECO:0000269|PubMed:1413528}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000269|PubMed:12021362}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000305|PubMed:1431806}.
DE  Reference Proteome: Yes;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0008234;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0039690;
GO  GO:0070613;
GO  GO:0018144;
GO  GO:0018259;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAY
SQ  AFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQ
SQ  LLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMT
SQ  WGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPG
SQ  EKDNAQSSPVILLEGLAGQMQNFCETTLVSVGKTCTAVNAISTCCGNLKALAGRILGMLRDFIWKTLGFETRFLADASLL
SQ  FGEDVDGWLKAISDLRDQFIAKSYCSQDEMMQILVLLEKGRQMRKSGLSKGGISPAIINLILKGINDLEQLNRSCSVQGV
SQ  RGVRKMPFTIFFQGKSRTGKSLLMSQVTKDFQDHYGLGGETVYSRNPCDQYWSGYRRQPFVLMDDFAAVVTEPSAEAQMI
SQ  NLISSAPYPLNMAGLEEKGICFDSQFVFVSTNFLEVSPEAKVRDDEAFKNRRHVIVQVSNDPAKAYDAANFASNQIYTIL
SQ  AWKDGRYNTVCVIEDYDELVAYLLTRSQQHAEEQEKNLANMMKSATFESHFKSLVEVLELGSMISAGFDIIRPEKLPSEA
SQ  KEKRVLYSIPYNGEYCNALIDDNYNVTCWFGECVGNPEQLSKYSEKMLLGAYEFLLCSESLNVVIQAHLKEMVCPHHYDK
SQ  ELNFIGKIGETYYHNQMVSNIGSMQKWHRAILFGIGVLLGKEKEKTWYQVQVANVKQALYDMYTKEIRDWPMPIKVTCGI
SQ  VLAAIGGSAFWKVFQQLVGSGNGPVLMGVAAGAFSAEPQSRKPNRFDMQQYRYNNVPLKRRVWADAQMSLDQSSVAIMSK
SQ  CRANLVFGGTNLQIVMVPGRRFLACKHFFTHIKTKLRVEIVMDGRRYYHQFDPANIYDIPDSELVLYSHPSLEDVSHSCW
SQ  DLFCWDPDKELPSVFGADFLSCKYNKFGGFYEAQYADIKVRTKKECLTIQSGNYVNKVSRYLEYEAPTIPEDCGSLVIAH
SQ  IGGKHKIVGVHVAGIQGKIGCASLLPPLEPIAQAQGAEEYFDFLPAEENVSSGVAMVAGLKQGVYIPLPTKTALVETPSE
SQ  WHLDTPCDKVPSILVPTDPRIPAQHEGYDPAKSGVSKYSQPMSALDPELLGEVANDVLELWHDCAVDWDDFGEVSLEEAL
SQ  NGCEGVEYMERIPLATSEGFPHILSRNGKEKGKRRFVQGDDCVVSLIPGTTVAKAYEELEASAHRFVPALVGIECPKDEK
SQ  LPMRKVFDKPKTRCFTILPMEYNLVVRRKFLNFVRFIMANRHRLSCQVGINPYSMEWSRLAARMKEKGNDVLCCDYSSFD
SQ  GLLSKQVMDVIASMINELCGGEDQLKNARRNLLMACCSRLAICKNTVWRVECGIPSGFPMTVIVNSIFNEILIRYHYKKL
SQ  MREQQAPELMVQSFDKLIGLVTYGDDNLISVNAVVTPYFDGKKLKQSLAQGGVTITDGKDKTSLELPFRRLEECDFLKRT
SQ  FVQRSSTIWDAPEDKASLWSQLHYVNCNNCEKEVAYLTNVVNVLRELYMHSPREATEFRRKVLKKVSWITSGDLPTLAQL
SQ  QEFYEYQRQQGGADNNDTCDLLTSVDLLGPPLSFEKEAMHGCKVSEEIVTKNLAYYDFKRKGEDEVVFLFNTLYPQSSLP
SQ  DGCHSVTWSQGSGRGGLPTQSWMSYNISRKDSNINKIIRTAVSSKKRVIFCARDNMVPVNIVALLCAVRNKLMPTAVSNA
SQ  TLVKVMENAKAFKFLPEEFNFAFSDV
//
ID  Q9Y6D9;
PN  Mitotic spindle assembly checkpoint protein MAD1;
GN  MAD1L1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22351768}. Nucleus envelope {ECO:0000269|PubMed:22351768}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22351768}. Note=Detected at the nucleus envelope during interphase (PubMed:22351768). From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Detected at kinetochores during prometaphase (PubMed:22351768). Colocalizes with NEK2 at the kinetochore (PubMed:14978040). Colocalizes with IK at spindle poles during metaphase and anaphase (PubMed:22351768). {ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:22351768}.
DR  UNIPROT: Q9Y6D9;
DR  UNIPROT: B3KR41;
DR  UNIPROT: Q13312;
DR  UNIPROT: Q75MI0;
DR  UNIPROT: Q86UM4;
DR  UNIPROT: Q9UNH0;
DR  PDB: 1GO4;
DR  PDB: 4DZO;
DR  Pfam: PF05557;
DR  OMIM: 602686;
DR  DisGeNET: 8379;
DE  Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding. {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:20133940}.
DE  Disease: Note=Defects in MAD1L1 are involved in the development and/or progression of various types of cancer. {ECO:0000269|PubMed:10597320, ECO:0000269|PubMed:11423979}.
DE  Reference Proteome: Yes;
DE  Interaction: P09917; IntAct: EBI-79934,EBI-742610; Score: 0.81
DE  Interaction: P12270; IntAct: EBI-1048528,EBI-742610; Score: 0.52
DE  Interaction: Self; IntAct: EBI-742610,EBI-742610; Score: 0.80
DE  Interaction: P38432; IntAct: EBI-945751,EBI-742610; Score: 0.37
DE  Interaction: Q13257; IntAct: EBI-742610,EBI-78203; Score: 0.98
DE  Interaction: Q9UL15; IntAct: EBI-356517,EBI-742610; Score: 0.78
DE  Interaction: Q63HK5; IntAct: EBI-9053916,EBI-742610; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-5453285,EBI-742610; Score: 0.72
DE  Interaction: Q9NX65; IntAct: EBI-739949,EBI-742610; Score: 0.56
DE  Interaction: P55081; IntAct: EBI-742610,EBI-1048159; Score: 0.72
DE  Interaction: Q12834; IntAct: EBI-367462,EBI-742610; Score: 0.35
DE  Interaction: Q8TD31-3; IntAct: EBI-742610,EBI-10175300; Score: 0.72
DE  Interaction: Q99576-3; IntAct: EBI-742610,EBI-10294415; Score: 0.56
DE  Interaction: Q9BW85; IntAct: EBI-742610,EBI-10300345; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-2514791,EBI-742610; Score: 0.56
DE  Interaction: Q14134; IntAct: EBI-702370,EBI-742610; Score: 0.78
DE  Interaction: O76041; IntAct: EBI-2880203,EBI-742610; Score: 0.78
DE  Interaction: O76064; IntAct: EBI-742610,EBI-373337; Score: 0.78
DE  Interaction: P06753; IntAct: EBI-742610,EBI-355607; Score: 0.85
DE  Interaction: P09493; IntAct: EBI-742610,EBI-351158; Score: 0.72
DE  Interaction: P25786; IntAct: EBI-742610,EBI-359352; Score: 0.56
DE  Interaction: Q3ZCW2; IntAct: EBI-742610,EBI-10241423; Score: 0.72
DE  Interaction: Q5VU62; IntAct: EBI-10184033,EBI-742610; Score: 0.56
DE  Interaction: Q9UM82; IntAct: EBI-742610,EBI-744066; Score: 0.56
DE  Interaction: Q9Y4E8; IntAct: EBI-742610,EBI-1043104; Score: 0.56
DE  Interaction: P11440; IntAct: EBI-846949,EBI-742610; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-2552918,EBI-742610; Score: 0.56
DE  Interaction: Q9DCX1; IntAct: EBI-308982,EBI-742610; Score: 0.56
DE  Interaction: P25054; IntAct: EBI-727707,EBI-742610; Score: 0.35
DE  Interaction: Q5SZD1; IntAct: EBI-10697767,EBI-742610; Score: 0.35
DE  Interaction: Q9H672; IntAct: EBI-3916346,EBI-742610; Score: 0.35
DE  Interaction: Q9UL15-2; IntAct: EBI-16399128,EBI-742610; Score: 0.35
DE  Interaction: O43448; IntAct: EBI-12050557,EBI-742610; Score: 0.35
DE  Interaction: Q8N4Q0; IntAct: EBI-5238790,EBI-742610; Score: 0.35
DE  Interaction: Q86YD7; IntAct: EBI-742610,EBI-6658203; Score: 0.56
DE  Interaction: P12792; IntAct: EBI-6152249,EBI-742610; Score: 0.35
DE  Interaction: Q8IYF3; IntAct: EBI-742397,EBI-742610; Score: 0.37
DE  Interaction: Q9Y2I6; IntAct: EBI-719716,EBI-742610; Score: 0.37
DE  Interaction: Q96AQ9; IntAct: EBI-741921,EBI-742610; Score: 0.37
DE  Interaction: Q9Y2J4; IntAct: EBI-746752,EBI-742610; Score: 0.37
DE  Interaction: Q9BVR6; IntAct: EBI-741889,EBI-742610; Score: 0.37
DE  Interaction: Q15233; IntAct: EBI-742610,EBI-350527; Score: 0.37
DE  Interaction: Q8TD31; IntAct: EBI-949834,EBI-742610; Score: 0.37
DE  Interaction: Q96M98; IntAct: EBI-742610,EBI-11927350; Score: 0.40
DE  Interaction: Q13077-2; IntAct: EBI-742610,EBI-20866402; Score: 0.40
DE  Interaction: Q07002; IntAct: EBI-742610,EBI-746238; Score: 0.56
DE  Interaction: P09493-10; IntAct: EBI-742610,EBI-12123928; Score: 0.72
DE  Interaction: Q5T7P8-2; IntAct: EBI-742610,EBI-10246152; Score: 0.56
DE  Interaction: Q96BZ8; IntAct: EBI-742610,EBI-726510; Score: 0.56
DE  Interaction: Q8TC71; IntAct: EBI-742610,EBI-11334239; Score: 0.56
DE  Interaction: Q99576; IntAct: EBI-742610,EBI-750174; Score: 0.56
DE  Interaction: O43247-2; IntAct: EBI-742610,EBI-12093053; Score: 0.56
DE  Interaction: Q9HAQ2; IntAct: EBI-8472129,EBI-742610; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-742610,EBI-741158; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-742610,EBI-14066006; Score: 0.56
DE  Interaction: Q8TAP4-4; IntAct: EBI-742610,EBI-11742507; Score: 0.56
DE  Interaction: Q16543; IntAct: EBI-742610,EBI-295634; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-742610,EBI-2557469; Score: 0.56
DE  Interaction: Q9Y4E8-2; IntAct: EBI-742610,EBI-12041225; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-742610,EBI-745392; Score: 0.56
DE  Interaction: P25800; IntAct: EBI-8639312,EBI-742610; Score: 0.56
DE  Interaction: Q9Y6W3; IntAct: EBI-742610,EBI-1765641; Score: 0.56
DE  Interaction: O95995; IntAct: EBI-742610,EBI-1052570; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-742610,EBI-739832; Score: 0.56
DE  Interaction: Q9BZW7; IntAct: EBI-742610,EBI-744794; Score: 0.56
DE  Interaction: Q92917; IntAct: EBI-742610,EBI-746309; Score: 0.56
DE  Interaction: Q2TAC2-2; IntAct: EBI-742610,EBI-10961624; Score: 0.56
DE  Interaction: Q9Y4C2-2; IntAct: EBI-742610,EBI-11974855; Score: 0.56
DE  Interaction: Q9H1Y0; IntAct: EBI-742610,EBI-1047414; Score: 0.56
DE  Interaction: O00267; IntAct: EBI-742610,EBI-710464; Score: 0.49
DE  Interaction: P08670; IntAct: EBI-353844,EBI-742610; Score: 0.37
DE  Interaction: P14373; IntAct: EBI-719493,EBI-742610; Score: 0.37
DE  Interaction: O00444; IntAct: EBI-746202,EBI-742610; Score: 0.37
DE  Interaction: Q8IYF3-3; IntAct: EBI-11523345,EBI-742610; Score: 0.37
DE  Interaction: P53933; IntAct: EBI-742610,EBI-28798; Score: 0.56
DE  Interaction: P32502; IntAct: EBI-742610,EBI-6260; Score: 0.56
DE  Interaction: P32571; IntAct: EBI-19840,EBI-742610; Score: 0.56
DE  Interaction: P28004; IntAct: EBI-742610,EBI-20640; Score: 0.56
DE  Interaction: P39976; IntAct: EBI-5933,EBI-742610; Score: 0.56
DE  Interaction: Q03718; IntAct: EBI-742610,EBI-27756; Score: 0.56
DE  Interaction: Q6NZI2; IntAct: EBI-2559016,EBI-742610; Score: 0.35
DE  Interaction: Q9Y240; IntAct: EBI-3957044,EBI-742610; Score: 0.35
DE  Interaction: P13497; IntAct: EBI-489827,EBI-742610; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-351896,EBI-742610; Score: 0.35
DE  Interaction: P09493-2; IntAct: EBI-21768246,EBI-742610; Score: 0.35
GO  GO:0005623;
GO  GO:0005813;
GO  GO:0000777;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0044615;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0043515;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007093;
GO  GO:0007094;
GO  GO:0042130;
GO  GO:0090235;
GO  GO:0048538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKR
SQ  ARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETIN
SQ  ALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAA
SQ  IVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERL
SQ  DQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKR
SQ  VLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKML
SQ  KSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLRED
SQ  HSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQ
SQ  IDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA
//
ID  Q8NFW9;
PN  Rab effector MyRIP;
GN  MYRIP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. {ECO:0000250|UniProtKB:Q7TNY7}.
DR  UNIPROT: Q8NFW9;
DR  UNIPROT: B3KWM3;
DR  UNIPROT: B3KWW4;
DR  UNIPROT: B7Z2H1;
DR  UNIPROT: B7Z9V3;
DR  UNIPROT: G3XAI8;
DR  UNIPROT: Q32M41;
DR  UNIPROT: Q32M42;
DR  UNIPROT: Q569F7;
DR  UNIPROT: Q8IUF5;
DR  UNIPROT: Q9Y3V4;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DR  OMIM: 611790;
DR  DisGeNET: 25924;
DE  Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P62993; IntAct: EBI-1759414,EBI-401755; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-389883,EBI-1759414; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-1759414,EBI-79464; Score: 0.40
DE  Interaction: Q8TAB5; IntAct: EBI-747505,EBI-1759414; Score: 0.72
DE  Interaction: O00194; IntAct: EBI-1759414,EBI-10179046; Score: 0.56
DE  Interaction: P51159; IntAct: EBI-1759414,EBI-716881; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-536879,EBI-1759414; Score: 0.56
GO  GO:0030864;
GO  GO:0031045;
GO  GO:0048471;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0017137;
GO  GO:0008270;
GO  GO:0006886;
GO  GO:0032024;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEERLSELKQKLDEEGSKCSILSKHQQFVEHCCMRCCSPFTFLVNTKRQ
SQ  CGDCKFNVCKSCCSYQKHEKAWVCCVCQQARLLRAQSLEWFYNNVKSRFKRFGSAKVLKNLYRKHRLESGACFDILGGSL
SQ  FESNLENEGSISGSDSTFYRQSEGHSVMDTLAVALRVAEEAIEEAISKAEAYGDSLDKQNEASYLRDHKEELTEELATTI
SQ  LQKIIRKQKSKSEQQVEEEPGWPHPQSCSTKVADEGTSASPGGYRAPAALWRSQSAFSITGEEALKTPPVEAPSRQPRDQ
SQ  GQHPRAESALPSWKSVDRLDETNLAPVLQSPDGNWVALKDGAPPPTRLLAKPKSGTFQALEVASSVASAYDEMGSDSEED
SQ  FDWSEALSKLCPRSRALPRNPQPQPTQAQSSDQGPIAASPSSALSPNPEAMCSDSETSSAGSSREVGHQARLSWLQRKAP
SQ  RNPAAEKMRLHGELDVNFNPQLASRETSDSSEPEEAPHTTDRRARRWRRARLGSEEPSKEPSSPSAQLRDLDTHQVSDDL
SQ  SETDISNEARDPQTLTDTTEEKRRNRLYELAMKMSEKETSSGEDQESEPKTESENQKESLSSEDNSQSVQEELKKKFSAV
SQ  SLCNISTEVLKVINATEELIAGSTGPWESPQVPPDRQKGMFPRGTDQVRLDEQLTSLEENVYLAAGTVYGLETQLTELED
SQ  AARCIHSGTDETHLADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNIAPCVRFTRRRDQKQRTQVQTIDTSRQQR
SQ  RKLPAPPVKAEKIETSSVTTIKTFNHNFILQGSSTNRTKERKGTTKDLMEPALESAVMY
//
ID  H2QL32;
PN  High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A;
GN  PDE9A;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
DR  UNIPROT: H2QL32;
DR  UNIPROT: K7AGW3;
DR  PDB: 4QGE;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DE  Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory. {ECO:0000250|UniProtKB:O76083, ECO:0000250|UniProtKB:Q8QZV1}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0047555;
GO  GO:0046872;
GO  GO:0046069;
GO  GO:0046068;
GO  GO:0019934;
GO  GO:0010613;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRP
SQ  VAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCCQEGQRIPPEREELIQSVLAQV
SQ  AEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
SQ  PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCV
SQ  AQMMYSMVWLCSLQENFSQMDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNI
SQ  FSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
SQ  LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAM
SQ  KELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
//
ID  Q13177;
PN  PAK-2p34;
GN  PAK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm. Note=MYO18A mediates the cellular distribution of the PAK2- ARHGEF7-GIT1 complex to the inner surface of the cell membrane. [PAK-2p34]: Nucleus. Cytoplasm, perinuclear region. Membrane; Lipid-anchor. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane.
DR  UNIPROT: Q13177;
DR  UNIPROT: Q13154;
DR  UNIPROT: Q6ISC3;
DR  PDB: 3PCS;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 605022;
DR  DisGeNET: 5062;
DE  Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase- mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation. {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:9171063}.
DE  Reference Proteome: Yes;
DE  Interaction: O60711; IntAct: EBI-744222,EBI-1045887; Score: 0.35
DE  Interaction: Q03001; IntAct: EBI-310758,EBI-1045887; Score: 0.37
DE  Interaction: Self; IntAct: EBI-1045887,EBI-1045887; Score: 0.60
DE  Interaction: P60953-1; IntAct: EBI-3625591,EBI-1045887; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-1045887,EBI-529989; Score: 0.37
DE  Interaction: P14618-1; IntAct: EBI-4304679,EBI-1045887; Score: 0.44
DE  Interaction: Q9BUB5; IntAct: EBI-1045887,EBI-73837; Score: 0.40
DE  Interaction: P42574; IntAct: EBI-524064,EBI-1045887; Score: 0.40
DE  Interaction: O60504; IntAct: EBI-741237,EBI-1045887; Score: 0.77
DE  Interaction: P60953; IntAct: EBI-1045887,EBI-81752; Score: 0.83
DE  Interaction: Q9H4E5; IntAct: EBI-1045887,EBI-6285694; Score: 0.72
DE  Interaction: P15056; IntAct: EBI-1045887,EBI-365980; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-447295,EBI-1045887; Score: 0.37
DE  Interaction: P63000; IntAct: EBI-1045887,EBI-413628; Score: 0.78
DE  Interaction: Q9WVM1; IntAct: EBI-2552104,EBI-1045887; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-2514016,EBI-1045887; Score: 0.35
DE  Interaction: Q3THE2; IntAct: EBI-770040,EBI-1045887; Score: 0.35
DE  Interaction: Q9Y2X7-3; IntAct: EBI-1045887,EBI-11070376; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-1045887,EBI-1046878; Score: 0.56
DE  Interaction: P63208; IntAct: EBI-1045887,EBI-307486; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-1045887,EBI-740282; Score: 0.53
DE  Interaction: Q14155-1; IntAct: EBI-1045887,EBI-717540; Score: 0.35
DE  Interaction: Q14161-4; IntAct: EBI-1045887,EBI-11070380; Score: 0.35
DE  Interaction: B7Z6G2; IntAct: EBI-1045887,EBI-11070369; Score: 0.35
DE  Interaction: Q9Y2X7; IntAct: EBI-1045887,EBI-466061; Score: 0.67
DE  Interaction: Q9NXV6; IntAct: EBI-2559836,EBI-1045887; Score: 0.35
DE  Interaction: P02675; IntAct: EBI-1034445,EBI-1045887; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-6124081,EBI-1045887; Score: 0.35
DE  Interaction: O60404; IntAct: EBI-21879932,EBI-1045887; Score: 0.35
DE  Interaction: Q9H4E5-2; IntAct: EBI-21868147,EBI-1045887; Score: 0.35
DE  Interaction: Q15052-2; IntAct: EBI-21521235,EBI-1045887; Score: 0.35
DE  Interaction: P55210; IntAct: EBI-1045887,EBI-523958; Score: 0.62
DE  Interaction: P42858; IntAct: EBI-466029,EBI-1045887; Score: 0.40
DE  Interaction: Q13153; IntAct: EBI-1307,EBI-1045887; Score: 0.53
DE  Interaction: O14730; IntAct: EBI-1045887,EBI-1047061; Score: 0.37
DE  Interaction: P53667; IntAct: EBI-1045887,EBI-444403; Score: 0.56
DE  Interaction: P04049; IntAct: EBI-1045887,EBI-365996; Score: 0.56
DE  Interaction: P24666; IntAct: EBI-717701,EBI-1045887; Score: 0.40
DE  Interaction: Q14697; IntAct: EBI-348004,EBI-1045887; Score: 0.40
DE  Interaction: Q9UNM6; IntAct: EBI-356070,EBI-1045887; Score: 0.40
DE  Interaction: Q13347; IntAct: EBI-354047,EBI-1045887; Score: 0.40
DE  Interaction: P25787; IntAct: EBI-603262,EBI-1045887; Score: 0.40
DE  Interaction: P62910; IntAct: EBI-438408,EBI-1045887; Score: 0.40
DE  Interaction: P00505; IntAct: EBI-720214,EBI-1045887; Score: 0.40
DE  Interaction: P62750; IntAct: EBI-353254,EBI-1045887; Score: 0.40
DE  Interaction: P61224; IntAct: EBI-358143,EBI-1045887; Score: 0.40
DE  Interaction: P27695; IntAct: EBI-1048805,EBI-1045887; Score: 0.40
DE  Interaction: P07355; IntAct: EBI-352622,EBI-1045887; Score: 0.40
DE  Interaction: P06730; IntAct: EBI-73440,EBI-1045887; Score: 0.40
DE  Interaction: Q13263; IntAct: EBI-78139,EBI-1045887; Score: 0.40
DE  Interaction: Q16630; IntAct: EBI-358410,EBI-1045887; Score: 0.40
DE  Interaction: Q04637; IntAct: EBI-73711,EBI-1045887; Score: 0.40
DE  Interaction: Q13526; IntAct: EBI-714158,EBI-1045887; Score: 0.40
DE  Interaction: P27797; IntAct: EBI-1049597,EBI-1045887; Score: 0.40
DE  Interaction: Q00005; IntAct: EBI-1052159,EBI-1045887; Score: 0.40
DE  Interaction: P20290; IntAct: EBI-1054687,EBI-1045887; Score: 0.40
DE  Interaction: P50395; IntAct: EBI-1049143,EBI-1045887; Score: 0.40
DE  Interaction: Q99436; IntAct: EBI-603319,EBI-1045887; Score: 0.40
DE  Interaction: P83731; IntAct: EBI-353146,EBI-1045887; Score: 0.40
DE  Interaction: P22061; IntAct: EBI-353343,EBI-1045887; Score: 0.40
DE  Interaction: P07237; IntAct: EBI-395883,EBI-1045887; Score: 0.40
DE  Interaction: P25205; IntAct: EBI-355153,EBI-1045887; Score: 0.40
DE  Interaction: P23526; IntAct: EBI-1053240,EBI-1045887; Score: 0.40
DE  Interaction: P35580; IntAct: EBI-351758,EBI-1045887; Score: 0.40
DE  Interaction: P30084; IntAct: EBI-719602,EBI-1045887; Score: 0.40
DE  Interaction: P54819; IntAct: EBI-1056291,EBI-1045887; Score: 0.40
DE  Interaction: Q9Y266; IntAct: EBI-357298,EBI-1045887; Score: 0.40
DE  Interaction: P21266; IntAct: EBI-350350,EBI-1045887; Score: 0.40
DE  Interaction: Q13404; IntAct: EBI-1050671,EBI-1045887; Score: 0.40
DE  Interaction: Q15019; IntAct: EBI-741220,EBI-1045887; Score: 0.40
DE  Interaction: O00264; IntAct: EBI-1045534,EBI-1045887; Score: 0.40
DE  Interaction: P04179; IntAct: EBI-716989,EBI-1045887; Score: 0.40
DE  Interaction: P25786; IntAct: EBI-359352,EBI-1045887; Score: 0.40
DE  Interaction: O75534; IntAct: EBI-719186,EBI-1045887; Score: 0.40
DE  Interaction: P30086; IntAct: EBI-716384,EBI-1045887; Score: 0.40
DE  Interaction: P49023; IntAct: EBI-702209,EBI-1045887; Score: 0.35
DE  Interaction: Q15052-1; IntAct: EBI-25409944,EBI-1045887; Score: 0.35
DE  Interaction: Q14155-4; IntAct: EBI-25410853,EBI-1045887; Score: 0.35
DE  Interaction: O43639; IntAct: EBI-713635,EBI-1045887; Score: 0.67
DE  Interaction: Q9NYB9-2; IntAct: EBI-11096309,EBI-1045887; Score: 0.56
DE  Interaction: P16333; IntAct: EBI-389883,EBI-1045887; Score: 0.71
DE  Interaction: Q15052; IntAct: EBI-1642523,EBI-1045887; Score: 0.71
DE  Interaction: Q8WVK2; IntAct: EBI-2512550,EBI-1045887; Score: 0.35
DE  Interaction: P05362; IntAct: EBI-1035358,EBI-1045887; Score: 0.35
DE  Interaction: Q9NYY3; IntAct: EBI-721354,EBI-1045887; Score: 0.35
DE  Interaction: Q96K76; IntAct: EBI-2514143,EBI-1045887; Score: 0.35
DE  Interaction: Q01968-2; IntAct: EBI-11749425,EBI-1045887; Score: 0.35
DE  Interaction: Q92845; IntAct: EBI-954040,EBI-1045887; Score: 0.35
DE  Interaction: Q9BTV5; IntAct: EBI-722073,EBI-1045887; Score: 0.35
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005524;
GO  GO:0045296;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0048365;
GO  GO:0031267;
GO  GO:0032147;
GO  GO:0034333;
GO  GO:0006915;
GO  GO:0070830;
GO  GO:0071407;
GO  GO:0060996;
GO  GO:0038095;
GO  GO:0035722;
GO  GO:0043066;
GO  GO:2001271;
GO  GO:0006469;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:2001238;
GO  GO:0050731;
GO  GO:0046777;
GO  GO:0150105;
GO  GO:0006468;
GO  GO:0051493;
GO  GO:0050690;
GO  GO:0040008;
GO  GO:0007346;
GO  GO:0007165;
GO  GO:0023014;
GO  GO:0002223;
GO  GO:0031098;
GO  GO:0031295;
GO  GO:0050852;
GO  GO:0048010;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16617111};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAK
SQ  GTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR
//
ID  Q9EPU0;
PN  Regulator of nonsense transcripts 1;
GN  Upf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27149095}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27149095}. Note=Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm (By similarity). Localized in the chromatoid bodies of round spermatids (PubMed:27149095). {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
DR  UNIPROT: Q9EPU0;
DR  UNIPROT: Q3UG00;
DR  UNIPROT: Q6GYP5;
DR  UNIPROT: Q6PHQ5;
DR  UNIPROT: Q8K0N4;
DR  UNIPROT: Q99PR4;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DR  Pfam: PF18141;
DR  Pfam: PF04851;
DR  Pfam: PF09416;
DE  Function: RNA-dependent helicase and ATPase required for nonsense- mediated decay (NMD) of mRNAs containing premature stop codons (PubMed:27149095). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1- UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (By similarity). Essential for embryonic viability (By similarity). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA hardoring long 3'UTR by inducing the NMD machinery (PubMed:27149095). {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
DE  Reference Proteome: Yes;
DE  Interaction: Q61584; IntAct: EBI-8350418,EBI-6876715; Score: 0.35
DE  Interaction: Q4U2R1; IntAct: EBI-11068779,EBI-6876715; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-1811542,EBI-6876715; Score: 0.35
DE  Interaction: Q8CJG0; IntAct: EBI-528299,EBI-6876715; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0000784;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0044530;
GO  GO:0005524;
GO  GO:0003682;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0042162;
GO  GO:0008270;
GO  GO:0061158;
GO  GO:0044770;
GO  GO:0071347;
GO  GO:0071222;
GO  GO:0006281;
GO  GO:0006260;
GO  GO:0009048;
GO  GO:0071044;
GO  GO:0000956;
GO  GO:0000294;
GO  GO:0000184;
GO  GO:0061014;
GO  GO:0032204;
GO  GO:0006449;
GO  GO:0032201;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGAGGPGGAGAGGAAGQLDAQVGPEGILQ
SQ  NGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKC
SQ  KEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKI
SQ  PSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQT
SQ  QDNITVRWDLGLNKKRIAFFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIE
SQ  LRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVVIKCQLPKRFTAQGLPDLNHS
SQ  QVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDS
SQ  PVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSIL
SQ  IDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSN
SQ  IFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIIT
SQ  PYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVG
SQ  NPKALSKQPLWNHLLSYYKEQKALVEGPLNNLRESLMQFSKPRKLVNTVNPGARFMTTAMYDAREAIIPGSVYDRSSQGR
SQ  PSNMYFQTHDQISMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKTKTGRGGRQKNRFGLPGPSQTT
SQ  LPNSQASQDVASQPFSQGALTQGYVSMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTG
SQ  LSQY
//
ID  Q8CHK4;
PN  Histone acetyltransferase KAT5;
GN  Kat5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000269|PubMed:12036595}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region. {ECO:0000250|UniProtKB:Q92993}.
DR  UNIPROT: Q8CHK4;
DR  UNIPROT: A1L394;
DR  UNIPROT: Q8CGZ3;
DR  UNIPROT: Q8CGZ4;
DR  UNIPROT: Q8VIH0;
DR  Pfam: PF01853;
DR  Pfam: PF11717;
DR  Pfam: PF17772;
DR  PROSITE: PS51726;
DE  Function: Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (By similarity). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (By similarity). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (By similarity). NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Also acetylates non-histone proteins, such as ATM, NR1D2, RAN, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:22539723). Directly acetylates and activates ATM. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (By similarity). Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. Acetylates RAN at 'Lys-134' (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:22539723). {ECO:0000250|UniProtKB:Q92993, ECO:0000269|PubMed:22539723}.
DE  Reference Proteome: Yes;
DE  Interaction: P54254; IntAct: EBI-1169948,EBI-1169713; Score: 0.40
DE  Interaction: P54253; IntAct: EBI-930964,EBI-1169948; Score: 0.40
DE  Interaction: O88495; IntAct: EBI-1169948,EBI-21227860; Score: 0.54
DE  Interaction: P0C0S6; IntAct: EBI-642131,EBI-1169948; Score: 0.35
DE  Interaction: P35583; IntAct: EBI-2893341,EBI-1169948; Score: 0.35
DE  Interaction: P28574; IntAct: EBI-1183003,EBI-1169948; Score: 0.46
DE  Interaction: Q9JI44; IntAct: EBI-2942577,EBI-1169948; Score: 0.46
DE  Interaction: P06151; IntAct: EBI-1169948,EBI-444940; Score: 0.35
DE  Interaction: P51859; IntAct: EBI-1169948,EBI-2943087; Score: 0.35
DE  Interaction: Q80YV3; IntAct: EBI-1169948,EBI-2942477; Score: 0.46
DE  Interaction: Q8CHI8; IntAct: EBI-1169948,EBI-2942504; Score: 0.46
DE  Interaction: Q8WTY4; IntAct: EBI-1169948,EBI-2943068; Score: 0.35
DE  Interaction: Q8R3B7; IntAct: EBI-1169948,EBI-2942609; Score: 0.46
DE  Interaction: P60762; IntAct: EBI-1169948,EBI-2943018; Score: 0.35
DE  Interaction: P63268; IntAct: EBI-1169948,EBI-2693783; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-1169948,EBI-353957; Score: 0.35
DE  Interaction: Q9Z2N8; IntAct: EBI-1169948,EBI-2942759; Score: 0.35
DE  Interaction: P63260; IntAct: EBI-1169948,EBI-351301; Score: 0.35
DE  Interaction: Q8VEK6; IntAct: EBI-1169948,EBI-2942903; Score: 0.35
DE  Interaction: Q15906; IntAct: EBI-1169948,EBI-399189; Score: 0.35
DE  Interaction: Q8C9X6; IntAct: EBI-1169948,EBI-2942636; Score: 0.35
DE  Interaction: Q8C0I4; IntAct: EBI-1169948,EBI-2942663; Score: 0.35
DE  Interaction: P01108; IntAct: EBI-1169948,EBI-1183114; Score: 0.35
GO  GO:0005829;
GO  GO:0000123;
GO  GO:0035267;
GO  GO:0000790;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032777;
GO  GO:0032991;
GO  GO:0000812;
GO  GO:0005667;
GO  GO:0003682;
GO  GO:0010485;
GO  GO:0004402;
GO  GO:0042393;
GO  GO:0046872;
GO  GO:0061733;
GO  GO:0043274;
GO  GO:0044877;
GO  GO:0070491;
GO  GO:0003713;
GO  GO:0008134;
GO  GO:0071392;
GO  GO:0006978;
GO  GO:0006302;
GO  GO:0016573;
GO  GO:0032703;
GO  GO:0000122;
GO  GO:0045892;
GO  GO:0018394;
GO  GO:0010508;
GO  GO:1901985;
GO  GO:0045944;
GO  GO:0045893;
GO  GO:0043161;
GO  GO:0040008;
GO  GO:0006357;
GO  GO:0010212;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTK
SQ  NGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPV
SQ  PSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
SQ  RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLA
SQ  KCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTG
SQ  TPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
SQ  VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
//
ID  Q16620;
PN  BDNF/NT-3 growth factors receptor;
GN  NTRK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15494731}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:P15209}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15209}. Early endosome membrane {ECO:0000250|UniProtKB:P15209}. Cell projection, axon {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63604}. Cell junction, synapse, postsynaptic density {ECO:0000250|UniProtKB:P15209}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000250|UniProtKB:P15209}.
DR  UNIPROT: Q16620;
DR  UNIPROT: B1ANZ4;
DR  UNIPROT: B4DFV9;
DR  UNIPROT: Q16675;
DR  UNIPROT: Q59GJ1;
DR  UNIPROT: Q8WXJ5;
DR  UNIPROT: Q8WXJ6;
DR  UNIPROT: Q8WXJ7;
DR  PDB: 1HCF;
DR  PDB: 1WWB;
DR  PDB: 2MFQ;
DR  PDB: 4ASZ;
DR  PDB: 4AT3;
DR  PDB: 4AT4;
DR  PDB: 4AT5;
DR  PDB: 5MO9;
DR  Pfam: PF07679;
DR  Pfam: PF13855;
DR  Pfam: PF01462;
DR  Pfam: PF07714;
DR  Pfam: PF16920;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS00239;
DR  OMIM: 600456;
DR  OMIM: 613886;
DR  OMIM: 617830;
DR  DisGeNET: 4915;
DE  Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity (By similarity). Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2 (PubMed:7574684, PubMed:15494731). Upon ligand- binding, undergoes homodimerization, autophosphorylation and activation (PubMed:15494731). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. {ECO:0000250|UniProtKB:P15209, ECO:0000269|PubMed:15494731, ECO:0000269|PubMed:7574684}.
DE  Disease: Epileptic encephalopathy, early infantile, 58 (EIEE58) [MIM:617830]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE58 is an autosomal dominant condition characterized by onset of refractory seizures in the first days or months of life. {ECO:0000269|PubMed:29100083}. Note=The disease may be caused by mutations affecting the gene represented in this entry. Obesity, hyperphagia, and developmental delay (OBHD) [MIM:613886]: A disorder characterized by early-onset obesity, hyperphagia, and severe developmental delay in motor function, speech, and language. {ECO:0000269|PubMed:15494731, ECO:0000269|PubMed:27884935, ECO:0000269|PubMed:29100083}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-297353,EBI-3904881; Score: 0.55
DE  Interaction: P34130; IntAct: EBI-3904881,EBI-3907456; Score: 0.59
DE  Interaction: P14618-1; IntAct: EBI-3904881,EBI-4304679; Score: 0.44
DE  Interaction: Q10567; IntAct: EBI-3904881,EBI-1171303; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-347928,EBI-3904881; Score: 0.37
DE  Interaction: Q9HAN9; IntAct: EBI-3904881,EBI-3917542; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-3904881,EBI-352572; Score: 0.40
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0030054;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0043235;
GO  GO:0043195;
GO  GO:0005524;
GO  GO:0048403;
GO  GO:0060175;
GO  GO:0043121;
GO  GO:0005030;
GO  GO:0042803;
GO  GO:0004713;
GO  GO:0004714;
GO  GO:0007202;
GO  GO:0031547;
GO  GO:0071230;
GO  GO:1990416;
GO  GO:1990090;
GO  GO:0021954;
GO  GO:0021987;
GO  GO:0007623;
GO  GO:0007631;
GO  GO:0014047;
GO  GO:0007612;
GO  GO:0060291;
GO  GO:0042490;
GO  GO:0007275;
GO  GO:0022011;
GO  GO:2000811;
GO  GO:0043524;
GO  GO:0007399;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0019227;
GO  GO:0048011;
GO  GO:0048709;
GO  GO:0048935;
GO  GO:0050772;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0010976;
GO  GO:1903997;
GO  GO:0033138;
GO  GO:0014068;
GO  GO:0001934;
GO  GO:0051965;
GO  GO:0046777;
GO  GO:0043087;
GO  GO:0043408;
GO  GO:0051896;
GO  GO:0046548;
GO  GO:0099183;
GO  GO:0099551;
GO  GO:0007169;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLE
SQ  IINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIK
SQ  TLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHM
SQ  NETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYN
SQ  GAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDY
SQ  GTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASP
SQ  LHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNL
SQ  CPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMA
SQ  EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWM
SQ  PPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNI
SQ  KGIHTLLQNLAKASPVYLDILG
//
ID  Q9Y272;
PN  Dexamethasone-induced Ras-related protein 1;
GN  RASD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q9Y272;
DR  UNIPROT: B2R709;
DR  UNIPROT: B4DFF4;
DR  UNIPROT: Q9NYB4;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DR  OMIM: 605550;
DR  DisGeNET: 51655;
DE  Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-740818,EBI-740019; Score: 0.37
DE  Interaction: O94972; IntAct: EBI-740818,EBI-741602; Score: 0.56
DE  Interaction: P43243; IntAct: EBI-352602,EBI-740818; Score: 0.72
DE  Interaction: P61978; IntAct: EBI-304185,EBI-740818; Score: 0.56
DE  Interaction: Q15415; IntAct: EBI-8642021,EBI-740818; Score: 0.72
DE  Interaction: Q9NYB9-2; IntAct: EBI-740818,EBI-11096309; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-740818,EBI-3867333; Score: 0.56
DE  Interaction: P10588; IntAct: EBI-740818,EBI-2681496; Score: 0.40
DE  Interaction: Q99PV5; IntAct: EBI-6143801,EBI-740818; Score: 0.37
DE  Interaction: Q13064; IntAct: EBI-2340269,EBI-740818; Score: 0.56
DE  Interaction: Q96B26; IntAct: EBI-371922,EBI-740818; Score: 0.56
DE  Interaction: Q86X02; IntAct: EBI-11063830,EBI-740818; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-22310682,EBI-740818; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-724076,EBI-740818; Score: 0.56
DE  Interaction: O75525; IntAct: EBI-722504,EBI-740818; Score: 0.56
DE  Interaction: P26371; IntAct: EBI-3958099,EBI-740818; Score: 0.56
DE  Interaction: P61978-2; IntAct: EBI-7060731,EBI-740818; Score: 0.56
DE  Interaction: O00308; IntAct: EBI-743923,EBI-740818; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-10172052,EBI-740818; Score: 0.56
DE  Interaction: Q2TAC2-2; IntAct: EBI-10961624,EBI-740818; Score: 0.56
DE  Interaction: O43390-2; IntAct: EBI-12236340,EBI-740818; Score: 0.56
DE  Interaction: Q86YV0; IntAct: EBI-3437896,EBI-740818; Score: 0.56
DE  Interaction: Q9NQX1-2; IntAct: EBI-12859340,EBI-740818; Score: 0.56
DE  Interaction: Q3LI66; IntAct: EBI-11962084,EBI-740818; Score: 0.56
DE  Interaction: Q6PEX3; IntAct: EBI-3957672,EBI-740818; Score: 0.56
DE  Interaction: Q5JR59-3; IntAct: EBI-11522433,EBI-740818; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-1047093,EBI-740818; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10171774,EBI-740818; Score: 0.56
DE  Interaction: Q16825; IntAct: EBI-2860264,EBI-740818; Score: 0.56
DE  Interaction: P0DJD3-2; IntAct: EBI-11994018,EBI-740818; Score: 0.56
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0007186;
GO  GO:0045892;
GO  GO:0007263;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTS
SQ  GNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREI
SQ  EQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPG
SQ  DAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS
//
ID  P0C6T6;
PN  Non-structural protein 11;
GN  1a;
OS  694006;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T6;
DR  UNIPROT: A3EXG5;
DR  Pfam: PF16348;
DR  Pfam: PF01661;
DR  Pfam: PF09401;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF05409;
DR  Pfam: PF11633;
DR  Pfam: PF08715;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:19264783}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003968;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0039548;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVPDPPKLKSMVVTTLKWCDPFANPNVTGWDIPIEEALEYAKQQLRTPEPQLVFVPYYLSHAPGISGDRVVITDSIWY
SQ  ATNFGWQPIRELAMDKDGVRYGRGGTHGVLLPMQDPSFIMGDIDIQIRKYGIGANSPPDVLPLWDGFSDPGPDVGPYLDF
SQ  PDNCCPTKPKAKRGGDVYLSDQYGFDNNGILVEPVMKLLGVIKSDFTLEQLLAALGKYRTEDGYDLPDGYVKVAIKVGRK
SQ  AVPVLKQSIFTVVGVTEQLVPGYYYPFSTSSVVEHTKPTRGGPVGKTVEAVMLSLYGTNNYNPATPVARLKCSYCDYYGW
SQ  TPLKDIGTVNCLCGAEFQLTSSCVDAESAGVIKPGCVMLLDKSPGMRLIPGNRTYVSFGGAIWSPIGKVNGVTVWVPRAY
SQ  SIVAGEHSGAVGSGDTVAINKELVEYLIEGIRVDADTLDNPTCATFIANLDCDTKAPVVHTVESLQGLCLANKIMLGDKP
SQ  LPTDEFHPFIVGLAYHVQRACWYGALASRTFEAFRDFVRTEEERFAQFFGKVCAPINGCVYLAYTTGRVTLFSAYQVLNT
SQ  AIAKSKDAFGGVAAIVVDMLKPILEWVLKKMSIAKGAWLPYAEGLLALFKAQFTVVKGKFQFLRASLNSKCHSLCDLLTT
SQ  IMSKLLTSVKWAGCKVDALYTGTYYYFSRKGVLTEVQLCAKRLGLLLTPKQQKMEVEVLDGDFDAPVTLTDLELEECTGV
SQ  LEEVFGASDVKLVKGTLVSLASKLFVRTEDGFLYRYVKSGGVLGKAFRLRGGGVSKVTFGDEEVHTIPNTVTVNFSYDVC
SQ  EGLDAILDKVMAPFQVEEGTKLEDLACVVQKAVYERLSDLFSDCPAELRPINLEDFLTSECFVYSKDYEKILMPEMYFSL
SQ  EDAVPVDDEMVDDIEDTVEQASDSDDQWLGDEGAEDCDNTIQDVDVATSMTTPCGYTKIAEHVYIKCADIVQEARNYSYA
SQ  VLVNAANVNLHHGGGVAGALNRATNNAMQKESSEYIKANGSLQPGGHVLLSSHGLASHGILHVVGPDKRLGQDLALLDAV
SQ  YAAYTGFDSVLTPLVSAGIFGFTVEESLCSLVKNVACTTYVVVYDRQLYERALATSFDVPGPQSSVQHVPAIDWAEAVEV
SQ  QESIVDQVETPSLGAVDTVDSNADSGLNETARSPENVVGSVPDDVVADVESCVRDLVRQVVKKVKRDKRPPPIVPQQTVE
SQ  QQPQEISSPGDCNTVLVDVVSMSFSAMVNFGKEKGLLIPVVIDYPAFLKVLKRFSPKEGLFSSNGYEFYGYSRDKPLHEV
SQ  SKDLNSLGRPLIMIPFGFIVNGQTLAVSAVSMRGLTVPHTVVVPSESSVPLYRAYFNGVFSGDTTAVQDFVVDILLNGAR
SQ  DWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETKLCAPEPLIKVLTTVDGINYSTV
SQ  LVSTAQSYRAQIGTVFCDGHDWSNKNPMPTDEGTHLYKQDNFSSAEVTAIREYYGVDDSNIIARAMSIRKTVQTWPYTVV
SQ  DGRVLLAQRDSNCYLNVAISLLQDIDVSFSTPWVCRAYDALKGGNPLPMAEVLIALGKATPGVSDDAHMVLSAVLNHGTV
SQ  TARRVMQTVCEHCGVSQMVFTGTDACTFYGSVVLDDLYAPVSVVCQCGRPAIRYVSEQKSPWLLMSCTPTQVPLDTSGIW
SQ  KTAIVFRGPVTAGHYMYAVNGTLISVYDANTRRRTSDLKLPATDILYGPTSFTSDSKVETYYLDGVKRTTIDPDFSKYVK
SQ  RGDYYFTTAPIEVVAAPKLVTSYDGFYLSSCQNPQLAESFNKAINATKTGPMKLLTMYPNVAGDVVAISDDNVVAHPYGS
SQ  LHMGKPVLFVTRPNTWKKLVPLLSTVVVNTPNTYDVLAVDPLPVNNETSEEPISVKAPIPLYGLKATMVLNGTTYVPGNK
SQ  GHLLCLKEFTLTDLQTFYVEGVQPFVLLKASHLSKVLGLRVSDSSLHVNHLSKGVVYAYAATRLTTRVTTSLLGGLVTRS
SQ  VRKTADFVRSTNPGSKCVGLLCLFYQLFMRFWLLVKKPPIVKVSGIIAYNTGCGVTTCVLNYLRSRCGNISWSRLLKLLR
SQ  YMLYIWFVWTCLTICGVWLSEPYAPSLVTRFKYFLGIVMPCDYVLVNETGTGWLHHLCMAGMDSLDYPALRMQQHRYGSP
SQ  YNYTYILMLLEAFFAYLLYTPALPIVGILAVLHLIVLYLPIPLGNSWLVVFLYYIIRLVPFTSMLRMYIVIAFLWLCYKG
SQ  FLHVRYGCNNVACLMCYKKNVAKRIECSTVVNGVKRMFYVNANGGTHFCTKHNWNCVSCDTYTVDSTFICRQVALDLSAQ
SQ  FKRPIIHTDEAYYEVTSVEVRNGYVYCYFESDGQRSYERFPMDAFTNVSKLHYSELKGAAPAFNVLVFDATNRIEENAVK
SQ  TAAIYYAQLACKPILLVDKRMVGVVGDDATIARAMFEAYAQNYLLKYSIAMDKVKHLYSTALQQISSGMTVESVLKVFVG
SQ  STRAEAKDLESDVDTNDLVSCIRLCHQEGWEWTTDSWNNLVPTYIKQDTLSTLEVGQFMTANAKYVNANIAKGAAVNLIW
SQ  RYADFIKLSESMRRQLKVAARKTGLNLLVTTSSLKADVPCMVTPFKIIGGHRRIVSWRRVLIHVFMLLVVLNPQWFTPWY
SQ  IMRPIEYNVVDFKVIDNAVIRDITSADQCFANKFSAFENWYSNRYGSYVNSRGCPMVVGVVSDIVGSLVPGLPARFLRVG
SQ  TTLLPLVNYGLGAVGSVCYTPHYAINYDVFDTSACVLAATCTLFSSASGERMPYCADAALIQNASRYDMLKPHVMYPFYE
SQ  HSGYIRFPEVISAGVHIVRTMAMEYCKVGRCDVSEAGLCMSLQPRWVVNNAYFRQQSGVYCGTSAFDLFMNMLLPIFTPV
SQ  GAVDITTSILMGALLAVVVSMSLYYLLRFRRAFGDYSGVIFTNILAFVLNVIVLCLEGPYPMLPSIYAMVFLYATCYFGS
SQ  DIACMMHVSFLIMFAGVVPLWVTVLYIVVVLSRHILWFASLCTKRTVQVGDLAFHSFQDAALQTFMLDKEVFLRLKREIS
SQ  SDAYFKYLAMYNKYKYYSGPMDTAAYREAACSHLVMALEKYSNGGGDTIYQPPRCSVASAALQAGLTRMAHPSGLVEPCL
SQ  VKVNYGSMTLNGIWLDNFVICPRHVMCSRDELANPDYPRLSMRAANYDFHVSQNGHNIRVIGHTMEGSLLKLTVDVNNPK
SQ  TPAYSFIRVSTGQAMSLLACYDGLPTGVYTCTLRSNGTMRASFLCGSCGSPGFVMNGKEVQFCYLHQLELPNGTHTGTDF
SQ  SGVFYGPFEDKQVPQLAAPDCTITVNVLAWLYAAVLSGENWFLTKSSISPAEFNNCAVKYMCQSVTSESLQVLQPLAAKT
SQ  GISVERMLSALKVLLSAGFCGRTIMGSCSLEDEHTPYDIGRQMLGVKLQGKFQSMFRWTLQWFAIIFVLTILILLQLAQW
SQ  TFVGALPFTLLLPLIGFVAVCVGFVSLLIKHKHTYLTVYLLPVAMVTAYYNFQYTPEGVQGYLLSLYNYVNPGRIDVIGT
SQ  DLLTMLIISVACTLLSVRMVRTDAYSRIWYVCTAVGWLYNCWTGSADTVAISYLTFMVSVFTNYTGVACASLYAAQFMVW
SQ  VLKFLDPTILLLYGRFRCVLVCYLLVGYLCTCYFGVFNLINRLFRCTLGNYEYVVSSQELRYMNSHGLLPPTNSWQALML
SQ  NIKLAGIGGIPIYRVSTIQSNMTDLKCTSVVLLSVLQQLRVESSSKLWALCVKLHNEILASNSPTEAFEAFVSLLSVLLS
SQ  LPGAINLDELCSSILENNSVLQAVASEFSNLSSYVDYENAQKAYDTAVATGAPASTVNALKKAMNVAKSVLDKDVATTRK
SQ  LERMSELAMTAMYKQARAEDRRSKVTAAMQTMLFNMIRRLDSDALSNILNNARNGVVPLGVIPRTAANKLLLVVPDFSVY
SQ  TATITMPTLTYAGSAWDVMQVADADGKTVNATDITRENSVNLAWPLVVTAQRQQATSPVKLQNNELMPQTVKRMNVVAGV
SQ  SQTACVTDAVAYYNATKEGRHVMAILADTDGLAFAKVEKSTGDGFVILELEPPCKFMVDTPKGPALKYLYFTKGLKNLCR
SQ  GTVLGTLACTVRLHAGSATEVASNSSILSLCSFSVDPEATYKDYLDNGGSPIGNCVKMLTPHTGTGLAITAKPDANIDQE
SQ  SFGGASCCLYCRCHIEHPGASGVCKYKGKFVQIPLVGVNDPIGFCIRNVVCAVCNMWQGYGCPCSSLREINLQARDECFL
SQ  NESGVLVE
//
ID  P09216;
PN  Protein kinase C epsilon type;
GN  Prkce;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts. In passaging cells, translocated to the cell periphery. Translocated to the nucleus in PMA-treated cells (By similarity). {ECO:0000250}.
DR  UNIPROT: P09216;
DR  PDB: 1GMI;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin- dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell- cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin- induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma- aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. {ECO:0000269|PubMed:11278835, ECO:0000269|PubMed:12665800, ECO:0000269|PubMed:17157309}.
DE  Reference Proteome: Yes;
DE  Interaction: P15336; IntAct: EBI-1170906,EBI-6049581; Score: 0.44
DE  Interaction: P48442; IntAct: EBI-6140357,EBI-6049581; Score: 0.40
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0098978;
GO  GO:0000139;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099523;
GO  GO:0030315;
GO  GO:0071889;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0035276;
GO  GO:0046872;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0004674;
GO  GO:0017124;
GO  GO:0030546;
GO  GO:0005102;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0071361;
GO  GO:0071456;
GO  GO:0036120;
GO  GO:0071380;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0035641;
GO  GO:0002281;
GO  GO:0043066;
GO  GO:0051562;
GO  GO:0010917;
GO  GO:0031397;
GO  GO:0051280;
GO  GO:0018105;
GO  GO:0030838;
GO  GO:0010811;
GO  GO:2001031;
GO  GO:0032467;
GO  GO:0010634;
GO  GO:0010763;
GO  GO:0043123;
GO  GO:0032024;
GO  GO:0050996;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0032230;
GO  GO:0090303;
GO  GO:0006468;
GO  GO:0061178;
GO  GO:0019216;
GO  GO:0050730;
GO  GO:0051279;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0035669;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIE
SQ  LAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAV
SQ  RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVN
SQ  MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR
SQ  KKLAAGAESPQPASGNSPSEDDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRASSSTDGQLASPGENGEVRQGQA
SQ  KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
SQ  RLFFVMEYVNGGDLMFQIQRSRKFDEPRSGFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHSKLADFGMCKEGILN
SQ  GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA
SQ  FMTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKMKPPFKPRIKTKRDVNNFDQDFTREEPILTLVDEAIVKQI
SQ  NQEEFKGFSYFGEDLMP
//
ID  Q96EF0;
PN  Myotubularin-related protein 8;
GN  MTMR8;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16787938}.
DR  UNIPROT: Q96EF0;
DR  UNIPROT: Q5JT99;
DR  UNIPROT: Q9NXP6;
DR  PDB: 4Y7I;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  DisGeNET: 55613;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (PubMed:22647598, PubMed:26143924). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (PubMed:22647598, PubMed:26143924). In complex with MTMR9, negatively regulates autophagy (PubMed:22647598). {ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:26143924}.
DE  Reference Proteome: Yes;
DE  Interaction: P20839-2; IntAct: EBI-20722853,EBI-750578; Score: 0.35
DE  Interaction: Q9Y216; IntAct: EBI-10293003,EBI-750578; Score: 0.35
DE  Interaction: Q96QG7; IntAct: EBI-744593,EBI-750578; Score: 0.75
DE  Interaction: Q969Q4; IntAct: EBI-751892,EBI-750578; Score: 0.35
DE  Interaction: Q96QG7-1; IntAct: EBI-22119846,EBI-750578; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0032991;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0004725;
GO  GO:0010507;
GO  GO:0006661;
GO  GO:0046856;
GO  GO:0010506;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDHITVPKVENVKLVDRYVSKKPANGILYLTATHLIYVEASGAARKETWIALHHIATVEKLPITSLGCPLTLRCKNFRVA
SQ  HFVLDSDLVCHEVYISLLKLSQPALPEDLYAFSYNPKSSKEMRESGWKLIDPISDFGRMGIPNRNWTITDANRNYEICST
SQ  YPPEIVVPKSVTLGTVVGSSKFRSKERVPVLSYLYKENNAAICRCSQPLSGFYTRCVDDELLLEAISQTNPGSQFMYVVD
SQ  TRPKLNAMANRAAGKGYENEDNYANIRFRFMGIENIHVMRSSLQKLLEVCELKTPTMSEFLSGLESSGWLRHIKAIMDAG
SQ  IFITKAVKVEKASVLVHCSDGWDRTAQVCSVASILLDPFYRTFKGLMILIEKEWISMGHKFSQRCGHLDGDSKEVSPIFT
SQ  QFLDCIWQLMEQFPCAFEFNENFLLEIHDHVFSCQFGNFLGNCQKDREDLRVYEKTHSVWPFLVQRKPDFRNPLYKGFTM
SQ  YGVLNPSTVPYNIQFWCGMYNRFDKGLQPKQSMLESLLEIKKQRAMLETDVHELEKKLKVRDEPPEEICTCSQLGNILSQ
SQ  HLGSPLTNPLGFMGINGDLNTLMENGTLSREGGLRAQMDQVKSQGADLHHNCCEIVGSLRAINISGDVGISEAMGISGDM
SQ  CTFEATGFSKDLGICGAMDISEATGISGNLGISEARGFSGDMGILGDTGISKASTKEADYSKHQ
//
ID  E9Q9A9;
PN  2'-5'-oligoadenylate synthase 2;
GN  Oas2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
DR  UNIPROT: E9Q9A9;
DR  UNIPROT: Q8K4E5;
DR  UNIPROT: Q8VI92;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00832;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179, ECO:0000303|PubMed:21142819}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0051607;
GO  GO:0045071;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009617;
GO  GO:0009615;
GO  GO:0006401;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P29728};
SQ  MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESL
SQ  KQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVK
SQ  HEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILL
SQ  VKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILL
SQ  HQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKL
SQ  FLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLE
SQ  EFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSI
SQ  CFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKY
SQ  RQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKV
SQ  PVMQTPGSCGGQIYPTVGGVTK
//
ID  Q68772;
PN  Non-structural protein 12;
GN  rep;
OS  38143;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q68772;
DR  UNIPROT: P89132;
DR  UNIPROT: Q87077;
DR  Pfam: PF16749;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The Nsp1 chain is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFCECPRSNLVVMCSGAFCCVLCGHRRRPRPASESDRAKYGPIVQYVEARVAHVYSGLEGRYCALEMIPITYGNKFPYCK
SQ  PLPVSFVIKTLAGVQGDLTRLEETPLPGGYGVIPCWGPHLAAVGYLSPAHVGRDWFEGATHAIVHIGSYGGHERPTTIPF
SQ  NTTGGDVYQLGTCTIVETIDHVEWHAGVKPGTAICPLDRIDFAQKVITAFPEGFLANKAWLGDKRGTLKVEADPETAALS
SQ  FEHGRCWLKLFPDPACELTTASTFGYQLNCGVQGKYIARRLQTNGLKLVQNQEGKFIAYTFHRGSWLGHIGHADESVPPD
SQ  CQIIARFDVLPYNEWSPLPLLKLPGKTYFGGNASSVSWPEWKYDEQLLYADSLTAGFCWLQLFPPLSRKSEAQRAILAQQ
SQ  VNNYGVTGTYLEYRLRQYGIVLAECDYGEHYIYAAASDSSIRHISPVPIHDRHHVFVTRLTARFGAFDEGFDLGFGTRYG
SQ  RRRGGGKKSGQSSGVRAPGRTTPDLAGDWGKAVDDQEKTASKVTTDKAMSTSEPAVVQVGCETKPVADAAAVPASVNSTG
SQ  CALLPVQADPCCTAGVAAKESEPKAVAAPSIPITFGAPAGETLPVAASPLVVKKDKRCISVKLTAKKALPKETFIPPPDG
SQ  GCGVHAFAAIQYHINTGHWPEQKPVVNWAYEAWTTNEDIGHMICSTETPAALEPCLHARYVVRLDSDHWVVDHYPNRPMC
SQ  FVEACAHGWCSSLLSEPTGEEGEHLVDCSALYDCLGKFRNGTEFADTVLGLSKTAHCCNKRVPTPRKQAIMSLLNRPNCV
SQ  PCIAPPSQVRTVDPSQPAAPLPPVPRPRKRKAAAQQVSKVPSEQDPSLAHDPPEKPDSVRPPKLGYLDRAWNNMLARTHK
SQ  LHNLQQRVFGLYPQLLSMLLPSGARPSTPRLLGCYFSMAVAMFFLFLGSPLFILCAVLAGVIAPSARYPKILCCCLVVVY
SQ  ICTLFADAISSVCDNDDADCRAFLSDLGDRYSTNQPVYITPGPATFFLAVSRNFFVVSVALFPLHLLLLMVDVLLVIGVL
SQ  CMDGYCFRCFSRCVRKAPEEVSLLTIPQSRVSRRFLLDICDFYSAPPVDIIRLATGLNGCFRGDYSPIGSSTSVITADKI
SQ  DVKKVSCRTVCSFPSCPSEAVKVLHVLSVRGQMCAHNEQKVEKVDALPCKNPLFPYDLSSKKIVPVDSGTYEILSSIGCD
SQ  MSHLVIGDGDFFKVMGVPRPSPFTVMRLRACRVVGGGRIFRTALAAAWVLFFVCAGYWVQMSTPCGIGTNDPFCKSSFGV
SQ  PTYVNQGVCHGQYCASSKGVSRATSILTVRNPAVAPYIVLAACLVYLASVYVPGIIEVSLLVLNALLPAGPAISALRTLV
SQ  MIIAAPHLSMKYIAFFCCTTAFVDFTSVVVVLTALLVGWILARYTGIGGFVTPYDIHDVVKSQRDGVAVANAPPNTYLGA
SQ  VRRAALTGKPAFFVANNTGIVLEGLLREKTRASNSVSVYGVTCGSGGLFSDGNNTVCLTATHVCGNNKAVVDYQGTRYEA
SQ  VFTTKGDYASAVVPIPGAFPPLKFAPQSYTGRAYWYANTGVETGFVGTTGCLVFSGPGDSGSPIITPDGLIVGVHTGSDS
SQ  KGSGAYTTPNGLTVSGPLSLKEMGAHYEGPIVDVPTRLPRNVHNDTKSVPQPLARLLESSINLEGGLGTIQLIIVAVVLW
SQ  KYAVDPLSIPFVVAFFLLNEILPKCLIRCFYNYSLFCLAAFSPLASRIFFIRLLTAALNRNPTALICHACFAGIAVLNDF
SQ  IILGDIRLALRFTSFYVVGVNHDAIAIAVIGALVCVAACCLELFGLPQMASVIGCHGSFDPTFLSRYVHEGIRQGVSSGF
SQ  GTESLSTALACALSEDELNFLAQAVDHKAIVSAIHVHKTLQDYILSKNAKILRASLASVHANHNASKALASLDKFLQGTS
SQ  TQLKPGDPVILLGSTSAELVSVFSGDSEYIAEPIRSHPVAGTICTLCVVQAKCEGGLVTQVNGKFSPAKYLAVAGKVLAD
SQ  HPDYKLENDGRFPRTREDRVKDSVQVDTVDIGSHTFKKMWNKTTGDVWYDIIMPESAANPLAVHDLDSAVAAIGMSKEIP
SQ  EKDMNRLRAIISKLQGLVSSEALNLLTAAGCTSADRSGLVITLDYAKIITHHARTRAFSSIDFKVVSPDEAMRTARLSPS
SQ  PQPIIASFSDDKFLLLRRHPPSLLDVLTKGLDATCREPLHSPGDQGIDGYLWDFEAPHSKEAIWLSNQIISACAARRGDA
SQ  PGCYPYKLHPVRGDPYRVGNVLKNTRFGDVTYTAVSDSDSPWLKVASINSGGCPVVTDRVLGSTIPVGSEIYLPTLPESV
SQ  LDYLDSRPDCPTYYTQHGCEAAALQDLKKFNLSTQGFILPEVLNIVRNYLLGTIGYRPAIYKPSTVPSNDSHAGINGLSF
SQ  STKTLQALPDIDELCEKAIAEVWQTVTPVTLKKQFCSKAKTRTILGTNAMASLALRALLSGVTQGFQLAGKNSPICLGKS
SQ  KFDPCTFEVKGRCLETDLASCDRSTPAIVRHFATKLLFEMACAERALPLYVVNCCHDLIVTQTSAATKRGGLSSGDPVTS
SQ  IANTIYSLVLYVQHMVLTLLENGHPLSLKFLSGKLNFQDLYKLQAFIVYSDDLILLNESDDLPNFERWVPHLELALGFKV
SQ  DPKKTVITSNPGFLGCEYRHGWLVPQKQRVLAALAYHVNAKDVHTYYINATAILNDASALSAFEPDWFDDLVIGLADCAR
SQ  KDGYSFPGPAAFREFFSRVSGYQFEGKEVQVCSICCSTARTTSLCGMALCDFCAHRHYHPGCHVLSSFCKHVIGSNTCKM
SQ  CSIPILKDRTKFAELLASDQYRSVCTVEVTVVDGYTDAAPGRYSYQKKQYMLRKERRGCPLDLPDGKYSMKLLPNSCSGI
SQ  CVPKAQENATLSNFVVGPPGSGKTTFISNLLDDDAVVYCPTHVSLIAYSKSLPAARFSVPRGQDPAEYGTPALSGPTLQL
SQ  LSAGYVPGAKHYLDEACYANPFDVFKLLSKTPITAIGDPAQLTPVGFDTPLYVFELMKKNALHAIYRFGQNICNAIQPCY
SQ  STKLVSQRQGDTEVIFQTKFAPRGKVLTPYHRDRVGAAVTIDSSQGSTYDVVTLYLPTKGSLTLARGLVGITRARERLYV
SQ  YDPHHQLAKYFNLQPSSTTIRPHAVVIDGKARVMLSDKCYAAPEDFPGMLCTARPATAADRKILEETCLKLDFLESGSLS
SQ  PLPRVCYNLGFYYSPDITKLLPIPSELAKHWPVATNRNNPEWPNRLVVSATRLSPLSHPAVCAGYYVGDSLFVGTPNVTS
SQ  YWLTKFLDGRAVPMEDSVYSTGRFEMDIRDYLDSAERDFAAKHPHAFIGDTKGTTVGGCHHITSQYLPHVLPADSVVKVG
SQ  VSKPGVAHKALCTVTDIYLPMLGSYTSPPTQSKVYKVNVDHKACKLMVWRDQTMYFQEGFDYHTLVDALRFVRLSSDGVY
SQ  RVAPELTPMIGNRRLDLGAKPLRPVDLAITPWDDPKCEFLVTHASPFDMSDEFLLVNAFDFIKEDLLGKSVTPVYFYKRL
SQ  SEPLHFDQNLPPHVGAILSKAPRFISLAKVFNFCFTPTACHCKVSVKTATGDHMCKCSLSSDEFLSRFNPTVGTP
//
ID  P46822;
PN  Kinesin light chain;
GN  klc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19605495}. Nucleus envelope {ECO:0000269|PubMed:19605495}. Note=Recruited to the nuclear envelope by unc-83 during nuclear migrations. {ECO:0000269|PubMed:19605495}.
DR  UNIPROT: P46822;
DR  UNIPROT: Q18088;
DR  UNIPROT: Q6BEW4;
DR  UNIPROT: Q8I7M2;
DR  UNIPROT: Q8TA80;
DR  UNIPROT: Q95QV1;
DR  PROSITE: PS01160;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport (Probable). The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Recruits unc-83 (within the unc-83-unc-84 LINC complex) to the nuclear envelope during nuclear migration to mediate the link between the nuclear envelope and the microtubule cytoskeleton in hypodermal precursor cells (PubMed:19605495, PubMed:27697906). {ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:27697906, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: P34609; IntAct: EBI-315684,EBI-315578; Score: 0.62
DE  Interaction: Self; IntAct: EBI-315578,EBI-315578; Score: 0.37
DE  Interaction: Q23064-3; IntAct: EBI-2902257,EBI-315578; Score: 0.37
DE  Interaction: Q23130; IntAct: EBI-315578,EBI-328747; Score: 0.37
DE  Interaction: G5EFD7; IntAct: EBI-315578,EBI-322609; Score: 0.37
DE  Interaction: O01482; IntAct: EBI-315611,EBI-315578; Score: 0.37
DE  Interaction: Q17581; IntAct: EBI-315606,EBI-315578; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-313007,EBI-315578; Score: 0.37
DE  Interaction: Q93228; IntAct: EBI-315621,EBI-315578; Score: 0.37
DE  Interaction: G5EBU5; IntAct: EBI-315617,EBI-315578; Score: 0.37
DE  Interaction: P25807; IntAct: EBI-315630,EBI-315578; Score: 0.37
DE  Interaction: P91131; IntAct: EBI-315625,EBI-315578; Score: 0.37
DE  Interaction: Q95Y99; IntAct: EBI-315648,EBI-315578; Score: 0.37
DE  Interaction: H2L044; IntAct: EBI-315644,EBI-315578; Score: 0.37
DE  Interaction: O01802; IntAct: EBI-312854,EBI-315578; Score: 0.37
DE  Interaction: Q9XW20; IntAct: EBI-315668,EBI-315578; Score: 0.37
DE  Interaction: Q9TZH8; IntAct: EBI-315663,EBI-315578; Score: 0.37
DE  Interaction: P34540; IntAct: EBI-315657,EBI-315578; Score: 0.37
DE  Interaction: Q95XR0; IntAct: EBI-314404,EBI-315578; Score: 0.37
DE  Interaction: Q966C7; IntAct: EBI-315672,EBI-315578; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0016938;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0019894;
GO  GO:0003777;
GO  GO:0048675;
GO  GO:0051295;
GO  GO:0040011;
GO  GO:0002119;
GO  GO:0030473;
GO  GO:0040038;
GO  GO:0048489;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNMSQDDVTTGLRTVQQGLEALREEHSTISNTLETSVKGVKEDEAPLPKQKLSQINDNLDKLVCGVDETSLMLMVFQLT
SQ  QGMDAQHQKYQAQRRRLCQENAWLRDELSSTQIKLQQSEQMVAQLEEENKHLKYMASIKQFDDGTQSDTKTSVDVGPQPV
SQ  TNETLQELGFGPEDEEDMNASQFNQPTPANQMAASANVGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTS
SQ  GHDHPDVATMLNILALVYRDQNKYKEAANLLNEALSIREKCLGESHPAVAATLNNLAVLFGKRGKFKDAEPLCKRALEIR
SQ  EKVLGDDHPDVAKQLNNLALLCQNQGKYEEVEKYYKRALEIYESKLGPDDPNVAKTKNNLSSAYLKQGKYKEAEELYKQI
SQ  LTRAHEREFGQISGENKPIWQIAEEREENKHKGEGATANEQAGWAKAAKVDSPTVTTTLKNLGALYRRQGKYEAAETLED
SQ  VALRAKKQHEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS
//
ID  Q5RHB5;
PN  Lymphoid-restricted membrane protein;
GN  lrmp;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22542100}; Single-pass type IV membrane protein {ECO:0000269|PubMed:22542100}. Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:22542100}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22542100}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22542100}. Chromosome {ECO:0000269|PubMed:22542100}. Note=Localized at both male and female pronuclear membranes during pronuclear congression and fusion. Colocalized with tubulin at the centrosome adjacent to the nuclear membrane. At prophase is localized at the centrosome on opposite sides of the zygotic nucleus and at the reforming nuclear membrane. At metaphase is juxtaposed with the centrosomes at the mitotic spindle poles. During chromosome segregation is localized with the chromatin. Undetectable at the centrosome at the onset of anaphase, but becomes again apparent by late mitosis.
DR  UNIPROT: Q5RHB5;
DR  UNIPROT: J9WMP5;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DR  Pfam: PF05781;
DE  Function: A maternally expressed membrane and cytoskeletal linker protein, which is essential for attachment of the centrosome to the male pronucleus. Promotes male and female pronucleus congression and subsequent fusion after fertilization. Congression is mediated by the sperm aster microtubules. {ECO:0000269|PubMed:12874114, ECO:0000269|PubMed:22542100}.
DE  Disease: Note=Defects in lrmp are a cause of pronuclear congression/fusion and chromosomal segregation abnormalities in the zygote named futile cycle (fue), a lethal recessive maternal-effect mutant. Mutant embryos undergo several cycles of anucleate cleavage and die. {ECO:0000269|PubMed:12874114}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0000785;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0072686;
GO  GO:0097431;
GO  GO:0031965;
GO  GO:0007052;
GO  GO:0051028;
GO  GO:0051984;
GO  GO:0007344;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVGVTPRRHNPVDSICRKLQTIQRRDQEINSPFQIPKFQTNSYDSPHSGLRFNLEAILKKHTVRPDDSDSASSAGMLTP
SQ  TASPGPGSSCNTPRAPITPVNATYSITSTLGTLGTIGDRRTSGTYSRPFRRNCSTPSAQTGDNYFNFTPRYSTQSQGPDT
SQ  DVRTSKIPTPGLFSYNLNFSSDISNMDSELAYPALVVKRLSLGEGSLFTSEPKKESMAEVSLICEEDLLDTIFQACDTQC
SQ  RGKVYVSHIVDFLRHTTCRSSEDSGLEELCNMLDPERKDISIDLDTYHAIMKEWIEDCRNQGKDLKNDTQQESSKLRDSL
SQ  SAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKM
SQ  GQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNAD
SQ  LQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSG
SQ  SLQTELALAQNPLEGLEHLSTSVCFASSLDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTE
SQ  NSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEV
SQ  DRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWDEEYVLSESPPLQELGPDQQMLEELCCDEEVLQALKQEEEEPTETV
SQ  SDKEKITAKSEGEGEATYDSGVENEEPQRDFTLSHMCLPDKKSERESNEAPFVGEGGEQRPCMSLKEEDRLPECTGPEDA
SQ  HEQAAPLPHTHCECAGDQPLTYDNLEVTSVKDHILSTEPSSLMTCELVSPSTGHPEVGNSITGRTEQLVGTNGEPEEERL
SQ  TTGADMSDLQRLGEGQLSKVSAKSDKSLLLPVAEEEEAMPEAVEVTSAGVNSPDKHKTGSKKTVVTSDSNSTGSADSLKD
SQ  PSEKVKDMTFDPAASEDNIPTVPATQSPKKDPLASRNKLKKEMSSMEVIEEQKAQEDGEPTVVTEKEGDTSVSSENASDS
SQ  TKDDKNSLSPSDKEIEAEFHRLSLGFKCDMFTLEKRLRLEERSRDLAEENVRKEVISCKALLQALIPRCEEDNQSMEIIH
SQ  RVQKNLEILVQSMTRVSSRSEMLGAIHQETRVGKTVEVMIQHVENLRRMYTKEHAELLELRENLTPNERSFGSHSERDDF
SQ  RNKKQTTSNIFKTTSRRISIATIPRSIGGQTHFDMPKDMAETEVERLSRRSPWNMAAKRPPLKRFVSSGTWADIDEPTLM
SQ  NSPTPSPTDNAPPSLMEGRPAVSRGARGIWIWVALFVVLAVLLALLASLMLQPAVDAAPVGTGDSWMTIQQLLWPYTGLR
SQ  HNGQPPV
//
ID  Q8K4D7;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  Plcz1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}.
DR  UNIPROT: Q8K4D7;
DR  UNIPROT: Q3KPE5;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:17933795, ECO:0000269|PubMed:18028898, ECO:0000269|PubMed:18322275, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0004629;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0032959;
GO  GO:0016042;
GO  GO:0007275;
GO  GO:0048015;
GO  GO:0007204;
GO  GO:0060470;
GO  GO:0051209;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESQLHELAEARWFLSKVQDDFRGGKINVEITHKLLEKLDFPCHFAHVKHIFKENDRQNQGRITIEEFRAIYRCIVHREE
SQ  ITEIFNTYTENRKILSENSLIEFLTQEQYEMEIDHSDSVEIINKYEPIEEVKGERQMSIEGFARYMFSSECLLFKENCKT
SQ  VYQDMNHPLSDYFISSSHNTYLISDQILGPSDIWGYVSALVKGCRCLEIDCWDGSQNEPIVYHGYTFTSKLLFKTVVQAI
SQ  NKYAFVTSDYPVVLSLENHCSPGQQEVMASILQSTFGDFLLSDMLEEFPDTLPSPEALKFKILVKNRKVGTLSETHERIG
SQ  TDKSGQVLEWKEVIYEDGDEDSGMDPETWDVFLSRIKEEREADPSTLSGIAGVKKRKRKMKIAMALSDLVIYTKAEKFRN
SQ  FQYSRVYQQFNETNSIGESRARKLSKLRVHEFIFHTAAFITRVYPKMMRADSSNFNPQEFWNVGCQMVALNFQTPGLPMD
SQ  LQNGKFLDNGGSGYILKPDILRDTTLGFNPNEPEYDDHPVTLTIRIISGIQLPVSSSSNTPDIVVIIEVYGVPNDHVKQQ
SQ  TRVVKNNAFSPKWNETFTFLIQVPELALIRFVVETQQGLLSGNELLGQYTLPVLCMNKGYRRVPLFSKSGANLEPSSLFI
SQ  YVWYFRE
//
ID  Q8R5M4;
PN  Optineurin;
GN  Optn;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q8R5M4;
DR  UNIPROT: Q5PQX8;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0042802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0031593;
GO  GO:0030674;
GO  GO:0008022;
GO  GO:0017137;
GO  GO:0001155;
GO  GO:0043130;
GO  GO:0006914;
GO  GO:0034613;
GO  GO:0070301;
GO  GO:1905232;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0034620;
GO  GO:0050663;
GO  GO:0050829;
GO  GO:0007030;
GO  GO:0090161;
GO  GO:0043001;
GO  GO:0008285;
GO  GO:0043124;
GO  GO:0043524;
GO  GO:0001920;
GO  GO:0003407;
GO  GO:0061734;
GO  GO:0010508;
GO  GO:0008284;
GO  GO:0001819;
GO  GO:0010628;
GO  GO:2000179;
GO  GO:0043525;
GO  GO:1904417;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSSCETPGNGPSNMVHPNLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRR
SQ  LQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQ
SQ  LLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEA
SQ  HTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKL
SQ  LQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFH
SQ  AERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCRHGARTSDSDQQAYLFQRGAEDMSWQHGQQPRSIPI
SQ  HSCPKCGEVLPDIDTLQIHVMDCII
//
ID  P0C6X2;
PN  2'-O-methyltransferase;
GN  rep;
OS  443239;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X2;
DR  UNIPROT: Q5MQD2;
DR  Pfam: PF13087;
DR  Pfam: PF16348;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF08715;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016896;
GO  GO:0008168;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0032259;
GO  GO:0039648;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0006351;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNHDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEEIVTGDNDDQIVVTGDDVDDIESIYDFDTYKA
SQ  LLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDY
SQ  LLTTIPKAIVLPQGGFVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGLDALFFYGDIVSHVCKCGHNMTLIAADLPCT
SQ  LHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELPQLYGLCI
SQ  TPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTI
SQ  LNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQIT
SQ  SVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINK
SQ  FDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGN
SQ  VFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVN
SQ  VACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIK
SQ  QESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKC
SQ  GSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFA
SQ  KVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWFCHDEASL
SQ  NSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLV
SQ  DVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYV
SQ  FSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPI
SQ  FVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVE
SQ  LVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGC
SQ  NKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPT
SQ  DASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLY
SQ  RPILLVDKKLITTACNGISVTQTMFDVYVDTFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSD
SQ  VETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDAFNQLTADL
SQ  QHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFFVSLICFILLWALLPTYSVYKSDIHLPAYAS
SQ  FKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTY
SQ  AFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPD
SQ  VISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTAS
SQ  SIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVVVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHL
SQ  QWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSL
SQ  YNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMT
SQ  LNGLWLDDKVYCPRHVICSSSNMNEPDYSALLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGNV
SQ  KPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYR
SQ  DAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSTEDFNVWAMANGFSQVKADLVLDALASMTGVSIETLLAAI
SQ  KRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIG
SQ  VTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGFTYVWLSYFVPAVNFTYVYEVFYGCILCVFA
SQ  IFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPY
SQ  IKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEV
SQ  SQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDE
SQ  VSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLA
SQ  LTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLSAIPALAANTLTIVIPDKQVFDKVVDNVY
SQ  VTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYY
SQ  NNGSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQ
SQ  AGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRAR
SQ  VEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCVGSSVAVQSKDLNFLNRVRGTSVNARLVPCA
SQ  SGLSTDVQLRAFDICNTNRAGIGLYYKVNCCRFQRIDDDGNKLDKFFVVKRTNLEVYNKEKTYYELTKSCGVVAEHDFFT
SQ  FDIDGSRVPHIVRRNLSKYTMLDLCYALRHFDRNDCSILCEILCEYADCKESYFSKKDWYDFVENPDIINIYKKLGPIFN
SQ  RALLNTVIFADTLVEVGLVGVLTLDNQDLYGQWYDFGDFIQTAPGFGVAVADSYYSYMMPMLTMCHVLDCELFVNDSYRQ
SQ  FDLVQYDFTDYKLELFNKYFKYWGMKYHPNTVDCDNDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYH
SQ  YKELGVVMNLDVDTHRYRLSLKDLLLYAADPAMHVASASALLDLRTCCFSVAAITSGIKFQTVKPGNFNQDFYEFVKSKG
SQ  LFKEGSTVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFN
SQ  KFGKARLYYEALSFEEQNEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPV
SQ  VIGTTKFYGGWDDMLRHLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEFCCSHGDRFYRLANECAQVLSEIV
SQ  MCGGCYYVKPGGTSSGDATTAFANSVFNICQAVTANVCSLMACNGHKIEDLSIRNLQKRLYSNVYRTDYVDYTFVNEYYE
SQ  FLCKHFSMMILSDDGVVCYNSDYASKGYIANISVFQQVLYYQNNVFMSESKCWVENDITNGPHEFCSQHTMLVKIDGDYV
SQ  YLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVHHENEEYQKVFRVYLEYIKKLYNDLGTQILDSYSVIL
SQ  STCDGLKFTEESFYKNMYLKSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATNHKYVLSVSPYVCNAPNC
SQ  DVSDVTKLYLGGMSYYCENHKPHYSFKLVMNGMVFGLYKQSCTGSPYIDDFNKIASCKWTEVDDYVLANECIERLKLFAA
SQ  ETQKATEEAFKQSYASATIQEIVSDREVILCWETGKVKPPLNKNYVFTGYHFTSTGKTVLGEYVFDKSELTNGVYYRATT
SQ  TYKLSIGDVFVLTSHSVASLSAPTLVPQENYASIRFSSVYSVPLVFQNNVANYQHIGMKRYCTVQGPPGTGKSHLAIGLA
SQ  VYYYTARVVYTAASHAAVDALCEKAYKFLNINDCTRIIPAKVRVDCYDKFKINDTTCKYVFTTINALPELVTDIVVVDEV
SQ  SMLTNYELSVINARIKAKHYVYIGDPAQLPAPRVLLSKGSLEPRHFNSITKIMCCLGPDIFLGNCYRCPKEIVETVSALV
SQ  YDNKLKAKNDNSSLCFKVYFKGQTTHESSSAVNIQQIYLISKFLKANPVWNSAVFISPYNSQNYVAKRVLGVQTQTVDSA
SQ  QGSEYDYVIYSQTAETAHSVNVNRFNVAITRAKKGIFCVMSNMQLFESLNFITLPLDKIQNQTLPRLHCTTNLFKDCSKS
SQ  CLGYHPAHAPSFLAVDDKYKVNENLAVNLNICEPVLTYSRLISLMGFKLDLTLDGYSKLFITKDEAIKRVRGWVGFDVEG
SQ  AHATRENIGTNFPLQIGFSTGVDFVVEATGLFAERDCYTFKKTVAKAPPGEKFKHLIPLMSKGQKWDIVRIRIVQMLSDY
SQ  LLDLSDSVVFITWSASFELTCLRYFAKLGRELNCNVCSNRATCYNSRTGYYGCWRHSYTCDYVYNPLIVDIQQWGYTGSL
SQ  TSNHDIICNVHKGAHVASADAIMTRCLAIYDCFCKSVNWNLEYPIISNEVSINTSCRLLQRVMLKAAMLCNRYNLCYDIG
SQ  NPKGLACVKDYEFKFYDAFPVAKSVKQLFYVYDVHKDNFKDGLCMFWNCNVDKYPSNSIVCRFDTRVLNKLNLPGCNGGS
SQ  LYVNKHAFHTNPFTRTVFENLKPMPFFYYSDTPCVYVDGLESKQVDYVPLRSATCITRCNLGGAVCSKHAEEYCNYLESY
SQ  NIVTTAGFTFWVYKNFDFYNLWNTFTTLQSLENVIYNLVNVGHYDGRTGELPCAIMNDKVVVKINNVDTVIFKNNTSFPT
SQ  NIAVELFTKRSIRHHPELKILRNLNIDICWKHVLWDYVKDSLFCSSTYGVCKYTDLKFIENLNILFDGRDTGALEAFRKA
SQ  RNGVFISTEKLSRLSMIKGPQRADLNGVIVDKVGELKVEFWFAMRKDGDDVIFSRTDSLCSSHYWSPQGNLGGNCAGNVI
SQ  GNDALTRFTIFTQSRVLSSFEPRSDLERDFIDMDDNLFIAKYGLEDYAFDHIVYGSFNHKVIGGLHLLIGLFRRKKKSNL
SQ  LIQEFLQYDSSIHSYFITDQECGSSKSVCTVIDLLLDDFVSIVKSLNLSCVSKVVNINVDFKDFQFMLWCNDNKIMTFYP
SQ  KMQATNDWKPGYSMPVLYKYLNVPLERVSLWNYGKPINLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSDKE
SQ  VAPGSAVLRQWLPSGSILVDNDLNPFVSDSLVTYFGDCMTLPFDCHWDLIISDMYDPLTKNIGDYNVSKDGFFTYICHLI
SQ  RDKLSLGGSVAIKITEFSWNADLYKLMSCFAFWTVFCTNVNASSSEGFLIGINYLGKSSFEIDGNVMHANYLFWRNSTTW
SQ  NGGAYSLFDMTKFSLKLAGTAVVNLRPDQLNDLVYSLIERGKLLVRDTRKEIFVGDSLVNTC
//
ID  Q9JI60;
PN  Lecithin retinol acyltransferase;
GN  Lrat;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17114808}; Single-pass membrane protein {ECO:0000269|PubMed:17114808}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9JI60;
DR  PDB: 4Q95;
DR  Pfam: PF04970;
DE  Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (By similarity). Retinyl esters are storage forms of vitamin A (By similarity). LRAT plays a critical role in vision (By similarity). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (PubMed:25416279). {ECO:0000250|UniProtKB:O95237, ECO:0000269|PubMed:25416279}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0102279;
GO  GO:0008374;
GO  GO:0047173;
GO  GO:0001972;
GO  GO:0019841;
GO  GO:0006653;
GO  GO:1990830;
GO  GO:0032370;
GO  GO:0009617;
GO  GO:0032526;
GO  GO:0033189;
GO  GO:0042572;
GO  GO:0007601;
GO  GO:0006776;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPMLEAASLLLEKLLLISNFKLFSVSVPGGGTGKNRPYEISSFVRGDVLEVSRTHFIHYGIYLGENRVAHLMPDILLA
SQ  LTNDKERTQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDGTLKKKSLLNEEVARRAEQQLGLTPYSLLWNN
SQ  CEHFVTYCRYGSRISPQAEKFYDTVKIIIRDQRSSLASAVLGLASIVYTGLASYMTLPAICIPFCLWMMSG
//
ID  S4R2P9;
PN  Sodium/calcium exchanger 3;
GN  Slc8a3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P70549}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70549}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P70549}. Cell membrane, sarcolemma {ECO:0000269|PubMed:14722618}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:14722618}. Cell junction {ECO:0000269|PubMed:14722618}. Mitochondrion outer membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Note=Detected at neuromuscular junctions. {ECO:0000269|PubMed:14722618}. [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}. [Isoform 2]: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: S4R2P9;
DR  UNIPROT: Q7TS90;
DR  UNIPROT: Q8VHJ8;
DR  PDB: 2LT9;
DR  Pfam: PF03160;
DR  Pfam: PF01699;
DR  Pfam: PF16494;
DE  Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain (PubMed:14722618, PubMed:21593315). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:14722618, PubMed:21593315). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:14722618). In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (PubMed:21593315). Required for normal oligodendrocyte differentiation and for normal myelination (PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis (PubMed:24616101). Isoform 1 displays higher calcium exchanger activity than isoform 2, probably because isoform 1 has a lower threshold for activation by cytoplasmic Ca(2+) (PubMed:24616101). {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21593315, ECO:0000269|PubMed:21959935, ECO:0000269|PubMed:24616101}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0031226;
GO  GO:0005874;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0016528;
GO  GO:0045202;
GO  GO:0015368;
GO  GO:1905060;
GO  GO:0005432;
GO  GO:0005516;
GO  GO:0099580;
GO  GO:0046872;
GO  GO:1990034;
GO  GO:0098703;
GO  GO:0070588;
GO  GO:0060402;
GO  GO:0007154;
GO  GO:0006874;
GO  GO:0071320;
GO  GO:0071456;
GO  GO:0002244;
GO  GO:0007612;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0007613;
GO  GO:0030001;
GO  GO:0051560;
GO  GO:0006851;
GO  GO:0098815;
GO  GO:0042552;
GO  GO:0071901;
GO  GO:0048709;
GO  GO:0014819;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0050808;
GO  GO:0021537;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLRLQPLTSAFLHFGLVTFVLFLNCLRAEAGDSGDVPSAGQNNESCSGSSDCKEGVILPIWYPENPSLGDKIARVIVY
SQ  FVALIYMFLGVSIIADRFMASIEVITSQEREVTIKKPNGETSTTTIRVWNETVSNLTLMALGSSAPEILLSLIEVCGHGF
SQ  IAGDLGPSTIVGSAAFNMFIIIGICVYVIPDGETRKIKHLRVFFVTAAWSIFAYIWLYMILAVFSPGVVQVWEGLLTLFF
SQ  FPVCVLLAWVADKRLLFYKYMHKKYRTDKHRGIIIETEGDHPKGIEMDGKMMNSHFLDGNFTPLEGKEVDESRREMIRIL
SQ  KDLKQKHPEKDLDQLVEMANYYALSHQQKSRAFYRIQATRMMTGAGNILKKHAAEQAKKTSSMSEVHTDEPEDFASKVFF
SQ  DPCSYQCLENCGAVLLTVVRKGGDISKTMYVDYKTEDGSANAGADYEFTEGTVVLKPGETQKEFSVGIIDDDIFEEDEHF
SQ  FVRLSNVRVEEEQLAEGMLPAILNSLPLPRAVLASPCVATVTILDDDHAGIFTFECDTIHVSESIGVMEVKVLRTSGARG
SQ  TVIVPFRTVEGTAKGGGEDFEDAYGELEFKNDETVKTIHIKVIDDKAYEKNKNYVIEMMGPRMVDMSVQKALLLSPEVTD
SQ  RKLTVEEEEAKRIAEMGKPVLGEHPKLEVIIEESYEFKSTVDKLIKKTNLALVVGTHSWRDQFMEAITVSAGGDEDEDES
SQ  GEERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFVVSILIIGMLTAIIGDLASHFGCTIGLKDSVTAVVFVAFGT
SQ  SVPDTFASKAAALQDVYADASIGNVTGSNAVNVFLGIGLAWSVAAIYWAMQGQEFHVSAGTLAFSVTLFTIFAFVCLSVL
SQ  LYRRRPHLGGELGGPRGCKLATTWLFVSLWLLYILFATLEAYCYIKGF
//
ID  O60356;
PN  Nuclear protein 1;
GN  NUPR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10092851, ECO:0000269|PubMed:16300740}. Cytoplasm {ECO:0000269|PubMed:16300740}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16300740}.
DR  UNIPROT: O60356;
DR  UNIPROT: B2R5C4;
DR  UNIPROT: O60357;
DR  UNIPROT: Q6FGG3;
DR  Pfam: PF10195;
DR  OMIM: 614812;
DR  DisGeNET: 26471;
DE  Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:16478804, PubMed:19650074, PubMed:16300740, PubMed:19723804, PubMed:11056169, PubMed:22858377, PubMed:11940591, PubMed:18690848, PubMed:22565310, PubMed:20181828, PubMed:30451898). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310). Negatively regulates apoptosis through interaction with PTMA (PubMed:16478804). Inhibits autophagy- induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates to DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (PubMed:19650074). Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (PubMed:11940591). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (PubMed:16300740). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O54842, ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:11056169, ECO:0000269|PubMed:11940591, ECO:0000269|PubMed:16300740, ECO:0000269|PubMed:16478804, ECO:0000269|PubMed:18690848, ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:19723804, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22858377, ECO:0000269|PubMed:30451898}.
DE  Reference Proteome: Yes;
DE  Interaction: P00352; IntAct: EBI-752170,EBI-3908808; Score: 0.37
DE  Interaction: Q15761; IntAct: EBI-3918088,EBI-3908808; Score: 0.37
DE  Interaction: Q01105; IntAct: EBI-3908808,EBI-1053182; Score: 0.37
DE  Interaction: Q02383; IntAct: EBI-3908808,EBI-2609565; Score: 0.35
DE  Interaction: P04279; IntAct: EBI-3908808,EBI-953955; Score: 0.35
DE  Interaction: Q9H221; IntAct: EBI-3908808,EBI-3908684; Score: 0.37
GO  GO:0005737;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032993;
GO  GO:0010698;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0003713;
GO  GO:0002526;
GO  GO:0042771;
GO  GO:0008584;
GO  GO:0043066;
GO  GO:1902902;
GO  GO:0010507;
GO  GO:0010667;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043433;
GO  GO:1904036;
GO  GO:0050680;
GO  GO:0048147;
GO  GO:0045820;
GO  GO:0062099;
GO  GO:1904691;
GO  GO:0045787;
GO  GO:2001244;
GO  GO:0150078;
GO  GO:0043525;
GO  GO:1903862;
GO  GO:1901800;
GO  GO:0031401;
GO  GO:0006473;
GO  GO:0065003;
GO  GO:0010506;
GO  GO:2000194;
GO  GO:1905897;
GO  GO:0009636;
GO  GO:0035914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGA
SQ  RR
//
ID  P58195;
PN  Phospholipid scramblase 1;
GN  Plscr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein. Membrane; Lipid-anchor {ECO:0000250}; Cytoplasmic side. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. {ECO:0000250|UniProtKB:O15162}.
DR  UNIPROT: P58195;
DR  Pfam: PF03803;
DE  Function: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0042609;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0019899;
GO  GO:0005154;
GO  GO:0017128;
GO  GO:0017124;
GO  GO:0006953;
GO  GO:0006915;
GO  GO:0071345;
GO  GO:0071222;
GO  GO:0051607;
GO  GO:0006955;
GO  GO:0097193;
GO  GO:0030099;
GO  GO:0032091;
GO  GO:0045071;
GO  GO:0006659;
GO  GO:0070782;
GO  GO:0015914;
GO  GO:0017121;
GO  GO:0043065;
GO  GO:2000373;
GO  GO:0010628;
GO  GO:0045089;
GO  GO:1902231;
GO  GO:0045944;
GO  GO:0060368;
GO  GO:0033003;
GO  GO:0035455;
GO  GO:0035456;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDP
SQ  SGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAV
SQ  EDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEK
SQ  RQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFM
SQ  FFERTGNEEQRSGVW
//
ID  O43586;
PN  Proline-serine-threonine phosphatase-interacting protein 1;
GN  PSTPIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9857189}. Cell membrane {ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:9857189}; Peripheral membrane protein {ECO:0000269|PubMed:9857189}. Cell projection, uropodium {ECO:0000269|PubMed:18480402}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97814}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P97814}. Cleavage furrow {ECO:0000250|UniProtKB:P97814}. Note=Mainly cytoplasmic in T-cells (PubMed:9857189). Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells (PubMed:9857189). In monocytes, forms a branched filamentous network in the cytoplasm (PubMed:19584923). In transfected cells, forms relatively straight filaments radiating out from the nucleus (PubMed:19584923). Filament formation requires an intact tubulin cytoskeleton (PubMed:19584923). In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (PubMed:18480402). Colocalized with PTPN12 in the cytoplasm and the perinuclear region. During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers. In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow. Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (By similarity). {ECO:0000250|UniProtKB:P97814, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
DR  UNIPROT: O43586;
DR  UNIPROT: B5BU74;
DR  UNIPROT: B5BUK4;
DR  UNIPROT: O43585;
DR  UNIPROT: O95657;
DR  PDB: 2DIL;
DR  Pfam: PF00611;
DR  Pfam: PF14604;
DR  PROSITE: PS51741;
DR  PROSITE: PS50002;
DR  OMIM: 604416;
DR  OMIM: 606347;
DR  DisGeNET: 9051;
DE  Function: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T- cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000250, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
DE  Disease: PAPA syndrome (PAPAS) [MIM:604416]: Characterized by autosomal dominant inheritance of early-onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction. {ECO:0000269|PubMed:11971877, ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:22161697}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-1050964,EBI-1050964; Score: 0.59
DE  Interaction: Q8WWY3; IntAct: EBI-1567797,EBI-1050964; Score: 0.81
DE  Interaction: O00560; IntAct: EBI-1050964,EBI-727004; Score: 0.56
DE  Interaction: O43684; IntAct: EBI-1050987,EBI-1050964; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-1050964,EBI-6658203; Score: 0.72
DE  Interaction: Q9H788; IntAct: EBI-747035,EBI-1050964; Score: 0.56
DE  Interaction: Q96B02; IntAct: EBI-716589,EBI-1050964; Score: 0.67
DE  Interaction: Q96D16; IntAct: EBI-1050964,EBI-744419; Score: 0.56
DE  Interaction: Q14D33; IntAct: EBI-10217913,EBI-1050964; Score: 0.72
DE  Interaction: O75386; IntAct: EBI-5357290,EBI-1050964; Score: 0.72
DE  Interaction: Q9UQ90; IntAct: EBI-1050964,EBI-717201; Score: 0.56
DE  Interaction: Q9Y228; IntAct: EBI-765817,EBI-1050964; Score: 0.56
DE  Interaction: Q9Y473; IntAct: EBI-3438881,EBI-1050964; Score: 0.56
DE  Interaction: Q9Y4Z0; IntAct: EBI-1050964,EBI-372521; Score: 0.72
DE  Interaction: Q9Y5E9; IntAct: EBI-1050964,EBI-10329013; Score: 0.72
DE  Interaction: P48023; IntAct: EBI-495538,EBI-1050964; Score: 0.70
DE  Interaction: X5D7R7; IntAct: EBI-1050964,EBI-21250265; Score: 0.37
DE  Interaction: X5DP17; IntAct: EBI-1050964,EBI-21250593; Score: 0.37
DE  Interaction: Q96T60; IntAct: EBI-1050964,EBI-1045072; Score: 0.56
DE  Interaction: Q09161; IntAct: EBI-464743,EBI-1050964; Score: 0.56
DE  Interaction: P62910; IntAct: EBI-438408,EBI-1050964; Score: 0.40
DE  Interaction: P31939; IntAct: EBI-1048599,EBI-1050964; Score: 0.40
DE  Interaction: Q9UMN6; IntAct: EBI-765774,EBI-1050964; Score: 0.40
DE  Interaction: Q9UBS9; IntAct: EBI-1056837,EBI-1050964; Score: 0.40
DE  Interaction: Q9BVP2; IntAct: EBI-641642,EBI-1050964; Score: 0.40
DE  Interaction: Q9UKX3; IntAct: EBI-1050964,EBI-373433; Score: 0.40
DE  Interaction: Q96LW2; IntAct: EBI-1054572,EBI-1050964; Score: 0.40
DE  Interaction: P49207; IntAct: EBI-1051893,EBI-1050964; Score: 0.40
DE  Interaction: P05408; IntAct: EBI-722635,EBI-1050964; Score: 0.40
DE  Interaction: P42766; IntAct: EBI-1050964,EBI-356819; Score: 0.40
DE  Interaction: P61513; IntAct: EBI-356793,EBI-1050964; Score: 0.40
DE  Interaction: Q15058; IntAct: EBI-1045252,EBI-1050964; Score: 0.40
DE  Interaction: Q9Y3U8; IntAct: EBI-1057689,EBI-1050964; Score: 0.40
DE  Interaction: Q75MH1; IntAct: EBI-1058398,EBI-1050964; Score: 0.40
DE  Interaction: Q7L1Q6; IntAct: EBI-1046727,EBI-1050964; Score: 0.40
DE  Interaction: Q8IZX4; IntAct: EBI-475871,EBI-1050964; Score: 0.40
DE  Interaction: P62750; IntAct: EBI-353254,EBI-1050964; Score: 0.40
DE  Interaction: P61254; IntAct: EBI-352405,EBI-1050964; Score: 0.40
DE  Interaction: Q9Y265; IntAct: EBI-353675,EBI-1050964; Score: 0.40
DE  Interaction: Q9UJX6; IntAct: EBI-396211,EBI-1050964; Score: 0.40
DE  Interaction: Q02543; IntAct: EBI-350523,EBI-1050964; Score: 0.40
DE  Interaction: P83881; IntAct: EBI-1054835,EBI-1050964; Score: 0.40
DE  Interaction: Q9Y6E2; IntAct: EBI-1051021,EBI-1050964; Score: 0.40
DE  Interaction: P18077; IntAct: EBI-353383,EBI-1050964; Score: 0.40
DE  Interaction: P37268; IntAct: EBI-714550,EBI-1050964; Score: 0.40
DE  Interaction: P62899; IntAct: EBI-1053664,EBI-1050964; Score: 0.40
DE  Interaction: P39023; IntAct: EBI-1056348,EBI-1050964; Score: 0.40
DE  Interaction: Q76P68; IntAct: EBI-1059174,EBI-1050964; Score: 0.40
DE  Interaction: Q99996; IntAct: EBI-1048311,EBI-1050964; Score: 0.40
DE  Interaction: P15924; IntAct: EBI-355041,EBI-1050964; Score: 0.40
DE  Interaction: P47914; IntAct: EBI-714039,EBI-1050964; Score: 0.40
DE  Interaction: P46779; IntAct: EBI-366357,EBI-1050964; Score: 0.40
DE  Interaction: Q9NR30; IntAct: EBI-357942,EBI-1050964; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-358372,EBI-1050964; Score: 0.40
DE  Interaction: O43390; IntAct: EBI-713419,EBI-1050964; Score: 0.40
DE  Interaction: Q53FD0-2; IntAct: EBI-1050964,EBI-14104088; Score: 0.56
DE  Interaction: Q8IX18; IntAct: EBI-1050964,EBI-2514301; Score: 0.56
DE  Interaction: Q05209; IntAct: EBI-1050964,EBI-2266035; Score: 0.78
DE  Interaction: Q15287; IntAct: EBI-1050964,EBI-395959; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-1050964,EBI-5453285; Score: 0.56
DE  Interaction: P00540; IntAct: EBI-1050964,EBI-1757866; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-1050964,EBI-748391; Score: 0.56
DE  Interaction: Q03014; IntAct: EBI-1050964,EBI-747421; Score: 0.56
DE  Interaction: P17752; IntAct: EBI-1050964,EBI-3956833; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-7116203,EBI-1050964; Score: 0.56
DE  Interaction: Q96GM5; IntAct: EBI-1050964,EBI-358489; Score: 0.56
DE  Interaction: A0A0S2Z5X4; IntAct: EBI-1050964,EBI-16429014; Score: 0.56
DE  Interaction: P28702-3; IntAct: EBI-1050964,EBI-16429492; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-1050964,EBI-710484; Score: 0.56
DE  Interaction: P32969; IntAct: EBI-1050964,EBI-358122; Score: 0.56
DE  Interaction: Q96GY3; IntAct: EBI-1050964,EBI-748884; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-1050964,EBI-2339219; Score: 0.56
DE  Interaction: Q9UK33; IntAct: EBI-1050964,EBI-746277; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-1050964,EBI-10241197; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-1050964,EBI-348259; Score: 0.56
DE  Interaction: Q9H9D4; IntAct: EBI-1050964,EBI-347633; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-1050964,EBI-2556193; Score: 0.56
DE  Interaction: Q14005-2; IntAct: EBI-1050964,EBI-17178971; Score: 0.56
DE  Interaction: P0CG20; IntAct: EBI-1050964,EBI-11986293; Score: 0.56
DE  Interaction: Q9GZV7; IntAct: EBI-1050964,EBI-11956675; Score: 0.56
DE  Interaction: Q06630; IntAct: EBI-1050964,EBI-36794; Score: 0.56
DE  Interaction: Q12446; IntAct: EBI-1050964,EBI-10022; Score: 0.56
DE  Interaction: O15553; IntAct: EBI-7644532,EBI-1050964; Score: 0.58
GO  GO:0032154;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001931;
GO  GO:0008092;
GO  GO:0042802;
GO  GO:0007155;
GO  GO:0006897;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9857189};
SQ  MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSL
SQ  KQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFER
SQ  ISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSM
SQ  QCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPK
SQ  TTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVE
SQ  RNGQRGFVPGSYLEKL
//
ID  Q13459;
PN  Unconventional myosin-IXb;
GN  MYO9B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000269|PubMed:8907710}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8907710}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8907710, ECO:0000269|PubMed:9490638}. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region. {ECO:0000269|PubMed:8907710}.
DR  UNIPROT: Q13459;
DR  UNIPROT: O75314;
DR  UNIPROT: Q9NUJ2;
DR  UNIPROT: Q9UHN0;
DR  PDB: 5C5S;
DR  PDB: 5HPY;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF00788;
DR  Pfam: PF00620;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS50200;
DR  PROSITE: PS50238;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 602129;
DR  OMIM: 609753;
DR  DisGeNET: 4650;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:9490638, PubMed:26529257). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269|PubMed:26529257, ECO:0000269|PubMed:9490638}.
DE  Disease: Celiac disease 4 (CELIAC4) [MIM:609753]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten-containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NID9; IntAct: EBI-721429,EBI-2798201; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-447544,EBI-721429; Score: 0.35
DE  Interaction: Q15345; IntAct: EBI-721429,EBI-721408; Score: 0.37
DE  Interaction: Q9Y3A3; IntAct: EBI-721429,EBI-713935; Score: 0.37
DE  Interaction: Q15651; IntAct: EBI-1758705,EBI-721429; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-5327611,EBI-721429; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-358372,EBI-721429; Score: 0.40
DE  Interaction: Q15293; IntAct: EBI-948278,EBI-721429; Score: 0.40
DE  Interaction: Q15155; IntAct: EBI-373107,EBI-721429; Score: 0.40
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0016459;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0005516;
GO  GO:0005096;
GO  GO:0046872;
GO  GO:0000146;
GO  GO:0017048;
GO  GO:0048495;
GO  GO:0030048;
GO  GO:0035023;
GO  GO:0051056;
GO  GO:0007266;
GO  GO:0035385;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGTKCYVLVEVKESGGEEWVLDA
SQ  NDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKYVHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEG
SQ  NLLKNLKHRFLQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVISGE
SQ  SGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVSYLESGIVRGAVVEKYLL
SQ  EKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPEDYFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQ
SQ  IFAVLSAILYLGNVTYKKRATGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDS
SQ  MAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFNQHIFKLEQEEY
SQ  QGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKV
SQ  KYQIKDFREKNMDYMRPDIVALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGA
SQ  QSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKSKGIKQKQIIPKNLLDSKSLK
SQ  LIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLE
SQ  TVRIRRSGYSAKYTFQDFTEQFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKI
SQ  LLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQASWRGYWQRKLYRHQKQSIIRLQSLCRGHLQ
SQ  RKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGGQQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEA
SQ  PSPEKTLPPQKTVAAESHEKVPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESRED
SQ  ETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRVSPPAPGSAPETPEDKSKPCG
SQ  SPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVAAASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDV
SQ  SKLLPSLAKAQPAAETTDGERSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENA
SQ  VSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRESVFRQITNANELKYLDEFLLN
SQ  KINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHVGYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFT
SQ  RGYTKNDFEPVKQSKAQKKKRKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSH
SQ  CSYTYGRKGEPGVEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLE
SQ  NFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNR
SQ  MSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNAPWPL
SQ  KLGFSSPYEGVLNKSPKTRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKEDITYRLPELDPRGSDEENLDSE
SQ  TSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPTVAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHL
SQ  PRWAPGAREAAAPVRRREPPARRPDQIHSVYITPGADLPVQGALEPLEEDGQPPGAKRRYSDPPTYCLPPASGQTNG
//
ID  Q00613;
PN  Heat shock factor protein 1;
GN  HSF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:19229036, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27189267, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Cytoplasm {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10359787}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21085490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18794143}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18794143}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18794143}. Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624, PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683, PubMed:10359787). Translocates in the nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic shuttling protein (PubMed:26159920). Colocalizes with IER5 in the nucleus (PubMed:27354066). Colocalizes with BAG3 to the nucleus upon heat stress (PubMed:8455624, PubMed:26159920). Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:11447121, PubMed:11514557, PubMed:10359787, PubMed:25963659, PubMed:10747973, PubMed:24581496, PubMed:19229036). Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:11447121, PubMed:12665592, PubMed:11514557, PubMed:14707147, PubMed:10359787). Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock (PubMed:21085490). Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response (PubMed:26159920). Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326). Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) (PubMed:26359349). Colocalizes with calcium- responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes (PubMed:18794143). Colocalizes with gamma tubulin at centrosome (PubMed:18794143). Localizes at spindle pole in metaphase (PubMed:18794143). Colocalizes with PLK1 at spindle poles during prometaphase (PubMed:18794143). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:24581496, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:8455624}.
DR  UNIPROT: Q00613;
DR  UNIPROT: A8K4L0;
DR  UNIPROT: A8MW26;
DR  UNIPROT: Q53XT4;
DR  PDB: 2LDU;
DR  PDB: 5D5U;
DR  PDB: 5D5V;
DR  PDB: 5HDG;
DR  PDB: 5HDN;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DR  OMIM: 140580;
DR  DisGeNET: 3297;
DE  Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage (PubMed:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Plays also several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress- induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:1871105, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:1986252, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26727489, ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:7760831, ECO:0000269|PubMed:7935471, ECO:0000269|PubMed:8455624, ECO:0000269|PubMed:8940068, ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9341107, ECO:0000269|PubMed:9499401, ECO:0000269|PubMed:9535852, ECO:0000269|PubMed:9727490}. (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {ECO:0000269|PubMed:27189267}.
DE  Reference Proteome: Yes;
DE  Interaction: O60271; IntAct: EBI-719620,EBI-1023301; Score: 0.27
DE  Interaction: Self; IntAct: EBI-719620,EBI-719620; Score: 0.61
DE  Interaction: Q96MT8-2; IntAct: EBI-719620,EBI-21369329; Score: 0.37
DE  Interaction: O00505; IntAct: EBI-719620,EBI-358297; Score: 0.64
DE  Interaction: O95817; IntAct: EBI-719620,EBI-747185; Score: 0.64
DE  Interaction: O95757; IntAct: EBI-719620,EBI-358652; Score: 0.35
DE  Interaction: Q9NZL4; IntAct: EBI-719620,EBI-356763; Score: 0.64
DE  Interaction: Q03933; IntAct: EBI-719620,EBI-2556750; Score: 0.73
DE  Interaction: P22392; IntAct: EBI-719620,EBI-713693; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-719620,EBI-352682; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-719620,EBI-396343; Score: 0.64
DE  Interaction: Q9ULV5; IntAct: EBI-766428,EBI-719620; Score: 0.35
DE  Interaction: P14618-1; IntAct: EBI-719620,EBI-4304679; Score: 0.44
DE  Interaction: Q04759; IntAct: EBI-719620,EBI-374762; Score: 0.54
DE  Interaction: Q9CQU5; IntAct: EBI-2551595,EBI-719620; Score: 0.40
DE  Interaction: O43529; IntAct: EBI-719620,EBI-3910509; Score: 0.37
DE  Interaction: Q9UKN8; IntAct: EBI-719620,EBI-1237240; Score: 0.27
DE  Interaction: Q9UBC2; IntAct: EBI-719620,EBI-2556746; Score: 0.27
DE  Interaction: Q96SB8; IntAct: EBI-719620,EBI-605415; Score: 0.51
DE  Interaction: Q8NET4; IntAct: EBI-3951768,EBI-719620; Score: 0.51
DE  Interaction: Q8NEH6; IntAct: EBI-719620,EBI-743811; Score: 0.51
DE  Interaction: Q5VZK9; IntAct: EBI-719620,EBI-2563775; Score: 0.51
DE  Interaction: Q15555; IntAct: EBI-719620,EBI-739717; Score: 0.27
DE  Interaction: Q15029; IntAct: EBI-719620,EBI-357897; Score: 0.51
DE  Interaction: Q14C86; IntAct: EBI-719620,EBI-1049788; Score: 0.27
DE  Interaction: Q14683; IntAct: EBI-719620,EBI-80690; Score: 0.27
DE  Interaction: Q14566; IntAct: EBI-719620,EBI-374900; Score: 0.27
DE  Interaction: P61962; IntAct: EBI-719620,EBI-359808; Score: 0.27
DE  Interaction: P53350; IntAct: EBI-719620,EBI-476768; Score: 0.51
DE  Interaction: P51157; IntAct: EBI-719620,EBI-11898753; Score: 0.27
DE  Interaction: P49736; IntAct: EBI-719620,EBI-374819; Score: 0.27
DE  Interaction: P34931; IntAct: EBI-719620,EBI-354912; Score: 0.51
DE  Interaction: P33991; IntAct: EBI-719620,EBI-374938; Score: 0.27
DE  Interaction: O43683; IntAct: EBI-719620,EBI-748936; Score: 0.51
DE  Interaction: Q9Y4E8; IntAct: EBI-719620,EBI-1043104; Score: 0.27
DE  Interaction: Q9Y6Y0; IntAct: EBI-719620,EBI-715774; Score: 0.27
DE  Interaction: Q9Y6A4; IntAct: EBI-719620,EBI-1046872; Score: 0.27
DE  Interaction: Q00534; IntAct: EBI-295663,EBI-719620; Score: 0.44
DE  Interaction: Q81JT7; IntAct: EBI-719620,EBI-2811219; Score: 0.37
DE  Interaction: Q81VE1; IntAct: EBI-719620,EBI-2811760; Score: 0.37
DE  Interaction: P49137; IntAct: EBI-993299,EBI-719620; Score: 0.60
DE  Interaction: P09104; IntAct: EBI-719620,EBI-713154; Score: 0.37
DE  Interaction: Q53FA3; IntAct: EBI-10972046,EBI-719620; Score: 0.35
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000791;
GO  GO:0000792;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0000790;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0045120;
GO  GO:1990904;
GO  GO:0031490;
GO  GO:0003677;
GO  GO:0003700;
GO  GO:0000981;
GO  GO:0001227;
GO  GO:0031072;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:1990841;
GO  GO:0046982;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0001162;
GO  GO:0043565;
GO  GO:0098847;
GO  GO:0097677;
GO  GO:0061770;
GO  GO:0034622;
GO  GO:1904385;
GO  GO:0071276;
GO  GO:0071280;
GO  GO:0072738;
GO  GO:0071392;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:0070301;
GO  GO:1904845;
GO  GO:0071222;
GO  GO:1904843;
GO  GO:0035865;
GO  GO:1903936;
GO  GO:0034620;
GO  GO:0006952;
GO  GO:0006281;
GO  GO:0001892;
GO  GO:0060136;
GO  GO:0007143;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0009299;
GO  GO:0051028;
GO  GO:0010667;
GO  GO:0008285;
GO  GO:2001033;
GO  GO:0090084;
GO  GO:1901215;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:0032720;
GO  GO:1902512;
GO  GO:0008284;
GO  GO:0120162;
GO  GO:0043280;
GO  GO:0090261;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0040018;
GO  GO:0045944;
GO  GO:0061408;
GO  GO:0042531;
GO  GO:1900034;
GO  GO:0043618;
GO  GO:0014823;
GO  GO:1990910;
GO  GO:1990911;
GO  GO:0033574;
GO  GO:0007283;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRK
SQ  VVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLA
SQ  MKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPY
SQ  SAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSS
SQ  VDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT
SQ  MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGS
SQ  VDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
//
ID  Q2TBA3;
PN  Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog;
GN  Malt1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250|UniProtKB:Q9UDY8}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10 (By similarity). {ECO:0000250|UniProtKB:Q9UDY8}.
DR  UNIPROT: Q2TBA3;
DR  UNIPROT: Q2TBA2;
DR  UNIPROT: Q811E3;
DR  UNIPROT: Q8BFT0;
DR  UNIPROT: Q8C7N9;
DR  PDB: 3V4L;
DR  Pfam: PF13895;
DR  Pfam: PF18703;
DR  PROSITE: PS50208;
DR  PROSITE: PS50835;
DE  Function: Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity). Involved in the induction of T helper 17 cells (Th17) differentiation. Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (PubMed:25282160). {ECO:0000250|UniProtKB:Q9UDY8, ECO:0000269|PubMed:25282160}.
DE  Reference Proteome: Yes;
DE  Interaction: Q60803; IntAct: EBI-15909803,EBI-520135; Score: 0.40
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0019209;
GO  GO:0008233;
GO  GO:0002020;
GO  GO:0043621;
GO  GO:0004842;
GO  GO:0007250;
GO  GO:0042113;
GO  GO:0001923;
GO  GO:0071222;
GO  GO:0045087;
GO  GO:0031663;
GO  GO:0051168;
GO  GO:0043280;
GO  GO:0032731;
GO  GO:0032743;
GO  GO:0051092;
GO  GO:0050870;
GO  GO:0002726;
GO  GO:2000321;
GO  GO:0006508;
GO  GO:0042981;
GO  GO:0050856;
GO  GO:0009620;
GO  GO:0042098;
GO  GO:0050852;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLWGQPLQASPPLAVRQPPTASSGPSTSPPAGATLNRLPEPLLRRLSESLDRAPEGRGWRQLAELAGSRGRLRLSGLDL
SQ  EQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQALEHTEVLPLLNPPGLKITVNPESKAVLAGQFVKLCCRATGHP
SQ  FVQYQWFKMNKEIPYGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFSQWSQLDVCDVAEVTDSFQGSMDGISESRLQICV
SQ  EPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYTVPYVDIEHEGTYWCHVYNDRDSQDSKKAEVTIGRT
SQ  DEAVECTEDELNNLGHPDNKEQTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMC
SQ  NAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDD
SQ  TIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGRQALEIRS
SQ  SLSEKRALTDPVQGAPCSAEALVRNLQWAKAHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYV
SQ  TDFPLDLDIDPKHANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLI
SQ  AKLDMHRGLGRKTCFQACRMPDEPYHSSTSTSAGAGHFHSSQDSFHDVYHSHLGNADSGMPPDRCHCSRTPHTFISNYPP
SQ  HHYCQFGRSNVPVETTDEMPFSFSDRLMISEN
//
ID  O00423;
PN  Echinoderm microtubule-associated protein-like 1;
GN  EML1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules (PubMed:24859200). Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity). {ECO:0000250|UniProtKB:Q05BC3, ECO:0000269|PubMed:24859200}.
DR  UNIPROT: O00423;
DR  UNIPROT: Q86U15;
DR  UNIPROT: Q8N536;
DR  UNIPROT: Q8N5C4;
DR  UNIPROT: Q8WWL6;
DR  PDB: 4CI8;
DR  Pfam: PF03451;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 600348;
DR  OMIM: 602033;
DR  DisGeNET: 2009;
DE  Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
DE  Disease: Band heterotopia (BH) [MIM:600348]: A brain malformation of the lissencephaly spectrum, resulting from disordered neuronal migration and characterized by bands of gray matter interposed in the central white matter. Disease features include severe developmental delay with intellectual disability, enlarged head circumference, periventricular and ribbon-like subcortical heterotopia, polymicrogyria and agenesis of the corpus callosum. {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:28556411}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H9L3; IntAct: EBI-751335,EBI-751327; Score: 0.62
DE  Interaction: Q9Y266; IntAct: EBI-751327,EBI-357298; Score: 0.40
DE  Interaction: Q14203; IntAct: EBI-724352,EBI-751327; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-740086,EBI-751327; Score: 0.35
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:1990023;
GO  GO:0097431;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008017;
GO  GO:0015631;
GO  GO:0007420;
GO  GO:0002244;
GO  GO:0000226;
GO  GO:0007052;
GO  GO:0007405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKG
SQ  PTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGS
SQ  TSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYL
SQ  LPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIG
SQ  IGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTL
SQ  EGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGK
SQ  DRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLT
SQ  CGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNF
SQ  LAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWAT
SQ  YTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLI
SQ  STGGKDTSIMQWRVI
//
ID  Q05655;
PN  Protein kinase C delta type catalytic subunit;
GN  PRKCD;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046, ECO:0000269|PubMed:18285462}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046}. Nucleus {ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046, ECO:0000269|PubMed:18285462}. Cell membrane {ECO:0000269|PubMed:17603046}; Peripheral membrane protein {ECO:0000305|PubMed:17603046}.
DR  UNIPROT: Q05655;
DR  UNIPROT: B0KZ81;
DR  UNIPROT: B2R834;
DR  UNIPROT: Q15144;
DR  UNIPROT: Q86XJ6;
DR  PDB: 1YRK;
DR  PDB: 2YUU;
DR  Pfam: PF00130;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 176977;
DR  OMIM: 615559;
DR  DisGeNET: 5580;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro- survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462). {ECO:0000250, ECO:0000269|PubMed:11748588, ECO:0000269|PubMed:11877440, ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:16940418, ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19587372, ECO:0000269|PubMed:19801500}.
DE  Disease: Autoimmune lymphoproliferative syndrome 3 (ALPS3) [MIM:615559]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. CVID9 patients have B-cell deficiency and severe autoimmunity. {ECO:0000269|PubMed:23319571}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P17677; IntAct: EBI-1267511,EBI-704279; Score: 0.60
DE  Interaction: P11388; IntAct: EBI-704279,EBI-539628; Score: 0.68
DE  Interaction: Q02880; IntAct: EBI-704279,EBI-2307774; Score: 0.35
DE  Interaction: P78527-2; IntAct: EBI-704279,EBI-7195896; Score: 0.35
DE  Interaction: P78527-1; IntAct: EBI-704279,EBI-3952976; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-366083,EBI-704279; Score: 0.60
DE  Interaction: Q96A56; IntAct: EBI-704279,EBI-9986117; Score: 0.40
DE  Interaction: P57078; IntAct: EBI-4422308,EBI-704279; Score: 0.53
DE  Interaction: P41594; IntAct: EBI-6595175,EBI-704279; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-704279,EBI-515315; Score: 0.75
DE  Interaction: P29353; IntAct: EBI-78835,EBI-704279; Score: 0.53
DE  Interaction: P19878; IntAct: EBI-704279,EBI-489611; Score: 0.54
DE  Interaction: Q9GZU8; IntAct: EBI-704279,EBI-2371956; Score: 0.35
DE  Interaction: P51114-2; IntAct: EBI-704279,EBI-11022345; Score: 0.35
DE  Interaction: A5PLN9-2; IntAct: EBI-704279,EBI-10985648; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-704279,EBI-395940; Score: 0.35
DE  Interaction: E7EVG6; IntAct: EBI-704279,EBI-11134881; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-704279,EBI-1773495; Score: 0.35
DE  Interaction: P29401; IntAct: EBI-704279,EBI-1050560; Score: 0.35
DE  Interaction: Q9BRD0; IntAct: EBI-704279,EBI-2561235; Score: 0.35
DE  Interaction: O60231; IntAct: EBI-704279,EBI-311446; Score: 0.35
DE  Interaction: Q9P013; IntAct: EBI-704279,EBI-2371709; Score: 0.35
DE  Interaction: Q3L8U1-2; IntAct: EBI-704279,EBI-10965785; Score: 0.35
DE  Interaction: P61513; IntAct: EBI-704279,EBI-356793; Score: 0.35
DE  Interaction: Q8IV50; IntAct: EBI-704279,EBI-11021255; Score: 0.35
DE  Interaction: O60814; IntAct: EBI-704279,EBI-4409738; Score: 0.35
DE  Interaction: P52739; IntAct: EBI-704279,EBI-2849346; Score: 0.35
DE  Interaction: Q8N5V2; IntAct: EBI-718372,EBI-704279; Score: 0.35
DE  Interaction: Q9NYF8; IntAct: EBI-437804,EBI-704279; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-704279,EBI-706216; Score: 0.35
DE  Interaction: Q04759; IntAct: EBI-704279,EBI-374762; Score: 0.35
DE  Interaction: P24001-2; IntAct: EBI-704279,EBI-8800907; Score: 0.73
DE  Interaction: P33993; IntAct: EBI-355924,EBI-704279; Score: 0.35
DE  Interaction: Q9BXL7; IntAct: EBI-7006141,EBI-704279; Score: 0.62
DE  Interaction: Q9UDY8; IntAct: EBI-704279,EBI-1047372; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-704279,EBI-359276; Score: 0.40
GO  GO:0035578;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0043560;
GO  GO:0019900;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0004674;
GO  GO:0032147;
GO  GO:0006915;
GO  GO:0042100;
GO  GO:0060326;
GO  GO:0007049;
GO  GO:1904385;
GO  GO:0070301;
GO  GO:0071447;
GO  GO:0090398;
GO  GO:0042742;
GO  GO:0038096;
GO  GO:0016572;
GO  GO:0016064;
GO  GO:0060333;
GO  GO:0032613;
GO  GO:0032615;
GO  GO:0035556;
GO  GO:0008631;
GO  GO:0030837;
GO  GO:0051490;
GO  GO:0034351;
GO  GO:0050728;
GO  GO:0046627;
GO  GO:0043407;
GO  GO:0050732;
GO  GO:0090331;
GO  GO:0032091;
GO  GO:0042119;
GO  GO:0043312;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0030168;
GO  GO:2001235;
GO  GO:2000304;
GO  GO:0032079;
GO  GO:2000753;
GO  GO:1900163;
GO  GO:0035307;
GO  GO:0042307;
GO  GO:2001022;
GO  GO:2000755;
GO  GO:0032930;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0032956;
GO  GO:0043488;
GO  GO:0010469;
GO  GO:0007165;
GO  GO:0002223;
GO  GO:0023021;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:17603046};
SQ  MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEP
SQ  VSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHE
SQ  FIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMS
SQ  PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKT
SQ  GVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRV
SQ  LTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVL
SQ  LDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI
SQ  RVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNE
SQ  KARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED
//
ID  O70582;
PN  Arachidonate 12-lipoxygenase, 12R-type;
GN  Alox12b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
DR  UNIPROT: O70582;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:16129665). Does not convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE (PubMed:10100631, PubMed:11256953). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega- hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:17403930, PubMed:17429434, PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (By similarity). {ECO:0000250|UniProtKB:O75342, ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665, ECO:0000269|PubMed:17403930, ECO:0000269|PubMed:17429434, ECO:0000269|PubMed:21558561}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0004052;
GO  GO:0047677;
GO  GO:0003824;
GO  GO:0005506;
GO  GO:1990136;
GO  GO:0016702;
GO  GO:0019369;
GO  GO:0046513;
GO  GO:0061436;
GO  GO:0051122;
GO  GO:0043651;
GO  GO:0019372;
GO  GO:0055114;
GO  GO:0010628;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0006497;
GO  GO:0006665;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKD
SQ  PWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIP
SQ  SYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIK
SQ  NIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRI
SQ  LDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLL
SQ  ESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLC
SQ  IPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTI
SQ  PELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPD
SQ  DRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI
//
ID  Q5VWP3;
PN  Muscular LMNA-interacting protein;
GN  MLIP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
DR  UNIPROT: Q5VWP3;
DR  UNIPROT: B7Z2N0;
DR  UNIPROT: D6RE05;
DR  UNIPROT: Q96H08;
DR  UNIPROT: Q96NF7;
DR  Pfam: PF15274;
DR  OMIM: 614106;
DR  DisGeNET: 90523;
DE  Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy. Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD. {ECO:0000250|UniProtKB:A0A096MK47, ECO:0000250|UniProtKB:Q5FW52}.
DE  Disease: Note=Expression is reduced in patients with dilated cardiomyocytes. In murine cardiomyopathy models, deletion of the encoding gene accelerates progress from hypertrophy to heart failure. {ECO:0000269|PubMed:26436652}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0042383;
GO  GO:0005521;
GO  GO:0003714;
GO  GO:0010614;
GO  GO:1903243;
GO  GO:0000122;
GO  GO:0045944;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5FW52};
SQ  MELEKREKRSLLNKNLEEKLTVSAGGSEAKPLIFTFVPTVRRLPTHTQLADTSKFLVKIPEESSDKSPETVNRSKSNDYL
SQ  TLNAGSQQERDQAKLTCPSEVSGTILQEREFEANKLQGMQQSDLFKAEYVLIVDSEGEDEAASRKVEQGPPGGIGTAAVR
SQ  PKSLAISSSLVSDVVRPKTQGTDLKTSSHPEMLHGMAPQQKHGQQYKTKSSYKAFAAIPTNTLLLEQKALDEPAKTESVS
SQ  KDNTLEPPVELYFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRSPKTLLGSDTVKTPTTLPRAAGRETKYANLSSPS
SQ  STVSESQLTKPGVIRPVPVKSRILLKKEEEVYEPNPFSKYLEDNSDLFSEQDVTVPPKPVSLHPLYQTKLYPPAKSLLHP
SQ  QTLSHADCLAPGPFSHLSFSLSDEQENSHTLLSHNACNKLSHPMVAIPEHEALDSKEQ
//
ID  O14976;
PN  Cyclin-G-associated kinase;
GN  GAK;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10625686}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10625686}. Cell junction, focal adhesion {ECO:0000305|PubMed:10625686}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions.
DR  UNIPROT: O14976;
DR  UNIPROT: Q5U4P5;
DR  UNIPROT: Q9BVY6;
DR  PDB: 4C57;
DR  PDB: 4C58;
DR  PDB: 4C59;
DR  PDB: 4O38;
DR  PDB: 4Y8D;
DR  PDB: 5Y7Z;
DR  PDB: 5Y80;
DR  Pfam: PF00069;
DR  Pfam: PF10409;
DR  PROSITE: PS51182;
DR  PROSITE: PS50076;
DR  PROSITE: PS51181;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602052;
DR  DisGeNET: 2580;
DE  Function: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. {ECO:0000269|PubMed:10625686}.
DE  Reference Proteome: Yes;
DE  Interaction: O14966; IntAct: EBI-372165,EBI-714707; Score: 0.35
DE  Interaction: P10275; IntAct: EBI-714707,EBI-608057; Score: 0.37
DE  Interaction: Q9Y6W8; IntAct: EBI-3922712,EBI-714707; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-6659161,EBI-714707; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-714707,EBI-5323863; Score: 0.79
DE  Interaction: P11142; IntAct: EBI-714707,EBI-351896; Score: 0.71
DE  Interaction: Q9UL15; IntAct: EBI-714707,EBI-356517; Score: 0.35
DE  Interaction: Q38SD2; IntAct: EBI-1050422,EBI-714707; Score: 0.44
DE  Interaction: Q76MZ3; IntAct: EBI-400413,EBI-714707; Score: 0.35
DE  Interaction: A2AUM9; IntAct: EBI-2554268,EBI-714707; Score: 0.35
DE  Interaction: P63005; IntAct: EBI-917499,EBI-714707; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-7597484,EBI-714707; Score: 0.35
DE  Interaction: P10126; IntAct: EBI-773865,EBI-714707; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079353,EBI-714707; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-726598,EBI-714707; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-714707; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-2803688,EBI-714707; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-354967,EBI-714707; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-357515,EBI-714707; Score: 0.35
DE  Interaction: P51805; IntAct: EBI-714707,EBI-7135904; Score: 0.35
DE  Interaction: Q9Y496; IntAct: EBI-714707,EBI-1104844; Score: 0.35
DE  Interaction: Q14789; IntAct: EBI-714707,EBI-709973; Score: 0.35
DE  Interaction: Q2M2I8-2; IntAct: EBI-714707,EBI-10965264; Score: 0.35
DE  Interaction: Q8N556; IntAct: EBI-714707,EBI-3893163; Score: 0.35
DE  Interaction: O43175; IntAct: EBI-714707,EBI-350495; Score: 0.35
DE  Interaction: O75146; IntAct: EBI-714707,EBI-4402639; Score: 0.53
DE  Interaction: P47756-2; IntAct: EBI-714707,EBI-353608; Score: 0.35
DE  Interaction: P27482; IntAct: EBI-714707,EBI-747537; Score: 0.35
DE  Interaction: P53992; IntAct: EBI-714707,EBI-81134; Score: 0.35
DE  Interaction: Q14677; IntAct: EBI-714707,EBI-1171113; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-714707,EBI-351479; Score: 0.35
DE  Interaction: P49757-4; IntAct: EBI-714707,EBI-10983190; Score: 0.35
DE  Interaction: Q9ULH0-4; IntAct: EBI-714707,EBI-10982220; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-714707,EBI-396684; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-714707,EBI-1046596; Score: 0.35
DE  Interaction: Q13813; IntAct: EBI-714707,EBI-351450; Score: 0.35
DE  Interaction: Q96PK6; IntAct: EBI-714707,EBI-954272; Score: 0.35
DE  Interaction: E9PK67; IntAct: EBI-714707,EBI-11017432; Score: 0.35
DE  Interaction: Q00610-2; IntAct: EBI-714707,EBI-10963396; Score: 0.35
DE  Interaction: Q96FJ0; IntAct: EBI-714707,EBI-745021; Score: 0.53
DE  Interaction: Q8IVT2; IntAct: EBI-714707,EBI-2555085; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-714707,EBI-358826; Score: 0.35
DE  Interaction: P09496-2; IntAct: EBI-714707,EBI-4401010; Score: 0.35
DE  Interaction: P08047; IntAct: EBI-714707,EBI-298336; Score: 0.35
DE  Interaction: Q9H0K6; IntAct: EBI-714707,EBI-5464419; Score: 0.35
DE  Interaction: Q8WXE9; IntAct: EBI-714707,EBI-539742; Score: 0.35
DE  Interaction: Q27J81; IntAct: EBI-714707,EBI-2557882; Score: 0.35
DE  Interaction: P14384; IntAct: EBI-714707,EBI-2561541; Score: 0.35
DE  Interaction: Q14677-3; IntAct: EBI-714707,EBI-10983245; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-714707,EBI-355475; Score: 0.35
DE  Interaction: Q3B7T1; IntAct: EBI-714707,EBI-2870947; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-714707,EBI-2556538; Score: 0.35
DE  Interaction: Q9UBH6; IntAct: EBI-714707,EBI-8799896; Score: 0.35
DE  Interaction: O00159-3; IntAct: EBI-714707,EBI-10965365; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-714707,EBI-351394; Score: 0.35
DE  Interaction: Q5T0W9; IntAct: EBI-714707,EBI-2556565; Score: 0.35
DE  Interaction: O00443; IntAct: EBI-714707,EBI-641094; Score: 0.35
DE  Interaction: H0YEF7; IntAct: EBI-714707,EBI-10983177; Score: 0.35
DE  Interaction: Q9NSY1; IntAct: EBI-714707,EBI-1383367; Score: 0.35
DE  Interaction: F5GWT4; IntAct: EBI-714707,EBI-11081194; Score: 0.35
DE  Interaction: P09497-2; IntAct: EBI-714707,EBI-10965328; Score: 0.35
DE  Interaction: Q9UM54-6; IntAct: EBI-714707,EBI-10983181; Score: 0.35
DE  Interaction: Q8N3V7-2; IntAct: EBI-714707,EBI-10965260; Score: 0.35
DE  Interaction: P0DP23; IntAct: EBI-714707,EBI-397435; Score: 0.35
DE  Interaction: Q9UK73; IntAct: EBI-714707,EBI-310482; Score: 0.35
DE  Interaction: Q13492-2; IntAct: EBI-714707,EBI-10983186; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-714707,EBI-432924; Score: 0.35
DE  Interaction: O94973-2; IntAct: EBI-714707,EBI-10981066; Score: 0.35
DE  Interaction: Q13470-2; IntAct: EBI-714707,EBI-11018037; Score: 0.35
DE  Interaction: Q8TDG2; IntAct: EBI-714707,EBI-11062242; Score: 0.35
DE  Interaction: O00291; IntAct: EBI-714707,EBI-473886; Score: 0.35
DE  Interaction: O95782-2; IntAct: EBI-714707,EBI-10965313; Score: 0.35
DE  Interaction: Q9BY43; IntAct: EBI-714707,EBI-747981; Score: 0.35
DE  Interaction: P98082; IntAct: EBI-714707,EBI-1171238; Score: 0.35
DE  Interaction: Q07912; IntAct: EBI-714707,EBI-603457; Score: 0.35
DE  Interaction: Q96CW1-2; IntAct: EBI-714707,EBI-10965256; Score: 0.35
DE  Interaction: Q9H2Y7; IntAct: EBI-714707,EBI-1211501; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-714707,EBI-1059012; Score: 0.35
DE  Interaction: O15027-5; IntAct: EBI-714707,EBI-10990372; Score: 0.35
DE  Interaction: Q8TEH3; IntAct: EBI-714707,EBI-8796791; Score: 0.35
DE  Interaction: Q8N684-2; IntAct: EBI-714707,EBI-5280595; Score: 0.35
DE  Interaction: P15735; IntAct: EBI-1383819,EBI-714707; Score: 0.35
DE  Interaction: Q9Y4C4; IntAct: EBI-2864441,EBI-714707; Score: 0.44
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-714707; Score: 0.35
DE  Interaction: Q8N3R9-2; IntAct: EBI-16399750,EBI-714707; Score: 0.35
DE  Interaction: Q9UJ41-2; IntAct: EBI-6448458,EBI-714707; Score: 0.35
DE  Interaction: Q9Q2G4; IntAct: EBI-6248094,EBI-714707; Score: 0.35
DE  Interaction: Q9NQ11; IntAct: EBI-714707,EBI-6308763; Score: 0.51
DE  Interaction: O60763; IntAct: EBI-356164,EBI-714707; Score: 0.37
DE  Interaction: P49023; IntAct: EBI-702209,EBI-714707; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-714707; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-714707; Score: 0.35
DE  Interaction: Q9P296; IntAct: EBI-2874691,EBI-714707; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-18636064,EBI-714707; Score: 0.35
DE  Interaction: Q09019; IntAct: EBI-724564,EBI-714707; Score: 0.35
DE  Interaction: Q9ULV8; IntAct: EBI-2341018,EBI-714707; Score: 0.35
DE  Interaction: Q8N2M8-3; IntAct: EBI-21570860,EBI-714707; Score: 0.35
DE  Interaction: Q96SL4; IntAct: EBI-749411,EBI-714707; Score: 0.35
DE  Interaction: Q9NSE4; IntAct: EBI-1054770,EBI-714707; Score: 0.35
DE  Interaction: Q9NZL4; IntAct: EBI-356763,EBI-714707; Score: 0.35
DE  Interaction: O95630; IntAct: EBI-396676,EBI-714707; Score: 0.35
DE  Interaction: O15169; IntAct: EBI-714707,EBI-710484; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0031982;
GO  GO:0005524;
GO  GO:0051087;
GO  GO:0030276;
GO  GO:0030332;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0051085;
GO  GO:0072318;
GO  GO:1905224;
GO  GO:0072583;
GO  GO:0007029;
GO  GO:0007030;
GO  GO:0090160;
GO  GO:0061024;
GO  GO:0010977;
GO  GO:0034067;
GO  GO:0072659;
GO  GO:0006898;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNR
SQ  AIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQ
SQ  HMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPI
SQ  GEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR
SQ  NVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSV
SQ  ANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAP
SQ  HLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMC
SQ  DMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDV
SQ  LIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAP
SQ  PWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEE
SQ  KEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDG
SQ  VDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADP
SQ  FGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAW
SQ  TETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQ
SQ  TSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKT
SQ  IAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAA
SQ  GQPYEQHAKMIFMELNDAWSEFENQGSRPLF
//
ID  O08788;
PN  Dynactin subunit 1;
GN  Dctn1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Localization at centrosome is regulated by SLK- dependent phosphorylation. Localizes to centrosome in a PARKDA- dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (By similarity). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}.
DR  UNIPROT: O08788;
DR  UNIPROT: E9QLJ1;
DR  UNIPROT: Q3TZG7;
DR  Pfam: PF01302;
DR  Pfam: PF12455;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DE  Function: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation. {ECO:0000250|UniProtKB:Q14203}.
DE  Reference Proteome: Yes;
DE  Interaction: Q4ACU6; IntAct: EBI-771450,EBI-776180; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-1811542,EBI-776180; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-776180,EBI-444308; Score: 0.40
DE  Interaction: Q9UJW0; IntAct: EBI-776180,EBI-2134033; Score: 0.56
DE  Interaction: P61163; IntAct: EBI-776180,EBI-774234; Score: 0.56
DE  Interaction: Q9NZ32; IntAct: EBI-776180,EBI-2559426; Score: 0.56
DE  Interaction: Q9BTE1; IntAct: EBI-776180,EBI-747324; Score: 0.56
DE  Interaction: Q14203; IntAct: EBI-776180,EBI-724352; Score: 0.56
DE  Interaction: O00399; IntAct: EBI-776180,EBI-2559415; Score: 0.56
DE  Interaction: P47755; IntAct: EBI-776180,EBI-762451; Score: 0.56
DE  Interaction: A8K8J9; IntAct: EBI-776180,EBI-2559432; Score: 0.40
DE  Interaction: O75935; IntAct: EBI-776180,EBI-347442; Score: 0.40
DE  Interaction: P42025; IntAct: EBI-776180,EBI-367493; Score: 0.56
DE  Interaction: P48651; IntAct: EBI-776180,EBI-8652106; Score: 0.35
DE  Interaction: Q9Y592; IntAct: EBI-776180,EBI-8600408; Score: 0.35
DE  Interaction: Q9NP97; IntAct: EBI-776180,EBI-372128; Score: 0.35
DE  Interaction: P47756-2; IntAct: EBI-776180,EBI-353608; Score: 0.35
DE  Interaction: P52907; IntAct: EBI-776180,EBI-355586; Score: 0.35
DE  Interaction: O14949; IntAct: EBI-776180,EBI-720294; Score: 0.35
DE  Interaction: Q86XL3; IntAct: EBI-776180,EBI-1773621; Score: 0.35
DE  Interaction: O15235; IntAct: EBI-776180,EBI-712205; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-776180,EBI-1053100; Score: 0.35
DE  Interaction: Q15643; IntAct: EBI-776180,EBI-1047183; Score: 0.35
DE  Interaction: O75935-3; IntAct: EBI-776180,EBI-10962292; Score: 0.35
DE  Interaction: B4E1G1; IntAct: EBI-776180,EBI-10984153; Score: 0.35
DE  Interaction: Q9Y6G9; IntAct: EBI-776180,EBI-2556107; Score: 0.35
DE  Interaction: Q96L93-6; IntAct: EBI-776180,EBI-10988217; Score: 0.35
DE  Interaction: Q13561; IntAct: EBI-776180,EBI-715074; Score: 0.53
DE  Interaction: Q8CG73; IntAct: EBI-4281130,EBI-776180; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-772928,EBI-776180; Score: 0.35
DE  Interaction: Q9CQV8; IntAct: EBI-771608,EBI-776180; Score: 0.35
GO  GO:0005623;
GO  GO:0005938;
GO  GO:0099738;
GO  GO:0031252;
GO  GO:0120103;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005829;
GO  GO:0045171;
GO  GO:0000776;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0072686;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0032991;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0003774;
GO  GO:0019901;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0010457;
GO  GO:0031122;
GO  GO:0000132;
GO  GO:0032402;
GO  GO:0034454;
GO  GO:0061744;
GO  GO:0007528;
GO  GO:0050905;
GO  GO:0070050;
GO  GO:1990535;
GO  GO:1905515;
GO  GO:0051081;
GO  GO:0090316;
GO  GO:0090063;
GO  GO:0031116;
GO  GO:1904398;
GO  GO:0060236;
GO  GO:0042147;
GO  GO:0010970;
GO  GO:0021517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFT
SQ  CDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGV
SQ  AGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSE
SQ  DKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAES
SQ  LQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQ
SQ  ELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARE
SQ  TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFA
SQ  ETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERP
SQ  GLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPL
SQ  TKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKK
SQ  IRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGS
SQ  PSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLK
SQ  IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQ
SQ  SKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMK
SQ  ASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSD
SQ  TIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLI
SQ  S
//
ID  Q96PP9;
PN  Guanylate-binding protein 4;
GN  GBP4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17266443}. Nucleus {ECO:0000269|PubMed:17266443}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:21151871}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
DR  UNIPROT: Q96PP9;
DR  UNIPROT: B2R630;
DR  UNIPROT: Q05D63;
DR  UNIPROT: Q6NSL0;
DR  UNIPROT: Q86T99;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DR  OMIM: 612466;
DR  DisGeNET: 115361;
DE  Function: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TCS8; IntAct: EBI-1052020,EBI-20840650; Score: 0.40
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0020005;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042803;
GO  GO:0071346;
GO  GO:0050830;
GO  GO:0042832;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGERTLHAAVPTPGYPESESIMMAPICLVENQEEQLTVNSKALEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGKRNGF
SQ  PLGSTVQSETKGIWMWCVPHLSKPNHTLVLLDTEGLGDVEKSNPKNDSWIFALAVLLSSSFVYNSVSTINHQALEQLHYV
SQ  TELAELIRAKSCPRPDEAEDSSEFASFFPDFIWTVRDFTLELKLDGNPITEDEYLENALKLIPGKNPKIQNSNMPRECIR
SQ  HFFRKRKCFVFDRPTNDKQYLNHMDEVPEENLERHFLMQSDNFCSYIFTHAKTKTLREGIIVTGKRLGTLVVTYVDAINS
SQ  GAVPCLENAVTALAQLENPAAVQRAADHYSQQMAQQLRLPTDTLQELLDVHAACEREAIAVFMEHSFKDENHEFQKKLVD
SQ  TIEKKKGDFVLQNEEASAKYCQAELKRLSEHLTESILRGIFSVPGGHNLYLEEKKQVEWDYKLVPRKGVKANEVLQNFLQ
SQ  SQVVVEESILQSDKALTAGEKAIAAERAMKEAAEKEQELLREKQKEQQQMMEAQERSFQEYMAQMEKKLEEERENLLREH
SQ  ERLLKHKLKVQEEMLKEEFQKKSEQLNKEINQLKEKIESTKNEQLRLLKILDMASNIMIVTLPGASKLLGVGTKYLGSRI
//
ID  O75112;
PN  LIM domain-binding protein 3;
GN  LDB3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
DR  UNIPROT: O75112;
DR  UNIPROT: A2TDB7;
DR  UNIPROT: A6NIV4;
DR  UNIPROT: B4E3K3;
DR  UNIPROT: Q5K6N9;
DR  UNIPROT: Q5K6P0;
DR  UNIPROT: Q5K6P1;
DR  UNIPROT: Q96FH2;
DR  UNIPROT: Q9Y4Z3;
DR  UNIPROT: Q9Y4Z4;
DR  UNIPROT: Q9Y4Z5;
DR  PDB: 1RGW;
DR  PDB: 4YDP;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  OMIM: 601493;
DR  OMIM: 605906;
DR  OMIM: 609452;
DR  DisGeNET: 11155;
DE  Function: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.
DE  Disease: Cardiomyopathy, dilated 1C, with or without left ventricular non-compaction (CMD1C) [MIM:601493]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Cardiomyopathy dilated type 1C is associated with left ventricular non-compaction in some patients. Left ventricular non- compaction is characterized by numerous prominent trabeculations and deep intertrabecular recesses in hypertrophied and hypokinetic segments of the left ventricle. {ECO:0000269|PubMed:14660611, ECO:0000269|PubMed:14662268}. Note=The disease is caused by mutations affecting the gene represented in this entry. Left ventricular non-compaction 3 (LVNC3) [MIM:601493]: A form of left ventricular non-compaction, a cardiomyopathy due to myocardial morphogenesis arrest and characterized by a hypertrophic left ventricle, a severely thickened 2-layered myocardium, numerous prominent trabeculations, deep intertrabecular recesses, and poor systolic function. Clinical manifestations are variable. Some affected individuals experience no symptoms at all, others develop heart failure. In some cases, left ventricular non-compaction is associated with other congenital heart anomalies. LVNC3 is an autosomal dominant condition. Note=The disease is caused by mutations affecting the gene represented in this entry. Myopathy, myofibrillar, 4 (MFM4) [MIM:609452]: A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM4 is characterized by distal and proximal muscle weakness with signs of cardiomyopathy and neuropathy. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02768; IntAct: EBI-714423,EBI-1222667; Score: 0.35
GO  GO:0005912;
GO  GO:0005856;
GO  GO:0031941;
GO  GO:0048471;
GO  GO:0031143;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0008092;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0005080;
GO  GO:0030036;
GO  GO:0007507;
GO  GO:0061061;
GO  GO:0045214;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTL
SQ  QKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASD
SQ  PGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVD
SQ  SASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPAS
SQ  AQPPAAASPSAASPPLATAAAHTAIASASTTAPASSPADSPRPQASSYSPAVAASSAPATHTSYSEGPAAPAPKPRVVTT
SQ  ASIRPSVYQPVPASTYSPSPGANYSPTPYTPSPAPAYTPSPAPAYTPSPVPTYTPSPAPAYTPSPAPNYNPAPSVAYSGG
SQ  PAEPASRPPWVTDDSFSQKFAPGKSTTSISKQTLPRGGPAYTPAGPQVPPLARGTVQRAERFPASSRTPLCGHCNNVIRG
SQ  PFLVAMGRSWHPEEFTCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPLCAKCNTKIMGEVMHALRQTWHTTCFVCAACK
SQ  KPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDRPLCKK
SQ  HAHTINL
//
ID  P30429;
PN  Cell death protein 4;
GN  ced;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Note=In non cell death induced cells, ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells. {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}.
DR  UNIPROT: P30429;
DR  UNIPROT: Q5BHI5;
DR  PDB: 2A5Y;
DR  PDB: 3LQQ;
DR  PDB: 3LQR;
DR  PDB: 4M9S;
DR  PDB: 4M9X;
DR  PDB: 4M9Y;
DR  PDB: 4M9Z;
DR  Pfam: PF00619;
DR  Pfam: PF00931;
DR  PROSITE: PS50209;
DE  Function: Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development (PubMed:3955651). During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1 (PubMed:9927601). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Regulates CEP neuron apoptosis in response to high Al(3+) levels (PubMed:23106139). During male tail morphogenesis, promotes apoptosis of the tail-spike cell upstream of ced-3 but independently of egl-1 and ced-9 (PubMed:17329362). May play a role in sex-specific cell apoptosis, probably by promoting ced-3-mediated cleavage of sex-determining protein fem-1 (PubMed:10764728). During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway (PubMed:26074078). Downstream of calreticulin crt-1 and upstream of ced-3 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy (PubMed:22629231). Together with ain-1, a component of the miRNA- induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development (PubMed:25432023). May play a role in resistance to S.typhimurium- mediated infection (PubMed:11226309). {ECO:0000269|PubMed:10764728, ECO:0000269|PubMed:11226309, ECO:0000269|PubMed:17329362, ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:22629231, ECO:0000269|PubMed:23106139, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:3955651, ECO:0000269|PubMed:9927601}. [Isoform a]: Plays a major role in programmed cell death (PubMed:1286611, PubMed:8706125). egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to induce caspase ced-3 autoproteolytic cleavage and activation (PubMed:15383288, PubMed:16208361, PubMed:20434985, PubMed:24065769). Also forms a holoenzyme with processed ced-3 enhancing ced-3 activity (PubMed:20434985). {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:1286611, ECO:0000269|PubMed:15383288, ECO:0000269|PubMed:16208361, ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:24065769, ECO:0000269|PubMed:8706125}. [Isoform b]: Prevents programmed cell death. {ECO:0000269|PubMed:8706125}.
DE  Reference Proteome: Yes;
DE  Interaction: P42573; IntAct: EBI-494118,EBI-494247; Score: 0.84
DE  Interaction: P41958; IntAct: EBI-494118,EBI-494110; Score: 0.84
DE  Interaction: Q07817; IntAct: EBI-78035,EBI-494118; Score: 0.40
DE  Interaction: O61667; IntAct: EBI-494118,EBI-495949; Score: 0.35
GO  GO:0008303;
GO  GO:0005623;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0051432;
GO  GO:0051434;
GO  GO:0089720;
GO  GO:0008656;
GO  GO:0061133;
GO  GO:0042802;
GO  GO:0000287;
GO  GO:0016505;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0048598;
GO  GO:0046716;
GO  GO:0043066;
GO  GO:0043065;
GO  GO:1904747;
GO  GO:2001056;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0030155;
GO  GO:0008361;
GO  GO:0043281;
GO  GO:0040034;
GO  GO:0031647;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQ
SQ  SHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGR
SQ  AGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLL
SQ  NFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDEC
SQ  YDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMAL
SQ  QRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDH
SQ  IIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQK
SQ  FYDSLKNFACC
//
ID  Q12912;
PN  Processed lymphoid-restricted membrane protein;
GN  LRMP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Processed lymphoid-restricted membrane protein]: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome {ECO:0000250}. Note=Colocalized with ITPR3 on the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q12912;
DR  UNIPROT: A0AVM2;
DR  UNIPROT: B4E077;
DR  UNIPROT: Q8N301;
DR  Pfam: PF05781;
DR  OMIM: 602003;
DR  DisGeNET: 4033;
DE  Function: Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion.
DE  Reference Proteome: Yes;
DE  Interaction: P62258; IntAct: EBI-2839307,EBI-356498; Score: 0.37
DE  Interaction: Q9H4A3; IntAct: EBI-457907,EBI-2839307; Score: 0.37
DE  Interaction: A0A0F7RGS7; IntAct: EBI-2839307,EBI-2816751; Score: 0.37
DE  Interaction: A0A0F7RC41; IntAct: EBI-2839328,EBI-2839307; Score: 0.37
DE  Interaction: A0A0F7R429; IntAct: EBI-2839307,EBI-2814691; Score: 0.37
DE  Interaction: Q81JR3; IntAct: EBI-2839354,EBI-2839307; Score: 0.37
DE  Interaction: Q9ULV4; IntAct: EBI-351384,EBI-2839307; Score: 0.40
GO  GO:0035577;
GO  GO:0005623;
GO  GO:0005694;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0000922;
GO  GO:0043312;
GO  GO:0007338;
GO  GO:0006906;
GO  GO:0006903;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESTPFSGVANQIHTLCERPTYGEVKDGALDVKRQHKCPGPTSGPSPGTNLSGCIRMNDDPSMEENGVERVCPESLLQSR
SQ  EYSSLPLPRHTSSTDGTITSSDPGLEILNMASCDLDRNSLCKKEEDTRSASPTIEAQGTSPAHDNIAFQDSTSKDKTILN
SQ  LEAKEEPETIEEHKKEHASGDSVVSPLPVTTVKSVNLRQSENTSANEKEVEAEFLRLSLGFKCDWFTLEKRVKLEERSRD
SQ  LAEENLKKEITNCLKLLESLTPLCEDDNQAQEIIKKLEKSIKFLSQCAARVASRAEMLGAINQESRVSKAVEVMIQHVEN
SQ  LKRMYAKEHAELEELKQVLLQNERSFNPLEDDDDCQIKKRSASLNSKPSSLRRVTIASLPRNIGNAGMVAGMENNDRFSR
SQ  RSSSWRILGSKQSEHRPSLPRFISTYSWADAEEEKCELKTKDDSEPSGEETVERTRKPSLSEKKNNPSKWDVSSVYDTIA
SQ  SWATNLKSSIRKANKALWLSIAFIVLFAALMSFLTGQLFQKSVDAAPTQQEDSWTSLEHILWPFTRLRHNGPPPV
//
ID  P35240;
PN  Merlin;
GN  NF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=In a fibroblastic cell line, isoform 1 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia. Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C- terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions. [Isoform 7]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 7 is absent from ruffling membranes and filopodia. [Isoform 9]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 9 is absent from ruffling membranes and filopodia. [Isoform 10]: Nucleus. Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasmic granule. Cytoplasm, cytoskeleton. Note=In a fibroblastic cell line, isoform 10 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia.
DR  UNIPROT: P35240;
DR  UNIPROT: O95683;
DR  UNIPROT: Q8WUJ2;
DR  UNIPROT: Q969N0;
DR  UNIPROT: Q969Q3;
DR  UNIPROT: Q96T30;
DR  UNIPROT: Q96T31;
DR  UNIPROT: Q96T32;
DR  UNIPROT: Q96T33;
DR  UNIPROT: Q9BTW3;
DR  UNIPROT: Q9UNG9;
DR  UNIPROT: Q9UNH3;
DR  UNIPROT: Q9UNH4;
DR  PDB: 1H4R;
DR  PDB: 3U8Z;
DR  PDB: 4ZRI;
DR  PDB: 4ZRJ;
DR  PDB: 6CDS;
DR  Pfam: PF00769;
DR  Pfam: PF09380;
DR  Pfam: PF00373;
DR  Pfam: PF09379;
DR  PROSITE: PS00660;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  OMIM: 101000;
DR  OMIM: 156240;
DR  OMIM: 162091;
DR  OMIM: 607379;
DR  DisGeNET: 4771;
DE  Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}.
DE  Disease: Neurofibromatosis 2 (NF2) [MIM:101000]: Genetic disorder characterized by bilateral vestibular schwannomas (formerly called acoustic neuromas), schwannomas of other cranial and peripheral nerves, meningiomas, and ependymomas. It is inherited in an autosomal dominant fashion with full penetrance. Affected individuals generally develop symptoms of eighth-nerve dysfunction in early adulthood, including deafness and balance disorder. Although the tumors of NF2 are histologically benign, their anatomic location makes management difficult, and patients suffer great morbidity and mortality. {ECO:0000269|PubMed:10090912, ECO:0000269|PubMed:10669747, ECO:0000269|PubMed:10790209, ECO:0000269|PubMed:12709270, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:20445339, ECO:0000269|PubMed:7666400, ECO:0000269|PubMed:7759081, ECO:0000269|PubMed:7913580, ECO:0000269|PubMed:8081368, ECO:0000269|PubMed:8230593, ECO:0000269|PubMed:8566958, ECO:0000269|PubMed:8698340, ECO:0000269|PubMed:9643284}. Note=The disease is caused by mutations affecting the gene represented in this entry. Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer syndrome in which patients develop multiple non-vestibular schwannomas, benign neoplasms that arise from Schwann cells of the cranial, peripheral, and autonomic nerves. {ECO:0000269|PubMed:18072270}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:12136076}. Note=The disease may be caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P31689; IntAct: EBI-1014472,EBI-347834; Score: 0.35
DE  Interaction: Self; IntAct: EBI-1014472,EBI-1014472; Score: 0.40
DE  Interaction: Q9BZE4; IntAct: EBI-1056249,EBI-1014472; Score: 0.61
DE  Interaction: Q9Y6K9; IntAct: EBI-81279,EBI-1014472; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-356349,EBI-1014472; Score: 0.35
DE  Interaction: Q8NFZ5; IntAct: EBI-359372,EBI-1014472; Score: 0.35
DE  Interaction: O14964; IntAct: EBI-740220,EBI-1014472; Score: 0.40
DE  Interaction: Q9Y2J4; IntAct: EBI-746752,EBI-1014472; Score: 0.53
DE  Interaction: P46937; IntAct: EBI-1044059,EBI-1014472; Score: 0.53
DE  Interaction: O95835; IntAct: EBI-1014472,EBI-444209; Score: 0.56
DE  Interaction: P57078; IntAct: EBI-4422308,EBI-1014472; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-2511319,EBI-1014472; Score: 0.81
DE  Interaction: Q4VCS5-2; IntAct: EBI-1014472,EBI-3891843; Score: 0.59
DE  Interaction: Q4VCS5-1; IntAct: EBI-3903812,EBI-1014472; Score: 0.50
DE  Interaction: Q68EM7-1; IntAct: EBI-3957761,EBI-1014472; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-724390,EBI-1014472; Score: 0.50
DE  Interaction: Q8N3R9; IntAct: EBI-2513978,EBI-1014472; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-1014472,EBI-1307; Score: 0.40
DE  Interaction: D4A9Q2; IntAct: EBI-3892226,EBI-1014472; Score: 0.40
DE  Interaction: Q8IY63; IntAct: EBI-1014472,EBI-1057112; Score: 0.53
DE  Interaction: P35240-2; IntAct: EBI-1014505,EBI-1014472; Score: 0.35
DE  Interaction: Q14324; IntAct: EBI-1014472,EBI-5653200; Score: 0.37
DE  Interaction: Q9H204; IntAct: EBI-514199,EBI-1014472; Score: 0.58
DE  Interaction: O14745; IntAct: EBI-1014472,EBI-349787; Score: 0.37
DE  Interaction: Q10728; IntAct: EBI-1014472,EBI-918263; Score: 0.52
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1014472; Score: 0.35
DE  Interaction: Q92918; IntAct: EBI-881,EBI-1014472; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-486809,EBI-1014472; Score: 0.40
DE  Interaction: O14964-1; IntAct: EBI-21239519,EBI-1014472; Score: 0.27
DE  Interaction: Q01082; IntAct: EBI-351561,EBI-1014472; Score: 0.40
DE  Interaction: O60884; IntAct: EBI-1014472,EBI-352957; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-1014472,EBI-1103245; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-1014472,EBI-356933; Score: 0.35
DE  Interaction: Q92598; IntAct: EBI-1014472,EBI-356829; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-1014472,EBI-349105; Score: 0.35
GO  GO:0005912;
GO  GO:0045177;
GO  GO:0044297;
GO  GO:0032154;
GO  GO:0030864;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0031527;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0003779;
GO  GO:0030036;
GO  GO:0045216;
GO  GO:0007398;
GO  GO:0021766;
GO  GO:0070306;
GO  GO:0001707;
GO  GO:0030336;
GO  GO:0008285;
GO  GO:0022408;
GO  GO:0001953;
GO  GO:0043409;
GO  GO:0006469;
GO  GO:0046426;
GO  GO:0042532;
GO  GO:0042475;
GO  GO:0045597;
GO  GO:0051496;
GO  GO:0042981;
GO  GO:0051726;
GO  GO:0014013;
GO  GO:0035330;
GO  GO:2000177;
GO  GO:1900180;
GO  GO:0031647;
GO  GO:0072091;
GO  GO:0014010;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKK
SQ  VLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKR
SQ  GFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALG
SQ  LHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQ
SQ  MKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQ
SQ  KAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPT
SQ  YPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDI
SQ  LHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL
//
ID  Q12123;
PN  Inactive diphosphatase DCS2;
GN  DCS2;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic. Localizes close to the perinuclear space before the diauxic growth shift. Recruited to the P-body after the post-diauxic growth shift. Colocalizes with the decapping activator protein LSM1 at P-body.
DR  UNIPROT: Q12123;
DR  UNIPROT: D6W2M9;
DR  Pfam: PF05652;
DR  PROSITE: PS00892;
DE  Function: Plays a role in the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Stress-induced regulatory protein that modulates the m7GpppX diphosphatase activity of DCS1. {ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:16963086}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06151; IntAct: EBI-38701,EBI-38973; Score: 0.87
DE  Interaction: Self; IntAct: EBI-38701,EBI-38701; Score: 0.37
DE  Interaction: P11484; IntAct: EBI-8627,EBI-38701; Score: 0.35
DE  Interaction: P37366; IntAct: EBI-4385,EBI-38701; Score: 0.53
DE  Interaction: Q06218; IntAct: EBI-5640,EBI-38701; Score: 0.27
DE  Interaction: P40024; IntAct: EBI-22498,EBI-38701; Score: 0.27
DE  Interaction: Q08004; IntAct: EBI-35455,EBI-38701; Score: 0.27
DE  Interaction: P07245; IntAct: EBI-3897,EBI-38701; Score: 0.27
DE  Interaction: P38829; IntAct: EBI-38701,EBI-24704; Score: 0.37
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004857;
GO  GO:0050072;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0000340;
GO  GO:0031670;
GO  GO:0009267;
GO  GO:0000290;
GO  GO:0000184;
GO  GO:0090342;
GO  GO:0009408;
GO  GO:0007584;
GO  GO:0006970;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSQDLASLIGRFKYVRVLDSNPHTKVISLLGSIDGKDAVLTAEKTHFIFDETVRRPSQSGRSTPIFFHREIDEYSFLNG
SQ  ITDLKELTSNDIYYWGLSVLKQHILHNPTAKVNLIWPASQFHIKGYDQQDLHVVRETPDMYRNIVVPFIQEMCTSERMKW
SQ  VNNILYEGAEDDRVVYKEYSSRNKEDGFVILPDMKWDGINIDSLYLVAIVYRDDIKSLRDLNPNHRDWLIRLNKKIKTII
SQ  PQHYDYNVNPDELRVFIHYQPSYYHFHVHIVNIRHPGVGEERGSGMTILLEDVIEALGFLGPEGYMKKTLTYVIGENHDL
SQ  WKKGFKEEVEKQLKHDGIATSPEKGSGFNTNLG
//
ID  O89019;
PN  Inversin;
GN  Invs;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle (By similarity). Membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium. Also nuclear and perinuclear. {ECO:0000250}.
DR  UNIPROT: O89019;
DR  UNIPROT: O88849;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  Pfam: PF00612;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS50096;
DE  Function: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin- proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:9744276, ECO:0000269|PubMed:9771707}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QZZ4; IntAct: EBI-4281382,EBI-4281337; Score: 0.40
DE  Interaction: Q8BP00; IntAct: EBI-4282243,EBI-4281337; Score: 0.52
DE  Interaction: Q91ZR4; IntAct: EBI-4281337,EBI-4282339; Score: 0.64
DE  Interaction: Q9QY53; IntAct: EBI-77230,EBI-4281337; Score: 0.40
DE  Interaction: Q8K3E5; IntAct: EBI-4281337,EBI-4280729; Score: 0.40
DE  Interaction: P11499; IntAct: EBI-4281337,EBI-492813; Score: 0.35
DE  Interaction: P63017; IntAct: EBI-4281337,EBI-433443; Score: 0.35
DE  Interaction: P38647; IntAct: EBI-4281337,EBI-772469; Score: 0.35
DE  Interaction: P20029; IntAct: EBI-4281337,EBI-772325; Score: 0.35
GO  GO:0097546;
GO  GO:0097543;
GO  GO:0005576;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0005516;
GO  GO:0048513;
GO  GO:0060971;
GO  GO:0060287;
GO  GO:0001822;
GO  GO:0090090;
GO  GO:0031016;
GO  GO:0009791;
GO  GO:1904108;
GO  GO:0006468;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNISEDVLSTGSSLASQVHAAAVNGDKGALQRLIVGNSALRDKEDRFGRTPLMYCVLADRVDCADALLKAGADVNKTDHS
SQ  RRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYN
SQ  NPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNLTVVDVL
SQ  TSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLQHPSVKDDSDL
SQ  EGRTSFMWAAGKGNDDVLRTMLSLKSDIDINMSDKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEM
SQ  GHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNA
SQ  DPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF
SQ  KIQAVYKGYKVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGQLDTDPPRSHCSSSAPVLPCPPSPQNEGS
SQ  KQDATPSKQPPASHTVQSPDPEHSRLPGRCPGRASQGDSSIDLQGTASRKPSETPIEHCRGPSACVHPRSWEGGNSSKNQ
SQ  GTSSVEKRRGETNGKHRRCEEGPSSARQPLCTGSGRPAEKGEDSSPAVASASQQDHPRKPNKRQDRAARPRGASQKRRTH
SQ  QLRDRCSPAGSSRPGSAKGEVACADQSSLHRHTPRSKVTQDKLIGGVSSGLPLSTEASRSGCKQLYEDICASPETGVAHG
SQ  PPPGQCMNIHLLPVEQRLLIIQRERSRKELFRRKNKAAAVIQRAWRSYQLRKHLSRLLHLKQLGAREVLRCTQVCTALLL
SQ  QVWRKELELKFPKSISVSRTSKSPSKGSSATKYARHSVLRQIYGCSQEGKGHHPIKSSKAPAVLHLSSVNSLQSIHLDNS
SQ  GRSKKFSYNLQPSSQSKNKPKL
//
ID  P13285;
PN  Latent membrane protein 2;
GN  LMP2;
OS  10377;
SL  Nucleus Position: SL-0382;
SL  Comments: [Isoform LMP2A]: Host cell membrane {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000269|PubMed:11163230}. [Isoform LMP2B]: Host endomembrane system {ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11961256}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11961256}. Note=Isoform LMP2B localizes to perinuclear regions. {ECO:0000269|PubMed:11961256}.
DR  UNIPROT: P13285;
DR  UNIPROT: Q777H4;
DR  UNIPROT: Q8AZK9;
DR  PDB: 1UXS;
DR  PDB: 1UXW;
DR  PDB: 2JO9;
DR  PDB: 3BVN;
DR  PDB: 3REW;
DR  PDB: 5GRD;
DR  PDB: 5GSD;
DR  Pfam: PF07415;
DE  Function: Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs. Isoform LMP2B may be a negative regulator of isoform LMP2A.
DE  Reference Proteome: Yes;
GO  GO:0033645;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0039649;
GO  GO:0019042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQ
SQ  DQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALS
SQ  LLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWR
SQ  RLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLN
SQ  LTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIV
SQ  AGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYC
SQ  LTLESEERPPTPYRNTV
//
ID  Q9LU93;
PN  Mitotic spindle checkpoint protein MAD2;
GN  MAD2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19710914, ECO:0000269|PubMed:22457071}. Nucleus envelope {ECO:0000269|PubMed:22457071}. Chromosome {ECO:0000269|PubMed:19710914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19710914}. Cytoplasm {ECO:0000269|PubMed:19710914, ECO:0000269|PubMed:22457071}. Note=Cytoplasmic in interphase cells. Accumulates onto both kinetochores and the spindle microtubules in cell arrested in metaphase. Present in chromocenters. Associates with unattached kinetochores upon spindle assembly checkpoint (SAC) activation. The nucleus envelope association requires the presence of NUA. {ECO:0000269|PubMed:22457071}.
DR  UNIPROT: Q9LU93;
DR  UNIPROT: Q67YV5;
DR  Pfam: PF02301;
DR  PROSITE: PS50815;
DE  Function: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:19710914}.
DE  Reference Proteome: Yes;
DE  Interaction: P92960; IntAct: EBI-2131524,EBI-974388; Score: 0.40
DE  Interaction: O82782; IntAct: EBI-2131524,EBI-2131520; Score: 0.40
DE  Interaction: Q940Y8; IntAct: EBI-2131524,EBI-2131509; Score: 0.40
DE  Interaction: Q9FIQ0; IntAct: EBI-2131524,EBI-2131528; Score: 0.40
DE  Interaction: Q9SIH1; IntAct: EBI-2131524,EBI-2131488; Score: 0.40
DE  Interaction: Q9ZVX3; IntAct: EBI-2131524,EBI-2131498; Score: 0.40
DE  Interaction: Q9FLL1; IntAct: EBI-2131524,EBI-2131516; Score: 0.40
DE  Interaction: Q8GXK3; IntAct: EBI-2131524,EBI-2131484; Score: 0.40
DE  Interaction: Q9M0I4; IntAct: EBI-2131524,EBI-2131481; Score: 0.40
DE  Interaction: Q9ZVJ4; IntAct: EBI-2131524,EBI-2131494; Score: 0.40
DE  Interaction: Q9SZP8; IntAct: EBI-2131524,EBI-2131501; Score: 0.40
DE  Interaction: Q9LW88; IntAct: EBI-2131524,EBI-2131512; Score: 0.40
DE  Interaction: Q9SN19; IntAct: EBI-2131524,EBI-2131505; Score: 0.40
DE  Interaction: Q6NLH0; IntAct: EBI-2131524,EBI-2130783; Score: 0.40
DE  Interaction: Q8LPJ4; IntAct: EBI-2131524,EBI-2130725; Score: 0.35
DE  Interaction: O48802; IntAct: EBI-2131524,EBI-3387496; Score: 0.35
DE  Interaction: Q9M0Z6; IntAct: EBI-2131524,EBI-3387490; Score: 0.35
DE  Interaction: Q8GYU3; IntAct: EBI-2131524,EBI-3387484; Score: 0.35
DE  Interaction: Q9FT72; IntAct: EBI-2131524,EBI-3387478; Score: 0.35
DE  Interaction: Q9SF16; IntAct: EBI-2131524,EBI-2130815; Score: 0.35
DE  Interaction: O64768; IntAct: EBI-2131524,EBI-3387499; Score: 0.35
DE  Interaction: Q9C5C8; IntAct: EBI-2131524,EBI-3387493; Score: 0.35
DE  Interaction: Q9SB63; IntAct: EBI-2131524,EBI-3387487; Score: 0.35
DE  Interaction: Q93VP3; IntAct: EBI-2131524,EBI-3387481; Score: 0.35
DE  Interaction: Q93ZX4; IntAct: EBI-2131524,EBI-3387381; Score: 0.35
DE  Interaction: Q9C774; IntAct: EBI-2131524,EBI-2130645; Score: 0.35
GO  GO:0010369;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005876;
GO  GO:0051301;
GO  GO:0007094;
GO  GO:0007346;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASKTAAAKDIITLHGSAAIVSEFFCYAANSILYNRAVYPEESFVKVKKYGLPMLLIEDESVKSFMSNLTSQISEWLEAG
SQ  KLQRVVLVIMSKATGEVLERWNFRIETDNEVVDKGVSREKSDKEIMREIQAIMRQVASSVTYLPCLDETCVFDVLAYTDT
SQ  DVAVPFTWIESDPKLIANPQMVKLHGFDTKIHKVDTLVSYKNDEWDEEE
//
ID  P34609;
PN  JNK-interacting protein;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026}. Note=Diffusely localized throughout cell body but intensely localized in regions adjacent to nucleus and at presumptive tips of neural processes.
DR  UNIPROT: P34609;
DR  UNIPROT: A7LPE3;
DR  UNIPROT: A7LPE4;
DR  UNIPROT: C0P271;
DR  UNIPROT: C7FZT6;
DR  UNIPROT: Q95V72;
DR  UNIPROT: S6EZN6;
DR  UNIPROT: S6EZP3;
DR  UNIPROT: S6F548;
DR  UNIPROT: S6F556;
DR  UNIPROT: S6FD02;
DR  UNIPROT: S6FN04;
DR  UNIPROT: S6FN08;
DR  UNIPROT: S6FWP4;
DR  UNIPROT: S6FWP6;
DR  UNIPROT: U4MKU8;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of synaptic vesicle transport, through interactions with the JNK-signaling components and motor proteins. Binds specific components of the JNK signaling pathway namely jnk-1, jkk-1 and sek-1. Associates with components of the motor protein, kinesin-1. Pre-assembled unc-16 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Regulates the retrograde transport of autophagosomes from the neurites to the cell body of AIY interneurons (PubMed:30880001). {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026, ECO:0000269|PubMed:30880001}.
DE  Reference Proteome: Yes;
DE  Interaction: P46822; IntAct: EBI-315684,EBI-315578; Score: 0.62
DE  Interaction: H2L0F6; IntAct: EBI-315684,EBI-329192; Score: 0.37
DE  Interaction: P34686; IntAct: EBI-332095,EBI-315684; Score: 0.37
DE  Interaction: Q93345; IntAct: EBI-322409,EBI-315684; Score: 0.37
DE  Interaction: Q18668; IntAct: EBI-317396,EBI-315684; Score: 0.37
DE  Interaction: Q5WRT0; IntAct: EBI-315684,EBI-322655; Score: 0.37
GO  GO:0030424;
GO  GO:0043194;
GO  GO:0043679;
GO  GO:0005623;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0008432;
GO  GO:0019900;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0030159;
GO  GO:0007257;
GO  GO:0030421;
GO  GO:0040011;
GO  GO:0018991;
GO  GO:0046328;
GO  GO:0048489;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACNLSPVNEMADSITSSTPSEIVYGGPGSPDEHRTMSDKVQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDL
SQ  AYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHAS
SQ  RLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTKYLMGSEKFELMQNMPLPNMQLRNKMGMAASVDASSIRGVSDLISA
SQ  HMTQSTTMDVNLANHITNEDWQDEFSSDIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQSEEEEADETTSVDPKE
SQ  NNDLLGADLTDDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSLGMGREVENLIKENSELLDMKNALNIVKNDLINQVDEL
SQ  NSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLME
SQ  LEESIKWTEMQRAKKMQQQQQNVNQKKSGGIWEFFSSLLGDSVTPPASSRGNRASSSRGKMTRSVEYIDPDMISERRAAE
SQ  RREQYKLVREHVKKEDGRIEAYGWSLPNVEAEVSSVPIPVCCRPLLDNEPSLKIWCATGVVLRGGRDERGQWIVGDPIYF
SQ  APASMKKTKTSNHRPELEDEIKRARNLDARESELDEWQSSSLVWVVSSNQGKSLIAVLDANNPNNIIETFPACDSHLLCI
SQ  QAVSGVMEGEPEMNEEQSKKYLSGGGKIKDLPEGLDGTDLGACEWVELRKMEDSEDGVPTYCSNDMKPSPKRTRDFSISE
SQ  VAPVDSSAPVKEDPLPPPANRPGGRAALPPHIRDAMSKYDGVSGQMSGALPTVWMGGQNQYIYIHSAVTAWKQCLRRIKM
SQ  PDAVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSATSSVRSLCLVSTNIWATYKNCVVVLDAESLQIV
SQ  KVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVDIEPYVTKMLGTSKLDFSYMRTTALLVSNRRLW
SQ  IGTGTGVIISVPFSGQLEKKIETKDSKRPAGPGGLVRVYGATSENATNDEKTNDDFIPYCNLAHAQLSFHGHKDSVKFFL
SQ  GVPGASKNGEDESAEVTLRRMLIMSGGDGYIDFRIGEENEPELTGQSIRPRDMSHLIIWEVDAELPILSK
//
ID  Q14643;
PN  Inositol 1,4,5-trisphosphate receptor type 1;
GN  ITPR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305|PubMed:27108798}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27108798}. Note=Endoplasmic reticulum and secretory granules (By similarity). {ECO:0000250|UniProtKB:Q9TU34}.
DR  UNIPROT: Q14643;
DR  UNIPROT: E7EPX7;
DR  UNIPROT: E9PDE9;
DR  UNIPROT: Q14660;
DR  UNIPROT: Q99897;
DR  Pfam: PF08709;
DR  Pfam: PF00520;
DR  Pfam: PF02815;
DR  Pfam: PF08454;
DR  Pfam: PF01365;
DR  PROSITE: PS50919;
DR  OMIM: 117360;
DR  OMIM: 147265;
DR  OMIM: 206700;
DR  OMIM: 606658;
DR  DisGeNET: 3708;
DE  Function: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate (PubMed:27108797). Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:27108797}.
DE  Disease: Spinocerebellar ataxia 15 (SCA15) [MIM:606658]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA15 is an autosomal dominant cerebellar ataxia (ADCA). It is very slow progressing form with a wide range of onset, ranging from childhood to adult. Most patients remain ambulatory. {ECO:0000269|PubMed:17590087, ECO:0000269|PubMed:18579805}. Note=The disease is caused by mutations affecting the gene represented in this entry. Spinocerebellar ataxia 29 (SCA29) [MIM:117360]: An autosomal dominant, congenital spinocerebellar ataxia characterized by early motor delay, hypotonia and mild cognitive delay. Affected individuals develop a very slowly progressive or non-progressive gait and limb ataxia associated with cerebellar atrophy on brain imaging. Additional variable features include nystagmus, dysarthria, and tremor. {ECO:0000269|PubMed:22986007, ECO:0000269|PubMed:26770814}. Note=The disease is caused by mutations affecting the gene represented in this entry. Gillespie syndrome (GLSP) [MIM:206700]: A rare disease characterized by bilateral iris hypoplasia, congenital hypotonia, non- progressive ataxia, progressive cerebellar atrophy, and mental retardation. {ECO:0000269|PubMed:27108797, ECO:0000269|PubMed:27108798}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-465548,EBI-641062; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-465548,EBI-529989; Score: 0.37
DE  Interaction: Q14108; IntAct: EBI-1564650,EBI-465548; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-2800296,EBI-465548; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-354932,EBI-465548; Score: 0.46
DE  Interaction: P31749; IntAct: EBI-296087,EBI-465548; Score: 0.59
DE  Interaction: P30405; IntAct: EBI-465548,EBI-5544229; Score: 0.40
DE  Interaction: Q81T40; IntAct: EBI-465548,EBI-2816570; Score: 0.37
DE  Interaction: Q15149; IntAct: EBI-297903,EBI-465548; Score: 0.40
DE  Interaction: Q9BS26; IntAct: EBI-465548,EBI-541644; Score: 0.40
DE  Interaction: Q9Y3M8; IntAct: EBI-465548,EBI-465487; Score: 0.37
GO  GO:0005955;
GO  GO:0005623;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031088;
GO  GO:0031094;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0016529;
GO  GO:0098685;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0019855;
GO  GO:0005509;
GO  GO:0015085;
GO  GO:0015278;
GO  GO:0070679;
GO  GO:0098695;
GO  GO:0005220;
GO  GO:0035091;
GO  GO:0006816;
GO  GO:0032469;
GO  GO:0042045;
GO  GO:0070059;
GO  GO:0050849;
GO  GO:0030168;
GO  GO:0009791;
GO  GO:0010506;
GO  GO:1903779;
GO  GO:0050796;
GO  GO:0051209;
GO  GO:0001666;
GO  GO:0007165;
GO  GO:0050882;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGA
SQ  NSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSW
SQ  FYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
SQ  RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP
SQ  DFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVH
SQ  STNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
SQ  VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVL
SQ  RHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVS
SQ  MNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDA
SQ  KEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVT
SQ  PVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFY
SQ  NFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAA
SQ  PEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDF
SQ  EHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVD
SQ  NYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQE
SQ  SASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEA
SQ  VTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRAS
SQ  FQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCY
SQ  VDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQ
SQ  LLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVL
SQ  AASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKL
SQ  CIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSG
SQ  RRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALL
SQ  EGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEV
SQ  RDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQN
SQ  NKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILN
SQ  DINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNV
SQ  GHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTE
SQ  RDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGL
SQ  LWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEF
SQ  LYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVD
SQ  RLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDV
SQ  LRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHI
SQ  KEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNL
SQ  SGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
//
ID  O60583;
PN  Cyclin-T2;
GN  CCNT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}. Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}.
DR  UNIPROT: O60583;
DR  UNIPROT: A8KA48;
DR  UNIPROT: D3DP73;
DR  UNIPROT: D3DP74;
DR  UNIPROT: O60582;
DR  UNIPROT: Q29R66;
DR  UNIPROT: Q53SR4;
DR  UNIPROT: Q5I1Y0;
DR  PDB: 2IVX;
DR  Pfam: PF00134;
DR  OMIM: 603862;
DR  DisGeNET: 905;
DE  Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy- terminal domain) of the large subunit of RNA polymerase II (RNAP II) (PubMed:9499409, PubMed:15563843). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity). {ECO:0000250|UniProtKB:Q7TQK0, ECO:0000269|PubMed:11713533, ECO:0000269|PubMed:15563843, ECO:0000269|PubMed:16331689, ECO:0000269|PubMed:9499409}. (Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters. {ECO:0000269|PubMed:21509660}.
DE  Reference Proteome: Yes;
DE  Interaction: Q16659; IntAct: EBI-1384105,EBI-2836757; Score: 0.35
DE  Interaction: A3KMF4; IntAct: EBI-11085928,EBI-2836757; Score: 0.35
DE  Interaction: Q9ERL0; IntAct: EBI-11086057,EBI-2836757; Score: 0.35
DE  Interaction: O95402; IntAct: EBI-394392,EBI-2836757; Score: 0.35
DE  Interaction: Q9UHB7; IntAct: EBI-395282,EBI-2836757; Score: 0.35
DE  Interaction: O00472; IntAct: EBI-395274,EBI-2836757; Score: 0.35
DE  Interaction: P42568; IntAct: EBI-716132,EBI-2836757; Score: 0.35
DE  Interaction: P50750; IntAct: EBI-1383449,EBI-2836757; Score: 0.64
DE  Interaction: A0A3Q0PRD7; IntAct: EBI-2810412,EBI-2836757; Score: 0.37
DE  Interaction: Q12802-1; IntAct: EBI-25409719,EBI-2836757; Score: 0.35
DE  Interaction: Q07139-1; IntAct: EBI-25410958,EBI-2836757; Score: 0.35
GO  GO:0008024;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097322;
GO  GO:0003682;
GO  GO:0061575;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0070063;
GO  GO:0001223;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0019085;
GO  GO:0019086;
GO  GO:0032786;
GO  GO:0045944;
GO  GO:0000079;
GO  GO:0051147;
GO  GO:0006357;
GO  GO:0007519;
GO  GO:0042795;
GO  GO:0006366;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKN
SQ  IISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCT
SQ  QLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEF
SQ  LQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNI
SQ  SVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKI
SQ  SDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTS
SQ  PIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKH
SQ  KEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKS
SQ  SGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLD
SQ  SLLSAQGMNM
//
ID  P04406;
PN  Glyceraldehyde-3-phosphate dehydrogenase;
GN  GAPDH;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions. {ECO:0000250}.
DR  UNIPROT: P04406;
DR  UNIPROT: E7EUT4;
DR  UNIPROT: P00354;
DR  UNIPROT: Q53X65;
DR  PDB: 1U8F;
DR  PDB: 1ZNQ;
DR  PDB: 2FEH;
DR  PDB: 3GPD;
DR  PDB: 4WNC;
DR  PDB: 4WNI;
DR  PDB: 6ADE;
DR  PDB: 6IQ6;
DR  Pfam: PF02800;
DR  Pfam: PF00044;
DR  PROSITE: PS00071;
DR  OMIM: 138400;
DR  DisGeNET: 2597;
DE  Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3- phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon- activated inhibitor of translation) complex which mediates interferon- gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000250, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:3170585}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-354056,EBI-297353; Score: 0.79
DE  Interaction: Self; IntAct: EBI-354056,EBI-354056; Score: 0.59
DE  Interaction: P28482; IntAct: EBI-959949,EBI-354056; Score: 0.37
DE  Interaction: P32121; IntAct: EBI-714559,EBI-354056; Score: 0.35
DE  Interaction: P42771; IntAct: EBI-375053,EBI-354056; Score: 0.35
DE  Interaction: O15264; IntAct: EBI-2116951,EBI-354056; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-354056; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-354056,EBI-990792; Score: 0.50
DE  Interaction: P04075; IntAct: EBI-709613,EBI-354056; Score: 0.35
DE  Interaction: P02730; IntAct: EBI-7576138,EBI-354056; Score: 0.37
DE  Interaction: P04920; IntAct: EBI-1390787,EBI-354056; Score: 0.40
DE  Interaction: P02730-2; IntAct: EBI-20795597,EBI-354056; Score: 0.40
DE  Interaction: P13569; IntAct: EBI-349854,EBI-354056; Score: 0.35
DE  Interaction: P48147; IntAct: EBI-1049962,EBI-354056; Score: 0.65
DE  Interaction: Q13043; IntAct: EBI-367376,EBI-354056; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-354056,EBI-466029; Score: 0.37
DE  Interaction: Q15303; IntAct: EBI-80371,EBI-354056; Score: 0.37
DE  Interaction: P04626; IntAct: EBI-641062,EBI-354056; Score: 0.55
DE  Interaction: Q60823; IntAct: EBI-400263,EBI-354056; Score: 0.50
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-354056; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-354056,EBI-297277; Score: 0.37
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-354056; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-712001,EBI-354056; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-354056; Score: 0.35
DE  Interaction: Q3KSU8; IntAct: EBI-354056,EBI-2621128; Score: 0.37
DE  Interaction: Q06187; IntAct: EBI-624835,EBI-354056; Score: 0.35
DE  Interaction: P43351; IntAct: EBI-706448,EBI-354056; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-354056; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-354056; Score: 0.35
DE  Interaction: P35228; IntAct: EBI-6662224,EBI-354056; Score: 0.50
DE  Interaction: P05109; IntAct: EBI-354056,EBI-355281; Score: 0.65
DE  Interaction: P06702; IntAct: EBI-354056,EBI-1055001; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-354056,EBI-358549; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-354056,EBI-302023; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-2551936,EBI-354056; Score: 0.35
DE  Interaction: O35071; IntAct: EBI-2366194,EBI-354056; Score: 0.35
DE  Interaction: P51451; IntAct: EBI-2105445,EBI-354056; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-354056; Score: 0.35
DE  Interaction: Q8N2N9-3; IntAct: EBI-354056,EBI-11053866; Score: 0.35
DE  Interaction: Q96G25; IntAct: EBI-354056,EBI-394405; Score: 0.35
DE  Interaction: Q8NG31-2; IntAct: EBI-354056,EBI-10973816; Score: 0.35
DE  Interaction: Q96FC7; IntAct: EBI-748888,EBI-354056; Score: 0.35
DE  Interaction: Q9H6K4; IntAct: EBI-8477908,EBI-354056; Score: 0.35
DE  Interaction: Q9Y2Z9; IntAct: EBI-718148,EBI-354056; Score: 0.35
DE  Interaction: Q99807; IntAct: EBI-11017131,EBI-354056; Score: 0.35
DE  Interaction: O75489; IntAct: EBI-1224896,EBI-354056; Score: 0.35
DE  Interaction: Q8TB22; IntAct: EBI-372221,EBI-354056; Score: 0.35
DE  Interaction: Q9NQH7; IntAct: EBI-1171467,EBI-354056; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-351437,EBI-354056; Score: 0.35
DE  Interaction: Q9C002; IntAct: EBI-3905285,EBI-354056; Score: 0.35
DE  Interaction: Q9HAC7; IntAct: EBI-21929540,EBI-354056; Score: 0.35
DE  Interaction: Q96HJ9; IntAct: EBI-16769656,EBI-354056; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-1049381,EBI-354056; Score: 0.35
DE  Interaction: O00746; IntAct: EBI-744871,EBI-354056; Score: 0.35
DE  Interaction: Q8N3Z0; IntAct: EBI-20628340,EBI-354056; Score: 0.35
DE  Interaction: Q3MIX3; IntAct: EBI-3923548,EBI-354056; Score: 0.35
DE  Interaction: P0C7P0; IntAct: EBI-11150788,EBI-354056; Score: 0.35
DE  Interaction: Q15051; IntAct: EBI-2805823,EBI-354056; Score: 0.35
DE  Interaction: P15336; IntAct: EBI-1170906,EBI-354056; Score: 0.35
DE  Interaction: P18084; IntAct: EBI-354056,EBI-1223434; Score: 0.37
DE  Interaction: P04487; IntAct: EBI-6150681,EBI-354056; Score: 0.35
DE  Interaction: P0C1C6; IntAct: EBI-6151657,EBI-354056; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-2547442,EBI-354056; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189824,EBI-354056; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-354056; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-456067,EBI-354056; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-716247,EBI-354056; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-486838,EBI-354056; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-359390,EBI-354056; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-354056; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-354056; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-354056; Score: 0.35
DE  Interaction: O00141; IntAct: EBI-354056,EBI-1042854; Score: 0.40
DE  Interaction: Q9H0J4; IntAct: EBI-1053637,EBI-354056; Score: 0.40
DE  Interaction: P10599; IntAct: EBI-354056,EBI-594644; Score: 0.40
DE  Interaction: O60739; IntAct: EBI-354056,EBI-1043343; Score: 0.40
DE  Interaction: O95292; IntAct: EBI-1188298,EBI-354056; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-741297,EBI-354056; Score: 0.35
DE  Interaction: O75602; IntAct: EBI-354056,EBI-20850469; Score: 0.40
DE  Interaction: O95425; IntAct: EBI-354056,EBI-487145; Score: 0.40
DE  Interaction: Q5VST9-6; IntAct: EBI-354056,EBI-10989451; Score: 0.40
DE  Interaction: Q502W7; IntAct: EBI-354056,EBI-20845787; Score: 0.40
DE  Interaction: P48751; IntAct: EBI-354056,EBI-20805570; Score: 0.40
DE  Interaction: Q00535; IntAct: EBI-354056,EBI-1041567; Score: 0.40
DE  Interaction: A1A4G5; IntAct: EBI-354056,EBI-12104738; Score: 0.40
DE  Interaction: Q5TZA2; IntAct: EBI-354056,EBI-3923672; Score: 0.40
DE  Interaction: P57740; IntAct: EBI-354056,EBI-295687; Score: 0.40
DE  Interaction: Q99442; IntAct: EBI-354056,EBI-949221; Score: 0.40
DE  Interaction: Q8NFJ5; IntAct: EBI-354056,EBI-2561555; Score: 0.40
DE  Interaction: Q6A163; IntAct: EBI-354056,EBI-11958242; Score: 0.40
DE  Interaction: O76041; IntAct: EBI-354056,EBI-2880203; Score: 0.40
DE  Interaction: Q69YH5; IntAct: EBI-354056,EBI-6911908; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-1047359,EBI-354056; Score: 0.40
DE  Interaction: Q63HK5; IntAct: EBI-354056,EBI-9053916; Score: 0.40
DE  Interaction: Q5T6S3; IntAct: EBI-354056,EBI-2339674; Score: 0.40
DE  Interaction: Q6P1J9; IntAct: EBI-354056,EBI-930143; Score: 0.40
DE  Interaction: O95139; IntAct: EBI-354056,EBI-1053340; Score: 0.40
DE  Interaction: O15015; IntAct: EBI-354056,EBI-745608; Score: 0.40
DE  Interaction: A8MT65; IntAct: EBI-354056,EBI-20869384; Score: 0.40
DE  Interaction: Q03936; IntAct: EBI-354056,EBI-12176441; Score: 0.40
DE  Interaction: P04908; IntAct: EBI-354056,EBI-358971; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475880,EBI-354056; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25475894,EBI-354056; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25475917,EBI-354056; Score: 0.35
DE  Interaction: Q9UBX2; IntAct: EBI-11600078,EBI-354056; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-1188238,EBI-354056; Score: 0.37
DE  Interaction: Q00537; IntAct: EBI-624648,EBI-354056; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-1213983,EBI-354056; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-354056; Score: 0.35
DE  Interaction: Q92696; IntAct: EBI-9104196,EBI-354056; Score: 0.35
DE  Interaction: Q9BZE9-2; IntAct: EBI-354056,EBI-21554613; Score: 0.35
DE  Interaction: O14556; IntAct: EBI-354056,EBI-1057431; Score: 0.35
DE  Interaction: Q15915; IntAct: EBI-11963196,EBI-354056; Score: 0.35
DE  Interaction: P15927; IntAct: EBI-621404,EBI-354056; Score: 0.51
DE  Interaction: Q9NXU5; IntAct: EBI-354056,EBI-711759; Score: 0.37
DE  Interaction: Q9BX70; IntAct: EBI-354056,EBI-710091; Score: 0.37
DE  Interaction: Q16363; IntAct: EBI-354056,EBI-711505; Score: 0.37
DE  Interaction: Q15102; IntAct: EBI-354056,EBI-711522; Score: 0.37
DE  Interaction: Q9UN74; IntAct: EBI-354056,EBI-712273; Score: 0.37
DE  Interaction: O00231; IntAct: EBI-354056,EBI-357816; Score: 0.37
DE  Interaction: P50453; IntAct: EBI-354056,EBI-711626; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-354056,EBI-712550; Score: 0.55
DE  Interaction: O43504; IntAct: EBI-354056,EBI-713382; Score: 0.37
DE  Interaction: Q06830; IntAct: EBI-354056,EBI-353193; Score: 0.37
DE  Interaction: Q99558; IntAct: EBI-354056,EBI-358011; Score: 0.40
DE  Interaction: O43353; IntAct: EBI-354056,EBI-358522; Score: 0.40
DE  Interaction: Q9UHD2; IntAct: EBI-354056,EBI-356402; Score: 0.56
DE  Interaction: P20333; IntAct: EBI-354056,EBI-358983; Score: 0.40
DE  Interaction: Q99759; IntAct: EBI-354056,EBI-307281; Score: 0.40
DE  Interaction: Q13077; IntAct: EBI-354056,EBI-359224; Score: 0.40
DE  Interaction: P60709; IntAct: EBI-353944,EBI-354056; Score: 0.40
DE  Interaction: Q13268; IntAct: EBI-354324,EBI-354056; Score: 0.40
DE  Interaction: Q04864; IntAct: EBI-354056,EBI-307352; Score: 0.40
DE  Interaction: Q92993; IntAct: EBI-399080,EBI-354056; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0097452;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:1990904;
GO  GO:0031982;
GO  GO:0019828;
GO  GO:0097718;
GO  GO:0004365;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051287;
GO  GO:0050661;
GO  GO:0035605;
GO  GO:0061844;
GO  GO:0061621;
GO  GO:0071346;
GO  GO:0050832;
GO  GO:0006094;
GO  GO:0006096;
GO  GO:0051873;
GO  GO:0031640;
GO  GO:0000226;
GO  GO:0010951;
GO  GO:0017148;
GO  GO:0051402;
GO  GO:0035606;
GO  GO:0052501;
GO  GO:0050715;
GO  GO:0050821;
GO  GO:0016241;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQER
SQ  DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL
SQ  AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SQ  SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY
SQ  SNRVVDLMAHMASKE
//
ID  Q80WJ1;
PN  Gametogenetin;
GN  Ggn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm, perinuclear region. Note=Localizes along the nuclear membrane. [Isoform 2]: Cytoplasmic vesicle. [Isoform 3]: Nucleus, nucleolus.
DR  UNIPROT: Q80WJ1;
DR  UNIPROT: Q5EBP4;
DR  UNIPROT: Q80WI9;
DR  UNIPROT: Q80WJ0;
DR  Pfam: PF15685;
DE  Function: May be involved in spermatogenesis. {ECO:0000269|PubMed:12574169}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0031625;
GO  GO:0030154;
GO  GO:0006302;
GO  GO:0007566;
GO  GO:0007276;
GO  GO:0008104;
GO  GO:0065003;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNVQSEPSAGGGSRKEQASDRASDSRRTPLVEPEVTPSSPAMRLARGLGVWFPGSSGPPGLLIPPEPQASSSPLPLTLE
SQ  LPSPVTPPPEEAAAVSTPPPPPVGTLLPAPSKWRKPTGTSVPRIRGLLEASHRGQGDPPSLRPLPPLPRQLTEKDPVLRA
SQ  PAPPPTPLEPRKQLPPAPSTCDPQPLSRRITLASSATSPTESQVRHSSEGQAAGGAHGGVPPQAGEGEMARSATSESGLS
SQ  LLCKVTFKSGPHLSPTSASGPLAAKASPGAGGGGLFASSGAISYAEVLKQGPQPPGATRPLGEVPPGATRPLGEVPRAAQ
SQ  ETEGGDGDGEGCSGPPSVPAPLARALPPPPYTTFPGSKPKFDWVSPPDGTERHFRFNGAVGGIGAPRRRTTTLSGPWGSP
SQ  PPRSGQTHPSSGPRRPTPALLAPPMFIFPAPNNGEPVRPVPPSPQQIPPLPPPPPTPPATPPPAPPPTPQPPALPRTPIL
SQ  VARPPTPGPGHLESALAPTPPSTLSPTAAADQVPAATPATVTSQVPATATAELSPPMPQPKTRTRRNKGPRAARGVIREE
SQ  GTSGDGPREPNTAPVTDSSSGGGGGGSNGTSTAGASNKGTARHWPPFEVLNSCPCKCYCRHQRRHRRLPRNVSAWLSTPT
SQ  NHLSEPPWVATVKLAGSLVAGLEHYDLQATHST
//
ID  Q15811;
PN  Intersectin-1;
GN  ITSN1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:11744688}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q9WVE9}. Cell projection, lamellipodium {ECO:0000269|PubMed:11744688}. Cell membrane {ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:20946875}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:20946875, ECO:0000269|PubMed:29887380}. Recycling endosome {ECO:0000269|PubMed:29030480}. Endosome {ECO:0000250|UniProtKB:Q9Z0R4}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Z0R4}. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits (PubMed:20946875). Colocalizes with RAB13 on cytoplasmic vesicles that are most likely recycling endosomes (PubMed:29030480). {ECO:0000269|PubMed:20946875, ECO:0000269|PubMed:29030480}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:29599122}. Endomembrane system {ECO:0000269|PubMed:21712076}. Nucleus envelope {ECO:0000269|PubMed:29599122}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000269|PubMed:29599122}. [Isoform 5]: Endomembrane system {ECO:0000269|PubMed:21712076}.
DR  UNIPROT: Q15811;
DR  UNIPROT: A7Y322;
DR  UNIPROT: A8CTX8;
DR  UNIPROT: A8CTY3;
DR  UNIPROT: A8CTY7;
DR  UNIPROT: A8D7D0;
DR  UNIPROT: A8DCP3;
DR  UNIPROT: B4DTM2;
DR  UNIPROT: E7ERJ1;
DR  UNIPROT: E9PE44;
DR  UNIPROT: E9PG01;
DR  UNIPROT: E9PHV2;
DR  UNIPROT: O95216;
DR  UNIPROT: Q0PW94;
DR  UNIPROT: Q0PW95;
DR  UNIPROT: Q0PW97;
DR  UNIPROT: Q14BD3;
DR  UNIPROT: Q1ED40;
DR  UNIPROT: Q20BK3;
DR  UNIPROT: Q9UET5;
DR  UNIPROT: Q9UK60;
DR  UNIPROT: Q9UNK1;
DR  UNIPROT: Q9UNK2;
DR  UNIPROT: Q9UQ92;
DR  PDB: 1KI1;
DR  PDB: 2KGR;
DR  PDB: 2KHN;
DR  PDB: 3FIA;
DR  PDB: 3QBV;
DR  PDB: 4IIM;
DR  PDB: 5HZI;
DR  PDB: 5HZJ;
DR  PDB: 5HZK;
DR  PDB: 6GBU;
DR  PDB: 6H5T;
DR  Pfam: PF00168;
DR  Pfam: PF12763;
DR  Pfam: PF16652;
DR  Pfam: PF00621;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  PROSITE: PS50004;
DR  PROSITE: PS00741;
DR  PROSITE: PS50010;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS50031;
DR  PROSITE: PS50003;
DR  PROSITE: PS50002;
DR  OMIM: 602442;
DR  DisGeNET: 6453;
DE  Function: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (PubMed:22648170). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (By similarity). Inhibits ARHGAP31 activity toward RAC1 (PubMed:11744688). {ECO:0000250|UniProtKB:Q9WVE9, ECO:0000250|UniProtKB:Q9Z0R4, ECO:0000269|PubMed:11584276, ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:29887380}. [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250|UniProtKB:Q9Z0R4}.
DE  Reference Proteome: Yes;
DE  Interaction: P35658; IntAct: EBI-602041,EBI-1222270; Score: 0.35
DE  Interaction: Q12840; IntAct: EBI-713468,EBI-602041; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-529989,EBI-602041; Score: 0.55
DE  Interaction: Q6NSK7; IntAct: EBI-602041,EBI-21369851; Score: 0.37
DE  Interaction: O43175; IntAct: EBI-350495,EBI-602041; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-432924,EBI-602041; Score: 0.37
DE  Interaction: O43150; IntAct: EBI-602041,EBI-310968; Score: 0.37
DE  Interaction: P22681; IntAct: EBI-518228,EBI-602041; Score: 0.73
DE  Interaction: Q6ZUJ8; IntAct: EBI-2654168,EBI-602041; Score: 0.37
DE  Interaction: Q15427; IntAct: EBI-348469,EBI-602041; Score: 0.37
DE  Interaction: P22674; IntAct: EBI-2556878,EBI-602041; Score: 0.37
DE  Interaction: Q99471; IntAct: EBI-602041,EBI-357275; Score: 0.37
DE  Interaction: Q9Y2W2; IntAct: EBI-714455,EBI-602041; Score: 0.37
DE  Interaction: Q07889; IntAct: EBI-297487,EBI-602041; Score: 0.64
DE  Interaction: Q92734; IntAct: EBI-357061,EBI-602041; Score: 0.35
DE  Interaction: Q9NS91; IntAct: EBI-2339393,EBI-602041; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-1056902,EBI-602041; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-602041; Score: 0.35
DE  Interaction: A0A1Q4LW06; IntAct: EBI-602041,EBI-2815425; Score: 0.37
DE  Interaction: O75940; IntAct: EBI-602041,EBI-1052641; Score: 0.40
DE  Interaction: Q8TAQ2; IntAct: EBI-357418,EBI-602041; Score: 0.37
DE  Interaction: Q15599; IntAct: EBI-602041,EBI-1149760; Score: 0.35
DE  Interaction: P22307; IntAct: EBI-602041,EBI-1050999; Score: 0.35
DE  Interaction: O95757; IntAct: EBI-602041,EBI-358652; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-602041,EBI-358398; Score: 0.35
DE  Interaction: Q9UBC2; IntAct: EBI-602041,EBI-2556746; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-602041,EBI-396684; Score: 0.56
DE  Interaction: Q13011; IntAct: EBI-602041,EBI-711968; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-602041,EBI-1171169; Score: 0.35
DE  Interaction: Q969X6; IntAct: EBI-602041,EBI-2602591; Score: 0.35
DE  Interaction: P04040; IntAct: EBI-602041,EBI-2432181; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-602041,EBI-297683; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-602041,EBI-1642835; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-602041,EBI-353552; Score: 0.35
DE  Interaction: Q07889-1; IntAct: EBI-25408451,EBI-602041; Score: 0.35
DE  Interaction: P60953-1; IntAct: EBI-602041,EBI-3625591; Score: 0.54
DE  Interaction: P68104; IntAct: EBI-352162,EBI-602041; Score: 0.37
DE  Interaction: Q13432; IntAct: EBI-711260,EBI-602041; Score: 0.37
DE  Interaction: Q9BYC9; IntAct: EBI-714361,EBI-602041; Score: 0.37
DE  Interaction: Q9Y5X3; IntAct: EBI-715760,EBI-602041; Score: 0.37
GO  GO:0097440;
GO  GO:0044305;
GO  GO:0030054;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0030139;
GO  GO:0098978;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0098871;
GO  GO:0098833;
GO  GO:0055037;
GO  GO:0005509;
GO  GO:0005085;
GO  GO:0019209;
GO  GO:0060090;
GO  GO:0070064;
GO  GO:0007420;
GO  GO:0034613;
GO  GO:0048013;
GO  GO:0006887;
GO  GO:0007186;
GO  GO:0061024;
GO  GO:0043524;
GO  GO:0043065;
GO  GO:2001288;
GO  GO:0060999;
GO  GO:0060124;
GO  GO:0051897;
GO  GO:0015031;
GO  GO:1905274;
GO  GO:0051056;
GO  GO:0007264;
GO  GO:0048488;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFPTPFGGSLDIWAITVEERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSI
SQ  AMKLIKLKLQGYQLPSALPPVMKQQPVAISSAPAFGMGGIASMPPLTAVAPVPMGSIPVVGMSPTLVSSVPTAAVPPLAN
SQ  GAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASVPPVAEWAVPQSSRLKYRQLFNSHDKTMSGHL
SQ  TGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGISVI
SQ  SSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQE
SQ  QERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEF
SQ  ELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSL
SQ  HRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKII
SQ  ELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAV
SQ  QAPWSTAEKGPLTISAQENVKVVYYRALYPFESRSHDEITIQPGDIVMVKGEWVDESQTGEPGWLGGELKGKTGWFPANY
SQ  AEKIPENEVPAPVKPVTDSTSAPAPKLALRETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLT
SQ  VPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGW
SQ  FPKSYVKLISGPIRKSTSMDSGSSESPASLKRVASPAAKPVVSGEEFIAMYTYESSEQGDLTFQQGDVILVTKKDGDWWT
SQ  GTVGDKAGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARG
SQ  KKRQIGWFPANYVKLLSPGTSKITPTEPPKSTALAAVCQVIGMYDYTAQNDDELAFNKGQIINVLNKEDPDWWKGEVNGQ
SQ  VGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAM
SQ  IFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSRQLNGAALIQQKTDEAPDFKEFVKRL
SQ  AMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHV
SQ  QCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPI
SQ  FLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMV
SQ  NVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEI
SQ  RVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
//
ID  Q99704;
PN  Docking protein 1;
GN  DOK1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm. Nucleus. [Isoform 3]: Cytoplasm, perinuclear region.
DR  UNIPROT: Q99704;
DR  UNIPROT: O43204;
DR  UNIPROT: Q53TY2;
DR  UNIPROT: Q9UHG6;
DR  PDB: 2V76;
DR  Pfam: PF02174;
DR  Pfam: PF00169;
DR  PROSITE: PS51064;
DR  OMIM: 602919;
DR  DisGeNET: 1796;
DE  Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269|PubMed:18156175}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-1384360,EBI-297353; Score: 0.55
DE  Interaction: Q7L591-3; IntAct: EBI-1384360,EBI-10694655; Score: 0.49
DE  Interaction: P46109; IntAct: EBI-1384360,EBI-910; Score: 0.49
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-1384360; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-1384360; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-1384360; Score: 0.35
DE  Interaction: Q9Q2G4; IntAct: EBI-6248094,EBI-1384360; Score: 0.50
DE  Interaction: Q06884; IntAct: EBI-1384360,EBI-22252855; Score: 0.35
DE  Interaction: Q9JJ31; IntAct: EBI-1384360,EBI-22250160; Score: 0.35
DE  Interaction: G3V8S2; IntAct: EBI-1384360,EBI-22241455; Score: 0.35
DE  Interaction: Q2LC84; IntAct: EBI-1384360,EBI-7865699; Score: 0.35
DE  Interaction: F1LRI5; IntAct: EBI-1384360,EBI-6250034; Score: 0.35
DE  Interaction: O08776; IntAct: EBI-1384360,EBI-22253777; Score: 0.35
DE  Interaction: A0A0G2JV77; IntAct: EBI-1384360,EBI-22253297; Score: 0.35
DE  Interaction: F1LMZ8; IntAct: EBI-1384360,EBI-22247004; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-1384360,EBI-22154492; Score: 0.35
DE  Interaction: B5DFA5; IntAct: EBI-1384360,EBI-22253756; Score: 0.35
DE  Interaction: P62845; IntAct: EBI-1384360,EBI-372679; Score: 0.35
DE  Interaction: P09875; IntAct: EBI-1384360,EBI-22253732; Score: 0.35
DE  Interaction: D3ZZM3; IntAct: EBI-1384360,EBI-22246785; Score: 0.35
DE  Interaction: G3V619; IntAct: EBI-1384360,EBI-22253708; Score: 0.35
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0007411;
GO  GO:0007166;
GO  GO:0038145;
GO  GO:0045742;
GO  GO:0007265;
GO  GO:0007165;
GO  GO:0007169;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVET
SQ  PPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQ
SQ  RTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGND
SQ  IFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLD
SQ  STSAQAGEGVQRKKPLYWDLYEHAQQQLLKAKLTDPKEDPIYDEPEGLAPVPPQGLYDLPREPKDAWWCQARVKEEGYEL
SQ  PYNPATDDYAVPPPRSTKPLLAPKPQGPAFPEPGTATGSGIKSHNSALYSQVQKSGASGSWDCGLSRVGTDKTGVKSEGS
SQ  T
//
ID  Q14517;
PN  Protocadherin Fat 1, nuclear form;
GN  FAT1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15922730}; Single-pass type I membrane protein {ECO:0000269|PubMed:15922730}. Nucleus {ECO:0000269|PubMed:15922730}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15922730}.
DR  UNIPROT: Q14517;
DR  Pfam: PF00028;
DR  Pfam: PF00008;
DR  Pfam: PF02210;
DR  PROSITE: PS00010;
DR  PROSITE: PS00232;
DR  PROSITE: PS50268;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS01187;
DR  PROSITE: PS50025;
DR  OMIM: 600976;
DR  DisGeNET: 2195;
DE  Function: Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P13569; IntAct: EBI-349854,EBI-1171918; Score: 0.35
DE  Interaction: P09055; IntAct: EBI-644224,EBI-1171918; Score: 0.35
DE  Interaction: Q9JLV5; IntAct: EBI-2551335,EBI-1171918; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-747644,EBI-1171918; Score: 0.35
DE  Interaction: Q15349; IntAct: EBI-1384149,EBI-1171918; Score: 0.35
DE  Interaction: Q15910; IntAct: EBI-530054,EBI-1171918; Score: 0.35
DE  Interaction: Q8K1S6; IntAct: EBI-11147680,EBI-1171918; Score: 0.35
DE  Interaction: Q9BPW8; IntAct: EBI-307125,EBI-1171918; Score: 0.35
DE  Interaction: Q13291; IntAct: EBI-4315002,EBI-1171918; Score: 0.35
DE  Interaction: Q86WN2; IntAct: EBI-21641408,EBI-1171918; Score: 0.35
DE  Interaction: Q92187; IntAct: EBI-21513582,EBI-1171918; Score: 0.35
DE  Interaction: Q99445; IntAct: EBI-21642183,EBI-1171918; Score: 0.35
DE  Interaction: Q9HD64; IntAct: EBI-2340004,EBI-1171918; Score: 0.35
DE  Interaction: P01127; IntAct: EBI-1554925,EBI-1171918; Score: 0.35
DE  Interaction: P83916; IntAct: EBI-78129,EBI-1171918; Score: 0.35
DE  Interaction: Q02750; IntAct: EBI-492564,EBI-1171918; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-446668,EBI-1171918; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-295351,EBI-1171918; Score: 0.35
DE  Interaction: Q13322; IntAct: EBI-80275,EBI-1171918; Score: 0.35
DE  Interaction: P46734; IntAct: EBI-602462,EBI-1171918; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-726632,EBI-1171918; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-476431,EBI-1171918; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-413628,EBI-1171918; Score: 0.35
DE  Interaction: Q9UQ74; IntAct: EBI-21595127,EBI-1171918; Score: 0.35
DE  Interaction: Q8N6T7; IntAct: EBI-712415,EBI-1171918; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-1753048,EBI-1171918; Score: 0.35
DE  Interaction: O95156; IntAct: EBI-21767608,EBI-1171918; Score: 0.35
DE  Interaction: Q96LS8; IntAct: EBI-21767722,EBI-1171918; Score: 0.35
DE  Interaction: Q76B58; IntAct: EBI-21759044,EBI-1171918; Score: 0.35
GO  GO:0016324;
GO  GO:0005911;
GO  GO:0070062;
GO  GO:0030175;
GO  GO:0005925;
GO  GO:0005887;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0007015;
GO  GO:0009653;
GO  GO:0048593;
GO  GO:0007155;
GO  GO:0016477;
GO  GO:0098609;
GO  GO:0007267;
GO  GO:0003382;
GO  GO:0007163;
GO  GO:0045197;
GO  GO:0007156;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRHLALLLLLLLLFQHFGDSDGSQRLEQTPLQFTHLEYNVTVQENSAAKTYVGHPVKMGVYITHPAWEVRYKIVSGDSE
SQ  NLFKAEEYILGDFCFLRIRTKGGNTAILNREVKDHYTLIVKALEKNTNVEARTKVRVQVLDTNDLRPLFSPTSYSVSLPE
SQ  NTAIRTSIARVSATDADIGTNGEFYYSFKDRTDMFAIHPTSGVIVLTGRLDYLETKLYEMEILAADRGMKLYGSSGISSM
SQ  AKLTVHIEQANECAPVITAVTLSPSELDRDPAYAIVTVDDCDQGANGDIASLSIVAGDLLQQFRTVRSFPGSKEYKVKAI
SQ  GGIDWDSHPFGYNLTLQAKDKGTPPQFSSVKVIHVTSPQFKAGPVKFEKDVYRAEISEFAPPNTPVVMVKAIPAYSHLRY
SQ  VFKSTPGKAKFSLNYNTGLISILEPVKRQQAAHFELEVTTSDRKASTKVLVKVLGANSNPPEFTQTAYKAAFDENVPIGT
SQ  TVMSLSAVDPDEGENGYVTYSIANLNHVPFAIDHFTGAVSTSENLDYELMPRVYTLRIRASDWGLPYRREVEVLATITLN
SQ  NLNDNTPLFEKINCEGTIPRDLGVGEQITTVSAIDADELQLVQYQIEAGNELDFFSLNPNSGVLSLKRSLMDGLGAKVSF
SQ  HSLRITATDGENFATPLYINITVAASHKLVNLQCEETGVAKMLAEKLLQANKLHNQGEVEDIFFDSHSVNAHIPQFRSTL
SQ  PTGIQVKENQPVGSSVIFMNSTDLDTGFNGKLVYAVSGGNEDSCFMIDMETGMLKILSPLDRETTDKYTLNITVYDLGIP
SQ  QKAAWRLLHVVVVDANDNPPEFLQESYFVEVSEDKEVHSEIIQVEATDKDLGPNGHVTYSIVTDTDTFSIDSVTGVVNIA
SQ  RPLDRELQHEHSLKIEARDQAREEPQLFSTVVVKVSLEDVNDNPPTFIPPNYRVKVREDLPEGTVIMWLEAHDPDLGQSG
SQ  QVRYSLLDHGEGNFDVDKLSGAVRIVQQLDFEKKQVYNLTVRAKDKGKPVSLSSTCYVEVEVVDVNENLHPPVFSSFVEK
SQ  GTVKEDAPVGSLVMTVSAHDEDARRDGEIRYSIRDGSGVGVFKIGEETGVIETSDRLDRESTSHYWLTVFATDQGVVPLS
SQ  SFIEIYIEVEDVNDNAPQTSEPVYYPEIMENSPKDVSVVQIEAFDPDSSSNDKLMYKITSGNPQGFFSIHPKTGLITTTS
SQ  RKLDREQQDEHILEVTVTDNGSPPKSTIARVIVKILDENDNKPQFLQKFYKIRLPEREKPDRERNARREPLYHVIATDKD
SQ  EGPNAEISYSIEDGNEHGKFFIEPKTGVVSSKRFSAAGEYDILSIKAVDNGRPQKSSTTRLHIEWISKPKPSLEPISFEE
SQ  SFFTFTVMESDPVAHMIGVISVEPPGIPLWFDITGGNYDSHFDVDKGTGTIIVAKPLDAEQKSNYNLTVEATDGTTTILT
SQ  QVFIKVIDTNDHRPQFSTSKYEVVIPEDTAPETEILQISAVDQDEKNKLIYTLQSSRDPLSLKKFRLDPATGSLYTSEKL
SQ  DHEAVHQHTLTVMVRDQDVPVKRNFARIVVNVSDTNDHAPWFTASSYKGRVYESAAVGSVVLQVTALDKDKGKNAEVLYS
SQ  IESGNIGNSFMIDPVLGSIKTAKELDRSNQAEYDLMVKATDKGSPPMSEITSVRIFVTIADNASPKFTSKEYSVELSETV
SQ  SIGSFVGMVTAHSQSSVVYEIKDGNTGDAFDINPHSGTIITQKALDFETLPIYTLIIQGTNMAGLSTNTTVLVHLQDEND
SQ  NAPVFMQAEYTGLISESASINSVVLTDRNVPLVIRAADADKDSNALLVYHIVEPSVHTYFAIDSSTGAIHTVLSLDYEET
SQ  SIFHFTVQVHDMGTPRLFAEYAANVTVHVIDINDCPPVFAKPLYEASLLLPTYKGVKVITVNATDADSSAFSQLIYSITE
SQ  GNIGEKFSMDYKTGALTVQNTTQLRSRYELTVRASDGRFAGLTSVKINVKESKESHLKFTQDVYSAVVKENSTEAETLAV
SQ  ITAIGNPINEPLFYHILNPDRRFKISRTSGVLSTTGTPFDREQQEAFDVVVEVTEEHKPSAVAHVVVKVIVEDQNDNAPV
SQ  FVNLPYYAVVKVDTEVGHVIRYVTAVDRDSGRNGEVHYYLKEHHEHFQIGPLGEISLKKQFELDTLNKEYLVTVVAKDGG
SQ  NPAFSAEVIVPITVMNKAMPVFEKPFYSAEIAESIQVHSPVVHVQANSPEGLKVFYSITDGDPFSQFTINFNTGVINVIA
SQ  PLDFEAHPAYKLSIRATDSLTGAHAEVFVDIIVDDINDNPPVFAQQSYAVTLSEASVIGTSVVQVRATDSDSEPNRGISY
SQ  QMFGNHSKSHDHFHVDSSTGLISLLRTLDYEQSRQHTIFVRAVDGGMPTLSSDVIVTVDVTDLNDNPPLFEQQIYEARIS
SQ  EHAPHGHFVTCVKAYDADSSDIDKLQYSILSGNDHKHFVIDSATGIITLSNLHRHALKPFYSLNLSVSDGVFRSSTQVHV
SQ  TVIGGNLHSPAFLQNEYEVELAENAPLHTLVMEVKTTDGDSGIYGHVTYHIVNDFAKDRFYINERGQIFTLEKLDRETPA
SQ  EKVISVRLMAKDAGGKVAFCTVNVILTDDNDNAPQFRATKYEVNIGSSAAKGTSVVKVLASDADEGSNADITYAIEADSE
SQ  SVKENLEINKLSGVITTKESLIGLENEFFTFFVRAVDNGSPSKESVVLVYVKILPPEMQLPKFSEPFYTFTVSEDVPIGT
SQ  EIDLIRAEHSGTVLYSLVKGNTPESNRDESFVIDRQSGRLKLEKSLDHETTKWYQFSILARCTQDDHEMVASVDVSIQVK
SQ  DANDNSPVFESSPYEAFIVENLPGGSRVIQIRASDADSGTNGQVMYSLDQSQSVEVIESFAINMETGWITTLKELDHEKR
SQ  DNYQIKVVASDHGEKIQLSSTAIVDVTVTDVNDSPPRFTAEIYKGTVSEDDPQGGVIAILSTTDADSEEINRQVTYFITG
SQ  GDPLGQFAVETIQNEWKVYVKKPLDREKRDNYLLTITATDGTFSSKAIVEVKVLDANDNSPVCEKTLYSDTIPEDVLPGK
SQ  LIMQISATDADIRSNAEITYTLLGSGAEKFKLNPDTGELKTSTPLDREEQAVYHLLVRATDGGGRFCQASIVLTLEDVND
SQ  NAPEFSADPYAITVFENTEPGTLLTRVQATDADAGLNRKILYSLIDSADGQFSINELSGIIQLEKPLDRELQAVYTLSLK
SQ  AVDQGLPRRLTATGTVIVSVLDINDNPPVFEYREYGATVSEDILVGTEVLQVYAASRDIEANAEITYSIISGNEHGKFSI
SQ  DSKTGAVFIIENLDYESSHEYYLTVEATDGGTPSLSDVATVNVNVTDINDNTPVFSQDTYTTVISEDAVLEQSVITVMAD
SQ  DADGPSNSHIHYSIIDGNQGSSFTIDPVRGEVKVTKLLDRETISGYTLTVQASDNGSPPRVNTTTVNIDVSDVNDNAPVF
SQ  SRGNYSVIIQENKPVGFSVLQLVVTDEDSSHNGPPFFFTIVTGNDEKAFEVNPQGVLLTSSAIKRKEKDHYLLQVKVADN
SQ  GKPQLSSLTYIDIRVIEESIYPPAILPLEIFITSSGEEYSGGVIGKIHATDQDVYDTLTYSLDPQMDNLFSVSSTGGKLI
SQ  AHKKLDIGQYLLNVSVTDGKFTTVADITVHIRQVTQEMLNHTIAIRFANLTPEEFVGDYWRNFQRALRNILGVRRNDIQI
SQ  VSLQSSEPHPHLDVLLFVEKPGSAQISTKQLLHKINSSVTDIEEIIGVRILNVFQKLCAGLDCPWKFCDEKVSVDESVMS
SQ  THSTARLSFVTPRHHRAAVCLCKEGRCPPVHHGCEDDPCPEGSECVSDPWEEKHTCVCPSGRFGQCPGSSSMTLTGNSYV
SQ  KYRLTENENKLEMKLTMRLRTYSTHAVVMYARGTDYSILEIHHGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVALEVNG
SQ  NYARLVLDQVHTASGTAPGTLKTLNLDNYVFFGGHIRQQGTRHGRSPQVGNGFRGCMDSIYLNGQELPLNSKPRSYAHIE
SQ  ESVDVSPGCFLTATEDCASNPCQNGGVCNPSPAGGYYCKCSALYIGTHCEISVNPCSSKPCLYGGTCVVDNGGFVCQCRG
SQ  LYTGQRCQLSPYCKDEPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECSGNPCLHGALCENTHGSYHCNCSHEYRGR
SQ  HCEDAAPNQYVSTPWNIGLAEGIGIVVFVAGIFLLVVVFVLCRKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKN
SQ  IYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDS
SQ  DSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEF
SQ  PNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRN
SQ  RQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVM
SQ  MSDYESGDDGHFEEVTIPPLDSQQHTEV
//
ID  P25028;
PN  Mitosis initiation protein fs(1)Ya;
GN  fs;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm. Note=In the nuclear envelope during interphase to metaphase. And in the nucleoplasm and cytoplasm during anaphase and telophase.
DR  UNIPROT: P25028;
DR  UNIPROT: Q8T057;
DR  UNIPROT: Q9W4W0;
DR  UNIPROT: Q9W4W1;
DR  PROSITE: PS00028;
DE  Function: Cell cycle-dependent nuclear envelope component required for embryonic mitosis.
DE  Reference Proteome: Yes;
DE  Interaction: P08928; IntAct: EBI-188444,EBI-106103; Score: 0.27
DE  Interaction: O61307; IntAct: EBI-118556,EBI-106103; Score: 0.35
DE  Interaction: P02283; IntAct: EBI-188137,EBI-106103; Score: 0.27
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0051301;
GO  GO:0006333;
GO  GO:0030261;
GO  GO:0006260;
GO  GO:0000278;
GO  GO:0006997;
GO  GO:0007344;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFSNVLIMRQPDEGKCHICKRVFCCGKCRQKHQFKAHAIAVREPLGLRSAGGGIIEHRHQMESGATTIYVFCPICERRP
SQ  LLLREEMHGELLAHIETCHLPLRCRKCQRNYTRVDDLREFSKCVDQQQSCTDVTGATETSKATLKKAANSTAISTQTSPS
SQ  VTPISLINMRWKAKSRVTHEEFISDSVSSIRNLSSFSNSSIRRSIGQLGVNPSETMEKGKVIRSTSTPLHVESVFAKPKE
SQ  PITFNASTGGHVSSIYHEEPSPTPESNPVQQQQQQQQPLQQRAWKMGARNKMSAATPLRQVMSKSIQKAFVEHGGMMVHQ
SQ  PPSAVVQRRVRLDLSEHSSHEAAGSSALDLRLSPAMRRTQSESSASEVNSGSSSSYSTSRNADLCKRQFLLSAQKLTTES
SQ  IIITRTNSSSQKTSSTVYNSCESVEIIRSTSESAEVCHVPAITPIRVTGAGINKKQIKFETPPKSSQQMRSNGEGDETKD
SQ  QFFTPEPGTPEIPERRHRQAIVPRQLSGEFSPKKDKPKEKGLAVMALISPPLQQPRVRPPLRECRQQRVYSGVQDVGEPE
SQ  VVDAEEEDEVFRPTNASTCNDKKLEAPNSGRLWSLMSSMMRLPASLRGEREKDRDRDRDSDKENAGSGSLIRRCASIAGS
SQ  LVRPSARDSSMEDQQCLKRKRTQTLDSQYCSPLSPSSSSKRYRIRPREPIERMRRQ
//
ID  Q9H4E7;
PN  Differentially expressed in FDCP 6 homolog;
GN  DEF6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15023524}. Cell membrane {ECO:0000269|PubMed:15023524, ECO:0000305|PubMed:12651066}. Nucleus {ECO:0000269|PubMed:15023524}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15023524}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15023524}. Cell projection, filopodium {ECO:0000269|PubMed:15023524}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate (PubMed:15023524). Binds to actin filaments (PubMed:15023524). {ECO:0000269|PubMed:15023524}.
DR  UNIPROT: Q9H4E7;
DR  UNIPROT: Q86VF4;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  OMIM: 610094;
DR  DisGeNET: 50619;
DE  Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1. Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:12651066, ECO:0000269|PubMed:15023524}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-745369,EBI-740019; Score: 0.56
DE  Interaction: Q9H0H0; IntAct: EBI-8471507,EBI-745369; Score: 0.56
DE  Interaction: Q61738-6; IntAct: EBI-1786329,EBI-745369; Score: 0.37
DE  Interaction: I6L996; IntAct: EBI-10181089,EBI-745369; Score: 0.72
DE  Interaction: Q8IX15-3; IntAct: EBI-745369,EBI-10172004; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-745369,EBI-533224; Score: 0.67
DE  Interaction: Q00587; IntAct: EBI-744130,EBI-745369; Score: 0.56
DE  Interaction: Q96AQ6; IntAct: EBI-740845,EBI-745369; Score: 0.56
DE  Interaction: Q9NRA8; IntAct: EBI-301024,EBI-745369; Score: 0.56
DE  Interaction: Q8ZAR2; IntAct: EBI-2842016,EBI-745369; Score: 0.37
DE  Interaction: Q8D0E1; IntAct: EBI-2851171,EBI-745369; Score: 0.37
DE  Interaction: Q7Z5H3-2; IntAct: EBI-745369,EBI-12084490; Score: 0.56
DE  Interaction: Q9BUH8; IntAct: EBI-742722,EBI-745369; Score: 0.37
DE  Interaction: A6NC98; IntAct: EBI-347573,EBI-745369; Score: 0.56
DE  Interaction: Q86T90; IntAct: EBI-3437878,EBI-745369; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-5916454,EBI-745369; Score: 0.56
DE  Interaction: Q96JM7-2; IntAct: EBI-11985629,EBI-745369; Score: 0.56
DE  Interaction: Q9NYA3; IntAct: EBI-11163335,EBI-745369; Score: 0.56
DE  Interaction: Q04864-2; IntAct: EBI-10829018,EBI-745369; Score: 0.56
DE  Interaction: O95391; IntAct: EBI-750559,EBI-745369; Score: 0.56
DE  Interaction: O00422; IntAct: EBI-1044156,EBI-745369; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-948001,EBI-745369; Score: 0.56
DE  Interaction: Q86YV0; IntAct: EBI-3437896,EBI-745369; Score: 0.56
DE  Interaction: Q8WZA2; IntAct: EBI-745369,EBI-948476; Score: 0.56
DE  Interaction: P25786; IntAct: EBI-359352,EBI-745369; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-11139477,EBI-745369; Score: 0.56
DE  Interaction: P0C7X2; IntAct: EBI-4395732,EBI-745369; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-6509505,EBI-745369; Score: 0.56
DE  Interaction: Q9ULK0; IntAct: EBI-745369,EBI-17496373; Score: 0.35
DE  Interaction: Q9P258; IntAct: EBI-745369,EBI-352547; Score: 0.35
DE  Interaction: Q9NXR7; IntAct: EBI-745369,EBI-949389; Score: 0.35
DE  Interaction: Q9NXF7; IntAct: EBI-745369,EBI-2559096; Score: 0.35
DE  Interaction: Q9NWV8; IntAct: EBI-745369,EBI-745725; Score: 0.35
DE  Interaction: Q9HCJ0-2; IntAct: EBI-745369,EBI-16811468; Score: 0.35
DE  Interaction: Q96JM3; IntAct: EBI-745369,EBI-2560420; Score: 0.35
DE  Interaction: Q92625; IntAct: EBI-745369,EBI-1048612; Score: 0.35
DE  Interaction: Q8N6N3-2; IntAct: EBI-745369,EBI-21558755; Score: 0.35
DE  Interaction: Q8IX15; IntAct: EBI-745369,EBI-10742083; Score: 0.35
DE  Interaction: Q8IUH3-3; IntAct: EBI-745369,EBI-10964453; Score: 0.35
DE  Interaction: Q7Z4W1; IntAct: EBI-745369,EBI-1044712; Score: 0.35
DE  Interaction: Q15018; IntAct: EBI-745369,EBI-1056583; Score: 0.35
DE  Interaction: Q04759; IntAct: EBI-745369,EBI-374762; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-745369,EBI-307326; Score: 0.35
DE  Interaction: P46736-2; IntAct: EBI-745369,EBI-21558747; Score: 0.35
DE  Interaction: P35612-2; IntAct: EBI-745369,EBI-21549355; Score: 0.35
DE  Interaction: P28370-2; IntAct: EBI-745369,EBI-21558739; Score: 0.35
DE  Interaction: A6NI28; IntAct: EBI-745369,EBI-21517923; Score: 0.35
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKV
SQ  EEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLG
SQ  ELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQL
SQ  QPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTS
SQ  LHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQL
SQ  REAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQ
SQ  ERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKR
SQ  PVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN
//
ID  P05129;
PN  Protein kinase C gamma type;
GN  PRKCG;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:29053796}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000250|UniProtKB:P63318}.
DR  UNIPROT: P05129;
DR  UNIPROT: B7Z8Q0;
DR  PDB: 2E73;
DR  PDB: 2UZP;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 176980;
DR  OMIM: 605361;
DR  DisGeNET: 5582;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity). {ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319, ECO:0000269|PubMed:16377624}.
DE  Disease: Spinocerebellar ataxia 14 (SCA14) [MIM:605361]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA). {ECO:0000269|PubMed:12644968, ECO:0000269|PubMed:29053796}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95831; IntAct: EBI-949799,EBI-356440; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-949799,EBI-79165; Score: 0.37
DE  Interaction: Q86UR1; IntAct: EBI-949814,EBI-949799; Score: 0.37
DE  Interaction: O00471; IntAct: EBI-949799,EBI-949824; Score: 0.37
DE  Interaction: Q8TD31; IntAct: EBI-949834,EBI-949799; Score: 0.37
DE  Interaction: P17252; IntAct: EBI-1383528,EBI-949799; Score: 0.53
DE  Interaction: P08238; IntAct: EBI-352572,EBI-949799; Score: 0.56
DE  Interaction: O60256; IntAct: EBI-949799,EBI-724960; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-949799,EBI-355275; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-949799,EBI-355133; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-949799,EBI-296047; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-949799,EBI-352528; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-949799,EBI-351896; Score: 0.35
DE  Interaction: P11908; IntAct: EBI-949799,EBI-4290895; Score: 0.35
DE  Interaction: P17066; IntAct: EBI-949799,EBI-355106; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-949799,EBI-877656; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-949799,EBI-347834; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-949799,EBI-1054052; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-949799,EBI-357448; Score: 0.35
DE  Interaction: P60891; IntAct: EBI-949799,EBI-749195; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-949799,EBI-351356; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-949799,EBI-358549; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-949799,EBI-356710; Score: 0.35
DE  Interaction: Q14558; IntAct: EBI-949799,EBI-724449; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-949799,EBI-295634; Score: 0.35
DE  Interaction: Q16822; IntAct: EBI-949799,EBI-2825219; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-949799,EBI-2961708; Score: 0.35
DE  Interaction: Q9BQ70; IntAct: EBI-949799,EBI-745182; Score: 0.35
DE  Interaction: Q9Y6Y0; IntAct: EBI-949799,EBI-715774; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-949799,EBI-352682; Score: 0.35
DE  Interaction: P11413; IntAct: EBI-949799,EBI-4289891; Score: 0.35
DE  Interaction: Q14766; IntAct: EBI-949799,EBI-947693; Score: 0.35
GO  GO:0044305;
GO  GO:0005911;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004672;
GO  GO:0004697;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0008270;
GO  GO:0007268;
GO  GO:0007635;
GO  GO:0060384;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0042177;
GO  GO:0031397;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:0030168;
GO  GO:0032425;
GO  GO:0099171;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0050764;
GO  GO:0032095;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:1990911;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGR
SQ  LQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSG
SQ  ENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
//
ID  P36268;
PN  Inactive glutathione hydrolase 2;
GN  GGT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23682772}. Endoplasmic reticulum {ECO:0000269|PubMed:23682772}. Note=Co-localizes with calnexin in the endoplasmic reticulum.
DR  UNIPROT: P36268;
DR  PROSITE: PS00462;
DR  OMIM: 137181;
DR  DisGeNET: 728441;
DE  Function: Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. {ECO:0000269|PubMed:23682772}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000048;
GO  GO:0006751;
GO  GO:1901750;
GO  GO:0031179;
GO  GO:0006508;
GO  GO:0002682;
GO  GO:0050727;
GO  GO:0032355;
GO  GO:0032496;
GO  GO:0034612;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAMAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNA
SQ  HSMGIGVGLFLTIYNSTTGKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPS
SQ  IQLARQGFPVGKGLAAVLENKRTVIEQQPVLWYVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKD
SQ  IQAAGGIVTAEDLNNYRAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAF
SQ  RFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTI
SQ  NLYFGSKVCSPVSGILFNNEWTTSALPAFTNEFGAPPSPANFIQPGKQPLLSMCLTIMVGQDGQVRMVVGAAGGTQITTD
SQ  TALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAALDS
SQ  RKGGEPAGY
//
ID  O80528;
PN  Serine/threonine-protein kinase haspin homolog;
GN  HASPIN;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21527018}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21527018}. Nucleus {ECO:0000269|PubMed:21527018}. Chromosome {ECO:0000269|PubMed:21527018}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21527018}. Note=During interphase, localized in the cytoplasm and at the nuclear periphery. During prometaphase and metaphase, localized on chromosomes, and around the cell plate during cytokinesis. {ECO:0000269|PubMed:21527018}.
DR  UNIPROT: O80528;
DR  UNIPROT: Q84WE0;
DR  PROSITE: PS50011;
DE  Function: Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph) and 'Thr-11' (H3T11ph), but not at 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Plays a role in mitotic cell division during plant growth (PubMed:21527018). Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph), but not at 'Thr-11' (H3T11ph), 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Involved in histone H3 phosphorylation in mitotic cells. Contributes to organ and plant development, as well as embryonic patterning (PubMed:21749502). {ECO:0000269|PubMed:21527018, ECO:0000269|PubMed:21749502}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0005524;
GO  GO:0035402;
GO  GO:0072354;
GO  GO:0004674;
GO  GO:0035407;
GO  GO:0072355;
GO  GO:0035556;
GO  GO:0000278;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGQRVDLWSEVIKSEEEDGDIPKIEAVFQRRKKPDKSSEAVNFGWLVKGARTSSVNGPKRDSWARSLSTRGRESIAVRAY
SQ  VNNQPQKKAAGRKKPPIPKGKVVKAPDFQKEKEYFRDIDAFELLEESPSPNKSSTWTMGEQVVPEMPHLSTRLEKWLISK
SQ  KLNHTCGPSSTLSKILENSAIHQESVCDNDAFDSLSLKTPDKSSAGNTSVFRLIPSCDENLAAEDVPVRKIKMESIDLED
SQ  ELKRLSLTSDLIPTHQDFDQPILDLLSACGQMRPSNFIEAFSKFCEPESIVKIGEGTYGEAFRAGSSVCKIVPIDGDFRV
SQ  NGEVQKRADELLEEVILSWTLNQLRECETTAQNLCPTYIKTQDIKLCQGPYDPILIKAWEEWDAKHGSENDHPDFPEKQC
SQ  YVMFVLEHGGKDLESFVLLNFDEARSLLVQATAGLAVAEAAFEFEHRDLHWGNILLSRNNSDTLPFILEGKQVCIKTFGV
SQ  QISIIDFTLSRINTGEKILFLDLTSDPYLFKGPKGDKQSETYRKMKAVTEDYWEGSFARTNVLWLIYLVDILLTKKSFER
SQ  SSKHERELRSLKKRMEKYESAKEAVSDPFFSDMLMDQIS
//
ID  B2RUJ5;
PN  Amyloid-beta A4 precursor protein-binding family A member 1;
GN  Apba1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. [Isoform 3]: Golgi apparatus.
DR  UNIPROT: B2RUJ5;
DR  UNIPROT: Q3UH49;
DR  UNIPROT: Q8BMF2;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DE  Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P61294; IntAct: EBI-8840254,EBI-529766; Score: 0.27
DE  Interaction: P20340-1; IntAct: EBI-8851226,EBI-8840254; Score: 0.44
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048787;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0001540;
GO  GO:0030165;
GO  GO:0005546;
GO  GO:0044877;
GO  GO:0007268;
GO  GO:0014051;
GO  GO:0014047;
GO  GO:0001701;
GO  GO:0006886;
GO  GO:0007626;
GO  GO:0035264;
GO  GO:0065003;
GO  GO:0010468;
GO  GO:2000300;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLA
SQ  RSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLE
SQ  HEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLH
SQ  HYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGL
SQ  PAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQR
SQ  PVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDK
SQ  TPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIV
SQ  VLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLL
SQ  NTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLV
SQ  GLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQS
SQ  VVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
//
ID  O95999;
PN  B-cell lymphoma/leukemia 10;
GN  BCL10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts.
DR  UNIPROT: O95999;
DR  UNIPROT: Q5VUF1;
DR  PDB: 2MB9;
DR  PDB: 6BZE;
DR  PDB: 6GK2;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  OMIM: 137245;
DR  OMIM: 603517;
DR  OMIM: 616098;
DR  DisGeNET: 8915;
DE  Function: Involved in adaptive immune response (PubMed:25365219). Promotes apoptosis, pro-caspase-9 maturation and activation of NF- kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex. Is a substrate for MALT1 (PubMed:18264101). {ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:25365219}.
DE  Disease: Note=A chromosomal aberration involving BCL10 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(1;14)(p22;q32). Although the BCL10/IgH translocation leaves the coding region of BCL10 intact, frequent BCL10 mutations could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. Immunodeficiency 37 (IMD37) [MIM:616098]: A form of primary combined immunodeficiency, a group of disorders characterized by severe recurrent infections, with normal numbers or an absence of T and B lymphocytes, and impaired cellular and humoral immunity. IMD37 is characterized by hypogammaglobulinemia without lymphopenia, but with profoundly reduced memory B cells and memory T cells, and increased numbers of circulating naive lymphocytes. Inheritance is autosomal recessive. {ECO:0000269|PubMed:25365219}. Note=The disease is caused by mutations affecting the gene represented in this entry. Lymphoma, mucosa-associated lymphoid type (MALTOMA) [MIM:137245]: A subtype of non-Hodgkin lymphoma, originating in mucosa- associated lymphoid tissue. MALT lymphomas occur most commonly in the gastro-intestinal tract but have been described in a variety of extranodal sites including the ocular adnexa, salivary gland, thyroid, lung, thymus, and breast. Histologically, they are characterized by an infiltrate of small to medium-sized lymphocytes with abundant cytoplasm and irregularly shaped nuclei. Scattered transformed blasts (large cells) also are present. Non-malignant reactive follicles are observed frequently. A pivotal feature is the presence of lymphoepithelial lesions, with invasion and partial destruction of mucosal glands and crypts by aggregates of tumor cells. {ECO:0000269|PubMed:9989495}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-958922,EBI-958922; Score: 0.75
DE  Interaction: Q12933; IntAct: EBI-958922,EBI-355744; Score: 0.81
DE  Interaction: P50750; IntAct: EBI-1383449,EBI-958922; Score: 0.37
DE  Interaction: Q13261; IntAct: EBI-958922,EBI-980354; Score: 0.37
DE  Interaction: Q07955; IntAct: EBI-398920,EBI-958922; Score: 0.37
DE  Interaction: Q8WUM9; IntAct: EBI-958922,EBI-3909857; Score: 0.37
DE  Interaction: O14745; IntAct: EBI-349787,EBI-958922; Score: 0.37
DE  Interaction: Q05513; IntAct: EBI-958922,EBI-295351; Score: 0.56
DE  Interaction: P33215; IntAct: EBI-2366213,EBI-958922; Score: 0.35
DE  Interaction: O95684; IntAct: EBI-1266334,EBI-958922; Score: 0.35
DE  Interaction: Q8N6Y0; IntAct: EBI-958922,EBI-739895; Score: 0.44
DE  Interaction: Q9BZD6; IntAct: EBI-958922,EBI-3918643; Score: 0.37
DE  Interaction: P62807; IntAct: EBI-354552,EBI-958922; Score: 0.40
DE  Interaction: Q14525; IntAct: EBI-1049638,EBI-958922; Score: 0.40
DE  Interaction: P31749; IntAct: EBI-296087,EBI-958922; Score: 0.69
DE  Interaction: P20749; IntAct: EBI-958922,EBI-958997; Score: 0.52
DE  Interaction: Q9H257; IntAct: EBI-958922,EBI-751319; Score: 0.55
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-958922; Score: 0.70
DE  Interaction: Q9BXL7; IntAct: EBI-7006141,EBI-958922; Score: 0.86
DE  Interaction: Q9UDY8; IntAct: EBI-1047372,EBI-958922; Score: 0.91
DE  Interaction: Q9Y6K9; IntAct: EBI-81279,EBI-958922; Score: 0.79
DE  Interaction: Q9H0F6; IntAct: EBI-3942966,EBI-958922; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-958922; Score: 0.35
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0001772;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0050700;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0051059;
GO  GO:0002020;
GO  GO:0008022;
GO  GO:0043422;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0044877;
GO  GO:0003713;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0001783;
GO  GO:0008219;
GO  GO:0006968;
GO  GO:0071222;
GO  GO:0071260;
GO  GO:0038095;
GO  GO:0007249;
GO  GO:0016064;
GO  GO:0045087;
GO  GO:0042226;
GO  GO:0031663;
GO  GO:0042109;
GO  GO:0002906;
GO  GO:0001843;
GO  GO:0043065;
GO  GO:0043280;
GO  GO:2001238;
GO  GO:0043123;
GO  GO:0045416;
GO  GO:0033674;
GO  GO:0032765;
GO  GO:0051092;
GO  GO:0042327;
GO  GO:0031398;
GO  GO:0050870;
GO  GO:0045893;
GO  GO:0016567;
GO  GO:0050856;
GO  GO:0032094;
GO  GO:0009620;
GO  GO:0002223;
GO  GO:0070231;
GO  GO:0050852;
GO  GO:0002224;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLD
SQ  TLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGES
SQ  STTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ
//
ID  P14142;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  Slc2a4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21907143, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27739494}; Multi-pass membrane protein {ECO:0000269|PubMed:21907143}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (PubMed:26629404, PubMed:26240143, PubMed:27354378). The dileucine internalization motif is critical for intracellular sequestration (PubMed:26240143, PubMed:26629404). Insulin stimulation induces translocation to the cell membrane (PubMed:27739494). {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378, ECO:0000269|PubMed:27739494}.
DR  UNIPROT: P14142;
DR  UNIPROT: Q3TPK6;
DR  UNIPROT: Q9JJN9;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  PROSITE: PS00217;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation (PubMed:26240143, PubMed:26629404). Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells (PubMed:26240143, PubMed:26629404). Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell (PubMed:26240143, PubMed:26629404). {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
DE  Disease: Note=Defects in Slc2a4 may be the cause of certain post- receptor defects in non-insulin-dependent diabetes mellitus (NIDDM).
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005768;
GO  GO:0009897;
GO  GO:0070062;
GO  GO:0032593;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0030140;
GO  GO:0012506;
GO  GO:0055056;
GO  GO:0005355;
GO  GO:0005360;
GO  GO:0010021;
GO  GO:0050873;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071470;
GO  GO:0071356;
GO  GO:0042593;
GO  GO:0046323;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0098694;
GO  GO:0045471;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTL
SQ  WALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYV
SQ  GEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPA
SQ  RKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVG
SQ  QPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPG
SQ  PIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQIS
SQ  AAFRRTPSLLEQEVKPSTELEYLGPDEND
//
ID  Q95ZK7;
PN  Defective in germ line development protein 3;
GN  gld;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Cytoplasmic granule {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Note=Localizes to P granules. Found also in particles near but not coincident with P granules. {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}.
DR  UNIPROT: Q95ZK7;
DR  UNIPROT: Q95ZK6;
DR  PDB: 3N89;
DR  PDB: 4ZRL;
DR  Pfam: PF17905;
DE  Function: Required maternally for germline survival and embryogenesis. Forms a complex with gls-1 which promotes the oogenic cell fate by freeing the translational repressor fbf to repress sperm promoting factors. Promotes maturation of primary spermatocytes to mature sperm. Required during hermaphrodite development to promote sperm fate, which is critical for determining the normal number of sperm. Promotion of sperm fate is at the expense of oogenesis, possibly through the negative regulation of fbf. Required during male development for the continued production of sperm and inhibition of oogenesis. Together with gld-2, promotes the transition from mitosis to meiosis. {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:15454534, ECO:0000269|PubMed:19461891}.
DE  Reference Proteome: Yes;
DE  Interaction: O17087; IntAct: EBI-317828,EBI-2420017; Score: 0.51
DE  Interaction: O76572; IntAct: EBI-6535465,EBI-317828; Score: 0.37
DE  Interaction: Q10666; IntAct: EBI-317870,EBI-317828; Score: 0.37
DE  Interaction: Q10953; IntAct: EBI-317828,EBI-2530558; Score: 0.37
DE  Interaction: Q8I4M5-3; IntAct: EBI-14989623,EBI-317828; Score: 0.37
DE  Interaction: Q8I4M5; IntAct: EBI-322416,EBI-317828; Score: 0.27
DE  Interaction: G5EFL5; IntAct: EBI-317828,EBI-316352; Score: 0.37
DE  Interaction: Q95QA6; IntAct: EBI-317828,EBI-327642; Score: 0.37
DE  Interaction: O17670; IntAct: EBI-317828,EBI-311862; Score: 0.37
DE  Interaction: G5EDS1; IntAct: EBI-317828,EBI-319610; Score: 0.37
GO  GO:0005737;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0031379;
GO  GO:0019904;
GO  GO:0003723;
GO  GO:0009792;
GO  GO:0018992;
GO  GO:0042078;
GO  GO:0042006;
GO  GO:0051321;
GO  GO:0000281;
GO  GO:0051100;
GO  GO:0002119;
GO  GO:0000280;
GO  GO:0045836;
GO  GO:0040018;
GO  GO:0043631;
GO  GO:0007283;
GO  GO:0040025;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGEQSHEKDHDEAHSYNPFVRSAVEYDADTRLQMAENAASARKLFVSSALKDIIVNPENFYHDFQQSAQMAEDANQRRQV
SQ  SYNTKREAHIHQLKAQGLPLPSNIPMIEINPTRVTLNMEFESQYYSLMTSDNGDHENVASIMAETNTLIQLPDRSVGGTT
SQ  PDPFAQQVTITGYFGDVDRARMLMRRNCHFTVFMALSKMKMPLHELQAHVRQNPIQNVEMSFVDAPEKNGIVTTYLRITA
SQ  REKNQHELIEAAKRLNEILFRESPAPENNFTLHFTLSTYYVDQVLGSSSTAQLMPVIERETTTIISYPCYNNRNETRGNI
SQ  YEIKVVGNIDNVLKARRYIMDLLPISMCFNIKNTDMAEPSRVSDRNIHMIIDESGIILKMTPSVYEPADLLSGEVPLNCA
SQ  SLRSKEFNIKKLYTAYQKVLSKKFDFIAPQPNDYDNSIWHHSLPANFLKNFNMPCRGELSDGSNGRRHRSSSIASSRSKH
SQ  SYMSKGKQFSESSGGPSRSHTRVSSFSENSSTVPIMQFPTPHFAPPMLTPHHHMLKYVYLQQHQQAQTFLKGAAGLHPGT
SQ  HIMFPPPIIVDGSFVSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRNMGNRPSSSTGSYYP
SQ  STTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYERQYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHR
SQ  DVRNSNEYDFHVGNSGPAKRSPSLEQVQLQMTHHLKLKSNDVDLDHEKLYMHESPHNDSDTTVSASGFGNDLMDGDFVQR
SQ  FLSNANINESGRRPRTVSCFTEKDGQSARYIDSDGAYSVVDHASTHQSRSYDSFRKVGDNGVTKTILEPRARVEKDYGKI
SQ  SLEHKTKYSNEYGDEEKSAENDTSSLGSRQYRIDPMKLIASVRESSEQLPRIHERQFSDVLNEKEKEIADKSIESTVTQD
SQ  LSLDETSTY
//
ID  Q90474;
PN  Heat shock protein HSP 90-alpha 1;
GN  hsp90a;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Melanosome {ECO:0000250|UniProtKB:P07900}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage.
DR  UNIPROT: Q90474;
DR  UNIPROT: Q5RG13;
DR  UNIPROT: Q6DI33;
DR  Pfam: PF02518;
DR  Pfam: PF00183;
DR  PROSITE: PS00298;
DE  Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly (PubMed:10364427, PubMed:17586488, PubMed:18182494, PubMed:18256191). {ECO:0000250|UniProtKB:P07900, ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:18182494, ECO:0000269|PubMed:18256191}.
DE  Reference Proteome: Yes;
GO  GO:0031672;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0043209;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0030018;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0097718;
GO  GO:0030235;
GO  GO:0051082;
GO  GO:0034605;
GO  GO:0050900;
GO  GO:0007517;
GO  GO:0030239;
GO  GO:0045429;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0010038;
GO  GO:0048769;
GO  GO:0030241;
GO  GO:0030240;
GO  GO:0014866;
GO  GO:0071688;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPD
SQ  QKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWE
SQ  SAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEV
SQ  AAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVK
SQ  HFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSK
SQ  ILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDT
SQ  QKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAK
SQ  YENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLR
SQ  EKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSR
SQ  MEEVD
//
ID  O95831;
PN  Apoptosis-inducing factor 1, mitochondrial;
GN  AIFM1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion intermembrane space {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:26004228}. Mitochondrion inner membrane. Cytoplasm {ECO:0000269|PubMed:15775970}. Nucleus {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17094969}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis (PubMed:15775970). Colocalizes with EIF3G in the nucleus and perinuclear region (PubMed:17094969). {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969}. [Isoform 3]: Mitochondrion intermembrane space {ECO:0000269|PubMed:20111043}. Mitochondrion inner membrane {ECO:0000269|PubMed:20111043}. Note=Has a stronger membrane anchorage than isoform 1. {ECO:0000269|PubMed:20111043}. [Isoform 4]: Mitochondrion {ECO:0000269|PubMed:16644725}. Cytoplasm, cytosol {ECO:0000269|PubMed:16644725}. Note=In pro-apoptotic conditions, is released from mitochondria to cytosol in a calpain/cathepsin-dependent manner. {ECO:0000269|PubMed:16644725}. [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:16365034}.
DR  UNIPROT: O95831;
DR  UNIPROT: A4QPB4;
DR  UNIPROT: B1ALN1;
DR  UNIPROT: B2RB08;
DR  UNIPROT: D3DTE9;
DR  UNIPROT: Q1L6K4;
DR  UNIPROT: Q1L6K6;
DR  UNIPROT: Q2QKE4;
DR  UNIPROT: Q5JUZ7;
DR  UNIPROT: Q6I9X6;
DR  UNIPROT: Q9Y3I3;
DR  UNIPROT: Q9Y3I4;
DR  PDB: 1M6I;
DR  PDB: 4BUR;
DR  PDB: 4BV6;
DR  PDB: 4FDC;
DR  PDB: 4LII;
DR  PDB: 5FMH;
DR  PDB: 5FS6;
DR  PDB: 5FS7;
DR  PDB: 5FS8;
DR  PDB: 5FS9;
DR  PDB: 5KVH;
DR  PDB: 5KVI;
DR  Pfam: PF14721;
DR  Pfam: PF07992;
DR  OMIM: 300169;
DR  OMIM: 300614;
DR  OMIM: 300816;
DR  OMIM: 310490;
DR  DisGeNET: 9131;
DE  Function: Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:20362274, PubMed:23217327, PubMed:17094969). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (By similarity). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase- independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228). {ECO:0000250|UniProtKB:Q9Z0X1, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225, ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:27178839}. [Isoform 4]: Has NADH oxidoreductase activity. Does not induce nuclear apoptosis. {ECO:0000269|PubMed:16644725}. [Isoform 5]: Pro-apoptotic isoform. {ECO:0000269|PubMed:16365034}.
DE  Disease: Combined oxidative phosphorylation deficiency 6 (COXPD6) [MIM:300816]: A mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy. {ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:22019070, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:26173962, ECO:0000269|PubMed:27178839}. Note=The disease is caused by mutations affecting the gene represented in this entry. Charcot-Marie-Tooth disease, X-linked recessive, 4, with or without cerebellar ataxia (CMTX4) [MIM:310490]: A neuromuscular disorder characterized by progressive sensorimotor axonal neuropathy, distal sensory impairment, difficulty walking due to peripheral neuropathy and/or cerebellar ataxia, and deafness due to auditory neuropathy. Additional features include cognitive impairment, cerebellar atrophy, dysarthria, abnormal extraocular movements, tremor, dysmetria and spasticity. The age at onset ranges from infancy to young adulthood. {ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228}. Note=The disease is caused by mutations affecting the gene represented in this entry. Deafness, X-linked, 5 (DFNX5) [MIM:300614]: A form of hearing loss characterized by absent or severely abnormal auditory brainstem response, abnormal middle ear reflexes, abnormal speech discrimination, loss of outer hair cell function, and cochlear nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with childhood onset, associated with distal sensory impairment affecting the peripheral nervous system. {ECO:0000269|PubMed:25986071}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-356440; Score: 0.35
DE  Interaction: O00165; IntAct: EBI-356440,EBI-357001; Score: 0.46
DE  Interaction: O15027; IntAct: EBI-356440,EBI-357515; Score: 0.46
DE  Interaction: O43715; IntAct: EBI-356440,EBI-2820212; Score: 0.35
DE  Interaction: Q9Y3Q8; IntAct: EBI-739485,EBI-356440; Score: 0.51
DE  Interaction: P13569; IntAct: EBI-349854,EBI-356440; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-356440; Score: 0.53
DE  Interaction: P09622; IntAct: EBI-353366,EBI-356440; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-715747,EBI-356440; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-6621955,EBI-356440; Score: 0.35
DE  Interaction: O43615; IntAct: EBI-356440,EBI-861737; Score: 0.35
DE  Interaction: Q8IXI1; IntAct: EBI-356440,EBI-1396563; Score: 0.46
DE  Interaction: Q7Z434; IntAct: EBI-356440,EBI-995373; Score: 0.35
DE  Interaction: P00403; IntAct: EBI-356440,EBI-2105756; Score: 0.46
DE  Interaction: Q6UXV4; IntAct: EBI-356440,EBI-9641073; Score: 0.35
DE  Interaction: O75431; IntAct: EBI-356440,EBI-7415268; Score: 0.35
DE  Interaction: Q9Y3D9; IntAct: EBI-356440,EBI-1054270; Score: 0.35
DE  Interaction: Q9NVH1; IntAct: EBI-356440,EBI-1055336; Score: 0.46
DE  Interaction: Q9BYN8; IntAct: EBI-356440,EBI-721378; Score: 0.35
DE  Interaction: Q99618; IntAct: EBI-356440,EBI-739534; Score: 0.35
DE  Interaction: Q96EY7; IntAct: EBI-356440,EBI-721110; Score: 0.35
DE  Interaction: Q8N4Q1; IntAct: EBI-356440,EBI-2562213; Score: 0.46
DE  Interaction: Q5JTV8; IntAct: EBI-356440,EBI-2559665; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-356440,EBI-473801; Score: 0.46
DE  Interaction: Q16775; IntAct: EBI-356440,EBI-3905342; Score: 0.35
DE  Interaction: Q15773; IntAct: EBI-356440,EBI-1051875; Score: 0.62
DE  Interaction: Q13011; IntAct: EBI-356440,EBI-711968; Score: 0.35
DE  Interaction: Q02952; IntAct: EBI-356440,EBI-2562430; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-356440,EBI-1050752; Score: 0.35
DE  Interaction: P50454; IntAct: EBI-356440,EBI-350723; Score: 0.35
DE  Interaction: P36542; IntAct: EBI-356440,EBI-711768; Score: 0.46
DE  Interaction: P31689; IntAct: EBI-356440,EBI-347834; Score: 0.35
DE  Interaction: P18085; IntAct: EBI-356440,EBI-1237085; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-356440,EBI-358933; Score: 0.35
DE  Interaction: P13804; IntAct: EBI-356440,EBI-1052886; Score: 0.35
DE  Interaction: O95721; IntAct: EBI-356440,EBI-490676; Score: 0.35
DE  Interaction: O76031; IntAct: EBI-356440,EBI-1052667; Score: 0.46
DE  Interaction: O75683; IntAct: EBI-356440,EBI-2691252; Score: 0.35
DE  Interaction: A8MXV4; IntAct: EBI-356440,EBI-11350801; Score: 0.35
DE  Interaction: Q9Y5L4; IntAct: EBI-356440,EBI-1057344; Score: 0.46
DE  Interaction: Q9Y5J9; IntAct: EBI-356440,EBI-1049085; Score: 0.46
DE  Interaction: Q9Y512; IntAct: EBI-356440,EBI-748409; Score: 0.46
DE  Interaction: Q9Y4W6; IntAct: EBI-356440,EBI-358755; Score: 0.35
DE  Interaction: Q9Y2W6; IntAct: EBI-356440,EBI-12842466; Score: 0.35
DE  Interaction: Q9Y2S7; IntAct: EBI-356440,EBI-713000; Score: 0.46
DE  Interaction: Q9Y2Q9; IntAct: EBI-356440,EBI-5325249; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-356440,EBI-357530; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-356440,EBI-1222503; Score: 0.35
DE  Interaction: Q9P0J0; IntAct: EBI-356440,EBI-372742; Score: 0.46
DE  Interaction: Q9P032; IntAct: EBI-356440,EBI-2606839; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-356440,EBI-743375; Score: 0.35
DE  Interaction: Q9NX40; IntAct: EBI-356440,EBI-2683029; Score: 0.35
DE  Interaction: Q9NX14; IntAct: EBI-356440,EBI-1246182; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-356440,EBI-352007; Score: 0.35
DE  Interaction: Q9NSE4; IntAct: EBI-356440,EBI-1054770; Score: 0.46
DE  Interaction: Q9NS69; IntAct: EBI-356440,EBI-1047508; Score: 0.35
DE  Interaction: Q9NPL8; IntAct: EBI-356440,EBI-6268651; Score: 0.35
DE  Interaction: Q9H845; IntAct: EBI-356440,EBI-2510719; Score: 0.35
DE  Interaction: Q9H078; IntAct: EBI-356440,EBI-2107221; Score: 0.46
DE  Interaction: Q9BW72; IntAct: EBI-356440,EBI-2867844; Score: 0.35
DE  Interaction: Q9BSH4; IntAct: EBI-356440,EBI-747797; Score: 0.35
DE  Interaction: Q9BPX6; IntAct: EBI-356440,EBI-2371996; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-356440,EBI-79964; Score: 0.35
DE  Interaction: Q96TA2; IntAct: EBI-356440,EBI-2818916; Score: 0.35
DE  Interaction: Q96EX1; IntAct: EBI-356440,EBI-2874543; Score: 0.35
DE  Interaction: Q96EL2; IntAct: EBI-356440,EBI-1055789; Score: 0.35
DE  Interaction: Q96E52; IntAct: EBI-356440,EBI-6570817; Score: 0.35
DE  Interaction: Q96C36; IntAct: EBI-356440,EBI-358366; Score: 0.35
DE  Interaction: Q96C01; IntAct: EBI-356440,EBI-373319; Score: 0.35
DE  Interaction: Q96BR5; IntAct: EBI-356440,EBI-6269632; Score: 0.35
DE  Interaction: Q96A73; IntAct: EBI-356440,EBI-725897; Score: 0.35
DE  Interaction: Q92667; IntAct: EBI-356440,EBI-2119593; Score: 0.35
DE  Interaction: Q92665; IntAct: EBI-356440,EBI-720602; Score: 0.35
DE  Interaction: Q8IYU8; IntAct: EBI-356440,EBI-3197790; Score: 0.35
DE  Interaction: Q8IUX1; IntAct: EBI-356440,EBI-2800657; Score: 0.35
DE  Interaction: Q86TX2; IntAct: EBI-356440,EBI-11109648; Score: 0.35
DE  Interaction: Q7L0Y3; IntAct: EBI-356440,EBI-2107046; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-356440,EBI-3248549; Score: 0.35
DE  Interaction: Q70CQ3; IntAct: EBI-356440,EBI-2512374; Score: 0.35
DE  Interaction: Q6UB35; IntAct: EBI-356440,EBI-1046835; Score: 0.46
DE  Interaction: Q6KCM7; IntAct: EBI-356440,EBI-11289059; Score: 0.35
DE  Interaction: Q6DKK2; IntAct: EBI-356440,EBI-948354; Score: 0.46
DE  Interaction: Q5TC12; IntAct: EBI-356440,EBI-1166891; Score: 0.35
DE  Interaction: Q5T9A4; IntAct: EBI-356440,EBI-1384144; Score: 0.35
DE  Interaction: Q5JTJ3; IntAct: EBI-356440,EBI-2874677; Score: 0.35
DE  Interaction: Q4VC31; IntAct: EBI-356440,EBI-1051617; Score: 0.35
DE  Interaction: Q49B96; IntAct: EBI-356440,EBI-16768453; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-356440,EBI-355175; Score: 0.35
DE  Interaction: Q16795; IntAct: EBI-356440,EBI-1045087; Score: 0.35
DE  Interaction: Q16740; IntAct: EBI-356440,EBI-1056029; Score: 0.35
DE  Interaction: Q16718; IntAct: EBI-356440,EBI-746417; Score: 0.35
DE  Interaction: Q14249; IntAct: EBI-356440,EBI-9369928; Score: 0.35
DE  Interaction: Q14061; IntAct: EBI-356440,EBI-711311; Score: 0.35
DE  Interaction: Q12849; IntAct: EBI-356440,EBI-1054150; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-356440,EBI-353460; Score: 0.35
DE  Interaction: P99999; IntAct: EBI-356440,EBI-446479; Score: 0.35
DE  Interaction: P83111; IntAct: EBI-356440,EBI-2878119; Score: 0.35
DE  Interaction: P62072; IntAct: EBI-356440,EBI-1200391; Score: 0.35
DE  Interaction: P61088; IntAct: EBI-356440,EBI-1052908; Score: 0.35
DE  Interaction: P56381; IntAct: EBI-356440,EBI-3904845; Score: 0.35
DE  Interaction: P56277; IntAct: EBI-356440,EBI-746397; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-356440,EBI-718281; Score: 0.35
DE  Interaction: P54819; IntAct: EBI-356440,EBI-1056291; Score: 0.46
DE  Interaction: P53701; IntAct: EBI-356440,EBI-10763431; Score: 0.35
DE  Interaction: P51970; IntAct: EBI-356440,EBI-1237250; Score: 0.46
DE  Interaction: P49821; IntAct: EBI-356440,EBI-748312; Score: 0.35
DE  Interaction: P49753; IntAct: EBI-356440,EBI-1052865; Score: 0.35
DE  Interaction: P48047; IntAct: EBI-356440,EBI-355815; Score: 0.35
DE  Interaction: P46199; IntAct: EBI-356440,EBI-359432; Score: 0.35
DE  Interaction: P38117; IntAct: EBI-356440,EBI-1056543; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-356440,EBI-351007; Score: 0.35
DE  Interaction: P36551; IntAct: EBI-356440,EBI-3907775; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-356440,EBI-354213; Score: 0.35
DE  Interaction: P34897; IntAct: EBI-356440,EBI-352908; Score: 0.35
DE  Interaction: P32322; IntAct: EBI-356440,EBI-848624; Score: 0.35
DE  Interaction: P31930; IntAct: EBI-356440,EBI-1052596; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-356440,EBI-1057265; Score: 0.35
DE  Interaction: P30405; IntAct: EBI-356440,EBI-5544229; Score: 0.35
DE  Interaction: P28331; IntAct: EBI-356440,EBI-1043922; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-356440,EBI-351437; Score: 0.35
DE  Interaction: P24539; IntAct: EBI-356440,EBI-1044810; Score: 0.35
DE  Interaction: P22695; IntAct: EBI-356440,EBI-1051424; Score: 0.35
DE  Interaction: P20674; IntAct: EBI-356440,EBI-715032; Score: 0.35
DE  Interaction: P19404; IntAct: EBI-356440,EBI-713665; Score: 0.35
DE  Interaction: P19367; IntAct: EBI-356440,EBI-713162; Score: 0.35
DE  Interaction: P18859; IntAct: EBI-356440,EBI-2606700; Score: 0.35
DE  Interaction: P14854; IntAct: EBI-356440,EBI-1047480; Score: 0.46
DE  Interaction: P13073; IntAct: EBI-356440,EBI-1056574; Score: 0.35
DE  Interaction: P10606; IntAct: EBI-356440,EBI-1053725; Score: 0.35
DE  Interaction: P10599; IntAct: EBI-356440,EBI-594644; Score: 0.46
DE  Interaction: P09669; IntAct: EBI-356440,EBI-715040; Score: 0.35
DE  Interaction: P08574; IntAct: EBI-356440,EBI-1224514; Score: 0.35
DE  Interaction: P07919; IntAct: EBI-356440,EBI-1224427; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-356440,EBI-356231; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-356440,EBI-358778; Score: 0.35
DE  Interaction: P00367; IntAct: EBI-356440,EBI-356544; Score: 0.35
DE  Interaction: O96008; IntAct: EBI-356440,EBI-1057581; Score: 0.46
DE  Interaction: O96000; IntAct: EBI-356440,EBI-1246371; Score: 0.35
DE  Interaction: O95202; IntAct: EBI-356440,EBI-1052895; Score: 0.35
DE  Interaction: O94925; IntAct: EBI-356440,EBI-1043737; Score: 0.35
DE  Interaction: O94826; IntAct: EBI-356440,EBI-2800236; Score: 0.35
DE  Interaction: O75964; IntAct: EBI-356440,EBI-1044001; Score: 0.35
DE  Interaction: O75947; IntAct: EBI-356440,EBI-724024; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-356440,EBI-1047585; Score: 0.35
DE  Interaction: O75616; IntAct: EBI-356440,EBI-6393536; Score: 0.46
DE  Interaction: O75489; IntAct: EBI-356440,EBI-1224896; Score: 0.35
DE  Interaction: O75380; IntAct: EBI-356440,EBI-719854; Score: 0.35
DE  Interaction: O75306; IntAct: EBI-356440,EBI-1224806; Score: 0.35
DE  Interaction: O60313; IntAct: EBI-356440,EBI-1054131; Score: 0.35
DE  Interaction: O60220; IntAct: EBI-356440,EBI-1049822; Score: 0.46
DE  Interaction: O43920; IntAct: EBI-356440,EBI-1246091; Score: 0.60
DE  Interaction: O43819; IntAct: EBI-356440,EBI-357012; Score: 0.46
DE  Interaction: O43464; IntAct: EBI-356440,EBI-517086; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-356440,EBI-724571; Score: 0.35
DE  Interaction: O00217; IntAct: EBI-356440,EBI-1246309; Score: 0.35
DE  Interaction: Q69YU5; IntAct: EBI-356440,EBI-16768469; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21259559,EBI-356440; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-356440; Score: 0.35
DE  Interaction: Q9BZR8; IntAct: EBI-1385773,EBI-356440; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-2807346,EBI-356440; Score: 0.35
DE  Interaction: Q96KQ7; IntAct: EBI-744366,EBI-356440; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-720706,EBI-356440; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-714746,EBI-356440; Score: 0.35
DE  Interaction: Q96JM2; IntAct: EBI-1210359,EBI-356440; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-4422308,EBI-356440; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-301713,EBI-356440; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-720768,EBI-356440; Score: 0.35
DE  Interaction: P40692; IntAct: EBI-744248,EBI-356440; Score: 0.37
DE  Interaction: O95166; IntAct: EBI-712001,EBI-356440; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-746969,EBI-356440; Score: 0.35
DE  Interaction: Q8N0X7; IntAct: EBI-2643803,EBI-356440; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-356440; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-494830,EBI-356440; Score: 0.35
DE  Interaction: P83887; IntAct: EBI-2553410,EBI-356440; Score: 0.40
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-356440; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-2514016,EBI-356440; Score: 0.35
DE  Interaction: P10398; IntAct: EBI-365961,EBI-356440; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-747644,EBI-356440; Score: 0.53
DE  Interaction: P51617; IntAct: EBI-358664,EBI-356440; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-356440; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-356440,EBI-932603; Score: 0.35
DE  Interaction: P53004; IntAct: EBI-356440,EBI-7410441; Score: 0.35
DE  Interaction: Q9HAV7; IntAct: EBI-356440,EBI-1043499; Score: 0.35
DE  Interaction: Q9H0I3; IntAct: EBI-356440,EBI-715690; Score: 0.35
DE  Interaction: Q92522; IntAct: EBI-356440,EBI-876335; Score: 0.35
DE  Interaction: P83881; IntAct: EBI-356440,EBI-1054835; Score: 0.35
DE  Interaction: P61604; IntAct: EBI-356440,EBI-711483; Score: 0.35
DE  Interaction: P27694; IntAct: EBI-356440,EBI-621389; Score: 0.35
DE  Interaction: P35244; IntAct: EBI-356440,EBI-621428; Score: 0.35
DE  Interaction: P15927; IntAct: EBI-356440,EBI-621404; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-356440,EBI-351479; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-356440,EBI-2689235; Score: 0.35
DE  Interaction: Q96HS1; IntAct: EBI-356440,EBI-713608; Score: 0.35
DE  Interaction: Q6PI48; IntAct: EBI-356440,EBI-3917045; Score: 0.35
DE  Interaction: Q10713; IntAct: EBI-356440,EBI-2514696; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-356440,EBI-359097; Score: 0.35
DE  Interaction: P18887; IntAct: EBI-356440,EBI-947466; Score: 0.35
DE  Interaction: P0DMV8; IntAct: EBI-356440,EBI-11052499; Score: 0.35
DE  Interaction: P00374; IntAct: EBI-356440,EBI-10039315; Score: 0.35
DE  Interaction: O43813; IntAct: EBI-356440,EBI-3046631; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-356440,EBI-354022; Score: 0.35
DE  Interaction: O95831-1; IntAct: EBI-5456281,EBI-356440; Score: 0.40
DE  Interaction: O95831-3; IntAct: EBI-5651213,EBI-356440; Score: 0.40
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-356440; Score: 0.35
DE  Interaction: Q8JPQ9; IntAct: EBI-6152703,EBI-356440; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-356440; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-359390,EBI-356440; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-1057139,EBI-356440; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-356440; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-356440; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-356440; Score: 0.35
DE  Interaction: O95747; IntAct: EBI-620853,EBI-356440; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-356440; Score: 0.35
DE  Interaction: Q15047; IntAct: EBI-79691,EBI-356440; Score: 0.37
DE  Interaction: O76061; IntAct: EBI-713858,EBI-356440; Score: 0.37
DE  Interaction: Q92956; IntAct: EBI-356440,EBI-1056653; Score: 0.40
DE  Interaction: Q9BUV8; IntAct: EBI-356440,EBI-1050079; Score: 0.40
DE  Interaction: P01889; IntAct: EBI-356440,EBI-1046513; Score: 0.40
DE  Interaction: Q9HAW0; IntAct: EBI-356440,EBI-1055224; Score: 0.40
DE  Interaction: Q9BRX2; IntAct: EBI-356440,EBI-1043580; Score: 0.40
DE  Interaction: O75365; IntAct: EBI-356440,EBI-1043866; Score: 0.40
DE  Interaction: Q8NC60; IntAct: EBI-717871,EBI-356440; Score: 0.37
DE  Interaction: Q8IX03; IntAct: EBI-715828,EBI-356440; Score: 0.37
DE  Interaction: Q13547; IntAct: EBI-301834,EBI-356440; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-295351,EBI-356440; Score: 0.35
DE  Interaction: Q13322; IntAct: EBI-80275,EBI-356440; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-1307,EBI-356440; Score: 0.35
DE  Interaction: P05129; IntAct: EBI-949799,EBI-356440; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-365996,EBI-356440; Score: 0.35
DE  Interaction: Q9Y6X8; IntAct: EBI-356440,EBI-948566; Score: 0.40
DE  Interaction: Q8IYE1; IntAct: EBI-356440,EBI-10961312; Score: 0.40
DE  Interaction: Q9H2G2; IntAct: EBI-356440,EBI-1022272; Score: 0.40
DE  Interaction: Q13061; IntAct: EBI-356440,EBI-10757323; Score: 0.40
DE  Interaction: Q9HCD5; IntAct: EBI-356440,EBI-2863498; Score: 0.40
DE  Interaction: O75311; IntAct: EBI-356440,EBI-16357053; Score: 0.40
DE  Interaction: P08621; IntAct: EBI-1049228,EBI-356440; Score: 0.40
DE  Interaction: Q86X27; IntAct: EBI-356440,EBI-1050841; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475880,EBI-356440; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-356440,EBI-437708; Score: 0.46
DE  Interaction: Q13509; IntAct: EBI-350989,EBI-356440; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-356440; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-2931238,EBI-356440; Score: 0.35
DE  Interaction: Q9NX70; IntAct: EBI-394656,EBI-356440; Score: 0.35
DE  Interaction: Q04206-2; IntAct: EBI-356440,EBI-289947; Score: 0.40
DE  Interaction: Q9Y572; IntAct: EBI-356440,EBI-298250; Score: 0.40
DE  Interaction: P20333; IntAct: EBI-356440,EBI-358983; Score: 0.40
DE  Interaction: Q13233; IntAct: EBI-356440,EBI-49776; Score: 0.40
DE  Interaction: Q99759; IntAct: EBI-356440,EBI-307281; Score: 0.40
DE  Interaction: Q00653; IntAct: EBI-356440,EBI-307326; Score: 0.40
DE  Interaction: Q15628; IntAct: EBI-356440,EBI-359215; Score: 0.40
GO  GO:0005829;
GO  GO:0005743;
GO  GO:0005758;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0071949;
GO  GO:0016174;
GO  GO:0016651;
GO  GO:0046983;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1904045;
GO  GO:0071392;
GO  GO:0070301;
GO  GO:0071732;
GO  GO:0090650;
GO  GO:0030261;
GO  GO:0070059;
GO  GO:0033108;
GO  GO:0032981;
GO  GO:0051402;
GO  GO:0030182;
GO  GO:0055114;
GO  GO:0043065;
GO  GO:0043525;
GO  GO:0045041;
GO  GO:1902510;
GO  GO:0002931;
GO  GO:1902065;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGA
SQ  GAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVL
SQ  IVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRD
SQ  NMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALG
SQ  RKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGL
SQ  EPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQS
SQ  MFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDY
SQ  GKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
//
ID  Q70KF4;
PN  Cardiomyopathy-associated protein 5;
GN  Cmya5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes. In skeletal muscles, localizes along myofiber periphery, at costameres. Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. In the mdx mouse model for Duchenne muscular dystrophy, exhibits a discontinuous localization at the myofiber periphery with extensive regions devoid of CMYA5. This highly irregular pattern is associated with an increased cytoplasmic localization, particularly in discrete foci within myofibers. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}.
DR  UNIPROT: Q70KF4;
DR  UNIPROT: Q70X91;
DR  UNIPROT: Q9CV01;
DR  UNIPROT: Q9CV02;
DR  UNIPROT: Q9ER93;
DR  UNIPROT: Q9ER96;
DR  Pfam: PF00041;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DE  Function: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration. Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle. {ECO:0000269|PubMed:17499862, ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:28740084}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-782290,EBI-782290; Score: 0.37
DE  Interaction: Q91WZ8; IntAct: EBI-782290,EBI-643186; Score: 0.59
GO  GO:0043034;
GO  GO:0031430;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
GO  GO:0042802;
GO  GO:0070885;
GO  GO:0032515;
GO  GO:0014733;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESGDSGLAAQGFLGWGADEEVAQELETEEESEGEGEETAAESEEEPDARLSDEDEEGKTKQECIVSDPSFSMVAVQRED
SQ  SGITWETNSSRSSTPWASGESQTSGICSLEGSALTSPPGSVSFIMDEVKRTRKRTQKSKRGSPSLRRKGSKKRNSLESQD
SQ  VLTNQEDGPSISESPVLNIENEKSSIGTYDKTRRKKTASNTPPITGAIYKEHKPLVLKPVYIGTVQYKIKMFNSVKEELI
SQ  PLQFYGTLPKGYVIKEIHYRRGKDSSISLEPDLSNGGSNIVPQRKLAQSPEEDKVRELAPPWRGALSKGSRTSLFSHEEQ
SQ  KKTYADSNLNVPSSTEHAFPSSARNDTADQEENLSLPQMMPQQPADESKTHRMEPPSIPATMVLERAKEELEQNAQGKES
SQ  SEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFEPDMEGLEPISTEKTEQASEYVTSSEPIV
SQ  HREEEHAPEPIVHREEEHAPEPIVHREEEHAPEPESIVHREEEHAPESIVHREEEHAPEPVPIVHREEEHAPEPESIVHR
SQ  EEEHAPEPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPESIVRKGEEHAPEPIVHREEEQVP
SQ  EPESIVHREEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPMVLREEHAPEPIVRREEEHAPEPIVHREEEHAPEPMVH
SQ  RKAQQLERGVETSTPITDITEPEDSSLEEEIIELDYPESPLASKETSPSPLSPEVEHRKEPILPTQMTFTPERITLSEEE
SQ  REENESVSTDSAFVSEYSVLQDLNHTPEKLEVEAVSVSDVKSSNEPAVFSEDDEERESYSPAMTSVSEQSLSPSTTEKTS
SQ  AIQSPLFSTVSPVLSGDEASENVCHSPESESAAEYSVPAHAQELLLKTGDHKLPLKSQRVSEPIIQAEDEKEDIGLLPPA
SQ  ALSQAVLSEDESLGSGSFASDSKLPFKPSVSQNATRESPQKTIDDMPQFKPRGLSDPATLLEEEKEAIGVGLSSSNEVSA
SQ  VECALPPQTTELLSESHAPPPWAISSEQVVQSEEGSRDQQRGSFSSTPELGHTSLLLKGASSPTGLSEQGQEEDNIGPLS
SQ  PDSAFASEFSFSPYPTQELEKRELGRDSPLCLTSPSEQTVLSEEDTEEADLFSPDSASQVSIPPYRIAETEQNKVEPDEL
SQ  LPTRSAPDYPYFSEADEEEAGSSVVTLVPEHSEPSQEREESSPCRPVFEDLSLPPSADKTGQAETMSDVPTISTSVSEYL
SQ  ILARQAKTQASLEPEAEDLVPPPTSGWEKRDAKSSLPAVTIAASSSALSSVVKEETTSVLPTSQPSVSPESTCVLKPEQE
SQ  PTAPLTLTSADEQMALPRVGREKAVLDSQEATAHKSQDQTPEPRLPNVPGSGMKYSVLSDLGDEPKADVKLNLAPTVTSE
SQ  LEQRMLSKNEPEVAKPHSPPEETSISGPKVLSAVKTEVKQESKITRELPAASSGRERGAEHSPPVPPALPALTEETGKDT
SQ  EASSSATTVPVTKLDSNSTKLGRDEVLTDPSLASPVEHPGLKGIGKSELGSGLPLPSMSASEVLRPEPKLPVNSGVEVER
SQ  EDNEPPPLQVSPTSKPTVPNDKHEEITRSPDSENLVSDDLAPTLLAFRHEMNRQAEETSSPVPGSFLSGEQELIKLPPEP
SQ  EKHKQLSEVPTAGSELIDSRDRDRSLGIEPVKPIGTEPGPSILEKGPAELQRRGKEQEENRKLPVPASAPLETASFDLPI
SQ  EQKEPKRTLHEGQAVEVPDESSSSADKPELGVKQLAEKKENLEQPKPFVTTERASVTGSKVKESLISPKDNIWMLEKPDG
SQ  LVNQHEDRKPGTGQLESSESTDLMSEKLGAASLDTDHTSETRNQETSKAPVSGEKLSQEPRRVQSKAVDDSEEGRKLASG
SQ  NVEVLTQSKSVPAVKAKATPQPPETPEVTQKPSEKSLVTEQGLPAEKGKKGISSFKSWMSSLLFGSSIPDSKVSDNEDLE
SQ  TRPGPSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPKGVSVKSSISQDLKEKLTFLSNEDVLKQPKSNSE
SQ  NYGQKELPGFSEGMGESLATSVGDKHPGIHPCSPMGEKVGMEEAQNMAPLHITESQRRQKPEVSPPSMWNISARKEEPSS
SQ  DHKETWLSSSDVVDRMPQKPKSAQSAFTRMNSEEPASMILPVESKGSLSDLGEDRLRQEMPKPTSLEHCEEEVERPTEEK
SQ  DGWETRSFSLAGKRGLAEKQEIMAPLELRENEAVGELQRMPESRPFKLEESKAAERLEQRISPTEKLMEKPSKTLALDRR
SQ  EKEVQEWVFSEGEKQEYPPAAMPVPGASAVSLDKAQPHLLAKPTPVVEKPEHIVTEVYPEIRERKAAETQPHPQEEGKTL
SQ  VEKTKVSRVESPHGEETDGHSLTQEGNLELEKSGESRVDLKEERRRFVMPELPLGASVAAEDGSVQPRPLSKDAARASDM
SQ  TDETKHLGTPPTQPSAVEPQTLVLGTSVEHAVKKQETWSDRPTVHTFQTSKDDTEEMLKQSVLISKHHLEAVEDVHRNEP
SQ  PSSAASNYAQFMLSASEISADGVPPMGGTAQEPEGTSVKDEEFSVTSKPAGLSEDQKSAFSIISEGCEILNIHAPAFIPS
SQ  VDQEESEQMQDKLQYLEEKASFKSISVHDEKKAAASHKTQKSKLEVPDRKITSLKENKTKETHKTKEEIATDSGMGDFTP
SQ  IQPTVSGEEDYFEKYTLIDYNLSPGSGKQKSTVEESSEEATKTLTSFPESSAEQALDHEYNLVKLDESFYGPEKDDSKLS
SQ  HAEMQKSLAIQKPDDRNAPKGISRDVDSRSPGMPLFDVEEGVLSKRQIFPTTPKAVNPELLEEPPALSFFYKDLYEGACG
SQ  EKNEGETASEGDSVDSETSFPRRHSDTDDGPGMYFEKYILKDDILHDESVTQEDQGQGLEEKPVGEEDSQQLRVAEREIR
SQ  RKPETSFWEKNLEEQHKVVGREGEPTGHMETLDEAAMQQKAPITEQVRAVTQKMSYAVPFQDTRCVLESEPSSQGNEAGN
SQ  ASPDVNLNVPVQVSFPEEESAAGATYAPEVLQERLVPSVSREERLHNTPVQDEYDFVGSLNQEAASQAILPEEPGSESSP
SQ  KEVLSQGSESFEHIREQELTSEGEPRMSASQEVWDRTEDQSARESVTAKTQKEPKKTQAESYCYTCKSLVSEMDKALDIH
SQ  KDHEVSALDTAISAVKVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSF
SQ  EEVKKKKMEFLHDQMVHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAMESTASLENMPAAFSLFEHYDD
SQ  SSARSDQMLKQVAVPQPPRLEPQEPSSATSTTIAVYWSVNKEDVVDSFQVYCVEEPQDDQEINELVEEYRLTVKESCCIF
SQ  EDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIHVEDCTVCWNTATVRWRPANPEATETYTLEYCRQHSPEGEG
SQ  LRSFSGIKGHQLKVNLPPNDNYFFYVRATNASGTSEQSEAALISTRGTRFLLLRETAHPALQISANGTVISFSERRRLTE
SQ  IPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGIVSEVHATERPARVG
SQ  ILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPGRCTLHLGLEPPDSVRHK
//
ID  P34689;
PN  ATP-dependent RNA helicase glh-1;
GN  glh;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21402787}. Cytoplasmic granule {ECO:0000269|PubMed:17699606}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17699606}. Note=Perinuclear localization in germ cells but disperses into particles in cellularized oocytes. Component of P granules. {ECO:0000269|PubMed:17699606}.
DR  UNIPROT: P34689;
DR  UNIPROT: Q22873;
DR  UNIPROT: Q7KQH5;
DR  UNIPROT: Q9TXH4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  Pfam: PF00098;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DR  PROSITE: PS50158;
DE  Function: Probable ATP-binding RNA helicase (PubMed:8415696). May act redundantly with the P-granule component glh-4 to regulate the formation of the granular structure of P-granules in embryos (PubMed:21402787, PubMed:24746798). May play a role in transgenerational epigenetic inheritance (PubMed:28533440). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246). {ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246, ECO:0000305|PubMed:28533440, ECO:0000305|PubMed:8415696}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0017151;
GO  GO:0008432;
GO  GO:0043621;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0008270;
GO  GO:0030154;
GO  GO:0007276;
GO  GO:0007281;
GO  GO:0009791;
GO  GO:0016070;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDGWSDSESAAKAKTGFGSGGGFGGGNNGGSGFGGGKNGGTGFGGGNTGGSGFGGGNTGGSGFGGGKTGGSGFGGGNTC
SQ  GSGFGGGSTGGSPYGGASSGFGGSTATSGFGSGEKSSAFGGSGGFGGSATGFGSGGGSFGGGNSGFGEGGHGGGERNNNC
SQ  FNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDGGFGGGEERG
SQ  PMKCFNCKGEGHRSAECPEPPRGCFNCGEQGHRSNECPNPAKPREGVEGEGPKATYVPVEDNMEDVFNMQKISEGLMFNK
SQ  FFDAEVKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIM
SQ  TRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIK
SQ  HFCEEGTIKLDKCRFFVLDEADRMIDAMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAID
SQ  KIGAANKCVLQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAR
SQ  EQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDCSLLSEL
SQ  VGVLADAQQIVPDWMQGAAGGNYGASGFGSSVPTQVPQDEEGW
//
ID  O95528;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  SLC2A10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}.
DR  UNIPROT: O95528;
DR  UNIPROT: A8K4J6;
DR  UNIPROT: Q3MIX5;
DR  UNIPROT: Q9H4I6;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  OMIM: 208050;
DR  OMIM: 606145;
DR  DisGeNET: 81031;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:11592815, ECO:0000269|PubMed:16550171}.
DE  Disease: Arterial tortuosity syndrome (ATORS) [MIM:208050]: An autosomal recessive disorder characterized by tortuosity and elongation of major arteries, often resulting in death at young age. Other typical features include aneurysms of large arteries and stenosis of the pulmonary artery, in association with facial features and several connective tissue manifestations such as soft skin and joint laxity. Histopathological findings include fragmentation of elastic fibers in the tunica media of large arteries. {ECO:0000269|PubMed:16550171, ECO:0000269|PubMed:17935213}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005351;
GO  GO:0046323;
GO  GO:1904659;
GO  GO:0008645;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILG
SQ  SNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGT
SQ  PWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVL
SQ  FQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFA
SQ  VPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPL
SQ  PARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFL
SQ  LYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS
//
ID  Q07065;
PN  Cytoskeleton-associated protein 4;
GN  CKAP4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation.
DR  UNIPROT: Q07065;
DR  UNIPROT: Q504S5;
DR  UNIPROT: Q53ES6;
DR  OMIM: 618595;
DR  DisGeNET: 10970;
DE  Function: High-affinity epithelial cell surface receptor for APF. Mediates the anchoring of the endoplasmic reticulum to microtubules.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-702400; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-2849976,EBI-702400; Score: 0.35
DE  Interaction: O76050; IntAct: EBI-702400,EBI-2129917; Score: 0.40
DE  Interaction: P00519; IntAct: EBI-375543,EBI-702400; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-297353,EBI-702400; Score: 0.35
DE  Interaction: Self; IntAct: EBI-702400,EBI-702400; Score: 0.37
DE  Interaction: P49407; IntAct: EBI-743313,EBI-702400; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-715747,EBI-702400; Score: 0.35
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-702400; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-702400; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-1057265,EBI-702400; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-351007,EBI-702400; Score: 0.35
DE  Interaction: P25100; IntAct: EBI-489993,EBI-702400; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-702400; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-702400; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-307486,EBI-702400; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-714746,EBI-702400; Score: 0.35
DE  Interaction: Q8IYT8; IntAct: EBI-714340,EBI-702400; Score: 0.35
DE  Interaction: P40692; IntAct: EBI-744248,EBI-702400; Score: 0.37
DE  Interaction: P60520; IntAct: EBI-720116,EBI-702400; Score: 0.35
DE  Interaction: Q70EL3; IntAct: EBI-2512953,EBI-702400; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-447544,EBI-702400; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-2551936,EBI-702400; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-702400; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11333674,EBI-702400; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-11334880,EBI-702400; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-702400; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-4402607,EBI-702400; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-702400; Score: 0.35
DE  Interaction: Q96Q45; IntAct: EBI-2602465,EBI-702400; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-702400; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-702400; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-2512037,EBI-702400; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-2551532,EBI-702400; Score: 0.35
DE  Interaction: Q3UJU9; IntAct: EBI-2554307,EBI-702400; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-998894,EBI-702400; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104531,EBI-702400; Score: 0.35
DE  Interaction: O60307; IntAct: EBI-311420,EBI-702400; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-1054923,EBI-702400; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-1056089,EBI-702400; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-8322817,EBI-702400; Score: 0.35
DE  Interaction: Q16513; IntAct: EBI-2511350,EBI-702400; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-2553509,EBI-702400; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-1059156,EBI-702400; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-359031,EBI-702400; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-6163737,EBI-702400; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-5347760,EBI-702400; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135403,EBI-702400; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-702400; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-702400; Score: 0.46
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-702400; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-1047508,EBI-702400; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-702400; Score: 0.46
DE  Interaction: Q96I36; IntAct: EBI-6570698,EBI-702400; Score: 0.35
DE  Interaction: P13073; IntAct: EBI-1056574,EBI-702400; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-702400; Score: 0.35
DE  Interaction: Q99689; IntAct: EBI-396435,EBI-702400; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-2561547,EBI-702400; Score: 0.35
DE  Interaction: Q9Y6Z7; IntAct: EBI-21859492,EBI-702400; Score: 0.35
DE  Interaction: Q9BZR6; IntAct: EBI-5240240,EBI-702400; Score: 0.35
DE  Interaction: Q5BJH7-3; IntAct: EBI-11127237,EBI-702400; Score: 0.35
DE  Interaction: P50876; IntAct: EBI-702400,EBI-2340657; Score: 0.40
DE  Interaction: O60858-3; IntAct: EBI-21523829,EBI-702400; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-740282,EBI-702400; Score: 0.35
DE  Interaction: P08842; IntAct: EBI-7183227,EBI-702400; Score: 0.35
DE  Interaction: P51888; IntAct: EBI-2827057,EBI-702400; Score: 0.35
DE  Interaction: P04578; IntAct: EBI-6163496,EBI-702400; Score: 0.46
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-702400; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-702400; Score: 0.35
DE  Interaction: P17568; IntAct: EBI-1246238,EBI-702400; Score: 0.37
DE  Interaction: Q14764; IntAct: EBI-2816254,EBI-702400; Score: 0.37
DE  Interaction: P18848; IntAct: EBI-492498,EBI-702400; Score: 0.37
DE  Interaction: Q9Y3C0; IntAct: EBI-712969,EBI-702400; Score: 0.37
DE  Interaction: P81172; IntAct: EBI-702400,EBI-3942179; Score: 0.37
DE  Interaction: Q6I9Y2; IntAct: EBI-716286,EBI-702400; Score: 0.37
DE  Interaction: Q9H1I8; IntAct: EBI-702400,EBI-711197; Score: 0.37
DE  Interaction: P21675; IntAct: EBI-702400,EBI-491289; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-358372,EBI-702400; Score: 0.40
DE  Interaction: Q6NUK1; IntAct: EBI-702400,EBI-4289949; Score: 0.40
DE  Interaction: Q8IVJ8; IntAct: EBI-702400,EBI-20844837; Score: 0.40
DE  Interaction: Q96NB3; IntAct: EBI-702400,EBI-3920997; Score: 0.40
DE  Interaction: Q9UKU6; IntAct: EBI-702400,EBI-2679650; Score: 0.40
DE  Interaction: Q8WXX0; IntAct: EBI-702400,EBI-1046155; Score: 0.40
DE  Interaction: P04275; IntAct: EBI-702400,EBI-981819; Score: 0.40
DE  Interaction: A6NNW6; IntAct: EBI-702400,EBI-20833177; Score: 0.40
DE  Interaction: Q9ULG1; IntAct: EBI-702400,EBI-769345; Score: 0.40
DE  Interaction: P29475; IntAct: EBI-7164065,EBI-702400; Score: 0.40
DE  Interaction: Q640N3-2; IntAct: EBI-25409036,EBI-702400; Score: 0.35
DE  Interaction: Q5FWK3; IntAct: EBI-17170552,EBI-702400; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-702400; Score: 0.35
DE  Interaction: Q92633; IntAct: EBI-3908414,EBI-702400; Score: 0.35
DE  Interaction: Q9H8X2; IntAct: EBI-8786596,EBI-702400; Score: 0.35
DE  Interaction: Q16581; IntAct: EBI-21515121,EBI-702400; Score: 0.35
DE  Interaction: Q6P5W5-2; IntAct: EBI-21515953,EBI-702400; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-9008641,EBI-702400; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-394678,EBI-702400; Score: 0.35
DE  Interaction: P30825; IntAct: EBI-4289564,EBI-702400; Score: 0.35
DE  Interaction: A2A2Y4-2; IntAct: EBI-21527498,EBI-702400; Score: 0.35
DE  Interaction: O75326; IntAct: EBI-1753538,EBI-702400; Score: 0.35
DE  Interaction: Q8WWF3; IntAct: EBI-17280858,EBI-702400; Score: 0.35
DE  Interaction: P49796-4; IntAct: EBI-12006708,EBI-702400; Score: 0.35
DE  Interaction: Q86Y78; IntAct: EBI-14035066,EBI-702400; Score: 0.35
DE  Interaction: O14763-2; IntAct: EBI-21548444,EBI-702400; Score: 0.35
DE  Interaction: Q16322; IntAct: EBI-12265328,EBI-702400; Score: 0.35
DE  Interaction: O94766; IntAct: EBI-3917958,EBI-702400; Score: 0.35
DE  Interaction: Q99871-2; IntAct: EBI-21525681,EBI-702400; Score: 0.35
DE  Interaction: Q7LGA3; IntAct: EBI-5461291,EBI-702400; Score: 0.35
DE  Interaction: Q99598; IntAct: EBI-742638,EBI-702400; Score: 0.37
GO  GO:0035577;
GO  GO:0036464;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0042599;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0035579;
GO  GO:0003723;
GO  GO:0044267;
GO  GO:0043312;
GO  GO:0043687;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSS
SQ  SSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQ
SQ  KVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEER
SQ  LTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESD
SQ  IYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFE
SQ  ALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQL
SQ  VLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSL
SQ  VAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV
//
ID  Q17RY0;
PN  Cytoplasmic polyadenylation element-binding protein 4;
GN  CPEB4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Cell junction, synapse, postsynaptic density {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TN98}.
DR  UNIPROT: Q17RY0;
DR  UNIPROT: B7ZLQ7;
DR  UNIPROT: Q7Z310;
DR  UNIPROT: Q8N405;
DR  UNIPROT: Q9C0J0;
DR  PDB: 2MKI;
DR  PDB: 2MKJ;
DR  PDB: 5DIF;
DR  Pfam: PF16366;
DR  Pfam: PF16367;
DR  PROSITE: PS50102;
DR  OMIM: 610607;
DR  DisGeNET: 80315;
DE  Function: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (PubMed:24990967). RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (PubMed:24990967). Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE- regulated mRNAs in conditions in which global protein synthesis is inhibited (By similarity). Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (PubMed:26398195). Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752). Stimulates proliferation of melanocytes (PubMed:27857118). In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (By similarity). {ECO:0000250|UniProtKB:Q7TN98, ECO:0000269|PubMed:22138752, ECO:0000269|PubMed:24990967, ECO:0000269|PubMed:26398195, ECO:0000269|PubMed:27857118}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZNJ1; IntAct: EBI-2862306,EBI-2848203; Score: 0.35
DE  Interaction: Q9H4B6; IntAct: EBI-1017775,EBI-2848203; Score: 0.35
DE  Interaction: Q9H6Z9; IntAct: EBI-1175354,EBI-2848203; Score: 0.35
DE  Interaction: Q8D052; IntAct: EBI-2844272,EBI-2848203; Score: 0.37
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005783;
GO  GO:0030426;
GO  GO:1990124;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0046872;
GO  GO:0003730;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008135;
GO  GO:0000900;
GO  GO:0071230;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0035235;
GO  GO:2000766;
GO  GO:0043524;
GO  GO:0002931;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKA
SQ  KSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTS
SQ  SASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQ
SQ  HHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRG
SQ  LNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDT
SQ  IKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLP
SQ  PDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRP
SQ  WNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAIS
SQ  ARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDR
SQ  PRHISFRWN
//
ID  Q5FVP8;
PN  Diacylglycerol O-acyltransferase 2;
GN  Dgat2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q5FVP8;
DR  UNIPROT: Q8K4Y4;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96PD7}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:1990578;
GO  GO:0048471;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0042803;
GO  GO:0050252;
GO  GO:0071400;
GO  GO:0035356;
GO  GO:0042632;
GO  GO:0046339;
GO  GO:0060613;
GO  GO:0055089;
GO  GO:0006071;
GO  GO:0019915;
GO  GO:0035336;
GO  GO:0034383;
GO  GO:0046322;
GO  GO:0045722;
GO  GO:0010867;
GO  GO:0090181;
GO  GO:0050746;
GO  GO:0097006;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKHLQVISVLQWVLSF
SQ  LVLGVACSVILMYTFCTDCWLIAALYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGY
SQ  HPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIVIVVGG
SQ  AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLF
SQ  SSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHTMYMEALVKLFDNHKTKFGLPETEVLEVN
//
ID  Q03001;
PN  Dystonin;
GN  DST;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Cell projection, axon {ECO:0000250|UniProtKB:Q91ZU6}. Note=Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. {ECO:0000250}. [Isoform 2]: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic actin filaments. {ECO:0000250}. [Isoform 3]: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Localizes to actin and intermediate filaments cytoskeletons (By similarity). Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes. {ECO:0000250}. [Isoform 6]: Nucleus {ECO:0000250|UniProtKB:Q91ZU6}. Nucleus envelope {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}; Single-pass membrane protein {ECO:0000269|PubMed:10428034}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q91ZU6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q91ZU6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Note=Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 7]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Cell projection, axon {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}. Note=Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons. [Isoform 8]: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
DR  UNIPROT: Q03001;
DR  UNIPROT: B7Z3H1;
DR  UNIPROT: E7ERU0;
DR  UNIPROT: O94833;
DR  UNIPROT: Q12825;
DR  UNIPROT: Q13266;
DR  UNIPROT: Q13267;
DR  UNIPROT: Q13775;
DR  UNIPROT: Q5TBT0;
DR  UNIPROT: Q5TBT2;
DR  UNIPROT: Q5TF23;
DR  UNIPROT: Q5TF24;
DR  UNIPROT: Q8N1T8;
DR  UNIPROT: Q8N8J3;
DR  UNIPROT: Q8WXK8;
DR  UNIPROT: Q8WXK9;
DR  UNIPROT: Q96AK9;
DR  UNIPROT: Q96DQ5;
DR  UNIPROT: Q96J76;
DR  UNIPROT: Q96QT5;
DR  UNIPROT: Q9H555;
DR  UNIPROT: Q9UGD7;
DR  UNIPROT: Q9UGD8;
DR  UNIPROT: Q9UN10;
DR  PDB: 3GJO;
DR  Pfam: PF00307;
DR  Pfam: PF13499;
DR  Pfam: PF02187;
DR  Pfam: PF00681;
DR  Pfam: PF17902;
DR  Pfam: PF00435;
DR  Pfam: PF18373;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51460;
DR  PROSITE: PS50002;
DR  OMIM: 113810;
DR  OMIM: 614653;
DR  OMIM: 615425;
DR  DisGeNET: 667;
DE  Function: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 3]: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. [Isoform 6]: required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}. [Isoform 7]: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.
DE  Disease: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe autosomal recessive disorder characterized by neonatal hypotonia, respiratory and feeding difficulties, lack of psychomotor development, and autonomic abnormalities including labile cardiovascular function, lack of corneal reflexes leading to corneal scarring, areflexia, and absent axonal flare response after intradermal histamine injection. {ECO:0000269|PubMed:22522446}. Note=The disease is caused by mutations affecting the gene represented in this entry. Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2) [MIM:615425]: A form of epidermolysis bullosa, a dermatologic disorder characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet. EBSB2 is characterized by trauma-induced blistering mainly occurring on the feet and ankles. Ultrastructural analysis of skin biopsy shows abnormal hemidesmosomes with poorly formed inner plaques. {ECO:0000269|PubMed:20164846, ECO:0000269|PubMed:22113475}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-296723,EBI-310758; Score: 0.37
DE  Interaction: P04626; IntAct: EBI-310758,EBI-641062; Score: 0.37
DE  Interaction: P51151; IntAct: EBI-4401353,EBI-310758; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-310758; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-310758,EBI-529989; Score: 0.55
DE  Interaction: Q8TDR0-2; IntAct: EBI-310758,EBI-11946508; Score: 0.37
DE  Interaction: Q9UKE5; IntAct: EBI-310758,EBI-1051794; Score: 0.55
DE  Interaction: Q96AC1; IntAct: EBI-310758,EBI-4399465; Score: 0.37
DE  Interaction: Q99459; IntAct: EBI-310758,EBI-374880; Score: 0.37
DE  Interaction: O60239; IntAct: EBI-310758,EBI-624860; Score: 0.37
DE  Interaction: Q96MT8-2; IntAct: EBI-310758,EBI-21369329; Score: 0.37
DE  Interaction: P61764; IntAct: EBI-310758,EBI-960169; Score: 0.37
DE  Interaction: Q9NV70; IntAct: EBI-310758,EBI-1045313; Score: 0.55
DE  Interaction: Q96BS2; IntAct: EBI-310758,EBI-740653; Score: 0.37
DE  Interaction: Q9BY11; IntAct: EBI-310758,EBI-721769; Score: 0.37
DE  Interaction: P13569; IntAct: EBI-349854,EBI-310758; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-1564650,EBI-310758; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-2800296,EBI-310758; Score: 0.35
DE  Interaction: Q9H8S9; IntAct: EBI-748229,EBI-310758; Score: 0.35
DE  Interaction: Q7L9L4; IntAct: EBI-2558745,EBI-310758; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-310758,EBI-6927928; Score: 0.37
DE  Interaction: P29991; IntAct: EBI-310758,EBI-8826488; Score: 0.37
DE  Interaction: Q13951; IntAct: EBI-310758,EBI-718750; Score: 0.40
DE  Interaction: P25054; IntAct: EBI-310758,EBI-727707; Score: 0.37
DE  Interaction: Q16659; IntAct: EBI-1384105,EBI-310758; Score: 0.37
DE  Interaction: Q13952; IntAct: EBI-310758,EBI-389755; Score: 0.37
DE  Interaction: Q13177; IntAct: EBI-310758,EBI-1045887; Score: 0.37
DE  Interaction: Q15691; IntAct: EBI-310758,EBI-1004115; Score: 0.73
DE  Interaction: P19838; IntAct: EBI-300010,EBI-310758; Score: 0.40
DE  Interaction: Q9NQW6; IntAct: EBI-2553589,EBI-310758; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11335160,EBI-310758; Score: 0.35
DE  Interaction: Q61166; IntAct: EBI-2027055,EBI-310758; Score: 0.70
DE  Interaction: Q3UH45; IntAct: EBI-11090767,EBI-310758; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-310758; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-350338,EBI-310758; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-876367,EBI-310758; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-310758; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-1047508,EBI-310758; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-310758; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-1056902,EBI-310758; Score: 0.35
DE  Interaction: P49841; IntAct: EBI-373586,EBI-310758; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-310758; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-310758; Score: 0.35
DE  Interaction: P43355; IntAct: EBI-740978,EBI-310758; Score: 0.35
DE  Interaction: O75386; IntAct: EBI-5357290,EBI-310758; Score: 0.37
DE  Interaction: Q14324; IntAct: EBI-310758,EBI-5653200; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-748974,EBI-310758; Score: 0.51
DE  Interaction: Q9UKG1; IntAct: EBI-741243,EBI-310758; Score: 0.51
DE  Interaction: Q8IZP0; IntAct: EBI-375446,EBI-310758; Score: 0.37
DE  Interaction: Q15327; IntAct: EBI-5653378,EBI-310758; Score: 0.37
DE  Interaction: P0C862; IntAct: EBI-310758,EBI-5654640; Score: 0.37
DE  Interaction: Q8N3C7; IntAct: EBI-310758,EBI-5655540; Score: 0.37
DE  Interaction: Q13188; IntAct: EBI-992580,EBI-310758; Score: 0.35
DE  Interaction: Q8TDR0; IntAct: EBI-310758,EBI-928811; Score: 0.37
DE  Interaction: Q9UHX1; IntAct: EBI-1053259,EBI-310758; Score: 0.40
DE  Interaction: Q15287; IntAct: EBI-310758,EBI-395959; Score: 0.40
DE  Interaction: P15121; IntAct: EBI-310758,EBI-1052491; Score: 0.40
DE  Interaction: O76021; IntAct: EBI-358028,EBI-310758; Score: 0.40
DE  Interaction: P50993; IntAct: EBI-2952691,EBI-310758; Score: 0.40
DE  Interaction: P05455; IntAct: EBI-358037,EBI-310758; Score: 0.40
DE  Interaction: Q12996; IntAct: EBI-1056775,EBI-310758; Score: 0.40
DE  Interaction: P49286; IntAct: EBI-1188341,EBI-310758; Score: 0.37
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-310758; Score: 0.35
DE  Interaction: Q9H9Q2; IntAct: EBI-2510162,EBI-310758; Score: 0.35
DE  Interaction: Q9NYQ7; IntAct: EBI-310758,EBI-308417; Score: 0.37
DE  Interaction: Q9HCM3; IntAct: EBI-310758,EBI-311350; Score: 0.37
DE  Interaction: P62993; IntAct: EBI-401755,EBI-310758; Score: 0.35
GO  GO:0015629;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0009925;
GO  GO:0005604;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005925;
GO  GO:0031673;
GO  GO:0030056;
GO  GO:0016021;
GO  GO:0005882;
GO  GO:0045111;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0005178;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0005198;
GO  GO:0007155;
GO  GO:0048870;
GO  GO:0031122;
GO  GO:0007010;
GO  GO:0031581;
GO  GO:0007229;
GO  GO:0045104;
GO  GO:0030011;
GO  GO:0000226;
GO  GO:0009611;
GO  GO:0008090;
GO  GO:0042060;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDT
SQ  LPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLW
SQ  TQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDE
SQ  KSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVTTMSERTFPNNPVELKALYNQYLQFKETE
SQ  IPPKETEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLEMLQQIANRVQRDSVIC
SQ  EDKLILAGNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNEC
SQ  SSVYSKGRILTTEQTKLMISGITQSLNSGFAQTLHPSLTSGLTQSLTPSLTSSSMTSGLSSGMTSRLTPSVTPAYTPGFP
SQ  SGLVPNFSSGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEINMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLEN
SQ  HKNVHRAIEEFESSLKEAKISEIQMTAPLKLTYAEKLHRLESQYAKLLNTSRNQERHLDTLHNFVSRATNELIWLNEKEE
SQ  EEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQH
SQ  IKENTAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEEKEELLQYKSTIANLMGKAKTIIQLKPR
SQ  NSDCPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDLANRIEQQYQ
SQ  NVLTLWHESHINMKSVVSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKE
SQ  VNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKELERLK
SQ  DDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQVYSMSSTYIDKLKTVNLVLKNTQAAEALVKLYETKLCEEEA
SQ  VIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVERWQNVHVQIDN
SQ  RLRDLEGIGKSLKYYRDTYHPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSA
SQ  TVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSADLIIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKK
SQ  EHVEKAKELQKWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKKEQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKT
SQ  LQESYNLLFSESLKQLQESQTSGDVKVEEKLDKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTGIRLLETQLMISGLISPE
SQ  LRKCFDLKDAKSHGLIDEQILCQLKELSKAKEIISAASPTTIPVLDALAQSMITESMAIKVLEILLSTGSLVIPATGEQL
SQ  TLQKAFQQNLVSSALFSKVLERQNMCKDLIDPCTSEKVSLIDMVQRSTLQENTGMWLLPVRPQEGGRITLKCGRNISILR
SQ  AAHEGLIDRETMFRLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSILTYQVQTGGIIQSNPAKRLTVDEAVQC
SQ  DLITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKILNGRQKIAALYIPESSQVIGLDAAKQLGIID
SQ  NNTASILKNITLPDKMPDLGDLEACKNARRWLSFCKFQPSTVHDYRQEEDVFDGEEPVTTQTSEETKKLFLSYLMINSYM
SQ  DANTGQRLLLYDGDLDEAVGMLLEGCHAEFDGNTAIKECLDVLSSSGVFLNNASGREKDECTATPSSFNKCHCGEPEHEE
SQ  TPENRKCAIDEEFNEMRNTVINSEFSQSGKLASTISIDPKVNSSPSVCVPSLISYLTQTELADISMLRSDSENILTNYEN
SQ  QSRVETNERANECSHSKNIQNFPSDLIENPIMKSKMSKFCGVNETENEDNTNRDSPIFDYSPRLSALLSHDKLMHSQGSF
SQ  NDTHTPESNGNKCEAPALSFSDKTMLSGQRIGEKFQDQFLGIAAINISLPGEQYGQKSLNMISSNPQVQYHNDKYISNTS
SQ  GEDEKTHPGFQQMPEDKEDESEIEEYSCAVTPGGDTDNAIVSLTCATPLLDETISASDYETSLLNDQQNNTGTDTDSDDD
SQ  FYDTPLFEDDDHDSLLLDGDDRDCLHPEDYDTLQEENDETASPADVFYDVSKENENSMVPQGAPVGSLSVKNKAHCLQDF
SQ  LMDVEKDELDSGEKIHLNPVGSDKVNGQSLETGSERECTNILEGDESDSLTDYDIVGGKESFTASLKFDDSGSWRGRKEE
SQ  YVTGQEFHSDTDHLDSMQSEESYGDYIYDSNDQDDDDDDGIDEEGGGIRDENGKPRCQNVAEDMDIQLCASILNENSDEN
SQ  ENINTMILLDKMHSCSSLEKQQRVNVVQLASPSENNLVTEKSNLPEYTTEIAGKSKENLLNHEMVLKDVLPPIIKDTESE
SQ  KTFGPASISHDNNNISSTSELGTDLANTKVKLIQGSELPELTDSVKGKDEYFKNMTPKVDSSLDHIICTEPDLIGKPAEE
SQ  SHLSLIASVTDKDPQGNGSDLIKGRDGKSDILIEDETSIQKMYLGEGEVLVEGLVEEENRHLKLLPGKNTRDSFKLINSQ
SQ  FPFPQITNNEELNQKGSLKKATVTLKDEPNNLQIIVSKSPVQFENLEEIFDTSVSKEISDDITSDITSWEGNTHFEESFT
SQ  DGPEKELDLFTYLKHCAKNIKAKDVAKPNEDVPSHVLITAPPMKEHLQLGVNNTKEKSTSTQKDSPLNDMIQSNDLCSKE
SQ  SISGGGTEISQFTPESIEATLSILSRKHVEDVGKNDFLQSERCANGLGNDNSSNTLNTDYSFLEINNKKERIEQQLPKEQ
SQ  ALSPRSQEKEVQIPELSQVFVEDVKDILKSRLKEGHMNPQEVEEPSACADTKILIQNLIKRITTSQLVNEASTVPSDSQM
SQ  SDSSGVSPMTNSSELKPESRDDPFCIGNLKSELLLNILKQDQHSQKITGVFELMRELTHMEYDLEKRGITSKVLPLQLEN
SQ  IFYKLLADGYSEKIEHVGDFNQKACSTSEMMEEKPHILGDIKSKEGNYYSPNLETVKEIGLESSTVWASTLPRDEKLKDL
SQ  CNDFPSHLECTSGSKEMASGDSSTEQFSSELQQCLQHTEKMHEYLTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFEL
SQ  GLAPIAVILRKDMKLAEEFLKSLPSDFPRGHVEELSISHQSLKTAFSSLSNVSSERTKQIMLAIDSEMSKLAVSHEEFLH
SQ  KLKSFSDWVSEKSKSVKDIEIVNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQDLSPNQSKQLLRL
SQ  LNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELK
SQ  KYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTAIK
SQ  EETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQVG
SQ  TTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHS
SQ  LQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKR
SQ  DGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQACEATASKHLSEPIAVDPK
SQ  NLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSL
SQ  SVQDGLDEMLDWMGNVESSLKEQGQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTDPSTASSLQAKM
SQ  KDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHL
SQ  EVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQP
SQ  SFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNNSGISLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEEFWANKGL
SQ  TSIKKDMTDISHGYEDLGLLLKDKIAELNTKLSKLQKAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKS
SQ  FEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQW
SQ  LVEKELMVSVLGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSL
SQ  TGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALC
SQ  EDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKSHPISAKLD
SQ  VLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKY
SQ  KEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSLI
SQ  QKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALKHQVDL
SQ  AKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLQGIGHFQNTIREMFSQFAEFDDELDSMAPV
SQ  GRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLATEETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTI
SQ  KRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQ
SQ  GLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKAQIQEQKLLQR
SQ  LLDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTI
SQ  EKRLVNCEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHS
SQ  RSELLQQALCNAKIFGEDEVELMNWLNEVHDKLSKLSVQDYSTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQ
SQ  TTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEASQAQM
SQ  RPKELKKEAKNNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAILRSQQFDQAADAE
SQ  LSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDT
SQ  ICQINSERYLQLERAQSLVNQFWETYEELWPWLTETQSIISQLPAPALEYETLRQQQEEHRQLRELIAEHKPHIDKMNKT
SQ  GPQLLELSPGEGFSIQEKYVAADTLYSQIKEDVKKRAVALDEAISQSTQFHDKIDQILESLERIVERLRQPPSISAEVEK
SQ  IKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGTDKDISAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVMELA
SQ  EKFWCDHMSLIVTIKDTQDFIRDLEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAACGEPDKPIVKKS
SQ  IDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVFDWVDIAGGKLASMSPIGTDLETVKQQIEELKQFKSEAYQQ
SQ  QIEMERLNHQAELLLKKVTEESDKHTVQDPLMELKLIWDSLEERIINRQHKLEGALLALGQFQHALDELLAWLTHTEGLL
SQ  SEQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQ
SQ  LDGALRQAKGFHGEIEDLQQWLTDTERHLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKS
SQ  AETNIDQDINNLKEKWESVETKLNERKTKLEEALNLAMEFHNSLQDFINWLTQAEQTLNVASRPSLILDTVLFQIDEHKV
SQ  FANEVNSHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWSKLMEWL
SQ  EESEKSLDSELEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSLADDNLKLDDMLSELRDKWDTICG
SQ  KSVERQNKLEEALLFSGQFTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARE
SQ  LIEGSRDDSSWVKVQMQELSTRWETVCALSISKQTRLEAALRQAEEFHSVVHALLEWLAEAEQTLRFHGVLPDDEDALRT
SQ  LIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASALAGLIAKQELL
SQ  EALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEEMTRKQPDVDKVTKTYKRRAADPSSLQSHIPVLDKGRAG
SQ  RKRFPASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKS
SQ  RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIED
SQ  EVTRQVAKCKCAKRFQVEQIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKML
SQ  RSESNSSITTTQPTIAKGRTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSVSSQAAQAASPQVPATTT
SQ  PKGTPIQGSKLRLPGYLSGKGFHSGEDSGLITTAAARVRTQFADSKKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEI
SQ  QSVCSDVETVPQTHRPTPRAGSRPSTAKPSKIPTPQRKSPASKLDKSSKR
//
ID  Q9NZ56;
PN  Formin-2;
GN  FMN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20082305}. Cytoplasm, cytosol {ECO:0000269|PubMed:20082305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9JL04}. Nucleus {ECO:0000269|PubMed:26287480}. Nucleus, nucleolus {ECO:0000269|PubMed:23375502}. Cell membrane {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9JL04}. Note=Colocalizes with the actin cytoskeleton (PubMed:20082305). Recruited to the membranes via its interaction with SPIRE1 (By similarity). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Accumulates in the nucleus following DNA damage (PubMed:26287480). {ECO:0000250|UniProtKB:Q9JL04, ECO:0000269|PubMed:20082305, ECO:0000269|PubMed:26287480}.
DR  UNIPROT: Q9NZ56;
DR  UNIPROT: B0QZA7;
DR  UNIPROT: B4DP05;
DR  UNIPROT: Q59GF6;
DR  UNIPROT: Q5VU37;
DR  UNIPROT: Q9NZ55;
DR  PDB: 2YLE;
DR  PDB: 3R7G;
DR  Pfam: PF06346;
DR  Pfam: PF02181;
DR  PROSITE: PS51444;
DR  OMIM: 606373;
DR  OMIM: 616193;
DR  DisGeNET: 56776;
DE  Function: Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization (PubMed:22330775, PubMed:21730168). Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:22330775, PubMed:21730168). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (By similarity). Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (PubMed:23375502). Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (PubMed:26287480). Protects cells against apoptosis by protecting CDKN1A against degradation (PubMed:23375502). {ECO:0000250|UniProtKB:Q9JL04, ECO:0000269|PubMed:21730168, ECO:0000269|PubMed:22330775, ECO:0000269|PubMed:23375502, ECO:0000269|PubMed:26287480}.
DE  Disease: Mental retardation, autosomal recessive 47 (MRT47) [MIM:616193]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT47 patients show delayed development, with cognition and speech more affected than motor skills. {ECO:0000269|PubMed:25480035}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BVQ7-2; IntAct: EBI-21531202,EBI-20840373; Score: 0.35
DE  Interaction: Q8NB37-2; IntAct: EBI-21529247,EBI-20840373; Score: 0.35
DE  Interaction: Q96IK1; IntAct: EBI-10979484,EBI-20840373; Score: 0.35
DE  Interaction: Q12974; IntAct: EBI-1046324,EBI-20840373; Score: 0.35
DE  Interaction: P29466-3; IntAct: EBI-12248206,EBI-20840373; Score: 0.35
DE  Interaction: P55145; IntAct: EBI-1044104,EBI-20840373; Score: 0.40
DE  Interaction: Q92870-2; IntAct: EBI-21535880,EBI-20840373; Score: 0.35
DE  Interaction: P43353; IntAct: EBI-2558314,EBI-20840373; Score: 0.35
DE  Interaction: Q8WUD1; IntAct: EBI-5542466,EBI-20840373; Score: 0.35
DE  Interaction: Q9Y664; IntAct: EBI-1048252,EBI-20840373; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-2837401,EBI-20840373; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-296151,EBI-20840373; Score: 0.35
GO  GO:0005623;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005902;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0006974;
GO  GO:0071456;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0051758;
GO  GO:0035556;
GO  GO:0046907;
GO  GO:0007275;
GO  GO:0043066;
GO  GO:0042177;
GO  GO:0048477;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9JL04};
SQ  MGNQDGKLKRSAGDALHEGGGGAEDALGPRDVEATKKGSGGKKALGKHGKGGGGGGGGGESGKKKSKSDSRASVFSNLRI
SQ  RKNLSKGKGAGGSREDVLDSQALQTGELDSAHSLLTKTPDLSLSADEAGLSDTECADPFEVTGPGGPGPAEARVGGRPIA
SQ  EDVETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQQLQLQLQQQQQQQQLQGAEEPAAPPTAVS
SQ  PQPGAFLGLDRFLLGPSGGAGEAPGSPDTEQALSALSDLPESLAAEPREPQQPPSPGGLPVSEAPSLPAAQPAAKDSPSS
SQ  TAFPFPEAGPGEEAAGAPVRGAGDTDEEGEEDAFEDAPRGSPGEEWAPEVGEDAPQRLGEEPEEEAQGPDAPAAASLPGS
SQ  PAPSQRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKRRPEPSLSRGSRTALASVAAPAKKHRADGGLAAGLS
SQ  RSADWTEELGARTPRVGGSAHLLERGVASDSGGGVSPALAAKASGAPAAADGFQNVFTGRTLLEKLFSQQENGPPEEAEK
SQ  FCSRIIAMGLLLPFSDCFREPCNQNAQTNAASFDQDQLYTWAAVSQPTHSLDYSEGQFPRRVPSMGPPSKPPDEEHRLED
SQ  AETESQSAVSETPQKRSDAVQKEVVDMKSEGQATVIQQLEQTIEDLRTKIAELERQYPALDTEVASGHQGLENGVTASGD
SQ  VCLEALRLEEKEVRHHRILEAKSIQTSPTEEGGVLTLPPVDGLPGRPPCPPGAESGPQTKFCSEISLIVSPRRISVQLDS
SQ  HQPTQSISQPPPPPSLLWSAGQGQPGSQPPHSISTEFQTSHEHSVSSAFKNSCNIPSPPPLPCTESSSSMPGLGMVPPPP
SQ  PPLPGMTVPTLPSTAIPQPPPLQGTEMLPPPPPPLPGAGIPPPPPLPGAGILPLPPLPGAGIPPPPPLPGAAIPPPPPLP
SQ  GAGIPLPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAG
SQ  IPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGAGIPP
SQ  PPPLPGAGIPPPPPLPGAGIPPPPPLPRVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGVGIPPPPP
SQ  LPGAGIPPPPPLPGMGIPPAPAPPLPPPGTGIPPPPLLPVSGPPLLPQVGSSTLPTPQVCGFLPPPLPSGLFGLGMNQDK
SQ  GSRKQPIEPCRPMKPLYWTRIQLHSKRDSSTSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLL
SQ  SNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHGRSSKDKENAKSLDKPEQFLYE
SQ  LSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNGGNKTRGQADGFGLDILP
SQ  KLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCLFPLPEPQDLFQASQMKFEDFQKDLRKLKKDLKACEVEAGKVYQV
SQ  SSKEHMQPFKENMEQFIIQAKIDQEAEENSLTETHKCFLETTAYFFMKPKLGEKEVSPNAFFSIWHEFSSDFKDFWKKEN
SQ  KLLLQERVKEAEEVCRQKKGKSLYKIKPRHDSGIKAKISMKT
//
ID  M9PBE2;
PN  E3 ubiquitin-protein ligase Hakai;
GN  Hakai;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}.
DR  UNIPROT: M9PBE2;
DR  UNIPROT: Q86NQ9;
DR  UNIPROT: Q8INV9;
DR  UNIPROT: Q8INW0;
DR  UNIPROT: Q95RE3;
DR  UNIPROT: Q9VIT1;
DR  Pfam: PF18408;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase required during early development (PubMed:19682089). E3 ubiquitin-protein ligases mediate ubiquitination of target proteins (PubMed:19682089). Required for epithelial integrity and midgut morphogenesis (PubMed:19682089). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189). Its function in the WMM complex is unknown (PubMed:29535189). {ECO:0000250|UniProtKB:Q75N03, ECO:0000250|UniProtKB:Q9JIY2, ECO:0000269|PubMed:19682089, ECO:0000305|PubMed:29535189}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VU72; IntAct: EBI-100923,EBI-166182; Score: 0.37
DE  Interaction: A1Z9X0; IntAct: EBI-100923,EBI-160861; Score: 0.37
DE  Interaction: Q9VI24; IntAct: EBI-100923,EBI-106037; Score: 0.37
DE  Interaction: Q24558; IntAct: EBI-100923,EBI-102508; Score: 0.37
DE  Interaction: Q9VI16; IntAct: EBI-100923,EBI-175006; Score: 0.37
DE  Interaction: P25171; IntAct: EBI-100923,EBI-181948; Score: 0.37
DE  Interaction: Q7KTX7; IntAct: EBI-100923,EBI-131530; Score: 0.37
DE  Interaction: Q9W2M4; IntAct: EBI-100923,EBI-138493; Score: 0.37
DE  Interaction: Q9VU89; IntAct: EBI-100923,EBI-157217; Score: 0.37
DE  Interaction: Q9VI55; IntAct: EBI-100923,EBI-172922; Score: 0.37
DE  Interaction: Q9VU18; IntAct: EBI-100923,EBI-172681; Score: 0.37
DE  Interaction: Q8T0I9; IntAct: EBI-100923,EBI-103726; Score: 0.37
DE  Interaction: Q9V472; IntAct: EBI-100923,EBI-497141; Score: 0.37
DE  Interaction: Q4Z8K6; IntAct: EBI-100923,EBI-183849; Score: 0.37
DE  Interaction: Q9VGB9; IntAct: EBI-100923,EBI-123122; Score: 0.37
DE  Interaction: Q9V9R6; IntAct: EBI-100923,EBI-160643; Score: 0.37
DE  Interaction: Q9VN36; IntAct: EBI-100923,EBI-134459; Score: 0.37
DE  Interaction: Q9VRC3; IntAct: EBI-100923,EBI-169095; Score: 0.37
DE  Interaction: Q9XZU1; IntAct: EBI-100923,EBI-126291; Score: 0.37
DE  Interaction: Q9VSQ3; IntAct: EBI-100923,EBI-145474; Score: 0.37
DE  Interaction: Q9VC48; IntAct: EBI-100923,EBI-146422; Score: 0.37
DE  Interaction: Q9VMS5; IntAct: EBI-100923,EBI-140737; Score: 0.37
DE  Interaction: Q8MYW5; IntAct: EBI-100923,EBI-186621; Score: 0.37
DE  Interaction: Q9VGU7; IntAct: EBI-100923,EBI-142527; Score: 0.37
DE  Interaction: Q9W550; IntAct: EBI-100923,EBI-118257; Score: 0.37
DE  Interaction: Q9VZT6; IntAct: EBI-100923,EBI-89759; Score: 0.37
DE  Interaction: P54356; IntAct: EBI-122038,EBI-100923; Score: 0.37
DE  Interaction: Q9VJE3; IntAct: EBI-100923,EBI-186054; Score: 0.37
DE  Interaction: Q9VJ53; IntAct: EBI-100923,EBI-122209; Score: 0.37
DE  Interaction: Q9VXD4; IntAct: EBI-100923,EBI-149308; Score: 0.37
DE  Interaction: Q9VMD4; IntAct: EBI-100923,EBI-86395; Score: 0.37
DE  Interaction: Q9VFU6; IntAct: EBI-100923,EBI-159819; Score: 0.37
DE  Interaction: Q9VCM3; IntAct: EBI-100923,EBI-99802; Score: 0.37
DE  Interaction: Q8T3Y1; IntAct: EBI-100923,EBI-166306; Score: 0.37
DE  Interaction: B7YZT2; IntAct: EBI-100923,EBI-182799; Score: 0.37
DE  Interaction: Q9V9V8; IntAct: EBI-100923,EBI-124864; Score: 0.37
DE  Interaction: Q9VVV6; IntAct: EBI-100923,EBI-135353; Score: 0.37
DE  Interaction: Q9VF73; IntAct: EBI-100923,EBI-164368; Score: 0.37
DE  Interaction: P42282; IntAct: EBI-100923,EBI-77008; Score: 0.37
DE  Interaction: Q9W3J9; IntAct: EBI-100923,EBI-98170; Score: 0.37
DE  Interaction: Q9V9V0; IntAct: EBI-100923,EBI-135868; Score: 0.37
DE  Interaction: O46070; IntAct: EBI-100923,EBI-122171; Score: 0.37
DE  Interaction: Q9W5B6; IntAct: EBI-100923,EBI-127398; Score: 0.37
DE  Interaction: Q9VEA5; IntAct: EBI-100923,EBI-83826; Score: 0.37
DE  Interaction: M9MRI4; IntAct: EBI-100923,EBI-156486; Score: 0.37
DE  Interaction: Q9VKQ0; IntAct: EBI-100923,EBI-111864; Score: 0.37
DE  Interaction: Q9V4B8; IntAct: EBI-100923,EBI-145217; Score: 0.37
DE  Interaction: Q9VZM9; IntAct: EBI-100923,EBI-158602; Score: 0.37
DE  Interaction: Q9VSB2; IntAct: EBI-100923,EBI-111803; Score: 0.37
DE  Interaction: Q9VPE1; IntAct: EBI-100923,EBI-147129; Score: 0.37
DE  Interaction: A1ZAC8; IntAct: EBI-100923,EBI-88363; Score: 0.37
DE  Interaction: Q9VQF9; IntAct: EBI-100923,EBI-88022; Score: 0.37
DE  Interaction: Q9VDC1; IntAct: EBI-100923,EBI-107959; Score: 0.37
DE  Interaction: Q9W1R5; IntAct: EBI-100923,EBI-122690; Score: 0.37
DE  Interaction: Q9VSY2; IntAct: EBI-100923,EBI-172334; Score: 0.37
DE  Interaction: P11455; IntAct: EBI-100923,EBI-85264; Score: 0.37
DE  Interaction: Q9Y156; IntAct: EBI-100923,EBI-181059; Score: 0.37
DE  Interaction: Q8IQB8; IntAct: EBI-100923,EBI-129121; Score: 0.37
DE  Interaction: Q9VAZ1; IntAct: EBI-100923,EBI-161824; Score: 0.37
DE  Interaction: Q9VD25; IntAct: EBI-100923,EBI-119510; Score: 0.37
DE  Interaction: Q7K4Z4; IntAct: EBI-100923,EBI-159623; Score: 0.37
DE  Interaction: Q94981; IntAct: EBI-100923,EBI-98607; Score: 0.37
DE  Interaction: O76924; IntAct: EBI-100923,EBI-150281; Score: 0.37
DE  Interaction: O97365; IntAct: EBI-100923,EBI-120898; Score: 0.37
DE  Interaction: Q7JXC4; IntAct: EBI-151216,EBI-100923; Score: 0.37
DE  Interaction: P23696; IntAct: EBI-100923,EBI-101960; Score: 0.37
DE  Interaction: Q9V460; IntAct: EBI-100923,EBI-134850; Score: 0.37
DE  Interaction: A1Z8L7; IntAct: EBI-100923,EBI-163776; Score: 0.37
DE  Interaction: Q9VLP3; IntAct: EBI-100923,EBI-179169; Score: 0.37
DE  Interaction: Q9VHR4; IntAct: EBI-100923,EBI-117032; Score: 0.37
DE  Interaction: Q7K127; IntAct: EBI-100923,EBI-169919; Score: 0.37
DE  Interaction: Q9VHG0; IntAct: EBI-100923,EBI-195376; Score: 0.37
DE  Interaction: Q9VHA9; IntAct: EBI-100923,EBI-150802; Score: 0.37
DE  Interaction: Q8T3X9; IntAct: EBI-100923,EBI-133004; Score: 0.37
DE  Interaction: Q9V428; IntAct: EBI-100923,EBI-96007; Score: 0.37
DE  Interaction: Q9W379; IntAct: EBI-100923,EBI-158956; Score: 0.37
DE  Interaction: Q9W5X1; IntAct: EBI-100923,EBI-195166; Score: 0.37
DE  Interaction: Q9VXE7; IntAct: EBI-100923,EBI-165741; Score: 0.37
GO  GO:0031410;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0036396;
GO  GO:0045296;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0007015;
GO  GO:0040003;
GO  GO:0007391;
GO  GO:0007427;
GO  GO:0060429;
GO  GO:0008258;
GO  GO:0007494;
GO  GO:0016567;
GO  GO:0030155;
GO  GO:0035282;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPG
SQ  ALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLK
SQ  WNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSR
SQ  YGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIAS
SQ  RPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESV
SQ  ADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR
//
ID  Q6RKD8;
PN  Leucine-rich repeat transmembrane protein FLRT1;
GN  Flrt1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, neuron projection {ECO:0000269|PubMed:20421966}. Cell junction {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along neurites and at contacts between neurite termini and other cells (PubMed:20421966). Proteolytic cleavage gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}.
DR  UNIPROT: Q6RKD8;
DR  UNIPROT: Q14DT7;
DR  UNIPROT: Q6RKD9;
DR  Pfam: PF13855;
DR  Pfam: PF01462;
DR  PROSITE: PS50853;
DR  PROSITE: PS51450;
DE  Function: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases (PubMed:16872596, PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length (PubMed:20421966). May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000305|PubMed:22405201}.
DE  Reference Proteome: Yes;
GO  GO:0005911;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0005887;
GO  GO:0044306;
GO  GO:0032809;
GO  GO:0048471;
GO  GO:0005104;
GO  GO:0007155;
GO  GO:0016358;
GO  GO:0008543;
GO  GO:1990138;
GO  GO:0051965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKV
SQ  QVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNH
SQ  LSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLP
SQ  SAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAA
SQ  VVNVRGLMCQGPEKVRGMAIKDITSEMDECFEAGSQGGAANAAAKTTVSNHASATTPQGSLFTLKAKRPGLRLPDSNIDY
SQ  PMATGDGAKTLVIQVKPLTADSIRITWKAMLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMV
SQ  TMETGNTYVADETPVCAKAETADSYGPTTTLNQEQNAGPMAGLPLAGIIGGAVALVFLFLVLGAICWYVHRAGELLTRER
SQ  VYNRGSRRKDDYMESGTKKDNSILEIRGPGLQMLPINPYRSKEEYVVHTIFPSNGSSLCKGAHTIGYGTTRGYREAGIPD
SQ  VDYSYT
//
ID  P49454;
PN  Centromere protein F;
GN  CENPF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus matrix. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Relocalizes to the kinetochore/centromere (coronal surface of the outer plate) and the spindle during mitosis. Observed in nucleus during interphase but not in the nucleolus. At metaphase becomes localized to areas including kinetochore and mitotic apparatus as well as cytoplasm. By telophase, is concentrated within the intracellular bridge at either side of the mid-body.
DR  UNIPROT: P49454;
DR  UNIPROT: Q13171;
DR  UNIPROT: Q13246;
DR  UNIPROT: Q5VVM7;
DR  Pfam: PF10490;
DR  Pfam: PF10473;
DR  Pfam: PF10481;
DR  OMIM: 243605;
DR  OMIM: 600236;
DR  DisGeNET: 1063;
DE  Function: Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing neonatal cardiomyocytes. Interaction with RB directs embryonic stem cells toward a cardiac lineage. Involved in the regulation of DNA synthesis and hence cell cycle progression, via its C-terminus. Has a potential role regulating skeletal myogenesis and in cell differentiation in embryogenesis. Involved in dendritic cell regulation of T-cell immunity against chlamydia. {ECO:0000269|PubMed:12974617, ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:7542657, ECO:0000269|PubMed:7651420}.
DE  Disease: Stromme syndrome (STROMS) [MIM:243605]: An autosomal recessive congenital disorder characterized by intestinal atresia, ocular anomalies, microcephaly, and renal and cardiac abnormalities in some patients. The disease has features of a ciliopathy, and lethality in early childhood is observed in severe cases. {ECO:0000269|PubMed:25564561, ECO:0000269|PubMed:26820108}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P43034; IntAct: EBI-720620,EBI-968343; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-714559,EBI-968343; Score: 0.35
DE  Interaction: Q9GZM8; IntAct: EBI-928842,EBI-968343; Score: 0.75
DE  Interaction: Q9NXR1; IntAct: EBI-941227,EBI-968343; Score: 0.40
DE  Interaction: Q02224; IntAct: EBI-968343,EBI-1375040; Score: 0.37
DE  Interaction: Q96JN8-2; IntAct: EBI-16811547,EBI-968343; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-968343,EBI-529989; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-968343; Score: 0.35
DE  Interaction: A2AUM9; IntAct: EBI-2554268,EBI-968343; Score: 0.40
DE  Interaction: P63005; IntAct: EBI-917499,EBI-968343; Score: 0.35
DE  Interaction: Q8BZQ7; IntAct: EBI-11026797,EBI-968343; Score: 0.35
DE  Interaction: Q96FF9; IntAct: EBI-718805,EBI-968343; Score: 0.35
DE  Interaction: Q7TSY8; IntAct: EBI-2552468,EBI-968343; Score: 0.35
DE  Interaction: Q99PT9; IntAct: EBI-11092400,EBI-968343; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-1047359,EBI-968343; Score: 0.35
DE  Interaction: Q08AG7; IntAct: EBI-2637198,EBI-968343; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-447544,EBI-968343; Score: 0.35
DE  Interaction: Q9QYY8; IntAct: EBI-11090415,EBI-968343; Score: 0.35
DE  Interaction: P70399; IntAct: EBI-769130,EBI-968343; Score: 0.35
DE  Interaction: Q71F23; IntAct: EBI-2515234,EBI-968343; Score: 0.35
DE  Interaction: Q8CI51; IntAct: EBI-299301,EBI-968343; Score: 0.35
DE  Interaction: Q9Y253; IntAct: EBI-2827270,EBI-968343; Score: 0.35
DE  Interaction: P25963; IntAct: EBI-307386,EBI-968343; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-876367,EBI-968343; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-3923210,EBI-968343; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-2130320,EBI-968343; Score: 0.35
DE  Interaction: Q96AP7; IntAct: EBI-4314670,EBI-968343; Score: 0.35
DE  Interaction: Q9UPY6; IntAct: EBI-3907133,EBI-968343; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-486838,EBI-968343; Score: 0.35
DE  Interaction: Q15714; IntAct: EBI-968343,EBI-712609; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-968343; Score: 0.40
DE  Interaction: Q9BYW2; IntAct: EBI-968343,EBI-945869; Score: 0.40
DE  Interaction: P30040; IntAct: EBI-946830,EBI-968343; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475888,EBI-968343; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-718324,EBI-968343; Score: 0.37
DE  Interaction: P49356; IntAct: EBI-602349,EBI-968343; Score: 0.35
DE  Interaction: Q96KS9; IntAct: EBI-10290462,EBI-968343; Score: 0.35
DE  Interaction: Q96EY4; IntAct: EBI-1045338,EBI-968343; Score: 0.35
DE  Interaction: Q9HD26-2; IntAct: EBI-11102276,EBI-968343; Score: 0.35
DE  Interaction: Q96T17-2; IntAct: EBI-16399739,EBI-968343; Score: 0.35
DE  Interaction: Q9UKA1; IntAct: EBI-2692340,EBI-968343; Score: 0.35
DE  Interaction: Q9Y6K9-2; IntAct: EBI-21581164,EBI-968343; Score: 0.35
DE  Interaction: Q9H2F9; IntAct: EBI-2813327,EBI-968343; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-968343; Score: 0.35
DE  Interaction: Q8N5R6-4; IntAct: EBI-21699064,EBI-968343; Score: 0.35
GO  GO:0005930;
GO  GO:0005623;
GO  GO:0005813;
GO  GO:0000775;
GO  GO:0036064;
GO  GO:0097539;
GO  GO:0000940;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0008134;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0071897;
GO  GO:0001822;
GO  GO:0051382;
GO  GO:0051310;
GO  GO:0000278;
GO  GO:0007094;
GO  GO:0007517;
GO  GO:0045892;
GO  GO:0015031;
GO  GO:0051726;
GO  GO:0010389;
GO  GO:0016202;
GO  GO:0042493;
GO  GO:0021591;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10852915};
SQ  MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKTEGTNLKRENQRLMEICESLE
SQ  KTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKRCKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYS
SQ  GSKYEDLKEKYNKEVEERKRLEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRD
SQ  FSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELRLQGHEKEMKGQVNKFQELQL
SQ  QLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTALEQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEEL
SQ  SRQQRSFQTLDQECIQMKARLTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRS
SQ  MEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDLQEKINQQENSLTLEKLKLAV
SQ  ADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLSALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENL
SQ  QSKINHLETCLKTQQIKSHEYNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIEN
SQ  MCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDHQRSLLAFDQQPAMHHSFANI
SQ  IGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLESQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAE
SQ  TSQRISKLQEDTSAHQNVVAETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSS
SQ  IISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQEKLILLQRCEETGNAYEDLS
SQ  QKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAKEHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNN
SQ  SKSEAGGLKQEIMTLKEEQNKMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKE
SQ  ISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISGLKDCEIDAEEKYISGPHELS
SQ  TSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTELNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGEL
SQ  VEDIPGGEFGEQPNEQHPVSLAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVD
SQ  SLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGAVSANQ
SQ  CSVDEVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQELEQLLSSERQELDCLRK
SQ  QYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQLQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSE
SQ  TTERTPKHDVHQICDKDAQQDLNLDIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPM
SQ  DFLGNQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEACIELEKIVGELKKENS
SQ  DLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGDNVAKVNDSWKERFLDVENELSRIRSEKASIEHEALY
SQ  LEADLEVVQTEKLCLEKDNENKQKVIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLH
SQ  CIQVAEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKEKELLVKESESLQARLS
SQ  ESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKLRVRIEADEKKQLHIAEKLKERERENDSLKDKVENLE
SQ  RELQMSEENQELVILDAENSKAEVETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLL
SQ  EEKEQAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIEKLRARLEADEKKQLCV
SQ  LQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKGEVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNE
SQ  LQKEQERISELEIINSSFENILQEKEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLEL
SQ  EKAQLLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQVEGEHQLWKEQNLELRN
SQ  LTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDKMSFVEKVNKMTAKETELQREMHEMAQKTAELQEELS
SQ  GEKNRLAGELQLLLEEIKSSKDQLKELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQ
SQ  YEVEIQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQLKKENERAQGKMKLLIK
SQ  SCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIKELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEM
SQ  LETQVAHLCSQQSKQDSRGSPLLGPVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKA
SQ  VMSGIHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSPLSLGKENLAESSKPTA
SQ  GGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSPREGLRVKRGRLVPSPKAGLESNGSENCKVQ
//
ID  Q96F07;
PN  Cytoplasmic FMR1-interacting protein 2;
GN  CYFIP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:17245118}. Nucleus {ECO:0000269|PubMed:17245118}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5SQX6}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q5SQX6}. Note=Highly expressed in the perinuclear regionand enriched in synaptosomes (By similarity). Treatment with leptomycin-B triggers translocation to the nucleus (PubMed:17245118). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:17245118}.
DR  UNIPROT: Q96F07;
DR  UNIPROT: A6NLT2;
DR  UNIPROT: D3DQJ3;
DR  UNIPROT: Q53EN5;
DR  UNIPROT: Q9NTK4;
DR  UNIPROT: Q9ULQ2;
DR  UNIPROT: Q9UN29;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DR  OMIM: 606323;
DR  OMIM: 618008;
DR  DisGeNET: 26999;
DE  Function: Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:17245118}.
DE  Disease: Epileptic encephalopathy, early infantile, 65 (EIEE65) [MIM:618008]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE65 is an autosomal dominant form characterized by onset of intractable seizures usually in the first 6 months of life and severe to profound psychomotor developmental delay. {ECO:0000269|PubMed:29534297}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-2433893; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-2433893,EBI-529989; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-2433893; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-359815,EBI-2433893; Score: 0.35
DE  Interaction: Q13485; IntAct: EBI-347263,EBI-2433893; Score: 0.49
DE  Interaction: P15311; IntAct: EBI-1056902,EBI-2433893; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-351896,EBI-2433893; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-2433893; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-2433893; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-2433893; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-306940,EBI-2433893; Score: 0.53
DE  Interaction: P00747; IntAct: EBI-999394,EBI-2433893; Score: 0.37
DE  Interaction: Q13489; IntAct: EBI-2433893,EBI-517709; Score: 0.37
DE  Interaction: Q5D1E8; IntAct: EBI-747793,EBI-2433893; Score: 0.37
DE  Interaction: Q81V90; IntAct: EBI-2810010,EBI-2433893; Score: 0.37
DE  Interaction: Q8IZP0; IntAct: EBI-375446,EBI-2433893; Score: 0.56
DE  Interaction: P63104; IntAct: EBI-347088,EBI-2433893; Score: 0.35
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0097202;
GO  GO:0006915;
GO  GO:0007411;
GO  GO:0000902;
GO  GO:0030031;
GO  GO:0098609;
GO  GO:0097484;
GO  GO:0038096;
GO  GO:0051388;
GO  GO:0045862;
GO  GO:0048010;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLAD
SQ  IVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLL
SQ  SKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIY
SQ  AALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQACQ
SQ  WSPRALFHPTGGTQGRRGCRSLLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCC
SQ  DLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVN
SQ  LCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAM
SQ  YKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYC
SQ  YNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKI
SQ  VKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQ
SQ  EEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVI
SQ  LTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDL
SQ  FDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC
//
ID  Q8BIA4;
PN  F-box/WD repeat-containing protein 8;
GN  Fbxw8;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DL28}. Golgi apparatus {ECO:0000250|UniProtKB:P0DL28}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}.
DR  UNIPROT: Q8BIA4;
DR  UNIPROT: Q8BI62;
DR  UNIPROT: Q8BI75;
DR  UNIPROT: Q8BI76;
DR  UNIPROT: Q8CID8;
DR  UNIPROT: Q921Z1;
DR  Pfam: PF12937;
DR  PROSITE: PS50181;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Substrate-recognition component of a Cul7-RING ubiquitin- protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7- RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). {ECO:0000250|UniProtKB:Q8N3Y1}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0031467;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0070545;
GO  GO:0048471;
GO  GO:0030687;
GO  GO:0019005;
GO  GO:0004842;
GO  GO:0008283;
GO  GO:0007030;
GO  GO:0060716;
GO  GO:0000460;
GO  GO:0000470;
GO  GO:0050775;
GO  GO:1901485;
GO  GO:0016567;
GO  GO:0060712;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDHNLEEFRRHWQEELAQSQALRRRRRLEAGERRSPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRGGDRKDT
SQ  SSRSRSPPDRDATEPEPLVDQLIRDLNELDDVPFFDVRLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLC
SQ  RQEGHLPHSRFSDYTCWKLILQECLAKEHTLRANWKNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGDVRVWDTRTW
SQ  DYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNIWDLRTGRFPIFRFEHDARIQALALSQEKPIVATASAF
SQ  DVVMLYPNEEGHWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKADDSARTLHYVYGQPATCLDVSASQVAF
SQ  GVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRIHDLRSDKIALSLSAHQLGVSA
SQ  VQMDDWKVVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYLSFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYE
SQ  FAVDQLAFQSPLPVCRLPRDIMAGYSYDLALSFPHDSI
//
ID  Q640M6;
PN  Glycerophosphodiester phosphodiesterase domain-containing protein 5;
GN  Gdpd5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693, ECO:0000305|PubMed:15276213}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15276213, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}. Cell projection, growth cone {ECO:0000269|PubMed:17275818}.
DR  UNIPROT: Q640M6;
DR  UNIPROT: Q8R0T5;
DR  UNIPROT: Q8R3N5;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (PubMed:17275818, PubMed:18667693). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (PubMed:18667693). {ECO:0000250|UniProtKB:Q3KTM2, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0097038;
GO  GO:0047389;
GO  GO:0008889;
GO  GO:0004435;
GO  GO:0021895;
GO  GO:0006629;
GO  GO:0045746;
GO  GO:0031175;
GO  GO:0045787;
GO  GO:0045666;
GO  GO:0048505;
GO  GO:0021522;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLVCTFSLTLTWLYFWWGVHNDYDEFNWYLYNRM
SQ  GYWSDWSVPILVTSAAAFTYIAGLLVLALCHIAVGQQLNLHWIHKMGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGT
SQ  APFLHIGALVAITALSWIVAGQFARAERSSSQLTILCTFFAVVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLA
SQ  PEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPF
SQ  WTASSLSPSDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPL
SQ  VRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHT
SQ  LSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISD
SQ  GVEVSDELSVCSDSSYDTYANANSTATPVGPRNAGSRAKTVTEQSGH
//
ID  P28491;
PN  Calreticulin;
GN  CALR;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000269|PubMed:2016321}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:2016321}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20222029}. Membrane {ECO:0000269|PubMed:20222029}. Note=During oocyte maturation and after parthenogenetic activation accumulates in the plasma membrane region. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (PubMed:20222029). {ECO:0000269|PubMed:20222029}.
DR  UNIPROT: P28491;
DR  UNIPROT: D4N5N1;
DR  Pfam: PF00262;
DR  PROSITE: PS00803;
DR  PROSITE: PS00804;
DR  PROSITE: PS00805;
DR  PROSITE: PS00014;
DE  Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. {ECO:0000250, ECO:0000269|PubMed:20222029}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0044322;
GO  GO:0009897;
GO  GO:0005615;
GO  GO:0042824;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0033018;
GO  GO:0050681;
GO  GO:0005509;
GO  GO:0030246;
GO  GO:0005178;
GO  GO:0003729;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0090398;
GO  GO:0030866;
GO  GO:0030968;
GO  GO:0071157;
GO  GO:0033144;
GO  GO:0045665;
GO  GO:0048387;
GO  GO:0000122;
GO  GO:0017148;
GO  GO:1901164;
GO  GO:0002502;
GO  GO:0008284;
GO  GO:2000510;
GO  GO:0010595;
GO  GO:0010628;
GO  GO:1901224;
GO  GO:0050766;
GO  GO:1900026;
GO  GO:0006611;
GO  GO:0006457;
GO  GO:0034504;
GO  GO:0050821;
GO  GO:0040020;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLLPVPLLLGLVGLAAAEPTIYFKEQFLDGDGWTDRWIESKHKPDFGRFVLSSGKFYGDQEKDKGLQTSQDARFYALSAR
SQ  FEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPDGLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKD
SQ  IRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAVKPEDWDERAKIDDPTDSKPEDWDKPE
SQ  HIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDSNIYAYENFAVLGLDLWQ
SQ  VKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEEKKRKEEEEVDKEDEEDKDEDEEEEDEK
SQ  EEEEEEDAAAGQAKDEL
//
ID  P35197;
PN  ADP-ribosylation factor GTPase-activating protein GCS1;
GN  GCS1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11839779}. Mitochondrion {ECO:0000269|PubMed:11839779}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839779}. Golgi apparatus {ECO:0000305|PubMed:11839779}. Note=Found also in the mitochondria and in the perinuclear region.
DR  UNIPROT: P35197;
DR  UNIPROT: D6VRC9;
DR  PDB: 5FJX;
DR  Pfam: PF01412;
DR  PROSITE: PS50115;
DE  Function: GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces. {ECO:0000269|PubMed:11756474, ECO:0000269|PubMed:11839779, ECO:0000269|PubMed:9927415}.
DE  Reference Proteome: Yes;
DE  Interaction: P32589; IntAct: EBI-8648,EBI-7475; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-7475; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-7475,EBI-8603; Score: 0.53
DE  Interaction: P10591; IntAct: EBI-7475,EBI-8591; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-7475,EBI-20254; Score: 0.35
DE  Interaction: P53919; IntAct: EBI-7475,EBI-28887; Score: 0.37
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0005096;
GO  GO:0046872;
GO  GO:0030037;
GO  GO:0048205;
GO  GO:0006888;
GO  GO:0043001;
GO  GO:0006890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRME
SQ  KGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREG
SQ  TPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQA
SQ  DPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAED
SQ  SSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF
//
ID  Q7L5N1;
PN  COP9 signalosome complex subunit 6;
GN  COPS6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9535219}. Cytoplasm {ECO:0000269|PubMed:9535219}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9520381}. Note=(Microbial infection) The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. {ECO:0000269|PubMed:9520381}.
DR  UNIPROT: Q7L5N1;
DR  UNIPROT: A4D2A3;
DR  UNIPROT: O15387;
DR  PDB: 4D10;
DR  PDB: 4D18;
DR  PDB: 4QFT;
DR  PDB: 4R14;
DR  PDB: 4WSN;
DR  PDB: 6R6H;
DR  PDB: 6R7F;
DR  PDB: 6R7H;
DR  PDB: 6R7I;
DR  Pfam: PF01398;
DR  Pfam: PF13012;
DR  PROSITE: PS50249;
DR  OMIM: 614729;
DR  DisGeNET: 10980;
DE  Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}.
DE  Reference Proteome: Yes;
DE  Interaction: O75569; IntAct: EBI-486838,EBI-713955; Score: 0.37
DE  Interaction: P04406; IntAct: EBI-486838,EBI-354056; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-486838,EBI-295644; Score: 0.35
DE  Interaction: P49454; IntAct: EBI-486838,EBI-968343; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-486838,EBI-489887; Score: 0.37
DE  Interaction: Q3TLR7; IntAct: EBI-2553626,EBI-486838; Score: 0.40
DE  Interaction: Q5JTH9; IntAct: EBI-486838,EBI-310743; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-346882,EBI-486838; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-486838; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-486838,EBI-529989; Score: 0.37
DE  Interaction: P06241; IntAct: EBI-486838,EBI-515315; Score: 0.37
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-486838; Score: 0.91
DE  Interaction: Q3U1J4; IntAct: EBI-2552275,EBI-486838; Score: 0.40
DE  Interaction: P24386; IntAct: EBI-2515129,EBI-486838; Score: 0.40
DE  Interaction: Q9C0D3; IntAct: EBI-486838,EBI-1811414; Score: 0.40
DE  Interaction: Q6TFL4; IntAct: EBI-486838,EBI-2510117; Score: 0.56
DE  Interaction: Q96SW2; IntAct: EBI-486838,EBI-2510250; Score: 0.67
DE  Interaction: Q9UNS2; IntAct: EBI-486838,EBI-350590; Score: 0.88
DE  Interaction: Q96Q07; IntAct: EBI-486838,EBI-2510245; Score: 0.56
DE  Interaction: Q15048; IntAct: EBI-486838,EBI-2510124; Score: 0.56
DE  Interaction: Q96EF6; IntAct: EBI-486838,EBI-2510157; Score: 0.67
DE  Interaction: Q13618; IntAct: EBI-486838,EBI-456129; Score: 0.56
DE  Interaction: Q96M94; IntAct: EBI-486838,EBI-2510129; Score: 0.56
DE  Interaction: Q8WXC6; IntAct: EBI-486838,EBI-2510257; Score: 0.56
DE  Interaction: P15374; IntAct: EBI-486838,EBI-954554; Score: 0.40
DE  Interaction: Q13616; IntAct: EBI-486838,EBI-359390; Score: 0.62
DE  Interaction: Q9UBW8; IntAct: EBI-486838,EBI-712982; Score: 0.74
DE  Interaction: Q99627; IntAct: EBI-486838,EBI-2510102; Score: 0.85
DE  Interaction: Q8NEZ5; IntAct: EBI-486838,EBI-2510137; Score: 0.40
DE  Interaction: Q9P2J3; IntAct: EBI-486838,EBI-2510152; Score: 0.56
DE  Interaction: Q13619; IntAct: EBI-486838,EBI-456106; Score: 0.67
DE  Interaction: Q9H078; IntAct: EBI-486838,EBI-2107221; Score: 0.40
DE  Interaction: Q9H4M3; IntAct: EBI-486838,EBI-2322644; Score: 0.56
DE  Interaction: Q9Y3I1; IntAct: EBI-486838,EBI-1161222; Score: 0.67
DE  Interaction: Q13620; IntAct: EBI-486838,EBI-456067; Score: 0.56
DE  Interaction: Q13617; IntAct: EBI-486838,EBI-456179; Score: 0.67
DE  Interaction: Q15369; IntAct: EBI-486838,EBI-301231; Score: 0.56
DE  Interaction: Q53GT1; IntAct: EBI-486838,EBI-1996072; Score: 0.56
DE  Interaction: Q9UK73; IntAct: EBI-486838,EBI-310482; Score: 0.67
DE  Interaction: B4DN30; IntAct: EBI-486838,EBI-2510114; Score: 0.40
DE  Interaction: Q8TBC3; IntAct: EBI-486838,EBI-724292; Score: 0.40
DE  Interaction: Q9H496; IntAct: EBI-486838,EBI-2510146; Score: 0.56
DE  Interaction: Q8TEB1; IntAct: EBI-486838,EBI-2213388; Score: 0.67
DE  Interaction: Q13309; IntAct: EBI-486838,EBI-456291; Score: 0.67
DE  Interaction: Q9P2K6; IntAct: EBI-486838,EBI-739890; Score: 0.56
DE  Interaction: Q13216; IntAct: EBI-486838,EBI-295260; Score: 0.56
DE  Interaction: Q9NZJ0; IntAct: EBI-486838,EBI-1176075; Score: 0.56
DE  Interaction: Q86XK2; IntAct: EBI-486838,EBI-1047804; Score: 0.56
DE  Interaction: Q92466; IntAct: EBI-486838,EBI-1176171; Score: 0.67
DE  Interaction: Q9BW61; IntAct: EBI-486838,EBI-2510241; Score: 0.56
DE  Interaction: Q9BT78; IntAct: EBI-486838,EBI-742413; Score: 0.88
DE  Interaction: Q647K1; IntAct: EBI-486838,EBI-2510264; Score: 0.40
DE  Interaction: Q9BX70; IntAct: EBI-486838,EBI-710091; Score: 0.75
DE  Interaction: Q9P2G9; IntAct: EBI-486838,EBI-949008; Score: 0.56
DE  Interaction: Q9Y597; IntAct: EBI-486838,EBI-373299; Score: 0.40
DE  Interaction: Q9H9Q2; IntAct: EBI-486838,EBI-2510162; Score: 0.74
DE  Interaction: P61201; IntAct: EBI-486838,EBI-1050386; Score: 0.81
DE  Interaction: Q9Y2M5; IntAct: EBI-486838,EBI-714379; Score: 0.40
DE  Interaction: Q96L50; IntAct: EBI-486838,EBI-2510106; Score: 0.67
DE  Interaction: Q13098; IntAct: EBI-486838,EBI-725197; Score: 0.86
DE  Interaction: Q9Y4B6; IntAct: EBI-486838,EBI-1996353; Score: 0.56
DE  Interaction: Q9H0C5; IntAct: EBI-486838,EBI-935503; Score: 0.67
DE  Interaction: P61024; IntAct: EBI-486838,EBI-456371; Score: 0.56
DE  Interaction: Q5XUX1; IntAct: EBI-486838,EBI-2322729; Score: 0.56
DE  Interaction: Q15843; IntAct: EBI-486838,EBI-716247; Score: 0.56
DE  Interaction: Q9P2N7; IntAct: EBI-486838,EBI-1996321; Score: 0.56
DE  Interaction: Q93034; IntAct: EBI-486838,EBI-1057139; Score: 0.56
DE  Interaction: Q9BQ90; IntAct: EBI-1055396,EBI-486838; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-1041660,EBI-486838; Score: 0.53
DE  Interaction: O94844; IntAct: EBI-486838,EBI-6426999; Score: 0.53
DE  Interaction: Q8WV16; IntAct: EBI-486838,EBI-2559135; Score: 0.53
DE  Interaction: Q13620-1; IntAct: EBI-486838,EBI-10983971; Score: 0.35
DE  Interaction: Q13618-2; IntAct: EBI-486838,EBI-21546135; Score: 0.35
DE  Interaction: Q13098-5; IntAct: EBI-486838,EBI-21591293; Score: 0.35
DE  Interaction: P61201-2; IntAct: EBI-486838,EBI-21591286; Score: 0.35
DE  Interaction: O43583; IntAct: EBI-716083,EBI-486838; Score: 0.35
DE  Interaction: Q7L5Y6; IntAct: EBI-6425391,EBI-486838; Score: 0.35
DE  Interaction: A1L190; IntAct: EBI-10283466,EBI-486838; Score: 0.35
DE  Interaction: Q6UXH8-3; IntAct: EBI-486838,EBI-12013534; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-739895,EBI-486838; Score: 0.56
DE  Interaction: Q02556; IntAct: EBI-2866563,EBI-486838; Score: 0.35
DE  Interaction: Q9UBL3; IntAct: EBI-540797,EBI-486838; Score: 0.37
DE  Interaction: P12520; IntAct: EBI-6164519,EBI-486838; Score: 0.35
DE  Interaction: Q5VW00; IntAct: EBI-486838,EBI-3951747; Score: 0.35
DE  Interaction: O15061; IntAct: EBI-486838,EBI-7843148; Score: 0.35
DE  Interaction: Q96ME1; IntAct: EBI-486838,EBI-6425558; Score: 0.35
DE  Interaction: Q12951; IntAct: EBI-486838,EBI-11318190; Score: 0.35
DE  Interaction: Q9H469; IntAct: EBI-486838,EBI-6144096; Score: 0.35
DE  Interaction: Q8N1E6; IntAct: EBI-486838,EBI-6425532; Score: 0.53
DE  Interaction: P10599; IntAct: EBI-486838,EBI-594644; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-486838,EBI-2949748; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-486838,EBI-351772; Score: 0.35
DE  Interaction: Q01085; IntAct: EBI-486838,EBI-2820828; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-486838,EBI-1024357; Score: 0.35
DE  Interaction: P09234; IntAct: EBI-486838,EBI-766589; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-486838,EBI-1049228; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-486838,EBI-355133; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-486838,EBI-1057265; Score: 0.35
DE  Interaction: P60866; IntAct: EBI-486838,EBI-353105; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-486838,EBI-443446; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-486838,EBI-347895; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-486838,EBI-352783; Score: 0.35
DE  Interaction: P05386; IntAct: EBI-486838,EBI-354582; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-486838,EBI-438527; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-486838,EBI-359655; Score: 0.35
DE  Interaction: P36578; IntAct: EBI-486838,EBI-348313; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-486838,EBI-1053664; Score: 0.35
DE  Interaction: P83731; IntAct: EBI-486838,EBI-353146; Score: 0.35
DE  Interaction: P62829; IntAct: EBI-486838,EBI-353303; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-486838,EBI-352694; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-486838,EBI-443462; Score: 0.55
DE  Interaction: Q06830; IntAct: EBI-486838,EBI-353193; Score: 0.35
DE  Interaction: P13647; IntAct: EBI-486838,EBI-702187; Score: 0.35
DE  Interaction: Q14568; IntAct: EBI-486838,EBI-2826582; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-486838,EBI-299727; Score: 0.35
DE  Interaction: Q99729; IntAct: EBI-486838,EBI-1044873; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-486838,EBI-352560; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-486838,EBI-358826; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-486838,EBI-347528; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-486838,EBI-353944; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-486838,EBI-350864; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-486838,EBI-1103245; Score: 0.35
DE  Interaction: Q92804; IntAct: EBI-486838,EBI-2255091; Score: 0.35
DE  Interaction: P62316; IntAct: EBI-486838,EBI-297993; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-486838,EBI-354303; Score: 0.35
DE  Interaction: P05387; IntAct: EBI-486838,EBI-352813; Score: 0.35
DE  Interaction: P62424; IntAct: EBI-486838,EBI-354172; Score: 0.35
DE  Interaction: P62913; IntAct: EBI-486838,EBI-354380; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-486838,EBI-1050630; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-486838,EBI-81531; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-486838,EBI-78579; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-486838,EBI-300010; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-486838,EBI-346967; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-486838,EBI-2949715; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-486838,EBI-354932; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-486838,EBI-877656; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-486838,EBI-354921; Score: 0.35
DE  Interaction: P52597; IntAct: EBI-486838,EBI-352986; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-486838,EBI-299674; Score: 0.35
DE  Interaction: Q05639; IntAct: EBI-486838,EBI-354943; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-486838,EBI-351962; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-486838,EBI-353779; Score: 0.35
DE  Interaction: P61962; IntAct: EBI-486838,EBI-359808; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-486838,EBI-351356; Score: 0.35
DE  Interaction: Q9Y3Z3; IntAct: EBI-486838,EBI-1054601; Score: 0.35
DE  Interaction: P63173; IntAct: EBI-486838,EBI-359141; Score: 0.35
DE  Interaction: P36639; IntAct: EBI-486838,EBI-1048967; Score: 0.35
DE  Interaction: P34931; IntAct: EBI-486838,EBI-354912; Score: 0.35
DE  Interaction: Q9BUJ2; IntAct: EBI-486838,EBI-1018153; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-486838,EBI-711437; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-486838,EBI-351590; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-486838,EBI-299649; Score: 0.35
DE  Interaction: P62280; IntAct: EBI-486838,EBI-1047710; Score: 0.35
DE  Interaction: P61626; IntAct: EBI-486838,EBI-355360; Score: 0.35
DE  Interaction: Q01546; IntAct: EBI-486838,EBI-2952745; Score: 0.35
DE  Interaction: Q2M2I5; IntAct: EBI-486838,EBI-2952736; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-486838,EBI-353389; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-486838,EBI-296047; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-486838,EBI-400434; Score: 0.35
DE  Interaction: P35527; IntAct: EBI-486838,EBI-356382; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-486838,EBI-359129; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-486838,EBI-739737; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-486838,EBI-444308; Score: 0.35
DE  Interaction: Q9UQE7; IntAct: EBI-486838,EBI-80718; Score: 0.35
DE  Interaction: Q71RC2; IntAct: EBI-486838,EBI-2878091; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-486838,EBI-357061; Score: 0.35
DE  Interaction: Q6P5R6; IntAct: EBI-486838,EBI-2512545; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-486838,EBI-351896; Score: 0.35
DE  Interaction: Q9BRP1; IntAct: EBI-486838,EBI-2372173; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-486838,EBI-2505886; Score: 0.35
DE  Interaction: P35908; IntAct: EBI-486838,EBI-1247312; Score: 0.35
DE  Interaction: P04264; IntAct: EBI-486838,EBI-298429; Score: 0.35
DE  Interaction: P13645; IntAct: EBI-486838,EBI-465144; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-486838,EBI-724495; Score: 0.35
DE  Interaction: Q8N1G4; IntAct: EBI-486838,EBI-2509921; Score: 0.35
DE  Interaction: Q96MP8; IntAct: EBI-486838,EBI-12537276; Score: 0.35
DE  Interaction: Q6PI47; IntAct: EBI-486838,EBI-20587542; Score: 0.35
DE  Interaction: Q9NXK8; IntAct: EBI-486838,EBI-719790; Score: 0.35
DE  Interaction: Q53G59; IntAct: EBI-486838,EBI-740929; Score: 0.35
DE  Interaction: P22830; IntAct: EBI-486838,EBI-1390356; Score: 0.35
DE  Interaction: O95219; IntAct: EBI-486838,EBI-724909; Score: 0.35
DE  Interaction: Q96T23; IntAct: EBI-486838,EBI-926768; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-486838,EBI-726050; Score: 0.35
DE  Interaction: O60237; IntAct: EBI-486838,EBI-2558026; Score: 0.35
DE  Interaction: Q8NDI1; IntAct: EBI-486838,EBI-2689720; Score: 0.35
DE  Interaction: Q9UGM3; IntAct: EBI-486838,EBI-1044970; Score: 0.35
DE  Interaction: Q6P3S6; IntAct: EBI-486838,EBI-2506081; Score: 0.35
DE  Interaction: Q96NC0; IntAct: EBI-486838,EBI-2682299; Score: 0.35
DE  Interaction: P13521; IntAct: EBI-486838,EBI-947132; Score: 0.35
DE  Interaction: Q92834; IntAct: EBI-486838,EBI-6558417; Score: 0.35
DE  Interaction: Q9H4K1; IntAct: EBI-486838,EBI-740128; Score: 0.35
DE  Interaction: Q05BQ5; IntAct: EBI-486838,EBI-5666902; Score: 0.35
DE  Interaction: Q8WXI2; IntAct: EBI-486838,EBI-1045119; Score: 0.35
DE  Interaction: P01042; IntAct: EBI-486838,EBI-6378713; Score: 0.35
DE  Interaction: Q9NXE8; IntAct: EBI-486838,EBI-746052; Score: 0.35
DE  Interaction: Q6IMN6; IntAct: EBI-486838,EBI-6918449; Score: 0.35
DE  Interaction: Q9GZY4; IntAct: EBI-486838,EBI-6570735; Score: 0.35
DE  Interaction: Q9BYV9; IntAct: EBI-486838,EBI-1642333; Score: 0.35
DE  Interaction: O75110; IntAct: EBI-486838,EBI-2878108; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-486838,EBI-746752; Score: 0.35
DE  Interaction: Q10570; IntAct: EBI-486838,EBI-347859; Score: 0.35
DE  Interaction: Q15370; IntAct: EBI-486838,EBI-301238; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-486838,EBI-307486; Score: 0.35
DE  Interaction: Q92673; IntAct: EBI-486838,EBI-1171329; Score: 0.35
DE  Interaction: Q00526; IntAct: EBI-486838,EBI-1245761; Score: 0.35
DE  Interaction: P78396; IntAct: EBI-486838,EBI-375065; Score: 0.35
DE  Interaction: Q9NXF7; IntAct: EBI-486838,EBI-2559096; Score: 0.35
DE  Interaction: Q3SXM0; IntAct: EBI-486838,EBI-20854462; Score: 0.35
DE  Interaction: Q8WVD3; IntAct: EBI-486838,EBI-749039; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-486838,EBI-350322; Score: 0.35
DE  Interaction: O94889; IntAct: EBI-486838,EBI-2510096; Score: 0.35
DE  Interaction: O94952; IntAct: EBI-486838,EBI-311435; Score: 0.35
DE  Interaction: Q5T6F0; IntAct: EBI-486838,EBI-2559113; Score: 0.35
DE  Interaction: Q92624; IntAct: EBI-486838,EBI-743771; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-486838,EBI-375096; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-486838,EBI-457097; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-486838,EBI-2563266; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-740086,EBI-486838; Score: 0.35
DE  Interaction: Q8N5D0; IntAct: EBI-486838,EBI-311222; Score: 0.35
DE  Interaction: Q5TAQ9; IntAct: EBI-486838,EBI-740686; Score: 0.35
DE  Interaction: Q5QP82; IntAct: EBI-486838,EBI-723230; Score: 0.35
DE  Interaction: Q96JK2; IntAct: EBI-486838,EBI-3253159; Score: 0.35
DE  Interaction: Q8TEL6; IntAct: EBI-486838,EBI-2559060; Score: 0.35
DE  Interaction: Q58WW2; IntAct: EBI-486838,EBI-2559044; Score: 0.35
DE  Interaction: Q9C0C7; IntAct: EBI-486838,EBI-2512975; Score: 0.35
DE  Interaction: Q53HC5; IntAct: EBI-486838,EBI-724915; Score: 0.35
DE  Interaction: P57775; IntAct: EBI-486838,EBI-2372268; Score: 0.35
DE  Interaction: Q9Y297; IntAct: EBI-486838,EBI-307461; Score: 0.56
DE  Interaction: Q9UKB1; IntAct: EBI-486838,EBI-355189; Score: 0.35
DE  Interaction: Q9UK99; IntAct: EBI-486838,EBI-2509901; Score: 0.35
DE  Interaction: P09466; IntAct: EBI-486838,EBI-465167; Score: 0.37
DE  Interaction: Q9H3D4; IntAct: EBI-2337775,EBI-486838; Score: 0.37
DE  Interaction: P23508; IntAct: EBI-486838,EBI-307531; Score: 0.40
DE  Interaction: P17858; IntAct: EBI-486838,EBI-487243; Score: 0.37
DE  Interaction: Q92561; IntAct: EBI-486838,EBI-716478; Score: 0.37
DE  Interaction: P07602; IntAct: EBI-486838,EBI-716699; Score: 0.37
DE  Interaction: P60484; IntAct: EBI-486838,EBI-696162; Score: 0.37
DE  Interaction: Q9BXR0; IntAct: EBI-486838,EBI-716832; Score: 0.37
DE  Interaction: P51159; IntAct: EBI-486838,EBI-716881; Score: 0.37
DE  Interaction: P11166; IntAct: EBI-486838,EBI-717153; Score: 0.37
DE  Interaction: Q16637; IntAct: EBI-486838,EBI-395421; Score: 0.55
DE  Interaction: Q13190; IntAct: EBI-486838,EBI-714206; Score: 0.37
DE  Interaction: P49888; IntAct: EBI-486838,EBI-712512; Score: 0.37
DE  Interaction: P13385; IntAct: EBI-486838,EBI-717375; Score: 0.37
DE  Interaction: O60315; IntAct: EBI-486838,EBI-717614; Score: 0.37
DE  Interaction: Q9Y4P8; IntAct: EBI-486838,EBI-719396; Score: 0.37
DE  Interaction: P62861; IntAct: EBI-486838,EBI-358093; Score: 0.37
DE  Interaction: Q8IYL3; IntAct: EBI-486838,EBI-715898; Score: 0.37
DE  Interaction: P60903; IntAct: EBI-486838,EBI-717048; Score: 0.37
DE  Interaction: P05154; IntAct: EBI-486838,EBI-722597; Score: 0.37
DE  Interaction: P11230; IntAct: EBI-486838,EBI-724218; Score: 0.37
DE  Interaction: Q15911-2; IntAct: EBI-486838,EBI-10237226; Score: 0.56
DE  Interaction: Q92529; IntAct: EBI-486838,EBI-79084; Score: 0.56
DE  Interaction: Q13515; IntAct: EBI-486838,EBI-10229433; Score: 0.56
DE  Interaction: Q8NBE8; IntAct: EBI-486838,EBI-2512246; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-959949,EBI-486838; Score: 0.54
DE  Interaction: A0A1J9WN09; IntAct: EBI-486838,EBI-2814859; Score: 0.37
DE  Interaction: O95704; IntAct: EBI-286427,EBI-486838; Score: 0.35
DE  Interaction: Q6JEL2; IntAct: EBI-6426253,EBI-486838; Score: 0.35
DE  Interaction: Q9UKA1; IntAct: EBI-2692340,EBI-486838; Score: 0.35
DE  Interaction: Q96RU7; IntAct: EBI-486838,EBI-492476; Score: 0.37
DE  Interaction: Q96HD1; IntAct: EBI-486838,EBI-713009; Score: 0.37
DE  Interaction: O43261; IntAct: EBI-486838,EBI-710057; Score: 0.37
DE  Interaction: Q3KQU3; IntAct: EBI-486838,EBI-713229; Score: 0.37
DE  Interaction: Q9GZN7; IntAct: EBI-486838,EBI-713255; Score: 0.37
DE  Interaction: Q16363; IntAct: EBI-486838,EBI-711505; Score: 0.37
DE  Interaction: Q15102; IntAct: EBI-486838,EBI-711522; Score: 0.37
DE  Interaction: Q6P1K2; IntAct: EBI-486838,EBI-713832; Score: 0.37
DE  Interaction: O00231; IntAct: EBI-486838,EBI-357816; Score: 0.37
DE  Interaction: P40937; IntAct: EBI-486838,EBI-712376; Score: 0.37
DE  Interaction: P15927; IntAct: EBI-621404,EBI-486838; Score: 0.37
DE  Interaction: P21673; IntAct: EBI-486838,EBI-711613; Score: 0.37
DE  Interaction: P50453; IntAct: EBI-486838,EBI-711626; Score: 0.37
DE  Interaction: P40425; IntAct: EBI-486838,EBI-348489; Score: 0.37
DE  Interaction: P62308; IntAct: EBI-486838,EBI-624585; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-486838,EBI-712550; Score: 0.55
DE  Interaction: P17028; IntAct: EBI-486838,EBI-707773; Score: 0.37
DE  Interaction: Q96SN7; IntAct: EBI-714817,EBI-486838; Score: 0.37
DE  Interaction: Q9Y6N8; IntAct: EBI-486838,EBI-714872; Score: 0.37
DE  Interaction: P42773; IntAct: EBI-486838,EBI-711290; Score: 0.37
DE  Interaction: Q14061; IntAct: EBI-486838,EBI-711311; Score: 0.37
DE  Interaction: P20674; IntAct: EBI-486838,EBI-715032; Score: 0.37
DE  Interaction: Q53FE4; IntAct: EBI-486838,EBI-715110; Score: 0.37
DE  Interaction: O14717; IntAct: EBI-486838,EBI-711937; Score: 0.37
DE  Interaction: P05305; IntAct: EBI-486838,EBI-715181; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-486838,EBI-447295; Score: 0.37
DE  Interaction: P84090; IntAct: EBI-486838,EBI-711389; Score: 0.37
DE  Interaction: Q9NY59; IntAct: EBI-486838,EBI-715400; Score: 0.37
DE  Interaction: P30519; IntAct: EBI-486838,EBI-712096; Score: 0.37
DE  Interaction: Q9BWC9; IntAct: EBI-486838,EBI-711501; Score: 0.37
DE  Interaction: P06858; IntAct: EBI-486838,EBI-715909; Score: 0.37
DE  Interaction: Q13113; IntAct: EBI-486838,EBI-716063; Score: 0.37
DE  Interaction: Q8IYB7; IntAct: EBI-486838,EBI-716104; Score: 0.37
DE  Interaction: Q8N2I9; IntAct: EBI-486838,EBI-716112; Score: 0.37
DE  Interaction: P51948; IntAct: EBI-486838,EBI-716139; Score: 0.37
DE  Interaction: Q99417; IntAct: EBI-486838,EBI-716185; Score: 0.37
DE  Interaction: P08670; IntAct: EBI-486838,EBI-353844; Score: 0.37
GO  GO:0008180;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0000715;
GO  GO:0043687;
GO  GO:0000338;
GO  GO:0006283;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRN
SQ  IEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKH
SQ  TDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILE
SQ  YVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGR
SQ  RMRGLFF
//
ID  Q9C5H9;
PN  Gamma-tubulin complex component 2;
GN  GCP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm. Cytoplasm, cell cortex. Note=Associated to motile complexes in the cytosol that transiently stabilized at fixed locations in the cell cortex (e.g. along the outer periclinal edge of newly formed crosswalls) from which microtubules grow away prior to microtubules nucleation. Colocalizes with gamma-tubulin at the nuclear surface where microtubules are nucleated.
DR  UNIPROT: Q9C5H9;
DR  UNIPROT: F4KGZ8;
DR  UNIPROT: Q9LF43;
DR  Pfam: PF04130;
DR  Pfam: PF17681;
DE  Function: Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs). Required for the positioning of the gamma-tubulin-containing complex on pre-existing microtubules and for the proper organization of cortical arrays. {ECO:0000269|PubMed:19509058, ECO:0000269|PubMed:20935636}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LT56; IntAct: EBI-4469161,EBI-4469157; Score: 0.37
GO  GO:0005938;
GO  GO:0055028;
GO  GO:0005737;
GO  GO:0000923;
GO  GO:0000930;
GO  GO:0008275;
GO  GO:0005635;
GO  GO:0000922;
GO  GO:0043015;
GO  GO:0031122;
GO  GO:0048229;
GO  GO:0033566;
GO  GO:0051321;
GO  GO:0051415;
GO  GO:0000278;
GO  GO:0090063;
GO  GO:0051225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESMTPISCPTTPRWNQDRPFLTGRFHQETRASSKFADSKRFTLDSSSSGVEQAIGCYDTPVQELIVIDDLLSALVGIEG
SQ  RYISIKRFHGKEDSIAFQVDPSMDLALQELAKRIFPLCEYYLLIDQFVESSSQFKNGLVNHAFAAALRALLLDYQAMVAQ
SQ  LEHQFRLGRLSIQGLWFYCQPMMGSMRALAAVIQQASTKQFVGSGVLNLLQSQAKAMAGDNSVRSLLEKMTECASNAYLS
SQ  ILERWVYEGIIDDPYGEFFIAENRSLKKESLSQDSTAKYWSQRYSLKDTIPGFLANIAATILTTGKYLNVMRECGHNVQV
SQ  PISERSKLTIFGSNHHYLECIKAAHEFASIELVNLIKDKYDLVGRLRSIKHYLLLDQGDFLVHFMDIAREELNKKVHEIS
SQ  VEKLQSLLDLALRTTAAAADPRHEDLTCCVDRASLLTTLGMHKDTDSNSIEDPMSITGLETFSLSYKVQWPLSIVISKKA
SQ  LSKYQLIFRFLFHCKHVERQLCGAWQIHQGIRSMNSKGTAILRSSLLCRSMLKFISSLLHYLTFEVLEPNWHVMHDRLQS
SQ  TRSVDEVIQHHDFFLDKCLRGCLLLLPDVLKKMEKLKSVCLQYAAATQWLISSSIDINSQSHPQKTMIRDTTVTESIFNF
SQ  EREFNSELQSLGPVLSKGSQAEPYLTHLSQWILGVSKE
//
ID  Q9FG37;
PN  Gamma-tubulin complex component 3;
GN  GCP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton, spindle. Note=Associated to motile complexes in the cytosol that transiently stabilized at fixed locations in the cell cortex (e.g. along the outer periclinal edge of newly formed crosswalls) from which microtubules grow away prior to microtubules nucleation. Colocalizes with gamma- tubulin at the nuclear surface where microtubules are nucleated. Localizes to both cortical cytoplasm and mitotic microtubule arrays of the nematode feeding giant cells.
DR  UNIPROT: Q9FG37;
DR  Pfam: PF04130;
DR  Pfam: PF17681;
DE  Function: Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs). Required for the positioning of the gamma-tubulin-containing complex on pre-existing microtubules and for the proper organization of cortical arrays. Gamma-tubulin complex is essential for the control of microtubular network remodeling in the course of initiation and development of giant-feeding cells, and for the successful reproduction of nematodes (e.g. Meloidogyne spp.) in their plant hosts.
DE  Reference Proteome: Yes;
DE  Interaction: Q39069; IntAct: EBI-2651349,EBI-3387032; Score: 0.35
GO  GO:0005938;
GO  GO:0055028;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0000923;
GO  GO:0000930;
GO  GO:0008275;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0043015;
GO  GO:0015631;
GO  GO:0031122;
GO  GO:0051321;
GO  GO:0007020;
GO  GO:0051415;
GO  GO:0000278;
GO  GO:0090063;
GO  GO:0009624;
GO  GO:0051225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDDDQQKAADLVQELVLRLVSQNPQTPNLDPNSPAFLKTLRYAFRILSSRLTPSVLPDATAIAESLKRRLATQGKSSDA
SQ  LAFADLYTKFASKTGPGSVNNKWALVYLLKIVSDDRKSAINGLDSSVLLPNLGIGDTGNGVLSRGEAKKKDWSNGVLLVS
SQ  KDPENLRDIAFREYAILVKEENEVTEEVLVRDVLYASQGIDGKYVKFNSEIDGYAVQESVKVPRATRIMVRMLSELGWLF
SQ  RKVKTFITESMDRFPAEDVGTVGQAFCAALQDELSDYYKLLAVLEAQAMNPIPLVSESASSNNYLSLRRLSVWFAEPMVK
SQ  MRLMAVLVDKCKVLRGGAMAGAIHLHAQHGDPLVHDFMMSLLRCVCSPLFEMVRSWVLEGELEDTFGEFFVVGQPVKVDL
SQ  LWREGYKLHPAMLPSFISPSLAQRILRTGKSINFLRVCCDDHGWADAASEAAAASGTTTRRGGLGYGETDALEHLVTEAA
SQ  KRIDKHLLDVLYKRYKFKEHCLAIKRYLLLGQGDFVQYLMDIVGPKLSEPANNISSFELAGFLEAAIRASNAQYDDRDML
SQ  DRLRVKMMPHGSGDRGWDVFSLEYEARVPLDTVFTESVLSKYLRVFNFLWKLKRVEHALIGIWKTMKPNCITSNSFVKLQ
SQ  SSVKLQLLSALRRCQVLWNEMNHFVTNFQYYIMFEVLEVSWSNFSKEMEAAKDLDDLLAAHEKYLNAIVGKSLLGEQSQT
SQ  IRESLFVLFELILRFRSHADRLYEGIHELQIRSKESGREKNKSQEPGSWISEGRKGLTQRAGEFLQSMSQDMDSIAKEYT
SQ  SSLDGFLSLLPLQQSVDLKFLFFRLDFTEFYSRLHSKG
//
ID  G5EFL0;
PN  Poly(A) RNA polymerase gld-4;
GN  gld;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19339688}. Cytoplasmic granule {ECO:0000269|PubMed:19339688}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19339688}. Note=Localizes to P granules. This association is less apparent during pachytene, becomes obvious in maturing oocytes and is most prominently visible in developing embryos. {ECO:0000269|PubMed:19339688}.
DR  UNIPROT: G5EFL0;
DR  Pfam: PF01909;
DR  Pfam: PF03828;
DE  Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. The enzymatic activity is enhanced by its interaction with gls-1. Required, together with gld-2, for early meiotic progression in male and female germ cells and for gld-1 protein accumulation in the hermaphrodite germline. In the germline, forms a complex with gls-1 which directly binds to gld-1 mRNA and prevents its degradation. {ECO:0000269|PubMed:19339688}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005730;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0031499;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0004652;
GO  GO:0071044;
GO  GO:0051321;
GO  GO:0006378;
GO  GO:0007275;
GO  GO:0071050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNEDSRLSSSQQPSTSTPRSSIPSTMNSDEPNTCRRLSQSQEQPSTSRTCKSETPEFGYSDSLPFAPWRRKRYGLNIQGL
SQ  HEEIVDMYHWIKPNEIESRLRTKVFEKVRDSVLRRWKQKTIKISMFGSLRTNLFLPTSDIDVLVECDDWVGTPGDWLAET
SQ  ARGLEADNIAESVMVYGGAFVPIVKMVDRDTRLSIDISFNTVQGVRAASYIAKVKEEFPLIEPLVLLLKQFLHYRNLNQT
SQ  FTGGLSSYGLVLLLVNFFQLYALNMRSRTIYDRGVNLGHLLLRFLELYSLEFNFEEMGISPGQCCYIPKSASGARYGHKQ
SQ  AQPGNLALEDPLLTANDVGRSTYNFSSIANAFGQAFQILLVAVTLRERKGKNHVAMRAYKGSLLHLIMPFTSKELTYRNW
SQ  LMSGVLSMPGQEAPASYDLNQLHNTLVSPMVDLSRYAWLRKAPAKAEKRDSRPLTIVNPADDRQTLAQQLKKQILEQTEA
SQ  KKSLEKMPACDDNKKEEELVATRETDVELEAEDTESEGHHNGENDLILTGPPLPTSTQSVNTSATVSTAASISEREDTDS
SQ  PGLSSSMGNQSSEEDEDNGINNRNNSAVPVQFKKPFNEVVAQPARESKRTQTTSEDKMQDQFHFNGYSYPPPSRYAAGTA
SQ  APSHKHRNAHPQRQRPSIRNLSQGSDGSDEYNVESWNNNIRQGRRASSNSPSPSRQQTNTRNCGPTNNIPYDSFRSQNKN
SQ  STLDGSNNSSEEPITMYADVVKKKSSITTSTNTSTADVNVTNGNPIPANGIIPQSMAVVNVGRGSYRNALTTSPMTPPSA
SQ  HTSMQKQHHLRKDNECGFDNNSATSSTDLSHHQPQLVPPVNRLQR
//
ID  Q8GTY0;
PN  Elongation factor 1-alpha 4;
GN  A4;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}.
DR  UNIPROT: Q8GTY0;
DR  UNIPROT: P13905;
DR  UNIPROT: Q0WSD5;
DR  UNIPROT: Q39093;
DR  UNIPROT: Q9C5L4;
DR  Pfam: PF00009;
DR  Pfam: PF03144;
DR  Pfam: PF03143;
DR  PROSITE: PS00301;
DR  PROSITE: PS51722;
DE  Function: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0005773;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0003746;
GO  GO:0006412;
GO  GO:0006414;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF
SQ  ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP
SQ  KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD
SQ  VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD
SQ  PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV
SQ  ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK
//
ID  A1L4K1;
PN  Fibronectin type III and SPRY domain-containing protein 2;
GN  FSD2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:H0UZ81}.
DR  UNIPROT: A1L4K1;
DR  UNIPROT: B3KVG1;
DR  UNIPROT: B7ZM02;
DR  Pfam: PF00041;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q7Z3I7; IntAct: EBI-10172590,EBI-5661036; Score: 0.60
DE  Interaction: Q7Z3B3; IntAct: EBI-740244,EBI-5661036; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-2557469,EBI-5661036; Score: 0.72
DE  Interaction: Q6P1J9; IntAct: EBI-5661036,EBI-930143; Score: 0.78
DE  Interaction: Q6PJG3; IntAct: EBI-10253976,EBI-5661036; Score: 0.56
DE  Interaction: Q86VK4; IntAct: EBI-720304,EBI-5661036; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-6658203,EBI-5661036; Score: 0.72
DE  Interaction: Q9BXY8; IntAct: EBI-5661036,EBI-745073; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-372911,EBI-5661036; Score: 0.60
DE  Interaction: Q9H0E9-2; IntAct: EBI-5661036,EBI-10304361; Score: 0.72
DE  Interaction: Q9H6F0; IntAct: EBI-5661036,EBI-10307481; Score: 0.56
DE  Interaction: Q9H788-2; IntAct: EBI-10308083,EBI-5661036; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-5661036,EBI-747035; Score: 0.72
DE  Interaction: Q9HC52; IntAct: EBI-712912,EBI-5661036; Score: 0.72
DE  Interaction: Q8NEF3; IntAct: EBI-745040,EBI-5661036; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-740727,EBI-5661036; Score: 0.72
DE  Interaction: Q8TD31-3; IntAct: EBI-5661036,EBI-10175300; Score: 0.72
DE  Interaction: Q96NC0; IntAct: EBI-5661036,EBI-2682299; Score: 0.56
DE  Interaction: Q96SQ5; IntAct: EBI-6427977,EBI-5661036; Score: 0.72
DE  Interaction: Q9P0T4; IntAct: EBI-5661036,EBI-745520; Score: 0.72
DE  Interaction: Q9UGP5-2; IntAct: EBI-10320765,EBI-5661036; Score: 0.60
DE  Interaction: Q96BZ8; IntAct: EBI-726510,EBI-5661036; Score: 0.72
DE  Interaction: Q14738; IntAct: EBI-396563,EBI-5661036; Score: 0.56
DE  Interaction: Q15973; IntAct: EBI-2555767,EBI-5661036; Score: 0.56
DE  Interaction: P28070; IntAct: EBI-603350,EBI-5661036; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-5661036,EBI-745213; Score: 0.56
DE  Interaction: P31146; IntAct: EBI-5661036,EBI-1046676; Score: 0.78
DE  Interaction: O95990-3; IntAct: EBI-5661036,EBI-10192902; Score: 0.56
DE  Interaction: P10768; IntAct: EBI-1052334,EBI-5661036; Score: 0.78
DE  Interaction: P17024; IntAct: EBI-5661036,EBI-717634; Score: 0.56
DE  Interaction: Q16670; IntAct: EBI-5661036,EBI-3920053; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-719941,EBI-5661036; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-5661036,EBI-740767; Score: 0.56
DE  Interaction: Q5JS98; IntAct: EBI-5661036,EBI-10244393; Score: 0.56
DE  Interaction: Q9Y3B7; IntAct: EBI-5661036,EBI-5453723; Score: 0.72
DE  Interaction: Q00994; IntAct: EBI-741753,EBI-5661036; Score: 0.72
DE  Interaction: Q06787-8; IntAct: EBI-10224470,EBI-5661036; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-717810,EBI-5661036; Score: 0.67
DE  Interaction: Q8IXW7; IntAct: EBI-5661036,EBI-11976595; Score: 0.37
DE  Interaction: Q99608; IntAct: EBI-5661036,EBI-718177; Score: 0.37
DE  Interaction: Q9UIE0; IntAct: EBI-1105361,EBI-5661036; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-5661036,EBI-744203; Score: 0.56
DE  Interaction: Q8N381; IntAct: EBI-749096,EBI-5661036; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-954696,EBI-5661036; Score: 0.56
DE  Interaction: P46013; IntAct: EBI-876367,EBI-5661036; Score: 0.35
DE  Interaction: Q07002; IntAct: EBI-5661036,EBI-746238; Score: 0.56
DE  Interaction: Q96HP4; IntAct: EBI-2862111,EBI-5661036; Score: 0.56
DE  Interaction: O43602-2; IntAct: EBI-14148644,EBI-5661036; Score: 0.56
DE  Interaction: P0CB47; IntAct: EBI-17208936,EBI-5661036; Score: 0.56
DE  Interaction: P56524-2; IntAct: EBI-11953488,EBI-5661036; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-10241197,EBI-5661036; Score: 0.56
DE  Interaction: O60645; IntAct: EBI-1052278,EBI-5661036; Score: 0.56
DE  Interaction: Q5W5X9-3; IntAct: EBI-9090990,EBI-5661036; Score: 0.56
DE  Interaction: Q14324; IntAct: EBI-5661036,EBI-5653200; Score: 0.37
DE  Interaction: O95990; IntAct: EBI-743396,EBI-5661036; Score: 0.37
DE  Interaction: Q8TD31; IntAct: EBI-949834,EBI-5661036; Score: 0.37
DE  Interaction: P40426; IntAct: EBI-5661036,EBI-6390275; Score: 0.37
DE  Interaction: Q9Y394; IntAct: EBI-1387800,EBI-5661036; Score: 0.40
DE  Interaction: Q9BWG6; IntAct: EBI-5661036,EBI-748391; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-5661036,EBI-10251462; Score: 0.56
DE  Interaction: Q9BT49; IntAct: EBI-5661036,EBI-741350; Score: 0.56
DE  Interaction: Q9H9D4; IntAct: EBI-5661036,EBI-347633; Score: 0.56
DE  Interaction: Q5T619; IntAct: EBI-5661036,EBI-11985915; Score: 0.56
DE  Interaction: Q96EG3; IntAct: EBI-5661036,EBI-11962574; Score: 0.56
DE  Interaction: Q96AL5; IntAct: EBI-5661036,EBI-741171; Score: 0.56
DE  Interaction: Q8IVT4; IntAct: EBI-5661036,EBI-14086479; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-5661036,EBI-739832; Score: 0.56
DE  Interaction: Q9P1Y5-2; IntAct: EBI-5661036,EBI-18121830; Score: 0.56
DE  Interaction: Q9UK33; IntAct: EBI-5661036,EBI-746277; Score: 0.56
DE  Interaction: P78358; IntAct: EBI-5661036,EBI-1188472; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-5661036,EBI-348259; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-5661036,EBI-1567797; Score: 0.56
DE  Interaction: O76064; IntAct: EBI-5661036,EBI-373337; Score: 0.56
DE  Interaction: Q8TAB5; IntAct: EBI-5661036,EBI-747505; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-5661036,EBI-536879; Score: 0.56
DE  Interaction: Q14119; IntAct: EBI-5661036,EBI-11980193; Score: 0.56
DE  Interaction: Q86VK4-3; IntAct: EBI-5661036,EBI-11741890; Score: 0.56
DE  Interaction: Q2TBA0; IntAct: EBI-7851314,EBI-5661036; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-5661036,EBI-2798416; Score: 0.56
DE  Interaction: Q9Y2P0; IntAct: EBI-5661036,EBI-5667516; Score: 0.56
DE  Interaction: O60941-5; IntAct: EBI-5661036,EBI-11984733; Score: 0.56
DE  Interaction: O95363; IntAct: EBI-5661036,EBI-2513774; Score: 0.56
DE  Interaction: O14964; IntAct: EBI-5661036,EBI-740220; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-5661036,EBI-5453285; Score: 0.56
DE  Interaction: Q9H0I2; IntAct: EBI-5661036,EBI-744099; Score: 0.56
DE  Interaction: Q9P2K3-2; IntAct: EBI-5661036,EBI-1504830; Score: 0.56
DE  Interaction: Q9H0A9-2; IntAct: EBI-5661036,EBI-11995806; Score: 0.56
DE  Interaction: Q9ULM2; IntAct: EBI-5661036,EBI-1105370; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-5661036,EBI-744556; Score: 0.56
DE  Interaction: Q9ULD5; IntAct: EBI-5661036,EBI-11975599; Score: 0.56
DE  Interaction: Q6ZNE5; IntAct: EBI-5661036,EBI-2690371; Score: 0.56
DE  Interaction: Q96PV4; IntAct: EBI-5661036,EBI-10171633; Score: 0.56
DE  Interaction: Q9BQ89; IntAct: EBI-5661036,EBI-1752811; Score: 0.56
DE  Interaction: P36508; IntAct: EBI-7254550,EBI-5661036; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-5661036,EBI-638194; Score: 0.56
DE  Interaction: Q8IYE0; IntAct: EBI-5661036,EBI-10749669; Score: 0.56
DE  Interaction: Q9UJV3-2; IntAct: EBI-5661036,EBI-10172526; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-5661036,EBI-742802; Score: 0.56
DE  Interaction: Q08117-2; IntAct: EBI-5661036,EBI-11741437; Score: 0.56
DE  Interaction: Q969G3; IntAct: EBI-5661036,EBI-455078; Score: 0.56
DE  Interaction: O95295; IntAct: EBI-5661036,EBI-296723; Score: 0.56
DE  Interaction: P13682; IntAct: EBI-11041653,EBI-5661036; Score: 0.56
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGL
SQ  EDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEE
SQ  YECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEV
SQ  FITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDF
SQ  IKDAVAMADRLGKFLKTKTDVEISAQPEFEDQTLDFSDVEQLMGSINTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDD
SQ  TVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAHNRAGPSPSSERAVYMTAPSPPIIKTKEIR
SQ  SCEEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRSEPATVH
SQ  TIGSYFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAF
SQ  ADVRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHE
SQ  FVHPCFSLEKPGCLKVHNGISMPKHVTFY
//
ID  Q9HCE0;
PN  Ectopic P granules protein 5 homolog;
GN  EPG5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29130391}. Lysosome {ECO:0000269|PubMed:29130391}.
DR  UNIPROT: Q9HCE0;
DR  UNIPROT: A2BDF3;
DR  UNIPROT: Q9H8C8;
DR  OMIM: 242840;
DR  OMIM: 615068;
DR  DisGeNET: 57724;
DE  Function: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. Plays a key role in innate and adaptive immune response triggered by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides from pathogens, and mediated by the nucleotide-sensing receptor TLR9. It is necessary for the translocation of CpG dinucleotides from early endosomes to late endosomes and lysosomes, where TLR9 is located (PubMed:29130391). {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:23222957, ECO:0000269|PubMed:29130391}.
DE  Disease: Vici syndrome (VICIS) [MIM:242840]: A rare congenital multisystem disorder characterized by agenesis of the corpus callosum, cataracts, pigmentary defects, progressive cardiomyopathy, and variable immunodeficiency. Affected individuals also have profound psychomotor retardation and hypotonia due to a myopathy. {ECO:0000269|PubMed:23222957, ECO:0000269|PubMed:25331754, ECO:0000269|PubMed:26917586, ECO:0000269|PubMed:27343256, ECO:0000269|PubMed:28168853, ECO:0000269|PubMed:29130391}. Note=The disease is caused by mutations affecting the gene represented in this entry. Affected individuals show homozygosity or compound heterozygosity for truncating mutations, aberrant splicing and/or missense mutations. Parental studies suggest recessive inheritance with no carrier manifestation (PubMed:23222957). {ECO:0000269|PubMed:23222957}.
DE  Reference Proteome: Yes;
DE  Interaction: O55234; IntAct: EBI-991760,EBI-7244641; Score: 0.35
GO  GO:0005737;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:1990786;
GO  GO:0032456;
GO  GO:0008333;
GO  GO:0006862;
GO  GO:0034162;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAVKPQRRAKAKASRTKTKEKKKYETPQREESSEVSLPKTSREQEIPSLACEFKGDHLKVVTDSQLQDDASGQNESEM
SQ  FDVPLTSLTISNEESLTCNTEPPKEGGEARPCVGDSAVTPKVHPGDNVGTKVETPKNFTEVEENMSVQGGLSESAPQSNF
SQ  SYTQPAMENIQVRETQNSKEDKQGLVCSSEVPQNVGLQSSCPAKHGFQTPRVKKLYPQLPAEIAGEAPALVAVKPLLRSE
SQ  RLYPELPSQLELVPFTKEQLKILEPGSWLENVESYLEEFDSMAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLTSDCQN
SQ  AKSRLWQFKEEQMSVQGICADQVKVFSYHRYQRVEMNENALVELKKLFDAKSEHLHQTLALHSYTSVLSRLQVESYIYAL
SQ  LSSSAVLRSSAIHQQGRASKQTESIPSDLCQLKECISVLFMFTRRVNEDTQFHDDILLWLQKLVSVLQRVGCPGDHLFLL
SQ  NHILRCPAGVSKWAVPFIQIKVLHNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSERKPSSSGPGSGTWTLVDEGGEED
SQ  EDPETSWILLNEDDLVTILAQFPFHELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLETFNRARYRQFV
SQ  KRIGYMIRMTLGYVSDHWAQYVSHNQGSGLAQQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQML
SQ  WKLFYLMHQVESENLQQLSSSLQPAQCKQQLQDPEHFTNFEKCLSSMNSSEEICLLTTFAQMAQARRTNVDEDFIKIIVL
SQ  EIYEVSYVTLSTRETFSKVGRELLGTITAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWQPSASEIAVIRDWLL
SQ  NYNLTVVKNKLACVILEGLNWGFAKQATLHLDQAVHAEVALMVLEAYQKYLAQKPYAGILSESMKQVSYLASIVRYGETP
SQ  ETSFNQWAWNLILRLKLHKNDYGIQPNCPAVPFSVTVPDMTESPTFHPLLKAVKAGMPIGCYLALSMTAVGHSIEKFCAE
SQ  GIPLLGILVQSRHLRTVVHVLDKILPLFYPCQYYLLKNEQFLSHLLLFLHLDSGVPQGVTQQVTHKVAQHLTGASHGDNV
SQ  KLLNSMIQAHISVSTQPNEVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKAAFQLMQEDCIQKLLYQQHKNALGYH
SQ  CDRSLLSSLVSWIVAGNITPSFVEGLATPTQVWFAWTVLNMESIFEEDSQLRRVIEGELVINSAFTPDQALKKAQTQLKL
SQ  PIVPSLQRLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPIDGCIGRRFFQSPAHINLLKEMKRRLTEVA
SQ  DFHHAASKALRVPAEGSEGLPESHSGTPGYLTSPELHKELVRLFNVYILWLEDENFQKGDTYIPSLPKHYDIHRLAKVMQ
SQ  NQQDLWMEYLNMERIYHEFQETVGLWTQAKLESHSTPCSLSVQLDFTDPLLAKERVLSNLRKHEAPQPPLALHPTKPPVP
SQ  VISSAVLLSQKDATQLVCTDLNLLQQQARTAALRESQQVALDGELLDTMPKQYVNREEQTTLHLECRGSSGKKCQGAAVV
SQ  TVQFEGMHKNEAISQQLHVLRKEVKQLQAEAAKPPSLNIVEAAVHAENLITALVNAYKLQPTPGIQKVGISLFFTIVDYV
SQ  SDETQRHPPTRQFFTSCIEILGQVFISGIKSECRKVLETILKNSRLCSLLSPFFTPNAAPAEFIQLYEQVVKFLSEDNSD
SQ  MIFMLLTKFDLKQWLSATKPPLSDRTRLLESIHLALTAWGLEPDEDILMPFNLFCKHWTYLLLYQFPDQYSDILRLLMQS
SQ  SAEQLLSPECWKATLRALGCCAPSCQQGAASTEGAVLPSSSDALLSDKQVMETIQWLSDFFYKLRLSKMDFKSFGLFSKW
SQ  SPYMADVKTFLGYLVKRLIDLEMTCLAQDPTASRKTVLKSLHSVIIQLFKPWILVLEDNESSQQRHYPWLESDTVVASSI
SQ  VQLFTDCIDSLHESFKDKLLPGDAGALWLHLMHYCEACTAPKMPEFILYAFHSTYRKLPWKDLHPDQMLMEAFFKVERGS
SQ  PKSCFLFLGSVLCEVNWVSVLSDAWNSSPHPETRSMIVCLLFMMILLAKEVQLVDQTDSPLLSLLGQTSSLSWHLVDIVS
SQ  YQSVLSYFSSHYPPSIILAKESYAELIMKLLKVSAGLSIPTDSQKHLDAVPKCQAFTHQMVQFLSTLEQNGKITLAVLEQ
SQ  EMSKLLDDIIVFNPPDMDSQTRHMALSSLFMEVLMMMNNATIPTAEFLRGSIRTWIGQKMHGLVVLPLLTAACQSLASVR
SQ  HMAETTEACITAYFKESPLNQNSGWGPILVSLQVPELTMEEFLQECLTLGSYLTLYVYLLQCLNSEQTLRNEMKVLLILS
SQ  KWLEQVYPSSVEEEAKLFLWWHQVLQLSLIQTEQNDSVLTESVIRILLLVQSRQNLVAEERLSSGILGAIGFGRKSPLSN
SQ  RFRVVARSMAAFLSVQVPMEDQIRLRPGSELHLTPKAQQALNALESMASSKQYVEYQDQILQATQFIRHPGHCLQDGKSF
SQ  LALLVNCLYPEVHYLDHIR
//
ID  P19525;
PN  Interferon-induced, double-stranded RNA-activated protein kinase;
GN  EIF2AK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Nuclear localization is elevated in acute leukemia, myelodysplastic syndrome (MDS), melanoma, breast, colon, prostate and lung cancer patient samples or cell lines as well as neurocytes from advanced Creutzfeldt-Jakob disease patients.
DR  UNIPROT: P19525;
DR  UNIPROT: A8K3P0;
DR  UNIPROT: D6W584;
DR  UNIPROT: E9PC80;
DR  UNIPROT: Q52M43;
DR  UNIPROT: Q7Z6F6;
DR  UNIPROT: Q9UIR4;
DR  PDB: 1QU6;
DR  PDB: 2A19;
DR  PDB: 2A1A;
DR  PDB: 3UIU;
DR  PDB: 6D3K;
DR  PDB: 6D3L;
DR  Pfam: PF00035;
DR  Pfam: PF00069;
DR  PROSITE: PS50137;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 176871;
DR  DisGeNET: 5610;
DE  Function: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up- regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD- mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. {ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035}.
DE  Reference Proteome: Yes;
DE  Interaction: O75569; IntAct: EBI-640775,EBI-713955; Score: 0.74
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-640775; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-640775; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-353366,EBI-640775; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-351007,EBI-640775; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-640775; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-295634,EBI-640775; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-720116,EBI-640775; Score: 0.35
DE  Interaction: P35570; IntAct: EBI-640775,EBI-520230; Score: 0.44
DE  Interaction: Q96FF9; IntAct: EBI-718805,EBI-640775; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-352398,EBI-640775; Score: 0.35
DE  Interaction: Q6PFD6; IntAct: EBI-11093565,EBI-640775; Score: 0.35
DE  Interaction: Q6PJG2; IntAct: EBI-2795569,EBI-640775; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-1564650,EBI-640775; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-8361659,EBI-640775; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-749627,EBI-640775; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-640775; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-10194262,EBI-640775; Score: 0.35
DE  Interaction: P78563-4; IntAct: EBI-12002366,EBI-640775; Score: 0.56
DE  Interaction: Q96C10; IntAct: EBI-744193,EBI-640775; Score: 0.50
DE  Interaction: Q8IY81; IntAct: EBI-640775,EBI-744088; Score: 0.50
DE  Interaction: P05455; IntAct: EBI-640775,EBI-358037; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-640775,EBI-356811; Score: 0.35
DE  Interaction: Q9HCE1; IntAct: EBI-640775,EBI-1055820; Score: 0.50
DE  Interaction: O00458; IntAct: EBI-640775,EBI-726897; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-640775,EBI-1048111; Score: 0.35
DE  Interaction: P07910; IntAct: EBI-640775,EBI-357966; Score: 0.35
DE  Interaction: P56537; IntAct: EBI-640775,EBI-372243; Score: 0.50
DE  Interaction: Q13310; IntAct: EBI-640775,EBI-372844; Score: 0.35
DE  Interaction: Q9NUL3; IntAct: EBI-640775,EBI-722938; Score: 0.50
DE  Interaction: Q9NZM5; IntAct: EBI-640775,EBI-720156; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-640775,EBI-1056249; Score: 0.35
DE  Interaction: Q9H0E2; IntAct: EBI-640775,EBI-74615; Score: 0.50
DE  Interaction: Q7L2E3; IntAct: EBI-640775,EBI-1211456; Score: 0.62
DE  Interaction: Q9H0D6; IntAct: EBI-640775,EBI-372110; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-640775,EBI-457097; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-640775,EBI-353803; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-640775,EBI-358174; Score: 0.35
DE  Interaction: O60812; IntAct: EBI-640775,EBI-1046507; Score: 0.35
DE  Interaction: Q8WTT2; IntAct: EBI-640775,EBI-2512539; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-640775,EBI-395506; Score: 0.50
DE  Interaction: Q9NX58; IntAct: EBI-640775,EBI-713507; Score: 0.35
DE  Interaction: Q8N5Z5; IntAct: EBI-640775,EBI-743960; Score: 0.35
DE  Interaction: Q96CT7; IntAct: EBI-640775,EBI-5461329; Score: 0.35
DE  Interaction: Q00577; IntAct: EBI-640775,EBI-1045860; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-640775,EBI-356283; Score: 0.35
DE  Interaction: Q15633; IntAct: EBI-640775,EBI-978581; Score: 0.50
DE  Interaction: Q6P2E9; IntAct: EBI-640775,EBI-1006038; Score: 0.50
DE  Interaction: Q9Y285; IntAct: EBI-640775,EBI-725361; Score: 0.35
DE  Interaction: Q9UL40; IntAct: EBI-640775,EBI-2462313; Score: 0.50
DE  Interaction: P16403; IntAct: EBI-640775,EBI-358372; Score: 0.35
DE  Interaction: Q00526; IntAct: EBI-640775,EBI-1245761; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-640775,EBI-876302; Score: 0.35
DE  Interaction: Q9BVP2; IntAct: EBI-640775,EBI-641642; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-640775,EBI-352022; Score: 0.50
DE  Interaction: P04591; IntAct: EBI-640775,EBI-6179727; Score: 0.40
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-640775; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-640775; Score: 0.35
DE  Interaction: O00425; IntAct: EBI-640775,EBI-1058566; Score: 0.35
DE  Interaction: Q9Y6M1; IntAct: EBI-640775,EBI-1024419; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-352572,EBI-640775; Score: 0.40
DE  Interaction: P05198; IntAct: EBI-640775,EBI-1056162; Score: 0.78
DE  Interaction: Q9UJU6; IntAct: EBI-640775,EBI-751783; Score: 0.40
DE  Interaction: Q15628-2; IntAct: EBI-640775,EBI-20868057; Score: 0.40
DE  Interaction: P51608; IntAct: EBI-1189067,EBI-640775; Score: 0.35
DE  Interaction: Q96SL4; IntAct: EBI-749411,EBI-640775; Score: 0.35
DE  Interaction: Q8N6M8-2; IntAct: EBI-21771049,EBI-640775; Score: 0.35
DE  Interaction: Q27968; IntAct: EBI-640793,EBI-640775; Score: 0.59
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005840;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0004694;
GO  GO:0042802;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0019888;
GO  GO:0004674;
GO  GO:0003723;
GO  GO:0000186;
GO  GO:0034198;
GO  GO:0051607;
GO  GO:0030968;
GO  GO:0045087;
GO  GO:0030683;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0033689;
GO  GO:0017148;
GO  GO:0045071;
GO  GO:0032722;
GO  GO:0001819;
GO  GO:0051092;
GO  GO:1901224;
GO  GO:0032874;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:1901532;
GO  GO:1902036;
GO  GO:1902033;
GO  GO:1900225;
GO  GO:0035455;
GO  GO:0009615;
GO  GO:0006412;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKK
SQ  AVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKL
SQ  AYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAK
SQ  RSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNI
SQ  VHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITK
SQ  GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE
SQ  LLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC
//
ID  Q8N3K9;
PN  Cardiomyopathy-associated protein 5;
GN  CMYA5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm {ECO:0000250|UniProtKB:Q70KF4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:20634290}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes (By similarity). In skeletal muscles, localizes along myofiber periphery, at costameres (By similarity). Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}.
DR  UNIPROT: Q8N3K9;
DR  UNIPROT: A0PJB7;
DR  UNIPROT: Q05CT4;
DR  UNIPROT: Q2NKX1;
DR  UNIPROT: Q2T9G9;
DR  UNIPROT: Q69YQ8;
DR  UNIPROT: Q69YQ9;
DR  UNIPROT: Q6P517;
DR  UNIPROT: Q6P5U3;
DR  UNIPROT: Q7Z4I1;
DR  UNIPROT: Q86T34;
DR  UNIPROT: Q86T49;
DR  UNIPROT: Q8N3S4;
DR  UNIPROT: Q8N3S7;
DR  UNIPROT: Q8NAG8;
DR  UNIPROT: Q9UK88;
DR  Pfam: PF00041;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DR  OMIM: 612193;
DR  DisGeNET: 202333;
DE  Function: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A (By similarity). May function as a repressor of calcineurin- mediated transcriptional activity. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration (By similarity). Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q70KF4}.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-2323272,EBI-296723; Score: 0.37
DE  Interaction: Self; IntAct: EBI-2323272,EBI-2323272; Score: 0.37
DE  Interaction: Q96EB6; IntAct: EBI-1802965,EBI-2323272; Score: 0.40
DE  Interaction: Q9NTG7; IntAct: EBI-724621,EBI-2323272; Score: 0.40
DE  Interaction: Q14324; IntAct: EBI-5653200,EBI-2323272; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-748974,EBI-2323272; Score: 0.37
DE  Interaction: O75923; IntAct: EBI-2323272,EBI-2799016; Score: 0.54
DE  Interaction: P20807; IntAct: EBI-2323272,EBI-5655000; Score: 0.37
DE  Interaction: Q8N3C7; IntAct: EBI-2323272,EBI-5655540; Score: 0.37
DE  Interaction: P40189; IntAct: EBI-2323272,EBI-1030834; Score: 0.37
DE  Interaction: Q7L1Q6; IntAct: EBI-2323272,EBI-1046727; Score: 0.40
DE  Interaction: P43686; IntAct: EBI-2323272,EBI-743997; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-2323272; Score: 0.40
GO  GO:0031430;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASRDSNHAGESFLGSDGDEEATRELETEEESEGEEDETAAESEEEPDSRLSDQDEEGKIKQEYIISDPSFSMVTVQRED
SQ  SGITWETNSSRSSTPWASEESQTSGVCSREGSTVNSPPGNVSFIVDEVKKVRKRTHKSKHGSPSLRRKGNRKRNSFESQD
SQ  VPTNKKGSPLTSASQVLTTEKEKSYTGIYDKARKKKTTSNTPPITGAIYKEHKPLVLRPVYIGTVQYKIKMFNSVKEELI
SQ  PLQFYGTLPKGYVIKEIHYRKGKDASISLEPDLDNSGSNTVSKTRKLVAQSIEDKVKEVFPPWRGALSKGSESLTLMFSH
SQ  EDQKKIYADSPLNATSALEHTVPSYSSSGRAEQGIQLRHSQSVPQQPEDEAKPHEVEPPSVTPDTPATMFLRTTKEECEL
SQ  ASPGTAASENDSSVSPSFANEVKKEDVYSAHHSISLEAASPGLAASTQDGLDPDQEQPDLTSIERAEPVSAKLTPTHPSV
SQ  KGEKEENMLEPSISLSEPLMLEEPEKEEIETSLPIAITPEPEDSNLVEEEIVELDYPESPLVSEKPFPPHMSPEVEHKEE
SQ  ELILPLLAASSPEHVALSEEEREEIASVSTGSAFVSEYSVPQDLNHELQEQEGEPVPPSNVEAIAEHAVLSEEENEEFEA
SQ  YSPAAAPTSESSLSPSTTEKTSENQSPLFSTVTPEYMVLSGDEASESGCYTPDSTSASEYSVPSLATKESLKKTIDRKSP
SQ  LILKGVSEYMIPSEEKEDTGSFTPAVAPASEPSLSPSTTEKTSECQSPLPSTATSEHVVPSEGEDLGSERFTPDSKLISK
SQ  YAAPLNATQESQKKIINEASQFKPKGISEHTVLSVDGKEVIGPSSPDLVVASEHSFPPHTTEMTSECQAPPLSATPSEYV
SQ  VLSDEEAVELERYTPSSTSASEFSVPPYATPEAQEEEIVHRSLNLKGASSPMNLSEEDQEDIGPFSPDSAFVSEFSFPPY
SQ  ATQEAEKREFECDSPICLTSPSEHTILSDEDTEEAELFSPDSASQVSIPPFRISETEKNELEPDSLLTAVSASGYSCFSE
SQ  ADEEDIGSTAATPVSEQFSSSQKQKAETFPLMSPLEDLSLPPSTDKSEKAEIKPEIPTTSTSVSEYLILAQKQKTQAYLE
SQ  PESEDLIPSHLTSEVEKGEREASSSVAAIPAALPAQSSIVKEETKPASPHSVLPDSVPAIKKEQEPTAALTLKAADEQMA
SQ  LSKVRKEEIVPDSQEATAHVSQDQKMEPQPPNVPESEMKYSVLPDMVDEPKKGVKPKLVLNVTSELEQRKLSKNEPEVIK
SQ  PYSPLKETSLSGPEALSAVKMEMKHDSKITTTPIVLHSASSGVEKQVEHGPPALAFSALSEEIKKEIEPSSSTTTASVTK
SQ  LDSNLTRAVKEEIPTDSSLITPVDRPVLTKVGKGELGSGLPPLVTSADEHSVLAEEDKVAIKGASPIETSSKHLAWSEAE
SQ  KEIKFDSLPSVSSIAEHSVLSEVEAKEVKAGLPVIKTSSSQHSDKSEEARVEDKQDLLFSTVCDSERLVSSQKKSLMSTS
SQ  EVLEPEHELPLSLWGEIKKKETELPSSQNVSPASKHIIPKGKDEETASSSPELENLASGLAPTLLLLSDDKNKPAVEVSS
SQ  TAQGDFPSEKQDVALAELSLEPEKKDKPHQPLELPNAGSEFSSDLGRQSGSIGTKQAKSPITETEDSVLEKGPAELRSRE
SQ  GKEENRELCASSTMPAISELSSLLREESQNEEIKPFSPKIISLESKEPPASVAEGGNPEEFQPFTFSLKGLSEEVSHPAD
SQ  FKKGGNQEIGPLPPTGNLKAQVMGDILDKLSEETGHPNSSQVLQSITEPSKIAPSDLLVEQKKTEKALHSDQTVKLPDVS
SQ  TSSEDKQDLGIKQFSLMRENLPLEQSKSFMTTKPADVKETKMEEFFISPKDENWMLGKPENVASQHEQRIAGSVQLDSSS
SQ  SNELRPGQLKAAVSSKDHTCEVRKQVLPHSAEESHLSSQEAVSALDTSSGNTETLSSKSYSSEEVKLAEEPKSLVLAGNV
SQ  ERNIAEGKEIHSLMESESLLLEKANTELSWPSKEDSQEKIKLPPERFFQKPVSGLSVEQVKSETISSSVKTAHFPAEGVE
SQ  PALGNEKEAHRSTPPFPEEKPLEESKMVQSKVIDDADEGKKPSPEVKIPTQRKPISSIHAREPQSPESPEVTQNPPTQPK
SQ  VAKPDLPEEKGKKGISSFKSWMSSLFFGSSTPDNKVAEQEDLETQPSPSVEKAVTVIDPEGTIPTNFNVAEKPADHSLSE
SQ  VKLKTADEPRGTLVKSGDGQNVKEKSMILSNVEDLQQPKFISEVSREDYGKKEISGDSEEMNINSVVTSADGENLEIQSY
SQ  SLIGEKLVMEEAKTIVPPHVTDSKRVQKPAIAPPSKWNISIFKEEPRSDQKQKSLLSFDVVDKVPQQPKSASSNFASKNI
SQ  TKESEKPESIILPVEESKGSLIDFSEDRLKKEMQNPTSLKISEEETKLRSVSPTEKKDNLENRSYTLAEKKVLAEKQNSV
SQ  APLELRDSNEIGKTQITLGSRSTELKESKADAMPQHFYQNEDYNERPKIIVGSEKEKGEEKENQVYVLSEGKKQQEHQPY
SQ  SVNVAESMSRESDISLGHSLGETQSFSLVKATSVTEKSEAMLAEAHPEIREAKAVGTQPHPLEESKVLVEKTKTFLPVAL
SQ  SCRDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFRESELSKGGSVDITKETVKQGFQEKAVGTQPRPLEESKVLVEKT
SQ  KTFLPVVLSCHDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFKESELWKGGSVDITKESMKEGFPSKESERTLARPFD
SQ  ETKSSETPPYLLSPVKPQTLASGASPEINAVKKKEMPRSELTPERHTVHTIQTSKDDTSDVPKQSVLVSKHHLEAAEDTR
SQ  VKEPLSSAKSNYAQFISNTSASNADKMVSNKEMPKEPEDTYAKGEDFTVTSKPAGLSEDQKTAFSIISEGCEILNIHAPA
SQ  FISSIDQEESEQMQDKLEYLEEKASFKTIPLPDDSETVACHKTLKSRLEDEKVTPLKENKQKETHKTKEEISTDSETDLS
SQ  FIQPTIPSEEDYFEKYTLIDYNISPDPEKQKAPQKLNVEEKLSKEVTEETISFPVSSVESALEHEYDLVKLDESFYGPEK
SQ  GHNILSHPETQSQNSADRNVSKDTKRDVDSKSPGMPLFEAEEGVLSRTQIFPTTIKVIDPEFLEEPPALAFLYKDLYEEA
SQ  VGEKKKEEETASEGDSVNSEASFPSRNSDTDDGTGIYFEKYILKDDILHDTSLTQKDQGQGLEEKRVGKDDSYQPIAAEG
SQ  EIWGKFGTICREKSLEEQKGVYGEGESVDHVETVGNVAMQKKAPITEDVRVATQKISYAVPFEDTHHVLERADEAGSHGN
SQ  EVGNASPEVNLNVPVQVSFPEEEFASGATHVQETSLEEPKILVPPEPSEERLRNSPVQDEYEFTESLHNEVVPQDILSEE
SQ  LSSESTPEDVLSQGKESFEHISENEFASEAEQSTPAEQKELGSERKEEDQLSSEVVTEKAQKELKKSQIDTYCYTCKCPI
SQ  SATDKVFGTHKDHEVSTLDTAISAVKVQLAEFLENLQEKSLRIEAFVSEIESFFNTIEENCSKNEKRLEEQNEEMMKKVL
SQ  AQYDEKAQSFEEVKKKKMEFLHEQMVHFLQSMDTAKDTLETIVREAEELDEAVFLTSFEEINERLLSAMESTASLEKMPA
SQ  AFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPNSATSTTIAVYWSMNKEDVIDSFQVYCMEEPQDDQEVNELVEEYR
SQ  LTVKESYCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIRAEDCTVCWNTATIRWRPTTPEATETYTLEY
SQ  CRQHSPEGEGLRSFSGIKGLQLKVNLQPNDNYFFYVRAINAFGTSEQSEAALISTRGTRFLLLRETAHPALHISSSGTVI
SQ  SFGERRRLTEIPSVLGEELPSCGQHYWETTVTDCPAYRLGICSSSAVQAGALGQGETSWYMHCSEPQRYTFFYSGIVSDV
SQ  HVTERPARVGILLDYNNQRLIFINAESEQLLFIIRHRFNEGVHPAFALEKPGKCTLHLGIEPPDSVRHK
//
ID  Q91ZU6;
PN  Dystonin;
GN  Dst;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell projection, axon {ECO:0000269|PubMed:17287360}. Note=Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons (By similarity). Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells. {ECO:0000250, ECO:0000269|PubMed:14576348}. [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and cytoplasmic actin filaments (PubMed:19932097). Localizes to vesicule- like structures associated with microtubules (PubMed:14581450, PubMed:17287360). {ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}. [Isoform 2]: Cell membrane, sarcolemma. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. [Isoform 5]: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes (By similarity). Localizes to actin and intermediate filaments cytoskeletons. {ECO:0000250}. [Isoform 6]: Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single- pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:14576348}. Note=Associates with actin cytoskeleton in sensory neurons (By similarity). Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus. {ECO:0000250}. [Isoform 7]: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cell membrane; Lipid-anchor.
DR  UNIPROT: Q91ZU6;
DR  UNIPROT: E9PXE5;
DR  UNIPROT: E9QL23;
DR  UNIPROT: Q1KP04;
DR  UNIPROT: Q3I6J6;
DR  UNIPROT: Q60824;
DR  UNIPROT: Q60845;
DR  UNIPROT: Q8K5D4;
DR  UNIPROT: Q91ZU7;
DR  UNIPROT: Q91ZU8;
DR  UNIPROT: Q9WU50;
DR  UNIPROT: S4R1U5;
DR  PDB: 2IAK;
DR  Pfam: PF00307;
DR  Pfam: PF13499;
DR  Pfam: PF02187;
DR  Pfam: PF00681;
DR  Pfam: PF17902;
DR  Pfam: PF00435;
DR  Pfam: PF18373;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51460;
DR  PROSITE: PS50002;
DE  Function: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1. {ECO:0000269|PubMed:17287360}. [Isoform 5]: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. [Isoform 6]: required for bundling actin filaments around the nucleus.
DE  Reference Proteome: Yes;
DE  Interaction: Q4U2R1; IntAct: EBI-11068779,EBI-446159; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-1811542,EBI-446159; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-7280013,EBI-446159; Score: 0.35
DE  Interaction: O70589; IntAct: EBI-771402,EBI-446159; Score: 0.35
DE  Interaction: P35279; IntAct: EBI-444674,EBI-446159; Score: 0.35
DE  Interaction: P21807; IntAct: EBI-446227,EBI-446159; Score: 0.54
DE  Interaction: P19527; IntAct: EBI-446360,EBI-446159; Score: 0.37
DE  Interaction: P16884; IntAct: EBI-446159,EBI-446344; Score: 0.37
GO  GO:0015629;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0005925;
GO  GO:0031673;
GO  GO:0030056;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0005882;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0060053;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0097038;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0042803;
GO  GO:0005198;
GO  GO:0007409;
GO  GO:0007155;
GO  GO:0031122;
GO  GO:0031581;
GO  GO:0045104;
GO  GO:0046907;
GO  GO:0031110;
GO  GO:0008090;
GO  GO:0042060;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDT
SQ  LPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLW
SQ  TQQATEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDE
SQ  KSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVVTMSERTFPNNPLELKALYNQYLQFKEKE
SQ  IPPKEMEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLDMLQQIATRVQRDSVSC
SQ  EDKLILARNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNEC
SQ  SSVYSKGRMLTTEQTKLMISGITQSLNSGFAQTLHPSLNSGLTQSLTPSLTSSSVTSGLSSGMTSRLTPSVTPVYAPGFP
SQ  SVVAPNFSLGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEVNMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLEN
SQ  HKNVHRAIEEFESSLKEAKISEIQMTAPLKLSYTDKLHRLESQYAKLLNTSRNQERHLDTLHNFVTRATNELIWLNEKEE
SQ  SEVAYDWSERNSSVARKKSYHAELMRELEQKEESIKAVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQH
SQ  IQENSAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEKEELLQYRSVVAGLMGRAKTVVQLKPRN
SQ  PDNPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDFANRIEQQYQS
SQ  VLTLWHESHINMKSVVSWHYLVNEIDRIRASNVASIKTMLPGEHQQVLSNLQSRLEDFLEDSQESQIFSGSDISQLEKEV
SQ  SVCRKYYQELLKSAEREEQEESVYNLYISEVRNIRLRLESCEDRLIRQIRTPLERDDLHESMLRITEQEKLKKELDRLKD
SQ  DLGTITNKCEEFFSQAADSPSVPALRSELSVVIQSLSQIYSMSSTYIEKLKTVNLVLKNTQAAEALVKLYETKLCEEEAV
SQ  IADKNNIENLMSTLKQWRSEVDEKREVFHALEDELQKAKAISDEMFKTHKERDLDFDWHKEKADQLVERWQSVHVQIDNR
SQ  LRDLEGIGKSLKHYRDSYHPLDDWIQHIETTQRKIQENQPENSKALALQLNQQKMLVSEIEVKQSKMDECQKYSEQYSAA
SQ  VKDYELQTMTYRAMVESQQKSPVKRRRIQSSADLVIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLDEEKKQ
SQ  HIEKAKELQKWVSNISKTLGDGEKAGKPLFSKQQMSSKEISTKKEQFSEALQTTQIFLAKHGDKLTEEERSDLEKQVKTL
SQ  QEGYNLLFSESLKQQELQPSGESKVPEKPDKVIAGTINQTTGEVLSVFQAVLRGLIDYETGIRLLEAQLVITGLISPELR
SQ  KCFDLRDAESHGLIDEQVLRQLKELNRAKQLISTASPTSIPVLDSLAQGMVSESMAIRVLEILLSAGPLLVPATGEHLTL
SQ  QQAFQQNLISSALFSKVLERQDTCKDLIDPCTSEKVSLTDMVQRSILQENTRMWLLPVRPQEAGRITLKCGRSVSILRAA
SQ  HEGLIDRETMFRLLGAQLLSGGLIDCNSGQKMTVEEAVAEGVIDRDTASSILTYQVQTGGIVHSNPAKRLTVDEAVQCEL
SQ  ITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELASKILNGRQKIAALYIPESSQVIGLDAAKQLGIIDNN
SQ  TASVLKSVTLPDKMPDLGDLEDCKNAKRWLSFCKLQPSTVHDYRQEEGGSDGEEPVTAQSSEQTKKLFLSYLMVNSYMDA
SQ  HTGQRLLLYDGDLDEAVGMLLESCGTELGADTSTRESLSVLTIPDAFPDCALSEEKHECSAAAAGPDKCHYSHPGHKESL
SQ  ENAKWDMNEAFCKMGNNDSNGELPRPENLADTTVVQKGSESPSRVRVPKPTSSSTQPEGSVLRPESGSILKGCKSQSEPV
SQ  TKKYPDGANHSHFLTSETSRPCDSNEREDEENIQKGPSVFDYSPRLSALLSHDELRQSQGRFSDTSTPQNTGYLCEASTL
SQ  SPSDQRVLADQSTREKFQDQFLGIAAISVSLQGAPCGQKPVDTECSSSQVHYHSEESMSDASAESGATRQTDESEKTGSK
SQ  VEDNSCTMVPGGGSRNDNTSDCGPLSHKGAIDAGDYETSLLAGQQSDTATDSDSDDYFYDTPLFEDEDHDSLILQGDDRD
SQ  CLQPEDYDTSLQEENDRTPPPDDIFYDVMKEKENPEFPHGGMDESLGVENKVCCPQGFPVGIEKPELYLAGEKEFNSGGS
SQ  EQLVESVSESENPPGLWDSESDSLTEGEIIGRKERLGASLTPDGHWRGDREECDTSRESQSDTDGVGSIQSSESYRPYMS
SQ  DGSDLDEEDNGGRSSEDSGDGRGGQGVADEGGEPQYQADPTQLYTAIRKEHGGETQNVSDMIPLDKTHSYSPLETQHGAG
SQ  VFQPESAGRGGWDTERSSHPELTTEADEEDEASLSTHMATKGVSLSNAEGTASEEIRLVQGPDSTGILKAEDLENVSPEI
SQ  SPSSDNIVRSEAELGGGASEDGHLSFTGSDRDQQGPGRGLVKGRDGQSDKLVDETSIREMGFQKEGVLMSSPEEGGEEER
SQ  DLEPFPNGSATESLNMGKSQVPPLLTHTEELSHRGAPHTTTMTTTMTLEGEAKNVQTGLTESPVLLETLAEIFDTPASKV
SQ  TRADLTSAVTASEMKSQVKEDSLTGGPEKETGPCTSLGHCDKCIHVDMLEPNEHTPSCALVAPPTVKDNLCSVNNAGEKS
SQ  VRPQEDWPPAAEVRLSDACVEESISEGKAGILQFTPENSDSTLSRLPHQSVAGWGKSADSVQARLPVSGVRHTSADTLDV
SQ  GCPQLESSREKASAEEEPHRERALSLKPQEREHHMLGFVEDGRSILKSSLDKVHMNLQEVGDPSAGTGTKISIQNLIRRA
SQ  ILSELPNEVSNVPSHGISPISNSSEVRAESGGDPFCITSFLHLLKQNQPPQETPGISELAKVLTQMDCDPEQRGLGSELL
SQ  PPQLKNAFYKLLFDGYATEKDQAEALGQTSCAVPKMAEEKPHVCSDLRNKEGHHCPLNPQAVGEAEVEPFSVHIAALPGG
SQ  EKLGELCSEPPEHSESTSGSKERSSDSSSKEKCSNGLQQCLQHTEKMHEYLVLLQDMKPPLDNQASVESSLEALKSQLKQ
SQ  LEAFELGLAPIAVFLRKDLKLAEEFLKSFPSDLPRRHHEELSKSHQRLQNAFSSLSSVSSERMKLIKLAINSEMSKLAVR
SQ  HEDFLHKLTSYSDWVSEKSRSVKAIQTVNVQDTELVKNSVKFLKNVLADLSHTKMQLETTAFDVQSFISDYAQDLSPSQS
SQ  RQLLRLLNTTQKGFLDLQELVTTEADRLEALLQLEQELGHQKVVAERQQEYREKLQGLCDLLTQTENRLISNQEAFVIGD
SQ  GTVELQKYQSKQEELQRDMQGSTQAMEEIVRNTELFLKESGDELSQADRALIEQKLNEVKMKCAQLNLKAEQSRKELDKA
SQ  VTTALKEETEKVAAVRQLEESKTKIENLLNWLSNVEEDSEGVWTKHTQPMEQNGTYLHEGDSKLGAGEEDEVNGNLLETD
SQ  AEGHSEATKGNLNQQYEKVKAQHGKIMAQHQAVLLATQSAQVLLEKQGHYLSPEEKEKLQKNTQELKVHYEKVLAECEKK
SQ  VKLTHSLQEELEKFDTDYSEFEHWLQQSEQELANLEAGADDLSGLMDKLTRQKSFSEDVISHKGDLRYITISGNRVIDAA
SQ  KSCSKRDSDRIGKDSVETSATHREVQTKLDQVTDRFRSLYSKCSVLGNNLKDLVDQYQQYEDASCGLLSGLQACEAKASK
SQ  HLREPIALDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDAKGSLLPAKNDIQKTLDDIVGRYDDLSKCVNERN
SQ  EKLQITLTRSLSVQDALDEMLDWMGSVESSLVKPGQVPLNSTALQDLISKDTMLEQDITGRQSSINAMNEKVKTFIETTD
SQ  PSTASSLQAKMKDLSARFSEASQKHKEKLAKMVELKAKVEQFEKLSDKLQTFLETQSQALTEVAMPGKDVPELSQHMQES
SQ  TAKFLEHRKDLEALHSLLKEISSHGLPGDKALVFEKTNNLSRKFKEMEDTIQEKKDALSSCQEQLSAFQTLAQSLKTWIK
SQ  ETTKQVPVVKPSLGTEDLRKSLEETKKLQEKWNLKAPEIHKANNSGVSLCNLLSALISPAKAIAAAKSGGVILNGEGTDT
SQ  NTQDFLANKGLTSIKKDMTDISHSYEDLGLLLKDKIVELNTKLSKLQKAQEESSAMMQWLEKMNKTASRWRQTPTPADTE
SQ  SVKLQVEQNKSFEAELKQNVNKVQELKDKLSELLEENPEAPEAQSWKQALAEMDTKWQELNQLTMDRQQKLEESSNNLTQ
SQ  FQTTEAQLKQWLMEKELMVSVLGPLSIDPNMLNTQKQQVQILLQEFDTRKPQYEQLTAAGQGILSRPGEDPSLHGIVNEQ
SQ  LEAVTQKWDNLTGQLRDRCDWIDQAIVKSTQYQSLLRSLSGTLTELDDKLSSGLTSGALPDAVNQQLEAAQRLKQEIEQQ
SQ  APKIKEAQEVCEDLSALVKEEYLKAELSRQLEGILKSFKDIEQKTENHVQHLQSACASSHQFQQMSKDFQAWLDAKKEEQ
SQ  RDSPPISAKLDVLESLLNSQKDFGKTFTEQSNIYEKTISEGENLLLKTQGAEKAALQLQLNTMKTDWDRFRKQVKEREEK
SQ  LKDSLEKALKYREQVETLRPWIDRCQHSLDGVTFSLDPTESESSIAELKSLQKEMDHHFGMLELLNNTANSLLSVCEVDK
SQ  EAVTEENQSLMEKVNRVTEQLQSKTVSLENMAQKFKEFQEVSRDTQRQLQDTKEQLEVHHSLGPQAYSNKHLSVLQAQQK
SQ  SLQTLKQQVDEAKRLAQDLVVEAADSKGTSDVLLQAETLAEEHSELSQQVDEKCSFLETKLQGLGHFQNTIREMFSQFTE
SQ  CDDELDGMAPVGRDAETLRKQKACMQTFLKKLEALMASNDSANRTCKMMLATEETSPDLIGVKRDLEALSKQCNKLLDRA
SQ  KTREEQVDGATEKLEEFHRKLEEFSTLLQKAEEHEESQGPVGTETETINQQLDVFKVFQKEEIEPLQVKQQDVNWLGQGL
SQ  IQSAAANTCTQGLEHDLDSVNSRWKTLNKKVAQRTSQLQEALLHCGRFQDALESLLSWMADTEELVANQKPPSAEFKVVK
SQ  AQIQEQKLLQRLLEDRKSTVEVIKREGEKIAASAEPADRVKLTRQLSLLDSRWEALLSRAEARNRQLEGISVVAQEFHET
SQ  LEPLNEWLTAVEKKLANSEPIGTQAPKLEEQISQHKALQEDILLRKQSVDQALLNGLELLKQTTGDEVLIIQDKLEAIKA
SQ  RYKDITKLSADVAKTLEHALQLAGQLQSMHKELCNWLDKVEVELLSYETQGLKGEAASQVQERQKELKNEVRSNKALVDS
SQ  LNEVSSALLELVPWRAREGLEKTIAEDNERYRLVSDTITQKVEEIDAAILRSQQFEQAADAELSWITETQKKLMSLGDIR
SQ  LEQDQTSAQLQVQKAFTMDILRHKDIIDELVTSGHKIMTTSSEEEKQSMKKKLDKVLKKYDAVCQINSERHLQLERAQSL
SQ  VSQFWETYEELWPWLTETQRIISQLPAPALEYETLRRQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPKEGIYIQEK
SQ  YVAADTLYSQIKEDVKKRAVVLDEAISQSTQFHDKIDQILESLERIAERLRQPPSISAEVEKIKEQIGENKSVSVDMEKL
SQ  QPLYETLRQRGEEMIARSEGTEKDVSARAVQDKLDQMVFIWGSIHTLVEEREAKLLDVMELAEKFWCDHMSLVVTIKDTQ
SQ  DFIRDLEDPGIDPSVVKQQQEAAEAIREEIDGLQEELDMVITLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDR
SQ  VDRLEEAMQAAVQYQDGLQGIFDWVDIAGNKLATMSPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKV
SQ  TEEADKHTVQDPLMELKLIWDSLDERIVSRQHKLEGALLALGQFQHALDELLAWLTHTKGLLSEQKPVGGDPKAIEIELA
SQ  KHHVLQNDVLAHQSTVEAVNKAGNDLIESSEGEEASNLQYKLRILNQRWQDILEKTDQRKQQLDSALRQAKGFHGEIEDL
SQ  QQWLTDTERHLLASKPLGGLPETAKEQLNAHMEVCTAFAIKEETYKSLMLRGQQMLARCPRSAETNIDQDITNLKEKWES
SQ  VKSKLNEKKTKLEEALHLAMNFHNSLQDFINWLTQAEQTLNVASRPSLILDTILFQIDEHKVFANEVNSHREQIIELDKT
SQ  GTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDEARKRAKQFHEAWSKLMEWLEESEKSLDSELEIANDPD
SQ  KIKAQLVQHKEFQKSLGGKHSVYDTTNRTGRSLKEKTSLADDNLKLDNMLSELRDKWDTICGKSVERQNKLEEALLFSGQ
SQ  FTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKVFQKELGKRTSSVQALKRSARELIEGSRDDSSWVRVQMQE
SQ  LSTRWETVCALSISKQTRLESALQQAEEFHSVVHTLLEWLAEAEQTLRFHGALPDDEDALRTLIEQHKEFMKRLEEKRAE
SQ  LSKATGMGDALLAVCHPDSITTIKHWITIIQARFEEVLAWAKQHQQRLAGALAGLIAKQELLETLLAWLQWAETTLTEKD
SQ  KEVIPQEIEEVKTLIAEHQTFMEEMTRKQPDVDKVTKTYKRRATDPPSLQSHIPVLDKGRAGRKRFPASGFYPSGSQTQI
SQ  ETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKIT
SQ  RQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIEDEVTRQVAKCKCAKRFQVE
SQ  QIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKMLRSESNSSITATQPTLAKG
SQ  RTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSASSHACQAASPPVPAAASTPKGTPIQGSKLRLPGYL
SQ  SGKGFHSGEDSALITTAAARVRTQFAESRKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEIQSVCSDVETVPQTHRPV
SQ  PRAGSRPSTAKPSKIPTPQRRSPASKLDKSSKR
//
ID  Q8BPY9;
PN  Fidgetin-like protein 1;
GN  Fignl1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000269|PubMed:22110678}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage- induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}.
DR  UNIPROT: Q8BPY9;
DR  UNIPROT: Q3UF48;
DR  UNIPROT: Q8C2I6;
DR  UNIPROT: Q9ERZ5;
DR  Pfam: PF00004;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:17352653). May play a role in the control of male meiosis dynamic (PubMed:22110678). {ECO:0000250|UniProtKB:Q6PIW4, ECO:0000269|PubMed:17352653, ECO:0000269|PubMed:22110678}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0008568;
GO  GO:0046034;
GO  GO:0071479;
GO  GO:0031122;
GO  GO:0007140;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0001649;
GO  GO:0033687;
GO  GO:0051726;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METSSSMSVETTRSVQVDEWQKNYCVVTSSICTPKQKADAYRALLLHIQYAYANSEISQVFATNLFKRYTEKYSAIIDSD
SQ  NVVTGLNNYAESIFALAGSRQADSNKWQSGLSIDNVFKMSCVQEMMQAGKKFEESLLEPADASVVLCKEPTAFEVPQLSV
SQ  CGGSEDADILSSSGHDTDKTQAIPGSSLRCSPFQSARLPKETNTTKTCLTSSTSLGESATAAFHMTPLFGNTEKDTQSFP
SQ  KTSTGLNMFLSNLSCVPSGCENPQERKAFNDSDIIDILSNPTLNKAPSKTEDRGRREDNSLPTFKTAKEQLWVDQKKKGH
SQ  QSQHTSKSSNGVMKKSLGAGRSRGIFGKFVPPVSNKQDGSEQHAKKHKSSRAGSAEPAHLTDDCLKNVEPRMVELIMNEI
SQ  MDHGPPVHWDDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT
SQ  SKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEI
SQ  DEAARRRLVKRLYIPLPEASARKQIVGNLMSKEQCCLSDEETDLVVQQSDGFSGADMTQLCREASLGPIRSLHAADIATI
SQ  SPDQVRPIAYIDFENAFKTVRPTVSPKDLELYENWNETFGCGK
//
ID  Q08DM1;
PN  Dematin;
GN  DMTN;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q08DM1;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DE  Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0048821;
GO  GO:0030032;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRERSLSPKSTSPPPSPEVWAESRSPGTISQASAPRTAGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRAESTGGSPQS
SQ  KHPIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQRE
SQ  ELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHAGTSKSSSLPAYGRTTLSRLQSTDFSPSGSEAESPGLQ
SQ  NGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNRGRTKLPPGVDRMRLERHLSAEDFSRVFSMSPEEFGKLALWKRNELK
SQ  KKASLF
//
ID  Q06787;
PN  Synaptic functional regulator FMR1;
GN  FMR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18936162}. Nucleus, nucleolus {ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:16407062, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:24658146}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8515814}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24658146}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:9659908}. Perikaryon {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell projection, neuron projection {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000269|PubMed:15380484}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Cell junction, synapse {ECO:0000250|UniProtKB:P35922}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Cytoplasm, Stress granule {ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458}. Note=Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (By similarity). Localizes on meiotic pachytene-stage chromosomes (By similarity). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (By similarity). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:10196376). Localizes to cytoplasmic ribonucleoprotein granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:9659908, PubMed:14532325). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:12417734, PubMed:15380484). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (By similarity). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (By similarity). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (By similarity). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (PubMed:12417734, PubMed:18093976, PubMed:16636078). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (By similarity). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (PubMed:18632687, PubMed:18664458, PubMed:16636078). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:9659908}. [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24204304}. [Isoform 9]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}. [Isoform 10]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}. Note=Colocalizes with Colin and SMN in Cajal bodies (PubMed:24204304). [Isoform 11]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}.
DR  UNIPROT: Q06787;
DR  UNIPROT: A6NNH4;
DR  UNIPROT: D3DWT0;
DR  UNIPROT: D3DWT1;
DR  UNIPROT: D3DWT2;
DR  UNIPROT: G8JL90;
DR  UNIPROT: Q16578;
DR  UNIPROT: Q5PQZ6;
DR  UNIPROT: Q99054;
DR  PDB: 2BKD;
DR  PDB: 2FMR;
DR  PDB: 2LA5;
DR  PDB: 2QND;
DR  PDB: 4OVA;
DR  PDB: 4QVZ;
DR  PDB: 4QW2;
DR  PDB: 5DE5;
DR  PDB: 5DE8;
DR  PDB: 5DEA;
DR  PDB: 5UWJ;
DR  PDB: 5UWO;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DR  OMIM: 300623;
DR  OMIM: 300624;
DR  OMIM: 309550;
DR  OMIM: 311360;
DR  OMIM: 616034;
DR  DisGeNET: 2332;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (By similarity). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11532944, PubMed:11157796, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:7692601, PubMed:11719189, PubMed:11157796, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:7692601, PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). In vitro, binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:7688265, PubMed:7781595, PubMed:12950170, PubMed:15381419, PubMed:8156595). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage- dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage- dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large- conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations (PubMed:24813610). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:11532944, ECO:0000269|PubMed:11719189, ECO:0000269|PubMed:12594214, ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:12950170, ECO:0000269|PubMed:14703574, ECO:0000269|PubMed:15282548, ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:17057366, ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:18579868, ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19097999, ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:25692235, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:7692601, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8156595}. [Isoform 10]: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304). {ECO:0000269|PubMed:24204304}. [Isoform 6]: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304). {ECO:0000269|PubMed:24204304}. (Microbial infection) Acts as a positive regulator of influenza A virus (IAV) replication. Required for the assembly and nuclear export of the viral ribonucleoprotein (vRNP) components. {ECO:0000269|PubMed:24514761}.
DE  Disease: Fragile X syndrome (FXS) [MIM:300624]: An X-linked dominant disease characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most patients results from an amplification of a CGG repeat region in the FMR1 gene and abnormal methylation. {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:17850748, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24514761, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:7633450, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:8156595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8490650, ECO:0000269|PubMed:9659908}. Note=The disease is caused by mutations affecting the gene represented in this entry. Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: In FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems. {ECO:0000269|PubMed:11445641}. Note=The disease is caused by mutations affecting the gene represented in this entry. Premature ovarian failure 1 (POF1) [MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:9719368}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P10909; IntAct: EBI-1104674,EBI-366305; Score: 0.37
DE  Interaction: P63165; IntAct: EBI-80140,EBI-366305; Score: 0.37
DE  Interaction: Self; IntAct: EBI-366305,EBI-366305; Score: 0.69
DE  Interaction: P63073; IntAct: EBI-2000006,EBI-366305; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-366305; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-353366,EBI-366305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-351007,EBI-366305; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-715747,EBI-366305; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-2862306,EBI-366305; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-358419,EBI-366305; Score: 0.35
DE  Interaction: O75925; IntAct: EBI-629434,EBI-366305; Score: 0.37
DE  Interaction: Q92538; IntAct: EBI-359050,EBI-366305; Score: 0.37
DE  Interaction: P52179; IntAct: EBI-5353249,EBI-366305; Score: 0.37
DE  Interaction: P12814; IntAct: EBI-351710,EBI-366305; Score: 0.37
DE  Interaction: O15379; IntAct: EBI-607682,EBI-366305; Score: 0.37
DE  Interaction: O14617; IntAct: EBI-1051639,EBI-366305; Score: 0.37
DE  Interaction: O75928; IntAct: EBI-348555,EBI-366305; Score: 0.37
DE  Interaction: O60229; IntAct: EBI-949233,EBI-366305; Score: 0.37
DE  Interaction: Q8WV44; IntAct: EBI-725997,EBI-366305; Score: 0.37
DE  Interaction: P54296; IntAct: EBI-5357134,EBI-366305; Score: 0.37
DE  Interaction: Q9NYA4; IntAct: EBI-1052346,EBI-366305; Score: 0.37
DE  Interaction: Q13023; IntAct: EBI-1056102,EBI-366305; Score: 0.37
DE  Interaction: Q9NRD5; IntAct: EBI-79165,EBI-366305; Score: 0.37
DE  Interaction: Q9UII2; IntAct: EBI-718459,EBI-366305; Score: 0.37
DE  Interaction: O15066; IntAct: EBI-3931791,EBI-366305; Score: 0.37
DE  Interaction: O75376; IntAct: EBI-347233,EBI-366305; Score: 0.37
DE  Interaction: Q9Y4A8; IntAct: EBI-10890629,EBI-366305; Score: 0.37
DE  Interaction: Q5JY77; IntAct: EBI-2514717,EBI-366305; Score: 0.37
DE  Interaction: P50749; IntAct: EBI-960081,EBI-366305; Score: 0.37
DE  Interaction: P43243; IntAct: EBI-352602,EBI-366305; Score: 0.37
DE  Interaction: Q9UKI8; IntAct: EBI-740492,EBI-366305; Score: 0.37
DE  Interaction: Q16181; IntAct: EBI-2009373,EBI-366305; Score: 0.37
DE  Interaction: O43295; IntAct: EBI-368166,EBI-366305; Score: 0.37
DE  Interaction: Q8N5U6; IntAct: EBI-714023,EBI-366305; Score: 0.37
DE  Interaction: Q96IV0; IntAct: EBI-6165879,EBI-366305; Score: 0.37
DE  Interaction: P10644; IntAct: EBI-476431,EBI-366305; Score: 0.37
DE  Interaction: P05771; IntAct: EBI-706216,EBI-366305; Score: 0.37
DE  Interaction: Q9Y5G2; IntAct: EBI-21384271,EBI-366305; Score: 0.37
DE  Interaction: Q9UHQ4; IntAct: EBI-2548400,EBI-366305; Score: 0.37
DE  Interaction: Q8NFW8; IntAct: EBI-2816175,EBI-366305; Score: 0.37
DE  Interaction: Q9NQZ6; IntAct: EBI-747993,EBI-366305; Score: 0.37
DE  Interaction: Q5T6F2; IntAct: EBI-2514383,EBI-366305; Score: 0.37
DE  Interaction: Q2TAA8; IntAct: EBI-6872498,EBI-366305; Score: 0.37
DE  Interaction: P17980; IntAct: EBI-359720,EBI-366305; Score: 0.37
DE  Interaction: Q9NR46; IntAct: EBI-749607,EBI-366305; Score: 0.37
DE  Interaction: Q9NRA8; IntAct: EBI-301024,EBI-366305; Score: 0.37
DE  Interaction: Q6PEZ3; IntAct: EBI-21384744,EBI-366305; Score: 0.37
DE  Interaction: O00231; IntAct: EBI-357816,EBI-366305; Score: 0.37
DE  Interaction: Q8N2N9; IntAct: EBI-2876112,EBI-366305; Score: 0.37
DE  Interaction: Q9P246; IntAct: EBI-448891,EBI-366305; Score: 0.37
DE  Interaction: Q9Y2V7; IntAct: EBI-3866319,EBI-366305; Score: 0.37
DE  Interaction: Q9NS37; IntAct: EBI-632965,EBI-366305; Score: 0.37
DE  Interaction: P15622; IntAct: EBI-739678,EBI-366305; Score: 0.37
DE  Interaction: Q9UNH7; IntAct: EBI-949294,EBI-366305; Score: 0.37
DE  Interaction: Q53G59; IntAct: EBI-740929,EBI-366305; Score: 0.37
DE  Interaction: Q15424; IntAct: EBI-348298,EBI-366305; Score: 0.37
DE  Interaction: P62979; IntAct: EBI-357375,EBI-366305; Score: 0.37
DE  Interaction: P62750; IntAct: EBI-353254,EBI-366305; Score: 0.37
DE  Interaction: P35268; IntAct: EBI-354533,EBI-366305; Score: 0.37
DE  Interaction: Q9C0C9; IntAct: EBI-2339946,EBI-366305; Score: 0.37
DE  Interaction: Q9H2G4; IntAct: EBI-947459,EBI-366305; Score: 0.37
DE  Interaction: P23246; IntAct: EBI-355453,EBI-366305; Score: 0.37
DE  Interaction: Q96BJ3; IntAct: EBI-4401674,EBI-366305; Score: 0.37
DE  Interaction: Q2KHR2; IntAct: EBI-1222187,EBI-366305; Score: 0.37
DE  Interaction: Q86XZ4; IntAct: EBI-6164306,EBI-366305; Score: 0.37
DE  Interaction: P28370; IntAct: EBI-2822460,EBI-366305; Score: 0.37
DE  Interaction: P51532; IntAct: EBI-302489,EBI-366305; Score: 0.37
DE  Interaction: Q14527; IntAct: EBI-1045161,EBI-366305; Score: 0.37
DE  Interaction: P18583; IntAct: EBI-1053513,EBI-366305; Score: 0.37
DE  Interaction: Q13813; IntAct: EBI-351450,EBI-366305; Score: 0.37
DE  Interaction: P21579; IntAct: EBI-524909,EBI-366305; Score: 0.37
DE  Interaction: P21675; IntAct: EBI-491289,EBI-366305; Score: 0.37
DE  Interaction: Q14241; IntAct: EBI-742350,EBI-366305; Score: 0.37
DE  Interaction: Q15906; IntAct: EBI-399189,EBI-366305; Score: 0.37
DE  Interaction: P10600; IntAct: EBI-1033020,EBI-366305; Score: 0.37
DE  Interaction: P10828; IntAct: EBI-78558,EBI-366305; Score: 0.37
DE  Interaction: P05452; IntAct: EBI-1047626,EBI-366305; Score: 0.37
DE  Interaction: P09936; IntAct: EBI-714860,EBI-366305; Score: 0.37
DE  Interaction: P63279; IntAct: EBI-80168,EBI-366305; Score: 0.37
DE  Interaction: Q15361; IntAct: EBI-7239664,EBI-366305; Score: 0.37
DE  Interaction: O96028; IntAct: EBI-2693298,EBI-366305; Score: 0.37
DE  Interaction: P52746; IntAct: EBI-3444189,EBI-366305; Score: 0.37
DE  Interaction: Q99676; IntAct: EBI-3907489,EBI-366305; Score: 0.37
DE  Interaction: P21506; IntAct: EBI-1105324,EBI-366305; Score: 0.37
DE  Interaction: Q06732; IntAct: EBI-474142,EBI-366305; Score: 0.37
DE  Interaction: Q06730; IntAct: EBI-3951772,EBI-366305; Score: 0.37
DE  Interaction: Q13029; IntAct: EBI-2686075,EBI-366305; Score: 0.37
DE  Interaction: Q86XK2; IntAct: EBI-1047804,EBI-366305; Score: 0.37
DE  Interaction: Q6ZS17; IntAct: EBI-2806927,EBI-366305; Score: 0.37
DE  Interaction: A6NKB5; IntAct: EBI-21311109,EBI-366305; Score: 0.37
DE  Interaction: P51114; IntAct: EBI-713291,EBI-366305; Score: 0.37
DE  Interaction: P45974; IntAct: EBI-741277,EBI-366305; Score: 0.37
DE  Interaction: Q8IZ26; IntAct: EBI-10264496,EBI-366305; Score: 0.37
DE  Interaction: Q9UQM7; IntAct: EBI-1383687,EBI-366305; Score: 0.37
DE  Interaction: Q6PIJ6; IntAct: EBI-2513135,EBI-366305; Score: 0.37
DE  Interaction: Q9H7E2; IntAct: EBI-3938232,EBI-366305; Score: 0.37
DE  Interaction: Q9BZR9; IntAct: EBI-2340370,EBI-366305; Score: 0.37
DE  Interaction: P51784; IntAct: EBI-306876,EBI-366305; Score: 0.37
DE  Interaction: P04632; IntAct: EBI-711828,EBI-366305; Score: 0.37
DE  Interaction: Q2LD37; IntAct: EBI-2683809,EBI-366305; Score: 0.37
DE  Interaction: Q9BSF8; IntAct: EBI-720180,EBI-366305; Score: 0.37
DE  Interaction: Q86W92; IntAct: EBI-1045582,EBI-366305; Score: 0.37
DE  Interaction: Q5VT25; IntAct: EBI-689171,EBI-366305; Score: 0.37
DE  Interaction: Q96JF6; IntAct: EBI-723614,EBI-366305; Score: 0.37
DE  Interaction: Q5H9K5; IntAct: EBI-2818620,EBI-366305; Score: 0.37
DE  Interaction: Q9BR77; IntAct: EBI-7851256,EBI-366305; Score: 0.37
DE  Interaction: O95267; IntAct: EBI-1054956,EBI-366305; Score: 0.37
DE  Interaction: Q9NP66; IntAct: EBI-740641,EBI-366305; Score: 0.37
DE  Interaction: Q7L5Y9; IntAct: EBI-10984762,EBI-366305; Score: 0.37
DE  Interaction: O60884; IntAct: EBI-352957,EBI-366305; Score: 0.37
DE  Interaction: Q9Y6X2; IntAct: EBI-2803703,EBI-366305; Score: 0.37
DE  Interaction: Q9BSL1; IntAct: EBI-749370,EBI-366305; Score: 0.37
DE  Interaction: P40123; IntAct: EBI-1051165,EBI-366305; Score: 0.37
DE  Interaction: Q99784; IntAct: EBI-1105073,EBI-366305; Score: 0.37
DE  Interaction: Q9UQB8; IntAct: EBI-525456,EBI-366305; Score: 0.37
DE  Interaction: Q14919; IntAct: EBI-712941,EBI-366305; Score: 0.37
DE  Interaction: O00471; IntAct: EBI-949824,EBI-366305; Score: 0.37
DE  Interaction: Q14314; IntAct: EBI-21370828,EBI-366305; Score: 0.37
DE  Interaction: Q9UBU8; IntAct: EBI-399246,EBI-366305; Score: 0.37
DE  Interaction: Q8N5Y2; IntAct: EBI-2560796,EBI-366305; Score: 0.37
DE  Interaction: Q13438; IntAct: EBI-725454,EBI-366305; Score: 0.37
DE  Interaction: O14647; IntAct: EBI-1210503,EBI-366305; Score: 0.37
DE  Interaction: P61964; IntAct: EBI-540834,EBI-366305; Score: 0.37
DE  Interaction: Q9UKN5; IntAct: EBI-2803427,EBI-366305; Score: 0.37
DE  Interaction: Q9UNN5; IntAct: EBI-718246,EBI-366305; Score: 0.37
DE  Interaction: Q9Y496; IntAct: EBI-1104844,EBI-366305; Score: 0.37
DE  Interaction: Q96RF0; IntAct: EBI-298169,EBI-366305; Score: 0.37
DE  Interaction: Q9C026; IntAct: EBI-720828,EBI-366305; Score: 0.37
DE  Interaction: Q96CW1; IntAct: EBI-297683,EBI-366305; Score: 0.37
DE  Interaction: Q96N64; IntAct: EBI-6597774,EBI-366305; Score: 0.37
DE  Interaction: Q96PV6; IntAct: EBI-739546,EBI-366305; Score: 0.37
DE  Interaction: Q96PY5; IntAct: EBI-3438448,EBI-366305; Score: 0.37
DE  Interaction: Q00610; IntAct: EBI-354967,EBI-366305; Score: 0.37
DE  Interaction: Q8N1A0; IntAct: EBI-8473062,EBI-366305; Score: 0.37
DE  Interaction: Q12860; IntAct: EBI-5564336,EBI-366305; Score: 0.37
DE  Interaction: Q14194; IntAct: EBI-473101,EBI-366305; Score: 0.37
DE  Interaction: Q96L42; IntAct: EBI-21372247,EBI-366305; Score: 0.37
DE  Interaction: Q8N3I7; IntAct: EBI-2892592,EBI-366305; Score: 0.37
DE  Interaction: P29400; IntAct: EBI-726908,EBI-366305; Score: 0.37
DE  Interaction: Q8WXF8; IntAct: EBI-5278558,EBI-366305; Score: 0.37
DE  Interaction: Q8TF20; IntAct: EBI-20859557,EBI-366305; Score: 0.37
DE  Interaction: Q6PEW1; IntAct: EBI-748373,EBI-366305; Score: 0.37
DE  Interaction: Q1L5Z9; IntAct: EBI-2510853,EBI-366305; Score: 0.37
DE  Interaction: Q12882; IntAct: EBI-2839838,EBI-366305; Score: 0.37
DE  Interaction: Q14204; IntAct: EBI-356015,EBI-366305; Score: 0.37
DE  Interaction: P29692; IntAct: EBI-358607,EBI-366305; Score: 0.37
DE  Interaction: O43491; IntAct: EBI-366305,EBI-1052044; Score: 0.37
DE  Interaction: Q9H4G0; IntAct: EBI-465536,EBI-366305; Score: 0.37
DE  Interaction: O60293; IntAct: EBI-746701,EBI-366305; Score: 0.37
DE  Interaction: P33121; IntAct: EBI-2838799,EBI-366305; Score: 0.37
DE  Interaction: P42566; IntAct: EBI-396684,EBI-366305; Score: 0.37
DE  Interaction: Q9Y483; IntAct: EBI-725816,EBI-366305; Score: 0.37
DE  Interaction: Q70YC4; IntAct: EBI-21374257,EBI-366305; Score: 0.37
DE  Interaction: Q9UPW8; IntAct: EBI-311017,EBI-366305; Score: 0.37
DE  Interaction: Q9UPY8; IntAct: EBI-726739,EBI-366305; Score: 0.37
DE  Interaction: Q96RU3; IntAct: EBI-1111248,EBI-366305; Score: 0.37
DE  Interaction: Q9UBB6; IntAct: EBI-1053490,EBI-366305; Score: 0.37
DE  Interaction: P21333; IntAct: EBI-350432,EBI-366305; Score: 0.37
DE  Interaction: Q9Y2J2; IntAct: EBI-310986,EBI-366305; Score: 0.37
DE  Interaction: O60333; IntAct: EBI-465633,EBI-366305; Score: 0.37
DE  Interaction: Q9BT88; IntAct: EBI-751770,EBI-366305; Score: 0.37
DE  Interaction: Q9Y5W8; IntAct: EBI-3917449,EBI-366305; Score: 0.37
DE  Interaction: O95490; IntAct: EBI-2865302,EBI-366305; Score: 0.37
DE  Interaction: Q9UJ04; IntAct: EBI-308511,EBI-366305; Score: 0.37
DE  Interaction: Q9C040; IntAct: EBI-749840,EBI-366305; Score: 0.37
DE  Interaction: O94874; IntAct: EBI-1048088,EBI-366305; Score: 0.37
DE  Interaction: Q7Z460; IntAct: EBI-913476,EBI-366305; Score: 0.37
DE  Interaction: Q96JC1; IntAct: EBI-1050197,EBI-366305; Score: 0.37
DE  Interaction: O75044; IntAct: EBI-1051034,EBI-366305; Score: 0.37
DE  Interaction: Q8N488; IntAct: EBI-752324,EBI-366305; Score: 0.37
DE  Interaction: O75533; IntAct: EBI-876542,EBI-366305; Score: 0.37
DE  Interaction: Q9UPN3; IntAct: EBI-366305,EBI-522925; Score: 0.37
DE  Interaction: Q9ULA0; IntAct: EBI-748356,EBI-366305; Score: 0.37
DE  Interaction: Q6PID6; IntAct: EBI-2555404,EBI-366305; Score: 0.37
DE  Interaction: Q8NAP3; IntAct: EBI-5235984,EBI-366305; Score: 0.37
DE  Interaction: Q8TF01; IntAct: EBI-3437793,EBI-366305; Score: 0.37
DE  Interaction: Q96DZ5; IntAct: EBI-12823145,EBI-366305; Score: 0.37
DE  Interaction: O43166; IntAct: EBI-310678,EBI-366305; Score: 0.37
DE  Interaction: Q9Y4E5; IntAct: EBI-747230,EBI-366305; Score: 0.37
DE  Interaction: Q9NUQ6; IntAct: EBI-5280638,EBI-366305; Score: 0.37
DE  Interaction: Q9ULX6; IntAct: EBI-357530,EBI-366305; Score: 0.37
DE  Interaction: Q96NJ3; IntAct: EBI-18064466,EBI-366305; Score: 0.37
DE  Interaction: Q06210; IntAct: EBI-1055540,EBI-366305; Score: 0.37
DE  Interaction: Q9UHB7; IntAct: EBI-395282,EBI-366305; Score: 0.37
DE  Interaction: Q9ULD5; IntAct: EBI-11975599,EBI-366305; Score: 0.37
DE  Interaction: Q9UMS4; IntAct: EBI-395746,EBI-366305; Score: 0.37
DE  Interaction: P38159; IntAct: EBI-743526,EBI-366305; Score: 0.37
DE  Interaction: Q86WH2; IntAct: EBI-2845202,EBI-366305; Score: 0.37
DE  Interaction: Q9HBT6; IntAct: EBI-21378130,EBI-366305; Score: 0.37
DE  Interaction: Q5JPE7; IntAct: EBI-2680477,EBI-366305; Score: 0.37
DE  Interaction: Q8N660; IntAct: EBI-2863570,EBI-366305; Score: 0.37
DE  Interaction: Q6NZI2; IntAct: EBI-2559016,EBI-366305; Score: 0.37
DE  Interaction: P07305; IntAct: EBI-725224,EBI-366305; Score: 0.37
DE  Interaction: Q9BWC9; IntAct: EBI-711501,EBI-366305; Score: 0.37
DE  Interaction: Q00341; IntAct: EBI-1049478,EBI-366305; Score: 0.37
DE  Interaction: P61978; IntAct: EBI-304185,EBI-366305; Score: 0.37
DE  Interaction: P11021; IntAct: EBI-354921,EBI-366305; Score: 0.37
DE  Interaction: Q5HYM0; IntAct: EBI-21379449,EBI-366305; Score: 0.37
DE  Interaction: P78318; IntAct: EBI-1055954,EBI-366305; Score: 0.37
DE  Interaction: Q13123; IntAct: EBI-713456,EBI-366305; Score: 0.37
DE  Interaction: O14782; IntAct: EBI-1104854,EBI-366305; Score: 0.37
DE  Interaction: A6QL64; IntAct: EBI-21379797,EBI-366305; Score: 0.37
DE  Interaction: O60282; IntAct: EBI-717170,EBI-366305; Score: 0.37
DE  Interaction: P33176; IntAct: EBI-355878,EBI-366305; Score: 0.37
DE  Interaction: Q12840; IntAct: EBI-713468,EBI-366305; Score: 0.37
DE  Interaction: A8MQT2; IntAct: EBI-21380453,EBI-366305; Score: 0.37
DE  Interaction: Q15784; IntAct: EBI-7399633,EBI-366305; Score: 0.37
DE  Interaction: Q14494; IntAct: EBI-2804436,EBI-366305; Score: 0.37
DE  Interaction: Q9UQ80; IntAct: EBI-924893,EBI-366305; Score: 0.37
DE  Interaction: P67809; IntAct: EBI-354065,EBI-366305; Score: 0.37
DE  Interaction: Q16656; IntAct: EBI-2547810,EBI-366305; Score: 0.37
DE  Interaction: Q6P4R8; IntAct: EBI-2511210,EBI-366305; Score: 0.37
DE  Interaction: P05165; IntAct: EBI-2211679,EBI-366305; Score: 0.37
DE  Interaction: Q15154; IntAct: EBI-741421,EBI-366305; Score: 0.37
DE  Interaction: Q9UJX3; IntAct: EBI-1384164,EBI-366305; Score: 0.37
DE  Interaction: O95071; IntAct: EBI-358329,EBI-366305; Score: 0.37
DE  Interaction: Q9UBS4; IntAct: EBI-713113,EBI-366305; Score: 0.37
DE  Interaction: Q7LFL8; IntAct: EBI-3940093,EBI-366305; Score: 0.37
DE  Interaction: Q99719; IntAct: EBI-373345,EBI-366305; Score: 0.37
DE  Interaction: Q9NZR2; IntAct: EBI-1642131,EBI-366305; Score: 0.37
DE  Interaction: Q9H0C5; IntAct: EBI-935503,EBI-366305; Score: 0.37
DE  Interaction: Q00169; IntAct: EBI-1042490,EBI-366305; Score: 0.37
DE  Interaction: O43236; IntAct: EBI-1047513,EBI-366305; Score: 0.37
DE  Interaction: P46100; IntAct: EBI-396461,EBI-366305; Score: 0.37
DE  Interaction: Q5T0N5; IntAct: EBI-714058,EBI-366305; Score: 0.37
DE  Interaction: Q6ZN54; IntAct: EBI-2857145,EBI-366305; Score: 0.37
DE  Interaction: Q8WUP2; IntAct: EBI-3864120,EBI-366305; Score: 0.37
DE  Interaction: Q8NDB2; IntAct: EBI-2837677,EBI-366305; Score: 0.37
DE  Interaction: Q8TEP8; IntAct: EBI-2339778,EBI-366305; Score: 0.37
DE  Interaction: Q8TC92; IntAct: EBI-713221,EBI-366305; Score: 0.37
DE  Interaction: Q8NEU8; IntAct: EBI-741261,EBI-366305; Score: 0.37
DE  Interaction: Q15172; IntAct: EBI-641666,EBI-366305; Score: 0.37
DE  Interaction: Q9P0M6; IntAct: EBI-3922608,EBI-366305; Score: 0.37
DE  Interaction: Q6VMQ6; IntAct: EBI-928732,EBI-366305; Score: 0.37
DE  Interaction: Q3V6T2; IntAct: EBI-2266839,EBI-366305; Score: 0.37
DE  Interaction: Q96S59; IntAct: EBI-636085,EBI-366305; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-395506,EBI-366305; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-745632,EBI-366305; Score: 0.35
DE  Interaction: P38919; IntAct: EBI-299104,EBI-366305; Score: 0.35
DE  Interaction: Q13131; IntAct: EBI-1181405,EBI-366305; Score: 0.40
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-366305; Score: 0.46
DE  Interaction: P03372; IntAct: EBI-78473,EBI-366305; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-2212028,EBI-366305; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-876367,EBI-366305; Score: 0.35
DE  Interaction: Q13137; IntAct: EBI-739580,EBI-366305; Score: 0.35
DE  Interaction: A7MCY6; IntAct: EBI-359969,EBI-366305; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-356402,EBI-366305; Score: 0.35
DE  Interaction: P48059; IntAct: EBI-306928,EBI-366305; Score: 0.37
DE  Interaction: Q6QDQ4; IntAct: EBI-5276623,EBI-366305; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-366305; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-366305; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-456129,EBI-366305; Score: 0.35
DE  Interaction: A0A384KBR0; IntAct: EBI-366305,EBI-2851265; Score: 0.37
DE  Interaction: Q13428; IntAct: EBI-396105,EBI-366305; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25492388,EBI-366305; Score: 0.35
DE  Interaction: P61326; IntAct: EBI-299134,EBI-366305; Score: 0.35
DE  Interaction: Q9UJV9; IntAct: EBI-1046350,EBI-366305; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-358174,EBI-366305; Score: 0.43
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0015030;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0044326;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0016020;
GO  GO:1990124;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0035770;
GO  GO:0045202;
GO  GO:0019034;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0044325;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0031369;
GO  GO:0045182;
GO  GO:0030371;
GO  GO:0006974;
GO  GO:0072711;
GO  GO:0034644;
GO  GO:0098586;
GO  GO:0031047;
GO  GO:0007215;
GO  GO:0044830;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:1900453;
GO  GO:1902373;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:2000637;
GO  GO:0033129;
GO  GO:1901254;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0001934;
GO  GO:0002092;
GO  GO:2001022;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVT
SQ  YDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVP
SQ  FVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRG
SQ  HGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTD
SQ  NRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
//
ID  O35346;
PN  Focal adhesion kinase 1;
GN  Ptk2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=Constituent of focal adhesions. Detected at microtubules (By similarity). {ECO:0000250}.
DR  UNIPROT: O35346;
DR  UNIPROT: Q62900;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:15494733}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XI86; IntAct: EBI-6252926,EBI-6252940; Score: 0.46
GO  GO:0005912;
GO  GO:0016324;
GO  GO:0016323;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0014704;
GO  GO:0030027;
GO  GO:0005815;
GO  GO:0016604;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042383;
GO  GO:0001725;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0008432;
GO  GO:0004715;
GO  GO:0019902;
GO  GO:0043548;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0042169;
GO  GO:0031625;
GO  GO:0001525;
GO  GO:0001568;
GO  GO:0030644;
GO  GO:0071560;
GO  GO:0021955;
GO  GO:0043542;
GO  GO:0048013;
GO  GO:0007173;
GO  GO:0030198;
GO  GO:0045444;
GO  GO:0060396;
GO  GO:0007229;
GO  GO:0007254;
GO  GO:0000165;
GO  GO:0000226;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0050771;
GO  GO:0030336;
GO  GO:0022408;
GO  GO:0046621;
GO  GO:0051964;
GO  GO:0001764;
GO  GO:0007097;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0097755;
GO  GO:0010613;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0060252;
GO  GO:0050766;
GO  GO:0014068;
GO  GO:0045860;
GO  GO:0051897;
GO  GO:0001934;
GO  GO:0014911;
GO  GO:0048661;
GO  GO:0050806;
GO  GO:2000060;
GO  GO:0046777;
GO  GO:0030155;
GO  GO:0033628;
GO  GO:0042127;
GO  GO:0008360;
GO  GO:0010632;
GO  GO:0051893;
GO  GO:0045667;
GO  GO:0001932;
GO  GO:1900024;
GO  GO:0046685;
GO  GO:0042493;
GO  GO:0032355;
GO  GO:0009749;
GO  GO:0009612;
GO  GO:0014070;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0007172;
GO  GO:0007179;
GO  GO:0001570;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHV
SQ  ACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIA
SQ  DQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
SQ  LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKI
SQ  AGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEI
SQ  IDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
SQ  PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV
SQ  KLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER
SQ  LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY
SQ  PSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMG
SQ  QVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPG
SQ  APGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEV
SQ  GLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDV
SQ  IDQARLKMLGQTRPH
//
ID  Q9C5X4;
PN  Histone H3-lysine(4) N-trimethyltransferase ATX1;
GN  ATX1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Nucleus {ECO:0000269|PubMed:16585509, ECO:0000269|PubMed:17881378}. Cytoplasm {ECO:0000269|PubMed:16585509}. Note=Shifts from nucleus to cytoplasm as PIP5 levels increase. When in the nucleus, associated with chromatin. When cytoplasmic, mostly localized along the plasma membrane, associated with PIP5. {ECO:0000269|PubMed:16585509}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}.
DR  UNIPROT: Q9C5X4;
DR  UNIPROT: Q84WP4;
DR  UNIPROT: Q9SIP3;
DR  Pfam: PF05965;
DR  Pfam: PF05964;
DR  Pfam: PF09465;
DR  Pfam: PF00855;
DR  Pfam: PF00856;
DR  PROSITE: PS51805;
DR  PROSITE: PS51543;
DR  PROSITE: PS51542;
DR  PROSITE: PS50868;
DR  PROSITE: PS50812;
DR  PROSITE: PS50280;
DR  PROSITE: PS50081;
DR  PROSITE: PS01359;
DR  PROSITE: PS50016;
DE  Function: [Isoform 1]: Binds to the promoter and regulates the transcription of target genes, maintaining them in an active state; at promoters, required for TATA binding proteins (TBPs, e.g. TBP1 and TBP2) and RNA polymerase II (Pol II) recruitment, and, in a subsequent event, is recruited by a phosphorylated form of Pol II to the +300-bp region of transcribed sequences to trimethylates nucleosomes (PubMed:21266657, PubMed:23284292). Histone trimethyltransferase that trimethylates 'Lys-4' of histone H3 (H3K4me3); H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation and is required for efficient elongation of transcription but not for transcription initiation (PubMed:17965588, PubMed:17881378, PubMed:18375658, PubMed:23284292). Methylates only a limited fraction of nucleosomes of target genes (e.g. FLC, NAP, XTH33 and WRKY70) (PubMed:18375658). Necessary for WDR5A occupancy at WRKY70 and LTP7 genes (PubMed:23284292). Required to maintain the active state of class A (AP1 and AP2), class B (PI and AP3) and class C (AG, AGAMOUS) floral homeotic genes at early stages of flower development (PubMed:17881378). Together with CLF, modulates AG nucleosome methylation statement (PubMed:17881378). Involved in epigenetic regulation (e.g. H3K4me3) of the floral repressors FLC, FT and SOC1 to prevent the transition from vegetative to reproductive development, independently of the photoperiod; binds the active FLC locus before flowering, but this interaction is released upon the transition to flowering (PubMed:18375656, PubMed:24102415, PubMed:30150325). Regulates floral organ identity and flowering transition. Functions as a receptor for the lipid messenger phosphatidylinositol 5-phosphate (PI5P), which regulates negatively its transcriptional activation activity. Exhibits histone methylase activity and subsequent transcriptional regulation on WRKY70 gene, and, to a lower extent on secondary defense-response targets salicylic acid (SA)-responsive gene PR1 and jasmonic acid (JA)- responsive gene THI2.1 (PubMed:17965588). Involved in response to dehydration stress-response in both abscisic acid (ABA)-dependent and ABA-independent pathways; this includes specific genes (e.g. COR15A, ADH1, CBF4, RD29A, RD29B, RD26, ABF3, NCED3 and ABA3) epigenetic regulation (e.g. H3K4me3 and Pol II recruitment) to promotes their transcription and influence ABA production (PubMed:19901554, PubMed:21309869). Implicated in stomatal closure regulation (PubMed:21309869). Indirect repressor of XTH genes (XTH33) (PubMed:19154201). Necessary for the phosphorylation of Pol II NRPB1 (e.g. Ser5P and Ser2P) at the promoters of target genes, thus regulating both early and late stages of transcription (PubMed:21266657). Controls root growth and architecture by regulating the timing of root development, stem cell niche maintenance (e.g. quiescent center (QC)), and cell patterning during primary and lateral root development (PubMed:25205583). Modulates cell cycle duration, cell production, and the transition from cell proliferation in the root apical meristem (RAM) to cell elongation (PubMed:25205583). {ECO:0000269|PubMed:12699618, ECO:0000269|PubMed:16585509, ECO:0000269|PubMed:17881378, ECO:0000269|PubMed:17965588, ECO:0000269|PubMed:18375656, ECO:0000269|PubMed:18375658, ECO:0000269|PubMed:19154201, ECO:0000269|PubMed:19901554, ECO:0000269|PubMed:21266657, ECO:0000269|PubMed:21309869, ECO:0000269|PubMed:23284292, ECO:0000269|PubMed:24102415, ECO:0000269|PubMed:25205583, ECO:0000269|PubMed:30150325}. [Isoform 3]: Trimethylates A4/EF1A post-translationally at Lys-396 (PubMed:21245040). Required for actin cytoskeleton organization (PubMed:21245040). {ECO:0000269|PubMed:21245040}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003682;
GO  GO:0018024;
GO  GO:0046872;
GO  GO:0010314;
GO  GO:0008276;
GO  GO:0044212;
GO  GO:0009738;
GO  GO:0030036;
GO  GO:0051568;
GO  GO:0080182;
GO  GO:0035556;
GO  GO:0009910;
GO  GO:0018022;
GO  GO:1904961;
GO  GO:0009909;
GO  GO:0040029;
GO  GO:2000023;
GO  GO:2000280;
GO  GO:2000067;
GO  GO:0090333;
GO  GO:0006357;
GO  GO:0006355;
GO  GO:0009414;
GO  GO:0010093;
GO  GO:0010228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACFSNETQIEIDVHDLVEAPIRYDSIESIYSIPSSALCCVNAVGSHSLMSKKVKAQKLPMIEQFEIEGSGVSASDDCCR
SQ  SDDYKLRIQRPEIVRVYYRRRKRPLRECLLDQAVAVKTESVELDEIDCFEEKKRRKIGNCELVKSGMESIGLRRCKENNA
SQ  FSGNKQNGSSRRKGSSSKNQDKATLASRSAKKWVRLSYDGVDPTSFIGLQCKVFWPLDALWYEGSIVGYSAERKRYTVKY
SQ  RDGCDEDIVFDREMIKFLVSREEMELLHLKFCTSNVTVDGRDYDEMVVLAATLDECQDFEPGDIVWAKLAGHAMWPAVIV
SQ  DESIIGERKGLNNKVSGGGSLLVQFFGTHDFARIKVKQAISFIKGLLSPSHLKCKQPRFEEGMQEAKMYLKAHRLPERMS
SQ  QLQKGADSVDSDMANSTEEGNSGGDLLNDGEVWLRPTEHVDFRHIIGDLLIINLGKVVTDSQFFKDENHIWPEGYTAMRK
SQ  FTSLTDHSASALYKMEVLRDAETKTHPLFIVTADSGEQFKGPTPSACWNKIYNRIKKVQNSDSPNILGEELNGSGTDMFG
SQ  LSNPEVIKLVQDLSKSRPSSHVSMCKNSLGRHQNQPTGYRPVRVDWKDLDKCNVCHMDEEYENNLFLQCDKCRMMVHAKC
SQ  YGELEPCDGALWLCNLCRPGAPDMPPRCCLCPVVGGAMKPTTDGRWAHLACAIWIPETCLSDVKKMEPIDGVNKVSKDRW
SQ  KLMCTICGVSYGACIQCSNNSCRVAYHPLCARAAGLCVELENDMSVEGEEADQCIRMLSFCKRHRQTSTACLGSEDRIKS
SQ  ATHKTSEYLPPPNPSGCARTEPYNCFGRRGRKEPEALAAASSKRLFVENQPYVIGGYSRLEFSTYKSIHGSKVSQMNTPS
SQ  NILSMAEKYRYMRETYRKRLAFGKSGIHGFGIFAKLPHRAGDMMIEYTGELVRPSIADKREQLIYNSMVGAGTYMFRIDD
SQ  ERVIDATRTGSIAHLINHSCVPNCYSRVITVNGDEHIIIFAKRHIPKWEELTYDYRFFSIGERLSCSCGFPGCRGVVNDT
SQ  EAEEQHAKICVPRCDLIDWTAE
//
ID  O18735;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  ERBB2;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. {ECO:0000250|UniProtKB:P04626}.
DR  UNIPROT: O18735;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0009925;
GO  GO:0005769;
GO  GO:0005887;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043235;
GO  GO:0005524;
GO  GO:0001042;
GO  GO:0004714;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0035556;
GO  GO:0007275;
GO  GO:0030182;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0090314;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEV
SQ  QGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQ
SQ  LCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQC
SQ  AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQ
SQ  EVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVF
SQ  EALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTV
SQ  PWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCL
SQ  PCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKG
SQ  CPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELR
SQ  KVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLM
SQ  PYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADG
SQ  GKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMI
SQ  DSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGG
SQ  TAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLP
SQ  PETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEY
SQ  LAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV
//
ID  Q9NV70;
PN  Exocyst complex component 1;
GN  EXOC1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Cytoplasm {ECO:0000269|PubMed:19889084}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19889084}. Note=Colocalizes with CNTRL/centriolin at the midbody ring. {ECO:0000269|PubMed:16213214}.
DR  UNIPROT: Q9NV70;
DR  UNIPROT: Q504V4;
DR  UNIPROT: Q8WUE7;
DR  UNIPROT: Q96T15;
DR  UNIPROT: Q9NZE4;
DR  Pfam: PF15277;
DR  Pfam: PF09763;
DR  OMIM: 607879;
DR  DisGeNET: 55763;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269|PubMed:19889084}.
DE  Reference Proteome: Yes;
DE  Interaction: O60645; IntAct: EBI-1045313,EBI-1052278; Score: 0.51
DE  Interaction: O95295; IntAct: EBI-296723,EBI-1045313; Score: 0.55
DE  Interaction: Q03001; IntAct: EBI-310758,EBI-1045313; Score: 0.55
DE  Interaction: Q12840; IntAct: EBI-713468,EBI-1045313; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-741048,EBI-1045313; Score: 0.67
DE  Interaction: Q8IYI6; IntAct: EBI-742102,EBI-1045313; Score: 0.51
DE  Interaction: Q8NF91; IntAct: EBI-928867,EBI-1045313; Score: 0.37
DE  Interaction: Q8TAG9; IntAct: EBI-1045313,EBI-1223394; Score: 0.51
DE  Interaction: Q8WXH0; IntAct: EBI-2372294,EBI-1045313; Score: 0.37
DE  Interaction: Q9ULU8; IntAct: EBI-724083,EBI-1045313; Score: 0.37
DE  Interaction: O43490; IntAct: EBI-3447549,EBI-1045313; Score: 0.37
DE  Interaction: P35609; IntAct: EBI-77797,EBI-1045313; Score: 0.37
DE  Interaction: Q8NEY1; IntAct: EBI-308358,EBI-1045313; Score: 0.37
DE  Interaction: O60239; IntAct: EBI-624860,EBI-1045313; Score: 0.55
DE  Interaction: O15066; IntAct: EBI-3931791,EBI-1045313; Score: 0.37
DE  Interaction: Q8WXA3; IntAct: EBI-2823360,EBI-1045313; Score: 0.37
DE  Interaction: Q99459; IntAct: EBI-1045313,EBI-374880; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-1045313,EBI-529989; Score: 0.55
DE  Interaction: Q8TDR0-2; IntAct: EBI-1045313,EBI-11946508; Score: 0.37
DE  Interaction: Q96SN8; IntAct: EBI-308374,EBI-1045313; Score: 0.37
DE  Interaction: Q4V328; IntAct: EBI-717919,EBI-1045313; Score: 0.37
DE  Interaction: Q8N2N9; IntAct: EBI-2876112,EBI-1045313; Score: 0.37
DE  Interaction: Q8IYE0; IntAct: EBI-10749669,EBI-1045313; Score: 0.37
DE  Interaction: Q7Z6B7; IntAct: EBI-2481729,EBI-1045313; Score: 0.37
DE  Interaction: Q96A65; IntAct: EBI-355383,EBI-1045313; Score: 0.80
DE  Interaction: Q49A88; IntAct: EBI-751035,EBI-1045313; Score: 0.37
DE  Interaction: Q13813; IntAct: EBI-351450,EBI-1045313; Score: 0.55
DE  Interaction: O75962; IntAct: EBI-718519,EBI-1045313; Score: 0.55
DE  Interaction: P53804; IntAct: EBI-2681313,EBI-1045313; Score: 0.37
DE  Interaction: Q8IYT3; IntAct: EBI-2808089,EBI-1045313; Score: 0.37
DE  Interaction: Q9BQD3; IntAct: EBI-739657,EBI-1045313; Score: 0.37
DE  Interaction: P55197; IntAct: EBI-1104952,EBI-1045313; Score: 0.37
DE  Interaction: Q9H2F5; IntAct: EBI-769270,EBI-1045313; Score: 0.37
DE  Interaction: Q5KU26; IntAct: EBI-1104680,EBI-1045313; Score: 0.55
DE  Interaction: Q9BZD4; IntAct: EBI-724102,EBI-1045313; Score: 0.55
DE  Interaction: Q9C0D2; IntAct: EBI-1104837,EBI-1045313; Score: 0.55
DE  Interaction: Q9UP83; IntAct: EBI-389502,EBI-1045313; Score: 0.37
DE  Interaction: O14795; IntAct: EBI-727343,EBI-1045313; Score: 0.37
DE  Interaction: Q96RF0; IntAct: EBI-298169,EBI-1045313; Score: 0.37
DE  Interaction: Q9C026; IntAct: EBI-720828,EBI-1045313; Score: 0.55
DE  Interaction: Q86XK3; IntAct: EBI-1104535,EBI-1045313; Score: 0.37
DE  Interaction: Q8TAB5; IntAct: EBI-747505,EBI-1045313; Score: 0.37
DE  Interaction: A0AUZ9; IntAct: EBI-5661988,EBI-1045313; Score: 0.37
DE  Interaction: Q7Z6K1; IntAct: EBI-2802307,EBI-1045313; Score: 0.37
DE  Interaction: O60341; IntAct: EBI-710124,EBI-1045313; Score: 0.37
DE  Interaction: Q9NYJ8; IntAct: EBI-358708,EBI-1045313; Score: 0.37
DE  Interaction: Q08AD1; IntAct: EBI-1051869,EBI-1045313; Score: 0.37
DE  Interaction: O75044; IntAct: EBI-1051034,EBI-1045313; Score: 0.37
DE  Interaction: Q9UPN3; IntAct: EBI-522925,EBI-1045313; Score: 0.55
DE  Interaction: O94822; IntAct: EBI-1044684,EBI-1045313; Score: 0.37
DE  Interaction: Q9UIF3; IntAct: EBI-11916475,EBI-1045313; Score: 0.37
DE  Interaction: Q96JM3; IntAct: EBI-2560420,EBI-1045313; Score: 0.37
DE  Interaction: Q13439; IntAct: EBI-1037845,EBI-1045313; Score: 0.55
DE  Interaction: Q8WYA0; IntAct: EBI-11321879,EBI-1045313; Score: 0.37
DE  Interaction: P28330; IntAct: EBI-12059321,EBI-1045313; Score: 0.37
DE  Interaction: Q14197; IntAct: EBI-1049413,EBI-1045313; Score: 0.37
DE  Interaction: Q14571; IntAct: EBI-2831342,EBI-1045313; Score: 0.37
DE  Interaction: Q6ZTA4; IntAct: EBI-21380498,EBI-1045313; Score: 0.37
DE  Interaction: O15230; IntAct: EBI-725060,EBI-1045313; Score: 0.37
DE  Interaction: Q14980; IntAct: EBI-521611,EBI-1045313; Score: 0.37
DE  Interaction: Q9ULH1; IntAct: EBI-346622,EBI-1045313; Score: 0.37
DE  Interaction: Q9NR80; IntAct: EBI-3389984,EBI-1045313; Score: 0.37
DE  Interaction: Q9Y383; IntAct: EBI-352851,EBI-1045313; Score: 0.37
DE  Interaction: Q9H7U1; IntAct: EBI-714702,EBI-1045313; Score: 0.55
DE  Interaction: Q567U6; IntAct: EBI-1104769,EBI-1045313; Score: 0.37
DE  Interaction: Q5T0N5; IntAct: EBI-714058,EBI-1045313; Score: 0.37
DE  Interaction: Q9HCM1; IntAct: EBI-308368,EBI-1045313; Score: 0.55
DE  Interaction: Q9NX95; IntAct: EBI-948293,EBI-1045313; Score: 0.37
DE  Interaction: Q7Z4S6; IntAct: EBI-2691397,EBI-1045313; Score: 0.37
DE  Interaction: Q3V6T2; IntAct: EBI-2266839,EBI-1045313; Score: 0.37
DE  Interaction: Q9Y275; IntAct: EBI-519169,EBI-1045313; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-4401271,EBI-1045313; Score: 0.35
DE  Interaction: Q80U62; IntAct: EBI-3506572,EBI-1045313; Score: 0.40
DE  Interaction: Q8CDJ3; IntAct: EBI-3506699,EBI-1045313; Score: 0.40
DE  Interaction: O00471; IntAct: EBI-949824,EBI-1045313; Score: 0.51
DE  Interaction: O95721; IntAct: EBI-490676,EBI-1045313; Score: 0.51
DE  Interaction: Q13445; IntAct: EBI-4310995,EBI-1045313; Score: 0.51
DE  Interaction: Q53HC9; IntAct: EBI-1055422,EBI-1045313; Score: 0.51
DE  Interaction: Q96KP1; IntAct: EBI-1045313,EBI-465715; Score: 0.80
DE  Interaction: P18848; IntAct: EBI-1045313,EBI-492498; Score: 0.56
DE  Interaction: Q15051; IntAct: EBI-2805823,EBI-1045313; Score: 0.64
DE  Interaction: A8K0Z3; IntAct: EBI-1045313,EBI-6160405; Score: 0.51
DE  Interaction: Q5NH32; IntAct: EBI-1045313,EBI-2799515; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-1045313,EBI-447544; Score: 0.40
DE  Interaction: Q8TD31-3; IntAct: EBI-10175300,EBI-1045313; Score: 0.56
DE  Interaction: Q9UEU0; IntAct: EBI-1045313,EBI-723716; Score: 0.51
DE  Interaction: Q9UPT5; IntAct: EBI-1045313,EBI-720048; Score: 0.51
DE  Interaction: Q13049; IntAct: EBI-1045313,EBI-742790; Score: 0.51
DE  Interaction: Q9H5N1; IntAct: EBI-1045313,EBI-3940735; Score: 0.51
DE  Interaction: Q9Y2D4; IntAct: EBI-2690026,EBI-1045313; Score: 0.51
DE  Interaction: Q15051-2; IntAct: EBI-11944935,EBI-1045313; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-1045313,EBI-1188238; Score: 0.37
DE  Interaction: P11234; IntAct: EBI-1045313,EBI-752162; Score: 0.27
GO  GO:0005737;
GO  GO:0098592;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0017049;
GO  GO:0005546;
GO  GO:0051607;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0048015;
GO  GO:0050714;
GO  GO:0015031;
GO  GO:0016241;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDA
SQ  KDAIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVTGGDEEVVDEY
SQ  QELNAREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEE
SQ  MLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNVALR
SQ  PGHDLLLAVKQQQQRFSDLRELFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDY
SQ  GKYEGLTKNYMDYLSRLYEREIKDFFEVAKIKMTGTTKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQ
SQ  SSGNRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQSMPGTMAEAEDLDGGTL
SQ  SRQHNCGTPLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVL
SQ  VTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFVNVEKVANES
SQ  QKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSY
SQ  QLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTI
SQ  QDILDYCSSIAQSH
//
ID  Q86VE9;
PN  Serine incorporator 5;
GN  SERINC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (PubMed:26416733, PubMed:26416734). Localizes to the cell membrane, where it is efficiently incorporated into budding virions and impairs subsequent virion entry into target cells (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}.
DR  UNIPROT: Q86VE9;
DR  UNIPROT: B4DMH7;
DR  UNIPROT: Q495A4;
DR  UNIPROT: Q495A6;
DR  Pfam: PF03348;
DR  OMIM: 614551;
DR  DisGeNET: 256987;
DE  Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043209;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0051607;
GO  GO:0009597;
GO  GO:0045087;
GO  GO:0006564;
GO  GO:0042552;
GO  GO:0006658;
GO  GO:0008654;
GO  GO:1904219;
GO  GO:1904222;
GO  GO:0006665;
GO  GO:0016032;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGD
SQ  TCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAV
SQ  GGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLC
SQ  LLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSL
SQ  LIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLA
SQ  SLYVMMTVTNWFNHVRSAFHLLP
//
ID  P21818;
PN  Stathmin-2;
GN  Stmn2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone. Cell projection, axon. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus. Endosome. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in the cell body, neuritis and growth cones of neurons. Colocalized with CIB1 to the leading edge of lamellipodia (By similarity). Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. Exists in both soluble and membrane-bound forms. Colocalized with CIB1 in neurites of developing hippocampal primary neurons. {ECO:0000250}.
DR  UNIPROT: P21818;
DR  UNIPROT: Q9ERH2;
DR  Pfam: PF00836;
DR  PROSITE: PS00563;
DR  PROSITE: PS01041;
DR  PROSITE: PS51663;
DE  Function: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone. {ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9012855}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0031982;
GO  GO:0048306;
GO  GO:0015631;
GO  GO:1990090;
GO  GO:0007019;
GO  GO:0007026;
GO  GO:0031115;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0031117;
GO  GO:0010976;
GO  GO:0051493;
GO  GO:0031110;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLS
SQ  LEEIQKKLEAAEGRRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEK
SQ  ERHAAEVRRNKELQVELSG
//
ID  O14188;
PN  Ras GTPase-activating-like protein rng2;
GN  rng2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localized to the F-actin ring and spindle pole body during interphase and mitosis. Also found in septum.
DR  UNIPROT: O14188;
DR  UNIPROT: Q9USG0;
DR  PDB: 1P2X;
DR  PDB: 1P5S;
DR  Pfam: PF00307;
DR  Pfam: PF00612;
DR  Pfam: PF00616;
DR  Pfam: PF03836;
DR  PROSITE: PS50021;
DR  PROSITE: PS50096;
DR  PROSITE: PS50018;
DE  Function: Required for cytokinesis. Component of the contractile F- actin ring; required for its construction following assembly of F-actin at the division site. {ECO:0000269|PubMed:9635188}.
DE  Reference Proteome: Yes;
GO  GO:0005826;
GO  GO:0120104;
GO  GO:0005737;
GO  GO:0071341;
GO  GO:0110085;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0005816;
GO  GO:0051015;
GO  GO:0005516;
GO  GO:0005096;
GO  GO:0051017;
GO  GO:1903478;
GO  GO:0000917;
GO  GO:1903475;
GO  GO:1903479;
GO  GO:1902405;
GO  GO:1903477;
GO  GO:0030835;
GO  GO:0030838;
GO  GO:1903476;
GO  GO:0071574;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQ
SQ  KFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSD
SQ  ENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEF
SQ  SKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTS
SQ  GLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSIS
SQ  RAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIP
SQ  LFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLE
SQ  KLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAIL
SQ  LRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVK
SQ  NFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKIN
SQ  TLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVI
SQ  KLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKL
SQ  TLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYV
SQ  APVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYF
SQ  EFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCT
SQ  IENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYT
SQ  ALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETL
SQ  QSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTV
SQ  KVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS
//
ID  P49021;
PN  Protein timeless;
GN  tim;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:8625406}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8625406}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization.
DR  UNIPROT: P49021;
DR  UNIPROT: A4V040;
DR  UNIPROT: B7Z007;
DR  UNIPROT: B7Z008;
DR  UNIPROT: C9QPB7;
DR  UNIPROT: M9MRE9;
DR  UNIPROT: O44380;
DR  UNIPROT: Q1WWF5;
DR  UNIPROT: Q59E16;
DR  UNIPROT: Q8I037;
DR  UNIPROT: Q95U67;
DR  UNIPROT: Q9VQR6;
DR  UNIPROT: Q9VQR7;
DR  Pfam: PF04821;
DE  Function: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition. {ECO:0000269|PubMed:7481772, ECO:0000269|PubMed:7481773, ECO:0000269|PubMed:8128247, ECO:0000269|PubMed:8625406, ECO:0000269|PubMed:9504927}.
DE  Reference Proteome: Yes;
DE  Interaction: O77059; IntAct: EBI-266295,EBI-94117; Score: 0.27
DE  Interaction: P07663; IntAct: EBI-266295,EBI-496170; Score: 0.50
DE  Interaction: Q9VDY1; IntAct: EBI-3414232,EBI-266295; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9933576,EBI-266295; Score: 0.35
DE  Interaction: Q24568; IntAct: EBI-3406532,EBI-266295; Score: 0.35
DE  Interaction: Q9V480; IntAct: EBI-171262,EBI-266295; Score: 0.37
DE  Interaction: Q9VQ30; IntAct: EBI-93669,EBI-266295; Score: 0.37
DE  Interaction: Q960S0; IntAct: EBI-160404,EBI-266295; Score: 0.37
DE  Interaction: P51123; IntAct: EBI-499582,EBI-266295; Score: 0.37
DE  Interaction: Q24432; IntAct: EBI-133159,EBI-266295; Score: 0.37
DE  Interaction: O61735; IntAct: EBI-266295,EBI-143834; Score: 0.27
DE  Interaction: P18431; IntAct: EBI-266295,EBI-242141; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000790;
GO  GO:0000228;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0031298;
GO  GO:0003677;
GO  GO:0046982;
GO  GO:0008134;
GO  GO:0071482;
GO  GO:0048512;
GO  GO:0003053;
GO  GO:0007623;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0006281;
GO  GO:0000076;
GO  GO:0008062;
GO  GO:0009649;
GO  GO:0045475;
GO  GO:0007617;
GO  GO:0046957;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0009648;
GO  GO:0050766;
GO  GO:0006606;
GO  GO:0042749;
GO  GO:0045187;
GO  GO:0050764;
GO  GO:0042306;
GO  GO:0043111;
GO  GO:0048478;
GO  GO:0007622;
GO  GO:0030431;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQNVRSDLIPLLENAKDDAVLE
SQ  SVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLYTSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNC
SQ  LLLLRNILHIPETHAHCVMPMMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTL
SQ  QKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMREGTAATLQEVSRKGQEYQNA
SQ  MARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMDDGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPL
SQ  NLTQQPADKVNNTTNPTSSAPQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKG
SQ  KCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKPRTIMSPMDKKELRRKKLVKR
SQ  SKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYLVEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDME
SQ  HIDTILTYDVLSYLTYEGVSLCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQ
SQ  ISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHITQFATLEVMHYYGILLEDFN
SQ  NNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIWEADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEM
SQ  TKEHNQEHTVCSWSQEEMDTLYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAE
SQ  YQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCFVKLTLRSGLKVPEGDHIMEP
SQ  VAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQLPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDA
SQ  SELEDATASSPSRYHHTGPRNSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYT
SQ  PDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTSMSTVNPTTTLSLNMLNTFMG
SQ  SHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEMDVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEK
SQ  EKELNSDNVSLASDLTRMYVSDEDDRLERTEIRVPHYH
//
ID  H2L056;
PN  UBX domain-containing protein 3;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:26842564}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Chromosome {ECO:0000269|PubMed:26842564}. Cytoplasm {ECO:0000269|PubMed:26842564}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the nucleus during S phase in a cdc-48 and npl-4-dependent manner (PubMed:26842564). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564}.
DR  UNIPROT: H2L056;
DR  UNIPROT: A0A0K3ARL0;
DR  UNIPROT: A0A0K3ATZ0;
DR  UNIPROT: A0A0K3AWX1;
DR  UNIPROT: Q6A589;
DR  PROSITE: PS50033;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550, PubMed:26842564, PubMed:28368371). Together with ubxn-1 and ubxn-2, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1 (PubMed:20977550). During mitosis, ensures the degradation of DNA licensing factor cdt-1 and the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:26842564, PubMed:28368371). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0036435;
GO  GO:0044877;
GO  GO:0030154;
GO  GO:0042006;
GO  GO:1903364;
GO  GO:0045977;
GO  GO:1905634;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSS
SQ  SRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSS
SQ  GSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSM
SQ  AIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKE
SQ  AFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQR
SQ  LAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASL
SQ  AADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQT
SQ  LINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI
//
ID  Q19253;
PN  Transducer of Cdc42-dependent actin assembly protein 1 homolog;
GN  toca;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:23150597}. Apical cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Basolateral cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Cytoplasmic vesicle {ECO:0000269|PubMed:19798448}. Cytoplasm {ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23150597}. Recycling endosome {ECO:0000269|PubMed:25775511}. Note=Co-localizes with ajm-1 at cell junctions (PubMed:19798448). Co-localizes with toca-2, rme-1, cdc-42 and wve-1 on recycling endosomes (PubMed:25775511). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
DR  UNIPROT: Q19253;
DR  UNIPROT: Q8MQ82;
DR  Pfam: PF00611;
DR  Pfam: PF00018;
DR  PROSITE: PS51741;
DR  PROSITE: PS51860;
DR  PROSITE: PS50002;
DE  Function: Plays a role in protein trafficking, actin organization and embryonic morphogenesis (PubMed:19798448). Potentially acts as cdc-42 effector (PubMed:25775511). May play a role in hypodermal P-cell nuclear positioning (PubMed:23150597). Together with toca-2, is required for protein trafficking regulating yolk protein clathrin- mediated endocytosis by oocytes during oogenesis and retrograde recycling and the sorting of recycling endosome cargo proteins such as mig-14 (PubMed:19798448, PubMed:25775511). Also, together with toca-2, controls the distribution of actin at cell junctions (PubMed:19798448, PubMed:26578656). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511, ECO:0000269|PubMed:26578656}.
DE  Reference Proteome: Yes;
DE  Interaction: P39055; IntAct: EBI-6533634,EBI-317945; Score: 0.37
DE  Interaction: A0A1C3NSL9; IntAct: EBI-327553,EBI-6533634; Score: 0.37
DE  Interaction: O17578; IntAct: EBI-6533634,EBI-2412885; Score: 0.37
DE  Interaction: Q09442; IntAct: EBI-2316106,EBI-6533634; Score: 0.37
DE  Interaction: G5ED57; IntAct: EBI-327853,EBI-6533634; Score: 0.37
DE  Interaction: Q9XZI6; IntAct: EBI-6533634,EBI-311866; Score: 0.37
DE  Interaction: B7WN72; IntAct: EBI-2914750,EBI-6533634; Score: 0.37
DE  Interaction: Q93343; IntAct: EBI-6533634,EBI-6533726; Score: 0.37
DE  Interaction: Q20877; IntAct: EBI-315480,EBI-6533634; Score: 0.37
DE  Interaction: Q19782; IntAct: EBI-6533634,EBI-320224; Score: 0.37
DE  Interaction: Q20010; IntAct: EBI-6533634,EBI-327608; Score: 0.37
DE  Interaction: G5EFY6; IntAct: EBI-6533634,EBI-317770; Score: 0.37
DE  Interaction: Q94246; IntAct: EBI-6533634,EBI-6461124; Score: 0.37
DE  Interaction: O01900; IntAct: EBI-315098,EBI-6533634; Score: 0.37
DE  Interaction: G5EF97; IntAct: EBI-6533634,EBI-6533878; Score: 0.37
DE  Interaction: Q9U304; IntAct: EBI-6533634,EBI-329038; Score: 0.37
DE  Interaction: G5EC72; IntAct: EBI-6531450,EBI-6533634; Score: 0.37
DE  Interaction: A8WFL0; IntAct: EBI-6533929,EBI-6533634; Score: 0.37
DE  Interaction: A5PEX6; IntAct: EBI-6532321,EBI-6533634; Score: 0.37
DE  Interaction: Q4VNJ8; IntAct: EBI-2918529,EBI-6533634; Score: 0.37
DE  Interaction: Q23571; IntAct: EBI-6533634,EBI-330837; Score: 0.37
DE  Interaction: O17577; IntAct: EBI-6542250,EBI-6533634; Score: 0.37
DE  Interaction: O61701; IntAct: EBI-6533634,EBI-6537266; Score: 0.37
DE  Interaction: Q95QQ9; IntAct: EBI-6533634,EBI-2317344; Score: 0.37
DE  Interaction: Q1XFY2; IntAct: EBI-2316564,EBI-6533634; Score: 0.37
DE  Interaction: G5ECJ4; IntAct: EBI-6533634,EBI-317668; Score: 0.37
DE  Interaction: F5GUF0; IntAct: EBI-6542338,EBI-6533634; Score: 0.37
DE  Interaction: Q95QA6; IntAct: EBI-6533634,EBI-327642; Score: 0.37
DE  Interaction: A8XQ35; IntAct: EBI-6533634,EBI-6542385; Score: 0.37
GO  GO:0016324;
GO  GO:0016323;
GO  GO:0005911;
GO  GO:0097708;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0048613;
GO  GO:0006897;
GO  GO:1904703;
GO  GO:2000370;
GO  GO:1901046;
GO  GO:0032956;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNDSCSWDQLWDQQGTLNEYTGKGIDLLERIMAYSKERASIELEYSSKLKALSKKTAMKMKSESELWNSVSYVKGFHDVI
SQ  AGIVPVATQHELIAENLKSAVIPFTTQKIAEYRVAKKQLESDNSNLGKQLRMVIDEMAKSHKEYVKCYKETEAAMLKYAK
SQ  AEKNMDISRLELEKTKNNYQQKCGMLEESKQTYAVMTTKANEEQSAHYDRKLPQLLDNYKKLHTNRILDTVEILSKCVEA
SQ  ESCVNQIIASCHNDMRRDIGLIDPSRDANLVVENMKSGHPVPQPFVFEDLGHPQDRSSFMGGGASGPAGSMDGMDATMKK
SQ  GGTLMSKNGKGVARKQSMHQKFFGGGTADKKTDSGDYGTLPPQQRARKIAGKISDLEKEKDRATQSREGVSKMQAAYREN
SQ  PKLGNPSDCDAQLAQYGHEIDALSNQIQKFKILLDDVNAQLGAGGLSATSVGGSDTPPSIRSVSSASSGVTSRVNTINDA
SQ  HRTNGGVGGGRRESFSGSNGGSDTDPTINGNGHGRDELYEECSNPNPVLGEAIAQFAFDGAQDGTIRMEANEKLWLIEKD
SQ  EGDGWTRVRKENNSADGFVPSSYLKVTWFGKV
//
ID  Q61382;
PN  TNF receptor-associated factor 4;
GN  Traf4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
DR  UNIPROT: Q61382;
DR  UNIPROT: Q8BHD9;
DR  Pfam: PF00097;
DR  Pfam: PF02176;
DR  PROSITE: PS50144;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  PROSITE: PS50145;
DE  Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor (TNFR) family to different signaling pathways. Plays a role in the activation of NF-kappa-B and JNK, and in the regulation of cell survival and apoptosis. Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions (By similarity). Required for normal skeleton development, and for normal development of the respiratory tract. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0031996;
GO  GO:0005164;
GO  GO:0031625;
GO  GO:0050699;
GO  GO:0008270;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0046330;
GO  GO:0045860;
GO  GO:0070534;
GO  GO:0042981;
GO  GO:0043122;
GO  GO:0007585;
GO  GO:0030323;
GO  GO:0033209;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLA
SQ  IRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVC
SQ  PQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLK
SQ  DSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRR
SQ  LQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAK
SQ  PQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS
//
ID  Q86Y07;
PN  Serine/threonine-protein kinase VRK2;
GN  VRK2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 1]: Cytoplasm. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8BN21}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16704422}. Nucleus {ECO:0000269|PubMed:16704422}.
DR  UNIPROT: Q86Y07;
DR  UNIPROT: B4DKL0;
DR  UNIPROT: D6W5D4;
DR  UNIPROT: D6W5D6;
DR  UNIPROT: Q49AK9;
DR  UNIPROT: Q53EU9;
DR  UNIPROT: Q53S39;
DR  UNIPROT: Q53S77;
DR  UNIPROT: Q53TU1;
DR  UNIPROT: Q86Y08;
DR  UNIPROT: Q86Y09;
DR  UNIPROT: Q86Y10;
DR  UNIPROT: Q86Y11;
DR  UNIPROT: Q86Y12;
DR  UNIPROT: Q8IXI5;
DR  UNIPROT: Q99987;
DR  PDB: 2V62;
DR  PDB: 5UU1;
DR  PDB: 6NCG;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602169;
DR  DisGeNET: 7444;
DE  Function: Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen- activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant. Isoform 2 phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-351935,EBI-1207615; Score: 0.35
DE  Interaction: P10415; IntAct: EBI-77694,EBI-1207615; Score: 0.37
DE  Interaction: P62826; IntAct: EBI-286642,EBI-1207615; Score: 0.27
DE  Interaction: O43318; IntAct: EBI-1207615,EBI-358684; Score: 0.40
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-1207615; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1207615; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-81752,EBI-1207615; Score: 0.37
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-1207615; Score: 0.65
DE  Interaction: Q02750; IntAct: EBI-492564,EBI-1207615; Score: 0.52
DE  Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-1207615; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-1207615; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-11334880,EBI-1207615; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-1207615; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-1207615; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-1207615; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-1207615; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104531,EBI-1207615; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-747644,EBI-1207615; Score: 0.35
DE  Interaction: Q86WU2; IntAct: EBI-11156684,EBI-1207615; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-876367,EBI-1207615; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1207615; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1207615; Score: 0.35
DE  Interaction: Q07817-1; IntAct: EBI-287195,EBI-1207615; Score: 0.27
DE  Interaction: Q07812; IntAct: EBI-516580,EBI-1207615; Score: 0.27
DE  Interaction: P03182; IntAct: EBI-1207615,EBI-1207659; Score: 0.60
DE  Interaction: Q0VAB0; IntAct: EBI-18271435,EBI-1207615; Score: 0.56
DE  Interaction: P36382; IntAct: EBI-750433,EBI-1207615; Score: 0.56
DE  Interaction: Q8N4V1; IntAct: EBI-6163737,EBI-1207615; Score: 0.56
DE  Interaction: Q6PEY1; IntAct: EBI-17198826,EBI-1207615; Score: 0.56
DE  Interaction: Q6UW68; IntAct: EBI-6269551,EBI-1207615; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-8638294,EBI-1207615; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-13059134,EBI-1207615; Score: 0.56
DE  Interaction: P38432; IntAct: EBI-1207615,EBI-945751; Score: 0.44
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0004674;
GO  GO:0034599;
GO  GO:0018105;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:2000659;
GO  GO:0043408;
GO  GO:0016032;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPPKRNEKYKLPIPFPEGKVLDDMEGNQWVLGKKIGSGGFGLIYLAFPTNKPEKDARHVVKVEYQENGPLFSELKFYQRV
SQ  AKKDCIKKWIERKQLDYLGIPLFYGSGLTEFKGRSYRFMVMERLGIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHEN
SQ  EYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGNHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCM
SQ  LRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLKWAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILNPHGIPL
SQ  GPLDFSTKGQSINVHTPNSQKVDSQKAATKQVNKAHNRLIEKKVHSERSAESCATWKVQKEEKLIGLMNNEAAQESTRRR
SQ  QKYQESQEPLNEVNSFPQKISYTQFPNSFYEPHQDFTSPDIFKKSRSPSWYKYTSTVSTGITDLESSTGLWPTISQFTLS
SQ  EETNADVYYYRIIIPVLLMLVFLALFFL
//
ID  P46061;
PN  Ran GTPase-activating protein 1;
GN  Rangap1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:9442102, PubMed:9456312, PubMed:26506250). Shuttles between nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}.
DR  UNIPROT: P46061;
DR  UNIPROT: Q60801;
DR  UNIPROT: Q6NZB5;
DR  PDB: 1KPS;
DR  Pfam: PF13516;
DR  Pfam: PF07834;
DE  Function: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:18305100). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development (PubMed:8314081). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:8314081}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-645094,EBI-1033051; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-8350418,EBI-1033051; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-912574,EBI-1033051; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-80168,EBI-1033051; Score: 0.44
DE  Interaction: Q9EPK7; IntAct: EBI-6908541,EBI-1033051; Score: 0.35
GO  GO:0016235;
GO  GO:1904115;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:1990723;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043231;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0008536;
GO  GO:0003723;
GO  GO:0031625;
GO  GO:0090630;
GO  GO:0071375;
GO  GO:1904117;
GO  GO:0046826;
GO  GO:0048678;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELK
SQ  RCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGK
SQ  ILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRV
SQ  INLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADK
SQ  AELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEP
SQ  PQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVAS
SQ  VFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPL
SQ  LLAFVTKPNGALETCSFARHNLLQTLYNI
//
ID  P19811;
PN  Non-structural protein 12;
GN  rep;
OS  299386;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1 papain-like cysteine proteinase]: Host nucleus. Host cytoplasm. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: P19811;
DR  UNIPROT: Q88625;
DR  UNIPROT: Q8QZQ5;
DR  UNIPROT: Q91DM2;
DR  PDB: 1MBM;
DR  PDB: 2L8K;
DR  PDB: 4IUM;
DR  PDB: 4N0N;
DR  PDB: 4N0O;
DR  PDB: 5F17;
DR  PDB: 5HBZ;
DR  PDB: 5HC1;
DR  Pfam: PF16749;
DR  Pfam: PF12581;
DR  Pfam: PF14755;
DR  Pfam: PF14754;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF17873;
DR  Pfam: PF01443;
DR  Pfam: PF17977;
DR  PROSITE: PS51538;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000269|PubMed:18078692}. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000269|PubMed:11172046}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. {ECO:0000269|PubMed:18078692}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000269|PubMed:18078692}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000269|PubMed:11000230, ECO:0000269|PubMed:24369429}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0070008;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0039648;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0006351;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATFSATGFGGSFVRDWSLDLPDACEHGAGLCCEVDGSTLCAECFRGCEGMEQCPGLFMGLLKLASPVPVGHKFLIGWYR
SQ  AAKVTGRYNFLELLQHPAFAQLRVVDARLAIEEASVFISTDHASAKRFPGARFALTPVYANAWVVSPAANSLIVTTDQEQ
SQ  DGFCWLKLLPPDRREAGLRLYYNHYREQRTGWLSKTGLRLWLGDLGLGINASSGGLKFHIMRGSPQRAWHITTRSCKLKS
SQ  YYVCDISEADWSCLPAGNYGGYNPPGDGACGYRCLAFMNGATVVSAGCSSDLWCDDELAYRVFQLSPTFTVTIPGGRVCP
SQ  NAKYAMICDKQHWRVKRAKGVGLCLDESCFRGICNCQRMSGPPPAPVSAAVLDHILEAATFGNVRVVTPEGQPRPVPAPR
SQ  VRPSANSSGDVKDPAPVPPVPKPRTKLATPNPTQAPIPAPRTRLQGASTQEPLASAGVASDSAPKWRVAKTVYSSAERFR
SQ  TELVQRARSVGDVLVQALPLKTPAVQRYTMTLKMMRSRFSWHCDVWYPLAVIACLLPIWPSLALLLSFAIGLIPSVGNNV
SQ  VLTALLVSSANYVASMDHQCEGAACLALLEEEHYYRAVRWRPITGALSLVLNLLGQVGYVARSTFDAAYVPCTVFDLCSF
SQ  AILYLCRNRCWRCFGRCVRVGPATHVLGSTGQRVSKLALIDLCDHFSKPTIDVVGMATGWSGCYTGTAAMERQCASTVDP
SQ  HSFDQKKAGATVYLTPPVNSGSALQCLNVMWKRPIGSTVLGEQTGAVVTAVKSISFSPPCCVSTTLPTRPGVTVVDHALY
SQ  NRLTASGVDPALLRVGQGDFLKLNPGFRLIGGWIYGICYFVLVVVSTFTCLPIKCGIGTRDPFCRRVFSVPVTKTQEHCH
SQ  AGMCASAEGISLDSLGLTQLQSYWIAAVTSGLVILLVCHRLAISALDLLTLASPLVLLVFPWASVGLLLACSLAGAAVKI
SQ  QLLATLFVNLFFPQATLVTMGYWACVAALAVYSLMGLRVKVNVPMCVTPAHFLLLARSAGQSREQMLRVSAAAPTNSLLG
SQ  VARDCYVTGTTRLYIPKEGGMVFEGLFRSPKARGNVGFVAGSSYGTGSVWTRNNEVVVLTASHVVGRANMATLKIGDAML
SQ  TLTFKKNGDFAEAVTTQSELPGNWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQGDAVVGVHTG
SQ  SNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADVDAVPRSLAMLIDGLSNRESSLSGPQLLLIA
SQ  CFMWSYLNQPAYLPYVLGFFAANFFLPKSVGRPVVTGLLWLCCLFTPLSMRLCLFHLVCATVTGNVISLWFYITAAGTSY
SQ  LSEMWFGGYPTMLFVPRFLVYQFPGWAIGTVLAVCSITMLAAALGHTLLLDVFSASGRFDRTFMMKYFLEGGVKESVTAS
SQ  VTRAYGKPITQESLTATLAALTDDDFQFLSDVLDCRAVRSAMNLRAALTSFQVAQYRNILNASLQVDRDAARSRRLMAKL
SQ  ADFAVEQEVTAGDRVVVIDGLDRMAHFKDDLVLVPLTTKVVGGSRCTICDVVKEEANDTPVKPMPSRRRRKGLPKGAQLE
SQ  WDRHQEEKRNAGDDDFAVSNDYVKRVPKYWDPSDTRGTTVKIAGTTYQKVVDYSGNVHYVEHQEDLLDYVLGKGSYEGLD
SQ  QDKVLDLTNMLKVDPTELSSKDKAKARQLAHLLLDLANPVEAVNQLNLRAPHIFPGDVGRRTFADSKDKGFVALHSRTMF
SQ  LAARDFLFNIKFVCDEEFTKTPKDTLLGYVRACPGYWFIFRRTHRSLIDAYWDSMECVYALPTISDFDVSPGDVAVTGER
SQ  WDFESPGGGRAKRLTADLVHAFQGFHGASYSYDDKVAAAVSGDPYRSDGVLYNTRWGNIPYSVPTNALEATACYRAGCEA
SQ  VTDGTNVIATIGPFPEQQPIPDIPKSVLDNCADISCDAFIAPAAETALCGDLEKYNLSTQGFVLPSVFSMVRAYLKEEIG
SQ  DAPPLYLPSTVPSKNSQAGINGAEFPTKSLQSYCLIDDMVSQSMKSNLQTATMATCKRQYCSKYKIRSILGTNNYIGLGL
SQ  RACLSGVTAAFQKAGKDGSPIYLGKSKFDPIPAPDKYCLETDLESCDRSTPALVRWFATNLIFELAGQPELVHSYVLNCC
SQ  HDLVVAGSVAFTKRGGLSSGDPITSISNTIYSLVLYTQHMLLCGLEGYFPEIAEKYLDGSLELRDMFKYVRVYIYSDDVV
SQ  LTTPNQHYAASFDRWVPHLQALLGFKVDPKKTVNTSSPSFLGCRFKQVDGKCYLASLQDRVTRSLLYHIGAKNPSEYYEA
SQ  AVSIFKDSIICCDEDWWTDLHRRISGAARTDGVEFPTIEMLTSFRTKQYESAVCTVCGAAPVAKSACGGWFCGNCVPYHA
SQ  GHCHTTSLFANCGHDIMYRSTYCTMCEGSPKQMVPKVPHPILDHLLCHIDYGSKEELTLVVADGRTTSPPGRYKVGHKVV
SQ  AVVADVGGNIVFGCGPGSHIAVPLQDTLKGVVVNKALKNAAASEYVEGPPGSGKTFHLVKDVLAVVGSATLVVPTHASML
SQ  DCINKLKQAGADPYFVVPKYTVLDFPRPGSGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILTQGRVKGYGDLNQLGC
SQ  VGPASVPRNLWLRHFVSLEPLRVCHRFGAAVCDLIKGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYHKDRGLGHRTID
SQ  SIQGCTFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLLKFTKEAEAQDLIHGPPTACHLGQEIDLWSNE
SQ  GLEYYKEVNLLYTHVPIKDGVIHSYPNCGPACGWEKQSNKISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDR
SQ  YPNCLQITLQQVCELSKPCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKARALPDSLFSSGRFETNSRAFLDEAEEKFAAA
SQ  HPHACLGEINKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAKAACSVVDVYAPSFEPYLHPETLSRVYKIMIDFK
SQ  PCRLMVWRNATFYVQEGVDAVTSALAAVSKLIKVPANEPVSFHVASGYRTNALVAPQAKISIGAYAAEWALSTEPPPAGY
SQ  AIVRRYIVKRLLSSTEVFLCRRGVVSSTSVQTICALEGCKPLFNFLQIGSVIGPV
//
ID  Q719N1;
PN  Spastin;
GN  SPAST;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP- Rule:MF_03021}.
DR  UNIPROT: Q719N1;
DR  UNIPROT: F1S3Z2;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP- Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0031122;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRGKKKGSGGPSSPVPPRPPPPCLASSRPAPRPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQ
SQ  RFSRALMAAKRSSRAAPAPASASPPAPVPGGEVERVRAFHKQAFEYISVALRIDEDEKVGQKEQAVEWYKKGIEELEKGI
SQ  AVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPVLQFSKSQMDVYNDSTNLTCRNGHLQSESGAVPKRKDPLT
SQ  HPSNSLPRSKAIMKTGSTGLSGHHRAPSCSGLSIVSGMRQGPGPTTATHKSTPKTNRTNKPSTPTTAPRKKKDLKNFRNV
SQ  DSNLANFIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN
SQ  ATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLRERREGEHDASRRLKTEFLIEFDGVQSAGDDRV
SQ  LVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARLTDGYSGSDLTALAKDAALGP
SQ  IRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
//
ID  Q6B9X6;
PN  Alpha-protein kinase vwkA;
GN  vwkA;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:15728726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15728726}. Contractile vacuole membrane {ECO:0000269|PubMed:15728726}. Note=Enriched adjacent to large spherical structures such as contractile vacuoles and Golgi-like structures (perinuclear).
DR  UNIPROT: Q6B9X6;
DR  UNIPROT: Q55FF0;
DR  Pfam: PF02816;
DR  PROSITE: PS51158;
DE  Function: Displays a modest preference for threonine over serine residues. Does not phosphorylate myosin II, however can phosphorylate MBP, in vitro. May be involved in the regulation of myosin II function during cytokinesis. Overexpression leads to impaired cell proliferation in suspension culture and fails to develop beyond the mound stage. Both overexpression and absence of the gene can result in defects in cytokinesis and alterations in myosin II abundance and assembly. {ECO:0000269|PubMed:15728726, ECO:0000269|PubMed:18381083}.
DE  Reference Proteome: Yes;
GO  GO:0031164;
GO  GO:0000331;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0004672;
GO  GO:0004674;
GO  GO:0070177;
GO  GO:0033298;
GO  GO:0006971;
GO  GO:0000281;
GO  GO:0031038;
GO  GO:0018209;
GO  GO:0018107;
GO  GO:0006468;
GO  GO:0031156;
GO  GO:0031288;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESKYVLSTEKESKTKPSGRVNVSDMDSISNSLSKTSLGTRKVPTSLKTDASRSGLSSGGSKTHISDESALRMVYGSTPR
SQ  DEKTTTTKDSITLAKEKEKKIEKRNEEIKLTFKAIRASECVDLLFIVDCTGSMDPYIEQIKSDIVKLQEALKLKHSFLDI
SQ  EFGFIRYTDFDVASNRCSTFQFSRSTVEFVRFVSEIRAGGGADGPEDVFGGMDLIKSMKWRPNSTRVVIHIADAPCHGTE
SQ  YHSMADSYPGGDPNGIKLDDLLTDIISLNINYYFGHINLKETGQMIDFFDKKTKEISRNKKSINSFDSKETSKMNERIFI
SQ  SIEESISVSRSVLTEQYLGHNIDGSTGKQRSEREFEINTNMDIDFGELPYIQMLQTKFKMPSDIVTCLSSSYEMKLNEIT
SQ  ISIKIAPNPFSHGACRLAYLGIDEHGKKVVLKQSKYIGGRENSKKRYFESMECQTVAAKFALEFNKQLSLTSSEHQITFT
SQ  VAKVLQMKHSEKPMYFGIETFINGEYQKYNSNCGWLKDDAMSEILQTFSHWTYQESKNKAIVVDIQGVKTSKGYLLTDPA
SQ  IHSTDTLRFGSCNLGKPGIIKFFQSHKCNQHCKKLGLTIPSFTSSSSTSSSSRSTSSSSSISYSY
//
ID  Q5SQN1;
PN  Synaptosomal-associated protein 47;
GN  SNAP47;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
DR  UNIPROT: Q5SQN1;
DR  UNIPROT: B6EDE0;
DR  UNIPROT: Q5HYB5;
DR  UNIPROT: Q5TBZ3;
DR  UNIPROT: Q8N558;
DR  UNIPROT: Q8TB31;
DR  UNIPROT: Q8TCW8;
DR  UNIPROT: Q8WV46;
DR  UNIPROT: Q96CQ3;
DR  UNIPROT: Q96FE1;
DR  UNIPROT: Q96I66;
DR  UNIPROT: Q96NU3;
DR  UNIPROT: Q9BT10;
DR  UNIPROT: Q9BVB2;
DR  PROSITE: PS50192;
DR  DisGeNET: 116841;
DE  Function: Plays a role in intracellular membrane fusion. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92844; IntAct: EBI-356349,EBI-10244848; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-10191195,EBI-10244848; Score: 0.35
DE  Interaction: P51809; IntAct: EBI-10244848,EBI-1052205; Score: 0.52
DE  Interaction: Q9BV40; IntAct: EBI-10244848,EBI-727028; Score: 0.40
DE  Interaction: O75379; IntAct: EBI-10244848,EBI-744953; Score: 0.40
DE  Interaction: Q15836; IntAct: EBI-10244848,EBI-722343; Score: 0.40
DE  Interaction: Q9Y6D6; IntAct: EBI-1044254,EBI-10244848; Score: 0.37
DE  Interaction: Q92845-3; IntAct: EBI-11294297,EBI-10244848; Score: 0.37
DE  Interaction: Q9UPN3-2; IntAct: EBI-4295250,EBI-10244848; Score: 0.37
DE  Interaction: Q13190; IntAct: EBI-10244848,EBI-714206; Score: 0.40
DE  Interaction: Q86Y82; IntAct: EBI-10244848,EBI-2691717; Score: 0.56
DE  Interaction: P32851; IntAct: EBI-539720,EBI-10244848; Score: 0.56
DE  Interaction: P43360; IntAct: EBI-10244848,EBI-1045155; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-10244848,EBI-618309; Score: 0.56
DE  Interaction: Q12846; IntAct: EBI-10244848,EBI-744942; Score: 0.56
DE  Interaction: Q6P597; IntAct: EBI-10244848,EBI-1643885; Score: 0.56
DE  Interaction: Q8IYX8-2; IntAct: EBI-10244848,EBI-10181988; Score: 0.56
DE  Interaction: Q8IZU0; IntAct: EBI-10175124,EBI-10244848; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-743099,EBI-10244848; Score: 0.56
DE  Interaction: Q96R06; IntAct: EBI-10244848,EBI-413317; Score: 0.56
DE  Interaction: Q9UJV3-2; IntAct: EBI-10172526,EBI-10244848; Score: 0.56
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-10244848; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-10244848; Score: 0.35
DE  Interaction: P28574; IntAct: EBI-1183003,EBI-10244848; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-711636,EBI-10244848; Score: 0.35
DE  Interaction: Q8IWR1; IntAct: EBI-10262539,EBI-10244848; Score: 0.56
DE  Interaction: P55056; IntAct: EBI-10244848,EBI-18302142; Score: 0.56
DE  Interaction: P61266; IntAct: EBI-9071709,EBI-10244848; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-712466,EBI-10244848; Score: 0.56
DE  Interaction: Q9Y624; IntAct: EBI-742600,EBI-10244848; Score: 0.56
DE  Interaction: Q96K19-5; IntAct: EBI-12055631,EBI-10244848; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-3920694,EBI-10244848; Score: 0.56
DE  Interaction: Q9HCJ2; IntAct: EBI-3925442,EBI-10244848; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-2830566,EBI-10244848; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-12701138,EBI-10244848; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-724754,EBI-10244848; Score: 0.56
DE  Interaction: P15151; IntAct: EBI-3919694,EBI-10244848; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-749265,EBI-10244848; Score: 0.56
DE  Interaction: Q8N137; IntAct: EBI-947360,EBI-10244848; Score: 0.35
DE  Interaction: Q9UJY5; IntAct: EBI-10244848,EBI-447141; Score: 0.27
DE  Interaction: Q9NTX5; IntAct: EBI-10244848,EBI-2807146; Score: 0.27
DE  Interaction: O75396; IntAct: EBI-1058865,EBI-10244848; Score: 0.35
DE  Interaction: Q9P2W9; IntAct: EBI-725334,EBI-10244848; Score: 0.35
DE  Interaction: O15400-2; IntAct: EBI-11042829,EBI-10244848; Score: 0.35
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0098686;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0031201;
GO  GO:0030672;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0060291;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRAARRGLHCAGAERPRRRGRLWDSSGVPQRQKRPGPWRTQTQEQMSRDVCIHTWPCTYYLEPKRRWVTGQLSLTSLSLR
SQ  FMTDSTGEILVSFPLSSIVEIKKEASHFIFSSITILEKGHAKHWFSSLRPSRNVVFSIIEHFWRELLLSQPGAVADASVP
SQ  RTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTELESPAWWPFSSKLWKTPPETKPRED
SQ  VSMTSCEPFGKEGILIKIPAVISHRTESHVKPGRLTVLVSGLEIHDSSSLLMHRFEREDVDDIKVHSPYEISIRQRFIGK
SQ  PDMAYRLISAKMPEVIPILEVQFSKKMELLEDALVLRSARTSSPAEKSCSVWHAASGLMGRTLHREPPAGDQEGTALHLQ
SQ  TSLPALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT
//
ID  Q8VIG6;
PN  E3 ubiquitin-protein ligase TRAIP;
GN  Traip;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BWF2}. Note=In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci. After UV irradiation, rapidly localizes to sites of DNA damage, where it colocalizes with phosphorylated histone H2AX (gamma-H2AX) and RPA2. {ECO:0000250|UniProtKB:Q9BWF2}.
DR  UNIPROT: Q8VIG6;
DR  UNIPROT: O08854;
DR  UNIPROT: Q922M8;
DR  UNIPROT: Q9CPP4;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity) (PubMed:17544371, PubMed:22945920). Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV- induced replication-blocking lesions during S phase. Might also play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity. The function in translesion synthesis is controversial (By similarity). {ECO:0000250|UniProtKB:Q9BWF2, ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0032688;
GO  GO:0032088;
GO  GO:0010804;
GO  GO:0016567;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKKTIINKLFFDLAQEEENVLDAEFLK
SQ  NELDSVKAQLSQKDREKRDSQAIIDTLRDTLEERNATVESLQNALNKAEMLCSTLKKQMKFLEQRQDETKQAREEAHRLK
SQ  CKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKATGELADRLKKDLVSSRSKLKTLN
SQ  TELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLSLPPATNETVSRLVFESPAPVEMMNPRLHQPPFGDEIDLNTT
SQ  FDVNTPPTQTSGSQHCLPKKLCLERARSPMQNVLKKVHKVSKPESQLSLGGQRCVGELDEELAGAFPLFIRNAVLGQKQP
SQ  NRTTAESRCSTDVVRIGFDGLGGRTKFIQPRDTTIIRPVPVKSKAKSKQKVRIKTVSSASQPKLDTFLCQ
//
ID  P46674;
PN  Nuclear mRNA export protein SAC3;
GN  SAC3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores.
DR  UNIPROT: P46674;
DR  UNIPROT: D6VSD9;
DR  PDB: 3FWB;
DR  PDB: 3FWC;
DR  PDB: 3T5V;
DR  PDB: 4C31;
DR  PDB: 4MBE;
DR  PDB: 4TRQ;
DR  PDB: 5G5P;
DR  PDB: 5L3T;
DR  Pfam: PF12209;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DE  Function: Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:12702719}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-16425,EBI-10420; Score: 0.35
DE  Interaction: Q06410; IntAct: EBI-16425,EBI-30856; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-8591,EBI-16425; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-16425,EBI-30084; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-16425; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-24570,EBI-16425; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-16425,EBI-8627; Score: 0.35
DE  Interaction: P47079; IntAct: EBI-16425,EBI-19072; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-16425; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-8648,EBI-16425; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-27500,EBI-16425; Score: 0.35
DE  Interaction: Q6WNK7; IntAct: EBI-1251050,EBI-16425; Score: 0.82
DE  Interaction: P38129; IntAct: EBI-18868,EBI-16425; Score: 0.35
DE  Interaction: Q08231; IntAct: EBI-32097,EBI-16425; Score: 0.88
GO  GO:0005737;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0030029;
GO  GO:0000278;
GO  GO:0031124;
GO  GO:0006406;
GO  GO:0071033;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0042274;
GO  GO:0006283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKKSQQPLQNLSHSPSYTENKPD
SQ  KKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNEL
SQ  YETLKKMRNTERSIMEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVF
SQ  ARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIVRIHLLILH
SQ  IMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMAL
SQ  CFRRVISNSAYTERGFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENM
SQ  LLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDNLASSVYVKD
SQ  PKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTSPKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVH
SQ  GDLSEQKQQQIKTVTDGGSPFVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQEN
SQ  ADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFE
SQ  KWQASYSQAKKNRILEEKKREEIKLVSHQLGVPGFKKSTCLFRTPYKGNVNSSFMLSSSDKNLIFSPVNDEFNKFATHLT
SQ  KISKLWRPLEMQSIYYDNLTKKFPSNSLTPANLFIYAKDWTSLSNRWILSKFNLQTAQDSKKFSNNIISSRIICIDDEYE
SQ  PSDFSDLQLLIFNTGVTNPDIFDLEMKLKDDGEELIKLITGISLNTNICFSLLIIYWESAENTLSESTIKHLLKLNRISK
SQ  NYSSVIERIDLMNLTEESPHKCLEDKLSEISHSYVYKLTERGKYDKTLRQKRSLAGIHSRSTQLQTTKDIDQKMKKMLEK
SQ  EKNKYQQQIGERNTYAHLESHIDASPRSKKRKLPILLSTSHSSQFKTPLASRLNTSGSSTSPPLPSHLAMKFRKNSRVTS
SQ  LHTVLPVSTPSHSNNIPAASFSGNNTTDIQSQQLIENQKSTSVYLNNVSERILGNQEICQTPINPVTPVLDGADQGKEDI
SQ  PDSILELKILIDSVKKKVNND
//
ID  Q3TBT3;
PN  Stimulator of interferon genes protein;
GN  Sting1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19776740}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:29056340, ECO:0000269|PubMed:29496741}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: Q3TBT3;
DR  UNIPROT: A7YGY9;
DR  UNIPROT: Q3TAV5;
DR  UNIPROT: Q3TYP5;
DR  UNIPROT: Q3TZY8;
DR  UNIPROT: Q3UJW3;
DR  UNIPROT: Q8C227;
DR  UNIPROT: Q8C5Q3;
DR  UNIPROT: Q8K393;
DR  UNIPROT: Q9CZY7;
DR  PDB: 4JC5;
DR  PDB: 4KBY;
DR  PDB: 4KC0;
DR  PDB: 4LOJ;
DR  PDB: 4LOK;
DR  PDB: 4LOL;
DR  PDB: 4YP1;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:26229117, PubMed:26669264). Innate immune response is triggered in response to non-CpG double- stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:26229117, PubMed:26669264). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:21947006, PubMed:23722158, PubMed:23258412, PubMed:23519410, PubMed:23910378). Upon binding of c- di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:25636800). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30568238). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (PubMed:29056340). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'- cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (PubMed:18559423). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:18559423, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:21947006, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23519410, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:23910378, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:26669264, ECO:0000269|PubMed:29056340, ECO:0000269|PubMed:30568238}.
DE  Reference Proteome: Yes;
DE  Interaction: P52633; IntAct: EBI-3862093,EBI-647085; Score: 0.35
DE  Interaction: Q9WUN2; IntAct: EBI-3862093,EBI-764193; Score: 0.56
DE  Interaction: O54957; IntAct: EBI-6390034,EBI-3862093; Score: 0.35
DE  Interaction: Q3U1F9; IntAct: EBI-8468834,EBI-3862093; Score: 0.35
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0035438;
GO  GO:0061507;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0071407;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032608;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0051259;
GO  GO:0031323;
GO  GO:0010468;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q86WV6};
SQ  MPYSNLHPAIPRPRGHRSKYVALIFLVASLMILWVAKDPPNHTLKYLALHLASHELGLLLKNLCCLAEELCHVQSRYQGS
SQ  YWKAVRACLGCPIHCMAMILLSSYFYFLQNTADIYLSWMFGLLVLYKSLSMLLGLQSLTPAEVSAVCEEKKLNVAHGLAW
SQ  SYYIGYLRLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDNLSVVDPNIRFRDMLPQQNIDRAGIKNRVYS
SQ  NSVYEILENGQPAGVCILEYATPLQTLFAMSQDAKAGFSREDRLEQAKLFCRTLEEILEDVPESRNNCRLIVYQEPTDGN
SQ  SFSLSQEVLRHIRQEEKEEVTMNAPMTSVAPPPSVLSQEPRLLISGMDQPLPLRTDLI
//
ID  Q5U349;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  Usp2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O88623}. [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12107281}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000269|PubMed:12107281}. [Isoform 2]: Nucleus {ECO:0000269|PubMed:12107281}. Membrane {ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}. Note=Predominantly expressed at membranes. {ECO:0000250|UniProtKB:O88623}.
DR  UNIPROT: Q5U349;
DR  UNIPROT: Q9QXL3;
DR  UNIPROT: Q9QXL4;
DR  UNIPROT: Q9R083;
DR  UNIPROT: Q9R084;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (PubMed:12107281). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (PubMed:23213472). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (PubMed:23213472). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (PubMed:12107281). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:O88623, ECO:0000269|PubMed:10938131, ECO:0000269|PubMed:12107281, ECO:0000269|PubMed:23213472}. [Isoform 2]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000250|UniProtKB:O88623}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030332;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004843;
GO  GO:0031625;
GO  GO:0007049;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007517;
GO  GO:0051926;
GO  GO:0048642;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:0048643;
GO  GO:0016579;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSQLSSTLKRYTESSRYTDAPYAKSGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPL
SQ  LRSDITGGSKRSESQTRGNERPSGSGLNGGSGFPYGVTSNSLSYLPMNARDQGVTLGQKKSNSQSDLARDFSSLRTSDSY
SQ  RTSDGYRASDGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPSRVPEVLSPT
SQ  YRPSGRYTLWEKNKGQASGPSRSTSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHT
SQ  SSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVAARPKPSPESL
SQ  DHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDV
SQ  LDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVS
SQ  NHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
//
ID  P34561;
PN  Vacuolar protein sorting-associated protein 53 homolog;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. {ECO:0000269|PubMed:27191843}.
DR  UNIPROT: P34561;
DR  UNIPROT: E5QCF9;
DR  Pfam: PF04100;
DE  Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0000938;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:1904810;
GO  GO:1904811;
GO  GO:0090326;
GO  GO:0060378;
GO  GO:0042147;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEEPTTSELKLSDNVMNEISDMCITEYCKPNMSLMAQINELFPTEQSLTQLDSIIASVEGEIGELDNELAYLVETNANVS
SQ  ERGEEALKHAQDAMIELEKSIGSIRERTKSSDEIVREMTRDIKQLDIAKRNLTASITTLHHLHILLTGVESLGAWVDKKD
SQ  YSSIARQLPAILNVLQLFDAYKESDQIANLSGQLDKLKASLTIQLAKDLKNAFQTGQLSDRITDMCRVAAALEGNVKENF
SQ  VKWFIEQQLSEYVIIYADNEEGAWLDKVDDRYKWFVRKLTDFERAGLSNIFPADWHMGRRLTSEFCTVTRDILYRIMTRR
SQ  RQDLDWKLLGHAIQHTKMFEALLTKRFPEKDGISFEKAIWSVFDTFLDVFINAQEKTLNEFLDTCASKIRSGEEKPSRES
SQ  STHAVPFPSSADMFLLLKKVITESSKLSSEPDALIRDVIGVVRVCLRGYATSCLVAFLPSLGSQQSGAANLFSLIREEIA
SQ  YPRLTPDQQFLVCCILATADWCAETSIQLQEKLSQRIPGVDISQETEAFYSITNQSLQVLVQDVESTCDAALQSISKVNW
SQ  TAVDCVGDESPFIGSMRAHLRQAVPLIRDMLSDRRKYFAHFCLKLATQLAHKFVGSLFRCRTISTHGAEQLLLDTHSLKT
SQ  FLLSVPSIDSIINSKPPTAYVTSVNAALTKAEMILKVVMCSLETVDEFVEQYIKLLPASDAAEMQKVLEMKGVKRQEHSA
SQ  VLNAYRLKIGASGSDPIQQSNSLTSRIGGALPTVGSAASVSEAFNAVVSMAADGLSDQAVTSSIDKLKRFERLVKRQL
//
ID  Q9HCX4;
PN  Short transient receptor potential channel 7;
GN  TRPC7;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21402151}; Multi-pass membrane protein {ECO:0000269|PubMed:21402151}. Nucleus envelope {ECO:0000269|PubMed:21402151}.
DR  UNIPROT: Q9HCX4;
DR  UNIPROT: A1A4Z4;
DR  UNIPROT: F5H5U9;
DR  UNIPROT: Q70T26;
DR  UNIPROT: Q8IWP7;
DR  Pfam: PF12796;
DR  Pfam: PF00520;
DR  Pfam: PF08344;
DR  DisGeNET: 57113;
DE  Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G- protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P20591; IntAct: EBI-929476,EBI-929581; Score: 0.40
GO  GO:0034703;
GO  GO:0005623;
GO  GO:0005801;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0070679;
GO  GO:0015279;
GO  GO:0070588;
GO  GO:0006828;
GO  GO:0030168;
GO  GO:0051480;
GO  GO:0007338;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRNSTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQN
SQ  ALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILNHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTR
SQ  FSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVL
SQ  TALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNFQVWSDHHRPSLSRIKLAIKYEVK
SQ  KFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGRTLRSPFMKFVAHAVSFTIFLG
SQ  LLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLS
SQ  IFVASFTARFMAFLKATEAQLYVDQHVQDDTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILP
SQ  ANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKY
SQ  DHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYY
SQ  LIMRIKMCLIKLCKSKAKSCENDLEMGMLNSKFKKTRYQAGMRNSENLTANNTLSKPTRYQKIMKRLIKRYVLKAQVDRE
SQ  NDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNKGKDI
//
ID  Q9N2W5;
PN  UBX domain-containing protein 2;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Nucleus {ECO:0000269|PubMed:23649807}. Cytoplasm {ECO:0000269|PubMed:23649807}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23649807}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Nuclear localization is cdc-48-dependent (PubMed:23649807). During embryonic mitotic metaphase, telophase and to a certain extent prophase, localizes to centrosomes (PubMed:23649807). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:23649807}.
DR  UNIPROT: Q9N2W5;
DR  UNIPROT: Q86DD7;
DR  Pfam: PF08059;
DR  Pfam: PF00789;
DR  PROSITE: PS51399;
DR  PROSITE: PS50033;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1 (PubMed:20977550). Probably in association with ATPase cdc-48.1 or/and cdc-48.2, regulates the centrosomal levels of kinase air-1 levels during mitotic progression by promoting air-1 removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation in the one-cell embryo by controlling centration and rotation of the pronuclei-centrosome complex in prophase (PubMed:23649807). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:23649807}.
DE  Reference Proteome: Yes;
DE  Interaction: P54812; IntAct: EBI-320265,EBI-323237; Score: 0.49
DE  Interaction: O44739; IntAct: EBI-323237,EBI-323218; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031616;
GO  GO:0036435;
GO  GO:0019901;
GO  GO:0043130;
GO  GO:0000045;
GO  GO:0030154;
GO  GO:0000132;
GO  GO:0007030;
GO  GO:0042006;
GO  GO:0061025;
GO  GO:1904780;
GO  GO:0031468;
GO  GO:1903364;
GO  GO:0043161;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRNIRTFRDIGNNDDGGPDSDDSGADAAERGAPQEFYAGSGQAVQGPRGAAARGPDSEAHIRRILQAAEVVQPEGGEAP
SQ  RGRPSGRETISLTLHLWSDGLSIEDGPLMSRQDPRTIEFLESVGKGEIPPSLVQQYPGKEIDFKVNRHHEEYVAPKMKPF
SQ  GGSGVRLGNVVPTVLGQSSSSATTAGTSSATTDHNPDHTAENEAKQLEDAKKELSTNMNEPTTNIQIRLPNNQRLVGIFN
SQ  HSHTLEAVRTFICTARPDMIYAPFQMMAAYPPKPFEDESQTLKDANVLNSVVAVKILPTTN
//
ID  E9P860;
PN  NFX1-type zinc finger-containing protein 1 homolog;
GN  znfx;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}. Cytoplasm {ECO:0000269|PubMed:29775580}. Note=Co-localizes with wago-4 in P- granules in germline blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with wago-4 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to perinuclear and cytoplasmic P-granules in germline blastomeres and germ cells (PubMed:29775580, PubMed:29769721). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}.
DR  UNIPROT: E9P860;
DR  UNIPROT: Q23388;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DE  Function: Epigenetic inheritance factor which, in association with the Argonaute protein wago-4, mediates small RNA-directed transgenerational epigenetic inheritance and thus balances the transgenerational inheritance of epigenetic information (PubMed:29775580, PubMed:29769721). Specifically, maintains a balanced production of small RNAs by preventing the spread of epigenetic signals towards the 5'-end of target mRNAs (PubMed:29775580). Plays a role in small RNA- induced gene silencing in the germline (PubMed:29775580). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}.
DE  Reference Proteome: Yes;
GO  GO:0000775;
GO  GO:0031380;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0003700;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0008270;
GO  GO:0030702;
GO  GO:0031048;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFL
SQ  QYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYE
SQ  ELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPG
SQ  LPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENS
SQ  SSSRRRFRDEEVQEEEGDHILSSEDVHAARNVCETKILVRGVPQKNDSELSKLINGSKLYVRFERPFVKLAHNLELLYVV
SQ  NYAISSRKSIVRDHSKAIIRGLFEKDFLLKLKSKFLESSFDNDTWTPEGTELLFEIFHLFFTTARYKGGFMLTLPRFAPS
SQ  WHDFSMAFDIADMDGLEEAGVGDDELRNLRRLIGYIETWIKRAERERNPSPLALRSYSVYEKAGSSDSGRQVLSESRGAG
SQ  SSNVYGHDEVDFVDHRRRDEFGHRDNYRTENRRHKSPDNFGEVHRRLDEQQQQRHEDESSRYRDDSRQSRRADDRRDQYQ
SQ  YNESTSMENHLGFHNGGGTVSEHSRDDKFVSPQNCEEKRKYCEEDTDAKPQQPYRFEEIKFEPIWVKCEKSEPPEDFKTL
SQ  PSVPVLSEYVNPVEPYLRRIQDDGKYKSVHHYLDVQFRLLKEDLVSPLRDGIDLYKKNGTCKGRRIEGAPCSDISIFNVE
SQ  KVDGKQVTERDGYEMRIIWPAQYDILKLLDNDREMKELGLVMLSCDRFKEDFHLGHIQSSYLMRNGSLHFAVHEETSPFK
SQ  PNTTYQMAQGTSYLPCYKHVLENLKRISSFKPLPFERYLVHGSKIIFRPNFQQAEKSEYQISEEKKLMKTYNELRSLAAC
SQ  ARYTKGKPIPRGVDDDDEDYEFSKSRELSKEDIDLEYRQLQEPIFRPLVGVDIKDSNLIQINKKWYNVSRLLDEFHPDYM
SQ  DESQRLAFCNTFKYELSLIQGPPGTGKTHIGVQIVKTILQNRSYWKITEPILVVCFTNSGLDNLLERIYQMIENDEELSK
SQ  DNGRPKIIRFGSKCDSNYLKRQNVMRQDVYEQYKSKVSDGAQKKMSKAGAARRHKADNLAISSYTLFCSRNKLLSYEMLS
SQ  RVMDPNHQMEIQQFTYDHVDTKGIPLSPDEAIGCWLLERDFGKATKSQTKKAKKPKFQGAQLDSEDENKDYFTVEDSDDE
SQ  EDELDDEKLLDKLFEKMNLECSGADILSAVHASHADEYYTKGPWEIVQDKRPSVVVLMEKKTKPCNAKFTVDEQINNLVS
SQ  EIKDMILSSQPVPKKDLNDIKYIFSLARLKRWSLYITWCDALRSIVTENLPRQIREYREACENFKNAQNRVDAEIMRMTM
SQ  IIGATTTGCSRLRPTLEKVGPRILIVEEAAEVLEAHIISAMISTVEHVVMIGDHKQLRPNPAVHELGVAYGLRISMFERL
SQ  VERGLPFSQLRQQHRMNLTISDKIVKLSFYDNVTDAENVGLYPDVQGMATNLFFWSHTSMEESPDEVSWLNKHEISMTVA
SQ  LVKHLLKQNYTTNDIVVLATYSAQKNLMYREYANVFGSTPDSNVIPVETVDSFQGKERKIVIVSLVRSHRGGRENTGIGF
SQ  LAVANRICVALTRAQHGMYIIGNGAYIMNNSELWNKIVNNLRRSNLIEYNLPLKCVAHGNIVTVKDPQDFATKSPEGGCM
SQ  QKCDTKKFCGHVCERLCHPNMEEEHLQRCLYNCDKKCSNPQFQHRCKKACYEECGSCLYLVEVTLDCGHRITTPCSRINS
SQ  SKCDQSCTKKLLCGHACAAKCGEECTLVSECSQLVGMPLSCGHIKQLTCSKISANEIDLTCDQRCEKTMLACPHKCAEIC
SQ  GQPCTVECMEVVNVTLGCSHSQDVVCSSFMPGMTDHIECLTKVPKTLSPCKHTELVLCKQAPSTKLCTRRCTSYLEKCGH
SQ  TCENDCGICFTTKTHICQNMCQKVLNCGHTCSAKCGESCPPCKAFCTNKCEHQSCGAGERGFGRDCSKLCALCVNNCSNK
SQ  CAHRSCTLKCFEECNVKPCTEPCTDKLKCGHACLGICGEQCPKICGTCERNKYIECVSGTSSTSRVHRLIMIPKCYHVFP
SQ  VEVLDDHVKKQKEANEKLKCPKCSAFIVGVLRYARYTKKYYLNENMRKLESNIRNIHQSTLEGRVFQAVQDSIGEIRNVT
SQ  TNLTNASEDILRNFHQKILDIRTSAETFKGKPEHKFKFASLLQVANCCLAITRLLSVSSKFRVSRRKDIPPTFDLMSVRV
SQ  LGDMPFPKLIDELNRVNIHLSNTYETFMPGAIIPKLKWLISRMTVLQQLTSMCHQLVLEKKDIADSDAHAINDACLNMFR
SQ  YNEQHNYALNIENFEAIVVKVAPKLLEPTPKFWSWRRLQVPEL
//
ID  Q95017;
PN  SUMO-conjugating enzyme UBC9;
GN  ubc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25475837}.
DR  UNIPROT: Q95017;
DR  UNIPROT: Q9GYI5;
DR  Pfam: PF00179;
DR  PROSITE: PS00183;
DR  PROSITE: PS50127;
DE  Function: Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1 and the Polycomb protein sop-2. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. {ECO:0000269|PubMed:11806825, ECO:0000269|PubMed:14711411, ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:15689373, ECO:0000269|PubMed:15990876, ECO:0000269|PubMed:16701625}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-328938,EBI-328938; Score: 0.55
DE  Interaction: Q94420; IntAct: EBI-320790,EBI-328938; Score: 0.37
DE  Interaction: Q9NA84; IntAct: EBI-328127,EBI-328938; Score: 0.49
DE  Interaction: P55853; IntAct: EBI-328938,EBI-313647; Score: 0.71
DE  Interaction: Q21747; IntAct: EBI-324374,EBI-328938; Score: 0.49
DE  Interaction: Q94361; IntAct: EBI-323258,EBI-328938; Score: 0.49
DE  Interaction: G5EF84; IntAct: EBI-2003997,EBI-328938; Score: 0.49
DE  Interaction: Q21209; IntAct: EBI-328938,EBI-3895480; Score: 0.51
DE  Interaction: Q95Q25; IntAct: EBI-328938,EBI-321895; Score: 0.67
DE  Interaction: P34342-1; IntAct: EBI-328938,EBI-6456879; Score: 0.37
DE  Interaction: Q23158; IntAct: EBI-328938,EBI-314014; Score: 0.37
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0001085;
GO  GO:0032093;
GO  GO:0061656;
GO  GO:0019789;
GO  GO:0009952;
GO  GO:0009792;
GO  GO:0000122;
GO  GO:0002119;
GO  GO:0043282;
GO  GO:0016925;
GO  GO:1903827;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGIAAGRLAEERKHWRKDHPFGFIAKPVKNADGTLNLFNWECAIPGRKDTIWEGGLYRIRMLFKDDFPSTPPKCKFEPP
SQ  LFHPNVYPSGTVCLSLLDENKDWKPSISIKQLLIGIQDLLNHPNIEDPAQAEAYQIYCQNRAEYEKRVKKEAVKYAAELV
SQ  QKQMLE
//
ID  Q9UL33;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  TRAPPC2L;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19416478}. Endoplasmic reticulum {ECO:0000269|PubMed:19416478}. Golgi apparatus {ECO:0000269|PubMed:19416478}.
DR  UNIPROT: Q9UL33;
DR  UNIPROT: B2R4M9;
DR  UNIPROT: Q6ZTA7;
DR  UNIPROT: Q9NZZ4;
DR  Pfam: PF04628;
DR  OMIM: 610970;
DR  OMIM: 618331;
DR  DisGeNET: 51693;
DE  Function: Plays a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:19416478, ECO:0000269|PubMed:30120216}.
DE  Disease: Encephalopathy, progressive, early-onset, with episodic rhabdomyolysis (PEERB) [MIM:618331]: An autosomal recessive disease characterized by progressive encephalopathy exacerbated by febrile illness and associated with severe neurodevelopmental delay, episodes of rhabdomyolysis, developmental regression, epilepsy and tetraplegia. {ECO:0000269|PubMed:30120216}. Note=The disease may be caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P09613; IntAct: EBI-21497244,EBI-747601; Score: 0.35
DE  Interaction: O43617; IntAct: EBI-747601,EBI-743566; Score: 0.84
DE  Interaction: Q96D71-2; IntAct: EBI-10284498,EBI-747601; Score: 0.56
DE  Interaction: Q96D71-3; IntAct: EBI-10284512,EBI-747601; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-307352,EBI-747601; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-747601,EBI-533224; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-742327,EBI-747601; Score: 0.56
DE  Interaction: Q8IYX8-2; IntAct: EBI-747601,EBI-10181988; Score: 0.56
DE  Interaction: Q9H2G9; IntAct: EBI-2548012,EBI-747601; Score: 0.56
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-747601; Score: 0.35
DE  Interaction: P48553; IntAct: EBI-6160572,EBI-747601; Score: 0.27
DE  Interaction: Q96QF0; IntAct: EBI-747844,EBI-747601; Score: 0.64
DE  Interaction: Q9Y2L5; IntAct: EBI-2820056,EBI-747601; Score: 0.40
DE  Interaction: A5PLN9; IntAct: EBI-2857298,EBI-747601; Score: 0.40
DE  Interaction: Q9NR12; IntAct: EBI-350517,EBI-747601; Score: 0.27
DE  Interaction: Q8IYB1; IntAct: EBI-11323212,EBI-747601; Score: 0.27
DE  Interaction: Q9Y5R8; IntAct: EBI-747601,EBI-6160554; Score: 0.27
DE  Interaction: Q9Y296; IntAct: EBI-747601,EBI-722888; Score: 0.27
DE  Interaction: Q96Q05; IntAct: EBI-747601,EBI-6160596; Score: 0.27
DE  Interaction: Q8TBN0; IntAct: EBI-747601,EBI-743796; Score: 0.27
DE  Interaction: Q8N9M5; IntAct: EBI-747601,EBI-1050459; Score: 0.27
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0048208;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSSRAFDNMVTSMMIQVC
//
ID  Q8VZG7;
PN  Ribonuclease TUDOR 1;
GN  TSN1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasmic granule {ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20484005}. Endoplasmic reticulum {ECO:0000269|PubMed:20484005}. Note=Accumulates heterogeneously in the cytosol, in patches around the nucleus and in the cell periphery, and relocates transiently to a diffuse pattern in response to salt stress (PubMed:20484005). Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25205572, PubMed:25736060). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}.
DR  UNIPROT: Q8VZG7;
DR  UNIPROT: F4K6N0;
DR  UNIPROT: Q9LY25;
DR  Pfam: PF00565;
DR  Pfam: PF00567;
DR  PROSITE: PS50830;
DR  PROSITE: PS50304;
DE  Function: Cytoprotective ribonuclease (RNase) required for resistance to abiotic stresses, acting as a positive regulator of mRNA decapping during stress (PubMed:25736060). Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat) (PubMed:25736060). Involved in gibberellic acid (GA) biosynthesis (PubMed:25205572). Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway (PubMed:20484005). Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA (PubMed:25205572). May inhibit the degradation of mRNAs involved in stress adaptation (PubMed:26237081). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060, ECO:0000269|PubMed:26237081}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LV27; IntAct: EBI-4453099,EBI-21137483; Score: 0.35
GO  GO:0005618;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016442;
GO  GO:0003729;
GO  GO:0004518;
GO  GO:0003723;
GO  GO:0034605;
GO  GO:0031047;
GO  GO:0006402;
GO  GO:0006397;
GO  GO:0010372;
GO  GO:0046686;
GO  GO:0009651;
GO  GO:0006401;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATGAENQWLKGRVKAVTSGDCLVITALSHNRAGPPPEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAF
SQ  KVDYKVEAIAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNQDKVSPYIKELLQLEELAKQEGYGRWSKVPGAAEASI
SQ  RNLPPSAIGDSAGFDAMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGVQAPSMGRRTTNGSVVETVPDE
SQ  PNGDVSAESRGPLTTAQRLAASAASSVEVSSDPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGETVKDLG
SQ  LELVENGLAKFVEWSANMMEEEAKKKLKAAELQCKKDKVKMWANYVPPATNSKAIHDQNFTGKVVEVVSGDCLIVADDAV
SQ  PFGSPAAERRVCLSSIRSPKMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKVTQGDGPTTSGAADRFMDFGS
SQ  VFLPSAAKADSDEVTAPPAAAIAGSQPVGVNIAELVLVRGFGNVVRHRDFEERSNHYDALLAAEARALAGKKGIHSAKES
SQ  PAMHITDLTVSAAKKAKDFLPSLQRIRRIPAVVEYVLSGHRFKLYIPKITCSIAFSFSGVRCPGRGEPYSEEAISVMRRR
SQ  IMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEQAERSAKNQKLKIWENYVEGEE
SQ  VSNGNTNTVETRQKETLKVVVTEVLGGGRFYVQSAGDQKIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWN
SQ  RAMIVTAPRAAVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVPSLEDDFGPEAGEYLHTVT
SQ  LGSGKEFKAVIEERDTSGGKVKGQGTGTEFVVTLIAVDDEISVNAAMLQEGIARMEKRQKWGHKGKQAALDALEKFQEEA
SQ  RKSRIGIWQYGDIESDDEDTGPARKPAGGRR
//
ID  Q94218;
PN  Ufm1-specific protease;
GN  odr;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23449979, ECO:0000269|PubMed:24603482}; Peripheral membrane protein {ECO:0000269|PubMed:24603482}. Cytoplasm {ECO:0000269|PubMed:24603482}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23449979}. Note=Recruited to the endoplasmic reticulum upon interaction with odr-4. {ECO:0000269|PubMed:24603482}.
DR  UNIPROT: Q94218;
DR  UNIPROT: Q86MF8;
DR  PDB: 5EJJ;
DR  PDB: 5XDA;
DR  Pfam: PF07910;
DE  Function: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins (By similarity). Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC. Operates in aggregation behavior, and responses to oxygen levels. {ECO:0000250|UniProtKB:Q9NUQ7, ECO:0000269|PubMed:12410303, ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:9590179}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0008234;
GO  GO:0006935;
GO  GO:0050921;
GO  GO:0097499;
GO  GO:0045471;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:24603482};
SQ  MTNSQTVSLIGPTQMAPQSTPPPPVNELWFIDAQAMFQNYANLRSFSKSNANEINTTIGGFVFGRKARKQVIHVLFAYAE
SQ  DLTESNRQFLESSLSADIELVGNLNIDGQSQILPGGQFTLQLTSRMLENRSISEFLDMNVMFNNEHVLMEGASCVSRVGY
SQ  EWSLRAGREQEDVKSAAERLSMASFRFTYLNAEHGLVIREQKPEAAQQKYLDKFSKGAVPYKDVIEFTAMQSLTRDTSND
SQ  TEDQKLVPTVKVTKDNKHFTRLVTIGEVVFPAFFGDSSLDLYKRSREAFNRRANNTMMVTVNGIRAGRGVTTTTSATYLP
SQ  PGWVSLLHLQLPTKWTDNEQRNYRIRLHKLFNLPSSKPVLRLSQALALHSESARLTNKKLIREPHLSITNYQPVGEITTV
SQ  NGPYNYHHYMQDGIDDSGWGCAYRSFQTIWSWFILNGYTDKPVPSHREIQQALVDIQDKQAKFVGSRQWIGSTEISFVLN
SQ  ELLKLECRFIATNSGAEVVERVRELARHFETSGTPVMIGGNMLAHTILGVDFNDTTGETKFLVLDPHYTGSEDIKTITSK
SQ  GWCAWKPASFWSKDHFYNMVLPQPPSDAI
//
ID  P30822;
PN  Exportin-1;
GN  CRM1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14562095}. Note=Localized in the nucleus and at its periphery.
DR  UNIPROT: P30822;
DR  UNIPROT: D6VV01;
DR  PDB: 3M1I;
DR  PDB: 3VYC;
DR  PDB: 3WYF;
DR  PDB: 3WYG;
DR  PDB: 4GMX;
DR  PDB: 4GPT;
DR  PDB: 4HAT;
DR  PDB: 4HAU;
DR  PDB: 4HAV;
DR  PDB: 4HAW;
DR  PDB: 4HAX;
DR  PDB: 4HAY;
DR  PDB: 4HAZ;
DR  PDB: 4HB0;
DR  PDB: 4HB2;
DR  PDB: 4HB3;
DR  PDB: 4HB4;
DR  PDB: 5DH9;
DR  PDB: 5DHA;
DR  PDB: 5DHF;
DR  PDB: 5DI9;
DR  PDB: 5DIF;
DR  PDB: 5JLJ;
DR  PDB: 5UWH;
DR  PDB: 5UWI;
DR  PDB: 5UWJ;
DR  PDB: 5UWO;
DR  PDB: 5UWP;
DR  PDB: 5UWQ;
DR  PDB: 5UWR;
DR  PDB: 5UWS;
DR  PDB: 5UWT;
DR  PDB: 5UWU;
DR  PDB: 5UWW;
DR  PDB: 5XOJ;
DR  PDB: 5YRO;
DR  PDB: 5YST;
DR  PDB: 5YSU;
DR  PDB: 5YTB;
DR  PDB: 5ZPU;
DR  PDB: 6A38;
DR  PDB: 6A3A;
DR  PDB: 6A3B;
DR  PDB: 6A3C;
DR  PDB: 6A3E;
DR  PDB: 6CIT;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES).
DE  Reference Proteome: Yes;
DE  Interaction: P06782; IntAct: EBI-20589,EBI-17516; Score: 0.35
DE  Interaction: P12683; IntAct: EBI-8377,EBI-20589; Score: 0.35
DE  Interaction: P12684; IntAct: EBI-8384,EBI-20589; Score: 0.35
DE  Interaction: P14906; IntAct: EBI-16636,EBI-20589; Score: 0.35
DE  Interaction: P20484; IntAct: EBI-20589,EBI-10930; Score: 0.35
DE  Interaction: P22147; IntAct: EBI-20589,EBI-9642; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-10420,EBI-20589; Score: 0.35
DE  Interaction: Q02630; IntAct: EBI-11703,EBI-20589; Score: 0.37
DE  Interaction: P39523; IntAct: EBI-27256,EBI-20589; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-20589,EBI-8603; Score: 0.53
DE  Interaction: Q12329; IntAct: EBI-20589,EBI-8571; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-20589,EBI-8632; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-8627,EBI-20589; Score: 0.64
DE  Interaction: P39079; IntAct: EBI-20589,EBI-19077; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-19049,EBI-20589; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-20589,EBI-8680; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-20589; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-20589; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-11178,EBI-20589; Score: 0.35
DE  Interaction: P32364; IntAct: EBI-20589,EBI-17497; Score: 0.35
DE  Interaction: P40078; IntAct: EBI-20589,EBI-22681; Score: 0.35
DE  Interaction: P14127; IntAct: EBI-20589,EBI-14531; Score: 0.35
DE  Interaction: P38284; IntAct: EBI-20589,EBI-20849; Score: 0.35
DE  Interaction: Q99207; IntAct: EBI-20589,EBI-35157; Score: 0.35
DE  Interaction: P53863; IntAct: EBI-20589,EBI-29183; Score: 0.35
DE  Interaction: P38806; IntAct: EBI-20589,EBI-24622; Score: 0.35
DE  Interaction: P38243; IntAct: EBI-20589,EBI-3698417; Score: 0.35
DE  Interaction: P53107; IntAct: EBI-20589,EBI-24056; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-20589,EBI-18146; Score: 0.35
DE  Interaction: Q01855; IntAct: EBI-20589,EBI-16058; Score: 0.35
DE  Interaction: Q04660; IntAct: EBI-20589,EBI-28098; Score: 0.35
DE  Interaction: P40010; IntAct: EBI-20589,EBI-22449; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-20589,EBI-340; Score: 0.35
DE  Interaction: P47017; IntAct: EBI-20589,EBI-174; Score: 0.35
DE  Interaction: P53550; IntAct: EBI-20589,EBI-270; Score: 0.35
DE  Interaction: P47149; IntAct: EBI-20589,EBI-12098; Score: 0.35
DE  Interaction: P47035; IntAct: EBI-20589,EBI-25953; Score: 0.35
DE  Interaction: P05755; IntAct: EBI-20589,EBI-16181; Score: 0.35
DE  Interaction: P34078; IntAct: EBI-20589,EBI-10248; Score: 0.35
DE  Interaction: P30771; IntAct: EBI-20589,EBI-11831; Score: 0.35
DE  Interaction: P25379; IntAct: EBI-20589,EBI-3804607; Score: 0.35
DE  Interaction: P40348; IntAct: EBI-20589,EBI-14992; Score: 0.35
DE  Interaction: P53935; IntAct: EBI-20589,EBI-28788; Score: 0.35
DE  Interaction: Q06631; IntAct: EBI-20589,EBI-36432; Score: 0.35
DE  Interaction: P21192; IntAct: EBI-20589,EBI-2073; Score: 0.59
DE  Interaction: P38987; IntAct: EBI-20589,EBI-19113; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-20589,EBI-15394; Score: 0.35
DE  Interaction: P32578; IntAct: EBI-20589,EBI-17179; Score: 0.35
DE  Interaction: P24276; IntAct: EBI-20589,EBI-18153; Score: 0.35
DE  Interaction: P48361; IntAct: EBI-20589,EBI-2993; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-20589,EBI-3824; Score: 0.35
DE  Interaction: P37262; IntAct: EBI-20589,EBI-17680; Score: 0.35
DE  Interaction: P25368; IntAct: EBI-20589,EBI-16019; Score: 0.35
DE  Interaction: P28004; IntAct: EBI-20589,EBI-20640; Score: 0.35
DE  Interaction: Q92331; IntAct: EBI-20589,EBI-20483; Score: 0.35
DE  Interaction: P36080; IntAct: EBI-20589,EBI-26762; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-20589,EBI-15398; Score: 0.35
DE  Interaction: Q12199; IntAct: EBI-20589,EBI-38123; Score: 0.35
DE  Interaction: P36104; IntAct: EBI-20589,EBI-26608; Score: 0.35
DE  Interaction: O13329; IntAct: EBI-20589,EBI-7040; Score: 0.35
DE  Interaction: P47083; IntAct: EBI-20589,EBI-11168; Score: 0.35
DE  Interaction: P23202; IntAct: EBI-20589,EBI-20138; Score: 0.35
DE  Interaction: P21339; IntAct: EBI-20589,EBI-11322; Score: 0.35
DE  Interaction: Q03063; IntAct: EBI-20589,EBI-29752; Score: 0.35
DE  Interaction: P09032; IntAct: EBI-20589,EBI-6275; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-20589,EBI-6270; Score: 0.35
DE  Interaction: P53830; IntAct: EBI-20589,EBI-28299; Score: 0.35
DE  Interaction: P40523; IntAct: EBI-20589,EBI-25031; Score: 0.35
DE  Interaction: P38254; IntAct: EBI-20589,EBI-21533; Score: 0.35
DE  Interaction: P36041; IntAct: EBI-20589,EBI-26995; Score: 0.35
DE  Interaction: P38835; IntAct: EBI-20589,EBI-24724; Score: 0.35
DE  Interaction: P27515; IntAct: EBI-20589,EBI-20151; Score: 0.35
DE  Interaction: P43639; IntAct: EBI-20589,EBI-9563; Score: 0.35
DE  Interaction: Q01080; IntAct: EBI-20589,EBI-15741; Score: 0.35
DE  Interaction: Q12532; IntAct: EBI-20589,EBI-33283; Score: 0.35
DE  Interaction: P53104; IntAct: EBI-20589,EBI-2657; Score: 0.35
DE  Interaction: P38856; IntAct: EBI-20589,EBI-24811; Score: 0.35
DE  Interaction: P26784; IntAct: EBI-20589,EBI-14508; Score: 0.35
DE  Interaction: Q03768; IntAct: EBI-20589,EBI-7618; Score: 0.35
DE  Interaction: P40054; IntAct: EBI-20589,EBI-16961; Score: 0.35
DE  Interaction: P40214; IntAct: EBI-20589,EBI-27290; Score: 0.35
DE  Interaction: P19880; IntAct: EBI-20589,EBI-31265; Score: 0.35
DE  Interaction: P32608; IntAct: EBI-20589,EBI-16322; Score: 0.35
DE  Interaction: P25333; IntAct: EBI-20589,EBI-16492; Score: 0.35
DE  Interaction: P08518; IntAct: EBI-20589,EBI-15767; Score: 0.35
DE  Interaction: Q08909; IntAct: EBI-20589,EBI-36654; Score: 0.35
DE  Interaction: P36000; IntAct: EBI-20589,EBI-2206; Score: 0.35
DE  Interaction: Q04740; IntAct: EBI-20589,EBI-15658; Score: 0.35
DE  Interaction: P20604; IntAct: EBI-20589,EBI-13707; Score: 0.35
DE  Interaction: Q07953; IntAct: EBI-20589,EBI-27124; Score: 0.35
DE  Interaction: P40531; IntAct: EBI-20589,EBI-25006; Score: 0.35
DE  Interaction: P25502; IntAct: EBI-20589,EBI-14307; Score: 0.35
DE  Interaction: Q12100; IntAct: EBI-20589,EBI-36072; Score: 0.35
DE  Interaction: P25344; IntAct: EBI-20589,EBI-18305; Score: 0.35
DE  Interaction: Q12453; IntAct: EBI-20589,EBI-31271; Score: 0.35
DE  Interaction: P05453; IntAct: EBI-20589,EBI-6540; Score: 0.35
DE  Interaction: P26570; IntAct: EBI-20589,EBI-13807; Score: 0.35
DE  Interaction: P38970; IntAct: EBI-20589,EBI-8142; Score: 0.35
DE  Interaction: P18899; IntAct: EBI-20589,EBI-6165; Score: 0.35
DE  Interaction: P53297; IntAct: EBI-20589,EBI-12961; Score: 0.35
DE  Interaction: P24309; IntAct: EBI-20589,EBI-5648; Score: 0.35
DE  Interaction: P07266; IntAct: EBI-20589,EBI-11278; Score: 0.35
DE  Interaction: P37263; IntAct: EBI-20589,EBI-21659; Score: 0.35
DE  Interaction: P53836; IntAct: EBI-20589,EBI-28275; Score: 0.35
DE  Interaction: P0CX52; IntAct: EBI-20589,EBI-5234556; Score: 0.35
DE  Interaction: P34761; IntAct: EBI-20589,EBI-20537; Score: 0.35
DE  Interaction: P35193; IntAct: EBI-20589,EBI-29291; Score: 0.35
DE  Interaction: Q05672; IntAct: EBI-20589,EBI-36115; Score: 0.35
DE  Interaction: Q12527; IntAct: EBI-20589,EBI-31977; Score: 0.35
DE  Interaction: Q12221; IntAct: EBI-20589,EBI-37840; Score: 0.35
DE  Interaction: P53309; IntAct: EBI-20589,EBI-23557; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-20589,EBI-724; Score: 0.35
DE  Interaction: Q03373; IntAct: EBI-20589,EBI-34019; Score: 0.35
DE  Interaction: Q04429; IntAct: EBI-20589,EBI-37461; Score: 0.35
DE  Interaction: Q04226; IntAct: EBI-20589,EBI-18884; Score: 0.35
DE  Interaction: Q03833; IntAct: EBI-20589,EBI-35786; Score: 0.35
DE  Interaction: P38070; IntAct: EBI-20589,EBI-9524; Score: 0.35
DE  Interaction: P32481; IntAct: EBI-20589,EBI-8924; Score: 0.35
DE  Interaction: P26786; IntAct: EBI-20589,EBI-16161; Score: 0.35
DE  Interaction: P53686; IntAct: EBI-20589,EBI-2070504; Score: 0.35
DE  Interaction: P32494; IntAct: EBI-20589,EBI-2192; Score: 0.35
DE  Interaction: Q06511; IntAct: EBI-20589,EBI-34602; Score: 0.35
DE  Interaction: P22517; IntAct: EBI-20589,EBI-9600; Score: 0.35
DE  Interaction: P40466; IntAct: EBI-20589,EBI-6965; Score: 0.35
DE  Interaction: Q3E7Y3; IntAct: EBI-20589,EBI-783138; Score: 0.35
DE  Interaction: Q06512; IntAct: EBI-20589,EBI-36459; Score: 0.35
DE  Interaction: P40992; IntAct: EBI-20589,EBI-15990; Score: 0.35
DE  Interaction: P32491; IntAct: EBI-20589,EBI-10973; Score: 0.35
DE  Interaction: P40210; IntAct: EBI-20589,EBI-27280; Score: 0.35
DE  Interaction: P36123; IntAct: EBI-20589,EBI-16392; Score: 0.35
DE  Interaction: Q00776; IntAct: EBI-20589,EBI-2624; Score: 0.35
DE  Interaction: P53040; IntAct: EBI-20589,EBI-18876; Score: 0.35
DE  Interaction: Q02931; IntAct: EBI-20589,EBI-37773; Score: 0.35
DE  Interaction: P40160; IntAct: EBI-20589,EBI-29124; Score: 0.35
DE  Interaction: P47049; IntAct: EBI-20589,EBI-25866; Score: 0.35
DE  Interaction: P40357; IntAct: EBI-20589,EBI-16904; Score: 0.35
DE  Interaction: P38333; IntAct: EBI-20589,EBI-6482; Score: 0.35
DE  Interaction: P38961; IntAct: EBI-20589,EBI-22139; Score: 0.35
DE  Interaction: P38861; IntAct: EBI-20589,EBI-12077; Score: 0.35
DE  Interaction: P53972; IntAct: EBI-20589,EBI-2883451; Score: 0.35
DE  Interaction: P53289; IntAct: EBI-20589,EBI-23393; Score: 0.35
DE  Interaction: Q02197; IntAct: EBI-20589,EBI-10924; Score: 0.35
DE  Interaction: P47019; IntAct: EBI-20589,EBI-26061; Score: 0.35
DE  Interaction: P10664; IntAct: EBI-20589,EBI-15390; Score: 0.35
DE  Interaction: Q07622; IntAct: EBI-20589,EBI-38674; Score: 0.35
DE  Interaction: P40356; IntAct: EBI-20589,EBI-13268; Score: 0.35
DE  Interaction: P53865; IntAct: EBI-20589,EBI-29172; Score: 0.35
DE  Interaction: P53930; IntAct: EBI-20589,EBI-28841; Score: 0.35
DE  Interaction: P35181; IntAct: EBI-20589,EBI-2612; Score: 0.35
DE  Interaction: P38011; IntAct: EBI-20589,EBI-7405; Score: 0.35
DE  Interaction: P53237; IntAct: EBI-20589,EBI-23176; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-20589,EBI-23061; Score: 0.35
DE  Interaction: P20424; IntAct: EBI-20589,EBI-17997; Score: 0.35
DE  Interaction: Q08972; IntAct: EBI-20589,EBI-32014; Score: 0.35
DE  Interaction: P32524; IntAct: EBI-20589,EBI-603; Score: 0.35
DE  Interaction: P29453; IntAct: EBI-20589,EBI-15435; Score: 0.35
DE  Interaction: P48164; IntAct: EBI-20589,EBI-16166; Score: 0.35
DE  Interaction: P47129; IntAct: EBI-20589,EBI-25556; Score: 0.35
DE  Interaction: P06634; IntAct: EBI-20589,EBI-5744; Score: 0.35
DE  Interaction: P32793; IntAct: EBI-20589,EBI-24460; Score: 0.55
DE  Interaction: Q05775; IntAct: EBI-20589,EBI-8944; Score: 0.35
DE  Interaction: Q04839; IntAct: EBI-20589,EBI-27549; Score: 0.35
DE  Interaction: Q05518; IntAct: EBI-20589,EBI-33452; Score: 0.35
DE  Interaction: Q04199; IntAct: EBI-20589,EBI-3920; Score: 0.35
DE  Interaction: Q06412; IntAct: EBI-20589,EBI-37117; Score: 0.35
DE  Interaction: Q03900; IntAct: EBI-20589,EBI-38156; Score: 0.35
DE  Interaction: P39939; IntAct: EBI-20589,EBI-14584; Score: 0.35
DE  Interaction: P39927; IntAct: EBI-20589,EBI-23382; Score: 0.35
DE  Interaction: P42944; IntAct: EBI-20589,EBI-8042; Score: 0.35
DE  Interaction: P38809; IntAct: EBI-20589,EBI-24634; Score: 0.35
DE  Interaction: P39985; IntAct: EBI-20589,EBI-6120; Score: 0.35
DE  Interaction: P20459; IntAct: EBI-20589,EBI-8915; Score: 0.35
DE  Interaction: Q04305; IntAct: EBI-20589,EBI-28183; Score: 0.35
DE  Interaction: Q08687; IntAct: EBI-20589,EBI-34720; Score: 0.35
DE  Interaction: P27999; IntAct: EBI-20589,EBI-15798; Score: 0.35
DE  Interaction: Q12102; IntAct: EBI-20589,EBI-31412; Score: 0.35
DE  Interaction: P38882; IntAct: EBI-20589,EBI-24892; Score: 0.35
DE  Interaction: P32913; IntAct: EBI-20589,EBI-20366; Score: 0.35
DE  Interaction: Q06834; IntAct: EBI-20589,EBI-33224; Score: 0.35
DE  Interaction: P38177; IntAct: EBI-20589,EBI-21323; Score: 0.35
DE  Interaction: P32914; IntAct: EBI-20589,EBI-17928; Score: 0.35
DE  Interaction: Q02796; IntAct: EBI-20589,EBI-30514; Score: 0.35
DE  Interaction: P53272; IntAct: EBI-20589,EBI-23284; Score: 0.35
DE  Interaction: P53091; IntAct: EBI-20589,EBI-10556; Score: 0.35
DE  Interaction: P34758; IntAct: EBI-20589,EBI-16685; Score: 0.35
DE  Interaction: Q12432; IntAct: EBI-20589,EBI-6281; Score: 0.35
DE  Interaction: P33322; IntAct: EBI-20589,EBI-4105; Score: 0.35
DE  Interaction: P43615; IntAct: EBI-20589,EBI-23028; Score: 0.35
DE  Interaction: P47160; IntAct: EBI-20589,EBI-25662; Score: 0.35
DE  Interaction: P38874; IntAct: EBI-20589,EBI-9061; Score: 0.35
DE  Interaction: Q06410; IntAct: EBI-20589,EBI-30856; Score: 0.35
DE  Interaction: P38817; IntAct: EBI-20589,EBI-7569; Score: 0.35
DE  Interaction: P53136; IntAct: EBI-20589,EBI-23920; Score: 0.35
DE  Interaction: P38789; IntAct: EBI-20589,EBI-18160; Score: 0.35
DE  Interaction: P32328; IntAct: EBI-20589,EBI-5588; Score: 0.35
DE  Interaction: P48415; IntAct: EBI-20589,EBI-16551; Score: 0.35
DE  Interaction: P39108; IntAct: EBI-20589,EBI-13183; Score: 0.35
DE  Interaction: P38282; IntAct: EBI-20589,EBI-443; Score: 0.35
DE  Interaction: P32605; IntAct: EBI-20589,EBI-680; Score: 0.35
DE  Interaction: P53094; IntAct: EBI-20589,EBI-10651; Score: 0.35
DE  Interaction: P38687; IntAct: EBI-20589,EBI-18004; Score: 0.35
DE  Interaction: P25343; IntAct: EBI-20589,EBI-14490; Score: 0.35
DE  Interaction: Q02948; IntAct: EBI-20589,EBI-2670; Score: 0.35
DE  Interaction: Q04868; IntAct: EBI-20589,EBI-27653; Score: 0.35
DE  Interaction: Q12271; IntAct: EBI-20589,EBI-36688; Score: 0.35
DE  Interaction: P15646; IntAct: EBI-20589,EBI-6838; Score: 0.35
DE  Interaction: P38747; IntAct: EBI-20589,EBI-3652313; Score: 0.35
DE  Interaction: P38630; IntAct: EBI-20589,EBI-14985; Score: 0.35
DE  Interaction: P39517; IntAct: EBI-20589,EBI-158; Score: 0.35
DE  Interaction: P05740; IntAct: EBI-20589,EBI-14518; Score: 0.35
DE  Interaction: P54783; IntAct: EBI-20589,EBI-2519; Score: 0.35
DE  Interaction: Q01919; IntAct: EBI-20589,EBI-2610950; Score: 0.35
DE  Interaction: Q07655; IntAct: EBI-20589,EBI-31312; Score: 0.35
DE  Interaction: P25367; IntAct: EBI-20589,EBI-21708; Score: 0.35
DE  Interaction: Q08921; IntAct: EBI-20589,EBI-37395; Score: 0.35
DE  Interaction: Q06436; IntAct: EBI-20589,EBI-30241; Score: 0.35
DE  Interaction: P12904; IntAct: EBI-20589,EBI-17537; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-20589,EBI-18084; Score: 0.35
DE  Interaction: Q03503; IntAct: EBI-20589,EBI-10388; Score: 0.35
DE  Interaction: P20134; IntAct: EBI-20589,EBI-17027; Score: 0.35
DE  Interaction: P38700; IntAct: EBI-20589,EBI-2705; Score: 0.35
DE  Interaction: P36024; IntAct: EBI-20589,EBI-17250; Score: 0.35
DE  Interaction: P12962; IntAct: EBI-20589,EBI-9010; Score: 0.35
DE  Interaction: Q12194; IntAct: EBI-20589,EBI-29434; Score: 0.35
DE  Interaction: P38990; IntAct: EBI-20589,EBI-12863; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-20589,EBI-16054; Score: 0.35
DE  Interaction: Q12347; IntAct: EBI-20589,EBI-30029; Score: 0.35
DE  Interaction: P25586; IntAct: EBI-20589,EBI-21773; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-20589,EBI-8958; Score: 0.35
DE  Interaction: Q03508; IntAct: EBI-20589,EBI-27589; Score: 0.35
DE  Interaction: P40208; IntAct: EBI-20589,EBI-27276; Score: 0.35
DE  Interaction: P39008; IntAct: EBI-20589,EBI-13629; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-20589,EBI-17136; Score: 0.35
DE  Interaction: P32829; IntAct: EBI-20589,EBI-11255; Score: 0.35
DE  Interaction: P53628; IntAct: EBI-20589,EBI-17564; Score: 0.35
DE  Interaction: P53583; IntAct: EBI-20589,EBI-11174; Score: 0.35
DE  Interaction: P40991; IntAct: EBI-20589,EBI-12110; Score: 0.35
DE  Interaction: P53965; IntAct: EBI-20589,EBI-28668; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-20589,EBI-8936; Score: 0.35
DE  Interaction: Q12428; IntAct: EBI-20589,EBI-29344; Score: 0.35
DE  Interaction: Q12406; IntAct: EBI-20589,EBI-2962; Score: 0.35
DE  Interaction: Q12502; IntAct: EBI-20589,EBI-2113927; Score: 0.35
DE  Interaction: P40484; IntAct: EBI-20589,EBI-11119; Score: 0.35
DE  Interaction: P36157; IntAct: EBI-20589,EBI-26503; Score: 0.35
DE  Interaction: Q12024; IntAct: EBI-20589,EBI-29589; Score: 0.35
DE  Interaction: Q00381; IntAct: EBI-20589,EBI-2608; Score: 0.35
DE  Interaction: Q06108; IntAct: EBI-20589,EBI-38709; Score: 0.35
DE  Interaction: P32342; IntAct: EBI-20589,EBI-17984; Score: 0.35
DE  Interaction: P40099; IntAct: EBI-20589,EBI-2059710; Score: 0.35
DE  Interaction: Q02939; IntAct: EBI-20589,EBI-2345544; Score: 0.35
DE  Interaction: Q03497; IntAct: EBI-20589,EBI-18285; Score: 0.35
DE  Interaction: P32607; IntAct: EBI-20589,EBI-16312; Score: 0.35
DE  Interaction: P39016; IntAct: EBI-20589,EBI-2052996; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-20589,EBI-12823; Score: 0.35
DE  Interaction: P32567; IntAct: EBI-20589,EBI-17478; Score: 0.35
DE  Interaction: P36083; IntAct: EBI-20589,EBI-26750; Score: 0.35
DE  Interaction: P32502; IntAct: EBI-20589,EBI-6260; Score: 0.35
DE  Interaction: Q03208; IntAct: EBI-20589,EBI-27965; Score: 0.35
DE  Interaction: Q12071; IntAct: EBI-20589,EBI-36751; Score: 0.35
DE  Interaction: P07347; IntAct: EBI-20589,EBI-2796; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-20589,EBI-25261; Score: 0.35
DE  Interaction: P53215; IntAct: EBI-20589,EBI-23112; Score: 0.35
DE  Interaction: P32590; IntAct: EBI-20589,EBI-8655; Score: 0.35
DE  Interaction: Q3E757; IntAct: EBI-20589,EBI-783263; Score: 0.35
DE  Interaction: P38236; IntAct: EBI-20589,EBI-11619; Score: 0.35
DE  Interaction: P40547; IntAct: EBI-20589,EBI-24957; Score: 0.35
DE  Interaction: Q07084; IntAct: EBI-20589,EBI-18184; Score: 0.35
DE  Interaction: P38682; IntAct: EBI-20589,EBI-7679; Score: 0.35
DE  Interaction: P36103; IntAct: EBI-20589,EBI-26614; Score: 0.35
DE  Interaction: P38151; IntAct: EBI-20589,EBI-12968; Score: 0.35
DE  Interaction: P40017; IntAct: EBI-20589,EBI-2345299; Score: 0.35
DE  Interaction: P16522; IntAct: EBI-20589,EBI-4216; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-20589,EBI-16150; Score: 0.35
DE  Interaction: Q03776; IntAct: EBI-20589,EBI-802; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-20589,EBI-35018; Score: 0.35
DE  Interaction: P11746; IntAct: EBI-20589,EBI-10528; Score: 0.35
DE  Interaction: P53734; IntAct: EBI-20589,EBI-5625; Score: 0.35
DE  Interaction: Q12515; IntAct: EBI-20589,EBI-38409; Score: 0.35
DE  Interaction: P15625; IntAct: EBI-20589,EBI-18678; Score: 0.35
DE  Interaction: Q03088; IntAct: EBI-20589,EBI-36005; Score: 0.35
DE  Interaction: Q04600; IntAct: EBI-20589,EBI-38802; Score: 0.35
DE  Interaction: P38691; IntAct: EBI-20589,EBI-9937; Score: 0.35
DE  Interaction: P47168; IntAct: EBI-20589,EBI-25698; Score: 0.35
DE  Interaction: P50091; IntAct: EBI-20589,EBI-23549; Score: 0.35
DE  Interaction: P53036; IntAct: EBI-20589,EBI-16467; Score: 0.35
DE  Interaction: P05738; IntAct: EBI-20589,EBI-15439; Score: 0.35
DE  Interaction: Q08096; IntAct: EBI-20589,EBI-14892; Score: 0.35
DE  Interaction: P38112; IntAct: EBI-20589,EBI-10394; Score: 0.35
DE  Interaction: P20433; IntAct: EBI-20589,EBI-15777; Score: 0.35
DE  Interaction: P29468; IntAct: EBI-20589,EBI-12917; Score: 0.35
DE  Interaction: Q99314; IntAct: EBI-20589,EBI-31212; Score: 0.35
DE  Interaction: P42846; IntAct: EBI-20589,EBI-28360; Score: 0.35
DE  Interaction: P43586; IntAct: EBI-20589,EBI-22906; Score: 0.35
DE  Interaction: P28263; IntAct: EBI-20589,EBI-19755; Score: 0.35
DE  Interaction: Q12417; IntAct: EBI-20589,EBI-710; Score: 0.35
DE  Interaction: Q06671; IntAct: EBI-20589,EBI-3685534; Score: 0.35
DE  Interaction: P15790; IntAct: EBI-20589,EBI-9533; Score: 0.35
DE  Interaction: Q12099; IntAct: EBI-20589,EBI-6776; Score: 0.35
DE  Interaction: P40007; IntAct: EBI-20589,EBI-22439; Score: 0.35
DE  Interaction: O13516; IntAct: EBI-20589,EBI-16176; Score: 0.35
DE  Interaction: P47122; IntAct: EBI-20589,EBI-25534; Score: 0.35
DE  Interaction: P53327; IntAct: EBI-20589,EBI-23623; Score: 0.35
DE  Interaction: P39936; IntAct: EBI-20589,EBI-9006; Score: 0.35
DE  Interaction: Q07915; IntAct: EBI-20589,EBI-35766; Score: 0.35
DE  Interaction: P53165; IntAct: EBI-20589,EBI-23812; Score: 0.35
DE  Interaction: P38272; IntAct: EBI-20589,EBI-21600; Score: 0.35
DE  Interaction: Q04461; IntAct: EBI-20589,EBI-27209; Score: 0.35
DE  Interaction: Q08287; IntAct: EBI-20589,EBI-12135; Score: 0.35
DE  Interaction: P52920; IntAct: EBI-20589,EBI-11880; Score: 0.35
DE  Interaction: Q06709; IntAct: EBI-20589,EBI-35391; Score: 0.35
DE  Interaction: Q02326; IntAct: EBI-20589,EBI-15403; Score: 0.35
DE  Interaction: P32351; IntAct: EBI-20589,EBI-9250; Score: 0.35
DE  Interaction: P47006; IntAct: EBI-20589,EBI-26109; Score: 0.35
DE  Interaction: P18888; IntAct: EBI-20589,EBI-17550; Score: 0.35
DE  Interaction: Q04934; IntAct: EBI-20589,EBI-35255; Score: 0.35
DE  Interaction: P39516; IntAct: EBI-20589,EBI-14464; Score: 0.35
DE  Interaction: Q12380; IntAct: EBI-20589,EBI-2664; Score: 0.35
DE  Interaction: P40963; IntAct: EBI-20589,EBI-16476; Score: 0.35
DE  Interaction: P15807; IntAct: EBI-20589,EBI-10770; Score: 0.35
DE  Interaction: Q12454; IntAct: EBI-20589,EBI-34560; Score: 0.35
DE  Interaction: Q00723; IntAct: EBI-20589,EBI-841; Score: 0.35
DE  Interaction: P18961; IntAct: EBI-20589,EBI-29484; Score: 0.35
DE  Interaction: Q12368; IntAct: EBI-20589,EBI-252; Score: 0.35
DE  Interaction: P42223; IntAct: EBI-20589,EBI-16498; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-20589,EBI-29626; Score: 0.35
DE  Interaction: Q05468; IntAct: EBI-20589,EBI-32961; Score: 0.35
DE  Interaction: P22209; IntAct: EBI-20589,EBI-9730; Score: 0.35
DE  Interaction: P38873; IntAct: EBI-20589,EBI-24864; Score: 0.35
DE  Interaction: P36053; IntAct: EBI-20589,EBI-26919; Score: 0.35
DE  Interaction: P38719; IntAct: EBI-20589,EBI-5633; Score: 0.35
DE  Interaction: P32591; IntAct: EBI-20589,EBI-18622; Score: 0.35
DE  Interaction: P38431; IntAct: EBI-20589,EBI-9038; Score: 0.35
DE  Interaction: P39998; IntAct: EBI-20589,EBI-22300; Score: 0.35
DE  Interaction: P14904; IntAct: EBI-20589,EBI-2571; Score: 0.35
DE  Interaction: P19454; IntAct: EBI-20589,EBI-9548; Score: 0.35
DE  Interaction: P32899; IntAct: EBI-20589,EBI-9237; Score: 0.35
DE  Interaction: P11433; IntAct: EBI-20589,EBI-4220; Score: 0.35
DE  Interaction: Q02864; IntAct: EBI-20589,EBI-38920; Score: 0.35
DE  Interaction: P40070; IntAct: EBI-20589,EBI-188; Score: 0.35
DE  Interaction: P53952; IntAct: EBI-20589,EBI-2102292; Score: 0.35
DE  Interaction: P16370; IntAct: EBI-20589,EBI-15773; Score: 0.35
DE  Interaction: Q02892; IntAct: EBI-20589,EBI-12105; Score: 0.35
DE  Interaction: Q08689; IntAct: EBI-20589,EBI-34404; Score: 0.35
DE  Interaction: P39955; IntAct: EBI-20589,EBI-16463; Score: 0.35
DE  Interaction: P41903; IntAct: EBI-20589,EBI-14154; Score: 0.35
DE  Interaction: P38315; IntAct: EBI-20589,EBI-20985; Score: 0.35
DE  Interaction: P39015; IntAct: EBI-20589,EBI-11238; Score: 0.35
DE  Interaction: P38041; IntAct: EBI-20589,EBI-3719; Score: 0.35
DE  Interaction: P45976; IntAct: EBI-20589,EBI-6940; Score: 0.35
DE  Interaction: P32497; IntAct: EBI-20589,EBI-8965; Score: 0.35
DE  Interaction: P37304; IntAct: EBI-20589,EBI-12870; Score: 0.35
DE  Interaction: P43597; IntAct: EBI-20589,EBI-22951; Score: 0.35
DE  Interaction: Q12191; IntAct: EBI-20589,EBI-32271; Score: 0.35
DE  Interaction: P38759; IntAct: EBI-20589,EBI-13092; Score: 0.35
DE  Interaction: P53883; IntAct: EBI-20589,EBI-29032; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-20589,EBI-9068; Score: 0.35
DE  Interaction: P38712; IntAct: EBI-20589,EBI-16007; Score: 0.35
DE  Interaction: P32495; IntAct: EBI-20589,EBI-12014; Score: 0.35
DE  Interaction: Q03656; IntAct: EBI-20589,EBI-9800; Score: 0.35
DE  Interaction: P38230; IntAct: EBI-20589,EBI-3774859; Score: 0.35
DE  Interaction: P53316; IntAct: EBI-20589,EBI-23586; Score: 0.35
DE  Interaction: P25390; IntAct: EBI-20589,EBI-18129; Score: 0.35
DE  Interaction: Q03862; IntAct: EBI-20589,EBI-31385; Score: 0.35
DE  Interaction: P25555; IntAct: EBI-20589,EBI-7410; Score: 0.35
DE  Interaction: P0CX73; IntAct: EBI-20589,EBI-11611501; Score: 0.35
DE  Interaction: P40453; IntAct: EBI-20589,EBI-19857; Score: 0.35
DE  Interaction: P34253; IntAct: EBI-20589,EBI-9950; Score: 0.35
DE  Interaction: P24784; IntAct: EBI-20589,EBI-5596; Score: 0.35
DE  Interaction: P39525; IntAct: EBI-20589,EBI-4467; Score: 0.35
DE  Interaction: P34239; IntAct: EBI-20589,EBI-26951; Score: 0.35
DE  Interaction: P38200; IntAct: EBI-20589,EBI-21213; Score: 0.35
DE  Interaction: Q12124; IntAct: EBI-20589,EBI-37542; Score: 0.35
DE  Interaction: P53199; IntAct: EBI-20589,EBI-6514; Score: 0.35
DE  Interaction: P47108; IntAct: EBI-20589,EBI-25492; Score: 0.35
DE  Interaction: P47148; IntAct: EBI-20589,EBI-25619; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-20589,EBI-14480; Score: 0.35
DE  Interaction: P12945; IntAct: EBI-20589,EBI-11868; Score: 0.35
DE  Interaction: Q12163; IntAct: EBI-20589,EBI-34713; Score: 0.35
DE  Interaction: P53063; IntAct: EBI-20589,EBI-24206; Score: 0.35
DE  Interaction: Q08208; IntAct: EBI-20589,EBI-35895; Score: 0.35
DE  Interaction: Q05949; IntAct: EBI-20589,EBI-30948; Score: 0.35
DE  Interaction: Q03760; IntAct: EBI-20589,EBI-27933; Score: 0.35
DE  Interaction: P36146; IntAct: EBI-20589,EBI-10053; Score: 0.35
DE  Interaction: Q08732; IntAct: EBI-20589,EBI-37488; Score: 0.35
DE  Interaction: Q07872; IntAct: EBI-20589,EBI-38931; Score: 0.35
DE  Interaction: P35182; IntAct: EBI-20589,EBI-12784; Score: 0.35
DE  Interaction: P25617; IntAct: EBI-20589,EBI-375711; Score: 0.35
DE  Interaction: P35178; IntAct: EBI-20589,EBI-16002; Score: 0.35
DE  Interaction: Q06078; IntAct: EBI-20589,EBI-359; Score: 0.35
DE  Interaction: Q04418; IntAct: EBI-20589,EBI-38743; Score: 0.35
DE  Interaction: Q04003; IntAct: EBI-20589,EBI-38500; Score: 0.35
DE  Interaction: P32909; IntAct: EBI-20589,EBI-17503; Score: 0.35
DE  Interaction: P23561; IntAct: EBI-20589,EBI-18259; Score: 0.35
DE  Interaction: P15274; IntAct: EBI-20589,EBI-2548; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-20589,EBI-505; Score: 0.35
DE  Interaction: P49704; IntAct: EBI-20589,EBI-347; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-20589,EBI-34508; Score: 0.35
DE  Interaction: P18494; IntAct: EBI-20589,EBI-7657; Score: 0.35
DE  Interaction: P20447; IntAct: EBI-20589,EBI-5608; Score: 0.35
DE  Interaction: P53145; IntAct: EBI-20589,EBI-23885; Score: 0.35
DE  Interaction: Q04347; IntAct: EBI-20589,EBI-28028; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-20589,EBI-17244; Score: 0.35
DE  Interaction: P40561; IntAct: EBI-20589,EBI-25362; Score: 0.35
DE  Interaction: Q00816; IntAct: EBI-20589,EBI-8270; Score: 0.35
DE  Interaction: Q03532; IntAct: EBI-20589,EBI-8170; Score: 0.35
DE  Interaction: P43573; IntAct: EBI-20589,EBI-22787; Score: 0.35
DE  Interaction: P25339; IntAct: EBI-20589,EBI-23703; Score: 0.35
DE  Interaction: P39702; IntAct: EBI-20589,EBI-20488; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-20589,EBI-28814; Score: 0.35
DE  Interaction: P48412; IntAct: EBI-20589,EBI-20117; Score: 0.35
DE  Interaction: P21374; IntAct: EBI-20589,EBI-9382; Score: 0.35
DE  Interaction: P38779; IntAct: EBI-20589,EBI-24538; Score: 0.35
DE  Interaction: P03871; IntAct: EBI-20589,EBI-14929; Score: 0.35
DE  Interaction: Q02554; IntAct: EBI-20589,EBI-654; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-20589,EBI-17148; Score: 0.35
DE  Interaction: P50109; IntAct: EBI-20589,EBI-14050; Score: 0.35
DE  Interaction: P34241; IntAct: EBI-20589,EBI-26595; Score: 0.35
DE  Interaction: P53892; IntAct: EBI-20589,EBI-28987; Score: 0.35
DE  Interaction: P53914; IntAct: EBI-20589,EBI-28914; Score: 0.35
DE  Interaction: P43572; IntAct: EBI-20589,EBI-22792; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-20589,EBI-31475; Score: 0.35
DE  Interaction: P48234; IntAct: EBI-20589,EBI-23354; Score: 0.35
DE  Interaction: P38321; IntAct: EBI-20589,EBI-21008; Score: 0.35
DE  Interaction: P53137; IntAct: EBI-20589,EBI-23916; Score: 0.35
DE  Interaction: Q12378; IntAct: EBI-20589,EBI-31807; Score: 0.35
DE  Interaction: P40956; IntAct: EBI-20589,EBI-7968; Score: 0.35
DE  Interaction: Q04673; IntAct: EBI-20589,EBI-18198; Score: 0.35
DE  Interaction: P40482; IntAct: EBI-20589,EBI-16592; Score: 0.35
DE  Interaction: Q03758; IntAct: EBI-20589,EBI-27941; Score: 0.35
DE  Interaction: P38823; IntAct: EBI-20589,EBI-24686; Score: 0.35
DE  Interaction: P40559; IntAct: EBI-20589,EBI-24915; Score: 0.35
DE  Interaction: Q07896; IntAct: EBI-20589,EBI-36093; Score: 0.35
DE  Interaction: Q06211; IntAct: EBI-20589,EBI-38894; Score: 0.35
DE  Interaction: P51534; IntAct: EBI-20589,EBI-17086; Score: 0.35
DE  Interaction: P13186; IntAct: EBI-20589,EBI-9723; Score: 0.35
DE  Interaction: P38281; IntAct: EBI-20589,EBI-20838; Score: 0.35
DE  Interaction: P15303; IntAct: EBI-20589,EBI-16584; Score: 0.35
DE  Interaction: Q08226; IntAct: EBI-20589,EBI-30025; Score: 0.35
DE  Interaction: P12688; IntAct: EBI-20589,EBI-29473; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-20589,EBI-15881; Score: 0.35
DE  Interaction: P32336; IntAct: EBI-20589,EBI-12361; Score: 0.35
DE  Interaction: Q12060; IntAct: EBI-20589,EBI-8287; Score: 0.35
DE  Interaction: P38697; IntAct: EBI-20589,EBI-9186; Score: 0.35
DE  Interaction: Q06344; IntAct: EBI-20589,EBI-34121; Score: 0.35
DE  Interaction: P32598; IntAct: EBI-20589,EBI-13715; Score: 0.35
DE  Interaction: P29366; IntAct: EBI-20589,EBI-3508; Score: 0.35
DE  Interaction: P34087; IntAct: EBI-20589,EBI-15790; Score: 0.35
DE  Interaction: P38344; IntAct: EBI-20589,EBI-21136; Score: 0.35
DE  Interaction: Q08649; IntAct: EBI-20589,EBI-6648; Score: 0.35
DE  Interaction: Q04408; IntAct: EBI-20589,EBI-36603; Score: 0.35
DE  Interaction: Q07381; IntAct: EBI-20589,EBI-35023; Score: 0.35
DE  Interaction: P09064; IntAct: EBI-20589,EBI-8920; Score: 0.35
DE  Interaction: P16892; IntAct: EBI-20589,EBI-7193; Score: 0.35
DE  Interaction: P43612; IntAct: EBI-20589,EBI-16370; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-20589,EBI-8973; Score: 0.35
DE  Interaction: P53251; IntAct: EBI-20589,EBI-23221; Score: 0.35
DE  Interaction: P14126; IntAct: EBI-20589,EBI-15364; Score: 0.35
DE  Interaction: Q04739; IntAct: EBI-20589,EBI-7244; Score: 0.35
DE  Interaction: Q12343; IntAct: EBI-20589,EBI-31503; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-20589,EBI-25710; Score: 0.35
DE  Interaction: P15624; IntAct: EBI-20589,EBI-18684; Score: 0.35
DE  Interaction: P47050; IntAct: EBI-20589,EBI-25861; Score: 0.35
DE  Interaction: Q08886; IntAct: EBI-20589,EBI-3655948; Score: 0.35
DE  Interaction: P51862; IntAct: EBI-20589,EBI-15702; Score: 0.35
DE  Interaction: P53941; IntAct: EBI-20589,EBI-9243; Score: 0.35
DE  Interaction: P54113; IntAct: EBI-20589,EBI-14213; Score: 0.35
DE  Interaction: Q12517; IntAct: EBI-20589,EBI-38519; Score: 0.35
DE  Interaction: P30665; IntAct: EBI-20589,EBI-4326; Score: 0.35
DE  Interaction: Q03785; IntAct: EBI-20589,EBI-35568; Score: 0.35
DE  Interaction: P11745; IntAct: EBI-20589,EBI-15648; Score: 0.53
DE  Interaction: P38249; IntAct: EBI-20589,EBI-8981; Score: 0.35
DE  Interaction: P53855; IntAct: EBI-20589,EBI-29212; Score: 0.35
DE  Interaction: P32786; IntAct: EBI-20589,EBI-15986; Score: 0.35
DE  Interaction: P53604; IntAct: EBI-20589,EBI-2086543; Score: 0.35
DE  Interaction: Q06628; IntAct: EBI-20589,EBI-36188; Score: 0.35
DE  Interaction: Q08237; IntAct: EBI-20589,EBI-30507; Score: 0.35
DE  Interaction: P39717; IntAct: EBI-20589,EBI-20711; Score: 0.35
DE  Interaction: P53942; IntAct: EBI-20589,EBI-15663; Score: 0.35
DE  Interaction: Q06218; IntAct: EBI-20589,EBI-5640; Score: 0.35
DE  Interaction: P53893; IntAct: EBI-20589,EBI-28980; Score: 0.35
DE  Interaction: Q12028; IntAct: EBI-20589,EBI-33025; Score: 0.35
DE  Interaction: Q12321; IntAct: EBI-20589,EBI-32854; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-20589,EBI-8951; Score: 0.35
DE  Interaction: Q07834; IntAct: EBI-20589,EBI-36507; Score: 0.35
DE  Interaction: Q01477; IntAct: EBI-20589,EBI-19834; Score: 0.35
DE  Interaction: Q03780; IntAct: EBI-20589,EBI-30094; Score: 0.35
DE  Interaction: Q06632; IntAct: EBI-20589,EBI-32872; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-20589,EBI-2186; Score: 0.35
DE  Interaction: P38165; IntAct: EBI-20589,EBI-16328; Score: 0.35
DE  Interaction: P47116; IntAct: EBI-20589,EBI-2613227; Score: 0.35
DE  Interaction: P38696; IntAct: EBI-20589,EBI-2920; Score: 0.35
DE  Interaction: P53949; IntAct: EBI-20589,EBI-28725; Score: 0.35
DE  Interaction: P38180; IntAct: EBI-20589,EBI-21315; Score: 0.35
DE  Interaction: Q04712; IntAct: EBI-20589,EBI-27790; Score: 0.35
DE  Interaction: P39731; IntAct: EBI-20589,EBI-11606; Score: 0.35
DE  Interaction: P53270; IntAct: EBI-20589,EBI-23280; Score: 0.35
DE  Interaction: P08018; IntAct: EBI-20589,EBI-12972; Score: 0.35
DE  Interaction: Q03769; IntAct: EBI-20589,EBI-2055743; Score: 0.35
DE  Interaction: P40091; IntAct: EBI-20589,EBI-13106; Score: 0.35
DE  Interaction: P37838; IntAct: EBI-20589,EBI-12122; Score: 0.35
DE  Interaction: Q03735; IntAct: EBI-20589,EBI-27955; Score: 0.35
DE  Interaction: P29055; IntAct: EBI-20589,EBI-19123; Score: 0.35
DE  Interaction: P38065; IntAct: EBI-20589,EBI-2181; Score: 0.35
DE  Interaction: P32047; IntAct: EBI-20589,EBI-2611643; Score: 0.35
DE  Interaction: P42841; IntAct: EBI-20589,EBI-28378; Score: 0.35
DE  Interaction: P53953; IntAct: EBI-20589,EBI-17006; Score: 0.35
DE  Interaction: P27476; IntAct: EBI-20589,EBI-12274; Score: 0.35
DE  Interaction: Q06132; IntAct: EBI-20589,EBI-34377; Score: 0.35
DE  Interaction: P21373; IntAct: EBI-20589,EBI-20174; Score: 0.35
DE  Interaction: Q03338; IntAct: EBI-20589,EBI-421; Score: 0.35
DE  Interaction: P27692; IntAct: EBI-20589,EBI-17937; Score: 0.35
DE  Interaction: P40693; IntAct: EBI-20589,EBI-15415; Score: 0.35
DE  Interaction: P43603; IntAct: EBI-20589,EBI-22980; Score: 0.55
DE  Interaction: P09734; IntAct: EBI-20589,EBI-18981; Score: 0.35
DE  Interaction: Q07913; IntAct: EBI-20589,EBI-30144; Score: 0.35
DE  Interaction: P06784; IntAct: EBI-20589,EBI-18389; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-20589,EBI-18868; Score: 0.35
DE  Interaction: P53873; IntAct: EBI-20589,EBI-29071; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-20589,EBI-29516; Score: 0.35
DE  Interaction: P47048; IntAct: EBI-20589,EBI-25870; Score: 0.35
DE  Interaction: Q02256; IntAct: EBI-20589,EBI-14322; Score: 0.35
DE  Interaction: P38798; IntAct: EBI-20589,EBI-12071; Score: 0.35
DE  Interaction: P25366; IntAct: EBI-20589,EBI-22021; Score: 0.35
DE  Interaction: Q12522; IntAct: EBI-20589,EBI-9046; Score: 0.35
DE  Interaction: Q12176; IntAct: EBI-20589,EBI-10944; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-20589,EBI-11835; Score: 0.35
DE  Interaction: Q12136; IntAct: EBI-20589,EBI-36084; Score: 0.35
DE  Interaction: P46990; IntAct: EBI-20589,EBI-14522; Score: 0.35
DE  Interaction: P40856; IntAct: EBI-20589,EBI-16384; Score: 0.35
DE  Interaction: P38930; IntAct: EBI-20589,EBI-9578; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-20589,EBI-13686; Score: 0.35
DE  Interaction: P14741; IntAct: EBI-20589,EBI-6253; Score: 0.35
DE  Interaction: Q04410; IntAct: EBI-20589,EBI-32083; Score: 0.35
DE  Interaction: P32523; IntAct: EBI-20589,EBI-493; Score: 0.35
DE  Interaction: Q12504; IntAct: EBI-20589,EBI-30749; Score: 0.35
DE  Interaction: P29295; IntAct: EBI-20589,EBI-8536; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-20589,EBI-28532; Score: 0.35
DE  Interaction: P38701; IntAct: EBI-20589,EBI-16081; Score: 0.35
DE  Interaction: Q02959; IntAct: EBI-20589,EBI-8484; Score: 0.35
DE  Interaction: Q12523; IntAct: EBI-20589,EBI-37062; Score: 0.35
DE  Interaction: P40535; IntAct: EBI-20589,EBI-2052; Score: 0.35
DE  Interaction: P34167; IntAct: EBI-20589,EBI-9025; Score: 0.35
DE  Interaction: Q02793; IntAct: EBI-20589,EBI-17260; Score: 0.35
DE  Interaction: P36076; IntAct: EBI-20589,EBI-26778; Score: 0.35
DE  Interaction: Q07825; IntAct: EBI-20589,EBI-32387; Score: 0.35
DE  Interaction: P53088; IntAct: EBI-20589,EBI-24137; Score: 0.35
DE  Interaction: P45978; IntAct: EBI-20589,EBI-16691; Score: 0.35
DE  Interaction: Q12094; IntAct: EBI-20589,EBI-29255; Score: 0.35
DE  Interaction: Q12421; IntAct: EBI-20589,EBI-34768; Score: 0.35
DE  Interaction: P06843; IntAct: EBI-20589,EBI-17914; Score: 0.35
DE  Interaction: P38738; IntAct: EBI-20589,EBI-24355; Score: 0.35
DE  Interaction: P33400; IntAct: EBI-20589,EBI-14422; Score: 0.35
DE  Interaction: P46675; IntAct: EBI-20589,EBI-18471; Score: 0.35
DE  Interaction: Q07532; IntAct: EBI-20589,EBI-33428; Score: 0.35
DE  Interaction: Q08726; IntAct: EBI-20589,EBI-37977; Score: 0.35
DE  Interaction: Q08217; IntAct: EBI-20589,EBI-9839; Score: 0.35
DE  Interaction: P25635; IntAct: EBI-20589,EBI-14332; Score: 0.35
DE  Interaction: P33442; IntAct: EBI-20589,EBI-16132; Score: 0.35
DE  Interaction: P38251; IntAct: EBI-20589,EBI-15016; Score: 0.35
DE  Interaction: P05750; IntAct: EBI-20589,EBI-16140; Score: 0.35
DE  Interaction: Q06205; IntAct: EBI-20589,EBI-6956; Score: 0.35
DE  Interaction: P04803; IntAct: EBI-20589,EBI-18837; Score: 0.35
DE  Interaction: P53238; IntAct: EBI-20589,EBI-23185; Score: 0.35
DE  Interaction: Q07844; IntAct: EBI-20589,EBI-27142; Score: 0.35
DE  Interaction: P39682; IntAct: EBI-20589,EBI-612; Score: 0.35
DE  Interaction: P39744; IntAct: EBI-20589,EBI-29259; Score: 0.35
DE  Interaction: P33201; IntAct: EBI-20589,EBI-26590; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-20589,EBI-3727; Score: 0.35
DE  Interaction: Q06337; IntAct: EBI-20589,EBI-35867; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-20589,EBI-20777; Score: 0.35
DE  Interaction: P38061; IntAct: EBI-20589,EBI-15346; Score: 0.35
DE  Interaction: Q04511; IntAct: EBI-20589,EBI-20020; Score: 0.35
DE  Interaction: Q12216; IntAct: EBI-20589,EBI-11987; Score: 0.35
DE  Interaction: Q07821; IntAct: EBI-20589,EBI-27136; Score: 0.35
DE  Interaction: P38213; IntAct: EBI-20589,EBI-21385; Score: 0.35
DE  Interaction: P46682; IntAct: EBI-20589,EBI-2213; Score: 0.35
DE  Interaction: P38153; IntAct: EBI-20589,EBI-2710; Score: 0.35
DE  Interaction: Q12092; IntAct: EBI-20589,EBI-38752; Score: 0.35
DE  Interaction: P39729; IntAct: EBI-20589,EBI-20651; Score: 0.35
DE  Interaction: P41819; IntAct: EBI-20589,EBI-5884; Score: 0.35
DE  Interaction: P42935; IntAct: EBI-20589,EBI-23459; Score: 0.35
DE  Interaction: P47089; IntAct: EBI-20589,EBI-5751; Score: 0.35
DE  Interaction: P38805; IntAct: EBI-20589,EBI-24614; Score: 0.35
DE  Interaction: Q07533; IntAct: EBI-20589,EBI-31510; Score: 0.35
DE  Interaction: P49960; IntAct: EBI-20589,EBI-212; Score: 0.35
DE  Interaction: P42843; IntAct: EBI-20589,EBI-28370; Score: 0.35
DE  Interaction: P0CX83; IntAct: EBI-20589,EBI-7433003; Score: 0.35
DE  Interaction: P0CX36; IntAct: EBI-20589,EBI-7433300; Score: 0.35
DE  Interaction: P0CX54; IntAct: EBI-20589,EBI-7432640; Score: 0.35
DE  Interaction: P0CX38; IntAct: EBI-20589,EBI-7432889; Score: 0.35
DE  Interaction: P0CX48; IntAct: EBI-20589,EBI-7433392; Score: 0.35
DE  Interaction: P0CX46; IntAct: EBI-20589,EBI-7433130; Score: 0.35
DE  Interaction: Q05937; IntAct: EBI-20589,EBI-7766412; Score: 0.35
DE  Interaction: P0CX56; IntAct: EBI-20589,EBI-7433160; Score: 0.35
DE  Interaction: P0CX32; IntAct: EBI-20589,EBI-7432762; Score: 0.35
DE  Interaction: P0CX40; IntAct: EBI-20589,EBI-7432610; Score: 0.35
DE  Interaction: Q06543; IntAct: EBI-20589,EBI-33132; Score: 0.35
DE  Interaction: P40059; IntAct: EBI-20589,EBI-6062; Score: 0.35
DE  Interaction: Q12049; IntAct: EBI-20589,EBI-34263; Score: 0.35
DE  Interaction: Q12129; IntAct: EBI-20589,EBI-30663; Score: 0.35
DE  Interaction: Q06188; IntAct: EBI-20589,EBI-35613; Score: 0.35
DE  Interaction: P38985; IntAct: EBI-20589,EBI-17977; Score: 0.35
DE  Interaction: Q12291; IntAct: EBI-20589,EBI-31876; Score: 0.35
DE  Interaction: P27351; IntAct: EBI-20589,EBI-2202; Score: 0.35
DE  Interaction: P38042; IntAct: EBI-20589,EBI-4249; Score: 0.35
DE  Interaction: P04449; IntAct: EBI-20589,EBI-14560; Score: 0.35
DE  Interaction: P38629; IntAct: EBI-20589,EBI-15000; Score: 0.35
DE  Interaction: P30619; IntAct: EBI-20589,EBI-16833; Score: 0.35
DE  Interaction: P23201; IntAct: EBI-20589,EBI-17803; Score: 0.35
DE  Interaction: Q12224; IntAct: EBI-20589,EBI-15468; Score: 0.35
DE  Interaction: P26785; IntAct: EBI-20589,EBI-14513; Score: 0.35
DE  Interaction: Q12196; IntAct: EBI-20589,EBI-15224; Score: 0.35
DE  Interaction: P47064; IntAct: EBI-20589,EBI-2619; Score: 0.35
DE  Interaction: P12754; IntAct: EBI-20589,EBI-6265; Score: 0.35
DE  Interaction: P40079; IntAct: EBI-20589,EBI-10103; Score: 0.35
DE  Interaction: P50278; IntAct: EBI-20589,EBI-17675; Score: 0.35
DE  Interaction: P32525; IntAct: EBI-20589,EBI-26215; Score: 0.35
DE  Interaction: Q02908; IntAct: EBI-20589,EBI-33957; Score: 0.35
DE  Interaction: Q06604; IntAct: EBI-20589,EBI-37047; Score: 0.35
DE  Interaction: Q07418; IntAct: EBI-20589,EBI-292; Score: 0.35
DE  Interaction: P27636; IntAct: EBI-20589,EBI-4200; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-20589,EBI-5612; Score: 0.35
DE  Interaction: P40157; IntAct: EBI-20589,EBI-29136; Score: 0.35
DE  Interaction: Q12090; IntAct: EBI-20589,EBI-2083048; Score: 0.35
DE  Interaction: P23292; IntAct: EBI-20589,EBI-4729; Score: 0.35
DE  Interaction: P47130; IntAct: EBI-20589,EBI-763; Score: 0.35
DE  Interaction: Q99369; IntAct: EBI-20589,EBI-3826891; Score: 0.35
DE  Interaction: P40021; IntAct: EBI-20589,EBI-22484; Score: 0.35
DE  Interaction: P38089; IntAct: EBI-20589,EBI-12814; Score: 0.35
DE  Interaction: P40013; IntAct: EBI-20589,EBI-3614; Score: 0.35
DE  Interaction: P21304; IntAct: EBI-20589,EBI-14328; Score: 0.35
DE  Interaction: P25042; IntAct: EBI-20589,EBI-15714; Score: 0.35
DE  Interaction: P20434; IntAct: EBI-20589,EBI-15781; Score: 0.35
DE  Interaction: P39743; IntAct: EBI-20589,EBI-14500; Score: 0.35
DE  Interaction: Q03466; IntAct: EBI-20589,EBI-31765; Score: 0.35
DE  Interaction: Q04377; IntAct: EBI-20589,EBI-35652; Score: 0.35
DE  Interaction: Q05123; IntAct: EBI-20589,EBI-2972; Score: 0.35
DE  Interaction: Q04372; IntAct: EBI-20589,EBI-18926; Score: 0.35
DE  Interaction: P50094; IntAct: EBI-20589,EBI-9195; Score: 0.35
DE  Interaction: P53901; IntAct: EBI-20589,EBI-28955; Score: 0.35
DE  Interaction: P25559; IntAct: EBI-20589,EBI-5661; Score: 0.35
DE  Interaction: P36049; IntAct: EBI-20589,EBI-6289; Score: 0.35
DE  Interaction: Q07350; IntAct: EBI-20589,EBI-688; Score: 0.35
DE  Interaction: P40335; IntAct: EBI-20589,EBI-20373; Score: 0.35
DE  Interaction: Q12034; IntAct: EBI-20589,EBI-17335; Score: 0.35
DE  Interaction: P15442; IntAct: EBI-20589,EBI-330; Score: 0.35
DE  Interaction: Q3E705; IntAct: EBI-20589,EBI-3666578; Score: 0.35
DE  Interaction: P34164; IntAct: EBI-20589,EBI-17187; Score: 0.35
DE  Interaction: P29478; IntAct: EBI-20589,EBI-16641; Score: 0.35
DE  Interaction: Q99216; IntAct: EBI-20589,EBI-31176; Score: 0.35
DE  Interaction: P34072; IntAct: EBI-20589,EBI-10978; Score: 0.35
DE  Interaction: Q02805; IntAct: EBI-20589,EBI-15679; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-20589,EBI-16136; Score: 0.35
DE  Interaction: Q08444; IntAct: EBI-20589,EBI-29777; Score: 0.35
DE  Interaction: P54000; IntAct: EBI-20589,EBI-18492; Score: 0.35
DE  Interaction: Q02884; IntAct: EBI-20589,EBI-35277; Score: 0.35
DE  Interaction: P10962; IntAct: EBI-20589,EBI-10937; Score: 0.35
DE  Interaction: P49955; IntAct: EBI-20589,EBI-664; Score: 0.35
DE  Interaction: Q08484; IntAct: EBI-20589,EBI-8005; Score: 0.35
DE  Interaction: P47135; IntAct: EBI-20589,EBI-9422; Score: 0.35
DE  Interaction: P53050; IntAct: EBI-20589,EBI-10850; Score: 0.35
DE  Interaction: Q99186; IntAct: EBI-20589,EBI-2715; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-20589,EBI-20415; Score: 0.35
DE  Interaction: Q08235; IntAct: EBI-20589,EBI-3775; Score: 0.35
DE  Interaction: P40187; IntAct: EBI-20589,EBI-13419; Score: 0.35
DE  Interaction: P07270; IntAct: EBI-20589,EBI-13378; Score: 0.35
DE  Interaction: P32566; IntAct: EBI-20589,EBI-17452; Score: 0.35
DE  Interaction: P46946; IntAct: EBI-20589,EBI-16440; Score: 0.35
DE  Interaction: Q12481; IntAct: EBI-20589,EBI-31770; Score: 0.35
DE  Interaction: Q04007; IntAct: EBI-20589,EBI-35560; Score: 0.35
DE  Interaction: P48562; IntAct: EBI-20589,EBI-4750; Score: 0.35
DE  Interaction: P25293; IntAct: EBI-20589,EBI-11850; Score: 0.35
DE  Interaction: P32790; IntAct: EBI-20589,EBI-17313; Score: 0.35
DE  Interaction: P50896; IntAct: EBI-20589,EBI-14046; Score: 0.35
DE  Interaction: P80235; IntAct: EBI-20589,EBI-3928; Score: 0.35
DE  Interaction: Q04304; IntAct: EBI-20589,EBI-28179; Score: 0.35
DE  Interaction: P43563; IntAct: EBI-20589,EBI-11125; Score: 0.35
DE  Interaction: P34243; IntAct: EBI-20589,EBI-26601; Score: 0.35
DE  Interaction: Q02354; IntAct: EBI-20589,EBI-22119; Score: 0.35
DE  Interaction: P53829; IntAct: EBI-20589,EBI-28306; Score: 0.35
DE  Interaction: P53741; IntAct: EBI-20589,EBI-28528; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-20589,EBI-6302; Score: 0.35
DE  Interaction: Q02875; IntAct: EBI-20589,EBI-33176; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-20589,EBI-7458; Score: 0.35
DE  Interaction: P17536; IntAct: EBI-20589,EBI-19408; Score: 0.35
DE  Interaction: P38080; IntAct: EBI-20589,EBI-9528; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-20589,EBI-15427; Score: 0.35
DE  Interaction: Q12186; IntAct: EBI-20589,EBI-34012; Score: 0.35
DE  Interaction: P53924; IntAct: EBI-20589,EBI-28867; Score: 0.35
DE  Interaction: P39960; IntAct: EBI-20589,EBI-3517; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-20589,EBI-25778; Score: 0.35
DE  Interaction: Q07807; IntAct: EBI-20589,EBI-38012; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-20589,EBI-11659; Score: 0.35
DE  Interaction: P53894; IntAct: EBI-20589,EBI-4110; Score: 0.35
DE  Interaction: P06844; IntAct: EBI-20589,EBI-17921; Score: 0.35
DE  Interaction: P40084; IntAct: EBI-20589,EBI-22713; Score: 0.35
DE  Interaction: P20053; IntAct: EBI-20589,EBI-219; Score: 0.35
DE  Interaction: Q03233; IntAct: EBI-20589,EBI-27402; Score: 0.35
DE  Interaction: P51401; IntAct: EBI-20589,EBI-15443; Score: 0.35
DE  Interaction: P32794; IntAct: EBI-20589,EBI-2310; Score: 0.35
DE  Interaction: Q12259; IntAct: EBI-20589,EBI-30776; Score: 0.35
DE  Interaction: P22204; IntAct: EBI-20589,EBI-5569; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-20589,EBI-28537; Score: 0.35
DE  Interaction: Q08951; IntAct: EBI-20589,EBI-29702; Score: 0.35
DE  Interaction: P09959; IntAct: EBI-20589,EBI-18641; Score: 0.35
DE  Interaction: Q12753; IntAct: EBI-20589,EBI-8118; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-20589,EBI-16993; Score: 0.35
DE  Interaction: P25644; IntAct: EBI-20589,EBI-204; Score: 0.35
DE  Interaction: P40339; IntAct: EBI-20589,EBI-15009; Score: 0.35
DE  Interaction: P36115; IntAct: EBI-20589,EBI-27090; Score: 0.35
DE  Interaction: Q08438; IntAct: EBI-20589,EBI-30482; Score: 0.35
DE  Interaction: P38688; IntAct: EBI-20589,EBI-18011; Score: 0.35
DE  Interaction: Q07362; IntAct: EBI-20589,EBI-37896; Score: 0.35
DE  Interaction: P50079; IntAct: EBI-20589,EBI-23505; Score: 0.35
DE  Interaction: P36119; IntAct: EBI-20589,EBI-26366; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-20589,EBI-16037; Score: 0.35
DE  Interaction: P09547; IntAct: EBI-20589,EBI-18617; Score: 0.35
DE  Interaction: P40449; IntAct: EBI-20589,EBI-25311; Score: 0.35
DE  Interaction: P38263; IntAct: EBI-20589,EBI-20304; Score: 0.35
DE  Interaction: P17076; IntAct: EBI-20589,EBI-15431; Score: 0.35
DE  Interaction: P13663; IntAct: EBI-5803,EBI-20589; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-26585,EBI-20589; Score: 0.35
DE  Interaction: P36013; IntAct: EBI-10412,EBI-20589; Score: 0.35
DE  Interaction: P38085; IntAct: EBI-20222,EBI-20589; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-2098,EBI-20589; Score: 0.35
DE  Interaction: Q07804; IntAct: EBI-36254,EBI-20589; Score: 0.35
DE  Interaction: P33417; IntAct: EBI-9401,EBI-20589; Score: 0.35
DE  Interaction: P38707; IntAct: EBI-18775,EBI-20589; Score: 0.35
DE  Interaction: P38703; IntAct: EBI-10035,EBI-20589; Score: 0.35
DE  Interaction: P0CI39; IntAct: EBI-18360,EBI-20589; Score: 0.35
DE  Interaction: P52593; IntAct: EBI-11763,EBI-20589; Score: 0.35
DE  Interaction: Q03529; IntAct: EBI-16747,EBI-20589; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-20589,EBI-6314; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-20589,EBI-10789; Score: 0.35
DE  Interaction: Q01939; IntAct: EBI-20589,EBI-13914; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-20589,EBI-13910; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-20589,EBI-11191; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-20589,EBI-25128; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-20589,EBI-8666; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-20589,EBI-7442; Score: 0.44
DE  Interaction: P00549; IntAct: EBI-20589,EBI-9890; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-20589,EBI-20254; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-20589,EBI-14372; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-20589,EBI-18986; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-20589,EBI-18976; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-20589,EBI-9017; Score: 0.35
DE  Interaction: P32454; IntAct: EBI-2641,EBI-20589; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-10067,EBI-20589; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-24359,EBI-20589; Score: 0.27
DE  Interaction: Q00955; IntAct: EBI-4814,EBI-20589; Score: 0.27
DE  Interaction: P39722; IntAct: EBI-20685,EBI-20589; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-2293,EBI-20589; Score: 0.27
DE  Interaction: P60010; IntAct: EBI-2169,EBI-20589; Score: 0.27
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005816;
GO  GO:0005049;
GO  GO:0061608;
GO  GO:0008536;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0034501;
GO  GO:0046825;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFSTNPQSKFIALSILDKLITRKWK
SQ  LLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKSDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLK
SQ  LLSEEVFDFSAEQMTQAKALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELLST
SQ  KFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLKATYANANGNDQSFLQDLAMFLT
SQ  TYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELFKTTLDYWHNLVADLFYEVQRLPATEMSPLIQLSVGSQAIST
SQ  GSGALNPEYMKRFPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLTHLNV
SQ  IDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVG
SQ  QYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQ
SQ  VHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGADFYPQ
SQ  LGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYM
SQ  NNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPA
SQ  AFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQALLLM
SQ  KLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIK
SQ  EVGGDPTDYLFAEDKENALMEQNRLEREKAAKIGGLLKPSELDD
//
ID  Q8NFU3;
PN  Thiosulfate:glutathione sulfurtransferase;
GN  TSTD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12817473}. Note=Localized around the nuclear membranes.
DR  UNIPROT: Q8NFU3;
DR  UNIPROT: Q5SY48;
DR  UNIPROT: Q5SY49;
DR  UNIPROT: Q5SY50;
DR  UNIPROT: Q5SY51;
DR  UNIPROT: Q8NFU2;
DR  UNIPROT: Q9BV22;
DR  PDB: 6BEV;
DR  Pfam: PF00581;
DR  PROSITE: PS50206;
DR  OMIM: 616041;
DR  DisGeNET: 100131187;
DE  Function: Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism (PubMed:24981631). Provides the link between the first step in mammalian H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate (PubMed:24981631). The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor (PubMed:24981631). {ECO:0000269|PubMed:24981631}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0050337;
GO  GO:0070221;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEHLVFFCQ
SQ  MGKRGLQATQLARSLGYTGARNYAGAYREWLEKES
//
ID  P57088;
PN  Transmembrane protein 33;
GN  TMEM33;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus envelope {ECO:0000269|PubMed:25612671}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Co-localizes with RTN4 at the ER sheets. {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:25612671}.
DR  UNIPROT: P57088;
DR  UNIPROT: B3KSS8;
DR  UNIPROT: Q9H953;
DR  Pfam: PF03661;
DR  OMIM: 618515;
DR  DisGeNET: 55161;
DE  Function: Acts as a regulator of the tubular endoplasmic reticulum (ER) network. Suppresses the RTN3/4-induced formation of the ER tubules (PubMed:25612671). Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling (PubMed:26268696). {ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-1048629; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-641062,EBI-1048629; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-349854,EBI-1048629; Score: 0.35
DE  Interaction: E9PS44; IntAct: EBI-21260290,EBI-1048629; Score: 0.35
DE  Interaction: O94966; IntAct: EBI-2511895,EBI-1048629; Score: 0.40
DE  Interaction: P62263; IntAct: EBI-1048629,EBI-352783; Score: 0.37
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-1048629; Score: 0.35
DE  Interaction: Q9CR14; IntAct: EBI-7529579,EBI-1048629; Score: 0.35
DE  Interaction: Q99549; IntAct: EBI-2653928,EBI-1048629; Score: 0.35
DE  Interaction: O55143; IntAct: EBI-770763,EBI-1048629; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-749204,EBI-1048629; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-1048629; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-1048629; Score: 0.35
DE  Interaction: Q8ZC32; IntAct: EBI-2852171,EBI-1048629; Score: 0.37
DE  Interaction: Q5NIP6; IntAct: EBI-2796567,EBI-1048629; Score: 0.37
DE  Interaction: P48039; IntAct: EBI-1188238,EBI-1048629; Score: 0.66
DE  Interaction: Q9BUV8; IntAct: EBI-1048629,EBI-1050079; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-1048629,EBI-307369; Score: 0.40
DE  Interaction: P11171; IntAct: EBI-1048629,EBI-1050906; Score: 0.40
DE  Interaction: P62140; IntAct: EBI-1048629,EBI-352350; Score: 0.40
DE  Interaction: Q9Y5J5; IntAct: EBI-1048629,EBI-1055859; Score: 0.40
DE  Interaction: Q99608; IntAct: EBI-1048629,EBI-718177; Score: 0.40
DE  Interaction: Q9P1U1; IntAct: EBI-1047175,EBI-1048629; Score: 0.40
DE  Interaction: Q9UET6; IntAct: EBI-1048629,EBI-1055987; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-1048629,EBI-447544; Score: 0.40
DE  Interaction: Q15714; IntAct: EBI-1048629,EBI-712609; Score: 0.40
DE  Interaction: Q9HAW0; IntAct: EBI-1048629,EBI-1055224; Score: 0.40
DE  Interaction: O75365; IntAct: EBI-1048629,EBI-1043866; Score: 0.40
DE  Interaction: Q15008; IntAct: EBI-1048629,EBI-359701; Score: 0.40
DE  Interaction: Q71U36; IntAct: EBI-302552,EBI-1048629; Score: 0.35
DE  Interaction: P30086; IntAct: EBI-716384,EBI-1048629; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-365996,EBI-1048629; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-301834,EBI-1048629; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-603607,EBI-1048629; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-446668,EBI-1048629; Score: 0.35
DE  Interaction: P15056; IntAct: EBI-365980,EBI-1048629; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-625518,EBI-1048629; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-1213983,EBI-1048629; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-726632,EBI-1048629; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-1307,EBI-1048629; Score: 0.35
DE  Interaction: P49023; IntAct: EBI-702209,EBI-1048629; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-358011,EBI-1048629; Score: 0.35
DE  Interaction: Q6KAU7-1; IntAct: EBI-25408849,EBI-1048629; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25475871,EBI-1048629; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25475894,EBI-1048629; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25475914,EBI-1048629; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25475917,EBI-1048629; Score: 0.35
DE  Interaction: Q96FB2; IntAct: EBI-1048629,EBI-2857623; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-486984,EBI-1048629; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:1903896;
GO  GO:1903899;
GO  GO:1903371;
GO  GO:0034976;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLS
SQ  RAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDARGSNSLPLLRSVLDKLSANQQNILKFI
SQ  ACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRTLFNELRIVVEHIIMKPACPLFVRRLCLQSIAFIS
SQ  RLAPTVP
//
ID  Q8TEY7;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  USP33;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19118533}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23486064}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (PubMed:23486064). {ECO:0000269|PubMed:23486064}. [Isoform 3]: Golgi apparatus {ECO:0000269|PubMed:21801292}.
DR  UNIPROT: Q8TEY7;
DR  UNIPROT: Q8TEY6;
DR  UNIPROT: Q96AV6;
DR  UNIPROT: Q9H9F0;
DR  UNIPROT: Q9UPQ5;
DR  PDB: 2UZG;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DR  OMIM: 615146;
DR  DisGeNET: 23032;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:23486064}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5W0B1; IntAct: EBI-719283,EBI-2562035; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-719283,EBI-529989; Score: 0.37
DE  Interaction: Q13228; IntAct: EBI-719283,EBI-711619; Score: 0.37
DE  Interaction: Q13325; IntAct: EBI-719283,EBI-725916; Score: 0.40
DE  Interaction: Q96KR1; IntAct: EBI-719283,EBI-2513582; Score: 0.40
DE  Interaction: Q13601; IntAct: EBI-719283,EBI-744525; Score: 0.40
DE  Interaction: Q5VTL8; IntAct: EBI-719283,EBI-1045334; Score: 0.40
DE  Interaction: Q9NY93; IntAct: EBI-719283,EBI-372376; Score: 0.37
DE  Interaction: Q13352; IntAct: EBI-719283,EBI-712105; Score: 0.37
GO  GO:0044297;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030891;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0017160;
GO  GO:0004843;
GO  GO:0036459;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0009267;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0032091;
GO  GO:0032092;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0050821;
GO  GO:0010506;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGTCQDCKVQGPNLWACLENRCS
SQ  YVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKT
SQ  PLVAVFDDLDIEADEEDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELW
SQ  HKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTITTEETMEEDKSQSDVDFQS
SQ  CESCSNSDRAENENGSRCFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVNSEGEFDKDRDSISETVDLNNQETV
SQ  KVQIHSRASEYITDVHSNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFD
SQ  GTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPS
SQ  WFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL
SQ  DLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQ
SQ  KERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGG
SQ  GPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQKEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAV
SQ  TKCGNVMLRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL
//
ID  Q9NRR5;
PN  Ubiquilin-4;
GN  UBQLN4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11001934, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}. Cytoplasm {ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}. Chromosome {ECO:0000269|PubMed:30612738}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23459205}. Note=Colocalizes with the proteasome, both in nucleus and cytoplasm (PubMed:15280365). Exported from the nucleus following interaction with DESI1/POST (PubMed:29666234). In response to DNA damage and phosphorylation at Ser-318 by ATM, localizes to the nucleus and is recruited to sites of DNA damage (PubMed:30612738). {ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}.
DR  UNIPROT: Q9NRR5;
DR  UNIPROT: A6ND44;
DR  UNIPROT: B2RAY7;
DR  UNIPROT: Q5VYA0;
DR  UNIPROT: Q5VYA1;
DR  UNIPROT: Q9BR98;
DR  UNIPROT: Q9UHX4;
DR  Pfam: PF00627;
DR  Pfam: PF00240;
DR  PROSITE: PS50030;
DR  PROSITE: PS50053;
DR  OMIM: 105400;
DR  OMIM: 605440;
DR  DisGeNET: 56893;
DE  Function: Regulator of protein degradation that mediates the proteasomal targeting of misfolded, mislocalized or accumulated proteins (PubMed:15280365, PubMed:27113755, PubMed:29666234, PubMed:30612738). Acts by binding polyubiquitin chains of target proteins via its UBA domain and by interacting with subunits of the proteasome via its ubiquitin-like domain (PubMed:15280365, PubMed:27113755, PubMed:30612738). Key regulator of DNA repair that represses homologous recombination repair: in response to DNA damage, recruited to sites of DNA damage following phosphorylation by ATM and acts by binding and removing ubiquitinated MRE11 from damaged chromatin, leading to MRE11 degradation by the proteasome (PubMed:30612738). MRE11 degradation prevents homologous recombination repair, redirecting double-strand break repair toward non-homologous end joining (NHEJ) (PubMed:30612738). Specifically recognizes and binds mislocalized transmembrane-containing proteins and targets them to proteasomal degradation (PubMed:27113755). Collaborates with DESI1/POST in the export of ubiquitinated proteins from the nucleus to the cytoplasm (PubMed:29666234). Also plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery (PubMed:23459205). Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:23459205). {ECO:0000250|UniProtKB:Q99NB8, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:27113755, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}.
DE  Disease: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:28463112}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. Note=Defects in UBQLN4 are the cause of the UBQLN4 deficiency syndrome (UBDS) (PubMed:30612738). Patients display intellectual impairment, growth retardation, microcephaly, facial dysmorphism, hearing loss, ataxia and anemia (PubMed:30612738). Cells display genomic instability characterized by hypersensitivity to genotoxic agents, leading to enhanced apoptotic cell death in response to DNA damage (PubMed:30612738). {ECO:0000269|PubMed:30612738}.
DE  Reference Proteome: Yes;
DE  Interaction: P53816; IntAct: EBI-711226,EBI-746318; Score: 0.37
DE  Interaction: Q09013; IntAct: EBI-692774,EBI-711226; Score: 0.37
DE  Interaction: Q9NRD5; IntAct: EBI-79165,EBI-711226; Score: 0.37
DE  Interaction: Self; IntAct: EBI-711226,EBI-711226; Score: 0.68
DE  Interaction: P54253; IntAct: EBI-930964,EBI-711226; Score: 0.59
DE  Interaction: P26885; IntAct: EBI-719873,EBI-711226; Score: 0.51
DE  Interaction: P55198; IntAct: EBI-740216,EBI-711226; Score: 0.51
DE  Interaction: Q9NR12; IntAct: EBI-350517,EBI-711226; Score: 0.51
DE  Interaction: Q13049; IntAct: EBI-711226,EBI-742790; Score: 0.51
DE  Interaction: O95201; IntAct: EBI-747343,EBI-711226; Score: 0.51
DE  Interaction: Q9BRR6; IntAct: EBI-711226,EBI-723761; Score: 0.37
DE  Interaction: O95994; IntAct: EBI-711226,EBI-712648; Score: 0.37
DE  Interaction: P15514; IntAct: EBI-711226,EBI-953674; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-711226,EBI-347552; Score: 0.49
DE  Interaction: Q56P03; IntAct: EBI-711226,EBI-748732; Score: 0.37
DE  Interaction: Q8N806; IntAct: EBI-711226,EBI-953685; Score: 0.37
DE  Interaction: Q969H8; IntAct: EBI-711226,EBI-718622; Score: 0.37
DE  Interaction: Q9BXJ1; IntAct: EBI-711226,EBI-750200; Score: 0.37
DE  Interaction: Q06455; IntAct: EBI-711226,EBI-743342; Score: 0.37
DE  Interaction: O00585; IntAct: EBI-711226,EBI-953695; Score: 0.37
DE  Interaction: P14209; IntAct: EBI-711226,EBI-748547; Score: 0.37
DE  Interaction: Q15517; IntAct: EBI-711226,EBI-953708; Score: 0.37
DE  Interaction: P27658; IntAct: EBI-711226,EBI-747133; Score: 0.37
DE  Interaction: P33240; IntAct: EBI-711226,EBI-711360; Score: 0.37
DE  Interaction: Q9H0L4; IntAct: EBI-711226,EBI-747012; Score: 0.49
DE  Interaction: Q15038; IntAct: EBI-711226,EBI-724310; Score: 0.37
DE  Interaction: Q86UW9; IntAct: EBI-711226,EBI-740376; Score: 0.37
DE  Interaction: P05305; IntAct: EBI-711226,EBI-715181; Score: 0.37
DE  Interaction: Q9UKW6; IntAct: EBI-711226,EBI-747605; Score: 0.37
DE  Interaction: Q14512; IntAct: EBI-711226,EBI-953742; Score: 0.37
DE  Interaction: Q7L4I2; IntAct: EBI-711226,EBI-953753; Score: 0.37
DE  Interaction: Q53HC5; IntAct: EBI-711226,EBI-724915; Score: 0.37
DE  Interaction: Q9H6E4; IntAct: EBI-711226,EBI-953766; Score: 0.37
DE  Interaction: Q96DN0; IntAct: EBI-711226,EBI-953772; Score: 0.37
DE  Interaction: Q8N5R6; IntAct: EBI-711226,EBI-740841; Score: 0.37
DE  Interaction: O75084; IntAct: EBI-711226,EBI-746917; Score: 0.37
DE  Interaction: O14764; IntAct: EBI-711226,EBI-744352; Score: 0.37
DE  Interaction: Q96SL4; IntAct: EBI-711226,EBI-749411; Score: 0.37
DE  Interaction: Q96D42; IntAct: EBI-711226,EBI-953786; Score: 0.37
DE  Interaction: P52789; IntAct: EBI-711226,EBI-741469; Score: 0.37
DE  Interaction: P24592; IntAct: EBI-711226,EBI-947015; Score: 0.49
DE  Interaction: P01871; IntAct: EBI-953797,EBI-711226; Score: 0.37
DE  Interaction: Q9P2K6; IntAct: EBI-711226,EBI-739890; Score: 0.37
DE  Interaction: Q6GPH6; IntAct: EBI-711226,EBI-953819; Score: 0.37
DE  Interaction: Q96DA0; IntAct: EBI-711226,EBI-953824; Score: 0.37
DE  Interaction: P21741; IntAct: EBI-711226,EBI-722444; Score: 0.49
DE  Interaction: Q13232; IntAct: EBI-713684,EBI-711226; Score: 0.49
DE  Interaction: O15259; IntAct: EBI-711226,EBI-953828; Score: 0.37
DE  Interaction: P01160; IntAct: EBI-711226,EBI-953859; Score: 0.37
DE  Interaction: Q9UHQ9; IntAct: EBI-711226,EBI-953870; Score: 0.37
DE  Interaction: Q9UBU9; IntAct: EBI-711226,EBI-398874; Score: 0.37
DE  Interaction: Q14554; IntAct: EBI-711226,EBI-953879; Score: 0.37
DE  Interaction: Q9HAT8; IntAct: EBI-711226,EBI-448407; Score: 0.37
DE  Interaction: Q13526; IntAct: EBI-711226,EBI-714158; Score: 0.37
DE  Interaction: Q9NP55; IntAct: EBI-711226,EBI-953896; Score: 0.37
DE  Interaction: P23284; IntAct: EBI-711226,EBI-359252; Score: 0.37
DE  Interaction: P45877; IntAct: EBI-711226,EBI-953909; Score: 0.37
DE  Interaction: P10124; IntAct: EBI-711226,EBI-744915; Score: 0.37
DE  Interaction: Q13876; IntAct: EBI-711226,EBI-953919; Score: 0.37
DE  Interaction: Q9Y5P3; IntAct: EBI-711226,EBI-746228; Score: 0.49
DE  Interaction: Q9NPQ8; IntAct: EBI-711226,EBI-717509; Score: 0.37
DE  Interaction: Q15287; IntAct: EBI-711226,EBI-395959; Score: 0.37
DE  Interaction: P04843; IntAct: EBI-711226,EBI-355963; Score: 0.37
DE  Interaction: Q96GD3; IntAct: EBI-711226,EBI-713793; Score: 0.37
DE  Interaction: P04279; IntAct: EBI-711226,EBI-953955; Score: 0.37
DE  Interaction: P05121; IntAct: EBI-711226,EBI-953978; Score: 0.37
DE  Interaction: O75830; IntAct: EBI-711226,EBI-750144; Score: 0.37
DE  Interaction: P05408; IntAct: EBI-711226,EBI-722635; Score: 0.55
DE  Interaction: Q96C03; IntAct: EBI-711226,EBI-750153; Score: 0.37
DE  Interaction: O43278; IntAct: EBI-711226,EBI-953990; Score: 0.37
DE  Interaction: P10451; IntAct: EBI-711226,EBI-723648; Score: 0.49
DE  Interaction: P48723; IntAct: EBI-711226,EBI-750892; Score: 0.37
DE  Interaction: P04155; IntAct: EBI-711226,EBI-743871; Score: 0.37
DE  Interaction: Q969W9; IntAct: EBI-711226,EBI-954013; Score: 0.37
DE  Interaction: Q96IX5; IntAct: EBI-711226,EBI-954033; Score: 0.37
DE  Interaction: P01282; IntAct: EBI-711226,EBI-751454; Score: 0.37
DE  Interaction: O60844; IntAct: EBI-711226,EBI-746479; Score: 0.37
DE  Interaction: Q16630; IntAct: EBI-358410,EBI-711226; Score: 0.37
DE  Interaction: Q9UBP4; IntAct: EBI-954409,EBI-711226; Score: 0.37
DE  Interaction: O95967; IntAct: EBI-743414,EBI-711226; Score: 0.37
DE  Interaction: Q5VSY0; IntAct: EBI-743722,EBI-711226; Score: 0.49
DE  Interaction: P78356; IntAct: EBI-947090,EBI-711226; Score: 0.49
DE  Interaction: Q99932; IntAct: EBI-954419,EBI-711226; Score: 0.37
DE  Interaction: O75886; IntAct: EBI-711226,EBI-373258; Score: 0.37
DE  Interaction: Q9UMX0; IntAct: EBI-741480,EBI-711226; Score: 0.72
DE  Interaction: Q9GZY6; IntAct: EBI-954435,EBI-711226; Score: 0.37
DE  Interaction: Q6GMX4; IntAct: EBI-711226,EBI-954686; Score: 0.37
DE  Interaction: Q6P1W5; IntAct: EBI-946029,EBI-711226; Score: 0.37
DE  Interaction: A9UHW6; IntAct: EBI-373498,EBI-711226; Score: 0.37
DE  Interaction: Q9BZ11; IntAct: EBI-946778,EBI-711226; Score: 0.37
DE  Interaction: P56559; IntAct: EBI-946814,EBI-711226; Score: 0.37
DE  Interaction: Q9UII2; IntAct: EBI-718459,EBI-711226; Score: 0.37
DE  Interaction: Q8N111; IntAct: EBI-946825,EBI-711226; Score: 0.37
DE  Interaction: P30040; IntAct: EBI-711226,EBI-946830; Score: 0.37
DE  Interaction: O43497; IntAct: EBI-946847,EBI-711226; Score: 0.37
DE  Interaction: Q49A88; IntAct: EBI-751035,EBI-711226; Score: 0.37
DE  Interaction: P53618; IntAct: EBI-359063,EBI-711226; Score: 0.37
DE  Interaction: Q9P021; IntAct: EBI-946968,EBI-711226; Score: 0.37
DE  Interaction: Q9UM22; IntAct: EBI-946972,EBI-711226; Score: 0.37
DE  Interaction: Q8NEM7; IntAct: EBI-946984,EBI-711226; Score: 0.37
DE  Interaction: O75400; IntAct: EBI-473291,EBI-711226; Score: 0.55
DE  Interaction: P31150; IntAct: EBI-946999,EBI-711226; Score: 0.37
DE  Interaction: O14964; IntAct: EBI-740220,EBI-711226; Score: 0.37
DE  Interaction: Q16891; IntAct: EBI-473801,EBI-711226; Score: 0.37
DE  Interaction: Q6ZTN6; IntAct: EBI-947028,EBI-711226; Score: 0.37
DE  Interaction: Q8WV48; IntAct: EBI-947033,EBI-711226; Score: 0.37
DE  Interaction: Q9H6J7; IntAct: EBI-721300,EBI-711226; Score: 0.37
DE  Interaction: Q96BY2; IntAct: EBI-739825,EBI-711226; Score: 0.37
DE  Interaction: Q96JN2; IntAct: EBI-947045,EBI-711226; Score: 0.37
DE  Interaction: Q15155; IntAct: EBI-373107,EBI-711226; Score: 0.37
DE  Interaction: P69849; IntAct: EBI-947048,EBI-711226; Score: 0.37
DE  Interaction: Q7Z3S9; IntAct: EBI-945833,EBI-711226; Score: 0.37
DE  Interaction: P04181; IntAct: EBI-721662,EBI-711226; Score: 0.37
DE  Interaction: Q96AQ6; IntAct: EBI-740845,EBI-711226; Score: 0.37
DE  Interaction: O14917; IntAct: EBI-947061,EBI-711226; Score: 0.37
DE  Interaction: O95206; IntAct: EBI-947069,EBI-711226; Score: 0.37
DE  Interaction: Q8ND90; IntAct: EBI-302345,EBI-711226; Score: 0.37
DE  Interaction: P21246; IntAct: EBI-473725,EBI-711226; Score: 0.55
DE  Interaction: Q16849; IntAct: EBI-728153,EBI-711226; Score: 0.37
DE  Interaction: Q92932; IntAct: EBI-310576,EBI-711226; Score: 0.37
DE  Interaction: P98175; IntAct: EBI-721525,EBI-711226; Score: 0.37
DE  Interaction: Q9HCK4; IntAct: EBI-399800,EBI-711226; Score: 0.37
DE  Interaction: P13521; IntAct: EBI-947132,EBI-711226; Score: 0.37
DE  Interaction: Q01130; IntAct: EBI-627047,EBI-711226; Score: 0.37
DE  Interaction: Q9H7N4; IntAct: EBI-1222181,EBI-711226; Score: 0.37
DE  Interaction: P16949; IntAct: EBI-445909,EBI-711226; Score: 0.37
DE  Interaction: O43294; IntAct: EBI-1051449,EBI-711226; Score: 0.37
DE  Interaction: Q9UPQ9; IntAct: EBI-947158,EBI-711226; Score: 0.37
DE  Interaction: Q12933; IntAct: EBI-355744,EBI-711226; Score: 0.37
DE  Interaction: Q92519; IntAct: EBI-947178,EBI-711226; Score: 0.37
DE  Interaction: Q9UHD9; IntAct: EBI-947187,EBI-711226; Score: 0.37
DE  Interaction: P10746; IntAct: EBI-947201,EBI-711226; Score: 0.37
DE  Interaction: Q9BTA9; IntAct: EBI-749118,EBI-711226; Score: 0.37
DE  Interaction: P27348; IntAct: EBI-359854,EBI-711226; Score: 0.37
DE  Interaction: Q9NYG2; IntAct: EBI-740248,EBI-711226; Score: 0.37
DE  Interaction: Q8WW38; IntAct: EBI-947213,EBI-711226; Score: 0.37
DE  Interaction: P54725; IntAct: EBI-746453,EBI-711226; Score: 0.37
DE  Interaction: P12268; IntAct: EBI-353389,EBI-711226; Score: 0.37
DE  Interaction: P13569; IntAct: EBI-349854,EBI-711226; Score: 0.35
DE  Interaction: Q5VZL5; IntAct: EBI-2514659,EBI-711226; Score: 0.35
DE  Interaction: Q13404; IntAct: EBI-1050671,EBI-711226; Score: 0.44
DE  Interaction: Q62925; IntAct: EBI-636664,EBI-711226; Score: 0.44
DE  Interaction: P08050; IntAct: EBI-711226,EBI-476947; Score: 0.40
DE  Interaction: P83917; IntAct: EBI-78119,EBI-711226; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-354921,EBI-711226; Score: 0.35
DE  Interaction: P84022; IntAct: EBI-711226,EBI-347161; Score: 0.37
DE  Interaction: O43913; IntAct: EBI-711226,EBI-374928; Score: 0.37
DE  Interaction: Q13564; IntAct: EBI-718631,EBI-711226; Score: 0.37
DE  Interaction: O15209; IntAct: EBI-711226,EBI-723574; Score: 0.37
DE  Interaction: P49286; IntAct: EBI-711226,EBI-1188341; Score: 0.37
DE  Interaction: O00624-2; IntAct: EBI-21654602,EBI-711226; Score: 0.35
DE  Interaction: P24390; IntAct: EBI-1043076,EBI-711226; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-352162,EBI-711226; Score: 0.37
DE  Interaction: Q13432; IntAct: EBI-711260,EBI-711226; Score: 0.37
DE  Interaction: P19793; IntAct: EBI-78598,EBI-711226; Score: 0.37
DE  Interaction: Q12824; IntAct: EBI-358419,EBI-711226; Score: 0.37
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0090734;
GO  GO:0042802;
GO  GO:0031593;
GO  GO:0006914;
GO  GO:0006974;
GO  GO:0006281;
GO  GO:1901097;
GO  GO:2000042;
GO  GO:0032434;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPSGAETRPPIRVTVKTPKDKEEIVICDRASVKEFKEEISRRFKAQQDQLVLIFAGKILKDGDTLNQHGIKDGLTVHL
SQ  VIKTPQKAQDPAAATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGSGSRRSSGGGPSPGAGEGSPSATASILS
SQ  GFGGILGLGSLGLGSANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLMRHMIMANPQMQQLMERNPEISHMLN
SQ  NPELMRQTMELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMFSAAREQFGNNPFSSLAGNSDSSSSQP
SQ  LRTENREPLPNPWSPSPPTSQAPGSGGEGTGGSGTSQVHPTVSNPFGINAASLGSGMFNSPEMQALLQQISENPQLMQNV
SQ  ISAPYMRSMMQTLAQNPDFAAQMMVNVPLFAGNPQLQEQLRLQLPVFLQQMQNPESLSILTNPRAMQALLQIQQGLQTLQ
SQ  TEAPGLVPSLGSFGISRTPAPSAGSNAGSTPEAPTSSPATPATSSPTGASSAQQQLMQQMIQLLAGSGNSQVQTPEVRFQ
SQ  QQLEQLNSMGFINREANLQALIATGGDINAAIERLLGSQLS
//
ID  G5EFV8;
PN  Vacuolar protein sorting-associated protein 52 homolog;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. {ECO:0000269|PubMed:27191843}.
DR  UNIPROT: G5EFV8;
DR  UNIPROT: G5EFV9;
DR  Pfam: PF04129;
DE  Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
DE  Reference Proteome: Yes;
DE  Interaction: O01839; IntAct: EBI-313277,EBI-318981; Score: 0.73
DE  Interaction: Q09501; IntAct: EBI-318986,EBI-318981; Score: 0.37
DE  Interaction: P32743; IntAct: EBI-318996,EBI-318981; Score: 0.37
DE  Interaction: O61975; IntAct: EBI-318991,EBI-318981; Score: 0.37
DE  Interaction: Q20742; IntAct: EBI-312606,EBI-318981; Score: 0.37
DE  Interaction: Q22227; IntAct: EBI-316403,EBI-318981; Score: 0.37
DE  Interaction: Q22544; IntAct: EBI-313477,EBI-318981; Score: 0.37
DE  Interaction: P91820; IntAct: EBI-313618,EBI-318981; Score: 0.37
DE  Interaction: P34574; IntAct: EBI-319001,EBI-318981; Score: 0.37
DE  Interaction: Q9N575; IntAct: EBI-319010,EBI-318981; Score: 0.37
GO  GO:0005829;
GO  GO:0000938;
GO  GO:0005797;
GO  GO:0000138;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0017137;
GO  GO:0019905;
GO  GO:0032456;
GO  GO:0006896;
GO  GO:0007041;
GO  GO:1904810;
GO  GO:1904811;
GO  GO:0090326;
GO  GO:0015031;
GO  GO:0042147;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQL
SQ  HNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDAND
SQ  RGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEF
SQ  LLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFS
SQ  IGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVL
SQ  KSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDA
SQ  RPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESK
SQ  HTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECI
SQ  QLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY
//
ID  O75569;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
GN  PRKRA;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm.
DR  UNIPROT: O75569;
DR  UNIPROT: A8K3I6;
DR  UNIPROT: Q53G24;
DR  UNIPROT: Q6X7T5;
DR  UNIPROT: Q8NDK4;
DR  PDB: 2DIX;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DR  OMIM: 603424;
DR  OMIM: 612067;
DR  DisGeNET: 8575;
DE  Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys- 386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:11238927, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:16982605, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:9687506}.
DE  Disease: Dystonia 16 (DYT16) [MIM:612067]: An early-onset dystonia- parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT16 patients have progressive, generalized dystonia with axial muscle involvement, oro-mandibular (sardonic smile) and laryngeal dystonia and, in some cases, parkinsonian features. {ECO:0000269|PubMed:18243799, ECO:0000269|PubMed:18420150}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-713955,EBI-713955; Score: 0.80
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-713955; Score: 0.35
DE  Interaction: P60953-1; IntAct: EBI-3625591,EBI-713955; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-395506,EBI-713955; Score: 0.74
DE  Interaction: Q9HA38; IntAct: EBI-2548480,EBI-713955; Score: 0.56
DE  Interaction: Q9NX58; IntAct: EBI-713955,EBI-713507; Score: 0.74
DE  Interaction: Q15633; IntAct: EBI-713955,EBI-978581; Score: 0.89
DE  Interaction: Q92731; IntAct: EBI-78505,EBI-713955; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-2547442,EBI-713955; Score: 0.67
DE  Interaction: P03485; IntAct: EBI-713955,EBI-2547543; Score: 0.37
DE  Interaction: P03495; IntAct: EBI-713955,EBI-2548993; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-347928,EBI-713955; Score: 0.37
DE  Interaction: Q8TES7; IntAct: EBI-2350063,EBI-713955; Score: 0.35
DE  Interaction: P61965; IntAct: EBI-1247084,EBI-713955; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-356625,EBI-713955; Score: 0.35
DE  Interaction: Q9H898-2; IntAct: EBI-11529334,EBI-713955; Score: 0.60
DE  Interaction: P19525; IntAct: EBI-640775,EBI-713955; Score: 0.74
DE  Interaction: O56264; IntAct: EBI-6150240,EBI-713955; Score: 0.35
DE  Interaction: Q0HD54; IntAct: EBI-6147978,EBI-713955; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-456077,EBI-713955; Score: 0.35
DE  Interaction: Q9UPE1; IntAct: EBI-6381269,EBI-713955; Score: 0.35
DE  Interaction: Q81YN3; IntAct: EBI-2819062,EBI-713955; Score: 0.37
DE  Interaction: O60506; IntAct: EBI-713955,EBI-1024357; Score: 0.40
DE  Interaction: Q14558; IntAct: EBI-724449,EBI-713955; Score: 0.40
DE  Interaction: Q9NZI8; IntAct: EBI-1053892,EBI-713955; Score: 0.40
DE  Interaction: Q9Y3U8; IntAct: EBI-1057689,EBI-713955; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25475891,EBI-713955; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-713955,EBI-740355; Score: 0.56
DE  Interaction: O95793; IntAct: EBI-358174,EBI-713955; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-713955,EBI-2339219; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-713955,EBI-739832; Score: 0.56
DE  Interaction: P78563-4; IntAct: EBI-12002366,EBI-713955; Score: 0.56
DE  Interaction: O15226; IntAct: EBI-713955,EBI-766011; Score: 0.67
DE  Interaction: O75928-2; IntAct: EBI-348567,EBI-713955; Score: 0.56
DE  Interaction: P38732; IntAct: EBI-713955,EBI-24379; Score: 0.61
DE  Interaction: Q7L5N1; IntAct: EBI-486838,EBI-713955; Score: 0.37
DE  Interaction: O60383; IntAct: EBI-473825,EBI-713955; Score: 0.37
DE  Interaction: Q15047; IntAct: EBI-79691,EBI-713955; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0034599;
GO  GO:0006955;
GO  GO:0042474;
GO  GO:0010586;
GO  GO:0008285;
GO  GO:0042473;
GO  GO:2001244;
GO  GO:0031054;
GO  GO:0035196;
GO  GO:0030422;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0009615;
GO  GO:0048705;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGE
SQ  GTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYT
SQ  TICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTD
SQ  YIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
//
ID  Q5U651;
PN  Ras-interacting protein 1;
GN  RASIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15031288}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:15031288}. Note=Associated with perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS.
DR  UNIPROT: Q5U651;
DR  UNIPROT: Q6U676;
DR  PDB: 5KHO;
DR  PDB: 5KHQ;
DR  Pfam: PF01843;
DR  Pfam: PF00788;
DR  PROSITE: PS51126;
DR  PROSITE: PS50200;
DR  OMIM: 609623;
DR  DisGeNET: 54922;
DE  Function: Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells (By similarity). May act as effector for Golgi-bound HRAS and other Ras- like proteins. May promote HRAS-mediated transformation. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000250, ECO:0000269|PubMed:15031288, ECO:0000269|PubMed:22354037}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NI89; IntAct: EBI-2796250,EBI-2797123; Score: 0.37
DE  Interaction: P60953; IntAct: EBI-81752,EBI-2797123; Score: 0.35
DE  Interaction: Q9H0H5; IntAct: EBI-717233,EBI-2797123; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-1001132,EBI-2797123; Score: 0.35
DE  Interaction: O43684; IntAct: EBI-1050987,EBI-2797123; Score: 0.35
DE  Interaction: Q7TSY8; IntAct: EBI-2552468,EBI-2797123; Score: 0.35
DE  Interaction: Q9H4P4; IntAct: EBI-2130266,EBI-2797123; Score: 0.35
DE  Interaction: Q9DC28; IntAct: EBI-6392453,EBI-2797123; Score: 0.35
DE  Interaction: Q9JLB0; IntAct: EBI-771456,EBI-2797123; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-299674,EBI-2797123; Score: 0.35
DE  Interaction: Q9NVK5; IntAct: EBI-1104764,EBI-2797123; Score: 0.35
DE  Interaction: Q9BRV8; IntAct: EBI-1773646,EBI-2797123; Score: 0.35
DE  Interaction: Q99PU7; IntAct: EBI-1791471,EBI-2797123; Score: 0.35
DE  Interaction: O95817; IntAct: EBI-747185,EBI-2797123; Score: 0.35
DE  Interaction: Q6NYC8; IntAct: EBI-2557469,EBI-2797123; Score: 0.35
DE  Interaction: Q8N6T3; IntAct: EBI-716933,EBI-2797123; Score: 0.37
DE  Interaction: A0A384KVT4; IntAct: EBI-2797123,EBI-2842443; Score: 0.37
DE  Interaction: P23528; IntAct: EBI-352733,EBI-2797123; Score: 0.40
GO  GO:0005911;
GO  GO:0005795;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0051020;
GO  GO:0042803;
GO  GO:0001525;
GO  GO:0048754;
GO  GO:0010507;
GO  GO:1905709;
GO  GO:0035024;
GO  GO:2000299;
GO  GO:0033625;
GO  GO:0043087;
GO  GO:0007165;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLSGERKEGGSPRFGKLHLPVGLWINSPRKQLAKLGRRWPSAASVKSSSSDTGSRSSEPLPPPPPHVELRRVGAVKAAGG
SQ  ASGSRAKRISQLFRGSGTGTTGSSGAGGPGTPGGAQRWASEKKLPELAAGVAPEPPLATRATAPPGVLKIFGAGLASGAN
SQ  YKSVLATARSTARELVAEALERYGLAGSPGGGPGESSCVDAFALCDALGRPAAAGVGSGEWRAEHLRVLGDSERPLLVQE
SQ  LWRARPGWARRFELRGREEARRLEQEAFGAADSEGTGAPSWRPQKNRSRAASGGAALASPGPGTGSGAPAGSGGKERSEN
SQ  LSLRRSVSELSLQGRRRRQQERRQQALSMAPGAADAQIGTADPGDFDQLTQCLIQAPSNRPYFLLLQGYQDAQDFVVYVM
SQ  TREQHVFGRGGNSSGRGGSPAPYVDTFLNAPDILPRHCTVRAGPEHPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLG
SQ  EHFLFMYKDPRTGGSGPARPPWLPARPGATPPGPGWAFSCRLCGRGLQERGEALAAYLDGREPVLRFRPREEEALLGEIV
SQ  RAAAAGSGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPENHPEGVPEVPLTPEAVS
SQ  VELRPLMLWMANTTELLSFVQEKVLEMEKEADQEDPQLCNDLELCDEAMALLDEVIMCTFQQSVYYLTKTLYSTLPALLD
SQ  SNPFTAGAELPGPGAELGAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQWS
SQ  RAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSMAVNLLCVPRTSLLKASWSSLRTDHPTLTPAQLHHLLSHYQLGPGRG
SQ  PPAAWDPPPAEREAVDTGDIFESFSSHPPLILPLGSSRLRLTGPVTDDALHRELRRLRRLLWDLEQQELPANYRHGPPVA
SQ  TSP
//
ID  Q9HAU5;
PN  Regulator of nonsense transcripts 2;
GN  UPF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187}.
DR  UNIPROT: Q9HAU5;
DR  UNIPROT: A6NLJ5;
DR  UNIPROT: D3DRS0;
DR  UNIPROT: Q14BM1;
DR  UNIPROT: Q5W0J4;
DR  UNIPROT: Q8N8U1;
DR  UNIPROT: Q9H1J2;
DR  UNIPROT: Q9NWL1;
DR  UNIPROT: Q9P2D9;
DR  UNIPROT: Q9Y4M9;
DR  PDB: 1UW4;
DR  PDB: 2WJV;
DR  PDB: 4CEK;
DR  PDB: 4CEM;
DR  Pfam: PF02854;
DR  Pfam: PF04050;
DR  OMIM: 605529;
DR  DisGeNET: 26019;
DE  Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:18066079}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-372073,EBI-372073; Score: 0.37
DE  Interaction: O00233; IntAct: EBI-372073,EBI-750973; Score: 0.44
DE  Interaction: Q9UHX1; IntAct: EBI-1053259,EBI-372073; Score: 0.56
DE  Interaction: P10242; IntAct: EBI-298355,EBI-372073; Score: 0.40
DE  Interaction: Q92900-2; IntAct: EBI-373492,EBI-372073; Score: 0.82
DE  Interaction: P0DPB3; IntAct: EBI-1397509,EBI-372073; Score: 0.40
DE  Interaction: Q9H3D4-1; IntAct: EBI-2400586,EBI-372073; Score: 0.35
DE  Interaction: Q9Y5S9; IntAct: EBI-447231,EBI-372073; Score: 0.64
DE  Interaction: Q9BZI7; IntAct: EBI-372780,EBI-372073; Score: 0.90
DE  Interaction: Q9NS87; IntAct: EBI-712159,EBI-372073; Score: 0.35
DE  Interaction: Q9H8T0; IntAct: EBI-372073,EBI-711399; Score: 0.37
DE  Interaction: P58526; IntAct: EBI-2851618,EBI-372073; Score: 0.37
DE  Interaction: Q92900; IntAct: EBI-373471,EBI-372073; Score: 0.95
DE  Interaction: Q08491; IntAct: EBI-1389,EBI-372073; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-372073; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-371922,EBI-372073; Score: 0.37
DE  Interaction: P26651; IntAct: EBI-374248,EBI-372073; Score: 0.37
DE  Interaction: Q8IZD4; IntAct: EBI-521595,EBI-372073; Score: 0.37
DE  Interaction: Q9Y3B2; IntAct: EBI-371892,EBI-372073; Score: 0.37
DE  Interaction: P42285; IntAct: EBI-347612,EBI-372073; Score: 0.37
DE  Interaction: Q9H0D6; IntAct: EBI-372110,EBI-372073; Score: 0.37
DE  Interaction: Q8IU60; IntAct: EBI-521577,EBI-372073; Score: 0.37
DE  Interaction: Q01780; IntAct: EBI-358236,EBI-372073; Score: 0.37
DE  Interaction: Q9H9D4; IntAct: EBI-347633,EBI-372073; Score: 0.37
DE  Interaction: O15116; IntAct: EBI-347619,EBI-372073; Score: 0.37
DE  Interaction: P62841; IntAct: EBI-372635,EBI-372073; Score: 0.37
DE  Interaction: P46777; IntAct: EBI-358018,EBI-372073; Score: 0.37
DE  Interaction: Q99623; IntAct: EBI-358348,EBI-372073; Score: 0.37
DE  Interaction: Q9GZQ8; IntAct: EBI-373144,EBI-372073; Score: 0.37
DE  Interaction: P62851; IntAct: EBI-353054,EBI-372073; Score: 0.37
DE  Interaction: Q9ULX3; IntAct: EBI-373285,EBI-372073; Score: 0.37
DE  Interaction: Q04637; IntAct: EBI-73711,EBI-372073; Score: 0.35
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003723;
GO  GO:0042162;
GO  GO:0031100;
GO  GO:0001889;
GO  GO:0006406;
GO  GO:0000184;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKV
SQ  KAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENF
SQ  FSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSL
SQ  LQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIA
SQ  GLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYE
SQ  EFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPA
SQ  ILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEAST
SQ  GSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDL
SQ  CSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPES
SQ  HLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPW
SQ  QDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYN
SQ  YRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLE
SQ  VWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGA
SQ  ETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKM
SQ  MLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWN
SQ  QQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR
//
ID  P15389;
PN  Sodium channel protein type 5 subunit alpha;
GN  Scn5a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q14524}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15579534}. Note=RANGRF promotes trafficking to the cell membrane. {ECO:0000250|UniProtKB:Q14524}.
DR  UNIPROT: P15389;
DR  UNIPROT: Q925G6;
DR  PDB: 6UZ0;
DR  PDB: 6UZ3;
DR  Pfam: PF00520;
DR  Pfam: PF06512;
DR  Pfam: PF11933;
DE  Function: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels. {ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0016328;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042383;
GO  GO:0034706;
GO  GO:0030315;
GO  GO:0001518;
GO  GO:0030018;
GO  GO:0030506;
GO  GO:0005516;
GO  GO:0005261;
GO  GO:0019899;
GO  GO:0017134;
GO  GO:0044325;
GO  GO:0050998;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0097110;
GO  GO:0031625;
GO  GO:0005244;
GO  GO:0005248;
GO  GO:0086060;
GO  GO:0086061;
GO  GO:0086006;
GO  GO:0086062;
GO  GO:0086063;
GO  GO:0086014;
GO  GO:0086016;
GO  GO:0086067;
GO  GO:0003360;
GO  GO:0086043;
GO  GO:0055074;
GO  GO:0086002;
GO  GO:0060048;
GO  GO:0003231;
GO  GO:0071277;
GO  GO:0021549;
GO  GO:0051899;
GO  GO:0086010;
GO  GO:0098912;
GO  GO:0086045;
GO  GO:0086048;
GO  GO:0086012;
GO  GO:0086047;
GO  GO:0086046;
GO  GO:0019228;
GO  GO:0042475;
GO  GO:0045760;
GO  GO:0050679;
GO  GO:0010460;
GO  GO:0010765;
GO  GO:0060371;
GO  GO:0060372;
GO  GO:0086004;
GO  GO:0002027;
GO  GO:0086091;
GO  GO:1902305;
GO  GO:0060373;
GO  GO:0060307;
GO  GO:0014894;
GO  GO:0014070;
GO  GO:0086015;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0021537;
GO  GO:0086005;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:D0E0C2};
SQ  MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQASKKLPDLYGNPPRELIGEP
SQ  LEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKY
SQ  VEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTI
SQ  VGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGLVWNSLDVYLNDPANYLLKNG
SQ  TTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFL
SQ  GSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERKSKRR
SQ  KRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRT
SQ  SLLVPWPLRHPSAQGQPGPGASAPGYVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSYLLRPMVLDRPPDTTTPSEEPGG
SQ  PQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFA
SQ  DLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLS
SQ  RMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLP
SQ  RWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMN
SQ  NLQLALARIQRGLRFVKRTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRPGQG
SQ  TPGDSEPVCVPIAVAESDTEDQEEDEENSLGTEEESSKQESQVVSGGHEPYQEPRAWSQVSETTSSEAGASTSQADWQQE
SQ  QKTEPQAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQSPGKVWWRLRKTC
SQ  YRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLI
SQ  VDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAG
SQ  KFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQP
SQ  QWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQ
SQ  GFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVV
SQ  VILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMAN
SQ  FAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIII
SQ  SFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINM
SQ  DLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQ
SQ  RSVKHASFLFRQQAGGSGLSDEDAPEREGLIAYMMNGNFSRRSAPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSR
SQ  SEDLADFPPSPDRDRESIV
//
ID  Q62910;
PN  Synaptojanin-1;
GN  Synj1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
DR  UNIPROT: Q62910;
DR  UNIPROT: O89092;
DR  UNIPROT: Q62911;
DR  UNIPROT: Q810Z8;
DR  Pfam: PF08952;
DR  Pfam: PF03372;
DR  Pfam: PF02383;
DR  PROSITE: PS50102;
DR  PROSITE: PS50275;
DE  Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)- bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By similarity). Has a role in clathrin-mediated endocytosis (PubMed:9428629). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426, ECO:0000269|PubMed:9428629}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-1149123; Score: 0.35
GO  GO:0005623;
GO  GO:0030132;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030117;
GO  GO:0043005;
GO  GO:0098688;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0097060;
GO  GO:0043195;
GO  GO:0012506;
GO  GO:1990175;
GO  GO:0052658;
GO  GO:0034595;
GO  GO:0004438;
GO  GO:0004439;
GO  GO:0043812;
GO  GO:0008022;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0017124;
GO  GO:0007420;
GO  GO:0046855;
GO  GO:0007612;
GO  GO:0006836;
GO  GO:0046856;
GO  GO:0046488;
GO  GO:1904980;
GO  GO:0014015;
GO  GO:0048260;
GO  GO:0098884;
GO  GO:0099149;
GO  GO:0034097;
GO  GO:0032526;
GO  GO:0048488;
GO  GO:0016082;
GO  GO:0048489;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYAKVLDAYGLLGVLRLNLGDTMLHYLVL
SQ  VTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFW
SQ  NQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLD
SQ  DCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLK
SQ  ASEHASDIHMVSFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFDGSAVQRCQSGTVRTNCLDCLDRTNSVQAFLGLE
SQ  MLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLL
SQ  LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKNMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTD
SQ  WLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFV
SQ  FIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLF
SQ  SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCR
SQ  TPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQK
SQ  IYKEVIAVQGPPDGTVLVSIKSSAQENTFFDDALIDELLQQFAHFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELL
SQ  NRTITITLKSPDWIKTLEEEMSLEKISVTLPSSTSSTLLGEDAEVSADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGT
SQ  SPSSSPRTSPCQSPTAPEYSAPSLPIRPSRAPSRTPGPLSSQGAPVDTQPAAQKESSQTIEPKRPPPPRPVAPPARPAPP
SQ  QRPPPPSGARSPAPARKEFGGVGAPPSPGVTRREMEAPKSPGTARKDNIGRNQPSPQAGLAGPGPSGYGAARPTIPARAG
SQ  VISAPQSQARVSAGRLTPESQSKPLETSKGPAVLPEPLKPQAAFPPQPSLPTPAQKLQDPLVPIAAPMPPSIPQSNLETP
SQ  PLPPPRSRSSQSLPSDSSPQLQQEQPTGQQVKINGACGVKQEPTLKSDPFEDLSLSVLAVSKAQPSAQISPVLTPDPKML
SQ  IQLPSASQSKVNSLSSVSCMLTMPPVPEQSKSQESVGSSANPFPSLPTRNPFTDRTAAPGNPFRVQSQESEATSWLSKEE
SQ  PVSNSPFPPLMPLSHDMSKPSSSLDGFEDNFDLQSQSTVKTSNPKGWVTFDEDEDFPTKGKSRSVYPDSLGNTAASFDDD
SQ  WSKGTNVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLSSKASPTLDFTER
//
ID  P05480;
PN  Neuronal proto-oncogene tyrosine-protein kinase Src;
GN  Src;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:21525037}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12615910}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain. Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions. {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:22801373}.
DR  UNIPROT: P05480;
DR  UNIPROT: Q2M4I4;
DR  PDB: 6F3F;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta- catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (PubMed:9344858). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta- arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth (By similarity). Required for podosome formation (PubMed:21525037). {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:8641341, ECO:0000269|PubMed:9344858, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8T4F7; IntAct: EBI-298680,EBI-466810; Score: 0.40
DE  Interaction: Q4ACU6; IntAct: EBI-771450,EBI-298680; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-771911,EBI-298680; Score: 0.35
DE  Interaction: Q8C180; IntAct: EBI-298680,EBI-6880000; Score: 0.44
DE  Interaction: Q9QWI6; IntAct: EBI-775592,EBI-298680; Score: 0.35
DE  Interaction: Q01973; IntAct: EBI-298680,EBI-6082337; Score: 0.60
DE  Interaction: P54763; IntAct: EBI-298680,EBI-537711; Score: 0.46
DE  Interaction: P19367; IntAct: EBI-713162,EBI-298680; Score: 0.64
DE  Interaction: P52789; IntAct: EBI-741469,EBI-298680; Score: 0.60
DE  Interaction: P35438; IntAct: EBI-400084,EBI-298680; Score: 0.64
DE  Interaction: Q01097; IntAct: EBI-400125,EBI-298680; Score: 0.35
DE  Interaction: Q9CQV8; IntAct: EBI-771608,EBI-298680; Score: 0.35
DE  Interaction: P16054; IntAct: EBI-298451,EBI-298680; Score: 0.35
DE  Interaction: P07141; IntAct: EBI-777188,EBI-298680; Score: 0.52
GO  GO:0005884;
GO  GO:0005901;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0005770;
GO  GO:0005764;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032587;
GO  GO:0005524;
GO  GO:0070700;
GO  GO:0050839;
GO  GO:0071253;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0030331;
GO  GO:0070851;
GO  GO:0020037;
GO  GO:0005158;
GO  GO:0005178;
GO  GO:0044325;
GO  GO:0016301;
GO  GO:0019900;
GO  GO:0004715;
GO  GO:0051219;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0005080;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0032148;
GO  GO:0034332;
GO  GO:0086098;
GO  GO:0045453;
GO  GO:0060444;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0008283;
GO  GO:0098609;
GO  GO:0071398;
GO  GO:0071498;
GO  GO:0070301;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071222;
GO  GO:0071375;
GO  GO:0036120;
GO  GO:0071393;
GO  GO:0034614;
GO  GO:0071560;
GO  GO:0007173;
GO  GO:0030900;
GO  GO:0007229;
GO  GO:0035556;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0051895;
GO  GO:2001243;
GO  GO:0051902;
GO  GO:0031333;
GO  GO:0051974;
GO  GO:0032211;
GO  GO:0045892;
GO  GO:0048011;
GO  GO:0042476;
GO  GO:0048477;
GO  GO:0036035;
GO  GO:0018105;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0016310;
GO  GO:0043065;
GO  GO:0090263;
GO  GO:0045785;
GO  GO:0045737;
GO  GO:0050715;
GO  GO:0035306;
GO  GO:2000573;
GO  GO:0010634;
GO  GO:0070374;
GO  GO:0010628;
GO  GO:0010907;
GO  GO:0046628;
GO  GO:1902533;
GO  GO:2000394;
GO  GO:0043406;
GO  GO:2000386;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:2000588;
GO  GO:0071803;
GO  GO:0031954;
GO  GO:0051897;
GO  GO:1900182;
GO  GO:0010954;
GO  GO:0071902;
GO  GO:0051222;
GO  GO:0051057;
GO  GO:0014911;
GO  GO:0045893;
GO  GO:0001545;
GO  GO:0050847;
GO  GO:0046777;
GO  GO:0031648;
GO  GO:0006468;
GO  GO:2001286;
GO  GO:0042127;
GO  GO:0060491;
GO  GO:0022407;
GO  GO:2000641;
GO  GO:0010632;
GO  GO:0033146;
GO  GO:0098962;
GO  GO:0043393;
GO  GO:0010447;
GO  GO:0051602;
GO  GO:0070555;
GO  GO:0009612;
GO  GO:0051385;
GO  GO:0031667;
GO  GO:0009615;
GO  GO:0043149;
GO  GO:0034446;
GO  GO:0045056;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0060065;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSNKSKPKDASQRRRSLEPSENVHGAGGAFPASQTPSKPASADGHRGPSAAFVPPAAEPKLFGGFNSSDTVTSPQRAGP
SQ  LAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTRKVDVREGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGK
SQ  ITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSK
SQ  HADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQ
SQ  VMKKLRHEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANI
SQ  LVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVL
SQ  DQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
//
ID  P54811;
PN  Transitional endoplasmic reticulum ATPase homolog 1;
GN  cdc;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}. Cytoplasm {ECO:0000269|PubMed:17369820}. Note=Colocalizes with ubxn-1, ubxn-2 and ubxn-3 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the perinuclear region in intestinal cells (PubMed:25721663). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}.
DR  UNIPROT: P54811;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF02933;
DR  Pfam: PF02359;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:18854144, PubMed:18782221, PubMed:22768338). Can also prevent aggregation of unfolded proteins also in an ATP- independent manner (PubMed:18782221). Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains (PubMed:19545544). Involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). In association with helicase him-6 and GTPase crp-1, regulates the unfolded protein response (UPR) following ER stress, probably independently of the ERAD pathway (PubMed:18458060). Together with udf-2 and chn-1, regulates myosin assembly in body wall muscles by targeting myosin chaperone unc- 45 for proteasomal degradation (PubMed:17369820). Together with the ufd-1-npl-4 complex, controls the switch from spermatogenesis to oogenesis by regulating E3 ligase cul-2 complex-mediated tra-1 proteasomal degradation (PubMed:19773360). During oocyte meiosis and together with cdc-48.2, required for chromosome condensation at the diakinesis phase in prophase I and for progression of metaphase I (PubMed:17512499). During the first embryonic cell division, regulates DNA replication and thus chromosome segregation and decondensation, and nuclear envelope re-assembly (PubMed:18097415, PubMed:18854144, PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). In S phase and in association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn- 3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564). During the first embryonic cell divisions and together with cdc-48.2, regulates the re- assembly of the nuclear envelope after mitosis possibly by inactivating kinase air-2, a component of the chromosomal passenger complex (CPC) (PubMed:18097415). However, in another study, cdc-48.1 does not appear to be implicated in the regulation of air-2 (PubMed:18854144). {ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049, ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18458060, ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144, ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:19773360, ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:25652260, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-320245,EBI-320245; Score: 0.55
DE  Interaction: Q17425; IntAct: EBI-2411422,EBI-320245; Score: 0.49
DE  Interaction: Q94230; IntAct: EBI-320245,EBI-895916; Score: 0.49
DE  Interaction: O17850; IntAct: EBI-320245,EBI-320650; Score: 0.49
DE  Interaction: P54812; IntAct: EBI-320265,EBI-320245; Score: 0.62
DE  Interaction: Q9TXH9; IntAct: EBI-320245,EBI-320236; Score: 0.62
DE  Interaction: Q22557; IntAct: EBI-2412448,EBI-320245; Score: 0.49
DE  Interaction: Q22560; IntAct: EBI-2002088,EBI-320245; Score: 0.37
DE  Interaction: G5EC44; IntAct: EBI-320245,EBI-323732; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034098;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0031593;
GO  GO:0044877;
GO  GO:0097352;
GO  GO:0008340;
GO  GO:0009792;
GO  GO:0071712;
GO  GO:0016236;
GO  GO:0051228;
GO  GO:0045977;
GO  GO:0032436;
GO  GO:1905634;
GO  GO:0030970;
GO  GO:0030433;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASVPTHQSEKEKKNDELSTAILKDKVKPNRLIVDQSEQDDNSVIAVSQAKMDELGLFRGDAVILKGKKRKESVAIIVSD
SQ  ESCPNEKVRMNRVVRNNLRIRLGDVVSITPAPNLSYGTRIHVLPIDDTIEGLTGNLFDVFLKPYFLEAYRPLHKGDIFTV
SQ  QAAMRTVEFKVVETEPAPACIVSPDTMIHYEGDPIKREEEEESMNDIGYDDLGGVRKQLAQIKEMVELPLRHPQLFKAIG
SQ  IKPPRGILLFGPPGTGKTLIARAVANETGSFFFLINGPEVMSKMSGESESNLRKAFEECEKNQPAILFIDEIDAIAPKRE
SQ  KTNGEVERRIVSQLLTLMDGVKGRSNLVVIAATNRPNSIDGALRRFGRFDREIDIGIPDAVGRLEILRIHTKNMKLADDV
SQ  DLEQIANECHGFVGADLASLCSEAALQQIREKMELIDLEDDQIDAEVLNSLAVTMENFRFAQGKSSPSALREAVVETPNT
SQ  TWSDIGGLQNVKRELQELVQYPVEHPEKYLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGE
SQ  SEANVRDVFDKARAAAPCVLFFDELDSIAKARGGGAGGDGGGASDRVINQVLTEMDGMNAKKNVFIIGATNRPDIIDPAV
SQ  LRPGRLDQLIYIPLPDEASRHQILKASLRKTPLSKDLDLTFLAKNTVGFSGADLTEICQRACKLAIRESIEKEIRIEKER
SQ  QDRQARGEELMEDDAVDPVPEITRAHFEEAMKFARRSVTDNDIRKYEMFAQTLQQSRGFGNNFKFPGEQRGSDAPSAPVP
SQ  AQDDDDLYN
//
ID  O94972;
PN  E3 ubiquitin-protein ligase TRIM37;
GN  TRIM37;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome {ECO:0000269|PubMed:11938494}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000269|PubMed:15885686}.
DR  UNIPROT: O94972;
DR  UNIPROT: A8K0V9;
DR  UNIPROT: A8K8U4;
DR  UNIPROT: A8MZ79;
DR  UNIPROT: B4DGZ3;
DR  UNIPROT: F8WEE6;
DR  UNIPROT: Q7Z3E6;
DR  UNIPROT: Q8IYF7;
DR  UNIPROT: Q8WYF7;
DR  PDB: 3LRQ;
DR  Pfam: PF00917;
DR  Pfam: PF00643;
DR  PROSITE: PS50144;
DR  PROSITE: PS50119;
DR  PROSITE: PS50089;
DR  OMIM: 253250;
DR  OMIM: 605073;
DR  DisGeNET: 4591;
DE  Function: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Has anti-HIV activity (PubMed:24317724). {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042}.
DE  Disease: Mulibrey nanism (MUL) [MIM:253250]: An autosomal recessive growth disorder characterized by severe growth failure of prenatal onset, constrictive pericardium and progressive cardiomyopathy, facial dysmorphism, and failure of sexual maturation. Additional clinical features include hepatomegaly, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, hypoplasia of various endocrine glands, insulin resistance with type 2 diabetes, and an increased risk for Wilms' tumor. {ECO:0000269|PubMed:10888877, ECO:0000269|PubMed:12754710, ECO:0000269|PubMed:15108285, ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:17100991, ECO:0000269|PubMed:17551331, ECO:0000269|PubMed:21865362, ECO:0000269|PubMed:23385855}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q7Z2E3; IntAct: EBI-741602,EBI-847814; Score: 0.49
DE  Interaction: Q5VVX9; IntAct: EBI-2130181,EBI-741602; Score: 0.37
DE  Interaction: Q9H5Z6; IntAct: EBI-741626,EBI-741602; Score: 0.55
DE  Interaction: Q7L590; IntAct: EBI-374912,EBI-741602; Score: 0.55
DE  Interaction: O43663; IntAct: EBI-741602,EBI-741137; Score: 0.63
DE  Interaction: Q8N5R6; IntAct: EBI-740841,EBI-741602; Score: 0.37
DE  Interaction: P62256; IntAct: EBI-2129909,EBI-741602; Score: 0.37
DE  Interaction: P54764-2; IntAct: EBI-741602,EBI-21371515; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-741602,EBI-529989; Score: 0.37
DE  Interaction: A8K932; IntAct: EBI-741602,EBI-10174671; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-741602,EBI-5453285; Score: 0.72
DE  Interaction: P57075; IntAct: EBI-2105393,EBI-741602; Score: 0.56
DE  Interaction: Q7TSJ6; IntAct: EBI-6305003,EBI-741602; Score: 0.35
DE  Interaction: Q86UD4; IntAct: EBI-7233259,EBI-741602; Score: 0.56
DE  Interaction: Q86Y33; IntAct: EBI-741602,EBI-10260504; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-740727,EBI-741602; Score: 0.67
DE  Interaction: Q96NC0; IntAct: EBI-2682299,EBI-741602; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-741602,EBI-748391; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-741602,EBI-399080; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-348259,EBI-741602; Score: 0.67
DE  Interaction: Q13895; IntAct: EBI-741602,EBI-358049; Score: 0.78
DE  Interaction: P26196; IntAct: EBI-351257,EBI-741602; Score: 0.56
DE  Interaction: P32969; IntAct: EBI-741602,EBI-358122; Score: 0.56
DE  Interaction: O95990-3; IntAct: EBI-10192902,EBI-741602; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-719941,EBI-741602; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-742802,EBI-741602; Score: 0.56
DE  Interaction: Q9Y272; IntAct: EBI-740818,EBI-741602; Score: 0.56
DE  Interaction: Q9Y2D8; IntAct: EBI-2212028,EBI-741602; Score: 0.67
DE  Interaction: Q96SN8; IntAct: EBI-741602,EBI-308374; Score: 0.37
DE  Interaction: X5D778; IntAct: EBI-741602,EBI-17183751; Score: 0.37
DE  Interaction: X5DP31; IntAct: EBI-741602,EBI-21247516; Score: 0.37
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-741602; Score: 0.46
DE  Interaction: Q6ZU80; IntAct: EBI-2873150,EBI-741602; Score: 0.35
DE  Interaction: Q96T60; IntAct: EBI-741602,EBI-1045072; Score: 0.67
DE  Interaction: P08238; IntAct: EBI-741602,EBI-352572; Score: 0.40
DE  Interaction: P58526; IntAct: EBI-2851618,EBI-741602; Score: 0.37
DE  Interaction: Q96M61; IntAct: EBI-741835,EBI-741602; Score: 0.37
DE  Interaction: Q8IYF1; IntAct: EBI-741705,EBI-741602; Score: 0.37
DE  Interaction: Q9UBZ4; IntAct: EBI-742588,EBI-741602; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-740459,EBI-741602; Score: 0.37
DE  Interaction: O95990; IntAct: EBI-743396,EBI-741602; Score: 0.37
DE  Interaction: Q6ZVK8; IntAct: EBI-740486,EBI-741602; Score: 0.37
DE  Interaction: Q96KB5; IntAct: EBI-536853,EBI-741602; Score: 0.37
DE  Interaction: P53618; IntAct: EBI-741602,EBI-359063; Score: 0.67
DE  Interaction: Q6ZU52; IntAct: EBI-739493,EBI-741602; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-741602,EBI-739737; Score: 0.37
DE  Interaction: Q9H4K1; IntAct: EBI-740128,EBI-741602; Score: 0.37
DE  Interaction: Q8TCX5; IntAct: EBI-746325,EBI-741602; Score: 0.37
DE  Interaction: Q8N720; IntAct: EBI-625509,EBI-741602; Score: 0.37
DE  Interaction: Q15398; IntAct: EBI-748280,EBI-741602; Score: 0.37
DE  Interaction: P07305; IntAct: EBI-725224,EBI-741602; Score: 0.40
DE  Interaction: Q8IVW4; IntAct: EBI-741602,EBI-3919850; Score: 0.56
DE  Interaction: O43167; IntAct: EBI-741602,EBI-744471; Score: 0.56
DE  Interaction: Q8N8B7-2; IntAct: EBI-741602,EBI-11955057; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-741602,EBI-745213; Score: 0.56
DE  Interaction: P28702-3; IntAct: EBI-741602,EBI-16429492; Score: 0.56
DE  Interaction: A0A0S2Z4G9; IntAct: EBI-741602,EBI-16428950; Score: 0.56
DE  Interaction: A0A0S2Z4M1; IntAct: EBI-741602,EBI-16429430; Score: 0.56
DE  Interaction: Q8IYY4; IntAct: EBI-741602,EBI-10264440; Score: 0.56
DE  Interaction: Q96SQ5; IntAct: EBI-6427977,EBI-741602; Score: 0.56
DE  Interaction: O60941-5; IntAct: EBI-741602,EBI-11984733; Score: 0.56
DE  Interaction: O00311; IntAct: EBI-741602,EBI-374980; Score: 0.56
DE  Interaction: Q96C24; IntAct: EBI-741602,EBI-747142; Score: 0.56
DE  Interaction: Q14241; IntAct: EBI-741602,EBI-742350; Score: 0.56
DE  Interaction: Q86Y33-5; IntAct: EBI-741602,EBI-11983537; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-741602,EBI-710484; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-741602; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-2361917,EBI-741602; Score: 0.35
DE  Interaction: Q8N137; IntAct: EBI-947360,EBI-741602; Score: 0.35
DE  Interaction: Q96KN7; IntAct: EBI-1050213,EBI-741602; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-741977,EBI-741602; Score: 0.35
DE  Interaction: Q96ST8; IntAct: EBI-2799206,EBI-741602; Score: 0.35
DE  Interaction: P39009; IntAct: EBI-741602,EBI-6194; Score: 0.56
DE  Interaction: Q12417; IntAct: EBI-741602,EBI-710; Score: 0.56
DE  Interaction: P32571; IntAct: EBI-741602,EBI-19840; Score: 0.56
GO  GO:0016235;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0003682;
GO  GO:0042803;
GO  GO:0005164;
GO  GO:0061630;
GO  GO:0031625;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0070842;
GO  GO:0035518;
GO  GO:0036353;
GO  GO:0046600;
GO  GO:0032088;
GO  GO:0000122;
GO  GO:0051091;
GO  GO:0051092;
GO  GO:0051865;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQ
SQ  LCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISL
SQ  VQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISK
SQ  SSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVV
SQ  RGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILR
SQ  FQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDM
SQ  LLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGEN
SQ  DVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPR
SQ  PPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAA
SQ  LAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGS
SQ  SQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSE
SQ  TGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDE
SQ  NSGR
//
ID  F4ICX9;
PN  TSK-associating protein 1;
GN  TSA1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum lumen. Nucleus envelope {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Cytoplasm {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Note=In interphase, found in ER bodies and at the nuclear envelope (PubMed:24348487). During mitosis, concentrates in limited areas close to the ends of spindle microtubules ahead of separating chromatids (PubMed:15964904). {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}.
DR  UNIPROT: F4ICX9;
DR  UNIPROT: F4ICY0;
DR  UNIPROT: Q94AE1;
DR  UNIPROT: Q9C831;
DE  Function: Involved in seedling development in the dark. May be involved, when interacting with TSK, in the organization of spindle microtubules and may participate, when interacting with GIP1, in structural links between the nuclear envelope and the cytoskeleton. {ECO:0000269|PubMed:22133685, ECO:0000269|PubMed:24348487}.
DE  Reference Proteome: Yes;
GO  GO:0009535;
GO  GO:0005788;
GO  GO:0005635;
GO  GO:0005777;
GO  GO:0099503;
GO  GO:0005773;
GO  GO:0005509;
GO  GO:0050832;
GO  GO:0009640;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEIYTMKTNFLVLALSLCILLSSFHEVSCQDDGSGLSNLDLIERDYQDSVNALQGKDDEDQSAKIQSENQNNTTVTDKNT
SQ  ISLSLSDESEVGSVSDESVGRSSLLDQIKLEFEAHHNSINQAGSDGVKAESKDDDEELSAHRQKMLEEIEHEFEAASDSL
SQ  KQLKTDDVNEGNDEEHSAKRQSLLEEIEREFEAATKELEQLKVNDFTGDKDDEEHSAKRKSMLEAIEREFEAAMEGIEAL
SQ  KVSDSTGSGDDEEQSAKRLSMLEEIEREFEAASKGLEQLRASDSTADNNEEEHAAKGQSLLEEIEREFEAATESLKQLQV
SQ  DDSTEDKEHFTAAKRQSLLEEIEREFEAATKDLKQLNDFTEGSADDEQSAKRNKMLEDIEREFEAATIGLEQLKANDFSE
SQ  GNNNEEQSAKRKSMLEEIEREFEAAIGGLKQIKVDDSRNLEEESAKRKIILEEMEREFEEAHSGINAKADKEESAKKQSG
SQ  SAIPEVLGLGQSGGCSCSKQDEDSSIVIPTKYSIEDILSEESAVQGTETSSLTASLTQLVENHRKEKESLLGHRVLTSPS
SQ  IASSTSESSATSETVETLRAKLNELRGLTARELVTRKDFGQILITAASFEELSSAPISYISRLAKYRNVIKEGLEASERV
SQ  HIAQVRAKMLKEVATEKQTAVDTHFATAKKLAQEGDALFVKIFAIKKLLAKLEAEKESVDGKFKETVKELSHLLADASEA
SQ  YEEYHGAVRKAKDEQAAEEFAKEATQSAEIIWVKFLSSL
//
ID  P0DTC1;
PN  Non-structural protein 11;
GN  R1A;
OS  2697049;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.
DR  UNIPROT: P0DTC1;
DR  PDB: 6Y2E;
DR  PDB: 6Y2F;
DR  PDB: 6Y2G;
DR  PROSITE: PS00867;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: [Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UM54; IntAct: EBI-25475882,EBI-350606; Score: 0.35
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0003723;
GO  GO:0036459;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0039548;
GO  GO:0039579;
GO  GO:0039502;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAP
SQ  HGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQEN
SQ  WNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAW
SQ  YTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTL
SQ  MKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKG
SQ  GRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASF
SQ  SASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVR
SQ  VLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVE
SQ  FLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKC
SQ  VKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYC
SQ  ALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVI
SQ  KTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPL
SQ  EFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYI
SQ  KNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGP
SQ  NVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVE
SQ  QKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLK
SQ  KDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSII
SQ  SNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLND
SQ  LNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQS
SQ  TQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLD
SQ  GADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATAL
SQ  LTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQT
SQ  TLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHIT
SQ  SKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPY
SQ  PNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNK
SQ  ATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPA
SQ  NNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRC
SQ  LNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCL
SQ  GSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTA
SQ  FGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHV
SQ  VDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRP
SQ  INPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVY
SQ  YSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQG
SQ  FVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMS
SQ  LSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHT
SQ  DFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGD
SQ  FLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGS
SQ  IIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGA
SQ  LDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDV
SQ  SFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLP
SQ  LTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCM
SQ  VQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPK
SQ  TPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDL
SQ  EGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQT
SQ  GIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQW
SQ  SLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLK
SQ  DCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVF
SQ  MCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKL
SQ  NIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLS
SQ  MQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRK
SQ  LEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTY
SQ  KNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQ
SQ  TACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRG
SQ  MVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQES
SQ  FGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFL
SQ  NGFAV
//
ID  F4IUX6;
PN  Regulator of nonsense transcripts UPF2;
GN  UPF2;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:19602621}. Cytoplasm {ECO:0000269|PubMed:19602621}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: F4IUX6;
DR  UNIPROT: O80955;
DR  Pfam: PF02854;
DR  Pfam: PF04050;
DE  Function: Recruited by UPF3 associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA (By similarity). Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Required for plant development and adaptation to environmental stresses, including plant defense and response to wounding. {ECO:0000250, ECO:0000269|PubMed:22353561}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0035145;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003729;
GO  GO:0042742;
GO  GO:0009867;
GO  GO:0048571;
GO  GO:0000184;
GO  GO:0009611;
GO  GO:0009863;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDHPEDESHSEKQDDEEALARLEEIKKSIEAKLTLRQNNLNPERPDSAYLRTLDSSIKRNTAVIKKLKQINEEQREGLMD
SQ  DLRGVNLSKFVSEAVTAICEAKLKSSDIQAAVQICSLLHQRYKEFSASLTQGLLKVFFPGKSAEDLEADKNSKAMKKRST
SQ  LKLLLELYYVGVIEDSNIFINIIKDLTSVEQLKDRDTTQTNLTLLTSFARQGRIFLGLPISGQDEDFFKGLDVTADQKKS
SQ  FKKAFNTYYDALADLLQSEHKLLLQMEKENAKLVNAKGELSEDSASSYEKLRKSYDHLYRNISSLAEALDMQPPVMPEDG
SQ  TTRLTAGDEASPSGTVKDTSVPEPIWDDEDTKTFYECLPDLRAFVPAVLLGEAEPKSNEQSAKAKEKLSESSSEVVENQQ
SQ  TTEDTTEVSADSASMDDRSNAEQPKEKEEVEKEKAKDTKKEKGKEKDSEKKMEHEKEKGKSLDVANFERLLQRLPGCVSR
SQ  DLIDQLTVEYCYLNSKTNRKKLVKALFNVPRTSLELLAYYSRMVATLASCMKDIPSMLVQMLEDEFNSLVHKKDQMNIET
SQ  KIRNIRFIGELCKFKIVPAGLVFSCLKACLDEFTHHNIDVACNLLETCGRFLYRSPETTLRMTNMLDILMRLKNVKNLDP
SQ  RQSTLVENAYYLCKPPERSARISKVRPPLHQYVRKLLFSDLDKDSIANVLKQLRKLPWSECEQYILKCFMKVHKGKYGQI
SQ  HLIASLTSGLSRHHDEFVVAVVDEVLEEIRVGLELNEYGAQQKRLAHMRFLGELYNYEHVDSSVIFETLYLTLLYGHDTS
SQ  EQEVLDPPEDFFRVRMVIILLETCGHYFDRGSSKKRLDQFLIHFQRYILSKGHLPLDIEFDLQDLFANLRPNMTRYSTID
SQ  EVNAAILQLEEREHASSGDKVSIERHSDTKPSNKSSSDVISSNGKSTAKDIRENGEAHGEESDSDSGSGSVVRDGQNEEL
SQ  DDGNHERGSESGDGDDYDDGDGPGSDDDKFRVRQKVVTVDLEEQADFDQELKALLQESMEQRKLELRGRPALNMTIPMSV
SQ  FEGSGKDHHHFGRVVGENGEEVLDEENGEQREVQVKVLVKRGNKQQTRQMLIPSDCALVQSTKQKEAAELEEKQDIKRLV
SQ  LEYNERDEEEANGLGTQILNWTSGGSRGSTRTGEGSGKSGGSRHRFYYHQGGGGSYHARRK
//
ID  O76070;
PN  Gamma-synuclein;
GN  SNCG;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.
DR  UNIPROT: O76070;
DR  UNIPROT: O15104;
DR  UNIPROT: Q96P61;
DR  Pfam: PF01387;
DR  OMIM: 602998;
DR  DisGeNET: 6623;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P36895; IntAct: EBI-2551936,EBI-1053810; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10967445,EBI-1053810; Score: 0.35
DE  Interaction: P15090; IntAct: EBI-1053810,EBI-715333; Score: 0.40
DE  Interaction: P16035; IntAct: EBI-1053810,EBI-1033507; Score: 0.40
DE  Interaction: P63167; IntAct: EBI-349105,EBI-1053810; Score: 0.40
DE  Interaction: P63162; IntAct: EBI-1053810,EBI-712493; Score: 0.40
DE  Interaction: Q93063; IntAct: EBI-1053810,EBI-1047761; Score: 0.40
DE  Interaction: P25205; IntAct: EBI-355153,EBI-1053810; Score: 0.40
DE  Interaction: A6NEW6; IntAct: EBI-1058455,EBI-1053810; Score: 0.40
DE  Interaction: P41235; IntAct: EBI-1053810,EBI-1049011; Score: 0.40
DE  Interaction: Q96AE4; IntAct: EBI-711404,EBI-1053810; Score: 0.40
DE  Interaction: P17844; IntAct: EBI-351962,EBI-1053810; Score: 0.40
DE  Interaction: P26038; IntAct: EBI-528768,EBI-1053810; Score: 0.40
GO  GO:0030424;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0043025;
GO  GO:0016604;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0045202;
GO  GO:0008344;
GO  GO:0007268;
GO  GO:0009306;
GO  GO:0014059;
GO  GO:0046928;
GO  GO:0050808;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATK
SQ  TVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD
//
ID  O15173;
PN  Membrane-associated progesterone receptor component 2;
GN  PGRMC2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305|PubMed:23793472}; Single- pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic reticulum {ECO:0000269|PubMed:27754849}.
DR  UNIPROT: O15173;
DR  UNIPROT: Q569H1;
DR  Pfam: PF00173;
DR  OMIM: 607735;
DR  DisGeNET: 10424;
DE  Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, reduces labile heme in the nucleus and increases stability of the heme-responsive transcriptional repressors NR1D1 and BACH1 (PubMed:28111073). {ECO:0000250|UniProtKB:Q80UU9, ECO:0000269|PubMed:28111073, ECO:0000305|PubMed:28396637}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-1050125; Score: 0.35
DE  Interaction: O14681; IntAct: EBI-1050125,EBI-2339413; Score: 0.56
DE  Interaction: Q9HBL7; IntAct: EBI-714824,EBI-1050125; Score: 0.35
DE  Interaction: Q96I36; IntAct: EBI-6570698,EBI-1050125; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-10235794,EBI-1050125; Score: 0.35
DE  Interaction: P04233; IntAct: EBI-2622890,EBI-1050125; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-2800296,EBI-1050125; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-11334880,EBI-1050125; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-1050125; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11349465,EBI-1050125; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-721260,EBI-1050125; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-7260649,EBI-1050125; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11343485,EBI-1050125; Score: 0.35
DE  Interaction: Q9Y4C4; IntAct: EBI-2864441,EBI-1050125; Score: 0.44
DE  Interaction: P11279; IntAct: EBI-2805407,EBI-1050125; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-351935,EBI-1050125; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-1752146,EBI-1050125; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-355947,EBI-1050125; Score: 0.46
DE  Interaction: Q9NWU2; IntAct: EBI-1050125,EBI-1051077; Score: 0.51
DE  Interaction: Q96G75; IntAct: EBI-1050125,EBI-745055; Score: 0.51
DE  Interaction: Q9NZ01; IntAct: EBI-1050125,EBI-2877718; Score: 0.56
DE  Interaction: Q8TDV0; IntAct: EBI-11955647,EBI-1050125; Score: 0.56
DE  Interaction: P0DOE9; IntAct: EBI-6138585,EBI-1050125; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6149376,EBI-1050125; Score: 0.35
DE  Interaction: Q14164; IntAct: EBI-1050125,EBI-307369; Score: 0.40
DE  Interaction: P05154; IntAct: EBI-1050125,EBI-722597; Score: 0.40
DE  Interaction: Q9BVC6; IntAct: EBI-1050125,EBI-1057733; Score: 0.40
DE  Interaction: M0R671; IntAct: EBI-1050125,EBI-22236610; Score: 0.35
DE  Interaction: F1LML3; IntAct: EBI-1050125,EBI-22250907; Score: 0.35
DE  Interaction: F1LM93; IntAct: EBI-1050125,EBI-22238190; Score: 0.35
DE  Interaction: A0A0G2K261; IntAct: EBI-1050125,EBI-22242041; Score: 0.35
DE  Interaction: Q5U2U8; IntAct: EBI-1050125,EBI-12593069; Score: 0.35
DE  Interaction: Q5RKH1; IntAct: EBI-1050125,EBI-22255293; Score: 0.35
DE  Interaction: D4A1H9; IntAct: EBI-1050125,EBI-22247753; Score: 0.35
DE  Interaction: D4A7J8; IntAct: EBI-1050125,EBI-22255230; Score: 0.35
DE  Interaction: P42346; IntAct: EBI-1050125,EBI-1571489; Score: 0.35
DE  Interaction: A0A0G2K781; IntAct: EBI-1050125,EBI-22253355; Score: 0.35
DE  Interaction: P00176; IntAct: EBI-1050125,EBI-22254579; Score: 0.35
DE  Interaction: O08662; IntAct: EBI-1050125,EBI-22259134; Score: 0.35
DE  Interaction: Q5PQL2; IntAct: EBI-1050125,EBI-920599; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-1050125,EBI-22084151; Score: 0.35
DE  Interaction: Q925D4; IntAct: EBI-1050125,EBI-21235177; Score: 0.35
DE  Interaction: D3ZGM1; IntAct: EBI-1050125,EBI-22255730; Score: 0.35
DE  Interaction: M0RBS9; IntAct: EBI-1050125,EBI-22254001; Score: 0.35
DE  Interaction: Q5RKH0; IntAct: EBI-1050125,EBI-22247688; Score: 0.35
DE  Interaction: D4A104; IntAct: EBI-1050125,EBI-22258567; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-2949658,EBI-1050125; Score: 0.56
DE  Interaction: O76064; IntAct: EBI-1050125,EBI-373337; Score: 0.56
DE  Interaction: O60906; IntAct: EBI-1050125,EBI-12828299; Score: 0.56
DE  Interaction: Q14656; IntAct: EBI-1050125,EBI-13046724; Score: 0.56
DE  Interaction: Q96H72; IntAct: EBI-1050125,EBI-10287091; Score: 0.56
DE  Interaction: Q96JF0-2; IntAct: EBI-1050125,EBI-12908338; Score: 0.56
DE  Interaction: Q9Y5Y5; IntAct: EBI-1050125,EBI-981985; Score: 0.56
DE  Interaction: Q9H2H9; IntAct: EBI-1050125,EBI-9978441; Score: 0.56
DE  Interaction: Q9H2L4; IntAct: EBI-1050125,EBI-2852148; Score: 0.56
DE  Interaction: P11215; IntAct: EBI-1050125,EBI-2568251; Score: 0.56
DE  Interaction: Q9UBY5; IntAct: EBI-1050125,EBI-12033434; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-1050125,EBI-718439; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-1050125,EBI-3914288; Score: 0.56
DE  Interaction: Q9P0L0; IntAct: EBI-1050125,EBI-1059156; Score: 0.56
DE  Interaction: P01031; IntAct: EBI-8558308,EBI-1050125; Score: 0.56
DE  Interaction: Q13021; IntAct: EBI-1050125,EBI-750078; Score: 0.56
DE  Interaction: Q9BWQ6; IntAct: EBI-1050125,EBI-751204; Score: 0.56
DE  Interaction: P02787; IntAct: EBI-1050125,EBI-714319; Score: 0.56
DE  Interaction: Q9H3K2; IntAct: EBI-1050125,EBI-2868909; Score: 0.56
DE  Interaction: P78329; IntAct: EBI-1050125,EBI-1752413; Score: 0.56
DE  Interaction: P59542; IntAct: EBI-1050125,EBI-12847034; Score: 0.56
DE  Interaction: Q7RTY0; IntAct: EBI-1050125,EBI-12243266; Score: 0.56
DE  Interaction: O43681; IntAct: EBI-1050125,EBI-2515857; Score: 0.56
DE  Interaction: Q86UD5; IntAct: EBI-1050125,EBI-9916342; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-1050125,EBI-10262251; Score: 0.56
DE  Interaction: Q8IWB1; IntAct: EBI-1050125,EBI-2556412; Score: 0.56
DE  Interaction: Q8IVQ6; IntAct: EBI-1050125,EBI-2849773; Score: 0.56
DE  Interaction: O14569; IntAct: EBI-1050125,EBI-717654; Score: 0.56
DE  Interaction: Q5RI15; IntAct: EBI-1050125,EBI-2834035; Score: 0.56
DE  Interaction: O00264; IntAct: EBI-1050125,EBI-1045534; Score: 0.56
DE  Interaction: Q9Y342; IntAct: EBI-1050125,EBI-3919291; Score: 0.56
DE  Interaction: Q9BTX3; IntAct: EBI-1050125,EBI-12876824; Score: 0.56
DE  Interaction: Q9P0S3; IntAct: EBI-1050125,EBI-1054848; Score: 0.56
DE  Interaction: Q6ZPD8; IntAct: EBI-1050125,EBI-12831978; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-1050125,EBI-2548832; Score: 0.56
DE  Interaction: Q96IV6; IntAct: EBI-1050125,EBI-12142299; Score: 0.56
DE  Interaction: O00124; IntAct: EBI-1050125,EBI-1993850; Score: 0.56
DE  Interaction: A0A024RCD1; IntAct: EBI-1050125,EBI-18958976; Score: 0.56
DE  Interaction: Q6N075; IntAct: EBI-1050125,EBI-3920969; Score: 0.56
DE  Interaction: Q7L5A8; IntAct: EBI-1050125,EBI-11337888; Score: 0.56
DE  Interaction: Q9H9B4; IntAct: EBI-1050125,EBI-355861; Score: 0.56
DE  Interaction: Q13277; IntAct: EBI-1050125,EBI-1394295; Score: 0.56
DE  Interaction: I3L0A0; IntAct: EBI-1050125,EBI-12213001; Score: 0.56
DE  Interaction: Q9H0Q3; IntAct: EBI-1050125,EBI-713304; Score: 0.56
DE  Interaction: Q96HH6; IntAct: EBI-1050125,EBI-741829; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-8636004,EBI-1050125; Score: 0.56
DE  Interaction: Q8N2M4; IntAct: EBI-1050125,EBI-12015604; Score: 0.56
DE  Interaction: Q96PS8; IntAct: EBI-1050125,EBI-12820279; Score: 0.56
DE  Interaction: Q6UX40; IntAct: EBI-1050125,EBI-12845616; Score: 0.56
DE  Interaction: Q01453; IntAct: EBI-1050125,EBI-2845982; Score: 0.56
DE  Interaction: Q8N5I4; IntAct: EBI-1050125,EBI-3923585; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-1805738,EBI-1050125; Score: 0.35
DE  Interaction: P22315; IntAct: EBI-1050125,EBI-7174007; Score: 0.50
DE  Interaction: Q78IK4; IntAct: EBI-1050125,EBI-12523754; Score: 0.35
DE  Interaction: Q8CI59; IntAct: EBI-1050125,EBI-10767480; Score: 0.35
DE  Interaction: Q62351; IntAct: EBI-1050125,EBI-3869520; Score: 0.35
DE  Interaction: Q9CR62; IntAct: EBI-1050125,EBI-299894; Score: 0.35
DE  Interaction: Q60930; IntAct: EBI-1050125,EBI-444578; Score: 0.35
DE  Interaction: P51881; IntAct: EBI-1050125,EBI-445370; Score: 0.35
DE  Interaction: P48962; IntAct: EBI-1050125,EBI-299469; Score: 0.35
DE  Interaction: Q61102; IntAct: EBI-1050125,EBI-6907927; Score: 0.35
DE  Interaction: Q9JI39; IntAct: EBI-1050125,EBI-10767359; Score: 0.35
DE  Interaction: Q9Z2I9; IntAct: EBI-1050125,EBI-773730; Score: 0.35
DE  Interaction: P08680; IntAct: EBI-1050125,EBI-10767448; Score: 0.35
DE  Interaction: P58281; IntAct: EBI-1050125,EBI-776163; Score: 0.35
DE  Interaction: Q8CAQ8; IntAct: EBI-1050125,EBI-776087; Score: 0.35
DE  Interaction: Q80UU9; IntAct: EBI-1050125,EBI-1634859; Score: 0.35
DE  Interaction: O55022; IntAct: EBI-1050125,EBI-770756; Score: 0.35
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0020037;
GO  GO:0015232;
GO  GO:0005496;
GO  GO:0003707;
GO  GO:0060612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGL
SQ  GAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCL
SQ  DKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD
//
ID  Q2T9M1;
PN  PRKCA-binding protein;
GN  PICK1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q2T9M1;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098842;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0032588;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0019904;
GO  GO:0005080;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0021782;
GO  GO:0006886;
GO  GO:0060292;
GO  GO:0034316;
GO  GO:0002092;
GO  GO:0043113;
GO  GO:0034315;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLGYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQEHVQDIVLQLQRFVSTMSKYYNDCYSVLRDADVFPIEVDLAHTTLAYGLSQDEFTDGEDEEDEDEEDTAAGEPPRD
SQ  SRGAAGPLDKGGSWCNS
//
ID  O54943;
PN  Period circadian protein homolog 2;
GN  Per2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:22208286}. Cytoplasm, perinuclear region. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization.
DR  UNIPROT: O54943;
DR  UNIPROT: O54954;
DR  PDB: 3GDI;
DR  PDB: 4CT0;
DR  PDB: 4U8H;
DR  Pfam: PF08447;
DR  Pfam: PF12114;
DR  PROSITE: PS50112;
DE  Function: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock- controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK- ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:16595674, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:17404161, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22504074, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:23977055, ECO:0000269|PubMed:24413057}.
DE  Reference Proteome: Yes;
DE  Interaction: Q923E4; IntAct: EBI-1802585,EBI-1266779; Score: 0.35
DE  Interaction: O08785; IntAct: EBI-79859,EBI-1266779; Score: 0.78
DE  Interaction: Q96EB6; IntAct: EBI-1802965,EBI-1266779; Score: 0.44
DE  Interaction: Q9WTL8-2; IntAct: EBI-644559,EBI-1266779; Score: 0.37
DE  Interaction: Q9WTL8; IntAct: EBI-1266779,EBI-644534; Score: 0.73
DE  Interaction: Q3ULA2; IntAct: EBI-896325,EBI-1266779; Score: 0.35
DE  Interaction: P97784; IntAct: EBI-1266779,EBI-1266607; Score: 0.97
DE  Interaction: Q9JMK2; IntAct: EBI-771709,EBI-1266779; Score: 0.75
DE  Interaction: Q9R194; IntAct: EBI-1266619,EBI-1266779; Score: 0.88
DE  Interaction: P67870; IntAct: EBI-1266779,EBI-348169; Score: 0.37
DE  Interaction: O14503; IntAct: EBI-1266779,EBI-711810; Score: 0.37
DE  Interaction: Q06486; IntAct: EBI-2910316,EBI-1266779; Score: 0.37
DE  Interaction: P51449; IntAct: EBI-1266779,EBI-3908771; Score: 0.37
DE  Interaction: Q99PV5; IntAct: EBI-6143801,EBI-1266779; Score: 0.37
DE  Interaction: Q16526; IntAct: EBI-741297,EBI-1266779; Score: 0.35
DE  Interaction: Q60953; IntAct: EBI-1266779,EBI-3895605; Score: 0.46
DE  Interaction: P29590; IntAct: EBI-295890,EBI-1266779; Score: 0.27
DE  Interaction: Q8C4V4; IntAct: EBI-1266779,EBI-1266589; Score: 0.59
DE  Interaction: Q8BFZ4; IntAct: EBI-6898235,EBI-1266779; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042826;
GO  GO:1990226;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0035257;
GO  GO:0036002;
GO  GO:0070063;
GO  GO:0000978;
GO  GO:0003713;
GO  GO:0001222;
GO  GO:0008134;
GO  GO:0000976;
GO  GO:0032922;
GO  GO:0097167;
GO  GO:0007623;
GO  GO:0043153;
GO  GO:0006631;
GO  GO:0006094;
GO  GO:0005978;
GO  GO:0070932;
GO  GO:0019249;
GO  GO:0042754;
GO  GO:0060567;
GO  GO:0070345;
GO  GO:0031397;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0045892;
GO  GO:0120162;
GO  GO:0051726;
GO  GO:0042752;
GO  GO:0051946;
GO  GO:0050796;
GO  GO:0050767;
GO  GO:0019229;
GO  GO:0002931;
GO  GO:0009416;
GO  GO:0050872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFR
SQ  LMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSE
SQ  SQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSY
SQ  TTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYE
SQ  APRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRT
SQ  RNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGY
SQ  GSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVAEMQSSPPAQVKAVTTIERDS
SQ  SGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESCSEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTS
SQ  HTEVSAHLSSLTLPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKE
SQ  VLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKTGKNRKLKSKRVKTRDSSEST
SQ  GSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVPAYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQ
SQ  PEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTP
SQ  PAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGTSRDRQPKAPPTCNEPSDTQN
SQ  SDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMI
SQ  PDTEESEQFIKYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGG
SQ  LPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT
//
ID  Q9LVD0;
PN  18S rRNA (guanine-N(7))-methyltransferase RID2;
GN  RID2;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:21401745}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:P25627}. Nucleus, nucleolus {ECO:0000269|PubMed:21401745}.
DR  UNIPROT: Q9LVD0;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DE  Function: Essential protein (PubMed:21401745). S-adenosyl-L-methionine- dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity). Involved in the pre-rRNA processing steps in the nucleolus leading to small- subunit rRNA production independently of its RNA-modifying catalytic activity. Supports cell proliferation (PubMed:21401745). Required for the initiation of lateral root primordia formation and for the root apical meristem (RAM) organization as well as for leaves development (PubMed:14522871). During callus formation from hypocotyl and root explants, required for the initial stage of reactivation of cell proliferation in the hypocotyl stele (PubMed:21401745). Involved in leaf polarity establishment by functioning cooperatively with AS2 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures (PubMed:27334696). {ECO:0000250|UniProtKB:P25627, ECO:0000269|PubMed:14522871, ECO:0000269|PubMed:21401745, ECO:0000269|PubMed:27334696}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016435;
GO  GO:1990110;
GO  GO:0048527;
GO  GO:0010078;
GO  GO:0048364;
GO  GO:0070476;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNRPELLAPPEIFYDDTEARKYTSSSRIVEIQAKLSERALELLALPEDGVPRFLLDIGCGSGLSGETLSEDGHHWIGLD
SQ  ISASMLHVAVEREVEGDLLLGDMGQGLGLRSGVIDGAISISAVQWLCNADKSSHEPRLRLKAFFGSLYRCLSRGARAVFQ
SQ  VYPENIAQRELILRQALQAGFGGGLVVDYPHSTKKRKEFLVLTCGTVQTSIQTSKNEYDESCSEDDNSDDEESEEVGVSD
SQ  RNRPRKRQRTNTKVKGREWVLRKKEQSRRKGKNVPADSKFTSRKRRTRF
//
ID  Q684P5;
PN  Rap1 GTPase-activating protein 2;
GN  RAP1GAP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15632203}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15632203}.
DR  UNIPROT: Q684P5;
DR  UNIPROT: B2RTY5;
DR  UNIPROT: Q684P4;
DR  UNIPROT: Q6AI00;
DR  UNIPROT: Q6ZVF0;
DR  UNIPROT: Q9UPW2;
DR  Pfam: PF02145;
DR  PROSITE: PS50085;
DR  OMIM: 618714;
DR  DisGeNET: 23108;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP- bound state. {ECO:0000269|PubMed:15632203}.
DE  Reference Proteome: Yes;
DE  Interaction: P62258; IntAct: EBI-356498,EBI-3452992; Score: 0.37
DE  Interaction: Q9H4A3; IntAct: EBI-3452992,EBI-457907; Score: 0.37
DE  Interaction: Q6FHY5; IntAct: EBI-16439278,EBI-3452992; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-3452992; Score: 0.35
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0043005;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0010977;
GO  GO:0008361;
GO  GO:0051056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQK
SQ  NKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRH
SQ  FLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVL
SQ  YPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVE
SQ  SVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYK
SQ  VSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGP
SQ  EEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPI
SQ  KRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSS
SQ  TSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDK
SQ  LSHASSGAGH
//
ID  Q4R834;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  SIRT2;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody {ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome {ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000250}. Cell projection {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Myelin membrane {ECO:0000250}. Note=Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. Colocalizes with PARD3 in internodal region of axons. Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6}.
DR  UNIPROT: Q4R834;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha- tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia- reoxygenation conditions. Plays a role as tumor suppressor (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0005720;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0004407;
GO  GO:0070403;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0033558;
GO  GO:0016740;
GO  GO:0042903;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0048012;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0022011;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045599;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0051726;
GO  GO:0031641;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVI
SQ  CLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGL
SQ  LLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLP
SQ  ARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMILGLGGGMDFDSKKAYRDVAW
SQ  LGDCDQGCLALAELLGWKKELEDLVRREHASIDAQSGAEAPNPSTSASPRKSPPPAQDEARTTEREKPQ
//
ID  Q08231;
PN  Nuclear mRNA export protein THP1;
GN  THP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores.
DR  UNIPROT: Q08231;
DR  UNIPROT: D6W1Z5;
DR  PDB: 3T5V;
DR  PDB: 4TRQ;
DR  PDB: 5G5P;
DR  PDB: 5L3T;
DR  PDB: 5UBP;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro. {ECO:0000269|PubMed:11139493, ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:12702719}.
DE  Reference Proteome: Yes;
DE  Interaction: P46674; IntAct: EBI-32097,EBI-16425; Score: 0.88
DE  Interaction: P10591; IntAct: EBI-8591,EBI-32097; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-8680,EBI-32097; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-32097,EBI-8627; Score: 0.35
DE  Interaction: Q05931; IntAct: EBI-32097,EBI-35227; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-32097; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-32097,EBI-8603; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-32097,EBI-8648; Score: 0.35
DE  Interaction: Q6WNK7; IntAct: EBI-1251050,EBI-32097; Score: 0.78
DE  Interaction: P21576; IntAct: EBI-32097,EBI-20460; Score: 0.35
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0000282;
GO  GO:0031124;
GO  GO:0006406;
GO  GO:0071033;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006368;
GO  GO:0006283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTRFKIMCTSFLNYARDVDPWSA
SQ  WSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFIINLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPR
SQ  GNASSTNIPGKQRILLYLVNKLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF
SQ  VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWSVLYKHVRYGNIQGVSLWLRQ
SQ  NERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQNKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNV
SQ  ENVLVTLINLGLLRANCFPQLQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
//
ID  Q13530;
PN  Serine incorporator 3;
GN  SERINC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q86VE9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9QZI9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9QZI9}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:26416734}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (Probable). {ECO:0000305|PubMed:26416734}.
DR  UNIPROT: Q13530;
DR  UNIPROT: B4DUE9;
DR  UNIPROT: O43717;
DR  UNIPROT: Q9BR33;
DR  Pfam: PF03348;
DR  OMIM: 607165;
DR  DisGeNET: 10955;
DE  Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.
DE  Reference Proteome: Yes;
DE  Interaction: P62841; IntAct: EBI-372635,EBI-1045571; Score: 0.37
DE  Interaction: A0A286YCX6; IntAct: EBI-11119299,EBI-1045571; Score: 0.35
DE  Interaction: O95393; IntAct: EBI-3922513,EBI-1045571; Score: 0.37
DE  Interaction: P53985; IntAct: EBI-1054708,EBI-1045571; Score: 0.40
DE  Interaction: P45880; IntAct: EBI-354022,EBI-1045571; Score: 0.40
DE  Interaction: Q9HAV4; IntAct: EBI-517949,EBI-1045571; Score: 0.40
DE  Interaction: Q9P035; IntAct: EBI-359013,EBI-1045571; Score: 0.40
DE  Interaction: Q9Y277; IntAct: EBI-354196,EBI-1045571; Score: 0.40
DE  Interaction: P33947; IntAct: EBI-1056498,EBI-1045571; Score: 0.40
DE  Interaction: O15260; IntAct: EBI-1045571,EBI-1044848; Score: 0.40
DE  Interaction: P24390; IntAct: EBI-1043076,EBI-1045571; Score: 0.40
DE  Interaction: Q99623; IntAct: EBI-358348,EBI-1045571; Score: 0.40
DE  Interaction: Q13263; IntAct: EBI-78139,EBI-1045571; Score: 0.40
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0051607;
GO  GO:0009597;
GO  GO:0045087;
GO  GO:0006564;
GO  GO:0006658;
GO  GO:1902237;
GO  GO:0006665;
GO  GO:0016032;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHE
SQ  ADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVW
SQ  FVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFF
SQ  ISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVV
SQ  PTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEG
SQ  VQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS
//
ID  F4JS25;
PN  Suppressor of RPS4-RLD 1;
GN  SRFR1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:21079790}. Cytoplasm {ECO:0000269|PubMed:18774967}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18774967}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:21079790}. Note=Found in microsomes when interacting with SNC1 and RPS4. {ECO:0000269|PubMed:21079790}.
DR  UNIPROT: F4JS25;
DR  UNIPROT: Q8GYX1;
DR  UNIPROT: Q9SZU6;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Negative regulator of effector-triggered immunity associated with the EDS1 resistance pathway (PubMed:15469494, PubMed:18774967, PubMed:19649196, PubMed:19525323, PubMed:20862316, PubMed:21079790). May localize its interactors to a microsomal membrane (PubMed:22158819). May therefore negatively regulate RPS4 and SNC1 translocation to the nucleus (PubMed:21079790). Contributes to the regulation of RPS2 and RPS4 protein levels and negatively regulates SNC1 stability (PubMed:20862316). {ECO:0000269|PubMed:15469494, ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:19525323, ECO:0000269|PubMed:19649196, ECO:0000269|PubMed:20862316, ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22158819}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9SUR9; IntAct: EBI-1778186,EBI-4436454; Score: 0.37
DE  Interaction: Q9SUT5; IntAct: EBI-1581364,EBI-4436454; Score: 0.37
DE  Interaction: Q9FPR2; IntAct: EBI-4481446,EBI-4436454; Score: 0.44
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042742;
GO  GO:0009816;
GO  GO:0031348;
GO  GO:0045892;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATATATSERFELAKHCSSRNWSKAIRVLDSLLAKESSILDICNRAFCYNQLELHKHVIKDCDKALLLEPFAIQAFILKG
SQ  RALLALGRKQEAVLVLEQGYKSALQQTADVKQLLELEELLKDARREIDGILKSHATESPQETPAYHSEKSDEKSDKLDNH
SQ  ESGASSNGNSHESSSELGEQSKIVSFSKVASKASKQSDGNSDLCNGSVYKEKENGKCGSQINGYYESCKPCNGSDLHDNL
SQ  AESSDRFGELSINGNKISIKSSKMSHKAEARCGISDESRKNKKYTIARISGTHSISVDFRLSRGIAQVNEGNYTKAISIF
SQ  DKVLKEEPTYPEALIGRGTAYAFQRELESAIADFTKAIQSNPAASEAWKRRGQARAALGEYVEAVEDLTKALVFEPNSPD
SQ  VLHERGIVNFKSKDFTAAVKDLSICLKQEKDNKSAYTYLGLAFASLGEYKKAEEAHLKSIQLDSNYLEAWLHLAQFYQEL
SQ  ADHCKALECIEQVLQVDNRVWKAYHLRGLVFHGLGEHRKAIQELSIGLSIENTIECLYLRGSCYHAVGEYRDAVKDYDAT
SQ  VDVELDAVEKFVLQCLAFYQKELALYTASKVSSEFLCFDIDGDIDPMFKEYWCKRLHPKNVCEKVYRQPPLRESLKKGKL
SQ  KKQDLAITKQKANILRFADLIGKRIQYDCPGFLPNKRQHRMAGLAVIEIAQKVSKAWRIEWRNSTKGTTKNGKKNRRRER
SQ  TNILSQNRGGAGCSSSSFSETSTGYASLEDRSSGRSILSWQDVYSPAVRWRQISEPCDPVVWVNKLSEEFNSGFGSHTPM
SQ  VLGQAKVVRYFPNYERTLTLAKSIIKDKLSVRSKKDKVIDLSKDEKIEKIMRAETCDELHNIVGEDFWVATWCDSTGSEG
SQ  KRLEGTRITCIQKPGRLGYDFSIRTPCTPARWSDFDEEMTSAWEALCTAYCGENYGSTELDALETVRDAILRMTYYWYNF
SQ  MPLARGTAVTGFVVLLGLLLAANMEFTETIPKGLQIDWEAILNVEPGSFVDSVKSWLYPSLKINTSWRDHTEISSAFSTT
SQ  GAVVAALSTYND
//
ID  P39015;
PN  Suppressor protein STM1;
GN  STM1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Concentrated in the perinuclear region.
DR  UNIPROT: P39015;
DR  UNIPROT: D6VYE5;
DR  PDB: 4U3M;
DR  PDB: 4U3N;
DR  PDB: 4U3U;
DR  PDB: 4U4N;
DR  PDB: 4U4O;
DR  PDB: 4U4Q;
DR  PDB: 4U4R;
DR  PDB: 4U4U;
DR  PDB: 4U4Y;
DR  PDB: 4U4Z;
DR  PDB: 4U50;
DR  PDB: 4U51;
DR  PDB: 4U52;
DR  PDB: 4U53;
DR  PDB: 4U55;
DR  PDB: 4U56;
DR  PDB: 4U6F;
DR  PDB: 4V88;
DR  PDB: 4V8Y;
DR  PDB: 4V8Z;
DR  PDB: 5DAT;
DR  PDB: 5DC3;
DR  PDB: 5DGE;
DR  PDB: 5FCI;
DR  PDB: 5FCJ;
DR  PDB: 5I4L;
DR  PDB: 5LYB;
DR  PDB: 5NDG;
DR  PDB: 5NDV;
DR  PDB: 5NDW;
DR  PDB: 5OBM;
DR  PDB: 5TGA;
DR  PDB: 5TGM;
DR  PDB: 6HHQ;
DR  Pfam: PF09598;
DE  Function: Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death. {ECO:0000269|PubMed:15044472}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-20589,EBI-11238; Score: 0.35
DE  Interaction: P39940; IntAct: EBI-11238,EBI-16219; Score: 0.44
DE  Interaction: P43582; IntAct: EBI-11238,EBI-22766; Score: 0.44
DE  Interaction: P40318; IntAct: EBI-11238,EBI-18208; Score: 0.44
DE  Interaction: P46995; IntAct: EBI-11238,EBI-16985; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-11238,EBI-6679; Score: 0.44
DE  Interaction: P33203; IntAct: EBI-11238,EBI-701; Score: 0.44
DE  Interaction: Q06525; IntAct: EBI-11238,EBI-35138; Score: 0.44
DE  Interaction: P10591; IntAct: EBI-8591,EBI-11238; Score: 0.53
DE  Interaction: P40454; IntAct: EBI-25278,EBI-11238; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-11238,EBI-8627; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-11238,EBI-24570; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-11238,EBI-8632; Score: 0.35
DE  Interaction: P22943; IntAct: EBI-8548,EBI-11238; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-17244,EBI-11238; Score: 0.35
DE  Interaction: Q08687; IntAct: EBI-34720,EBI-11238; Score: 0.35
DE  Interaction: P32790; IntAct: EBI-17313,EBI-11238; Score: 0.35
DE  Interaction: P38199; IntAct: EBI-21217,EBI-11238; Score: 0.35
DE  Interaction: P07280; IntAct: EBI-14536,EBI-11238; Score: 0.35
DE  Interaction: P38968; IntAct: EBI-20524,EBI-11238; Score: 0.35
DE  Interaction: P11632; IntAct: EBI-12019,EBI-11238; Score: 0.35
DE  Interaction: P38700; IntAct: EBI-2705,EBI-11238; Score: 0.27
DE  Interaction: P32357; IntAct: EBI-340,EBI-11238; Score: 0.27
DE  Interaction: P38285; IntAct: EBI-20853,EBI-11238; Score: 0.27
DE  Interaction: P40522; IntAct: EBI-11238,EBI-25035; Score: 0.27
DE  Interaction: Q12389; IntAct: EBI-5644,EBI-11238; Score: 0.27
DE  Interaction: P00330; IntAct: EBI-2218,EBI-11238; Score: 0.27
DE  Interaction: Q02486; IntAct: EBI-2028,EBI-11238; Score: 0.27
DE  Interaction: P02293; IntAct: EBI-8088,EBI-11238; Score: 0.27
DE  Interaction: P38822; IntAct: EBI-3889,EBI-11238; Score: 0.27
DE  Interaction: Q12114; IntAct: EBI-4640,EBI-11238; Score: 0.35
DE  Interaction: P07270; IntAct: EBI-13378,EBI-11238; Score: 0.35
DE  Interaction: P22082; IntAct: EBI-17526,EBI-11238; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003677;
GO  GO:0043022;
GO  GO:0042162;
GO  GO:0045142;
GO  GO:0043066;
GO  GO:0043558;
GO  GO:0000723;
GO  GO:0031929;
GO  GO:0006414;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSA
SQ  TTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQAN
SQ  NQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGR
SQ  GARKGNNTANATNSANTVQKNRNIDVSNLPSLA
//
ID  P22147;
PN  5'-3' exoribonuclease 1;
GN  XRN1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body.
DR  UNIPROT: P22147;
DR  UNIPROT: D6VTX9;
DR  PDB: 6Q8Y;
DR  Pfam: PF18129;
DR  Pfam: PF18332;
DR  Pfam: PF18334;
DR  Pfam: PF18194;
DR  Pfam: PF17846;
DR  Pfam: PF03159;
DE  Function: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus- like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post- transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth. {ECO:0000269|PubMed:10454540, ECO:0000269|PubMed:11142370, ECO:0000269|PubMed:11238889, ECO:0000269|PubMed:11910109, ECO:0000269|PubMed:12423748, ECO:0000269|PubMed:12799443, ECO:0000269|PubMed:12853617, ECO:0000269|PubMed:14561886, ECO:0000269|PubMed:14690598, ECO:0000269|PubMed:14729943, ECO:0000269|PubMed:15013450, ECO:0000269|PubMed:15358132, ECO:0000269|PubMed:15967792, ECO:0000269|PubMed:15989963, ECO:0000269|PubMed:16240118, ECO:0000269|PubMed:16373495, ECO:0000269|PubMed:16501073, ECO:0000269|PubMed:16714281, ECO:0000269|PubMed:16885161, ECO:0000269|PubMed:17761681, ECO:0000269|PubMed:18162578, ECO:0000269|PubMed:18443146, ECO:0000269|PubMed:18469165, ECO:0000269|PubMed:18640978, ECO:0000269|PubMed:18676807, ECO:0000269|PubMed:18715869, ECO:0000269|PubMed:19324962, ECO:0000269|PubMed:2076815, ECO:0000269|PubMed:7597069, ECO:0000269|PubMed:7926736, ECO:0000269|PubMed:9315672, ECO:0000269|PubMed:9482746, ECO:0000269|PubMed:9488433, ECO:0000269|PubMed:9685486, ECO:0000269|PubMed:9742129}.
DE  Reference Proteome: Yes;
DE  Interaction: P39523; IntAct: EBI-27256,EBI-9642; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-8591,EBI-9642; Score: 0.53
DE  Interaction: P53940; IntAct: EBI-2612341,EBI-9642; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-22339,EBI-9642; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-9642,EBI-8648; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-8627,EBI-9642; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-8603,EBI-9642; Score: 0.53
DE  Interaction: P33416; IntAct: EBI-9642,EBI-8680; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-9642,EBI-24570; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-9642,EBI-8659; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-505,EBI-9642; Score: 0.53
DE  Interaction: P30822; IntAct: EBI-20589,EBI-9642; Score: 0.35
DE  Interaction: P32495; IntAct: EBI-12014,EBI-9642; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-6302,EBI-9642; Score: 0.35
DE  Interaction: P40070; IntAct: EBI-188,EBI-9642; Score: 0.68
DE  Interaction: P53730; IntAct: EBI-28496,EBI-9642; Score: 0.35
DE  Interaction: Q12180; IntAct: EBI-37549,EBI-9642; Score: 0.35
DE  Interaction: P38112; IntAct: EBI-10394,EBI-9642; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-8936,EBI-9642; Score: 0.35
DE  Interaction: Q12230; IntAct: EBI-34978,EBI-9642; Score: 0.56
DE  Interaction: P50094; IntAct: EBI-9195,EBI-9642; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-11835,EBI-9642; Score: 0.35
DE  Interaction: P36520; IntAct: EBI-15501,EBI-9642; Score: 0.35
DE  Interaction: P25644; IntAct: EBI-204,EBI-9642; Score: 0.67
DE  Interaction: P07347; IntAct: EBI-2796,EBI-9642; Score: 0.35
DE  Interaction: P39935; IntAct: EBI-9002,EBI-9642; Score: 0.35
DE  Interaction: P33759; IntAct: EBI-413,EBI-9642; Score: 0.35
DE  Interaction: P32588; IntAct: EBI-14231,EBI-9642; Score: 0.35
DE  Interaction: P39928; IntAct: EBI-17357,EBI-9642; Score: 0.35
DE  Interaction: P38934; IntAct: EBI-3593,EBI-9642; Score: 0.35
DE  Interaction: P38996; IntAct: EBI-11776,EBI-9642; Score: 0.35
DE  Interaction: P50095; IntAct: EBI-9190,EBI-9642; Score: 0.35
DE  Interaction: P28007; IntAct: EBI-7321,EBI-9642; Score: 0.35
DE  Interaction: P53917; IntAct: EBI-28900,EBI-9642; Score: 0.35
DE  Interaction: Q07508; IntAct: EBI-673,EBI-9642; Score: 0.35
DE  Interaction: P06102; IntAct: EBI-12165,EBI-9642; Score: 0.35
DE  Interaction: P21954; IntAct: EBI-8898,EBI-9642; Score: 0.35
DE  Interaction: P57743; IntAct: EBI-10227,EBI-9642; Score: 0.69
DE  Interaction: P38199; IntAct: EBI-21217,EBI-9642; Score: 0.35
DE  Interaction: P37838; IntAct: EBI-12122,EBI-9642; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-15881,EBI-9642; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-20647,EBI-9642; Score: 0.35
DE  Interaction: P47017; IntAct: EBI-174,EBI-9642; Score: 0.69
DE  Interaction: P53849; IntAct: EBI-29244,EBI-9642; Score: 0.35
DE  Interaction: P07280; IntAct: EBI-14536,EBI-9642; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-20627,EBI-9642; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-8076,EBI-9642; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-18146,EBI-9642; Score: 0.56
DE  Interaction: P53883; IntAct: EBI-29032,EBI-9642; Score: 0.67
DE  Interaction: P38203; IntAct: EBI-180,EBI-9642; Score: 0.68
DE  Interaction: Q03782; IntAct: EBI-627,EBI-9642; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-12228,EBI-9642; Score: 0.35
DE  Interaction: P41544; IntAct: EBI-25763,EBI-9642; Score: 0.35
DE  Interaction: P42846; IntAct: EBI-28360,EBI-9642; Score: 0.35
DE  Interaction: P46677; IntAct: EBI-18855,EBI-9642; Score: 0.35
DE  Interaction: Q06406; IntAct: EBI-196,EBI-9642; Score: 0.69
DE  Interaction: P07260; IntAct: EBI-150,EBI-9642; Score: 0.61
DE  Interaction: Q12339; IntAct: EBI-30231,EBI-9642; Score: 0.35
DE  Interaction: P51998; IntAct: EBI-450,EBI-9642; Score: 0.35
DE  Interaction: P27476; IntAct: EBI-12274,EBI-9642; Score: 0.35
DE  Interaction: P31334; IntAct: EBI-15497,EBI-9642; Score: 0.35
DE  Interaction: P46995; IntAct: EBI-16985,EBI-9642; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-9152,EBI-9642; Score: 0.35
DE  Interaction: P53550; IntAct: EBI-9642,EBI-270; Score: 0.55
DE  Interaction: Q12517; IntAct: EBI-9642,EBI-38519; Score: 0.44
DE  Interaction: P53905; IntAct: EBI-141,EBI-9642; Score: 0.56
DE  Interaction: P40089; IntAct: EBI-10236,EBI-9642; Score: 0.69
DE  Interaction: P33322; IntAct: EBI-4105,EBI-9642; Score: 0.61
DE  Interaction: P39998; IntAct: EBI-22300,EBI-9642; Score: 0.35
DE  Interaction: P38789; IntAct: EBI-18160,EBI-9642; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-340,EBI-9642; Score: 0.27
DE  Interaction: P20448; IntAct: EBI-5612,EBI-9642; Score: 0.27
DE  Interaction: P07246; IntAct: EBI-2227,EBI-9642; Score: 0.27
DE  Interaction: P23293; IntAct: EBI-17078,EBI-9642; Score: 0.53
DE  Interaction: P32493; IntAct: EBI-11898,EBI-9642; Score: 0.27
DE  Interaction: P07270; IntAct: EBI-13378,EBI-9642; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-20777,EBI-9642; Score: 0.35
DE  Interaction: Q04264; IntAct: EBI-13077,EBI-9642; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0090512;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004534;
GO  GO:0003682;
GO  GO:0003729;
GO  GO:0000741;
GO  GO:0061157;
GO  GO:0016242;
GO  GO:0070651;
GO  GO:0000956;
GO  GO:0000184;
GO  GO:0032968;
GO  GO:0060261;
GO  GO:0006364;
GO  GO:0043144;
GO  GO:0007089;
GO  GO:0016078;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIPKFFRYISERWPMILQLIEGTQIPEFDNLYLDMNSILHNCTHGNDDDVTKRLTEEEVFAKICTYIDHLFQTIKPKKI
SQ  FYMAIDGVAPRAKMNQQRARRFRTAMDAEKALKKAIENGDEIPKGEPFDSNSITPGTEFMAKLTKNLQYFIHDKISNDSK
SQ  WREVQIIFSGHEVPGEGEHKIMNFIRHLKSQKDFNQNTRHCIYGLDADLIMLGLSTHGPHFALLREEVTFGRRNSEKKSL
SQ  EHQNFYLLHLSLLREYMELEFKEIADEMQFEYNFERILDDFILVMFVIGNDFLPNLPDLHLNKGAFPVLLQTFKEALLHT
SQ  DGYINEHGKINLKRLGVWLNYLSQFELLNFEKDDIDVEWFNKQLENISLEGERKRQRVGKKLLVKQQKKLIGSIKPWLME
SQ  QLQEKLSPDLPDEEIPTLELPKDLDMKDHLEFLKEFAFDLGLFITHSKSKGSYSLKMDLDSINPDETEEEFQNRVNSIRK
SQ  TIKKYQNAIIVEDKEELETEKTIYNERFERWKHEYYHDKLKFTTDSEEKVRDLAKDYVEGLQWVLYYYYRGCPSWSWYYP
SQ  HHYAPRISDLAKGLDQDIEFDLSKPFTPFQQLMAVLPERSKNLIPPAFRPLMYDEQSPIHDFYPAEVQLDKNGKTADWEA
SQ  VVLISFVDEKRLIEAMQPYLRKLSPEEKTRNQFGKDLIYSFNPQVDNLYKSPLGGIFSDIEHNHCVEKEYITIPLDSSEI
SQ  RYGLLPNAKLGAEMLAGFPTLLSLPFTSSLEYNETMVFQQPSKQQSMVLQITDIYKTNNVTLEDFSKRHLNKVIYTRWPY
SQ  LRESKLVSLTDGKTIYEYQESNDKKKFGFITKPAETQDKKLFNSLKNSMLRMYAKQKAVKIGPMEAIATVFPVTGLVRDS
SQ  DGGYIKTFSPTPDYYPLQLVVESVVNEDERYKERGPIPIEEEFPLNSKVIFLGDYAYGGETTIDGYSSDRRLKITVEKKF
SQ  LDSEPTIGKERLQMDHQAVKYYPSYIVSKNMHLHPLFLSKITSKFMITDATGKHINVGIPVKFEARHQKVLGYARRNPRG
SQ  WEYSNLTLNLLKEYRQTFPDFFFRLSKVGNDIPVLEDLFPDTSTKDAMNLLDGIKQWLKYVSSKFIAVSLESDSLTKTSI
SQ  AAVEDHIMKYAANIEGHERKQLAKVPREAVLNPRSSFALLRSQKFDLGDRVVYIQDSGKVPIFSKGTVVGYTTLSSSLSI
SQ  QVLFDHEIVAGNNFGGRLRTNRGLGLDASFLLNITNRQFIYHSKASKKALEKKKQSNNRNNNTKTAHKTPSKQQSEEKLR
SQ  KERAHDLLNFIKKDTNEKNSESVDNKSMGSQKDSKPAKKVLLKRPAQKSSENVQVDLANFEKAPLDNPTVAGSIFNAVAN
SQ  QYSDGIGSNLNIPTPPHPMNVVGGPIPGANDVADVGLPYNIPPGFMTHPNGLHPLHPHQMPYPNMNGMSIPPPAPHGFGQ
SQ  PISFPPPPPMTNVSDQGSRIVVNEKESQDLKKFINGKQHSNGSTIGGETKNSRKGEIKPSSGTNSTECQSPKSQSNAADR
SQ  DNKKDEST
//
ID  P39929;
PN  Vacuolar-sorting protein SNF7;
GN  SNF7;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12194857}. Endosome membrane {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}; Peripheral membrane protein {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}. Nucleus envelope {ECO:0000269|PubMed:25303532}.
DR  UNIPROT: P39929;
DR  UNIPROT: D6VY27;
DR  UNIPROT: E9P8V6;
DR  PDB: 5FD7;
DR  PDB: 5FD9;
DR  PDB: 5T8L;
DR  PDB: 5T8N;
DR  Pfam: PF03357;
DE  Function: Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed:11559748, PubMed:12194857). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857). Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499). ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499). SNF7 is the most abundant ESCRT-III subunit which forms membrane- sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543). Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543). SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593). The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593). SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532). {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:15935782, ECO:0000269|PubMed:24139821, ECO:0000269|PubMed:24711499, ECO:0000269|PubMed:25303532, ECO:0000269|PubMed:26522593, ECO:0000269|PubMed:3062374}.
DE  Reference Proteome: Yes;
DE  Interaction: P38181; IntAct: EBI-11756,EBI-17554; Score: 0.44
DE  Interaction: Self; IntAct: EBI-17554,EBI-17554; Score: 0.83
DE  Interaction: Q04272; IntAct: EBI-17554,EBI-28157; Score: 0.76
DE  Interaction: Q02796; IntAct: EBI-30514,EBI-17554; Score: 0.35
DE  Interaction: Q07979; IntAct: EBI-36549,EBI-17554; Score: 0.35
DE  Interaction: P40340; IntAct: EBI-19030,EBI-17554; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-17554,EBI-8591; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-17554,EBI-8627; Score: 0.35
DE  Interaction: Q05931; IntAct: EBI-17554,EBI-35227; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-8603,EBI-17554; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-3003,EBI-17554; Score: 0.35
DE  Interaction: Q12495; IntAct: EBI-3913,EBI-17554; Score: 0.35
DE  Interaction: Q03281; IntAct: EBI-22131,EBI-17554; Score: 0.58
DE  Interaction: Q03707; IntAct: EBI-17554,EBI-18064; Score: 0.37
DE  Interaction: P48582; IntAct: EBI-17554,EBI-3768; Score: 0.64
DE  Interaction: P36108; IntAct: EBI-26574,EBI-17554; Score: 0.53
DE  Interaction: Q12483; IntAct: EBI-17554,EBI-30277; Score: 0.62
DE  Interaction: P47142; IntAct: EBI-17554,EBI-25595; Score: 0.55
DE  Interaction: Q06696; IntAct: EBI-17554,EBI-36540; Score: 0.55
DE  Interaction: P08539; IntAct: EBI-17554,EBI-7376; Score: 0.27
DE  Interaction: P52917; IntAct: EBI-20475,EBI-17554; Score: 0.68
DE  Interaction: Q08817; IntAct: EBI-17554,EBI-30849; Score: 0.37
GO  GO:0005737;
GO  GO:0000815;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:1904669;
GO  GO:0071454;
GO  GO:1904902;
GO  GO:0070676;
GO  GO:0045324;
GO  GO:0015031;
GO  GO:0061709;
GO  GO:0043162;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKV
SQ  EGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDE
SQ  DELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL
//
ID  Q86UE8;
PN  Serine/threonine-protein kinase tousled-like 2;
GN  TLK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.
DR  UNIPROT: Q86UE8;
DR  UNIPROT: D3DU07;
DR  UNIPROT: Q9UKI7;
DR  UNIPROT: Q9Y4F7;
DR  PDB: 5O0Y;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 608439;
DR  OMIM: 618050;
DR  DisGeNET: 11011;
DE  Function: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:9427565}.
DE  Disease: Mental retardation, autosomal dominant 57 (MRD57) [MIM:618050]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD57 is characterized by delayed psychomotor development apparent in infancy or early childhood, and a variety of behavioral abnormalities. Affected individuals may have severe gastro- intestinal problems, and facial dysmorphism. MRD57 inheritance is autosomal dominant. {ECO:0000269|PubMed:27479843, ECO:0000269|PubMed:29861108}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-1047967,EBI-1047967; Score: 0.56
DE  Interaction: Q0D2I5; IntAct: EBI-742894,EBI-1047967; Score: 0.27
DE  Interaction: Q53SF7; IntAct: EBI-2835780,EBI-1047967; Score: 0.27
DE  Interaction: Q15306; IntAct: EBI-751345,EBI-1047967; Score: 0.50
DE  Interaction: Q92985; IntAct: EBI-968267,EBI-1047967; Score: 0.50
DE  Interaction: Q15418; IntAct: EBI-963034,EBI-1047967; Score: 0.35
DE  Interaction: Q9NVP2; IntAct: EBI-1047967,EBI-1055650; Score: 0.40
DE  Interaction: Q8NHQ1; IntAct: EBI-739624,EBI-1047967; Score: 0.56
DE  Interaction: P26367; IntAct: EBI-747278,EBI-1047967; Score: 0.56
DE  Interaction: Q02548; IntAct: EBI-296331,EBI-1047967; Score: 0.56
DE  Interaction: Q96NE9-2; IntAct: EBI-13213391,EBI-1047967; Score: 0.56
DE  Interaction: Q9NPF5; IntAct: EBI-399105,EBI-1047967; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-10180829,EBI-1047967; Score: 0.56
DE  Interaction: Q96IK5; IntAct: EBI-2548508,EBI-1047967; Score: 0.56
DE  Interaction: Q96FJ2; IntAct: EBI-742371,EBI-1047967; Score: 0.51
DE  Interaction: P63167; IntAct: EBI-349105,EBI-1047967; Score: 0.51
DE  Interaction: Q9BWV3; IntAct: EBI-11898670,EBI-1047967; Score: 0.27
DE  Interaction: Q8IY63; IntAct: EBI-1057112,EBI-1047967; Score: 0.27
DE  Interaction: Q9UN30; IntAct: EBI-6911404,EBI-1047967; Score: 0.27
GO  GO:0005882;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0006325;
GO  GO:0007059;
GO  GO:0035556;
GO  GO:0010507;
GO  GO:0032435;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0001672;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPR
SQ  GHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLD
SQ  TEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLR
SQ  ANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQN
SQ  LIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLA
SQ  EYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAF
SQ  DLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHK
SQ  LMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGT
SQ  YWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRR
SQ  CLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
//
ID  P40383;
PN  5'-3' exoribonuclease 1;
GN  exo2;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
DR  UNIPROT: P40383;
DR  Pfam: PF18129;
DR  Pfam: PF18332;
DR  Pfam: PF18334;
DR  Pfam: PF17846;
DR  Pfam: PF03159;
DE  Function: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy (By similarity). Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004534;
GO  GO:0000287;
GO  GO:0004540;
GO  GO:0003723;
GO  GO:0000741;
GO  GO:0000184;
GO  GO:0090502;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIPKFFRWMSERYPLCSQLIENDRIPEFDNLYLDMNGILHNCTHKNDDHSSPPLPEEEMYIAIFNYIEHLFEKIKPKKL
SQ  LYMAVDGCAPRAKMNQQRSRRFRTAKDAHDARLKAERNGEDFPEEQFDSNCITPGTTFMERVSRQLYYFIHKKVTNDSQW
SQ  QNIEVIFSGHDCPGEGEHKIMEYIRTQKAQPSYNPNTRHCLYGLDADLIMLGLLSHDPHFCLLREEVTFGPASRNRSKEL
SQ  AHQKFYLLHLSLLREYLEFEFQECRSTFTFKYDLEKILDDFILLAFFVGNDFLPHLPGLHINEGALALMFSIYKKVMPSA
SQ  GGYINEKGVINMARLELILLELENFEKEIFKAEVSETKNNGNSDKPSFDFLKYITESTNDIKAMTGEQKNYFLQIKKFLS
SQ  SREPFIDFSANISSVDQRFLRRLCNDLHLSFSKIIKVDGTHLLRITFRDLEFNDEDEDEIEQDEIERVLQKYDNIPLLNE
SQ  EQALKEKNVEKDFIQWKDDYYRSKVGFSYYDEEALKAMAERYVEGLQWVLFYYYRGCQSWGWYYNYHFAPKISDVLKGLD
SQ  VKIDFKMGTPFRPFEQLMAVLPARSQALVPPCFRDLMVNSESPIIDFYPENFALDQNGKTASWEAVVIIPFIDETRLIDA
SQ  LASKDKFLTEEERKRNSFNAPTVFSLAEDYTSFYPSSLPSLFPDLVTRCIQKPYSLPSMEGKEYLVGLCPGVFLGAFGMV
SQ  GFPSFHTLKHKAELVYHGINVFGNESRNPSVIVNVEDVKSALTSEQIAMQYVGKRIFVDWPYLREAYVESAMDESYMYLA
SQ  SNSTIEKRDLAEIEKSQWGRKCSHKIREYSKRFGVLFGDISLLLQVRPIKGLEYTREGALVKIFNESVLEDYPAQLVVEK
SQ  IAIDDPRFTEREAPPVEVEYPPGTKAFHLGEYNYGRPAQITGCKDNKLIIWLSTAPGLDAQWGRVLVNDSKSKEKYYPSY
SQ  IVAKLLNIHPLLLSKITSSFLISNGTKRENIGLNLKFDARNQKVLGFSRKSTKGWEFSNKTVALVKEYINTFPQLFNILT
SQ  THATKDNLTVKDCFPKDDTQQLAAVKHWIKEKGINSLTRVSLDEDALDSDIIKLIEEKASTIDSTYQVPKKVFGVPRYAL
SQ  LKPSQTRGILHSQEFALGDRVVYVQDSGKVPIAAYGTVVGIMLHHLDVVFDLPFMSGTTLDGRCSPYHGMQVEVSMVLNV
SQ  TNPQFVVNTRAGKNRKTNVSANNVSQGTDSRLVTKPTSTFPSPPSPPSSSVWNKREHHPKPFSLHQVPPPESLIHKSKSK
SQ  FSKGNHHSTNGTQSIRGRGGKRGKPLRSKELNRKHDHIVQPMGKLQIN
//
ID  Q8NE71;
PN  ATP-binding cassette sub-family F member 1;
GN  ABCF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19570978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19570978}. Nucleus envelope {ECO:0000269|PubMed:19570978}.
DR  UNIPROT: Q8NE71;
DR  UNIPROT: A2BF75;
DR  UNIPROT: O14897;
DR  UNIPROT: Q69YP6;
DR  PDB: 5ZXD;
DR  Pfam: PF00005;
DR  Pfam: PF12848;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DR  OMIM: 603429;
DR  DisGeNET: 23;
DE  Function: Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. {ECO:0000269|PubMed:19570978}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-720571; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-78473,EBI-720571; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-714746,EBI-720571; Score: 0.35
DE  Interaction: P35550; IntAct: EBI-7817407,EBI-720571; Score: 0.35
DE  Interaction: Q16666-2; IntAct: EBI-6273540,EBI-720571; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-1058491,EBI-720571; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-8361659,EBI-720571; Score: 0.35
DE  Interaction: Q17RP2; IntAct: EBI-11051395,EBI-720571; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-396034,EBI-720571; Score: 0.35
DE  Interaction: O75530; IntAct: EBI-923794,EBI-720571; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-359031,EBI-720571; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-372051,EBI-720571; Score: 0.35
DE  Interaction: P51858; IntAct: EBI-3910118,EBI-720571; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-456179,EBI-720571; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-594661,EBI-720571; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-1220319,EBI-720571; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-539478,EBI-720571; Score: 0.44
DE  Interaction: Q9Y478; IntAct: EBI-720571,EBI-719769; Score: 0.40
DE  Interaction: Q96BK5; IntAct: EBI-720571,EBI-721782; Score: 0.40
DE  Interaction: Q9NX58; IntAct: EBI-720571,EBI-713507; Score: 0.40
DE  Interaction: Q13352; IntAct: EBI-720571,EBI-712105; Score: 0.37
DE  Interaction: P16333; IntAct: EBI-389883,EBI-720571; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-352469,EBI-720571; Score: 0.40
DE  Interaction: P0C0S5; IntAct: EBI-1199859,EBI-720571; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-358900,EBI-720571; Score: 0.40
DE  Interaction: Q5TID7; IntAct: EBI-7267656,EBI-720571; Score: 0.40
DE  Interaction: Q6UW60; IntAct: EBI-720571,EBI-13342757; Score: 0.40
DE  Interaction: P05204; IntAct: EBI-1758689,EBI-720571; Score: 0.40
DE  Interaction: Q68CZ1-2; IntAct: EBI-9356215,EBI-720571; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-720571; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-1222758,EBI-720571; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-5235485,EBI-720571; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005840;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0008135;
GO  GO:0006954;
GO  GO:0045727;
GO  GO:0006412;
GO  GO:0006413;
GO  GO:0055085;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTR
SQ  KGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNR
SQ  INKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEE
SQ  GGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFV
SQ  NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQ
SQ  LEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN
SQ  HLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKE
SQ  LKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPL
SQ  FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQ
SQ  DARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDAR
SQ  LITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE
//
ID  A9CB27;
PN  Zinc finger protein ZPR1;
GN  ZNF259;
OS  9555;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: A9CB27;
DR  Pfam: PF03367;
DE  Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0015030;
GO  GO:0005737;
GO  GO:0097504;
GO  GO:0030426;
GO  GO:0043025;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0030971;
GO  GO:0031369;
GO  GO:0008270;
GO  GO:1902742;
GO  GO:0061564;
GO  GO:0030576;
GO  GO:0071364;
GO  GO:0042023;
GO  GO:0001833;
GO  GO:0000226;
GO  GO:0006397;
GO  GO:2000672;
GO  GO:0010628;
GO  GO:0045927;
GO  GO:0042307;
GO  GO:0033120;
GO  GO:0071931;
GO  GO:1990261;
GO  GO:0031641;
GO  GO:0008380;
GO  GO:0021510;
GO  GO:0001834;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSC
SQ  EHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD
SQ  QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPA
SQ  EKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSD
SQ  MTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKERLQEFSQKMDQIIEGNMK
SQ  AHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLASQR
//
ID  A6QLT2;
PN  Myotubularin-related protein 2;
GN  MTMR2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DR  UNIPROT: A6QLT2;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3- phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5- phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005774;
GO  GO:0042802;
GO  GO:0052629;
GO  GO:0004438;
GO  GO:0004725;
GO  GO:0046855;
GO  GO:0032288;
GO  GO:0031642;
GO  GO:0048666;
GO  GO:0046856;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13614};
SQ  MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLP
SQ  GENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRN
SQ  LRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTY
SQ  PALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD
SQ  ARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGAL
SQ  RIADRVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVF
SQ  LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPRRTVSLWSYINSQLEDFTNPLYGSYS
SQ  NHVLYPVASMRHLELWVGYYVRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERAGSPAQCVTPVQ
SQ  TVV
//
ID  Q9VCW3;
PN  Nuclear pore complex protein Nup133;
GN  Nup133;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. {ECO:0000250|UniProtKB:Q8WUM0}.
DR  UNIPROT: Q9VCW3;
DR  UNIPROT: Q86PB8;
DR  UNIPROT: Q961A9;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Probable component of the nuclear pore complex (NPC) (Probable). Plays a role in NPC assembly and/or maintenance (PubMed:20547758). {ECO:0000269|PubMed:20547758, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q95TK6; IntAct: EBI-500275,EBI-179690; Score: 0.37
DE  Interaction: Q9VZU6; IntAct: EBI-500389,EBI-179690; Score: 0.37
DE  Interaction: Q9VKQ7; IntAct: EBI-165360,EBI-179690; Score: 0.37
DE  Interaction: O17144; IntAct: EBI-466327,EBI-179690; Score: 0.37
DE  Interaction: Q8SY59; IntAct: EBI-130585,EBI-179690; Score: 0.37
DE  Interaction: Q867V1; IntAct: EBI-500225,EBI-179690; Score: 0.37
DE  Interaction: A1Z6E0; IntAct: EBI-75338,EBI-179690; Score: 0.37
DE  Interaction: Q9W5Y0; IntAct: EBI-87449,EBI-179690; Score: 0.37
DE  Interaction: P55841; IntAct: EBI-188266,EBI-179690; Score: 0.37
DE  Interaction: Q8IMH4; IntAct: EBI-498380,EBI-179690; Score: 0.37
DE  Interaction: P51123; IntAct: EBI-499582,EBI-179690; Score: 0.37
DE  Interaction: O97143; IntAct: EBI-162366,EBI-179690; Score: 0.37
DE  Interaction: Q9VME5; IntAct: EBI-191523,EBI-179690; Score: 0.37
DE  Interaction: A1Z8Z7; IntAct: EBI-179690,EBI-138643; Score: 0.37
DE  Interaction: P05812; IntAct: EBI-179690,EBI-108518; Score: 0.37
DE  Interaction: Q24564; IntAct: EBI-179690,EBI-180142; Score: 0.37
DE  Interaction: Q9VJ00; IntAct: EBI-179690,EBI-165907; Score: 0.37
GO  GO:0016020;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0031081;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERNLQKQLYGISRESSPGARRYSMPAASADSTRKSIFGGSASCAQMSGSLKRTALTNSRLSLSVRSTQSIAGIRSDYNS
SQ  VESFGCPLPVVVNEALTFAGPGAGTVTAKVTQNGWAWVVQGRRLLIWQYKDTAKSGSPPRVGKLARRGGGLAQCRELTLP
SQ  YSDLGHKSDLISVFQTEGQQMASCIAVSATGEVRYWSSIAHDGNSVDLSILTGQEFVQLLSLPTQQGYLAVTTTCNLVFL
SQ  RVGLTNGRYTLHHKTIKPATSFLGGFGKKFASILIGMNTGADKDQTLVGMCCESNLESGETIVAVLSDRAIQRWSLSNNG
SQ  NTENLLYEDADMLRRIREEFITNFWKFRLPADSLEIDLHLLDFHVVKNKAYILAGAVNAAHAPQMCYALVTGTAQAERML
SQ  LESFTPLNMNKFFSAKTEEDCLSVRFVVGSSHIYLYTSKVVYPLHLTNSVPTAELEAEKIEFHQHDDRILSAVICSQLPL
SQ  FFSRTHGLVSITPGDFDGTEMMNMSSCNTPDLYAPNSCNASFAVADHSALTNSTNNLHLFELDPDEMYNELSDEVGQLKA
SQ  AFLYHMKRNSNMVKTIVDELLRNVTAADPSGAPMDAYKLDRIVITIAEDLAEDIPIADPRWEEALADQEMNRHAIGSSRS
SQ  MQIINQLRDKIIAFQHFITFLHSSLVWDKLNVIPCGSHSLKPTGCILADISEKIVAAMALRSIQTKLPKLIEEAIDATVA
SQ  LWHEEPQGSLTYQDIFYVKLSRFQNVFEALADIADDRIAAQNQTTISVAHFVNEINSIVLDVLGQVFKYRKQHASSFRLS
SQ  HEKLPSYENLPWTAMAGSAGVRDTLTRLIDISVRYGSHCVSETELKQQLYQQIFELIDLVLDGRKTYLKSVRDTEKFNVL
SQ  QQQFEAQRRELISVLIKDRQYEYAAKIAEKYLDFQSLVLICDETQDKERLEDYTRKYEEYDFSQFAINWHLRQNRHGEVF
SQ  ERFKGNQTALAQFMRDHPSLGWIQLIFNGDFERAAKVLYELAQCETEFVARKKSMLSLAKLAAFAAAESDLTAQVEKINA
SQ  DLTLVEYQSQLGHDVLESFGFDPAEQKVLKAEEIISLYIAEENETASETEFRKALELLSYVEQPYDMRHKIWCAAIKRDN
SQ  WTDYDPNNAVHYMQKLLFYKIIEISQLMGNDSENVLPPMEDFLESVELGDLPQQKPFQYLLKLTYEYVADMFKQPDDMEL
//
ID  Q7TPN9;
PN  Proline-rich protein 14;
GN  Prr14;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associates with chromatin at the onset of anaphase and relocalizes to the nuclear lamina in telophase. {ECO:0000250|UniProtKB:Q9BWN1}.
DR  UNIPROT: Q7TPN9;
DR  UNIPROT: Q922N8;
DR  Pfam: PF15386;
DE  Function: Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (By similarity). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (By similarity). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157) (By similarity). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1, ECO:0000269|PubMed:25906157}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPGNSSPFTQPSLCRQPLSRASWEARSPKRPRLQPLGTPSSLEKASRRVLAVVLEDVMTTNRVPLTHKEDTPSPLTHN
SQ  HHQDPVCTQSPALPSQQVKWSMQARPPDPLHLCREPLTRARQSSPALRMRSRAASGPEESPSKKTDQVPQPTLVVVLEDI
SQ  ASGRQPAEGFDEDQPNLIVPAQSTFRSLKGPGKHCHRRGLDLEARPTLTLSLHPRAEPVTKAGQPMPTPSDLEPPFQLST
SQ  LPADPPESPVPDPALETPVIPTSSSLLRPRLSPWGLAPLFRSVRSKLESFADIFFTPNKTPQPPPPSPPMKLELKIAISE
SQ  AEQSRATEKITSVSPRPPIRQWRTQCNSLAPVSKSSLGRSYSCPDLGPPDPGSWPPVPSQPSQSRPRRHTVGCGEMARTP
SQ  PPPRPCLRKEVFPLGGVGVSPSLTTSCSANAPASFFCEPAEPRLGSTKGKELRASKDKVFSDPETKTMGKVSRFRIRRTP
SQ  VRLQPNLTPMGLPRPIRLNKKEFTLEEIYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRAVEFRDSSLPRSR
SQ  RPSRGVRTAASRTLTPNLAPSQDVGSLLQERLRELDALLLEEETDKEHPCHL
//
ID  Q0GNC1;
PN  Inverted formin-2;
GN  Inf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q0GNC1;
DR  UNIPROT: Q14C56;
DR  UNIPROT: Q499F7;
DR  UNIPROT: Q6P9T3;
DR  Pfam: PF06367;
DR  Pfam: PF06371;
DR  Pfam: PF02181;
DR  Pfam: PF02205;
DR  PROSITE: PS51444;
DR  PROSITE: PS51232;
DR  PROSITE: PS51082;
DE  Function: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000269|PubMed:16818491}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-912574,EBI-6908712; Score: 0.35
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0017048;
GO  GO:0030036;
GO  GO:0032535;
GO  GO:0090140;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVKEGAQRKWAALKEKLGPQDSDPTEANLESAEPELCIRLLQMPSVVNYSGLRKRLESSDGGWMVQFLEQSGLDLLLEA
SQ  LARLSGRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHAL
SQ  TLDALDHYKMVCSQQYRFSVIMSELSDSDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRLRDLEDAD
SQ  LLIQLEAFEEAKAEDEEELQRISDGINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLLWEALENLVN
SQ  RAVLLASDAQACTLEEVVERLLSIKGRPRPSPLDKAHKSVQTNSVQNQGSSSQNTTTPTTKVEGQQPVVASPCQHVGSIQ
SQ  SSSVDIAPQPVALEQCITALPLPTPPLSSSTPVLPPTPPPLPGPGATSPLPPPPPPLPPPLPGSGTTSPPPPPPPPPPLP
SQ  PPLPGSGTISPPPPPPPPPLPGTGAVSPPPPPPLPSLPDSHKTQPPPPPPPPLPGMCPVPPPPPLPRAGQIPPPPPLPGF
SQ  SVPSMMGGVEEIIVAQVDHSLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVARERNSMWATLGSPCTAAVEPDFSSIEQL
SQ  FSFPTAKPKEPSAAPARKEPKEVTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIEN
SQ  LRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMMLCEGTAIVLDMVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNF
SQ  LNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASANLKKL
SQ  LEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKEN
SQ  KDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTEASGRVAPTDP
SQ  PKATEPATASNPTQGTNHPASEPLDTTAADEPQGWDLVDAVTPSPQPSKEEDGPPALERRSSWYVDAIDFLDPEDTPDAQ
SQ  PSEGVWPVTLGDGQALNPLEFSSNKPPGVKSSHQDATDPEALWGVHQTEADSTSEGPEDEAQRGQSTHLPRTGPGEDEDG
SQ  EDTAPESALDTSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEEFVPDSDDIKAKRLCVIQ
//
ID  A8WVD2;
PN  Nucleoporin SEH1;
GN  npp;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: A8WVD2;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Probable component of the nuclear pore complex (NPC) which is involved in the trafficking of macromolecules between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:O45933}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0034629;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSADKSPYQIEPYKTVGAHRDLIHCVSFDPHGRRMATCASDMTMAIWDRQPDGNWRRSAHWKCHGGAVWRVIWAHPEFGQ
SQ  IVASCSYDRTIVIWEEQIVRTEKDLKCKESQWIRRTIISDNRSDVTDICFSPRHLGLSLASCNVLGAVRIYEAPDVVDAS
SQ  RWNLIHELQAFHTRCGCVTWSLSRMHRPLIAVGSDEKKAGGKERVVIYENIDGLRKWQRIHSLVFDMPCPITDLKFSPIS
SQ  MVDSHQLAIASGDVHVFNIKVPRTAILEEDGVDNPIHLADYSFQRVALLGDQRKAWRIRYNLIGSVITSTSLDGTLRSWK
SQ  SLFVNQWVKLSEMNVDDYVPTADEVHKIVEAKTTERLPSQLDKVYF
//
ID  O13965;
PN  Meiotically up-regulated gene 70 protein;
GN  mug70;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: O13965;
DR  UNIPROT: Q9USF6;
DR  Pfam: PF00571;
DR  Pfam: PF00564;
DR  PROSITE: PS51371;
DR  PROSITE: PS51745;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTVGTLSVVSSTASDTASHVSDTRKRQYQRDEALRKKIISELGKKSGNFESPVRKIRRNGEPGTVDSAALDPALTVHMQS
SQ  LVTETAQLMAAKRQNCVLVVDDDEQLAGIVTATDIATRCVGAGLNARQTLIADIMSTSPLCITSDTRFDDALLLMIEHKF
SQ  RHLPVVSDGGPDGSAGDEGDVIGIINMRACLREPLNRIARQQEAAQKLVEALEGAQEEIENKSVSGNTNSSSVSGNHAAE
SQ  FLEYVESLKKKASGLEIMSLIDSSEEPFLVGTRTTVAEATESMARSGVSAVLVMDNGAVSGVFTAHDVVLRVLAAGLDPY
SQ  RSSVIRVMTPHPDCALASLRVSTALERMIEGKFSNLPVVDESDAIIGMLSLFHLATAIEQTPEEEEEVFDQAENDAGIEP
SQ  SNGFEDQQQQLLGNSNEVVENYDVNPPLPLNPLPSNTQQSESTYEYSARQLPKPPVQAWQNENLSSNNKPQEYVGVENDY
SQ  NFSNNPPTAMSEQSFHPSVSQKPMDTPENGSNSFAASPYLQPYNSASQLAPSYVGSLPQYHGNPSFVEQALQDLVQPTDS
SQ  ASQIFPLNPQSPSQFTIKYRSIAGRVHRLRLDGINSVSDLRTAVEEREKEQLVTLTYIDDEGDVVELVSDSDLREAILLA
SQ  RRRGLPRLEVRGVAAFTNHLESSHPPISTVDSSIGSASVVEKGVANSIVDIHQPTAKADKGNSKKPIYIGIVSSSIVILA
SQ  VSMWYLRRKR
//
ID  Q99LY2;
PN  Lysophospholipase D GDPD3;
GN  Gdpd3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25528375}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalized with CANX (PubMed:25528375). {ECO:0000269|PubMed:25528375}.
DR  UNIPROT: Q99LY2;
DR  UNIPROT: Q9D1C0;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375). Shows a preference for 1-O-alkyl-sn-glycero-3- phosphocholine (lyso-PAF) and lysophosphatidylcholine (lyso-PC), and to a lesser extent for lysophosphatidylethanolamine (lyso-PE) (PubMed:25528375). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0034638;
GO  GO:0006644;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIPLLYFVLPTLGSYVMLSIFFLRRPHLLHTPRAPVFPIRLAAHRGGSGERLENTMEAVENSMAQRADLLEFDCQLTRDG
SQ  VVVVSHDKNLSRQSGLNKDVNTLDFEELPLYKEELEIYFSPGHFAHGSDRHMISLEDVFQKFPRTPMCLEVKERNEELIH
SQ  KVANLTRRFDRNEITIWAAEKSSVMKRCRAANPEMPMAFTIWRSFWILLLYYLGLLPFVSIPEKFFFCFLPTIINRTYFP
SQ  FRCGWMNQLSATITKWIIMRKSLIRHLQDRGVQVLFWCLNEESDFEVAFSLGANGVMTDYPTALRHYLDKQEEETQPPQP
SQ  EALSCLSLKK
//
ID  V6CJ04;
PN  Protein bicaudal D homolog;
GN  bicd;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:20005871}. Perikaryon {ECO:0000269|PubMed:21205795}. Cell projection, dendrite {ECO:0000269|PubMed:21205795}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}.
DR  UNIPROT: V6CJ04;
DR  UNIPROT: V6CK55;
DR  Pfam: PF09730;
DE  Function: Part of a complex with dlc-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871) (Probable). Required for the formation of dendritic branches of PVD sensory neurons (PubMed:21205795). {ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:21205795, ECO:0000305|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17902; IntAct: EBI-2006416,EBI-328330; Score: 0.51
DE  Interaction: Q23064; IntAct: EBI-2006416,EBI-2902228; Score: 0.37
DE  Interaction: Q23064-3; IntAct: EBI-2006416,EBI-2902257; Score: 0.51
DE  Interaction: O01590; IntAct: EBI-323641,EBI-2006416; Score: 0.49
DE  Interaction: Q22771; IntAct: EBI-2414743,EBI-2006416; Score: 0.49
DE  Interaction: Q9N4I1; IntAct: EBI-6460061,EBI-2006416; Score: 0.37
DE  Interaction: Q9XVN3; IntAct: EBI-2006416,EBI-6534803; Score: 0.37
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0008093;
GO  GO:0070840;
GO  GO:0048814;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESELEKLRQDIAILTEKYEQAKEDIHKAANAGLELLRQKEDLEKRLAEMQAELDLARTEIDKTNQTLAEYRSQHQRST
SQ  RSELENEESLLEESSAKEEEYLQRIAKLEADLKKKEQELAEKKEELESIEKKHSKEIDSGAALEDERRKLRAELKETKER
SQ  EQRLISEYSELEEENIGLQKTVANLRGSQVEYESLRIDNNRLEETIEIMKMAAEEDEILRVIADKQLEEALLTAQQERDQ
SQ  RLAMKRELEQTRNAEHISSLNDMLFGLERLGEDGELPPPQPGASDLFSELQGSSDVKVRELEAAKEGLQEELKSREKIFI
SQ  EFVTGLADTLNIHRPTNELDYMHARQQKDVVLEKIQNIARDTDRHDKEGEEKRSGILKADLRTLVLVAGEKSAQLAAAQD
SQ  AMIQVSDQLYQFYHQMTQNQGVQTEKSVQEIVKKLRLLARANAEDVPRVSLADEGVESGTETDVNASRSIPLNSDRLVIA
SQ  PSFAKEIEKKLASVKIGDVLSETDLRQRILTEGNAISETTESLKKMIQVVKRTSEQAFNQAVMASGAENEIEMQNMKLRS
SQ  LLSTKRDQISTLRTVLKSNKLTAESALTSMREKYESEKKMMMEINDKMRRELKQLKEDAATFASHRAMFTARGEELKSKV
SQ  EELSNELRANEEEKKTLNQLLRLAIQQKLTLTQRLEEVEVDRDRQVFKRSSTRAPTRETYQPPRAVRYPGSTTTAQQPAP
SQ  SSSGGSRGGPRRGDNQQ
//
ID  A0A125S9M5;
PN  Lamin-2;
GN  LMN2;
OS  232323;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side {ECO:0000269|PubMed:26840051}. Note=Localization is restricted to the nuclear periphery which is consistent with the presence of a C-terminal isoprenylation motif (PubMed:26840051). {ECO:0000269|PubMed:26840051}.
DR  UNIPROT: A0A125S9M5;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Intermediate filament (IF) protein, component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope (PubMed:26840051). {ECO:0000305|PubMed:26840051}.
DE  Reference Proteome: No;
GO  GO:0005882;
GO  GO:0005637;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:26840051};
SQ  MSAQVSKKRGGSNPPKTGQHAASSTTSRTESSATSQTIYERQEVETRTQRTPGGLLLAASSAEVSSGTAGLAGSPLSRHQ
SQ  EKEEFKLLNNRFANYIDTIRAQQEEISVLRRKVETVSSKEVVENQKIKERYNLEIANLRRALDEVSRDLAAAIIERDSLR
SQ  PERDARLLLDNEKKTLQKRSKDAEAALKDAKNQLAALRDQAKDHDNEIHGLTTENSSLKLQIENLKKDLSQETNLRVDAE
SQ  NRLQSEREKNALLEGIHNEEIVSLRNQRRTEITEVETRMGEEYQSKIVEQLNDLRADLEAVAHEMRLDLERSYQNQLEDS
SQ  QDLANRYRDEARALLADLSAAQDRIKETQTRSEKQLQELRLQLQRLQAELNGKDDEVQRLQKLLADRQAELQNTHHELSR
SQ  QIASYQELLDEKIHLDAELATYNALLRTEEERLNMKSPPFPSTPDSQRRGTKRRIADSYTRTRFRNEASATGDIHISEID
SQ  AEGQFVRLENKSGQDVVIGGWKLLMVSDNGEDNKTDYKIHSNQVIKAHSSTTIWSANTNVVHEPPADIVMEGRWLVGDHT
SQ  SVTLSTSDGVEVARREMTQSSTRDDSYLGPSGLPKRSRLVVADSSDHQKNCVIM
//
ID  Q8BXR9;
PN  Oxysterol-binding protein-related protein 6;
GN  Osbpl6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:14593528}. Cytoplasm, cytosol {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14593528}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000269|PubMed:30028970}.
DR  UNIPROT: Q8BXR9;
DR  UNIPROT: Q8BYW2;
DR  Pfam: PF01237;
DR  Pfam: PF15409;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Regulates cellular transport and efflux of cholesterol (By similarity). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (PubMed:30028970). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (PubMed:30028970). Weakly binds 25-hydroxycholesterol (By similarity). {ECO:0000250|UniProtKB:Q9BZF3, ECO:0000269|PubMed:30028970}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EPK7; IntAct: EBI-6908541,EBI-17170664; Score: 0.35
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0015485;
GO  GO:0008289;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0032374;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSSDEKGISPAHKTSTPTHRSASSSTSSQRESRQSIHVLERTASSSTEPSVSRQLLEPEPIPLSKEADSWEIIEGLKIGQ
SQ  TNVQKPDRHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYH
SQ  LKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPATSTAESSPAANVSVVDGKMQPNSFPWQSPLPCSNSLPAT
SQ  CTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSV
SQ  SKDTKIQLQEGPPAKGQFNTTRRRQRLAAAVATTVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQ
SQ  EEFCLIAQKVHSLLKSAFNSIAIEKEKLKQVVSEQDHNKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESTICDHVV
SQ  SVNIIPSPDEPGEQIHVSLPLSQQVANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVAD
SQ  NISRQILNGELTGGAFRNGRRTCLPAPCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKA
SQ  SETDDPYERMVLVAAFAVSGYCSTYFRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIR
SQ  WKNKFWGKSMEILPVGTLNVTLPKYGDYYVWNKVTTCIHNILSGRRWIEHYGEVTLRNTKSSVCICKLTFVKVNYWNSNV
SQ  NEVQGVVIDQEGKVVHRLFGKWHEGLYCGVAPSAKCIWRPGSLPTNYELYYGFTRFAVELNELDPVLKDLLPPTDARFRP
SQ  DQRFLEEGNLEAAAAEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW
//
ID  Q0IIE8;
PN  DnaJ homolog subfamily B member 14;
GN  DNAJB14;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single- pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
DR  UNIPROT: Q0IIE8;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q8TBM8}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0034622;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGGGDQSKPNCTKD
SQ  SSSGSGESGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLS
SQ  NPEKRKQYDLTGNEEQACNQQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSNQHQHRHSGHEREE
SQ  ERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVIYYVNKDFKNEYKGMLLQKVEKSV
SQ  EEDYVTNIRNNCWKERQQKTDMQYAAKVYHDERLRRKAEALSMDNCKELERLTSIYKGG
//
ID  Q2M2T9;
PN  Telomere repeats-binding bouquet formation protein 2;
GN  TERB2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q9D494}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D494}. Note=Localizes to telomeres throughout meiotic prophase I and disapears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D494}.
DR  UNIPROT: Q2M2T9;
DR  Pfam: PF15101;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000250|UniProtKB:Q9D494}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0000784;
GO  GO:0005637;
GO  GO:0070197;
GO  GO:0045141;
GO  GO:0007129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFQGQRGWFCGSVSHDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAEIKNS
SQ  VALGHFILPPASLQKEIRRKIGSFIWEQDQHFLIEKHDEVTSNELKVFRESSVLATDHKKDLSKSTEKHFIRTPVVEKQM
SQ  YFPLQHYPVNNMVTGYISIDAMKKFLGELHDFIPGSSGYLAYHVQNEINMSAIKNKLKNKY
//
ID  Q753I3;
PN  CTP-dependent diacylglycerol kinase 1;
GN  DGK1;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q753I3;
DE  Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. Involved in pre-tRNA splicing (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000139;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0004143;
GO  GO:0006654;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANEEELQTAESAFVTGARRYSNDYSESESSSKHSGCSTPVEGTPAEAATTIGARASGGSTTWQRLRQLLMERGSDVHLP
SQ  VTEIHLKSQEWFGDFITKHEVPRKVFHSSIGFFTLALYVRDVDYRNVRLPLIVGFVHVLLLDVIRLHWPAFNTLYCQVTG
SQ  LLMRKKEVHTYNGVLWYLLGLIFAFSFFSKDVALVSLFLLSWCDTAASTVGRLYGHLTPRISRNKSLAGSLAAFVVGVIS
SQ  CAVFYGYFVPAYSHVNHPGEIMWNPETSRLSLVQLSLLGGFVASLSEGIDLFNWDDNFTIPVLSAIFMHTIIAFSQR
//
ID  P10536;
PN  Ras-related protein Rab-1B;
GN  Rab1b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}. Membrane {ECO:0000269|PubMed:1918138}; Lipid-anchor {ECO:0000269|PubMed:1918138}; Cytoplasmic side {ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23188820}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:23188820}.
DR  UNIPROT: P10536;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (PubMed:1918138). Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-915426,EBI-916259; Score: 0.35
GO  GO:0012505;
GO  GO:0005793;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0045202;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000045;
GO  GO:0006888;
GO  GO:0006886;
GO  GO:1903020;
GO  GO:0032482;
GO  GO:2000785;
GO  GO:0019068;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1648736};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC
//
ID  P16258;
PN  Oxysterol-binding protein 1;
GN  OSBP;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic. {ECO:0000250|UniProtKB:P22059}.
DR  UNIPROT: P16258;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (By similarity). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:18165705). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (By similarity). Regulates cholesterol efflux by decreasing ABCA1 stability (By similarity). {ECO:0000250|UniProtKB:P22059, ECO:0000269|PubMed:18165705}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0015485;
GO  GO:0070273;
GO  GO:0120015;
GO  GO:0032367;
GO  GO:0015918;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P22059};
SQ  MAATELRGVVGPGPAAIAAPGGGGAGPPVVGGGGGGRGDAGPGSGAASGTVAAAAAGGQGPGAGGVAAAAGPAPTPPAGG
SQ  SGSSGTGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQT
SQ  YHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRS
SQ  LSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLVLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHL
SQ  ERAFRGATVLPAHTSGSAGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQL
SQ  EETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAA
SQ  FTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMP
SQ  LGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKV
SQ  HFALLGTWDEKMDCFKVQPVSGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWEGGTAPTDSRLR
SQ  PDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQ
SQ  DWNSCPDIF
//
ID  Q9BYT3;
PN  Serine/threonine-protein kinase 33;
GN  STK33;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q9BYT3;
DR  UNIPROT: Q658S6;
DR  UNIPROT: Q8NEF5;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 607670;
DR  DisGeNET: 65975;
DE  Function: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines. {ECO:0000250, ECO:0000269|PubMed:21742770}.
DE  Reference Proteome: Yes;
DE  Interaction: P14618-1; IntAct: EBI-4304679,EBI-2687040; Score: 0.44
DE  Interaction: Q5S007; IntAct: EBI-2687040,EBI-5323863; Score: 0.44
DE  Interaction: P29692; IntAct: EBI-2687040,EBI-358607; Score: 0.40
DE  Interaction: Q8IVS8; IntAct: EBI-2687040,EBI-748515; Score: 0.37
DE  Interaction: O43852; IntAct: EBI-1171069,EBI-2687040; Score: 0.40
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004674;
GO  GO:0044773;
GO  GO:0046777;
GO  GO:0042770;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADSGLDKKSTKCPDCSSASQKDVLCVCSSKTRVPPVLVVEMSQTSSIGSAESLISLERKKEKNINRDITSRKDLPSRTS
SQ  NVERKASQQQWGRGNFTEGKVPHIRIENGAAIEEIYTFGRILGKGSFGIVIEATDKETETKWAIKKVNKEKAGSSAVKLL
SQ  EREVNILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRDLK
SQ  LENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQATCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGE
SQ  PPFLASSEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNKLSSVRPTNVLEMMKE
SQ  WKNNPESVEENTTEEKNKPSTEEKLKSYQPWGNVPDANYTSDEEEEKQSTAYEKQFPATSKDNFDMCSSSFTSSKLLPAE
SQ  IKGEMEKTPVTPSQGTATKYPAKSGALSRTKKKL
//
ID  E1BPK6;
PN  Unconventional myosin-VI;
GN  MYO6;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q29122}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocytic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54}.
DR  UNIPROT: E1BPK6;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro- survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}.
DE  Reference Proteome: Yes;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0005902;
GO  GO:0016459;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0006897;
GO  GO:0015031;
GO  GO:0007605;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UM54};
SQ  MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTEN
SQ  TKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
SQ  EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRM
SQ  CTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQSLEYCAELLGLDQDDLRVSLTTRVMLTTAG
SQ  GTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKL
SQ  QQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLMGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIP
SQ  RKSKLAVHRNIRDDEGFIVRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSF
SQ  ISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHDFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKK
SQ  YMPDKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAQLVKRVNHWLICSRWKKVQWCS
SQ  LSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKAEMNKQVKDLEISIDA
SQ  LMAKIKSTMMTREQIQKEYDALVKSSEVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEM
SQ  EAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIARSEAELIIDEAQADPAALRSLDF
SQ  HPVTSKINGTRRTMTPEQMAKEMSEILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLK
SQ  VYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKK
SQ  GWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQ
SQ  ARPTYATAMLQNLLK
//
ID  Q9V4W1;
PN  Nucleoporin Gle1;
GN  Gle1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9V4W1;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P18824; IntAct: EBI-216128,EBI-3430902; Score: 0.35
DE  Interaction: P49415; IntAct: EBI-198254,EBI-3430902; Score: 0.35
DE  Interaction: Q9VT04; IntAct: EBI-125572,EBI-3430902; Score: 0.35
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDMMRAMDCLNMAATLRNAALASATCTGRTLGEDREPIWVEGSRKTPEPPLPEESPAPEPNNEIPLLPKIDFEPNISCF
SQ  PDLQAINASIVRRELEEEGKRCVRQQLKAIRDKQDAMRLSRETQQRKEERQRDQLQQKALRERNESLLIQKADQMTAAQL
SQ  EAQQREQLALRQQIDQKLHKLALEGVSRCQRRFNQKYEGIAKILLSLNPETVKVCAAQNTQLKELGQKFEQLVSSVKMGN
SQ  CEMQSQFLCSIIKAEEFCKSLDALELDIIKQLAEFSEQIQQQLKMEAAKKLEDERQRQQQQEEERQKLEEQQKLEEQEKL
SQ  RKEKEESAAKEKQQEAETAKADAANVPAPLEPKSQDVPPAATATSTSVHPDRLKFYNDILALYQSKVDAVKPLQTEESLK
SQ  QYRTGCQRAINLPLNAISAVSPQHLAQNFDKLYSFFAGQPTKVMNGTITINDHPLARDYCMLLMAKKFVSQTETAICSNP
SQ  QAAFPFASVIITFWKLLPDFGKVFLAYMYKESPFLVPYVIPQQQGQTPEQYLKTIGYRLTDKNELEKPDIYLKRQTGLAR
SQ  LYAAVIISQGRKAAGPDECFELNEGWLWLAHMVHVKPLPDISATLIMEILQTLGFELWRTYGKQFVKLLVYIQNIYMPQL
SQ  AAYDEGGPKTRLEMLLAKFLRERQIAQAVGVLPPGFW
//
ID  Q55FW7;
PN  Nucleoporin GLE1;
GN  gle1;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q55FW7;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031012;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKTSSNNISNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNRILSPFKRNNSKENGNGSVTITLEPLVSPFKLIK
SQ  SNFKDDVHTNNINNNNNKIKRFLDEDNEFEITIPIRRSGNSINFNIGIVPSSNKKQQQQQQQQQKQKQKKKKTLSPLKKA
SQ  PGIYSLKDLTIDSDSDSDSYSDNDDNEEYNIKLKSPIKNKIVNNNNNQQQQQKQKEKEEKEEKEKVEKDKKEKDKKKLIL
SQ  NSFQSELIINRVEREREIKINRIVEEKNKEIDDKWVEIKEYNQNQMIKERKEFHSQQIRLNNLIKKQHKKDIKEFSIKLK
SQ  QAKQKHQSELSESLSLLNQLNKLEQQEIDRHNEELLKYELAIKEEKRKQQQLIERYEQKKREEKQRQLQQEQKEKQEKLE
SQ  KEEKEKEQQEQQKQLLIKLAKEKEEKEKFEKEQQQQKEKELQKEKELLQQKEKEKEKEKLQQQQQQQQQQQQQQQQQLQQ
SQ  QQQQQNQQNNNLGYIKKDGIIFSLNENSKNFNDFKERSKEFDMIIKFINEKKSMLSREMVEFERQNSKLINIAINQISAS
SQ  QEQVNEKTNKLIKSIQDSQQSDYLKKSTILSIVKKSLSQVESQITFHNASSFPLALVLVRVGEKYPELIDCLLASLNEKC
SQ  CYTVPYYVSPKENESQSSISKRMGYAFSNDIVGDNDKPIETEDEFHKRICGYLSLYCALILKSEQPHKSSSSSSSSSSST
SQ  MMFGFGTQIGNNNNNKLINKNLNIESSLRWLKDLVSLRPRRITSYLFVTFFTHLGNLLSKNQKSSLEFKIIVGKIVEENF
SQ  FNQMNKPGTEGSFSRLKNLIEEYYKTGTFQQHEGVDF
//
ID  Q66672;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  82831;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q66672;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRERPRKTREPASPGSVLSKRSKLSRKSLALRSLNKFHPYKAPSSVRSLKKAHTLVSNGDFFNGISLNCEFGKDFLREM
SQ  DTPICTSKVICLPLDVHEIAPGRCLVLSPLGHACNMGFYCEKCTQSGQNSYSQFQGRGGNAKMAAQNSKDDLHSVTLTFY
SQ  NQVSKVVQNKNFYLSLLSHSLTTIKKSFVQPSLLYSYTVLRALCDDVFPIFKDTENGLCMFALFKTDDLHVSETCLRHLV
SQ  DNLIHYRVTLDCVKHTYMLKFSPIRAEANGMTIQEVEICEAITGLDFTDEIKQEIISGQELVSEL
//
ID  Q6UDK0;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q6UDK0;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDVALKRNSSFFRAKARLTLLKRRDGGVISRSLEHRRSSRRRSSVSAPTRRVSGTLAKLGADDRRQFFDAFFRMTAVSP
SQ  EETVSLLRSMTVPVIQQENISLPYDINAKFAPGDCISLSEMGYTLEMGGCCSLCSYGWSTTTPPELPALELAFMHHLSSV
SQ  VEFKELVTSLRVCAGNSIVGNGAYENEGLLRMIKHLLEQSTLFYAYYTVKGGVSHDFRVLISEDGGGDGGSPAYAMYFVF
SQ  KPGSPLHLGAKLIRQLIFNCPGYKWHADVHEGAFLLVVTRDRCSAIPEPRRVKLDPEDVYRRYCDVLVTEEKVHDYSRLY
SQ  STFSTYCPPASRREQTAAPATAKQV
//
ID  Q66IJ0;
PN  Nucleoporin NUP35;
GN  nup35;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}.
DR  UNIPROT: Q66IJ0;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAFSMEPMGAEPMALGSPTSPKPSAGAQFLPGFLLGDIPTPVTPQQRPSIGVMEMRSPLLSGGSPPQPVVPTHKDKSGA
SQ  PPVRSIYDDIASPGLGSTPLNPRKTASFSVLHTPLSGVIPSSPECKNISGSRKRPASSVFSPATIGHSRKTTLSPAQMDP
SQ  FYTQGDALTSDDQLDDTWVTVFGFPQASASYILLQFAQYGNIIKHVMSNNGNWMHIQYQSKLQARKALSKDGRIFGESIM
SQ  IGVKPCIDKSVMEATEKVSTPTVSSVFTPPVKNIGTPTQSVGTPRAASMRPLAATYKTPASADYQVVADKQAPRKDESIV
SQ  SKAMEYMFGW
//
ID  Q8VHK5;
PN  Membrane protein MLC1;
GN  Mlc1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q8VHK5;
DE  Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0097450;
GO  GO:0016323;
GO  GO:0005901;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0072584;
GO  GO:0071397;
GO  GO:0034220;
GO  GO:0032388;
GO  GO:0015031;
GO  GO:0047484;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTREGQFREELGYDRMPTLERGRQDAGRQDPGSYTPDSKPKDLQLSKRLPPCFSYKTWVFSVLMGSCLLVTSGFSLYLGN
SQ  VFPSEMDYLRCAAGSCIPSAIVSFAVGRRNVSAIPNFQILFVSTFAVTTTCLIWFGCKLILNPSAININFNLILLLLLEL
SQ  LMAATVIISARSSEEPCKKKKGSISDGSNILDEVTFPARVLKSYSVVEVIAGVSAVLGGVIALNVEEAVSGPHLSVTFFW
SQ  ILVACFPSAIASHVTAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSVMRVVEIFKDYPPAIKSYDVLLLLLLLLLLLQ
SQ  GGLNTGTAIQCVSFKVSARLQAASWDPQSCPQERPAGEVVRGPLKEFDKEKAWRAVVVQMAQ
//
ID  O74476;
PN  Importin subunit beta-3;
GN  sal3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74476;
DR  UNIPROT: Q9US74;
DR  Pfam: PF18808;
DR  Pfam: PF18816;
DR  Pfam: PF18829;
DE  Function: Involved in the nuclear import of cdc25 and mcs1. {ECO:0000269|PubMed:12399381}. Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1 (PubMed:12399381). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P32337, ECO:0000269|PubMed:12399381}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006606;
GO  GO:0010389;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLP
SQ  GDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVF
SQ  RTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLAD
SQ  CLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDV
SQ  AGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAE
SQ  GAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVN
SQ  FSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGK
SQ  TMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKP
SQ  DFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHD
SQ  GVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVA
SQ  AVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGN
SQ  DTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLE
SQ  LPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTII
SQ  TILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF
//
ID  P09283;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P09283;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHLKPTRFFHANQPPMPHSYEMEDLCFDDMQYRWSPSNTPYRSMSRRYKSVSRSGPSMRVRSRTPCRRQTIRGKLMSKER
SQ  SVYRHYFNYIARSPPEELATVRGLIVPIIKTTPVTLPFNLGQTVADNCLSLSGMGYHLGLGGYCPTCTASGEPRLCRTDR
SQ  AALILAYVQQLNNIYEYRVFLASILALSDRANMQAASAEPLLSSVLAQPELFFMYHIMREGGMRDIRVLFYRDGDAGGFM
SQ  MYVIFPGKSVHLHYRLIDHIQAACRGYKIVAHVWQTTFLLSVCRNPEQQTETVVPSIGTSDVYCKMCDLNFDGELLLEYK
SQ  RLYALFDDFVPPR
//
ID  A0A0G2JXT6;
PN  Myotubularin-related protein 6;
GN  Mtmr6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:23188820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23188820}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y217}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q8VE11, ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.
DR  UNIPROT: A0A0G2JXT6;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By similarity). Negatively regulates ER-Golgi protein transport (PubMed:23188820). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3- phosphate. Negatively regulates proliferation of reactivated CD4(+) T- cells. In complex with MTMR9, negatively regulates DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (By similarity). {ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0015269;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0004725;
GO  GO:0006897;
GO  GO:0046856;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHF
SQ  IVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYP
SQ  RELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTR
SQ  PKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQ
SQ  KLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMK
SQ  GFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQ
SQ  KEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQ
SQ  NKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSE
SQ  PAVVSLEYGVARMTC
//
ID  Q9V3H8;
PN  NTF2-related export protein;
GN  Nxt1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:31384064}. Nucleus envelope {ECO:0000269|PubMed:31384064}. Note=Associates with the nuclear pore complex. {ECO:0000269|PubMed:31384064}.
DR  UNIPROT: Q9V3H8;
DR  PDB: 6IHJ;
DR  PDB: 6MRK;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Stimulator of protein export for NES-containing proteins (By similarity). Plays a role in the nuclear export of mRNA (PubMed:14729961). Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA (By similarity). In the ovaries, forms a complex with nxf2, Panx and piwi which acts as effectors of cotranscriptional transposon silencing (PubMed:31219034, PubMed:31368590, PubMed:31570835, PubMed:31384064). {ECO:0000250|UniProtKB:Q9UKK6, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9U1H9; IntAct: EBI-144932,EBI-160435; Score: 0.27
DE  Interaction: C4IXW3; IntAct: EBI-15132858,EBI-160435; Score: 0.49
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0090568;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0050829;
GO  GO:0045824;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSDLKAKVESCARTADTFTRLYYASVDNRRQQIGRLYLDNATLSWNGNGAIGRQMIESYFQELPSSNHQLNTLDAQPIV
SQ  DQAVSNQLAYLIMASGSVKFADQQLRKFQQTFIVTAENDKWKVVSDCYRMQEV
//
ID  F4KBW6;
PN  Nuclear pore complex protein NUP205;
GN  NUP205;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4KBW6;
DR  UNIPROT: Q9LU53;
DR  Pfam: PF11894;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVSPKDLVAIVHSSLLGTSRPTPTQRIELTHAIRNSFPSLQNLLSFPPPKPSDRAQVQSKEIRLPDSLPISLDDQDIAIS
SQ  LKLSDELHLNEIDSVRLLVSSNQEWGLMGRDPLEIQRLATGLWYTGRRDLTSTLYTLLRAVVLDEGLEPDLIADIQGLLE
SQ  ELIEAGLRQRLITLIKELNREDPTGLGGPLCERYLIDSRGALVERRAVVQRERLILGHCLVLSILVDRPGSKDVKDIYYI
SQ  LKDNAAQLTEGNDTISSQITFSLLFSLIITFVSDAISRLSDKSSMISQDASFRTDFQDIVMASGSDPTADGFIGGIRLAW
SQ  AVHLMLIHDGISGMDTISTASTTDMGHICSCLESIFSKNVFQFLLDNVLRTAAYQNDEEDIIYIYNAYLHKLASCFLSHP
SQ  IARDKVKESKDMAMSVLNSYRTSDPLDGSMQTEESDRPLPFISLMEFKEPELLSGNDVLWTFVNFAGEDHTNFKTLVAFL
SQ  EMLCTLASTQEGASKVYELLRGTSFRSIGWPTLFDCIRIYDEKFKQSLQTAGAMMPEFLEGDAKALVAYLNVLQKVVENG
SQ  NPTERKNWFPDIEPFFKLLGYENIPPYLKGALRKTIAAFVNVFPEMRDSIWAFLEQYDLPVVVGSQVGKSDQSSQVYDMQ
SQ  FELNEVEARREQYPSTISFLNLINALIAGEKDVNDRGRRAYSDPCEKWQLVVACLQHFHMILSMYDIQEEDLDGFTEHPH
SQ  FLVSLETSSLQTQLPIIELLKDFMSGKALYRNLMGILQVGVNSIISERLSKTYGKILEKAVQLSLEILLLVFEKDLLVSD
SQ  VWRPLYQPLDIILSQDHNQIIALLEYVRYDSLPQIQRSSIKIMNILRCSRLVGLVPMLIKIDAANSLIEDYAACLEGRLE
SQ  EGEVVENSCDDLGVLIMQLLVDNINRPAPSITHLLLKFDLDAPVEGTVLQPKFHYSCLKVILEMLEKLPNPDINFLLFEF
SQ  GFQLLCELNLDPLTSGPTMDLLSSKKYQFFLQHLDTIGVATLPKRSGSQALRISSLHQRAWLLKLLAIALHTGSGSSSAH
SQ  LEACQSILSHLFGREVTEAANEPFSSSTYPQDGLDYAGTSSISKSKALALLEILQFRSPDASMQLPQIVSSLKYDSLVED
SQ  ILGNRDTSVSGSIYYYSERGDRLIDLSSFSNKLWQKLHSGFPLVDSFPNVAELSEVRETIQQLLKWGWKYNRNLEEQAAQ
SQ  LHMLAGWSQIVEVSACRRISSLDNRSEILYRILDASLSASASPDCSLKMAFVLTQVALTCIAKLRDDRFSFQGALSSDTV
SQ  TCLDVMMVKHLSTGACHSVLFKLVMAILRHESSESLRRRQYALLLSYFQYCQHMIALDVPTSVVQFLLLNEQDGEDLDIQ
SQ  KIDKEQADLARANFFIIKKEAQGILDLVIKDASQGSEFGKTISLYVLEALVCIDHERYFLSQLQSRGFIRSCLGSISNIS
SQ  YQDGTHLLESQQRACTLEAELALLLRISHKYGKSGGQVLFSMGALEHIASCRAISFKGNMRRVDMKLQSDVGYNVQKQRT
SQ  IITAVLRLVFALTSLVETSEFFEGRNKIVRDVVEFIKGHQSLFDQLLREDFTQADDLLMEQIILAVGILSKVWPFEENDG
SQ  YGFVQGLFDMMSKLFIASPIKSILSQGSELKLSQLRFSLTSYLYFLVTKNSLRLQVSDDSLDSSTKLRQPTLLLLASLLS
SQ  HVTDSLERAAEKKSLLLHKIRDINELSRQDVDAIIKICDSQEYVTPSDNIHKRRYIAMVEMCQIVGNRDQLITLLLQLAE
SQ  HVLNIILIHLQDRSVSSNERGSYGSKSHIQQEVTDLCGKLSPTIDRLALLNEGKVGHNLKVFQRLATTVKEMAIQKCV
//
ID  Q9P6S6;
PN  PGA2-homolog C27.01c;
GN  SPBC27;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9P6S6;
DR  UNIPROT: P78948;
DR  Pfam: PF07543;
DE  Function: Involved processing and trafficking glycosylated proteins. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10169; IntAct: EBI-7989032,EBI-21244109; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006886;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFDVAGYLQSYSLKDWIRIIVYVGGYMLIRPYLMKLGAKIQEREHRKSLLEGEVDGTLDPEMTHGTKPKEHGEFDTDDE
SQ  EEEENPDAEFRWGYSARRRIRKQREEYFKNQDKSPLDAYADDDEDIEEHLED
//
ID  Q08920;
PN  Nuclear cap-binding protein subunit 2;
GN  CBC2;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Note=Predominantly nuclear, is able to exit the nucleus in an RNA- dependent manner.
DR  UNIPROT: Q08920;
DR  UNIPROT: D6W3J0;
DR  PDB: 6N7P;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Component of the CBC complex, which binds co- transcriptionally to the cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive- strand RNA virus BMV. {ECO:0000269|PubMed:10490594, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:12756324, ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:15753296, ECO:0000269|PubMed:16166263, ECO:0000269|PubMed:8682299, ECO:0000269|PubMed:8811086, ECO:0000269|PubMed:8858145, ECO:0000269|PubMed:9215889}.
DE  Reference Proteome: Yes;
DE  Interaction: P34160; IntAct: EBI-33556,EBI-745; Score: 0.82
DE  Interaction: Q02821; IntAct: EBI-33556,EBI-1797; Score: 0.77
DE  Interaction: Q06142; IntAct: EBI-33556,EBI-9145; Score: 0.67
DE  Interaction: P53316; IntAct: EBI-23586,EBI-33556; Score: 0.37
DE  Interaction: P39987; IntAct: EBI-33556,EBI-22339; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-33556,EBI-8637; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-33556,EBI-8603; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-33556,EBI-8571; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-33556,EBI-8627; Score: 0.53
DE  Interaction: P39078; IntAct: EBI-33556,EBI-19054; Score: 0.35
DE  Interaction: P12612; IntAct: EBI-33556,EBI-19045; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-33556,EBI-19049; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-33556,EBI-8591; Score: 0.53
DE  Interaction: P25303; IntAct: EBI-16711,EBI-33556; Score: 0.35
DE  Interaction: P53207; IntAct: EBI-736,EBI-33556; Score: 0.53
DE  Interaction: Q00539; IntAct: EBI-11835,EBI-33556; Score: 0.53
DE  Interaction: P38996; IntAct: EBI-11776,EBI-33556; Score: 0.53
DE  Interaction: P32605; IntAct: EBI-680,EBI-33556; Score: 0.35
DE  Interaction: P39936; IntAct: EBI-33556,EBI-9006; Score: 0.53
DE  Interaction: Q03782; IntAct: EBI-33556,EBI-627; Score: 0.53
DE  Interaction: Q00916; IntAct: EBI-33556,EBI-724; Score: 0.53
DE  Interaction: Q06217; IntAct: EBI-33556,EBI-235; Score: 0.53
DE  Interaction: Q04693; IntAct: EBI-33556,EBI-519; Score: 0.53
DE  Interaction: P33334; IntAct: EBI-33556,EBI-465; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-33556,EBI-12823; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-33556,EBI-12228; Score: 0.64
DE  Interaction: Q01560; IntAct: EBI-33556,EBI-12114; Score: 0.53
DE  Interaction: Q03735; IntAct: EBI-33556,EBI-27955; Score: 0.53
DE  Interaction: Q07508; IntAct: EBI-33556,EBI-673; Score: 0.53
DE  Interaction: P50094; IntAct: EBI-33556,EBI-9195; Score: 0.35
DE  Interaction: P50095; IntAct: EBI-33556,EBI-9190; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-31475,EBI-33556; Score: 0.27
DE  Interaction: P32357; IntAct: EBI-340,EBI-33556; Score: 0.27
DE  Interaction: P20448; IntAct: EBI-5612,EBI-33556; Score: 0.27
DE  Interaction: P47130; IntAct: EBI-763,EBI-33556; Score: 0.27
DE  Interaction: P40018; IntAct: EBI-432,EBI-33556; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-7458,EBI-33556; Score: 0.35
DE  Interaction: P38074; IntAct: EBI-33556,EBI-8394; Score: 0.37
GO  GO:0000243;
GO  GO:0005846;
GO  GO:0048471;
GO  GO:0000339;
GO  GO:0045292;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLEEFDEVKYDHSTKRLDTPSRYLLRKARRNPNGLQELRESMKSSTIYVGNLSFYTSEEQIYELFSKCGTIKRIIMGLD
SQ  RFKFTPCGFCFIIYSCPDEALNALKYLSDTKLDEKTITIDLDPGFEDGRQFGRGKSGGQVSDELRFDFDASRGGFAIPFA
SQ  ERVGVPHSRFDNSSSQSNTNNYIPPPDAMGTFRPGFDEEREDDNYVPQ
//
ID  Q99222;
PN  ARF3-interacting protein 1;
GN  AFI1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Note=Enriched at the nuclear envelope and at the plasma membrane, especially in daughter cells and at the bud neck.
DR  UNIPROT: Q99222;
DR  UNIPROT: D6W2I7;
DR  UNIPROT: Q92274;
DR  Pfam: PF07792;
DR  PROSITE: PS50211;
DE  Function: Involved in actin patch polarization. Required for maintaining a proper budding pattern in yeast cells. Required for proper polarized localization of the ADP-ribosylation factor ARF3 at the plasma membrane. {ECO:0000269|PubMed:18397879}.
DE  Reference Proteome: Yes;
DE  Interaction: P53865; IntAct: EBI-1781795,EBI-29172; Score: 0.55
DE  Interaction: P11484; IntAct: EBI-1781795,EBI-8627; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-1781795,EBI-8648; Score: 0.35
GO  GO:0005938;
GO  GO:0005935;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0051666;
GO  GO:0000282;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRRELNNSISNRSIENESFPFERPNVSYIISAEFDNKLGPILKHQYPKDIPGFNQFSHEQRNGNTSVSMNLASLMIPSS
SQ  IERNPGKQDITVFTLYYNKFTQNYQLFPVPKDPRFSFNLHHREQSDGSVTNSIYYDAENHQDAKNNRYTIVLEDDELECQ
SQ  EVQNNQKAIDNEPLFFINVANTVLDTTNDRGAVIKSIAIGTPLKTFFAFKNIIVLVLDLYMKAPTQAAATDILLDCFNML
SQ  NSIDLTLINDIHSKSSIQEVLHSIHDESIITKVFLDPDSTLKKLFCINGFDTKDKYGNIVTFHDQLIQYHFTRFQPKTLP
SQ  PFLLKIPLQFNMIRREPIYIENDYNELVLKFLDKFVPYLLKAGQKVNAWKLVINSTKLSKEDLCAFILSLANITATYASD
SQ  PQSYFKGNAALIFPYMDISLVDGLRAYVASNSDFVGCFAIIGTANPIFRYQLDIWDYYYDVDEGVFYENNSPEKEKPDTV
SQ  AEVKIGPNPLRKIFNRPHFSTNAVNESQVNLGQKLFSLLIDEYHDSDTIMSVLRRLNVLQLENLLDALKRREIPPNIALK
SQ  DEYIMFYKDFFIFPEFFDYFTLHSIELLSNLDNCLFSLGNTCQLFSTEQIYSQLSQILDIVKELFRMVSVSRTNIEKFLN
SQ  ACLNYSPFKILPTAQLHGDNISRWSFESEVRQGFDNFNSYMGIEKDPHGVIVSAIDLFTQIYSFDILAFFLTFITKESGQ
SQ  DLPFTKSLSRRRTYLTRIAQSSSLRQFLQLSTRPNIRILGGNGQGTGNSNYPEFTNASSVISPKLRASPLLERRASKICY
SQ  AITKLLYRLECHPIGMALLKKYLHNQLREAYLESKRHFISKKGDSTNTSSTIASSSFAGASVPLSSNESGMLNGLKQINE
SQ  QQESTLETTQKED
//
ID  P61204;
PN  ADP-ribosylation factor 3;
GN  ARF3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}.
DR  UNIPROT: P61204;
DR  UNIPROT: A8K6G8;
DR  UNIPROT: B7ZB63;
DR  UNIPROT: P16587;
DR  PDB: 6II6;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DR  OMIM: 103190;
DR  DisGeNET: 377;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
DE  Reference Proteome: Yes;
DE  Interaction: P54259; IntAct: EBI-641535,EBI-945980; Score: 0.37
DE  Interaction: O15264; IntAct: EBI-2116951,EBI-641535; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-5323863,EBI-641535; Score: 0.35
DE  Interaction: Q14186; IntAct: EBI-749713,EBI-641535; Score: 0.35
DE  Interaction: O35071; IntAct: EBI-2366194,EBI-641535; Score: 0.40
DE  Interaction: P97302; IntAct: EBI-2552417,EBI-641535; Score: 0.40
DE  Interaction: Q8VD62; IntAct: EBI-762039,EBI-641535; Score: 0.40
DE  Interaction: Q5PRE5; IntAct: EBI-2553990,EBI-641535; Score: 0.40
DE  Interaction: Q8TBB1; IntAct: EBI-739832,EBI-641535; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-638194,EBI-641535; Score: 0.37
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006661;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  Q66669;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  82831;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q66669;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MNGSKRLVAQLCQVVRSFICQPGTAVDLWQCAAGPHVFAKGSTQPICIVKLVHGQIYNLEFVYKYWCHILQSEKFPYSPV
SQ  FIISNNGLAITLKCFLCEPMDLHSQFGRCLSMDTDVYLPKNTSVVLSQDDFTKFKTNLVFSKDLNVFNSMVVCRTYLTDF
SQ  RQALQFLVVKAKNPKRVTAILGTIAQTLGLTPDTRSGEGGKNSERGEDDMVRRPIRAHRAGDSGGSPGTLPAEPQGAPTP
SQ  PGGGLGLSSGLGLVRRWTRCAFQRYFTVLAVGAVAAATFLAGAKLTG
//
ID  Q06616;
PN  Nuclear envelope protein YPR174C;
GN  YPR174C;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
DR  UNIPROT: Q06616;
DR  UNIPROT: D6W4H5;
DR  Pfam: PF08537;
DE  Function: Specialized component of the nuclear membrane that may be involved in the connection of the spindle pole body (SPB) to the nuclear envelope. {ECO:0000269|PubMed:15282802}.
DE  Reference Proteome: Yes;
DE  Interaction: P40069; IntAct: EBI-36065,EBI-9166; Score: 0.53
DE  Interaction: P47069; IntAct: EBI-36065,EBI-25811; Score: 0.37
DE  Interaction: P08456; IntAct: EBI-14055,EBI-36065; Score: 0.37
DE  Interaction: P32562; IntAct: EBI-36065,EBI-4440; Score: 0.37
DE  Interaction: P40578; IntAct: EBI-10855,EBI-36065; Score: 0.37
DE  Interaction: Q03860; IntAct: EBI-36065,EBI-37537; Score: 0.37
DE  Interaction: P53174; IntAct: EBI-6200,EBI-36065; Score: 0.37
DE  Interaction: Q5SW96; IntAct: EBI-36065,EBI-747813; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-749265,EBI-36065; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-36065,EBI-743099; Score: 0.56
DE  Interaction: P07259; IntAct: EBI-36065,EBI-14372; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-37072,EBI-36065; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-20647,EBI-36065; Score: 0.27
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGIQEKTLGIRKERKLVVVPRERNHVRHASQRTRSKNYKNISKKRAQQHAFGFNIAKTLAKIQAFVWGSPADEEEESVVP
SQ  LSKNSQDCVPLQWQAKFAQLRQQLHSTQKELQFVKEKCHLLQSVLDDANIDQRYLESRRDMKNIERDNLKPTENLPPSPV
SQ  RAVNPLVTSSPIHMSPLQSRQRPVSSLQPPKGPNFYAKYPKLPQTNILRESPTEDSVPHAE
//
ID  O46382;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
GN  ARFGEF1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}.
DR  UNIPROT: O46382;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0030532;
GO  GO:0005802;
GO  GO:0005086;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007030;
GO  GO:0030837;
GO  GO:0034260;
GO  GO:0090284;
GO  GO:0090303;
GO  GO:0015031;
GO  GO:0032012;
GO  GO:2000114;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKY
SQ  FLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVT
SQ  SQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHE
SQ  PESPQLRYLPPQTVDHIPQEHEGDLDPQTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGENHD
SQ  CEEKPQDIVQSIVEEMVNIVVGDTGERTTINVSADGNNGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDT
SQ  QESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFGTNEMFINA
SQ  IKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQ
SQ  SVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTL
SQ  GQEKPSEQETSEMKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFTKKPKRGIQYL
SQ  QEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRL
SQ  MEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGK
SQ  KISMKETKELTIPAKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAF
SQ  SVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYL
SQ  GNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGAKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQS
SQ  VVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGC
SQ  NPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFS
SQ  VFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQA
SQ  FKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGYTYEKHWWQDLFRIVFRIFDNMKL
SQ  PEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIW
SQ  DKTCNCTLDIFKTTIPHALLTWRPISGETAPPTPSPVSENQLDTISQKSVDIHDSIQPRSADNRQQAPLASVSTVNEEIS
SQ  KIKPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSRKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLF
SQ  KLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRASAWEEVQQRLLNVCSE
SQ  ALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPP
SQ  EQELGINKQ
//
ID  P52465;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10370;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P52465;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MANVLKEKMYDELLSATCRILKLGSHDYRITERNLLSKNPKFPLCDIILKLDYAYNLEYLLSLWEHVTKQEPRFVFKNTG
SQ  GAVSMSCYLHAPVKVEGHHAVRECNILRVNECLTVRMSDIVAMKPSTFAVFTKCIIRRNRDDTYVVEFVAFGPENESEYI
SQ  SLLKAIFLKKCSMGKQHLESNRFCQGLRRRSSHVLEKGRFESSGKVVNKASAVVTSQESIKQFYEKEKSLLSGVKFWRLS
SQ  ERHCRFALVGICFLLALYFCYVLLKKTPTPASGSVV
//
ID  Q6ZPJ0;
PN  Testis-expressed protein 2;
GN  Tex2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi- pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus- vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833, ECO:0000250|UniProtKB:Q8IWB9}.
DR  UNIPROT: Q6ZPJ0;
DR  UNIPROT: B1ATR1;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000250|UniProtKB:Q8IWB9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0008289;
GO  GO:0006869;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTSLNGRHAEKTIDMPKPSAPKVHVQRSVSRDTIAIHFSASGEEEEEEEEEFRGYLEEGLDDQSIVTGLEAKEDLYLESQ
SQ  GGHDPAGPVSTAPADGLSVSESPAILPVSENTVKLLESPAPALQVLSPVPLALSPGSSSSGPLASSPSVSSLSEQKTSSS
SQ  SPLSSPSKSPVLSSSASSSALSSAKPFMSLVKSLSTEVEPKESPHPPRHRHLMKTLVKSLSTDTSRQESDTVSYKPPDSK
SQ  LNLHLFKQFTQPRNTGGDSKTAPSSPLTSPSDTRSFFKVPEMEAKIEDTKRRLSEVIYEPFQLLSKIIGEESGSHRPKAL
SQ  SASASELSSLSGLNGHLESNNYSIKEEEGDSEGEGYGSDSNTSRSDHLKPTEDASKEVEPKGSQASSLKDLGLKTSSLVL
SQ  EKCSLSALVSKEDEEFCELYTEDFELETEGEGRLDKTLDLPLKPEVLASDGVALESEDEEDSATEHQELPVKTLGFFIMC
SQ  VYAYLILPLPYYMSGLFLGVGLGFMTAVCMIWFFTPPSAHKHHKSLKALRHQSTRSLDIKEPEILKGWMNEIYNYDPETY
SQ  HATLTHSVFVRLEGGTLRLSKPNKNISRRASYNETKPEVTYISQKIYDLSDSKIYLVPKSLARKRIWNKKYPICIELGRQ
SQ  DDFMSKAQSDKEATEEKPPPEKELPSEDLKKPPQPQEGTKSSQRDPILYLFGRTGREKEEWFRRFILASRLKSELRKPAG
SQ  VSGSKSGLLPAHSRHSSPSGHLSHSRSSSKGSVEEMMSQPKQKELVGSVRQKMLLDYSVYMGRCVPQDNRSPHRSPVQSA
SQ  ESSPTASKKLPEAPPSEEEEQEAWVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKI
SQ  LQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLGKEPLVEALKVGEIGKEGCRPRAYCLADSDEESSSAGSSEED
SQ  DPPEPTAGDKQPLPGAEGYVGGHRTSKIMRFVDKITKSKYFQKATETEFIKKKIEEVSNTPLLLTVEVQECRGTLAVNIP
SQ  PPPTDRIWYGFRKPPYVELKARPKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIPIMHSAMDPRSTSCLLKEP
SQ  PVETSDQL
//
ID  Q3UFJ6;
PN  Transmembrane protein 184A;
GN  Tmem184a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q1RMW2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18321981}; Multi-pass membrane protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19097053}. Note=Colocalizes with the secretory granule marker VAMP2 in pancreatic acinar cells (PubMed:19097053). {ECO:0000269|PubMed:19097053}.
DR  UNIPROT: Q3UFJ6;
DR  UNIPROT: Q8BII8;
DR  UNIPROT: Q8K1B0;
DR  Pfam: PF03619;
DE  Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (PubMed:18321981, PubMed:19097053). {ECO:0000250|UniProtKB:Q4QQS1, ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0008201;
GO  GO:0018992;
GO  GO:0032880;
GO  GO:0051046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSH
SQ  LRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKP
SQ  IRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYA
SQ  LFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFAS
SQ  LALRYAFPSQVYSEKKNSPVPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPAPSTHPG
SQ  PASGSGGGKKSRNIEKRMLIPSEDL
//
ID  Q9E6N5;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q9E6N5;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MEVIPNINSRRAGLIARIKLIVRGDLTTGNYDPVLAESFSGCIPTRSAFQFSGADGVESAFPVEYVMRMMNDWAKGECNP
SQ  YIKIQNTGVSVLIEGFFDPPINATKAPLCTDKVNVLLNTTESTGIVLSDINKIKQSIGVDCRPFQACLIVNCFVRLPIVQ
SQ  LAFRFVGPSDPGRTTKLLDSAIAAYDAKIRQRRKRNLQIMESKSQDHTSDGCIPIPIIDETHRSGITGESKSLFGMFKNI
SQ  ASGECVTTIRIPRYIVMLWIFSVLLAMVTWGSYRLYS
//
ID  Q6UDJ7;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q6UDJ7;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MRSDKYSQLVSVVNAGLGACGTSATLVYIRNNARVAPTGDIITLPARLDGPPIPAEYILEAMTSLLSIRTAWLRIQNTGQ
SQ  AVIVAGCSTQNFHHGDVTWEPPASTVTLTTAKSLWVSASAVREMKVIQRIRTAPLAAMMFMCFYRGGKNEVTVRFAFYKS
SQ  DSEPNLLKISKCVYEAIDAEATRNLPKPRGFDTPPCAVLAQRMRPLGAAEGGDRETSAQTHSPAAQAQHVMQHATATKSW
SQ  GALGRTLKHKKNLGWILFTCALSLAAAFVTAYIK
//
ID  Q0IIG6;
PN  RISC-loading complex subunit TARBP2;
GN  TARBP2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034}.
DR  UNIPROT: Q0IIG6;
DR  Pfam: PF00035;
DR  PROSITE: PS50137;
DE  Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. {ECO:0000255|HAMAP- Rule:MF_03034}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0019899;
GO  GO:0035198;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0035197;
GO  GO:0035280;
GO  GO:0035264;
GO  GO:0050689;
GO  GO:0061351;
GO  GO:0051149;
GO  GO:0045727;
GO  GO:0045070;
GO  GO:0031054;
GO  GO:0030422;
GO  GO:1903798;
GO  GO:0090065;
GO  GO:0046782;
GO  GO:0007338;
GO  GO:0035087;
GO  GO:0043403;
GO  GO:0007286;
GO  GO:0030423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSK
SQ  KAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDVPVFTAAAAATPVPSAVPTRSSPMEVQPPVSPQQSECNP
SQ  VGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEP
SQ  EDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCSVLSELSEEQAFHVSYLDIEELSLS
SQ  GLCQCLVELSTQPATVCHGSAATREAARGEAARRALQYLKIMAGSK
//
ID  O04326;
PN  Nuclear pore complex protein NUP35;
GN  NUP35;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: O04326;
DR  UNIPROT: Q8VYL9;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9C933; IntAct: EBI-4452551,EBI-4424446; Score: 0.37
DE  Interaction: Q8GYN0; IntAct: EBI-4424446,EBI-4450073; Score: 0.37
DE  Interaction: Q8L586; IntAct: EBI-4424446,EBI-4455687; Score: 0.37
DE  Interaction: Q8LB17; IntAct: EBI-4434215,EBI-4424446; Score: 0.37
DE  Interaction: Q8LF05; IntAct: EBI-4424446,EBI-4439718; Score: 0.37
DE  Interaction: Q8RXL7; IntAct: EBI-4424446,EBI-4427323; Score: 0.37
DE  Interaction: Q8RY62; IntAct: EBI-4458877,EBI-4424446; Score: 0.37
DE  Interaction: Q93VN2; IntAct: EBI-4424446,EBI-4452986; Score: 0.37
DE  Interaction: Q93XX0; IntAct: EBI-4424446,EBI-4435989; Score: 0.37
DE  Interaction: Q93Z42; IntAct: EBI-4466134,EBI-4424446; Score: 0.37
DE  Interaction: Q93ZQ3; IntAct: EBI-4450641,EBI-4424446; Score: 0.37
DE  Interaction: Q93ZW4; IntAct: EBI-4455720,EBI-4424446; Score: 0.37
DE  Interaction: Q946Y7; IntAct: EBI-4438441,EBI-4424446; Score: 0.37
DE  Interaction: Q94A32; IntAct: EBI-4438745,EBI-4424446; Score: 0.37
DE  Interaction: Q94A99; IntAct: EBI-4451043,EBI-4424446; Score: 0.37
DE  Interaction: Q94CH8; IntAct: EBI-4424550,EBI-4424446; Score: 0.37
DE  Interaction: Q94JU2; IntAct: EBI-4459794,EBI-4424446; Score: 0.37
DE  Interaction: Q9CAN1; IntAct: EBI-4424446,EBI-4424904; Score: 0.37
DE  Interaction: Q9FI47; IntAct: EBI-4424446,EBI-4435326; Score: 0.37
DE  Interaction: Q9FZ98; IntAct: EBI-4424446,EBI-4425682; Score: 0.37
DE  Interaction: Q9LJU6; IntAct: EBI-4424446,EBI-4429742; Score: 0.37
DE  Interaction: Q9LQ32; IntAct: EBI-4436710,EBI-4424446; Score: 0.37
DE  Interaction: Q9LSW5; IntAct: EBI-4424446,EBI-4425852; Score: 0.37
DE  Interaction: Q9LVD9; IntAct: EBI-4431584,EBI-4424446; Score: 0.37
DE  Interaction: Q9LXV1; IntAct: EBI-4424446,EBI-4430604; Score: 0.37
DE  Interaction: Q9LYP1; IntAct: EBI-4436922,EBI-4424446; Score: 0.37
DE  Interaction: Q9M1J1; IntAct: EBI-4424446,EBI-4436721; Score: 0.37
DE  Interaction: Q9M1J7; IntAct: EBI-4438348,EBI-4424446; Score: 0.37
DE  Interaction: Q9M2J9; IntAct: EBI-4434027,EBI-4424446; Score: 0.37
DE  Interaction: Q9M9S6; IntAct: EBI-4424446,EBI-4434173; Score: 0.37
DE  Interaction: Q9SA23; IntAct: EBI-4436558,EBI-4424446; Score: 0.37
DE  Interaction: Q9SD04; IntAct: EBI-4459803,EBI-4424446; Score: 0.37
DE  Interaction: Q9SHG7; IntAct: EBI-4424446,EBI-4436589; Score: 0.37
DE  Interaction: Q9SIH4; IntAct: EBI-4451446,EBI-4424446; Score: 0.37
DE  Interaction: Q9SIQ8; IntAct: EBI-532034,EBI-4424446; Score: 0.37
DE  Interaction: O48741; IntAct: EBI-4436108,EBI-4424446; Score: 0.37
DE  Interaction: O65397; IntAct: EBI-4457543,EBI-4424446; Score: 0.37
DE  Interaction: O80594; IntAct: EBI-4428472,EBI-4424446; Score: 0.37
DE  Interaction: O80895; IntAct: EBI-4424446,EBI-4456509; Score: 0.37
DE  Interaction: O81062; IntAct: EBI-4440921,EBI-4424446; Score: 0.37
DE  Interaction: O82174; IntAct: EBI-4424446,EBI-4453441; Score: 0.37
DE  Interaction: O82219; IntAct: EBI-4424446,EBI-4433315; Score: 0.37
DE  Interaction: P26587; IntAct: EBI-4460900,EBI-4424446; Score: 0.37
DE  Interaction: P27202; IntAct: EBI-4461393,EBI-4424446; Score: 0.37
DE  Interaction: P30302; IntAct: EBI-4431139,EBI-4424446; Score: 0.37
DE  Interaction: P42813; IntAct: EBI-4424446,EBI-4432112; Score: 0.37
DE  Interaction: P47192; IntAct: EBI-4424446,EBI-4433747; Score: 0.37
DE  Interaction: P53799; IntAct: EBI-4424446,EBI-4476955; Score: 0.37
DE  Interaction: P82874; IntAct: EBI-2352074,EBI-4424446; Score: 0.37
DE  Interaction: P92941; IntAct: EBI-4438503,EBI-4424446; Score: 0.37
DE  Interaction: Q147J7; IntAct: EBI-4432597,EBI-4424446; Score: 0.37
DE  Interaction: Q38935; IntAct: EBI-4444120,EBI-4424446; Score: 0.37
DE  Interaction: Q41975; IntAct: EBI-4449798,EBI-4424446; Score: 0.37
DE  Interaction: Q42328; IntAct: EBI-4436355,EBI-4424446; Score: 0.37
DE  Interaction: Q42342; IntAct: EBI-4424446,EBI-2295493; Score: 0.37
DE  Interaction: Q5XF13; IntAct: EBI-4424446,EBI-4431954; Score: 0.37
DE  Interaction: Q5XF36; IntAct: EBI-4431742,EBI-4424446; Score: 0.37
DE  Interaction: Q6IDC5; IntAct: EBI-4431568,EBI-4424446; Score: 0.37
DE  Interaction: Q6NLF5; IntAct: EBI-4424446,EBI-4431243; Score: 0.37
DE  Interaction: Q7XA86; IntAct: EBI-4429137,EBI-4424446; Score: 0.37
DE  Interaction: Q84WI4; IntAct: EBI-4429346,EBI-4424446; Score: 0.37
DE  Interaction: Q8GWH4; IntAct: EBI-4426287,EBI-4424446; Score: 0.37
DE  Interaction: Q8GWM8; IntAct: EBI-4424446,EBI-4425706; Score: 0.37
DE  Interaction: Q8GWT5; IntAct: EBI-4424446,EBI-4439395; Score: 0.37
DE  Interaction: Q8GX78; IntAct: EBI-4425789,EBI-4424446; Score: 0.37
DE  Interaction: Q9SRE4; IntAct: EBI-4434931,EBI-4424446; Score: 0.37
DE  Interaction: Q9SRT3; IntAct: EBI-4455819,EBI-4424446; Score: 0.37
DE  Interaction: Q9STW3; IntAct: EBI-4429423,EBI-4424446; Score: 0.37
DE  Interaction: Q9XI60; IntAct: EBI-4424446,EBI-4424450; Score: 0.37
DE  Interaction: Q9ZSD4; IntAct: EBI-4476863,EBI-4424446; Score: 0.37
DE  Interaction: Q9ZV66; IntAct: EBI-4424446,EBI-4429327; Score: 0.37
DE  Interaction: O22690; IntAct: EBI-4424446,EBI-4436104; Score: 0.37
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAAAHRTPKSGRQSLLFQDLASPVSARRGKFSSPGQAAAVSALWRENFGGSDLPPPPMYTLDDRSDFSPESGIADYSAS
SQ  PDAKSDRRTPFQSSGKNIVTPGKGKLEASPSFSLLNAQQSQQVSGSPSWWSQSKAGSSTEQDDKGKGSPVEGVVQPGALV
SQ  TLPPPREVARPEVQRQIIPTGNLDEEEWVTVYGFSPGDTNLVLREFEKCGMVLKHVPGPRNANWMHILYQNRSDAHKALN
SQ  KAGMMINGVVIVGVKPVDPIQKQALNERLNNQGFMPLPPPSSTRNTARPLSRPQYLQNGSAFSPQPSGGAMASPSKSMVS
SQ  KFFDLMFGV
//
ID  Q55AP1;
PN  Metabotropic glutamate receptor-like protein A;
GN  grlA;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17950724}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17950724}.
DR  UNIPROT: Q55AP1;
DR  Pfam: PF00003;
DR  Pfam: PF02608;
DR  PROSITE: PS50259;
DE  Function: May play an important role in the terminal differentiation. {ECO:0000269|PubMed:17950724}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0004930;
GO  GO:0030587;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNKLKFLIILFITFLFNLKYINSLKQCKISVLLSGDWSDMGYNYQMNNARIKAESALNLEMSLCYKNLEVSIDLAKQAIE
SQ  DSIKKGANFIVISSSVHTSIGYEYARLHRDKDIYWLIRGRGRPVPDDLPKVAVINFNTHLLHYTLGLVSGYLTTSGTVGF
SQ  ISPGPQILALANSNSFYLGALASRKNVTFLNAYTGSWYNPEVAYKASQMLISNGADFIGMSQDDMSVQKALMDSGKMALG
SQ  ITGFSNRLIWGSDIALSYITDWSDVFIKYAGHILNDTWPEYTDYYTTLAEGGSLLFDTFSYRVPSEVQKLVSLEIEKLKN
SQ  SSYQPFRCNPMYSQINLNFDSNGCANDMEFKNTKLLLKGTDISKTINLGLYTIPIEFVDYSNSMKLGLTIVSGFCILFCI
SQ  ISMVLVIMFRHAKIIKSASPIFCLLILFGCIIIFSGCIIFSLSPTDGICGARVWLLSIGYTIFLGSLLVKNWRIWLLFDN
SQ  PKLKKRSITNWKLYPFVAGILAADVLILALWQGLGDIRSESRIGIDSLTKYQYANVCSSNDQGSVALYILLVFHGIKLLA
SQ  ACFISFKIKAVDIEEFNESKPIASSIYIITFCLFIVIPLMVSPQSVASQVITIVVCAIVTTLISISLLFGSKFYMMATQG
SQ  LALNQTFATNTKSSSFSLSLEKQKSKSNGLEFEDSDESEEKLPQIKNYSNSEIPNLQHNHSRLAHFSSDSCTSAEQDSKL
SQ  DLENQNDENEIENNQNNQNNIVEDCQKVEKLEKDENLEKDENLEKDENLEKDNENQSIIQKKRLSKNFNQSEIDPDDV
//
ID  O22224;
PN  Nuclear pore complex protein NUP93A;
GN  NUP93A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: O22224;
DR  UNIPROT: Q94CF2;
DR  Pfam: PF04097;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q01525; IntAct: EBI-637502,EBI-2356241; Score: 0.35
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANDQEMSGWTDLLHSSSKLLEQAAPSSQFPPLQRNLDQLEALSKKLKAKTLRNEAPSQSIAATRLLAREGINAEQLARD
SQ  LKSFELKTTFEDVFPAEATSVEEYLQQVHEMAMVSAIQEAQKDNVRSFNDYMMKVLEEDWRKEKRDFLQSLSRISMLPKT
SQ  NMIDTSREAHAGQLVPVGSSPRVSSTPGKELVALANIPIHEKKAYVYGEVVKKLNTSRERGMPFRPAMCFKDAYDTLGAE
SQ  VTRGKSVNMQKIWQLVQAITGEDSAVRQGVSKRMALAIGARHHLQHGHEKFIMDTIQTHPTQAALGGSVGNLQRIRAFLR
SQ  IRLRDYGVLDFDSTDARRQPPVDTTWQQIYFCLRTGYYEEAREIARSTRSSQQFAPLLTEWITTDGMVAAESAAIASEEC
SQ  EKMLRMGDRLGRTAYDKKKLLLYTIISGSRRQIERILRDLSTLFNTIEDFLWFKLSCIRDVTGGSSSVVLNDGLAPYSLD
SQ  DLQAYLNKFEPSYYTKNGKDPLVYPYVLLLSVQLLPAIMHLSKEAGDGGYNIDAVHIAISLVDHSVLSEGSGTGHKLSVM
SQ  DSNAEASSMIRQYGSMFLHHGDLQMTVEYYAQAAATVGGGQLAWSGRSNVDQQRQRNLMLKQLLTEILLRERGIYFLLGA
SQ  RGSGEEGQLGRFFPDSRLRQQFLVEAAHQCQEAGLYDKSIELQKRVGAFSAALETINKCLSEAICSLARGRLDGESRTSG
SQ  LILAGNDILETYKYYPEVSLQERERVMEQETILRELEAILSIHKLGRLGNHLDALREIAKLPFLHLDPRMPDATADVFQS
SQ  ASPYFQTCVPDLLKVALTCLDNVPDTDGSIRAMRSKIAGFLASNTHRNWPRDLYEKVARSF
//
ID  F6S3G9;
PN  Aquaporin-11;
GN  AQP11;
OS  9796;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery of lipid droplets. it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
DR  UNIPROT: F6S3G9;
DR  Pfam: PF00230;
DE  Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (By similarity). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating to the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development (By similarity). {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000250|UniProtKB:Q8NBQ7}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015267;
GO  GO:0015254;
GO  GO:0015250;
GO  GO:0009992;
GO  GO:0048388;
GO  GO:0080170;
GO  GO:0050680;
GO  GO:1904293;
GO  GO:0032364;
GO  GO:0008284;
GO  GO:0033577;
GO  GO:0051260;
GO  GO:0006612;
GO  GO:0072014;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTALRALWSEMQDTCTSLGLMLSVVLLAGLARVVARQQQLHRPMAHAFVLEFLATLQLCCCTHELLLLSEQEPAHPTWPL
SQ  TLIYFFTLVHGLTLVGTSSNPCGVMMQMMLGGMSPEMGAVRLLAQLIGALGSRYCIGALWSLGLTKYHVSERSFACKNPI
SQ  QVDLPKAVIVEALCSFIFHSALLNFQEVRPKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFKCFDEAFLQFFIVY
SQ  WLAPSLGILLMILMFSFFLPWLYNNHTINKKE
//
ID  O42446;
PN  Deoxyribonuclease-1;
GN  dnase1;
OS  8127;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: O42446;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9395327). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (By similarity). Binds specifically to G-actin and blocks actin polymerization. Preferentially attacks double-stranded DNA and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini (PubMed:9395327). {ECO:0000250|UniProtKB:P21704, ECO:0000269|PubMed:9395327}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0004530;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQTYRSRMHLVCSLGLFLTLLHLSNSLLLGAFNIKSFGDTKASNATLMNIITKIVKRYDVILIQEVRDSDLSATQTLMNY
SQ  VNKDSPQYKYIVSEPLGASTYKERYLFLYREALVSVVKSYTYDDGPEETGQDTFSREPFVVMFSSKNTAVRDFTLIPQHT
SQ  SPDLAVRELNALYDVVLDVRARWNTNDIVLLGDFNAGCSYVSGSAWQQIRIFTDKTFHWLITDAADTTVSQTVCPYDRIV
SQ  VTTDMMRGVVQNSAKVYNYMTDLNLKQDLALAVSDHFPVEVKLS
//
ID  Q2TLY1;
PN  Macoilin-2;
GN  maco1b;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TQE6}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TQE6}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q2TLY1;
DR  UNIPROT: B7ZUY4;
DR  Pfam: PF09726;
DE  Function: May play a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0051015;
GO  GO:0008017;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQ
SQ  NGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTE
SQ  NLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPSSSASSSSKGDRKQKYGGGKNSASHR
SQ  DPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQA
SQ  KQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDIK
SQ  VKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQ
SQ  EIKDLKQKIAEVMAVMPSVVYSADTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPLKK
//
ID  Q5W5U4;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  DDX4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q5W5U4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. {ECO:0000250|UniProtKB:Q61496}.
DE  Reference Proteome: Yes;
GO  GO:0033391;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0007276;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0007275;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEIIKPHISSYVPVFEKDRYSSGANGDTFNRTPASSSEMGDGSSRRDHFMRSGFASGRSLGNRDPGESNKREN
SQ  TSTVGGFGVGKSFGNRGFSNNKFEEGDSSGFWRESSIDCEDNQTRNRGFSKRGGYQDGNDSEALGSSRRGGRGSFRGCRG
SQ  GFGRGSPNSDYEQDEGTQRSGGIFGSRRSALSGAGNGDTFQSRSGGGSGRGGYKGLNEEVITGSGKNSWKSEAEGGESGD
SQ  TQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDPPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYS
SQ  IPIIQGGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVV
SQ  IYGGTQLGHSIRQIVQGCNILCATPGRLMDVIGKEKIGLRQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTL
SQ  MFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIAT
SQ  FLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTG
SQ  RAISFFDLESDSQLAQPLVKVLSDAQQDVPAWLEEIAFSTYGPGFSGNARGNVFASVDTRKNYPGKSSLNTAGFSSTQAP
SQ  NPVDDESWD
//
ID  O22873;
PN  bZIP transcription factor 18;
GN  BZIP18;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm {ECO:0000269|PubMed:27896439}.
DR  UNIPROT: O22873;
DR  UNIPROT: O23726;
DR  Pfam: PF00170;
DR  PROSITE: PS50217;
DE  Function: Transcription factor that may participate with bZIP34 in the gametophytic control of pollen development. {ECO:0000269|PubMed:27896439}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LZW4; IntAct: EBI-4438646,EBI-307576; Score: 0.56
DE  Interaction: Q94AY3; IntAct: EBI-1787347,EBI-4438646; Score: 0.37
GO  GO:0005737;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003700;
GO  GO:0043621;
GO  GO:0044212;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDPSNPQPNQSNLSQCPPLATAPTPAPVRGPYHRRAHSEVQFRLPEDLDLSEPFGGFDELGSEDDLFCSYMDIEKLGSG
SQ  SGSASDSAGPSAPRSDNPFSAENGGAEAGNSRPRHRHSLSVDGSSTLESIEAKKAMAPDKLAELWVVDPKRAKRIIANRQ
SQ  SAARSKERKARYILELERKVQTLQTEATTLSAQLSLFQRDTTGLSSENTELKLRLQVMEQQAKLRDALNEQLKKEVERLK
SQ  FATGEVSPADAYNLGMAHMQYQQQPQQSFFQHHHQQQTDAQNLQQMTHQFHLFQPNNNQNQSSRTNPPTAHQLMHHATSN
SQ  APAQSHSYSEAMHEDHLGRLQGLDISSCGRGSNFGRSDTVSESSSTM
//
ID  P59595;
PN  Nucleoprotein;
GN  N;
OS  694009;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:19106108}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17210170}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
DR  UNIPROT: P59595;
DR  UNIPROT: Q7T3Z4;
DR  UNIPROT: Q7TA14;
DR  UNIPROT: Q7TF99;
DR  UNIPROT: Q80E50;
DR  PDB: 1SSK;
DR  PDB: 1X7Q;
DR  PDB: 2CJR;
DR  PDB: 2GIB;
DR  PDB: 2JW8;
DR  PDB: 2OFZ;
DR  PDB: 2OG3;
DR  PDB: 3I6L;
DR  PDB: 6IEX;
DR  Pfam: PF00937;
DE  Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}.
DE  Reference Proteome: Yes;
DE  Interaction: Self; IntAct: EBI-7602718,EBI-7602718; Score: 0.81
DE  Interaction: P61769; IntAct: EBI-714718,EBI-7602718; Score: 0.52
DE  Interaction: P59596; IntAct: EBI-7602718,EBI-25487824; Score: 0.61
DE  Interaction: P63279; IntAct: EBI-7602718,EBI-80168; Score: 0.75
DE  Interaction: Q05639; IntAct: EBI-7602718,EBI-354943; Score: 0.69
DE  Interaction: P62937; IntAct: EBI-7602718,EBI-437708; Score: 0.54
GO  GO:0044172;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0019013;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSG
SQ  PDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVL
SQ  QLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQ
SQ  QQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSR
SQ  IGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAAD
SQ  MDDFSRQLQNSMSGASADSTQA
//
ID  Q5Y5T1;
PN  Palmitoyltransferase ZDHHC20;
GN  Zdhhc20;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}.
DR  UNIPROT: Q5Y5T1;
DR  UNIPROT: Q3TDL1;
DR  UNIPROT: Q8VCL6;
DR  UNIPROT: Q9D3Q8;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Catalyzes palmitoylation of Cys residues on target proteins (PubMed:15603741). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains (By similarity). {ECO:0000250|UniProtKB:Q5W0Z9, ECO:0000305|PubMed:15603741}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016409;
GO  GO:0019706;
GO  GO:0008270;
GO  GO:0018230;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5W0Z9};
SQ  MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVSTISRTGEKGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASP
SQ  SKEFYLSNSEKERYEKEFSQERQQDILRRAARDLPIYTTSASKAIRYCEKCQLIKPDRAHHCSACDRCVLKMDHHCPWVN
SQ  NCVGFTNYKFFMLFLLYSLLYCLFVAATVLEYFIKFWTLCRRKSTENCPKNEPTVLNFPSAKFHVLFLFFVSAMFFVSVL
SQ  SLFSYHCWLVGKNRTTIESFRAPMFSYGIDGNGFSLGCSKNWRQVFGDEKKYWLVPIFSSLGDGCSFPARLVGMDPEQAS
SQ  VANQSDYVRSIGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGVTKSGTNNHVTVEIEN
//
ID  Q9WNW0;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  76875;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: Q9WNW0;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0018144;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFSTMQVVVGFLKTSMGLQSIRDIVQKAKVDEKDKTLLHIHLCFFHANEMARDLNEGMDVSQIHSSAAIKYRAAIVTRH
SQ  VKMNVETGGYDRKRMVEYNNETCVNWFSCEFKEEKEESQELPVDEDCVEEIVENFLENCGISDQNDQISTTSNANYAFGQ
SQ  GLYEYATRVSDAIVAVISGSIKKGIDEFLDKVYAAMSQIFAAWMPKIRAAFQWFENIKEVVKNWARTMHEKINCILVGME
SQ  DCLYMGAGLVAATCIVTLLEKFMVVTKILPAPCGAATLFLTTAMATISAAYVCTKAVEKSVMLTNVLHFVTTNCQIVLNA
SQ  LFNHDATKKELGANQNEGEAPTGVGQFGISTMLQDVANLMSTWSTNSVTEIGRTFGAISQIKNGILALRDMVYFVFEKLS
SQ  DLAHKVLGFESQVLADLTILLGENVADWLSECDCMVSYMLEFNSRNREIFDRLSQLIEKGRLIRTGVLRTGHRGSSQVMA
SQ  LVTKALEKLIELHNSVVMSGSNTTRKAPFMVFFTGASGTGKTSVVQRVAINWLQEEQLGTNEIYSRNGQDPFWSGYKRHA
SQ  VVTYDDFGAVPGTTSNEAEIINVISRNPYATVMAGLAEKGMYFDSRLVLASRNFLAANPESGVHDSEAYERRRHAVIRVS
SQ  LKPGVPYNADDPCANQTYTLLDSKTPFREIQTFETYAELWSYLYTSFKEHEVQEELYLKSLPILDSDKKEALEGLVGLTV
SQ  IATSFAPKAVMQYGMEKFPGHHFLVSDGEKCYFWHGDGSVESASVEQMQLSKQDVAQLKQQGLSTAMMYKDLAKAFPTLN
SQ  SLAVLYAKNIVVKRWVGPDLEPTKTCEDVYMREQIGNLPKWQRAYLYVLSKYLTTQSPRGWFMECLEETKKNLRATYLWE
SQ  YKQWPLPLKLALGSLIAIMAGGAIWYSLQSLWCMSGDASFVAGAATVFSVSSFAGQSDIPNRDNSERSFRNRKVRARTWQ
SQ  GQSSCFGDSALWIAETCMATLTFSNVRTQVCLAPGRGFFGVNHCLAAIPAGVMVKMDSSIGVTYFVWGKEKLLQFDGNEI
SQ  ALYMTSTLPKTVDSLLGRIHFDVETLPKTFSAVFFSYKYDPMIQQMVPELGSVTCKVHNKAYTLAHGEYRREIPQSLSYE
SQ  ASTVAGDCGSLILAEIEGKFKLVGMHVAFNGREGSASFMPYHASLDQKVGQGDFMLKYQEWAEPKILGPGCRAMGLIDPE
SQ  HALAASGKTTFVETPEEWHLDYPCDKLPSVLARGDPRLAGTVHADYDPFASGMSKYAKEAGPFDAASLKQVCSGIVEIWE
SQ  DASADFPMDEVDLDTAINGLENVEFFDALVLGTSEGFPYRLDRGPGDKGKSRYVSGESGSLKITDEGVLSDIAWFEEVSK
SQ  TQVPDLYCIECVKDERLPIRKVLHEPKSRLFTVLPMSYNIVIRKKFLNFVRFFMKRRDVLTAQVGINPYSREWTRMANKL
SQ  LSKGNNILCCDYSRFDGFLPKCIMNEIGNMIARLMKTDEVSRTQIKNLMLACTSRYAMCNRVLYRVENGIPSGFPLTVIV
SQ  NSILNEILVKYAYWHCFEDNPSVQSNFDAHVSMVVYGDDNLISVSDAISSRFDGNFLVSFMEGLGIKVTDGIDKTKVGIE
SQ  FRRLENCDFLKRSFKMSPDGTWRSPMSKESLWPQLHFVKAKKLEMAEAYINNCNNILRELWLHDVKEAEEFRNKVLRNLR
SQ  WIGHEQLLNMQQLAVFHSEQMNGVSDFLSTCVTVDSIPLMDPLVPGMLPVKTSEIIPRVFVAAEKHFEGNFNDFFTISIT
SQ  TSRKFEEDKGFVLLFPYGAGRGGLPTTQFMRENVIRKGCSIQKKFRQAYEKGNNILFISQSSVVPSYVFAVMLLHSIGAI
SQ  SRLSSNKALTQAMQTCKRLEYLPKEYEEFF
//
ID  Q9USQ0;
PN  Sporulation-specific protein spo7;
GN  spo7;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9USQ0;
DR  Pfam: PF03907;
DE  Function: Probable regulatory component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0019888;
GO  GO:0030437;
GO  GO:0071072;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSYVPNTLSVYHNLLILEASFRKTYLQLQVRRQKYMAFYVSLLVWNFYFGYRVFYRISKYSLIDLTYKLCLLCGIVTLL
SQ  LFYFSGLYRTTIVYPSRYVQQVNKAMRFFNIRLVITPVPWFQVRKPLDCGVHLILSSKRFDILVIEGWEAFRSSYFASIH
SQ  RKNNSIQSNESSESPSSKQN
//
ID  Q9V8W3;
PN  Rab proteins geranylgeranyltransferase component A;
GN  Rep;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10082978}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10082978}. Note=Coordinated with the cell cycle, located around nuclei during prophase and telophase. Located to spindle poles during metaphase.
DR  UNIPROT: Q9V8W3;
DR  UNIPROT: O97142;
DR  Pfam: PF00996;
DE  Function: Binds unprenylated Rab proteins, presents it to the catalytic component B, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab to a protein acceptor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A0B4K7J4; IntAct: EBI-186105,EBI-16584693; Score: 0.37
GO  GO:0005818;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005968;
GO  GO:0000922;
GO  GO:0008021;
GO  GO:0005092;
GO  GO:0005096;
GO  GO:0017137;
GO  GO:0007049;
GO  GO:0006886;
GO  GO:0007269;
GO  GO:1905552;
GO  GO:0018344;
GO  GO:0007264;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLDDLPEQFDLVVIGTGFTESCIAAAGSRIGKSVLHLDSNEYYGDVWSSFSMDALCARLDQEVEPHSALRNARYTWHSME
SQ  KESETDAQSWNRDSVLAKSRRFSLDLCPRILYAAGELVQLLIKSNICRYAEFRAVDHVCMRHNGEIVSVPCSRSDVFNTK
SQ  TLTIVEKRLLMKFLTACNDYGEDKCNEDSLEFRGRTFLEYLQAQRVTEKISSCVMQAIAMCGPSTSFEEGMQRTQRFLGS
SQ  LGRYGNTPFLFPMYGCGELPQCFCRLCAVYGGIYCLKRAVDDIALDSNSNEFLLSSAGKTLRAKNVVSAPGYTPVSKGIE
SQ  LKPHISRGLFISSSPLGNEELNKGGGGVNLLRLLDNEGGREAFLIQLSHYTGACPEGLYIFHLTTPALSEDPASDLAIFT
SQ  SQLFDQSDAQIIFSSYFTIAAQSSKSPAAEHIYYTDPPTYELDYDAAIANARDIFGKMFPDADFLPRAPDPEEIVVDGED
SQ  PSALNEHTLPEDLRAQLHDMQQATQEMDIQE
//
ID  Q4PCB8;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  237631;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q4PCB8;
DR  UNIPROT: A0A0D1E5R0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTTVTSSSAGLSLSAERPKNIETQHEDMVHDAQLDFYGKRLATCSSDRTVKVFDIVNGTPSTTAETLHGHQGPVWQVAWA
SQ  HPTFGDILASCSYDGKVVIWKDNGAGASIGASAPYGSQSAYGAPTSSAGGWTKIKEHTLHTASVNSISWAPHELGSILAC
SQ  ASSDGNVSVLTFNNDGTWAVDLVAAHPVGCNAVSWAPAVVPGSLISAQSVGANAGAASNGEAKLVKRFASAGCDNTVKIW
SQ  EFSQEANRFVEVEALQGHSDWVRDVAFAPNVGLPRSYLATASQDRTVLIWTQDSPTAAWSKTALNPISASAAAGAGSNKF
SQ  PDTVWRVSWSVSGNVLAVSCGDGKITLWKENLKGAWECVSEMDS
//
ID  F4HXY7;
PN  CDP-diacylglycerol--serine O-phosphatidyltransferase 1;
GN  PSS1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21554450}; Multi-pass membrane protein {ECO:0000269|PubMed:21554450}. Nucleus envelope {ECO:0000269|PubMed:21554450}. Note=Mainly localized in nuclei and ER membranes during pollen development.
DR  UNIPROT: F4HXY7;
DR  UNIPROT: Q9XI59;
DR  Pfam: PF03034;
DE  Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Is essential for phosphatidylserine (PS) biosynthesis and PE seems to be the most plausible substrate. Plays an important role in microspore maturation. {ECO:0000269|PubMed:21554450}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003882;
GO  GO:0009556;
GO  GO:0006646;
GO  GO:0006659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPNGYRKERRKEQHLGRMNGGGGDVETDLDPWTAWAYKPRTISLLLIGACFLIWASGALDPDSTTSDDLVTSVKRGVWA
SQ  MIAVFLAYSLLQAPSTVLIRPHPAIWRLVHGMAVIYLVALTFLLFQRRDDARQFMKFLHPDLGIELPEKSYGADCRIYVP
SQ  DHPTNRFKNLYDTVFDEFFLAHIFGWWGKAILIRNQPLLWVLSIGFELLEVTFRHMLPNFNECWWDSIVLDILICNWFGI
SQ  WAGMYTVRYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAHWDKDEWHPLQGPWRFIQVLTLCIIFLTVELNTFFLKFSL
SQ  WIPPRNPVILYRLILWWLIAIPTTREYNSYLQDRKPVKKVGAFCWLSLGICIVELLICIKFGSGLYPTEMPLWVVTLWGS
SQ  VGLGLVAFLLSWTWKIQKILAQKRR
//
ID  Q9UTB5;
PN  Phosphatidylserine decarboxylase 2 alpha chain;
GN  psd2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: [Phosphatidylserine decarboxylase 2 beta chain]: Mitochondrion {ECO:0000305|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}. [Phosphatidylserine decarboxylase 2 alpha chain]: Mitochondrion {ECO:0000305|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
DR  UNIPROT: Q9UTB5;
DR  Pfam: PF02666;
DE  Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd3, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980). {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19286980}.
DE  Reference Proteome: Yes;
GO  GO:0031305;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0004609;
GO  GO:0006656;
GO  GO:0006646;
GO  GO:0016540;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03208};
SQ  MRPRQRFRRFHPRWSKVNLRGFGGVGALKGVKALNGMNVRVSMRLKWISNRIHRIRRSRRLGRLSISVRPNGSWQVYLLS
SQ  SLPLRSLSRVWGQFNRAHLPTFLRTPGFKLYAWVFGCNLSELKDPDLTHYRNFQDFFCRELRPETRPVDPVSPVVSPVDG
SQ  RIVCQGVVDNNRIQHVKGLSYSLEALLGGISSSNPLVVNFEDEITPDLIQKHEQFAEQHSISLNSNNRYRKADASAAVVD
SQ  EHSDEEALLCAFTDHPHFYLNDSRNSLNYFCPFSAFEDISNSVRSSCGKRLSPSSNFDLNNLGGDDDLRSESSSDFESAP
SQ  ASILEHEPTNWDDWVQEADVTDIDSLPWHNIRPGNKLFYSVIYLAPGDYHRFHSPADWVIESRRHFSGELFSVSPFLARR
SQ  LHNLFVLNERVALLGRYEHGFMSMIPVGATNVGSIVINCDPTLSTNRLVLRKKSLGTFQEAVYKNASPVLDGMPVSRGEQ
SQ  VGGFQLGSTVVLVFEAPADFEFSTYQGQYVRVGEAL
//
ID  Q8T0B1;
PN  Nuclear envelope phosphatase-regulatory subunit 1 homolog;
GN  CG8009;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q8T0B1;
DR  UNIPROT: Q9VTA4;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase l(1)G0269 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPSACEDLKAFERRLTEVVSSYRPSTFRWRKLLAVVLSAMSMCTAISAWYWLRDPRTTVVPLTESLWIHPVFTVATLTL
SQ  VVLFILGIQKLVIAPQIITSRTRMVLGDFNMSCDDTGKLILKPRQSNNNST
//
ID  F0JAI6;
PN  Kinetochore and Eb1-associated basic protein;
GN  Kebab;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21912673}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21912673}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21912673}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21912673}. Note=During metaphase expressed in the kinetochores. During anaphase expression in the kinetochores progressively increases, and at late anaphase it is also expressed in the microtubules, specifically in the central spindle and centrosomal region. During telophase expression increases in the microtubules, and it is associated with residual spindle microtubules between chromosomes that have separated. At interphase it is expressed in the cytoplasm particularly around the nucleus. {ECO:0000269|PubMed:21912673}.
DR  UNIPROT: F0JAI6;
DR  UNIPROT: Q961C7;
DR  UNIPROT: Q9VQ69;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q7JN06; IntAct: EBI-134484,EBI-126566; Score: 0.37
GO  GO:0000777;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0043515;
GO  GO:0008017;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERS
SQ  LYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKEN
SQ  QELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKG
SQ  IKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQ
SQ  LQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKI
SQ  EKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCI
SQ  EAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP
//
ID  Q8VHC3;
PN  Selenoprotein M;
GN  Selenom;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
DR  UNIPROT: Q8VHC3;
DR  UNIPROT: B2RVS9;
DR  UNIPROT: Q3V374;
DR  UNIPROT: Q8CBT7;
DR  UNIPROT: Q8VCJ0;
DR  PDB: 2A2P;
DR  Pfam: PF08806;
DE  Function: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0016491;
GO  GO:0060612;
GO  GO:0035934;
GO  GO:0042445;
GO  GO:0035264;
GO  GO:0010269;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSILLSPPSLLLLLAALVAPATSTTNYRPDWNRLRGLARGRVETCGGUQLNRLKEVKAFVTEDIQLYHNLVMKHLPGADP
SQ  ELVLLSRNYQELERIPLSQMTRDEINALVQELGFYRKSAPEAQVPPEYLWAPAKPPEEASEHDDL
//
ID  Q6ZQH8;
PN  Nucleoporin NUP188 homolog;
GN  Nup188;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305}.
DR  UNIPROT: Q6ZQH8;
DR  UNIPROT: Q4VA15;
DR  UNIPROT: Q80UL4;
DR  UNIPROT: Q8C7A1;
DR  UNIPROT: Q8R3F1;
DR  Pfam: PF10487;
DE  Function: May function as a component of the nuclear pore complex (NPC).
DE  Reference Proteome: Yes;
DE  Interaction: P52948; IntAct: EBI-2554037,EBI-295727; Score: 0.40
DE  Interaction: P62826; IntAct: EBI-2554037,EBI-286642; Score: 0.40
DE  Interaction: Q5SRE5; IntAct: EBI-2554037,EBI-1049404; Score: 0.40
DE  Interaction: P78406; IntAct: EBI-2554037,EBI-724495; Score: 0.40
DE  Interaction: O15294; IntAct: EBI-2554037,EBI-539828; Score: 0.40
DE  Interaction: Q8WYU3; IntAct: EBI-2554037,EBI-2555238; Score: 0.40
DE  Interaction: B4DYZ6; IntAct: EBI-2554037,EBI-2562666; Score: 0.40
DE  Interaction: Q99567; IntAct: EBI-2554037,EBI-726178; Score: 0.56
DE  Interaction: O14980; IntAct: EBI-2554037,EBI-355867; Score: 0.40
DE  Interaction: P14618; IntAct: EBI-2554037,EBI-353408; Score: 0.40
DE  Interaction: Q8N1F7; IntAct: EBI-2554037,EBI-1042703; Score: 0.56
DE  Interaction: Q92878; IntAct: EBI-2554037,EBI-495494; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-2554037,EBI-354515; Score: 0.35
DE  Interaction: Q9BRJ2; IntAct: EBI-2554037,EBI-2514313; Score: 0.35
DE  Interaction: E9PJN9; IntAct: EBI-2554037,EBI-10969856; Score: 0.35
DE  Interaction: Q567V2-2; IntAct: EBI-2554037,EBI-10969860; Score: 0.35
DE  Interaction: P35658-4; IntAct: EBI-2554037,EBI-10966398; Score: 0.35
DE  Interaction: Q5T0N5-3; IntAct: EBI-2554037,EBI-4403262; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-2554037,EBI-286735; Score: 0.35
DE  Interaction: Q9BXS6-2; IntAct: EBI-2554037,EBI-10969852; Score: 0.35
DE  Interaction: Q9HCN8; IntAct: EBI-2554037,EBI-2339921; Score: 0.35
DE  Interaction: Q9H5Q4; IntAct: EBI-2554037,EBI-1043912; Score: 0.35
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAGGPCVRSSRELWTILLGRSALRELNQIEAELNKYWQRLLEGLSYYKPPSPSSAERVKANKDVASPLKELGLRVSK
SQ  FLGLDEEQSVQLLQCYLQEDYRGTRDSLKTVLQDERQSQALTLKIADYYYEERTCILRCVLHLLTYFQDERHPYRAEYAD
SQ  CVDKLEKELVLKYRQQFEELYRTEAPTWETHGNLMTERQVSRWLVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFK
SQ  EQGFGSRQTSRHLVGGTMDPFVDRIGYFSALILVEGMDIESLHKYALDDRRELHQFAQDGLICQDMDRAMLTLGDIPHHA
SQ  PVLLAWALLRHTLSPEETSSVVRKIGGTAIQLNVFQYLTRLLRSLASGGNDCTTSTACMCVYGLLSFALTSLELHTLGNQ
SQ  QDVIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELHKH
SQ  KPHDVLSHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQ
SQ  HCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVNVIASCVNCLTVLAARNPAKVWTDLRHTGFLP
SQ  FVAHPVSNMTQMISAEGMNAGGYGSLLMNSEQPQGEYGVTIAFLRLVTTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHK
SQ  WRYNSHGVRELIGCLILELIHAILNLCQETELHSSHTPSLPSLCICSLAYTEAGQTVISIMGIGVDTIDMVMAAQPRSDG
SQ  PEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALTQHGAHGNNLIAVLAKYIYHRHDPALPRLAIQLLKRLAT
SQ  VAPMSVYACLGSDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSNGSKEFSLGVWSCLH
SQ  VVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSVLETCALIM
SQ  KIICLEIYYVVKGSLDQSLKDTLKKFSSEKRFAYWSGYVKSLAVYMADTEGSSCTSLLEYQMLVSAWRILLIIAASHADV
SQ  MHLTDMAVRRQLFLDVLDGTKALLLVAASVNCLRLGSMMCTLLLILLRQWKRELGAVEKILGPLTEILEGVLQADQQLME
SQ  KTKAKVFSAFITVLQMKELRVGDIPQYSQLVLNVCETLQEEVIALFDQTRHSLASDSAAEDKDSMETDDCPRPRHKDQRD
SQ  GVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEAALHLLLTLARTQQGATAVAGAGITQ
SQ  SICLPLLSVYQLSSNGTGQTPSTSRKSLDAPSWPGVYRLSMSLMERLLKTLRYNFLTEALDFVGVHQERTLQCLNAVKTV
SQ  QSLACLEEADHTVGFILQLSHFRKEWHFHLPQLMRDVQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVTPRAQR
SQ  PSTTTTTTTTTTALATPAGCSSKQPTADTEASEQRALHTVQYGLLKILSRTLAALRHFTPDVCQILLDQSLDLAEYNFLF
SQ  ALSFTTPTFDSEVAPSFGTLLATVNVALNMLGELDKKKESLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAVRYL
SQ  RDPAVHPRDKQRMKQELSSELSTLLSSLSRYFRRGAPSSPAAGVLPSPQGKATSLSKASPESQEPLIQLVQAFVRHVQR
//
ID  Q296J9;
PN  Nurim homolog;
GN  nrm;
OS  46245;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q296J9;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATFAKVMLLLSSVATFGYTFFVVGKLMLFLSTPRSISKAHTWIFNLLDNKSRLETAYGPIVFDTLYLIGFIFQHSFLKS
SQ  ALVKNLWRKLGLAAAERTIYSLTSSICLHYLLKNWLPAQSIVLWQVDVDESAPLWWTFVVTHGLGWAVIFGGSLIMDLPE
SQ  LLGVKQVYYDLKEYGEPVAYKSSELRNLYSHVRHPSFVGLSVILFATNVMSLDRLLLASLLTVYMYVAWSTDDKDVAYQK
SQ  QQLRNKKHELKAQ
//
ID  Q64GA5;
PN  Cytosolic phospholipase A2 gamma;
GN  Pla2g4c;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:15950603}. Nucleus envelope {ECO:0000269|PubMed:15950603}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15950603}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15950603}. Note=In germinal vesicle stage oocytes and early embryos, shows mainly uniform nuclear and cortical expression. During germinal vesicle breakdown, found in intensely stained foci which accumulate near the dissolving nuclear envelope. Also localizes to spindle poles at metaphase II. {ECO:0000269|PubMed:15950603}.
DR  UNIPROT: Q64GA5;
DR  UNIPROT: Q08EC7;
DR  UNIPROT: Q3UWS1;
DR  UNIPROT: Q7TN01;
DR  Pfam: PF01735;
DR  PROSITE: PS51210;
DE  Function: Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. {ECO:0000250|UniProtKB:Q9UP65}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:0004623;
GO  GO:0102567;
GO  GO:0102568;
GO  GO:0046475;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELSSGVCPATRLQEAEKAAVHKRSPKVLEALRKLNIQADQAPVIAVLGSGGGLRAHIACLGVLSELKELGLLDAVTYLA
SQ  GVSGSTWALSSLYTKNGNMEGIEEELKHRYEKNEWDFHESLEKAIQASKRENYSLTDFWAYLIVSRQIRELQDSNLSSLK
SQ  KQVEEGVLPYPIFAAIDEDLLADWRERKTQNSWFEFTPHHAGYPALGAYVPITEFGSRFENGKLVKSEPERDLTFLRGLW
SQ  GSAFADIKEIKNYILNYFRNPFGKLKFIEGPVTYSEAPRMNVDAMLLDLVMAYFTDMNDPSIKDKLCALQQALGTETDEF
SQ  GIEMAEIIQNWNETSAEKKEQFLDHLLDRFKKTQEDTTTYSLMNWNTGLVWDRCVFVNETRKCVSKWQWGTVYNFLYKHG
SQ  KIADETMCSRELLHLVDAGFAINTPYPLVLPPVRETHLILSFDFSAGDPLETIRATADYCQRHEIPFPEVSEDQLKEWAK
SQ  APASCYVLRGETGPVVMHFTLFNKDNCGDDIETWRKKYGTVKLSDSYTPDLVRDLLRVSKENVKKNKINILSEMRKVAGN
SQ  PGNIPRVNKEACLGDRVKDPQGSQTVEFKKSHNISKD
//
ID  Q59WU8;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q59WU8;
DR  UNIPROT: A0A1D8PPH8;
DR  UNIPROT: A0A1D8PPH9;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYP
SQ  SECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNEL
SQ  KAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILIN
SQ  EKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEK
SQ  NEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSI
SQ  FNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMK
SQ  VVDID
//
ID  Q55BX5;
PN  Nuclear pore complex protein nup54;
GN  nup54;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}.
DR  UNIPROT: Q55BX5;
DR  Pfam: PF13634;
DR  Pfam: PF13874;
DE  Function: Probable component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}.
DE  Reference Proteome: Yes;
GO  GO:0044613;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0036228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLFGNTTTGGGGLFGNTTTPTQTTGGGLFGNTTTGGGLFGNTATPTTGGGGLFGNTATPTLTTGGGGGLFGNTTAPTTG
SQ  GGGLFGNTPTQTTGGGLFGNTATGGGGLFGNTQQQQQQQQQQQQQQQQQQQQQPSTSLFSQSSLGSQSSLGSQSSLGSQS
SQ  SLGSQSSLGSFGQTQQPQTSSLFGNLQQQQQLQQPQRSIIEQKLYDFMQSISPNSLNCRFLYWFYNYQANGQLVDPNSIP
SQ  KPPNVTVDQWAYALSNNPDPSILIPVAAKSFDDLINRRMKQEETIIALDQNTQEALKRMRDLENHLNFHIHTQLEMMRKK
SQ  QIELIQRYIEVWSNLEIYQSKGKTFTTSEERIMKKIYELFEEINQPNSIKSKVEEISNQLKLGSMEKEKIKYEISPEAVE
SQ  PLYNLLKNMTISIERITNELEIAVKDAQILKNELYQLKKC
//
ID  Q9VBU8;
PN  Nucleoporin Nup37;
GN  Nup37;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH4}.
DR  UNIPROT: Q9VBU8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: As part of the nuclear pore complex (NPC), has a role in its assembly and function. {ECO:0000250|UniProtKB:Q8NFH4}. (Microbial infection) Required for optimal replication of E.chaffeensis. {ECO:0000269|PubMed:22851751}.
DE  Reference Proteome: Yes;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRSVIEPDHSIQLNEAIYCYDICTNDFAYNLIAVAFRKHLSLLLVGLPEESGEFGYTRLQDMDLGEKEQRSVSALAFSPD
SQ  TSLNCTPNNVTLCAANGSQLKLYRTDLGQFTSLQVLRGHGDYVNDVSWVCDGELLASVSDDFTCRFWTTTGGGENVITFG
SQ  LSSAGMSVKSHPEDPNKVLVAEKKGIIHLYNVTLKQTVISVESPKFPLMSADWAHSNRLFITSLAGGDVVTWDLNRPYVP
SQ  ADVKQVHEDCGRVVRFAPGSSEMVIAMVIGLTLKVFAAKSTVPLLEASLKSYGGMAWHQRLPYISAVSDRKLLFWKVQMK
//
ID  O94353;
PN  Nuclear membrane organization protein apq12;
GN  apq12;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94353;
DR  Pfam: PF12716;
DE  Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0044255;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNK
SQ  TTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF
//
ID  B1A8Z2;
PN  Calcium and integrin-binding protein 1;
GN  CIB1;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid- anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
DR  UNIPROT: B1A8Z2;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0032433;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0005815;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0005509;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0007229;
GO  GO:0007283;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTS
SQ  PSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  P28971;
PN  Protein UL20 homolog;
GN  41;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P28971;
DR  UNIPROT: Q6S6T0;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:16352534}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPQVLMGNTRLHAPLEDGIPLIENDENSSQNEVDLYDYVSMSSYGGDNDFLISSAGGNITPENRPSFSAHVVLFAISALV
SQ  IKPVCCFIFLNHYVITGSYDFAVAGGVCTVLYYMRLALTAWFMFRNIQSDMLPLNVWQQFVIGCMALGRTVAFMVVSYTT
SQ  LFIRSELFFSMLAPNAGREYITPIIAHKLMPLISVRSAVCLVIISTAVYAADAICDTIGFTLPRMWMCILMRSSSVKRS
//
ID  G0S4T0;
PN  Nucleoporin NUP192;
GN  NUP192;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P47054}. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution). {ECO:0000250|UniProtKB:P47054}.
DR  UNIPROT: G0S4T0;
DR  UNIPROT: G0ZGU6;
DR  PDB: 4KNH;
DR  PDB: 5CWV;
DR  PDB: 5HB4;
DR  Pfam: PF11894;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs. {ECO:0000250|UniProtKB:P47054}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-4325187,; Score: 0.73
DE  Interaction: G0S156; IntAct: EBI-4325187,; Score: 0.68
DE  Interaction: G0SFH5; IntAct: EBI-4325194,EBI-4325187; Score: 0.35
DE  Interaction: G0S7B6; IntAct: EBI-4325187,; Score: 0.53
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDLRKLEALQALHAELVAVRQHRFEGLQVLETLLEEQTDAFKALIAKPARDTKDREALGKEPKKLKIGEEEYSLNEDFV
SQ  NDCLKLADELDLNEKESARILIDCDAEGDVETQSRPLWECGVIRFHQERKYLLDCMRLILEIAADEDIDAGLQESFGVAA
SQ  EDKIFGIPPPWERNKENQPTQVKKFIPRCMEAMKGVRSMLQCMADKANARNMLQQASLVRPLDNQETLDFSRLSLVEQHE
SQ  CLASILHAAVQRHHATIADFQDFIKILRKWDKYDHFLIHLIPVLAAYITEFGSPEGMGDLQQARRLNDFICKGGDEDSWA
SQ  LPVLGAAVRAWWIAEHNGFYLDDTVQDLRGINLDEEDEQRTKQFLDALKEGAFDFILSVAADCKAQEWQDPSQLGARQWL
SQ  QRKIPSLPSEPFPFSHFLQHSLMVHLEGFVDATISNLPDVLRKLRTEEDEQRQLRPNHEQDMDLERFLIIISYAYEGRPD
SQ  AAMSFWEDPDSNLAGFLQWASRRASTPLVSAFCEMLRCLADNEECATAAHNFLLDEGHQASGKMKRSQSLTWSQIFKELE
SQ  YFTTKVCSERPNPPQASMHRPGRPGADPAEIEPESALMLECYLRLIAKLATESEIARKRLIMDEDFNLVDTILKLSVGVI
SQ  PHRLRACIFYVLKALMIRKTHEELDAMWRWVEAWMTNPFSSLPGSQGAPQRISFLGQTPGPQECMEMMFREFGTGFEQSN
SQ  AFIQLLTTLLVPPEGLNSLNDSVPFPEWLGSSIRTLGIEPYVDFVFDVFANRTKDISDPSQLRILRLSCLDFVMVCLVTF
SQ  NEDLIVLGHESNISIDDAMAATNLATYVRLHPFSRVMEWLFNEKVITSLINTIHQDPISLGSASPDSPLVVSILRAIQVM
SQ  IKALELQETYLHLVRPEVLRYQGEAGVRRKPVANAAYSAFEDGILSHLSLVVDLGKYCNLGHAELTLACLKLLEKISTSS
SQ  RILSAWSPDSGRLGHRNKAIVQLERNGEGETISASLSASIMATLDPALAASGENYRVKLAILDFLYACLRATPDQPTIAH
SQ  QLLGFHCELSKLGIEPKGPFDMQKSLFHSLLNVLITLTVSEEEQGMRGYLVTLKYRVLRILQLLWKSPLSASLVMDELRA
SQ  TNFLFHMLLREVQIQPQLPWDGQLVTGCEFLLSDASLAYIDYLASRAAIFEYIGKELCSVSQNRIPSIKRQIFDALNGQI
SQ  FVDEEAPLTIPSIFDFFDFINTDYKWEEIPSPHFTYLKDLDLGPCILEHKYAGVHYDIRKAQEILALKRKEYEHSQLATP
SQ  EFLETVELEEKVLIEWLTVRNRANLLLTARLNLLQAWANLLLVMIESNDFKSTPKMAFLLQALQAILPTLEAFSSLKSDE
SQ  AFELARVAKVLLWKLDFSQDSDAGLDREQFTVGNLIGDKLFQLFQLCLSAISQCSGTPELRSLYYSICYRYLTAVVDNDA
SQ  TVAATPASSTIGPTRSVTNARARTLKAITLYGDRLLNVICDDAYGSDTTCQTAAMILLNALVHTSRASSAAGVSPADVDC
SQ  PIIDALNRLNFIGVLVDSLKEILNEWLAPSSTFDPSLSTNASPSLPIPASPSQQYTSAKLALLLQLCQTRQGAKYVLQAN
SQ  LFRALEQSGVFAADPELVEVDSESGVPRVVALERHYALLVALARVVGAAVTARGAHNIVQGRKFLTQHRGLVVHVLKKNA
SQ  GIGGGVVGNSLASSINGGSTATMTRRDEILAQQALEERIEELAEAFMLLITATGFLEYESEQVPSEQPRAHTTFFH
//
ID  Q9EP64;
PN  Tenomodulin;
GN  Tnmd;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q9EP64;
DR  UNIPROT: Q8CET4;
DR  Pfam: PF04089;
DR  PROSITE: PS50869;
DE  Function: May be an angiogenesis inhibitor.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071773;
GO  GO:0001886;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0030948;
GO  GO:0035990;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKNPPENCEGCHILNAEALKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYDMEHTFYSNGEKKKIYME
SQ  IDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAE
SQ  KPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRHTRQASE
SQ  EDLPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
//
ID  O77507;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: O77507;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. {ECO:0000250|UniProtKB:Q06609}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0003690;
GO  GO:0000150;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0006974;
GO  GO:0071479;
GO  GO:0000730;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0036297;
GO  GO:1990426;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPVSRLEQCGINANDVKKLEEAGFHTEEAVAYAPKKELINIKGISEAKADKILTEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVTVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  Q00702;
PN  Protein UL20;
GN  UL20;
OS  10349;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q00702;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:10799582, ECO:0000269|PubMed:9188641}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEDAAADVDAAADAKLTGENDALLSSAFVGARPPRPRFSSHVVSLLALALALRPACCLVLALHGSRATLAALLTALAFYA
SQ  RAAVCAVLVARNVARDRMPLSPAQQAALGLLAAARLAFLYVALDAGRHYAPALAGALYGADCVCDALAFLLPRAYARSIM
SQ  H
//
ID  Q6GNM0;
PN  Nurim;
GN  nrm;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6GNM0;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSANVQVSGQLSSGPSLPACIVLSAVSLLCFVAGFGTGAEFVRFLSFGAIFRNISGGLDGEIPLTWSEAIRNTQFQCCIG
SQ  IDIGLLFLFVLQHSLMAWTAVKKNVLHVFGVLQRSIYILCTALSLQVLMRFWQPCPHGPYLWNVSSDPWSAWLPLLCALV
SQ  HTISWLLIFSVLLIFDYAELMGIKQVYYFCLGMGDPLSHKSPRVARLYAHLRHPIYLELLLILWAVPCLPPDRLILAIFF
SQ  TLYLSLVHRLDVQDYAYLRSQLEKKFLLFSREEASAVGGQIRKNN
//
ID  P59235;
PN  Nucleoporin Nup43;
GN  Nup43;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: P59235;
DR  UNIPROT: E9QPN3;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-912574,EBI-8460031; Score: 0.35
DE  Interaction: P61021; IntAct: EBI-8320093,EBI-8460031; Score: 0.35
GO  GO:0000777;
GO  GO:0031080;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEIYAKFVSQKISKTRWRPVPSGSLQTTETFATGSWDNEENCVSLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDL
SQ  QFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWPAAHYHTGPSSPSYSSAPCTGIVCDNPEIVTVGEDGRINLFRVDH
SQ  KEAVRTIDNADSSTLHAVTFLRTPEIVTVNSIGQLKIWDFRQQGSEPCQILSLTGDRVPLHCVDRHPDQQHVVATGGQDG
SQ  MLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPDHLFTCSEDGSLWHWDASTDAPEKSSLFHQGGRSSTFLSHSLSNQA
SQ  GVHQSLVSSWLSTDPAKDRIEITSLLPSRTLSVNSLDVLGPCLVCGTDAEAIYVTRQLFS
//
ID  Q9C500;
PN  WPP domain-containing protein 2;
GN  WPP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:15548735}. Cytoplasm {ECO:0000269|PubMed:15548735}. Nucleus {ECO:0000269|PubMed:15548735}. Golgi apparatus {ECO:0000250}. Note=Associated to the nuclear envelope (NE) in undifferentiated cells of the root tip. Associated with the outer NE and the nuclear pores in interphase cells and with the immature cell plate during cytokinesis. In differentiated cells, localized in both cytoplasm and nucleus. Accumulate in speckles of the cytoplasm belonging to the Golgi apparatus (By similarity). Appears at the NE as cells reenter the cell cycle during dedifferentiation. {ECO:0000250}.
DR  UNIPROT: Q9C500;
DR  UNIPROT: Q8LE13;
DR  Pfam: PF13943;
DE  Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting. {ECO:0000269|PubMed:15548735, ECO:0000269|PubMed:19617588}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779367,EBI-1779618; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1779618,EBI-1796628; Score: 0.35
DE  Interaction: Q94AV5; IntAct: EBI-1779618,EBI-1779487; Score: 0.37
DE  Interaction: A8MQR0; IntAct: EBI-1779618,EBI-1796632; Score: 0.35
DE  Interaction: Q9FH18; IntAct: EBI-1779466,EBI-1779618; Score: 0.37
DE  Interaction: Q8L4Q6; IntAct: EBI-1779618,EBI-4448402; Score: 0.37
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0048527;
GO  GO:0000278;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETAETINTTISSPPPESESSTTISAMTDPTSQEAASKDTDLTKEAESEKKPGGISLRIWPPTQKTRDAVLNRLIETLS
SQ  TESILSKRYGTLKSDDATTVAKLIEEEAYGVASNAVSSDDDGIKILELYSKEISKRMLESVKARSNASVGNGSVEDANTD
SQ  ASEVSKDDAGPASEEEKSEA
//
ID  Q9UTH0;
PN  Nucleoporin nup132;
GN  nup132;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15226438, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UTH0;
DR  UNIPROT: Q9UU23;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10331; IntAct: EBI-295788,EBI-295780; Score: 0.57
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0031081;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0090234;
GO  GO:0006355;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSILGKRKNEEVVSFSPLKRISVEKSLLDSTAYNNSLDWLRSKNFKVSCLLKHFNSKIINDHPLSGSCYTDIGYALINS
SQ  RKACFILSYRQSLGTAEPPTITFPLPEEDSNGFSGQNALTAFVPSDASDKEPGLLIVMPISGRIAYWTSIGNALAQSYIC
SQ  PQGMESLIKLLPKEKCEHLCCSNPMKFIISTNFGRLFSVQLRDPAGQPDVSVQLFASDISTFSTILQKMKIFNYPSIHII
SQ  ALKSPPLFSPYQHLLYVAEASGLLEIYDLKLENKLVSGMNLSPIFKQVLREGCPDASGLEVLDLTICPTNGNLVSFLVCW
SQ  KNSINYRYMIISLDFSDISSPSVMNIHPLYSFSSKSLESSKLHYSSSGNSLFVVLTDAVIIVHVQEDDKDIVSRTSWEEV
SQ  IRMNTNVSGGIFMSTCYKYVLGKYSIPTESCFIATPYSGIAEIEVHSLEHPANNESLVKSKLEEAVFYSFLPGNPIDFSC
SQ  NYLRSIKKPELERIIVDLGMDILNSRSTHLPPLFASLMQHLSCRLNSLNNLVRYIRSMSLDVDRQVLYKLRVMGEKCNSV
SQ  RYLWNTIDTEFSTVSHSLIFQRIIYRLTQSASSDNALREWFLHNIESIDQLIAQAHEFCIDSGSRVQELPLEVLDVIMEA
SQ  NEVILAIQSSALAYRRESQKIYKLSIDTFGEEVPWTSTPETLVLLCRQFELTRSALVQSHQGTSDVENTFKIKDKGVLRN
SQ  VVSNLEVQLVALTEVCFDAYSERIRWIEQRCGKDASEIQDVKEAFAVNRRFWVQTLSDIGKGSSAIRIAEKYSDYRSLVE
SQ  LCYQLYEDNELTDALNNYLDLFGIKFAFILYDYFVENGMALELLNSDRFNKSYLKQFFKSRDYNQISWMHDMRLGDYDAA
SQ  SHRLLQLATKQEKLVDKKESELSLSKLFLYAVPSNSGNIRDLVLVEQKLEQLHIQKMVSKSVMPVVERLRSQGKKYQLVE
SQ  AVVDDLIGAKVAPVIARQVMQRVVKKFIAGQVVEATELLEYLSFSLYRREDLVEGEVTDYYLALRLLLTTRLTDDAKRFY
SQ  ENTIWRRAVLHDNWIQVLDTQGKNDAIIETQFRMSALYRTLEAVTINGLFHEGLIRPGSLSSCKFEGYDPQNLISIYPPA
SQ  RFGDVTEVTKVLNRESVKLDHYLTKTNLNTCYISMCLSCDTI
//
ID  Q9TXH9;
PN  UBX domain-containing protein 1;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes. {ECO:0000269|PubMed:20977550}.
DR  UNIPROT: Q9TXH9;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DR  PROSITE: PS00028;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. {ECO:0000269|PubMed:20977550}.
DE  Reference Proteome: Yes;
DE  Interaction: P54811; IntAct: EBI-320245,EBI-320236; Score: 0.62
DE  Interaction: Q19019; IntAct: EBI-320236,EBI-315356; Score: 0.37
DE  Interaction: P34327; IntAct: EBI-320255,EBI-320236; Score: 0.37
DE  Interaction: Q18157; IntAct: EBI-320259,EBI-320236; Score: 0.37
DE  Interaction: Q18426; IntAct: EBI-316187,EBI-320236; Score: 0.37
DE  Interaction: Q18938; IntAct: EBI-318532,EBI-320236; Score: 0.37
DE  Interaction: O45521; IntAct: EBI-313236,EBI-320236; Score: 0.37
DE  Interaction: P54812; IntAct: EBI-320265,EBI-320236; Score: 0.37
DE  Interaction: Q9XUT0; IntAct: EBI-320276,EBI-320236; Score: 0.37
DE  Interaction: P45972; IntAct: EBI-319208,EBI-320236; Score: 0.37
DE  Interaction: Q23182; IntAct: EBI-320284,EBI-320236; Score: 0.37
DE  Interaction: Q7YTU4; IntAct: EBI-320288,EBI-320236; Score: 0.37
GO  GO:0048471;
GO  GO:0036435;
GO  GO:0003676;
GO  GO:0030154;
GO  GO:0042006;
GO  GO:1903364;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSIAQQLMDMGFPADKAEAAAGNNRNLDQALDWIEKDGAGVPMETDAPAQAAPGAADSGAPPVAASFKCDDCGKLLANDD
SQ  AIMFHASKTKHENFSESSEAIKPLTAEEKAAKVLEIREKIKVHQAKKAKLEAEENREKEKKRREDGKAMISHKEAARDRE
SQ  IREAAQDRRREKNEDEIARKRVLEQIRLDKEARKAKASGQPVPEAKPAPSAAPVAPPKDYSTTTLQFRLLDGQTVRQQFE
SQ  ANEPLAMVRAWVETNHANGVPFTLMTPFPRKVFTEDDMGTPLKVLNLVPSANVILNRAA
//
ID  Q5RBP6;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q5RBP6;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0072606;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGVKAAQTGIWASQGQSIRVVGFQAQTAHRAICLLGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDAIDRFLCTH
SQ  IIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSNIASNTQSRRTFIKSVPPFLRTHGFD
SQ  GLDLAWLYPGQRDKQHFTTLIKEMRAEFIKEAQPGKKQLLLSAAVSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWR
SQ  GTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLEAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGT
SQ  LAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKERQLAGAMVWALDLDDFQGSFCGQDLRFPLT
SQ  NAIKDALAAT
//
ID  O54940;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2;
GN  Bnip2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}.
DR  UNIPROT: O54940;
DR  UNIPROT: Q8K4H0;
DR  Pfam: PF12496;
DR  Pfam: PF13716;
DR  PROSITE: PS50191;
DE  Function: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0031616;
GO  GO:0004309;
GO  GO:0006915;
GO  GO:0001824;
GO  GO:0007098;
GO  GO:0006798;
GO  GO:0043410;
GO  GO:0045666;
GO  GO:0051057;
GO  GO:0090649;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEV
SQ  DLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYY
SQ  GDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKN
SQ  LKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQE
SQ  PPKSEQ
//
ID  Q62825;
PN  Exocyst complex component 3;
GN  Exoc3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection, neuron projection {ECO:0000269|PubMed:12954101}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}. Note=Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (PubMed:12954101). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (By similarity). {ECO:0000250|UniProtKB:O60645, ECO:0000269|PubMed:12954101}.
DR  UNIPROT: Q62825;
DR  UNIPROT: Q4QQU2;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
DE  Reference Proteome: Yes;
DE  Interaction: P07949; IntAct: EBI-2480756,EBI-15885246; Score: 0.35
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0042734;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCKDSACFSTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALN
SQ  DVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLEC
SQ  SRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRK
SQ  KQTGFVPPGRPKNWKEKMFAVLDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLVIAKNLLVQCFPPHYDIFKN
SQ  LLSMYHQALSIRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVNALEPLLSPNVVSELLDTYMSTLTSN
SQ  IIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQ
SQ  LYKEEHLRNRQHPHCYVQYMVAIINNCQTFKESIISLKRKYLKPETEESLCQSQPSMDGILDAIAKEGCSSLLEEVFLDL
SQ  EQHLNELMTKKWMLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKM
SQ  VREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQT
SQ  IMETLEQGPMQASPNYVPIFQEIVVPSLNVAKLLK
//
ID  O14089;
PN  Importin subunit beta-2;
GN  kap104;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14089;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:P38217}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:1990023;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVS
SQ  SLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICE
SQ  DSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVC
SQ  QALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLL
SQ  LLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAAL
SQ  DVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLG
SQ  RYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVL
SQ  ILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNT
SQ  LYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYC
SQ  FDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIG
SQ  RLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKI
SQ  LQGSVELFNGKASWQASPEVLAQIQAQYGV
//
ID  Q3T005;
PN  PDZ and LIM domain protein 4;
GN  PDLIM4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DR  UNIPROT: Q3T005;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DE  Reference Proteome: Yes;
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051393;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0042803;
GO  GO:0019903;
GO  GO:0030036;
GO  GO:0031532;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0061061;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36202};
SQ  MPHSVTLRGPSPWGFRLVGGRDFSVPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCRDHLTLSV
SQ  SRPEGRSWPSTPEDNKAQAHRIHIDSEAQDGSPLTSRRPSATGLGPEDGRPGLGSPYGQSPRLPVPHNGSNSEATLLAQM
SQ  GALHVSPPHSTDPARGLPRSRDCGVDLGSEVYRMLREPAEPAAAEPKQSGSFRYLQGMLEAGEGGERPGPGGPRNLKPTA
SQ  SKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVV
SQ  AVYPNAKVELV
//
ID  Q8GWR1;
PN  Aladin;
GN  AAAS;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8GWR1;
DR  UNIPROT: Q9LER8;
DR  Pfam: PF00400;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q8GWK2; IntAct: EBI-25521547,EBI-4425567; Score: 0.56
DE  Interaction: Q9LXJ0; IntAct: EBI-2430270,EBI-4425567; Score: 0.37
DE  Interaction: Q9SJH7; IntAct: EBI-4429038,EBI-4425567; Score: 0.37
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASFPHPGSVTVCEINRDLITAQNLSDERAQETYGKVLGMVFSPVSFDSTPSSLQENEGQENGDKASGESKGLVATLQMK
SQ  VADSLKQILQPTDVTLLSEIDLQGVSWHQGKHIIAFISGANQVTIRDYEDKDEKEPCILTSDSQRNVKALEWRPNGGKSL
SQ  SIACRGGICIWAASYPGNMALVRSGGSALRGSLSRGSGTRWILVDFLRCQNDEQISALSWSPCGRYLASASYDSSSFTIW
SQ  DVSQGAGTPIRRGLGGISMLKWSPTGDYFFAARFDGTFCLWETNTWTSEPWSLSSGSGSVTGAIWDPEGRFILISFSKSS
SQ  TLGSVHFSSKPPSLDAHLLPVELPEIASLTGCEGIEKIAWDASGERLAVSYKGGDENYKGLIAIYDTRRTPIVSASLVGF
SQ  IRGPGENPKALSFSFHDKFKQGPLLSVCWSTGFCCTYPLIFRSHVLP
//
ID  O35646;
PN  Calpain-6;
GN  Capn6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}.
DR  UNIPROT: O35646;
DR  UNIPROT: Q3UM55;
DR  Pfam: PF00168;
DR  Pfam: PF01067;
DR  Pfam: PF00648;
DR  PROSITE: PS50004;
DR  PROSITE: PS50203;
DE  Function: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues. {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0008017;
GO  GO:0001578;
GO  GO:0006508;
GO  GO:0051493;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGN
SQ  KAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWN
SQ  ALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQ
SQ  EVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDD
SQ  GEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIM
SQ  SLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTS
SQ  EFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVH
SQ  AIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTE
SQ  L
//
ID  P0DPR2;
PN  E3 ubiquitin-protein ligase RNF43;
GN  rnf43;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q68DV7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q68DV7}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Nucleus envelope {ECO:0000250|UniProtKB:Q68DV7}.
DR  UNIPROT: P0DPR2;
DR  Pfam: PF13639;
DR  Pfam: PF18212;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (By similarity). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (PubMed:29769720). {ECO:0000250|UniProtKB:Q68DV7, ECO:0000269|PubMed:29769720}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0016740;
GO  GO:0007275;
GO  GO:0016567;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFH
SQ  PLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWG
SQ  PDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRR
SQ  YQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPR
SQ  PLAHRAPSQTQLWGRYPGSARLMSHLPPHGTPMVFPTPNNSLFLPRAPYYLDHTHHWQMPEQMAMQMRTHRRGAEGTREL
SQ  GISPGCQDSSGYLPDDPGSDSSSGPCHGSSSENCTDISLHCLHGTSSSSVHSSQSNQEDSSPPALASYLLPQGELPALNP
SQ  LLSTQASYASHVHFHQHRHHHYRRNQPSMSHSHPHRSKRRTKVSRADPSYYREHRHTTGANGELRSLMVRREPRPSCSRT
SQ  CFDPRTNREHPRHQQSMPQAASVVQGSSEPDVATSLRGSRTDPPSRTYRKKKSSAPSHLPLLYSPRHCHPANSVQMSESS
SQ  HPRWAEEVRLLHSRVNSHRENTAMMHLYHPPHHNQGATEEIEAVCEHAV
//
ID  O13818;
PN  Uncharacterized PH domain-containing protein C19A8.02;
GN  SPAC19A8;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10759889}.
DR  UNIPROT: O13818;
DR  UNIPROT: Q9USA8;
DR  Pfam: PF00169;
DR  Pfam: PF16016;
DR  PROSITE: PS50003;
DR  PROSITE: PS51778;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005816;
GO  GO:0016538;
GO  GO:0061817;
GO  GO:0045737;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAPANASSKKDHVIPVLLNECSIDSPSFRASMYYLGNQIKAFNEWSHDFLCCCNKFIESIMAIEPIVASMSLNAMPSNV
SQ  ASGFFDPDYATTALLHGQDLFRSSYMVQLQQAKNLRKFIVAPLDLFRDSKVKPLLQLNDRFKAEQAKYDAEVLRYSSLGH
SQ  SKDLSQMRDEAKSLYEARKSYFTVALQYVVRVTSFRSSIDFIVIESICKFSIETFRLTDRLHESNRHINDQLIRLLSYET
SQ  KLKESYPSLKRIVSNVFDRIEKEILKRVQPPTNLDAYRFDPQQICQTNATKRQGWLLRNISSSKADNKAIWRKYWFFVDN
SQ  GYVGYLINDANGGVFESEKIGVLLCKFSVLPSNHRKFCFQIKTKSVSYILQAETHMEMLEWGSVINNAREHCINSGISAN
SQ  RILSPTLPSFSAKATSIINPQVNGRSNSTGKIGKNYRPRRTYSGRLLCGPNNYEVSTIMRSPTISTVPPPKYLSNSINGA
SQ  KFLNPLAPWTLVNAPLITNLTHETITSLLDQEAFFHGNSPCALLANFWGSVNYGHVLERQNVYIEDLSNPSYKRLAREIH
SQ  IEKLPSELKLRNAEFRGIFGESEASTVLFVCRVCSKREDQIRMPGRMYCTMKGIYIYYNINGLVLIEHFPISSILNVKQF
SQ  ASTKCDYFYMNIQNIGTVRFRLYLDSSKALTDRLNVLLCNYIADKPNSSIQLLSCIKRLNDDVKRFERGGDDNALKSYGV
SQ  QPSQEDLLIRRGRSSRALTNLINKNESNDSFMEDLRDFKIAMLPKETVQVVRSHHLDDIVFDRVYNVSTKALFHIVFGDR
SQ  STVLSGAYNLHGVDDVEFLPWGKDPKTNLSRRYINYKVYNYDQEGQCQSYHYEDCQIMDVRNDYHLYIMTWLHHSWTLPY
SQ  RDYFKIVTKTSISHLRREKSRLLISVGLEWIVKPFAISKVIEAECRKLAIKYIKTEVNFLEKATRRARNQPLIAIINQYG
SQ  RVGDYNESMVYRRKIPFNCELKNLSIIDIIRNNWWLFLQGLAIDLLKLPWAVFHIFLRYLFSHSFLVIIFACSVILNLSL
SQ  MFCFGAKYWDERQNNKFVGQVFDEFKNIETSARYVYMKDVDDLLVGLPTYLHPNVTYPSECLQSFALKSSPQKSHWLRKR
SQ  NYIAEKRKKILENLASLNYYEYIIHEDAVYQYIQQELLGCDKAREFDLYPPSMQRYCDSCTQDWRNRTLFFGKDTLATRL
SQ  LTLETVENADYAA
//
ID  Q6FU40;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6FU40;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVG
SQ  LSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVS
SQ  ETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKK
SQ  TIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKL
SQ  PTLEQQYLGNFAQALSNIDKQVLSASLQWQYDYDVVFANLYAALDLLNSNLNSSVKKIEQIEHVIDTIIVDTSFLNDQLA
SQ  NLILIPSTILRAFSFIGVKRVIIAIIVLYFKSTLLCLVHYGQSFRIAALLMSATAGIFCSKLLMSYIYN
//
ID  A5DJU3;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  294746;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A5DJU3;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKKILRLVFILVYTNISTFVSAHELEDAASFTADELDRLLEDPPGCIQLAMRPIFEKCVLNGIHAVDPKDRRSSAIEMSV
SQ  CEFESAGVEYPAECSTTDYDTCIWKLGLVPQYWTTFSGNYRDIGLFCEGVSRNNEKEQLVLLYSNITKVFAGFRHAFYES
SQ  YSKSQEMKDEMEEGFSRWSADFDIAKDQHKEFYEFVAKQQEHIKIELMKNQKVIFDFHDEQEVRFNSYSNHIVDVIDSMA
SQ  VDLDIILAKLADDGIIEDMENQKSKSLDIMKSYSEDAELTLSRIVSELERVGIIQKNDVSIVENLNSGLADTSNKVSKLN
SQ  KDFEDLDSHFQHTKDLIESEVSFLFANLIGEMETKLSQALENVDDRIELHFVSQLEFLDKSLNETWEAILTFKQDWQIFT
SQ  SIFENFENIPKSISHFVTSGLYKTNEILTQTSYFWSTILNIPVSLLSNILRYTMAASWIAILFILISLRYGSTKSFLLVI
SQ  MVLLVVFLNTHRW
//
ID  Q9US10;
PN  Uncharacterized membrane protein C6F6.13c;
GN  SPAC607;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9US10;
DR  Pfam: PF05277;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0016298;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEQKIISLFDDDACTRYTILIASTIGEMREKKESIIDNTDPEIVKYLSQLLDVFRENFDTWAMAVVNRTGCALDPSTPK
SQ  DQVEVKKFRQFSETEKSECFIKCLLLLILSLGNYSPYSRNLLYSIAEKLGLSSIVVYKAELITSSMLLDTFQTMESNQEM
SQ  YELSGTRKMRRRIAMGLAGLAGGALIGLTGGLAAPFVAAGLGTLFAGLGLGTMIGATYLGTLITSAPMITALFGGFGAKM
SQ  SMQQMGDVSKGLTDFEFIPLSVQSHLPVTIGISGWLGDYNEVDAAWKSLTVGDKSYYWGDIYALKFEVEALVDLGKSLSR
SQ  ILFSAGLGWVKGEVISRTILAPLAAALWPLSLLKVGNILGNSWRIAFNLSIKAGEALANALCVRAQGMRPVTLIGFSLGA
SQ  RTILECLLHLADRGETNLVENVIVMGAPMPTDAKLWLKMRCVVAGRFVNVYSASDYVLQLVYRVNSAQSTAAGLGPVSLD
SQ  SNTLENVDVGDLVEGHLQYRWLVAKILKERLGYDNISDAEIQSLAVQEEKYESKQRTYYSQKEQEEEIEQEVLFDASSDT
SQ  ELAIQKKEDEVNEVRENKK
//
ID  Q6CIJ3;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6CIJ3;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITA
SQ  VRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDM
SQ  YSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDE
SQ  VNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDE
SQ  LMQTQEETIHLIFQYNKLVHESVIPLLTDDLLPVVRGVSNSIVENLDNMNVELTSHLENVSQTIEVKFKALEKETDRSLL
SQ  KAKEVESNLRNLNNLVSTSLKGLQTIVRLLTFLLKRQVVLVGILQIFLRKYISMNLYLYAIAVVVTALAGSKVGSWGSLL
SQ  MKSFVTR
//
ID  Q759Y0;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q759Y0;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLEILLFLCVIIQRSHINAEITHVVSHLAETALRQDTNFQLLSQDIIAKKFPILDSSCVRRALSDFLPQCLQYGFETVPS
SQ  DVRTQAAVKLSICELQASGVDNMPPECVGAVHFGACLRAMERTPQWWTTYSGNYQHLPSTCFENALPYEKEQLLSLFLNI
SQ  TDVYSNFQDDLVVDLEKYRANFEATVEASLRLMKASLMEGTHEIVNQLKDDLNYVNSKLADMGETITEHTDNVRTVFNDI
SQ  SDELNDYDMAGQIAHLKEDTMSLWQKINSDMGTYHDVQMSSLYNINAVFDTFYNRATESVQQVRTSVIESQLETLDLIAD
SQ  FNSLVRKSILPVLADELQPQLQEMSVSISRSLVGLSASYNEHLQAWSNRVNETLSEMESHLNNTMSQVEHMNDSIETLEN
SQ  KVFVLVSLGNALTTYVKWIYTFSRALISGYGIVTLIMSMLVVRYSIKLNSSWIKVLGRSTFILVAVVLGARTGSMLSY
//
ID  Q6BNJ4;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6BNJ4;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDCVNISWFLITLFAAIATSTMHDGENNNVGKMLQEPTYLQSEMIESIMSRHLESFSLTESDFEDIIFMKPRSKCVKDAL
SQ  KDIIPECMRLGVDSIEPGLQKKAAIQLSICEFENSKVTYPSSCYNMINDNDFDSCIFDIERAPQYWTTFSGYYREITKIC
SQ  YEESLPFEKEQIISLYSNITKLYSKMFQDLNDSYKDSTHIQQMMKNEFKELQRMMKVILDQNEKTSEEVKEKYEEFSEQY
SQ  SSMLSTSLEISKKFSLGTENLVEDMANNIKYLDFELSRISIAIEDLDFETKLTDMKNSVLDDVRNLSDESISLLDSILTN
SQ  LESLDILSQDAQNITNGISQSLKKNEVLSNNMNNALIETDTQLHEHNEVIRFEFEETISYLSQFSDQAIDNAIRDTSEEI
SQ  TKHVATFIDSINLRLEETTTKLEEVIYNIDDLSDKVGNASSYLIEGLNLLTSNGIMDALLLTYNNVASGLESGFGMLTTL
SQ  KSDIFKIVRFITACILFAILFIWSMNRLFSQNRTKHTTLSSISPIGILNFRRIFRFLTNLALWLSVMGGTLLAVIVTNFL
SQ  IQLKVYISKLSTND
//
ID  A5E4Z8;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  379508;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A5E4Z8;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVGASAISGVVIIANVVAAIAAAAGDGDGGIASTTDTILTLDGIKILNNALLQWKDDCNQRALAEVMPQCIHGVENITPS
SQ  QQKHTAMELSICEFENNGLDYPLECHASVRNLNTNTCIQALEKSPQYWTTFSGNYRAVKDICHQISLPYEKDQIIEVYEN
SQ  MTLLYRSVMEDLKSSHHKYTVELEMKIQNKFNKLFSVVDDLMRSRAEENNKVNQTFNKFYENFQVSISNALVVMQNSYDG
SQ  ANTNFELMQRHVSYFATELQRILLLVQEQGEKLQVQQEQLVTGNVKLSIQQERLFDNMQLFGNELDKLHNAEVSRVSSVN
SQ  KQLKLTEFSIRHANSILRENTDELHLQRMLIAEYTPIILGNITTLLMHFLNQSASEIVENFEHSLNLSLEKLSLKIDETA
SQ  NSLAVVNATIARCSIFASSVVETLDSLKNSTIRMMMLFMSMITPSVTFDGLISGAKAIIAFFTLVTRLAAVIAICLLIIL
SQ  IWPIVKSLFFQPLCYLMRRCSYIVVSILVGVAAANFSVWLLQK
//
ID  P09290;
PN  Protein UL20 homolog;
GN  39;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P09290;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPPQARVSEQTKDLLSVMVNQHPEEDAKVCKSSDNSPLYNTMVMLSYGGDTDLLLSSACTRTSTVNRSAFTQHSVFYII
SQ  STVLIQPICCIFFFFYYKATRCMLLFTAGLLLTILHHFRLIIMLLCVYRNIRSDLLPLSTSQQLLLGIIVVTRTMLFCIT
SQ  AYYTLFIDTRVFFLITGHLQSEVIFPDSVSKILPVSWGPSPAVLLVMAAVIYAMDCLVDTVSFIGPRVWVRVMLKTSISF
//
ID  Q5ZJY9;
PN  Nuclear envelope integral membrane protein 2;
GN  NEMP2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q5ZJY9;
DR  Pfam: PF10225;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPRRLPWARPGPALGLLLLALAGAVPAAGGSCSLLEEGNTIQKLHEDCFCYVQNRTMHLQYIWSTVQVKINSTRTFRFV
SQ  PTPEKSNCRNSETVFEFAACAVQILWRPETSTETFLKIKQYGEDFCFRIQPFKEELYTVSMTREMLDGKLLFLFAAGIFL
SQ  FHFANSLSRSTNFFYLSGIILGVLALLVFVLLALKRFIPRRSTFWILLSGCWMSSLYLIYCFKENMQWLWSEHRIYVLGY
SQ  FVAVGTLSFATCYQHGPLTSELSITLFTWTLQLTAFVFIYCGVNIPQVAYAIIAVKPSPKGLGYPPAAAWHIGRKMKNHF
SQ  QSKKVVVRCLTEEEYREQGETETVRALEELRSFCKNPDFSSWLAVSKLQSPHRFAGFVLGSPHVSPAETKAHDEEYGIGS
SQ  SFLEEQLFETRTESEQDETTSYIHEGDDENEDEIHEPISFPYATELL
//
ID  Q6C994;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6C994;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLSYSFNTTIFTENRDLVAALQPQTNCARTALTLIVSDCGKLSSFNEDQQLRVSLAVGLAVCEFKAAQVTYPDACNNIE
SQ  DWMSTSACTQQLVSSPQWWTTYHGCYNSVKQICHMHEASRECDRALKTHSQIVDMQEKLHTKMDQYWELVETMSDHRDAV
SQ  LDYWNDTFDFMSETLAHMKETSVSLNAVYRDNFAQAQEHFQMLSENLQEARVQMENLGWAAQDAVVSLSKSTLAEQSLVS
SQ  ERLKNDASSLHKLLVLAHQDTTESFETQLQQSLTILVESSDNVLLNHVQQVSSRLSALMSDLEESQKKNMDMQHQLQQKV
SQ  RTINDDIEGFTDTVKQGLEASHSLLNLVKSKIQLVNGVVSIFSRPVRSAFQLASFIIMIRAAFIGGIYTSIGLVMGSMLG
SQ  VLVMQQV
//
ID  A0A1I9LN01;
PN  Protein LONG AFTER FAR-RED 3;
GN  LAF3;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}.
DR  UNIPROT: A0A1I9LN01;
DR  UNIPROT: F4IY42;
DR  UNIPROT: Q7Y048;
DR  UNIPROT: Q7Y049;
DR  UNIPROT: Q93ZE1;
DR  UNIPROT: Q9LY60;
DR  Pfam: PF07969;
DE  Function: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. {ECO:0000269|PubMed:14645728}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0016810;
GO  GO:0009704;
GO  GO:0010218;
GO  GO:0009845;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILK
SQ  VGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWN
SQ  NDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPW
SQ  VKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLK
SQ  LQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMIL
SQ  DMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALL
SQ  ALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSW
SQ  DEFSKDVSASVLATYVGGKQLYP
//
ID  Q3U487;
PN  E3 ubiquitin-protein ligase HECTD3;
GN  Hectd3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}.
DR  UNIPROT: Q3U487;
DR  UNIPROT: B1AUL1;
DR  UNIPROT: Q3TN76;
DR  UNIPROT: Q641P3;
DR  UNIPROT: Q8BQ74;
DR  UNIPROT: Q8R1L6;
DR  Pfam: PF03256;
DR  Pfam: PF00632;
DR  PROSITE: PS51284;
DR  PROSITE: PS50237;
DE  Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the turn-over of TRIOBP (By similarity). Mediates also ubiquitination of STX8. {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019905;
GO  GO:0004842;
GO  GO:0043161;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGPGPGAALESPRQLLGRVRFLAEAARSLRAGLPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAVGA
SQ  APGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLSDCSLDEGWLLVCRPAEGGARLVPIDTPDH
SQ  LQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYTEAIQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSV
SQ  KQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNL
SQ  KKLSDVNIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPASLVRYPRLEGTD
SQ  PEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPSLVAQCLRDSESSKPSFMPRLYINRRL
SQ  AMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSA
SQ  DTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPA
SQ  VDSVLVKLLEVMEGVDKETFEFKFGKELTFTTVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEESKEQVAAMQA
SQ  GLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA
SQ  RIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
//
ID  Q9C900;
PN  Protein SINE3;
GN  SINE3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9C900;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: F4I1K2; IntAct: EBI-16891164,EBI-16950094; Score: 0.37
DE  Interaction: F4KIB2; IntAct: EBI-16891164,EBI-16944564; Score: 0.37
DE  Interaction: Q9SV74; IntAct: EBI-16891164,EBI-16932071; Score: 0.37
DE  Interaction: Q6NKQ9; IntAct: EBI-16891164,EBI-16944414; Score: 0.37
DE  Interaction: Q7XA70; IntAct: EBI-16891164,EBI-16949315; Score: 0.37
DE  Interaction: Q9ZW05; IntAct: EBI-16891164,EBI-16882734; Score: 0.37
DE  Interaction: Q9M8T0; IntAct: EBI-16891164,EBI-1238677; Score: 0.37
DE  Interaction: O82390; IntAct: EBI-16891164,EBI-16904508; Score: 0.37
DE  Interaction: Q9C7S5; IntAct: EBI-16891164,EBI-16904988; Score: 0.37
DE  Interaction: Q67ZM7; IntAct: EBI-16891164,EBI-16930733; Score: 0.37
DE  Interaction: Q8RXK1; IntAct: EBI-16891164,EBI-16945132; Score: 0.37
DE  Interaction: Q9FE70; IntAct: EBI-16891164,EBI-16953503; Score: 0.37
DE  Interaction: Q9LRT1; IntAct: EBI-16891164,EBI-16956175; Score: 0.37
DE  Interaction: Q9SY89; IntAct: EBI-16891164,EBI-16954786; Score: 0.37
DE  Interaction: Q9FZB1; IntAct: EBI-16891164,EBI-16954721; Score: 0.37
DE  Interaction: Q9SNA0; IntAct: EBI-16891164,EBI-16956496; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKEIQIPRKSFARSSELGAKRLKDPEMKNRKVTTEKRQIATFSDVSFESTKDPMDFSPISQISGAISDSEAESVIQGSSL
SQ  DLMSTPEICLPADDSPVSTITSVEARIDTSSTDRIQSIVDLPASVQSLRGEINELKKLICSVDNSAEINWVDRVVTVKFR
SQ  IVLLSFILWAILAAIVVFFSSGEERAYRGPLPT
//
ID  Q9SW31;
PN  Protein SINE4;
GN  SINE4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9SW31;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEEREESSSHEHLKEKLRELEEEWTAMKTGKNSSAVSWITVEDALEYVENSPRNLMLSLQHKPKAEMIQEISPLRRKLFH
SQ  DSDDDDQTKKTTLLSHSSCWSSNVTSSSDTTKAKKKTTIRRFVSVTMVLLLSWVLVVLMNHFDHLSMNTQIITLVPT
//
ID  P41391;
PN  Ran GTPase-activating protein 1;
GN  rna1;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000305}. Note=Possibly enriched in the nuclear periphery.
DR  UNIPROT: P41391;
DR  PDB: 1K5D;
DR  PDB: 1K5G;
DR  PDB: 1YRG;
DR  PDB: 2CA6;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-286642,EBI-1032893; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0046827;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIP
SQ  EALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPP
SQ  LRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIAL
SQ  KSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDD
SQ  VVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI
//
ID  Q6FV75;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6FV75;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0004577;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVL
SQ  LNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHL
SQ  TLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGI
SQ  LV
//
ID  O94473;
PN  Uncharacterized membrane protein C1919.04;
GN  SPCC1919;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94473;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLSFIEGFETIWTVVRAVVLNYLLRSLKILSTILYVSAVISWNVSLKVFGNVLLPGFLTIRTVVIFILRIVSLFLWILA
SQ  DPAILLVQSVYWYFIRAPARFILMVGITLYPLYVLLSWAVFLGIIVGFSLNSVFTFIDSFATPSSNSTVTEAMTKMKNEK
SQ  VLEYPYKDRNIMLGDLASRIPSKDSEKLDEERQPIALEKTKSLDSISHSSSSSRKSSTELKIPPVETRIVAEIPVPSSVK
SQ  RRRHRPNKSMGSIKNS
//
ID  O59744;
PN  Uncharacterized transcriptional regulatory protein C530.08;
GN  SPBC530;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O59744;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
GO  GO:0006351;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDNESHSQETESKILEGAKVATRRRRVTRACDMCRRKKIKCDGLRPCKNCKAGKLECTYHMPSSRKSSFSPEYVENLESR
SQ  VRYLETLLKKNTNFDLSSNSPSFLFFLREQKFQATNELENMSPERKVIFTSMINYGNLFVDAKHGTRYFRGGSSIHVLIQ
SQ  HLIRRLPGDFEICEPYSAYPLGNKNIQFDDNDPEYQFFTPTPRFSIDFMVSSVDPREIQLPGIEEALCITKAAVSYVSGI
SQ  VFYTTYADFPKKIRLLYSGNYQGNFFPLFLSILCVGYYHHLLNNPSNTELQSLIKKYSFYSERLVKSADNFTIESIQCLL
SQ  ILSIYRYCRTEISAAWYYMKLGLNCCLRLGLHRNITEGFTEEQIDSRRRIFWAIYCYDRQLCTLFGFPLGVRDEDIDQCL
SQ  PVTPKFPSVTEIEANARLFFFHGVKLYKISSRILTKLYSPNSRNVTKKHISYAVIQDLEQLLDGFYNSLPRVFRAEQPGE
SQ  FQANHFFYNLQLVYYSFRMLIYRPLLHYLEADSPAMQALKVPDRQTAFTLACKCVDSAIVCVQNLSHLSKGLKRTLDRYY
SQ  WTTVYCGFSTIVTLIFAALLTKNTNLLIHISVARESIEALAHECVTRRLLPLIDKMRESLMKILESNADGYKQMSPTKAP
SQ  QVFESESNVPINNGPQQSIDKESNSNTQLPQVETEGQQQSVFDGNIGTIPYQAYNMNEDSFIDINTLSSMLNYHTQAVSI
SQ  HHPSFYISRSDVPLEEEFQIPNELLAVDPVAESMQENSDIINEAFGLVDPDVSDGKSRESSSLNNSTPFNPTVNIDPASI
SQ  LEHFSQNVMKDSQNS
//
ID  Q9CXE6;
PN  DNA repair protein XRCC3;
GN  Xrcc3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair. {ECO:0000250}.
DR  UNIPROT: Q9CXE6;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DE  Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0008821;
GO  GO:0008094;
GO  GO:0000400;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0045003;
GO  GO:0036297;
GO  GO:0090267;
GO  GO:0010824;
GO  GO:0071140;
GO  GO:0010033;
GO  GO:0090656;
GO  GO:0000722;
GO  GO:0090737;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLDQLDLNPRITAAVKRGRLKSVKEILCYSGPDLQRLTGLPSHDVQCLLRAASLHLRGSRVLSALHLFQQKESFPEQHQ
SQ  RLSLGCPVLDQFLGGGLPLEGITGLAGCSSAGKTQLALQLCLAVQFPRQYGGLEAGAVYICTEDAFPSKRLWQLIAQQRR
SQ  LRTDAPEELIEKIRFSNHIFIEHAADVDTLLECVSKKVPILLSRGMARLVVVDSIAAPFRCEFHLQASAIRAKLLLSLGA
SQ  TLRRLSSTFRSPVLCINQVTDMVEDQQSVSRSLGASEERLSPALGITWANQLLMRLMVDRTHEDDVTTGLPRSPVRTLRV
SQ  LFAPHLPLSSCCYTVSGEGIRGMPGTQSY
//
ID  Q15283;
PN  Ras GTPase-activating protein 2;
GN  RASA2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region.
DR  UNIPROT: Q15283;
DR  UNIPROT: A8K7K1;
DR  UNIPROT: G3V0F9;
DR  UNIPROT: O00695;
DR  UNIPROT: Q15284;
DR  UNIPROT: Q92594;
DR  UNIPROT: Q99577;
DR  UNIPROT: Q9UEQ2;
DR  Pfam: PF00779;
DR  Pfam: PF00168;
DR  Pfam: PF00169;
DR  Pfam: PF00616;
DR  PROSITE: PS50004;
DR  PROSITE: PS50003;
DR  PROSITE: PS00509;
DR  PROSITE: PS50018;
DR  PROSITE: PS51113;
DR  OMIM: 601589;
DR  DisGeNET: 5922;
DE  Function: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0000165;
GO  GO:0046580;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQEEVYRTQVVE
SQ  KSLSPFFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVAIKKEDLCNHSGKETWFSLQPVDSNSEVQGKVHLELKLN
SQ  ELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQ
SQ  FQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIKVPVNVLRTDSSHQAWYLLQPRDNGNKSSKTDDLGSLRLNICYTEDYV
SQ  LPSEYYGPLKTLLLKSPDVQPISASAAYILSEICRDKNDAVLPLVRLLLHHDKLVPFATAVAELDLKDTQDANTIFRGNS
SQ  LATRCLDEMMKIVGGHYLKVTLKPILDEICDSSKSCEIDPIKLKEGDNVENNKENLRYYVDKLFNTIVKSSMSCPTVMCD
SQ  IFYSLRQMATQRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFHLRPHHPDAQTIRTLTLISKTIQTLGSWGSLSKSKSS
SQ  FKETFMCEFFKMFQEEGYIIAVKKFLDEISSTETKESSGTSEPVHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTY
SQ  HKQPGSKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSRCNQNRLSFYHPSVY
SQ  LNGNWLCCQETGENTLGCKPCTAGVPADIQIDIDEDRETERIYSLFTLSLLKLQKMEEACGTIAVYQGPQKEPDDYSNFV
SQ  IEDSVTTFKTIQQIKSIIEKLDEPHEKYRKKRSSSAKYGSKENPIVGKAS
//
ID  Q750Y9;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q750Y9;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0004577;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVG
SQ  YTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVV
SQ  LFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV
//
ID  Q0VGK4;
PN  Lysophospholipase D GDPD1;
GN  Gdpd1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q9CRY7}; Multi- pass membrane protein {ECO:0000250|UniProtKB:Q9CRY7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CRY7}.
DR  UNIPROT: Q0VGK4;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine. {ECO:0000250|UniProtKB:Q9CRY7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0047391;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
GO  GO:0006644;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKD
SQ  EQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLI
SQ  QKVSELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKE
SQ  PHIISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNNMSA
//
ID  Q8BX43;
PN  Tumor necrosis factor receptor superfamily member 19L;
GN  Relt;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q969Z4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q969Z4}.
DR  UNIPROT: Q8BX43;
DR  UNIPROT: Q497Z8;
DR  UNIPROT: Q8BTV0;
DR  Pfam: PF12606;
DR  Pfam: PF00020;
DE  Function: May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation (PubMed:30506946). {ECO:0000250|UniProtKB:Q969Z4, ECO:0000269|PubMed:30506946}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097186;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLQGLMMKRTLLCWPLSCLFVLLPWPLATPTPITPWLCPPGKEPDPDPGQGTLCRTCPPGTFSASWNSYPCQPHYRCSL
SQ  QKRLEAQAGTATHDTMCGDCQHGWFGPQGVPHVPCQPCSKAPPSTGGCDESGRRGRRGVEVAAGTSSNGEPRQPGNGTRA
SQ  GGPEETAAQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAQKEVGPSPGGGGSGINPAYRTEDANEDTIGVLVRLITE
SQ  KKENAAALEELLKEYHSKQLVQTSHRPVPRLLPASPSIPHICPHHHHLHTVQGLASLSGPCCSRCSQKWPEVLLSPEAAA
SQ  ATTPAPTLLPTASRAPKASAKPGRQGEITILSVGRFRVARIPEQRTSSLLSEVKTITEAGPSEGDLPDSPQPGLPPEQRA
SQ  LLGSGGSHTKWLKPPAENKAEENRYVVRLSESNLVI
//
ID  A6ZUA4;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: A6ZUA4;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  Q6UDI5;
PN  Protein UL20;
GN  UL20;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6UDI5;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADASAPDKKNAPTNALKPDLIKIAVERVLAAIDTENNEDLILAAAREPREVVAARAPDLFTSAAYSWSEEDELGTRMRA
SQ  SSFFPVASMFAKIICCLFLLWAKSCTGHGAMVTGLTACTGAYAIASLLCSFVVYYNVRTDNMPFGTYTKLFQIAACIGCG
SQ  CYALGLTMEKLFGDSEMYFALFPDAKNSPLVGATAKGSALILPQGCSVAPYVPLAVSVAYCAAVVYDIADTIFPLLWVRT
SQ  TLNEFAVF
//
ID  Q77MS4;
PN  Protein UL20 homolog;
GN  MDV032;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q77MS4;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0019012;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKHGFGYYATEANEYTIPLDDIDDGRSDTDAKTLGSVLTQLSEEVDWDDAVDYATMSSYLGDYVFTIPNSYDIHPKFTR
SQ  YVVLFGLSTFVLRPSCCLIFLFYAIYAQDNRFLILGTTITAFFYGTLMLEMYYMYANIKYDLMPLSKFQQVLIGALSMLG
SQ  PIIFVAISYNMIFKDVTFMKKILAFDTNLKTSGFVIYLVMIASLAYSITSISDAIGFLLPRLWTRAVLKSCVPF
//
ID  Q24JJ9;
PN  Nuclear pore complex protein NUP43;
GN  NUP43;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q24JJ9;
DR  UNIPROT: O65565;
DR  UNIPROT: Q8LCD6;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMMQDSFQVHRIPQSKYVDGVRWLPQASALNRFFATASYDADCDSSSIEIQSLDPNPRGNHNTNPLIESLSSWTSPSRV
SQ  SSLEVAGNGGGGGSFKPMVSAATSSGSLHVLMIDLVEGAAIEEFYAAEGERFHVGRVEGVDWREGGECVTVGEDGRVNVV
SQ  KIVNGEGLRYRKVFDGNGLVAYRAVKWASPTEFVTGGYGFGLQLWDQRKSGEAVSQLKGNWFQGKTSAIVHSIDIHPSRK
SQ  HTCIAGGSSGTVFAWDLRWPQQPIVLSGVGASENINNPLSESEVWEVQYDSYTKSNVSSSRILPVMTCSEDGILGIIEQG
SQ  EEPIELLAEPCAINSFDIDRQNPQDVICSLEWESIAVFSRP
//
ID  Q5ZSQ2;
PN  Adenosine monophosphate-protein hydrolase SidD;
GN  sidD;
OS  272624;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:21680813}.
DR  UNIPROT: Q5ZSQ2;
DR  PDB: 4IIK;
DR  PDB: 4IIP;
DE  Function: Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as an adenosine monophosphate-protein hydrolase (de-AMPylase) by mediating the hydrolysis of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby releasing RAB1B from bacterial phagosomes and rendering RAB1B accessible for inactivation by LepB. De- AMPylation of RAB1B cannot take place when LidA is bound to RAB1B. {ECO:0000269|PubMed:21680813, ECO:0000269|PubMed:21734656, ECO:0000269|PubMed:22228731}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0046872;
GO  GO:0044603;
GO  GO:0017137;
GO  GO:0009405;
GO  GO:0018117;
GO  GO:0044602;
GO  GO:0043087;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVYYEIIKDIVFTYNLQFTHLIHNDRISEVNLGGVTMRSIITQICNGVLHGQSYQSGSNDLDKGNSEIFASSLFVHLNEQ
SQ  GKEIIKHKDSDDKIVIGYTKDGMAFQIVVDGFYGCERQAVFSFIDNYVLPLIDNFSLDLTRYPDSKKVTESLIHTIYSLR
SQ  SKHAPLAEFTMSLCVTYQKDEQLFCAGFGIGDTGIAIKRNEGTIEQLVCHTEVDGFKDAFDNYSSANIDLVIERNSVFNT
SQ  KVMPGDELVGYTYVPPMLEMTEKEFEVETVDGKKINKRIVRHLNLDPGNFDDKDPLFSQLLQVVKSKQKQLVEQAKETGQ
SQ  IQRFGDDFTVGRLVIPDQLLINQLRIHALSIGVSDGLLSYIKNENENKGFLGIYGFFTGADKNIEKATLYKNLIAKYQNN
SQ  HFISLIILSALVSDSKTPLMTQYLVGYLDFPSKALLANKITELLLKELENPDMREILGSRLATDVIEELETKIIRYIHNP
SQ  AGSDIHSTLNLWTADKIKAATNSSLTI
//
ID  F1R0H0;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  slc2a10;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
DR  UNIPROT: F1R0H0;
DR  UNIPROT: A8KB28;
DR  UNIPROT: I1SV80;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:22116938}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0005351;
GO  GO:0072358;
GO  GO:0046323;
GO  GO:0030903;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCSVLLLTITVSTLGGLVFGYELGIISGALPQLQTHFSLGCVQQEAVVSALLIGSLFASIIGGWLIDRHGRRTSILLSN
SQ  LLILAGSVILTTGTSFFALVIGRAVIGFAMTVSSMSCCIFVSEMVTPERRGLMVTLYEVGITVGILIAYAVNYIFNNVPL
SQ  TGWRYMFGFAIIPSLIQLASIVLLPKQAEVFVIHDDDSRQADRLTEETETSNQHQQSEKYGVSDLFKSKDNMRRRTVIGV
SQ  GLVLSQQFTGQPNVLFYASTILFSVGFQSNASAILASVGFGIVKVIATLLAMLCSDRAGRRSLLIGGCSMLAVGLILTGF
SQ  LCRQSVIDTTKRCTSVGPHSNLTLSAEHDEGVGFSSQTLDVHEHLRSFSQSEDIYKWIIFTCLMAVVSAFSVSFGPMTWV
SQ  VLSEIFPKDIRGRAFSFINCFNVGANLIVSFSFLSIIDVIGLSGVFLMYGVVGIAGVVFIYLVLPETKGKSLQDIDRELS
SQ  QTRMIHRQELCSIFQRRRFSPGYQRVQLTSTAT
//
ID  Q93367;
PN  Messenger RNA-binding inhibitor of apoptosis 1;
GN  mina;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30728462}.
DR  UNIPROT: Q93367;
DR  PDB: 6FBL;
DR  Pfam: PF00013;
DE  Function: RNA-binding protein which binds to its own mRNA and target mRNAs to negatively regulate gene expression to modulate apoptosis and differentiation in the germline (PubMed:30728462). Negatively regulates the expression of the argonaute protein wago-4, and may thus play a role in RNA-mediated gene silencing (RNAi) in the germline (PubMed:30728462). {ECO:0000269|PubMed:30728462}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0043066;
GO  GO:0010629;
GO  GO:0060968;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDSTPYPVPQELYIPQKMKAFMAEPQGCALVAALEGQFQCSIVVINDHLSVISSADGVAVDINQIEKILRDVWRKRDVQ
SQ  IMIREAALNASCTHICHTLLPRAYCAVVLFFSSDLQRRSRCTDIIIDQFTGKVTMFGTEQAVNKAREMMIECLTEHFGLL
SQ  EMNIPPTQRTTRMGYTNSYNPEIRTHLPPNSFLNSVFPMGEPNAILTSTPPTTSIMDEPLLSASLEKHLLFPSDFSVPPP
SQ  RLSPVQELPLTPPKTCVVEKIKQWIPTTEVGKILGNRAAVKKHIERQFNCVITVHTEVQSSFGATPVEIVAQNKEQCQEA
SQ  RNAVMSLMQSHQDKPASNPPDSGFSTPGSPFTSDSSSTTPEKRGNSRQYHRGSFRDQPKVMLALTPRKLSPSD
//
ID  Q09353;
PN  Sentrin-specific protease;
GN  ulp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25475837}.
DR  UNIPROT: Q09353;
DR  UNIPROT: Q8IU18;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form. {ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:25475837}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0008234;
GO  GO:0009792;
GO  GO:1904333;
GO  GO:0016926;
GO  GO:0032880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRRSDLSDKDSQSRKRHWLTDQAVTNEEKEQSPTKRTRKTKSQGLGGLFNTFFGMFVSSNSGEKEKTEVSGEVQVQEDD
SQ  EIIVEGTTRRVAENKKYMIFLNEDAPVRANAGSEENEVIIEKHVQKNVEIRNDEEKQEVQGDLVLTLSSSPKSPKNLEKS
SQ  FEVQQDDEEPDVLFEKVVKTPNKQLQEARRFQNELIFLNDNPDTPDDVSVISDSRSKEFISPTPDDSVSRPITPSLSSLS
SQ  NYTSNNVRDYWRRNSAKKPEVLRRVPVRHQFKHSTSVRKMNTIIDLKKIKNHLSSRDRLLQGVVASGQYEAKAISGIVEK
SQ  KPKKMQRTSSTDILARAKNKIAELGGSRSNTPSLLSREPSIIIDSEESTSSSYRQHARSNSSESDSYRKLNDILSQINSL
SQ  GIGSAYRGPQRYQNSYQLSKQKEDKLLEEARIREGHRSQTRGDRLEDVRKRLELQGIAIRPKVEKKKVDDFMALPDAADA
SQ  LVERAWSGGNPNEQFVDAFSIQICKKDLATLSGLHWLNDEIINFYLQLICDRSNGDSKYPKIYAFNTFFYSNIVSKGYAS
SQ  VKRWTRKVDIFAFDIVLVPVHLGMHWCMAVIDMGEKKIEFYDSLYDGNTAVLPALRGYLEAESLDKKKTAMNFSGWTIQQ
SQ  MTDIPRQQNGSDCGVFSCQFGEWASRRTTPRFTQKNMPYYRKRMVYEIVSKKLLATI
//
ID  Q3TB82;
PN  Pleckstrin homology domain-containing family F member 1;
GN  Plekhf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16188880}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16188880}. Lysosome {ECO:0000269|PubMed:16188880}. Note=Translocates to lysosome during apoptosis.
DR  UNIPROT: Q3TB82;
DR  UNIPROT: Q99M16;
DR  Pfam: PF01363;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  PROSITE: PS50178;
DE  Function: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005768;
GO  GO:0005764;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0035091;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0006915;
GO  GO:0007032;
GO  GO:0010508;
GO  GO:2001244;
GO  GO:0072659;
GO  GO:0046902;
GO  GO:0016050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLSKRKYRSQHII
SQ  PLEEVTLEPLPETLQAKNRWMIKTAKKSFVVSAASTTERQEWISHIEECVRRQLLATGRQPTTEHAAPWIPDKATDICMR
SQ  CTQTRFSALTRRHHCRKCGFVVCAECSRERFLLPRLSPKPLRVCSLCYRELAAQKLREEAREGIGGSPPQLSHLGGTVCG
SQ  ASSGDDDDSDEDREGNGDGDWPTQVEFYASGVSWSAFHS
//
ID  A1A4S6;
PN  Rho GTPase-activating protein 10;
GN  ARHGAP10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to cell membrane is dependent on PH domain. {ECO:0000250}.
DR  UNIPROT: A1A4S6;
DR  UNIPROT: A1L0S5;
DR  UNIPROT: Q2VPC4;
DR  UNIPROT: Q2VPC5;
DR  UNIPROT: Q96EV3;
DR  UNIPROT: Q96S75;
DR  PDB: 2MIO;
DR  Pfam: PF00169;
DR  Pfam: PF00620;
DR  Pfam: PF14604;
DR  PROSITE: PS50003;
DR  PROSITE: PS50238;
DR  PROSITE: PS50002;
DR  OMIM: 609746;
DR  DisGeNET: 79658;
DE  Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:11432776}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-78473,EBI-1390944; Score: 0.35
DE  Interaction: Q92625; IntAct: EBI-1390944,EBI-1048612; Score: 0.37
DE  Interaction: P78314; IntAct: EBI-1390944,EBI-727062; Score: 0.49
DE  Interaction: P46013; IntAct: EBI-876367,EBI-1390944; Score: 0.35
DE  Interaction: Q9UNA1; IntAct: EBI-1390944,EBI-1390913; Score: 0.27
DE  Interaction: Q9ULB1; IntAct: EBI-1390944,EBI-522901; Score: 0.27
DE  Interaction: Q02539; IntAct: EBI-932603,EBI-1390944; Score: 0.40
DE  Interaction: Q9Y426-2; IntAct: EBI-21517991,EBI-1390944; Score: 0.35
DE  Interaction: C9J6V4; IntAct: EBI-21517910,EBI-1390944; Score: 0.35
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0007010;
GO  GO:0043066;
GO  GO:0051056;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDE
SQ  RCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHL
SQ  QEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFE
SQ  GTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFF
SQ  LKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIR
SQ  KCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFI
SQ  VPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQN
SQ  IVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDS
SQ  LSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATV
SQ  ADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
//
ID  A5D7H5;
PN  Protein CASC3;
GN  CASC3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: A5D7H5;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon- exon junctions. Binds poly(G) and poly(U) RNA homopolymer. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003723;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRQRASQDTEDEESGASGSDSGGSPARGGGSCSGSVGGGGSGSLPSQRGGRAGALHLRRVESGGAKSAEESECESE
SQ  DGIEGDAVLSDYESAEDSEGDDGEYSEEENSKVELKSEANDAANSSAKDEKGEEKPDTKGTVTGERQSGDGQESTEPVEN
SQ  KVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALY
SQ  GYDIRSAHNPDDIKPRRIRKPRFGSPPQRDPSWIGERPNKSHRHQGPGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFK
SQ  EGRTGFRPAEAGGQHAGRSGETVKHETSYRSRHLEQTPVRDPSPEADAQVLGSPEKEEVAPEIPNPAPDTAPPVPDRPVE
SQ  KKSYSRARRTRIKAGDAGKVAEEVPPPPEGLTPAPPVPEATPPTPAKTGNWEAPVDSTTGGLEQDVAQLNITEQNWSPGQ
SQ  PAFLQSRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTH
SQ  GDSPAPLPPQGMIVQPEMHLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPG
SQ  ALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS
//
ID  Q9UST7;
PN  Transcription factor tau subunit sfc3;
GN  sfc3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UST7;
DR  Pfam: PF04182;
DE  Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with sfc6 in DNA binding. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization. {ECO:0000250|UniProtKB:P34111, ECO:0000269|PubMed:10906331, ECO:0000269|PubMed:16751097}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0000127;
GO  GO:0003677;
GO  GO:0000995;
GO  GO:0042791;
GO  GO:0006384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSLIRHCSEEIALDGSSGCSIDRLWEFAANFFFRQGIVQNLDDNYKTFVWPLILKEDGIEVWIEDEDATGLRSKMQEIP
SQ  WNYQDITIELRARIRLFASEDRQWLTLTYKTKTDSKIQPLAFELLSCISRYRQEGVDRIQLCKETKQEPRSVYGRIQALE
SQ  DASLISKVAINRSRAQTALLVLKRFESENSTINETVAQVSGKQIYNTEKIRSNICDAVQSSRNGICRHVDARAMVNLNHS
SQ  RWERRYYARQVTYLHNNGYLRKCLTFVPNSPERCIRCLQFIKPYISSLDATEDDVDFTEVDDIPEDDELEEEEPLLPSKE
SQ  EFDASFLQPLADVGPTLPQWSRFRPLEFQCFVLIRNAGFHGVITLQILSGLTGIRFNKPLFKLLGSLVEHRSSVPNHLSH
SQ  MSITRFEDKTKKSRQYRYFTLQSQLNRLIRDGIPAETISKLLPHVHSLAGEFSPIDSSLFLNSLHHKGNMESNAEVSPDG
SQ  MTLLPRKRGRPRKSANISVTSSPIRPSKNENNLPSLAISPVSEGFIQNATISTPSTSSNLSIAGSLTPSKTSRIYRGLAP
SQ  LKNPEFNEDHVKKAEHLEPLLNVSSSVPSKNFTVSSPDHLKYGNTSSLQVSDSQSSIDLDSSFHYPVSVDSQLSHSTGSL
SQ  MANFSSPTKKRRLESVDFIFLQRKGLILSYLVEQNGAFEISRKMFEDLADLKVRRNPETSRTVMDRRTFQQTLEKLMQEK
SQ  KVRKLVIATNNGLGKLVRKDIVVQYDMKPDSPRFQQLRAQITTPEIEKQSTPEILKDVDVDFLKRNTSLSRRKSMPAEIK
SQ  RHKESSETKPVDKEEVKKNEKEKDDPMRLAQQLLESLAPDFALHENTQQKSPVEKPKKLRKDRYASVEEFDYFSSTEHAS
SQ  KRSVKRFKNDFTSDEDETLIRAVVITQIYYGGTNRLIKWEAVQKCFPNRDIYALTRRYLSIRQHTKFKGLQQFLSENWQQ
SQ  MYKDAVSRKDLMPYPDSVDDFDPTPYVKASCRPYMISSSNLATTRLPRDLVDVYETYNIEVVKQETNFREMIFDPSLSVA
SQ  SKMNAYCDMPFTMPLSLNDKQNNEGDENCEKGQLFDAKSTIKSIVAIPDATYDARFSQERLMQYPEDILIAAHQELLDKR
SQ  IITRVNSENSRLQPGRNFQFTEKFASSLKSPLPPFLLSQAKRFNKFLLEGFQNHKNHLFEETSNSGTLACILDLLSQGKL
SQ  QISIVGSKFNEYGLSEGYRTRLLEHDNINVTLVLSGKESESKKNYGVTEKLATPPSHEPRLWLNGKCELIEMIWMNIEQS
SQ  IVYQLLRKPGILRSQLTNLLFPGLEPREFNEVLDYFIAAGAAIEKDGLYLNHNYLFKLT
//
ID  P60877;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: P60877;
DR  UNIPROT: P13795;
DR  UNIPROT: P36974;
DR  UNIPROT: P70557;
DR  UNIPROT: P70558;
DR  UNIPROT: Q8IXK3;
DR  UNIPROT: Q96FM2;
DR  UNIPROT: Q9BR45;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0031201;
GO  GO:0070032;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0006887;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  Q6PBT6;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  gchfr;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: Q6PBT6;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0044549;
GO  GO:0009890;
GO  GO:0043105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYILISTQIRLETGPTMVGDEYSDPSIMNYLGARKITVLGNNFSEYHVDEPPRLVLDKLDKIGYRVVSMTGVGQTLVWC
SQ  LHKESSNTL
//
ID  P41917;
PN  GTP-binding nuclear protein Ran-2;
GN  RAN2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:17530257}. Nucleus envelope {ECO:0000269|PubMed:17530257}. Note=Localized in the perinuclear region with the highest concentration at the nuclear envelope at the interphase.
DR  UNIPROT: P41917;
DR  UNIPROT: Q0WVD9;
DR  UNIPROT: Q94K33;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8RWG8; IntAct: EBI-2325867,EBI-2325919; Score: 0.37
DE  Interaction: Q9LMK7; IntAct: EBI-2325844,EBI-2325919; Score: 0.37
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009536;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006606;
GO  GO:0046686;
GO  GO:0000054;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRD
SQ  GYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNF
SQ  EKPFLYLARKLAGDQNLHFVESPALAPPEVHLDIAAQQQNEADLAAAAAQPLPDDDDDAFE
//
ID  P04888;
PN  Matrix protein;
GN  M;
OS  696863;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: P04888;
DR  UNIPROT: Q91DS1;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSTLRKLFGIKKSKGTPPTYEETLATAPVLMDTHDTHSHSLQWMRYHVELDVKLDTPLKTMSDLLGLLKNWDVDYKGSRN
SQ  KRRFYRLIMFRCALELKHVSGTYSVDGSALYSNKVQGSCYVPHRFGQMPPFKREIEVFRYPVHQHGYNGMVDLRMSICDL
SQ  NGEKIGLNLLKECQVAHPNHFQKYLEEVGLEAACSATGEWILDWTFPMPVDVVPRVPSLFMGD
//
ID  Q91892;
PN  Chloride channel CLIC-like protein 1;
GN  clcc1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: Q91892;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (By similarity). {ECO:0000250|UniProtKB:Q99LI2, ECO:0000250|UniProtKB:Q9WU61}.
DE  Reference Proteome: No;
GO  GO:0034707;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLFLLVALYLSPVYGDYTDEWIDPSDMLNYDAASGKMKNKPQVESTQSYYSVENTVSQDATQQPAQKANELHQNPDMTC
SQ  SAEYQEYKTKLENLKGQLEETKRMEKSKSKSQAIFKRYLNKILIEAGRIGLPDESYPKAHYDAEVVFTMEMLQEIQSFLN
SQ  NGDWNVGALDDALSSTLVQFKHHNEEEWKWKFEDSFGVDVYTLFMLILCVLCLVKLIATEIWTHIGWFTQLKRLLILSTV
SQ  ISFGWNWMYLYKVAFAERQAELAKLQDFDKCSQKISWSESLFDWMKGAATFQNDPCEDYFKALIVSPTLMVPPTKALALT
SQ  FTNFITEPLKHIGKGIGEFLNALLSEIPLFFQVPVLIFIAVLLLAFFYGAGTAVMNPVNLYRRLTGPEREKPLPVEPTRS
SQ  NRKRFIEDVRVPPALGQLPRDNDVVNIPKQQPLDDIDGSNNPPVTAPADPSDTGQVKSNNTGEPLVQEDHSIKKSIKESR
SQ  NDERPNTESPEAKPQRPEEPVVETLRST
//
ID  O94573;
PN  Uncharacterized transcriptional regulatory protein C1773.16c;
GN  SPBC1773;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94573;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0000228;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
GO  GO:0006351;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRIRNACELCRRKKLRCNGELTCQNCMVYGEECRYVKRVKHDNRAAVQENERYPILYTPLSTSDHDNDEENEINELKNA
SQ  VKALDKRFDNFELKLEALFSLLRSQQDSERKVKPGGFPSLVSQILSAGALVDSKLQAYTMRTNFFSNGFSSNDLFPHSFP
SQ  TWKSAFRDVPDKDWAKTCLDWYFRFINCNWPIFYKKQYMESFEKLYIDKNLVKGAWIVSFYAILALAVSRDKRVDNSKLA
SQ  ESFFATSWFLIQRPGFFLTPQLEKIQALVIMIQFASHLSLYNLCKKLCGQVCLMVKDLNLHKESTDKDLDQDMAELHRRI
SQ  FWVCYIFETTTSLIFGTPPVLGDLEIECKYPDINYAHCFAENVQGDLIFTCEISLTVLKHEIRTKLYNSNNVFLDKGQKG
SQ  VISNIQTKILNFERAIPSEMKHYFEILKAGNGLPEELDIIKQHFFTACVEIYLSYCNTLIYLYLADDSIEGSKICLSTAR
SQ  AAIDVIKGFLVVLDPISKNICYLWLFLYCPFTPFLTVFSHLLEDDDLDADICVKDVDRLYSIHAFFLKMKDISGEFAERL
SQ  SVITENFIQSAEQYLALQNTSVFGTFDALSESFSI
//
ID  Q22908;
PN  Ras and EF-hand domain-containing protein homolog;
GN  rsef;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: Q22908;
DR  UNIPROT: Q21466;
DR  UNIPROT: Q22906;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds GTP and GDP (By similarity). Plays a role in uterine seam cell development (PubMed:25281934). {ECO:0000250|UniProtKB:Q8IZ41, ECO:0000269|PubMed:25281934}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0032482;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKPEVENLFSLCDSESKGYLTMEDLRKVCPQLDDNDLRFIFTELDQDGSGKIEKLEFLRGFQDTVQHGESHGLNGMQRR
SQ  ASVAVEDPPMFLRDEQMFDSESDSTSSRPAIRVFDEEHYHSESDTNINIDFSVPCQEEVLVLYEQLQSSGVPALLRKFER
SQ  VVGSFHKELSEKKHENERLQRIYASEREMYNRRMEEMESEVDQQLELTEMKARQEERDRLTKEKEEMRQRMSDEMSEMRN
SQ  NIERLQKMEKALERENERLNHQKELSDKLKVVNEENNDLRQNLAENHLELAMIKSELAQVRCEFDQKQDELSARRGILFQ
SQ  LEPINSLSSSDQASHATEESESVRKQLQLLFDANRKLHETNESLRDALDSRASVLRQFNLRTPSPGLLSSNRNSVENFQT
SQ  STNVFRSVPLHAISTEEQGTIFGTIEEKTSLILDDAHSLQGLDTPGDLMGLNDANGPAERTFRIVMCGDAAVGKSSFVMR
SQ  VIRRQFTNQLPSTLGVDFHVKTVNVDGRNVALQLWDTAGQERFRSLCKSYFRRADGAILVYDVCAEQSFLRVRDWIETIK
SQ  ESTERSIPIILVGNKVDMRISTPGSVAKTDGASMAAAMGVLFMETSALDGSNIDNAMLALTRELMAVEDVEIRSTGVVLN
SQ  PAVAKKGGCFSKCRGS
//
ID  P17698;
PN  Clusterin alpha chain;
GN  CLU;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P17698;
DR  Pfam: PF01093;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0051082;
GO  GO:0002434;
GO  GO:1905907;
GO  GO:0043065;
GO  GO:0048260;
GO  GO:0050821;
GO  GO:0042127;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY
//
ID  Q3T0C9;
PN  Synaptojanin-2-binding protein;
GN  SYNJ2BP;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}; Single- pass type IV membrane protein {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}.
DR  UNIPROT: Q3T0C9;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DE  Function: Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. {ECO:0000250|UniProtKB:Q9D6K5}.
DE  Reference Proteome: Yes;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0031594;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0098839;
GO  GO:0098609;
GO  GO:0007268;
GO  GO:0006897;
GO  GO:0045197;
GO  GO:0016525;
GO  GO:0010596;
GO  GO:0001937;
GO  GO:0070373;
GO  GO:1903671;
GO  GO:0043113;
GO  GO:0097120;
GO  GO:0008593;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIFVSRIKENGAAALDGRLQEGDKILSVNGQDLKNLLHQD
SQ  AVDLFRNAGYAVSLRVQHRLQVQNGPIGPQGEGEPSGIPIAMVLVPVFALTMVAAWAFMRYRQRL
//
ID  O54923;
PN  Exocyst complex component 6;
GN  Exoc6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (PubMed:12954101). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:Q8TAG9, ECO:0000269|PubMed:12954101}.
DR  UNIPROT: O54923;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000269|PubMed:20890297}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0030218;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0015031;
GO  GO:0006904;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESGEALGTVPEHERILQEIESTDTACVGPTLRSVYDGQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITEL
SQ  LKVRADAEKLKVQVTDTNRRFQDAGKEVIEQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMQRYYSALKT
SQ  MEQLENVYFPRVSQYRFCQLMMDTLPKLREDIKDISMSDLKDFLESIRKHSDKIGETAMKQAQQQKSFSIAVQKQTNMRF
SQ  GKNMHVNNDRTLEEKSDIILKHTLEEEAENDEEVLTVQDLVDFSPVYRCSHIYSALGDEETFENYYRKQRKKQARLVLQP
SQ  QSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFA
SQ  DTLQGYGFSVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKMVISKFPFQDPDLEKQSFPKKFP
SQ  MSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQA
SQ  CKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFL
SQ  RSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFID
SQ  LRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVKQLRGLVTGM
SQ  SQHM
//
ID  Q2VWQ2;
PN  Protein kinase C-binding protein NELL1;
GN  Nell1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region. {ECO:0000250}.
DR  UNIPROT: Q2VWQ2;
DR  Pfam: PF12947;
DR  Pfam: PF07645;
DR  Pfam: PF02210;
DR  Pfam: PF00093;
DR  PROSITE: PS00010;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS01187;
DR  PROSITE: PS50025;
DR  PROSITE: PS01208;
DR  PROSITE: PS50184;
DE  Function: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:16537572}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008201;
GO  GO:0042802;
GO  GO:0005080;
GO  GO:0030154;
GO  GO:1903363;
GO  GO:0033689;
GO  GO:0043065;
GO  GO:0030501;
GO  GO:0045778;
GO  GO:0045669;
GO  GO:0010468;
GO  GO:0045667;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPMDVILVLWFCVCTARTVLGFGMDPDLQMDIITELDLVNTTLGVTQVAGLHNASKAFLFQDVQREIHSAPHVSEKLIQL
SQ  FRNKSEFTFLATVQQKPSTSGVILSIRELEHSYFELESSGPREEIRYHYIHGGKPRTEALPYRMADGQWHKVALSVSASH
SQ  LLLHVDCNRIYERVIDPPETNLPPGSNLWLGQRNQKHGFFKGIIQDGKIIFMPNGFITQCPNLNRTCPTCSDFLSLVQGI
SQ  MDLQELLAKMTAKLNYAETRLGQLENCHCEKTCQVSGLLYRDQDSWVDGDNCRNCTCKSGAVECRRMSCPPLNCSPDSLP
SQ  VHISGQCCKVCRPKCIYGGKVLAEGQRILTKTCRECRGGVLVKITEACPPLNCSEKDHILPENQCCRVCRGHNFCAEAPK
SQ  CGENSECKNWNTKATCECKNGYISVQGNSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCIPGYIRVDDFSCTEHDDC
SQ  GSGQHNCDKNAICTNTVQGHSCTCQPGYVGNGTVCKAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECAEGFVEC
SQ  HNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGL
SQ  KHNGQVWILREDRCSVCSCKDGKIFCRRTACDCQNPNVDLFCCPECDTRVTSQCLDQSGQKLYRSGDNWTHSCQQCRCLE
SQ  GEADCWPLACPSLSCEYTAIFEGECCPRCVSDPCLADNIAYDIRKTCLDSSGISRLSGAVWTMAGSPCTTCQCKNGRVCC
SQ  SVDLVCLENN
//
ID  Q10475;
PN  Eukaryotic translation initiation factor 4 gamma;
GN  tif471;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12581158}. Note=Localized to the perinuclear region, the growing tips and septum.
DR  UNIPROT: Q10475;
DR  UNIPROT: P78832;
DR  Pfam: PF12152;
DR  Pfam: PF08017;
DR  Pfam: PF02854;
DE  Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. {ECO:0000269|PubMed:12581158}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9USV1; IntAct: EBI-927233,EBI-2477564; Score: 0.35
DE  Interaction: Q9UUB7; IntAct: EBI-926902,EBI-2477564; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0016281;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0005198;
GO  GO:0003743;
GO  GO:0002183;
GO  GO:0042273;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNS
SQ  SKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPV
SQ  STVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNT
SQ  NTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHY
SQ  QHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQ
SQ  YIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIV
SQ  NPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEEN
SQ  AKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEK
SQ  AKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAP
SQ  LASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQ
SQ  FITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRS
SQ  GSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKP
SQ  DPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRK
SQ  ENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKA
SQ  NLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVN
SQ  IDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSS
SQ  GRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALR
SQ  REQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS
//
ID  E7FDB3;
PN  Nanos homolog 1;
GN  nanos1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11691838}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11691838}.
DR  UNIPROT: E7FDB3;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Acts as a translational repressor. Can mediate repression affecting different steps in the translation process: cap-driven, IRES- driven, polyadenylated RNAs or nonpolyadenylated RNAs (By similarity). Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival. {ECO:0000250, ECO:0000269|PubMed:11691838}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0060293;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0007281;
GO  GO:0008354;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDFLNHNYLSARASYDYTFNFWNDYLGLSTLVTKNSKHSVPQNPNSITESLKATLGLDDSPPCPCVMGEGDSGGHLDSCC
SQ  CPPPASISILDLKERFSILSPFQNQNQGSLLSSSQEREIGIGGGFAGFDLFGVERKMRKPAARNKQEPKICVFCRNNGAP
SQ  EEVYGSHVLKTPDGRVVCPILRAYTCPLCSANGDNAHTIKYCPLSKDQPAQRVLKGGRAVGGKRVKIF
//
ID  Q8AIH4;
PN  Protein Nef;
GN  NEF;
OS  388910;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8AIH4;
DR  Pfam: PF00469;
DE  Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28 and probably other immunity surface molecules. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019012;
GO  GO:0005525;
GO  GO:0017124;
GO  GO:0030683;
GO  GO:0009405;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNIFGRWPGARKAIEDLHNTSSEPVGQASQDLQNKGGLTTNTLGTSADVLEYSADHTEEEVGFPVRPAVPMRPMTEKLA
SQ  IDLSWFLKEKGGLDGLFFSPKRAAILDTWMYNTQGVFPDWQNYTPGPGIRYPLCRGWLFKLVPVDPPEDDEKNILLHPAC
SQ  SHGTTDPDGETLIWRFDSSLARRHIARERYPEYFK
//
ID  Q9D081;
PN  UDP-N-acetylglucosamine transferase subunit ALG14 homolog;
GN  Alg14;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9D081;
DR  UNIPROT: Q8CEP2;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSILILAATAAGLVILLFQRLWTVLGPHHVTPRESLRLLIVAGSGGHTTEILRLVGSLSNAYSPRHYVIAESDEMSAKK
SQ  IHSLEELSRAQNDSTTEYPKYHLHRIPRSREVRQSWLSSVFTTFYSMWFSFPLVLRIKPDLVLCNGPGTCVPICVSALLL
SQ  GILGVKKVIIVYVESICRVETLSLSGKILRHLSDYFIVQWPTLKEKYPKSVYLGRIV
//
ID  P87310;
PN  Mediator of RNA polymerase II transcription subunit 10;
GN  med10;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: P87310;
DR  PDB: 5N9J;
DR  Pfam: PF09748;
DE  Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0045944;
GO  GO:0060261;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLPQDDMTDEMKSLASRLEDTTQAFYDLALIVYNLEDTTPSDAIPESLDTLIRDLKSLPDISRKVNNLIPQDVLEYIEQG
SQ  RNPDVYARQFSELVQKDNQYVNGKLYAIEGFQKAFAEEIKQAYPEVSSVVDKILNEGKVESTVS
//
ID  Q568Z6;
PN  IST1 homolog;
GN  Ist1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the nuclear envelope during late anaphase. {ECO:0000250|UniProtKB:P53990}.
DR  UNIPROT: Q568Z6;
DR  Pfam: PF03398;
DE  Function: ESCRT-III-like protein involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST. {ECO:0000250|UniProtKB:P53990}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0000785;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005793;
GO  GO:0070062;
GO  GO:0090543;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0090541;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0009838;
GO  GO:0051301;
GO  GO:0061640;
GO  GO:0045184;
GO  GO:0048672;
GO  GO:0045862;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0046745;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPVGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGAPDGTMPMPMPMPMPMPS
SQ  PSPNAPFAYPLPKGPSDFSGLPVGTYQAFPNIHPPQIPATPPSYESVDDINADKNVSSAQIVGPKPEAPAKPPSRPVDNY
SQ  NTFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
//
ID  Q6BMD0;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6BMD0;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFESQLCIKVVLLLLPFFIIGIRLLWVLPAVNSPAMGSEKEKGLSQIPSELRGSNIMIFLGSGGHTGEMMRILANVDLN
SQ  NFNRTWVTSSGDSTSILKCKKYEDERLTSGQNKSDYLVLHRARTVGESIISSVFSTVRSLISTIKHLYELPQFPSILLLN
SQ  GPGTSVPLAYIIFLLKFLGLCKTRIIYIESLARVKQLSVSGLLILPITDRFIVQWKQLAVKYKRAEYYGILI
//
ID  Q4WNB5;
PN  UDP-N-acetylglucosamine transferase subunit alg14;
GN  alg14;
OS  330879;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q4WNB5;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPL
SQ  STLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVK
SQ  RSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD
//
ID  Q6NVE8;
PN  WD repeat-containing protein 44;
GN  Wdr44;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}.
DR  UNIPROT: Q6NVE8;
DR  UNIPROT: Q3UT13;
DR  UNIPROT: Q8BTS1;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0017137;
GO  GO:0030334;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASESDTEEFYDAPEDVHLGTGYPVGSPGKVGLLSFKEAENTANQAGNESPVQELRQDVSKKIIESIIEESQKVLQLEDD
SQ  SLDSKGKGLSDEATAGPSVAGTEFSNIPGLLAIEHELQQDSEKAESQNVAEESELETQKCFPSDETCEKSEKTVDETDNL
SQ  TEVSSGEQLDASGLEAETLNKEALEVKEGDVLDPASLDTLSTTDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPP
SQ  PTNFPPPRPPPPSRPAPPPRKKKSELEFEALKTPDLDVPKENITSDSLLTTNMASENTVRDSLPSLDLASATSGDKIVTA
SQ  QENGKAPDVQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSN
SQ  DATQSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMP
SQ  YTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEG
SQ  RVSPSPSQESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRR
SQ  ECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIF
SQ  YDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDF
SQ  TYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLD
SQ  STSTGIVKTDNTEVLLSADFTGAIKVFINKRKTVS
//
ID  Q8CFE4;
PN  SCY1-like protein 2;
GN  Scyl2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Endosome membrane {ECO:0000250}. Note=Plasma membrane-associated in clathrin- coated vesicles. Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8CFE4;
DR  UNIPROT: Q3UT57;
DR  UNIPROT: Q3UWU9;
DR  UNIPROT: Q8K0M4;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DE  Function: Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. May be a serine/threonine-protein kinase. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030136;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0005102;
GO  GO:0008333;
GO  GO:0090090;
GO  GO:2000370;
GO  GO:0002092;
GO  GO:2000286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKD
SQ  QIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSSISPDIKDYKLYDVETKYGLLQ
SQ  VSEGLSFLHSSVKMVHGNVTPENVILNKSGAWKIMGFDFCVSSSNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILS
SQ  VSCETASDMYSLGAVMYAVFNQGRPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTSIPEEVREHVKLLLNVTPTVRPDADQ
SQ  MTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEEC
SQ  TKEEYIKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLID
SQ  YPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLG
SQ  ITKEQLAGKVLPHLIPLSIENNLNLNQFSSFIAVIKEMLSRLESEHRTKLEQLHVMQEQQRSLDIGNQMSTSEETKVAHS
SQ  GSQQIDKVFNNIGADLLSGSESENREDGMQGKQKRGSLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPIAPIKQTKDLT
SQ  DTLMENMSSLTSLSVSTPKISASSTFTPVPSTGLGMMFSTPIDNTKRNLTNGLNANMGFQTSGFSMPVNPNQNFFSGTGT
SQ  AGVTTMSLGAPPTMSNFSPLTIPPASVKQPQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFAPPQGSPVMGSA
SQ  AMGTQGNVMGQAAFGMQGNPFFNPQNFAQPPPTTMTSSSSASNDLKDLFG
//
ID  Q6PGD0;
PN  All-trans retinoic acid-induced differentiation factor;
GN  Atraid;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region. {ECO:0000250|UniProtKB:Q6UW56}.
DR  UNIPROT: Q6PGD0;
DR  UNIPROT: Q3UAH4;
DR  UNIPROT: Q810Q3;
DR  UNIPROT: Q9DD14;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DE  Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030154;
GO  GO:1903363;
GO  GO:0033689;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPG
SQ  PNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCP
SQ  ENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS
//
ID  P32767;
PN  Importin beta-like protein KAP122;
GN  KAP122;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10617640}.
DR  UNIPROT: P32767;
DR  UNIPROT: D6VUC1;
DR  PDB: 6Q82;
DR  PDB: 6Q83;
DR  PDB: 6Q84;
DE  Function: Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of the complex composed the large subunit (TOA1) and the small subunit (TOA2) of the general transcription factor IIA (TFIIA). Required for the nuclear import of the RNR2-RNR4 heterodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR). May play a role in regulation of pleiotropic drug resistance. {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:16432237, ECO:0000269|PubMed:1882553, ECO:0000269|PubMed:18838542}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-10420,EBI-13044; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-13044,EBI-20254; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-13044,EBI-14372; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-13044,EBI-18981; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-13044,EBI-18986; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-13044,EBI-6314; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-13044,EBI-8627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-13044,EBI-8603; Score: 0.35
DE  Interaction: Q04062; IntAct: EBI-13044,EBI-15944; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-13044,EBI-11191; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-13044,EBI-25128; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-13044,EBI-9890; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-13044,EBI-3242; Score: 0.44
DE  Interaction: P50085; IntAct: EBI-23530,EBI-13044; Score: 0.35
DE  Interaction: Q00955; IntAct: EBI-4814,EBI-13044; Score: 0.27
DE  Interaction: P39925; IntAct: EBI-2317,EBI-13044; Score: 0.27
DE  Interaction: Q06625; IntAct: EBI-37861,EBI-13044; Score: 0.27
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0006606;
GO  GO:0008361;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSIHEVVALIEELYSPHPKHDVNQIQQSLQSIQKSEQGFHLANELLSDDKYSANVKYFGALTLTVQLNTRGENDYETLW
SQ  NVFRSNLLYLTKFSTLYVSNPNMYGQSLIIIKKLMSNLSLIFTKINDPQLNNAGNENMIKQWNNPINTFIQLMSVQNQNI
SQ  NADQLLLDSINCSLTYEQLSQFVSLSQKHNELALTFTEVIVEDLTKFQTKRHSMSQIHEVVHEHLYISTMALINLNLTAQ
SQ  AVFNPTVFDCITAWINYISLTRSVSSSGRMDLSEIFQNLIDLMYQSTEGSDGYENAEKILTIFGNVFANDPLLMSYDLRQ
SQ  QIECIFLGVVRPDSGITDISNKNSWMLQYMNYLVTNDFFSELKELAICIVDFLQINTLSVCNKLFTNIQAADNGQVQDEY
SQ  IQEYIKVLLQMTNFPLTPVLQEFFSVRMVDFWLDLSDAYTNLASETLRPNSIELSTQIFQQLINIYLPKISLSVKQRIIE
SQ  EEGESTSVNEFEDFRNAVSDLAQSLWSILGNDNLTNVLIDGMGQMPAASDETLIIKDTDVLFRIETMCFVLNTILVDMTL
SQ  SESPWIKNIVDANKFFNQNVISVFQTGFQTSASTKVSQILKLDFVRTSTTLIGTLAGYFKQEPFQLNPYVEALFQGLHTC
SQ  TNFTSKNEQEKISNDKLEVMVIKTVSTLCETCREELTPYLMHFISFLNTVIMPDSNVSHFTRTKLVRSIGYVVQCQVSNG
SQ  PEEQAKYILQLTNLLSGSIEHCLASSVQLQEQQDYINCLLYCISELATSLIQPTEIIENDALLQRLSEFQSFWSSDPLQI
SQ  RSKIMCTIDKVLDNSIYCKNSAFVEIGCLIVGKGLNLPDGEPYFLKYNMSEVMNFVLRHVPNCELATCLPYFVYLLEKLI
SQ  SEFRKELTPQEFDFMFEKILLVYYDAYIINDPDLLQMTIGFVNNVLDVKPGLAIGSKHWTSFILPQFLKLIPSREKFTIV
SQ  AVAKFWTKLINNKKYNQEELTTVRQQVSSIGGDLVYQIMYGLFHTQRSDLNSYTDLLRALVAKFPIEAREWLVAVLPQIC
SQ  NNPAGHEKFINKLLITRGSRAAGNVILQWWLDCTTLPNYQG
//
ID  A0A096MK47;
PN  Muscular LMNA-interacting protein;
GN  Mlip;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
DR  UNIPROT: A0A096MK47;
DR  UNIPROT: D4A3C4;
DR  UNIPROT: Q569A0;
DR  Pfam: PF15274;
DE  Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy (PubMed:22343712, PubMed:26436652). Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD (By similarity). {ECO:0000250|UniProtKB:Q5FW52, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0042383;
GO  GO:0005521;
GO  GO:0003714;
GO  GO:0010614;
GO  GO:1903243;
GO  GO:0000122;
GO  GO:0045944;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5FW52};
SQ  MEFEKHEQGNALKKNEKLEERVTFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYV
SQ  FIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTT
SQ  SEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSA
SQ  QLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSH
SQ  GSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKS
SQ  LSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSL
SQ  ADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRH
SQ  SDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSL
SQ  PVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVEHSSDSP
SQ  SRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDS
SQ  SGLFSEQ
//
ID  P0CM10;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P0CM10;
DR  UNIPROT: Q55XH5;
DR  UNIPROT: Q5KMF9;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYC
SQ  HGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNG
SQ  PGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV
//
ID  P0DPK0;
PN  Protein CUSTOS;
GN  custos;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25157132}.
DR  UNIPROT: P0DPK0;
DE  Function: Essential for Spemann-Mangold organizer formation and subsequent anterior head development in the embryo. Inhibits canonical Wnt signaling pathway by antagonizing nuclear import of beta-catenin (ctnnb1) during embryogenesis. {ECO:0000269|PubMed:25157132}.
DE  Reference Proteome: No;
GO  GO:0005635;
GO  GO:0007275;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRRGTQKSDSDSSDEDLDRFREAAWVPPGAHQKVSDEQNEKIALPSLRVRPDCHEHDGNELQTTPEFRSHVAKKLAA
SQ  ILDSSIREVSQNEAVHISKAGNGDSEDEGFRLFRTSLPGEAGIVTSTIPRRKLASSSSEDSEEEQQRCREAAVSACDILR
SQ  HSTLQQEPQSTPSNVCDNQPPKKKRKKKKKDRGDTSQINSVEETMHIEPGKNELQAKRKKKKKQKLEMAHCDELGNE
//
ID  Q9LTB0;
PN  Exocyst complex component EXO84B;
GN  EXO84B;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19895414}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Note=Localized to globular structures in the perinuclear region (PubMed:19895414). During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:20870962}.
DR  UNIPROT: Q9LTB0;
DR  Pfam: PF16528;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. Probable component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi- independent import into the vacuole. {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:23944713}.
DE  Reference Proteome: Yes;
GO  GO:0005618;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0005576;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0008104;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAKTARSKATPTKENGVRVEEGLSLFKSDKFDADAYVQSKCSINEKDIKQLCSYLLDLKRASAEEMRRSVYANYPAFIR
SQ  TSKEISDLEGELSSIRNLLSTQATLIHGLADGVNIDDDKVSDESLANGLLNFEDNGLSDLEKWATEFPDHLDALLAERRV
SQ  DEALAAFDEGEILVSQANEKHTLSSSVLSSLQFAIAERKQKLADQLAKAACQPSTRGGELRSAIAALKRLGDGPRAHTVL
SQ  LDAHFQRYQYNMQSLRPSSTSYGGAYTAALSQLVFSAISQASSDSLGIFGKEPAYSSELVTWATKQTEAFSLLVKRHALA
SQ  SSAAAGGLRAAAECAQIALGHCSLLEARGLSLCPVLLKHFKPIVEQALEANLKRIEENTAAMAAADDWVLTSPPAGSRHA
SQ  STAFQNKLTSSAHRFNLMVQDFFEDVGPLLSMQLGSKALEGLFRVFNSYVDVLVRALPGSIEEEDPNFESSCNKIVQMAE
SQ  TEANQLALLANASLLADELLPRAAMKLSLDQTGQRTDDLRRPLDRQNRNPEQREWKRRLLSTVDKLKDAFCRQHALDLIF
SQ  TEEGDSHLSADMYVNIDENGEDVDFFPSLIFQELFAKLNRMASLAADMFVGRERFAISLLMRLTETVILWLSGDQSFWDD
SQ  IEEGPRPLGPLGLRQLYLDMKFVICFASQGRYLSRNLHRGTNEIISKALAAFTATGIDPYSELPEDDWFNDICVDAMERL
SQ  SGKTKGNNGDVHSPTASVSAQSVSSARSHGSY
//
ID  Q3MHM8;
PN  ADP-ribosylation factor-like protein 6-interacting protein 6;
GN  ARL6IP6;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q3MHM8;
DR  Pfam: PF15062;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVESGRRSAPLRRRPGTPVPFARPAYSVFSQGDSWGEGEVEEEEGCDQVARDLRAEFSAGSSSKLRKDPVLQPDGDGS
SQ  PVLPDKRNGIFSADAGGKALARRWPVQVLSILCSLLFAILLACLLAITYLIVKELHAENLKNEDDVNTGLLGFWSLLIIS
SQ  LTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKMTGHSFHMGYSMAILNGIVAALTVAWCLM
//
ID  Q6ZMK1;
PN  Cysteine and histidine-rich protein 1;
GN  CYHR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250}.
DR  UNIPROT: Q6ZMK1;
DR  UNIPROT: B3KSX0;
DR  UNIPROT: D3DWM3;
DR  UNIPROT: Q9BSF6;
DR  UNIPROT: Q9BSU6;
DR  PROSITE: PS50145;
DR  OMIM: 616635;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O00629; IntAct: EBI-3908824,EBI-396343; Score: 0.56
DE  Interaction: P30838; IntAct: EBI-3908824,EBI-3905126; Score: 0.37
DE  Interaction: P45984; IntAct: EBI-713568,EBI-3908824; Score: 0.37
DE  Interaction: P61086; IntAct: EBI-473850,EBI-3908824; Score: 0.51
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0008270;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPKPGAEWSTALSHLVLGVVSLHAAVSTAEASRGAAAGFLLQVLAATTTLAPGLSTHEDCLAGAWVATVIGLPLLAFDF
SQ  HWCTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCCRNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQ
SQ  DRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGSELMEILDGMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYR
SQ  TDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTLSFQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHF
SQ  VFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLFQIQK
//
ID  Q54DN3;
PN  Exportin-7;
GN  xpo7;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q54DN3;
DE  Function: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0006611;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSIQSEQDFFKFEELCKDFYLKPEETIKIDDILHQYFLNPNFLIEYKQILSFTKNSYVVAQVIRGLIKCVTSFWTSLTPN
SQ  QKNDMSKSIEHHCIGLRILKDIISEFNEYIGEHLTVLQHRNISISLRDNILLDIFCISLESLNYALANSMDEKFKSIKEL
SQ  ALDLSYSCLSFDFIKTTSIDSSEEILTVQIPSQWKSTFDENNPLELFFKIYKQYHSTKSLECILQIVSIRRSFFTTEDER
SQ  VKFLASIVQYTTEILKSNIGFNEPNNHLVFSRVIERLKTNYHLNNLVTVVGYNDWISNLSTFTIDTLKNPQFSPNSIYFL
SQ  LTLWAKLVSSIIYVKGDPSKTYLEKYSPIIMESFINSKIDNSYSDEEDEHLMDYEKMVEILEGIPHLGRITYQATCRQII
SQ  LLFDSISSKFLNETNPTQLEVYERQCAWLVYIIGCLILGRTSINSSEEHDKIDGELSVRVFILIGYNDKKLSAESNTQYQ
SQ  YRTSRISLELSFIYFMQNFRRIYIGENSISSSKIYQRISELSGPTDHTSVLFSIVQKIGFNFKYWAENDEIIKKSLDMFW
SQ  ESVNGHSTSKMLIDNKITKDILKTHSSQVFPFLEKNSNPRNRTSLYKTIGKLLFTDENMGFFDEFIAPFDDTIKHLLNIS
SQ  TPEQFRTEEIKRKVIGLLRDLRGIITSANSKRSYLLFFEWIHLNFSEVLIKIINVWVDSPEVTTSLLKFISEFVFNRQSR
SQ  LIFDSSSANGFIIFRDTSKILVSYASLILKANISKQDLYKFKIKGIQTSMLLFTRCLVGGYCNFGVFELYGDPSFTSAID
SQ  YIFQLCLSVSLDELMSFPKASKAYVTMLEALCLGHTLSIIQLNQQYFIHIMKSLHRCLDSQDVTMSSSSCTSIEKIITVC
SQ  YYHLKKKNSQCLQAIHQNFFSNSNILYEIIDKIISIIIYEDNFNQFMFSKLLLTCIIFHQDTFTTLKQKYIHSFNSQCPE
SQ  KVEKAFVQLMENTLDNLETKNKDKFTSNVSIFRKEMKLISSSTGRYL
//
ID  Q6FS52;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q6FS52;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEVDVPELLFERVWLQVDRDRDGFIYAKQMPSFITQCEQVIKDTVNTNKTDFHMTRFKNRLKLPLLPKLHMDLIDAFAK
SQ  ETPYYKIYKESFSDMLNKLTGNNFSTVINKIFEDCDGFPASFISALEVKADVKSSPRSKADSLGSPIKVDLLRNLKPQEE
SQ  PETPRRINRKYKSLELQLESMKRELEDKEKTIMNNERNLTELRSTISKLKEKYDLLSEEYEQRHIHGGNNGTAIKHDVVI
SQ  GELKSRLQEQNRLIRILQEQIQFDPQLKRETRVHDNKSKNNTFNGAIAYVIPFLLFIFVIRSLITKEDIGDATMALPWWE
SQ  RNNLASRLAWYFRDVFSNDSAKFLESDAYDKVFGIH
//
ID  O13999;
PN  Meiotically up-regulated gene 155 protein;
GN  mug155;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13999;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPTSGCSKDDTIQKQNRRHNTVDNKQEKLPLSIEIFLNKQINKISFDTIRSKQNCRLKEIYCRLKIRCRLKKKFIKSLS
SQ  KKIISYHFISFHTIVVLLLLPPFSHLLVLVYPSVFTTAFYHQKWALRLNPCLPTYFFHRQRQCVTLLIRNANENMRARRV
SQ  NSVMLTKPKQFLFLLEFITLFIFTYCL
//
ID  Q8BFW9;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  Slc2a12;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:23041416}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q8BFW9;
DR  UNIPROT: Q14B60;
DR  UNIPROT: Q3UPR6;
DR  UNIPROT: Q8BZB7;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-independent facilitative glucose transporter. {ECO:0000269|PubMed:23041416}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005351;
GO  GO:0046323;
GO  GO:1904659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTC
SQ  HEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIA
SQ  EIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKV
SQ  LRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAA
SQ  SLASTGVGVVKVVSTIPATLLVDHIGSKTFLCIGSSVMSASLLTMGIVNLNINMNFTNICRSHSLLNQSLEEFVFYATGN
SQ  LSISNSSLREHFKRITPYSKGSFMPMGNGMEPKGEMTFTSSLPNAGLSRTEHQGVTDTAVVPAAYKWLSLASLLVYVAAF
SQ  SIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGVNLLISLTFLTVTDLIGLSWVCFIYTIMSLASLAFVVLFIPETKGC
SQ  SLEQISVELAKANYVKNNICFMSHHQEELVPTQLQKRKPQEQLPECNHLCGRGQSQRPSPDT
//
ID  C5E2E7;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C5E2E7;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDTERHATLLLDLVWPEVDEKAQGFIYAKDFPLVVSRMEEILNRGKLERDRAQLVSETGREILRKFGSDQEFFKVYKEDF
SQ  RELFDGLVGTSFKSAVKSCAGDGVLDRLQDSQAVDGIQDEKTSSHALQEEVMRLREQVRVLSSKNDEKDREITARDEIIA
SQ  DLQGKDASPAGSPRSLQRMRTLQARVTSLEDELSFRDEVIREKDRELLNLTKRVGEFKDKYQFLEREFQFYKGHREQKSP
SQ  DSIKEATRHEFIISELRRKITEQSEIIGQMRMQVEAKPGALHPQGIGSTAGLPLNLPLRLVLRLIIGAILAYLAFDIGIR
SQ  SLKAVGGLFGSSSPATLTPKSELSWWEQNTLLSKLLWFFKDLFDTYNLDAGRDEVVSANYDKLFGV
//
ID  Q755A9;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q755A9;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWREEAREQLRRGRCCFAAASVVSTAKHNKSLGNCTHGSGVMTEAEGILNNVWDAVDSKQQGFIYAKDMPDLVGRFGQFL
SQ  AQSLTSRANDEAIAAFASEKPFYKLDKEQFKSTFQTLVGTSLQTAVELAGHGEPRPRLFGAIRRASATGDEQAREELERK
SQ  SAELSRVRDELDEWKSKYQFLEREFLFYQTHHENSVDSTQHEFIISEMKRTIEEQTRMIGQLRRQVQGGTQVLARAGKRA
SQ  SPVDVFMYVSRQGLLLLMRMPKAAFLLLLLGYFVWYTVMGGAVQGPDPSVALPEPPKQPWWEQNNIISALYWYLTDTFEP
SQ  SQRINDTVNDNYNSLFGL
//
ID  Q6CS73;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q6CS73;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKQISKSTQYKPSKSTLVSAKLFSMNRTESTRLLDRAWSVLESGSDGYVYAKDIPEIISFIDRELPSKLTTQSNDKVIE
SQ  SWVNNDPMKTLSKEQFLEAFSMLVGTSFDTAVQIAMQSDILTPTRRGASLFGSYRRSSNDLEQVLPAEQIKALKRELQEW
SQ  KDKYTFLEHEFQFFLSQEKKNPEVIDNTKHEFIISELNRKLREQDEAIEDLKSQLDYGLVPELKDKTNWIKALQRKAYNY
SQ  LLPKILICLLLLLLYYCLAAKILFTKSSSTDDVPSFIRQQSWWERNKILSRIQWYFKDRIENNVVRNSSEVIQNYNSVFG
SQ  IH
//
ID  C5E006;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C5E006;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFDKSSSSLVLDLAWNQVDKKNQDFIYAKDFPALIMSIEEILSRGQQTPLAFLSNTGKSVIDTFAREKEFFKIYRDEFK
SQ  EIFHGLVGKTFKDTIEGTNVSRSVLDEQGQEPDVSTTPTRQQRSSPRKVNRLLKNLETRVASMKDELKFKDEILAEKDRE
SQ  LIQLTRKLSDYKDKYEFVQRQFSFYKDHGESPRRNSSESEQLNLEQNASTKHEFIISELKRKLQEQTLAISNLKEQLQRG
SQ  EGAGVLYTNYSKRYNPLHNDGPMVLVLATLVFLTIILLIGSMIWVTGGKDDSNSFSQYSWWENNSLLSRIGWFFRDWSDT
SQ  GVDYVNFEPSSDAYERIMGIRRI
//
ID  Q91W69;
PN  Epsin-3;
GN  Epn3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q91W69;
DR  UNIPROT: Q9CV55;
DR  Pfam: PF01417;
DR  Pfam: PF02809;
DR  PROSITE: PS50942;
DR  PROSITE: PS50330;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0019897;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990175;
GO  GO:0008289;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTL
SQ  LDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMG
SQ  IGSGQLGYSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAERPVPPASHRDEDLQLQLALSL
SQ  SRQEHEKGVRSWKGDDSPVANGAEPAGQRRQRDREPEREERKEEEKLKTSQSSILDLADIFAPAPALPSTHCSADPWDIP
SQ  GLRPNTEPSGSSWGPSADPWSPVPSGNALSRSQPWDLLPTLSSSEPWGRTPVLPSGPPIADPWAPSSPTRKLPSTGADPW
SQ  GASMETSDTSALGGASPFDPFAKPLESTEPKESRDSAQALPTGKSPSTVELDPFGDSSPSCKQNGMKEPEALDLGVLGEA
SQ  LPQQPGKEARPCRTPESFLGPSASSLVNLDSLVKAPLAARTRNPFLTGLGVPSPTNPFGAGDQGRPTLNQMRTGSPALGL
SQ  PPGGPVGAPVGSMTYSASLPLPLSSVPVGATLPASVSVFPQAGAFAPPPASLPQPLLPTSGPMGPLPPQAGTNPFL
//
ID  Q5XTS1;
PN  Calcium-independent phospholipase A2-gamma;
GN  PNPLA8;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15629460}.
DR  UNIPROT: Q5XTS1;
DR  Pfam: PF01734;
DR  PROSITE: PS51635;
DE  Function: Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0016042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSINLTIDICIYLLSNARNLCGKHRSKQLHLVCSPNHCWKIRHVSLQRGLHPHKVRCKWTKSETHSCSKHYYSPSNHGLH
SQ  IGILKLSTSAPKGLTKVSIRMSRIKSTLNSVSKAVFGSQNEMISRLAQFKPSSRILRKVSDSGWLKQESIKQAIRSLKKY
SQ  SDKSTEKSPVPEGRNHIIDKEDDIGKQSLFHYTGNITTKFGESFYFLSNHINSYFKRAEKMSQDKENSHFQEKSELEGKK
SQ  VEEGKSSSLDPGILTSQADKPDPKSSAGTMDKATSPSGTPESLPISTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKYD
SQ  SKSQAEEQEEPAKSEPAGSKDKTVEEKKHLSLQREKIIARVSIDNRTRALVQALRRTADPKLCITRVEELTFHLLEFPEG
SQ  KGVAVKERLIPCLLRLRQMKDETLQAAVREILALIGYVDPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPVHQLF
SQ  DYICGVSTGAILAFMLGLFHLPLDECEELYRKLGSDIFSQNVIVGTVKMSWSHAFYDSQTWEKILKERMGSALMIETARN
SQ  PMCPKVAAVSTIVNRGSTPKAFVFRNYGHFPGSQSHYLGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPS
SQ  ALAMHECKCLWPDAPLECIVSLGTGRYESDVRNNTTYTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCEN
SQ  IPLDESRNEKLDQLQLEGSKYIERNEHKMKKVAKILSQEKTTLQKINDWIKLKTDMYEGLPFFSKL
//
ID  Q86D96;
PN  Guanine nucleotide-binding protein subunit alpha-1;
GN  GA1;
OS  5722;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Endomembrane system; Lipid-anchor. Note=Predominantly perinuclear.
DR  UNIPROT: Q86D96;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0012505;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0007186;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCSASKPSEPSNAKLPSAPVPKKVEQVPEPKPEPQPQPEPQPQPEPPKPAEPAPAPAPAPEPQKPAEPAPKVVAVEDDT
SQ  NEAYGLLLCGAGESGKTTFTRQLKLRYLNGFNEKDCRDFLRTIRGNLVETMQLLLVWLEHNNIEIEDSELSSMAQDIIDV
SQ  DPQDCEFNEELVEKLKALWENEQIKKAFEHKDETAVPDHMPYFFAKIDELAGEDYIPSNEDVLRARIRSIGIEAITFDLQ
SQ  GARIRIFDVGGQKSERSKWANVMNQVEGVIFCVSFAEFDKPMFEDQNVLRINDSLEIFGNITHQEKFSNSPIFLVCNKFD
SQ  VFTEKIKNTDAFVKIFPEFSGDSHNPEACADYLIQRFLDKAAPLSEDRPIIQYKIVALNGDQVVETADAICKFISDKYYQ
SQ  DA
//
ID  P39996;
PN  Glutathione transferase 3;
GN  GTT3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P39996;
DR  UNIPROT: D3DLN3;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P48363; IntAct: EBI-13239,EBI-22308; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-8632,EBI-22308; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-8659,EBI-22308; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-22308,EBI-10267100; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-749265,EBI-22308; Score: 0.56
DE  Interaction: P00359; IntAct: EBI-22308,EBI-7218; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-22308,EBI-6333; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-22308,EBI-2218; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-22308,EBI-26307; Score: 0.37
DE  Interaction: Q02159; IntAct: EBI-22308,EBI-19749; Score: 0.37
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0034399;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTKSTFSRWKKADLIDLANKLEIDGFPNYAKKSDMIDYLESHLNHLEKPVDFKDDYPELRSFYESMTVDQSKDERNEYG
SQ  SGSGNGSGSGSCDTATNDSDLEKAYIKEDDDEKPQSGDETSATKPLSSRNANSNAKTNFNLLDFSTDNDSSTSAFTKFKF
SQ  NFQEYLSDIRYQTQKLNENVQDYLSTISAVDTIFSLLEFSFLVRNILAAGQPTSSSSLASSLEAAVAAHNKYQYTLDFCL
SQ  PILTWLLFFRGIPTLVSYYINFIRYDLNIELDPMTFNLTKFLISLAIFKTCNNKNIDFHSFRCVNQLWTQLCTVNRSLGM
SQ  VPLVFSMVSCLLTLYVL
//
ID  Q9HDX1;
PN  Uncharacterized transcriptional regulatory protein PB1A11.04c;
GN  SPAPB1A11;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9HDX1;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
GO  GO:0006351;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIAAVEKDAVPRKRRVISQVSQACIRCRQKKIKCSGEKPSCQACSNNKVECIWPDRPNMRGKKPSSAARTLSPLTGIVQP
SQ  YLGSHPFSPTILSPSSPNMDFTYSINSFGDYQKQLRLPTSRKLLQLWDIFLKTSYTELFGIFNKAQITSQIASDTAPPVL
SQ  VLCICAHAARFSQEEVNRFKSSTAASDYYANQAFSLLPCRFQDISLTNITCLLLLCLIELGSCRGAKAWLLLGMALRMVD
SQ  SLDLGNEINDNPLTMGSNTVSWTEAEQKRRVYWACFFVERLLSTGYMAPSKLRSLSLSLQKTSIQLPCPEPNFLFNQPIL
SQ  TELFDGSLPENTQSDTTSMAPYQRSLQLEFMTGSLIRLSNLWSEISRWALCGGYTKDITPPWLNQSQFHRSFELLKAWHE
SQ  NLPPRAVWSYTNYSAYSSPGESAGACYTFMHLLYHTTLTYLLRNVLDLFPEKSRQKSKLFSSVSQRFGQQPPTVWMDMIL
SQ  DQVITSADFITKLSKDPLNYIMSPFVGFSILTAATIHMLLKFCVVNIDQNYISSSRLVHVDHQILQDRSKYWKINQAMLV
SQ  TLQRLYNFYRFQYLEEQSLYNFKIPGFPLCILEYGIVEDQSMKSNPDLNSFSKELFSRGTNELLNNGDDTQSGNSTPAMG
SQ  VSEIRTDTILDEEVPVDPLITSILDDGRWWEEMFGSERKAGFKETVFEDMNGRSIRL
//
ID  Q1ECZ4;
PN  Protein CASC3;
GN  casc3;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a xpo1/crm1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: Q1ECZ4;
DR  UNIPROT: Q7T1P0;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003723;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRRRRRASQDSEEEDESASGSESGRSFSASRKTRGREPEPVESPAERVAAKSDDESECVSEDGVGEAVLSDYDSAD
SQ  LEENGSHTEGGEEEEEAEHFSEEEASRPAAESKPVADAPTEELVEGEERDESVKEVKADEKGNLAGERQSGDGQESTEDP
SQ  ENKGSKGQKLDDDEDRKNPAYIPRKGLFFEHDVRGQATEEERPKGRNRKLWKDEGRWEHDKFREEEQAPKSRDELIAFYG
SQ  YDIRNGTGPSDGRSYRSRKPRHAGSPSREPRRYREGDKSVRSSWQGPPPGHRNAPQSVTVQSGQPLAPLSAPKPSGRPST
SQ  QPPQRSFQGSRAPSAPHRTEGRGPSKPSLDGAPLRGPRSQPVEGERGPRLRGRSSHAVHADRSPSLVVEDICSEEEEEEG
SQ  EIPTATTTYTAHHYKTEKERVPSPRKQDSGMVMEGGSAAGQVRELSPPQERQVEKKSYSRARRATRTRPSDLSKQASLDD
SQ  SSSAVQQAPVAAKSESWQEQSEAGTQSGLTGLDQDLARLSLTGQNWAQNPPSYLQAEMRGIRGSMHMAGGPPQYGNMEDM
SQ  GVGGGRAKRYSSQRQRPVPEPAPMHIGVMEGHYYEPMTFQGPIYTHGESPAALPPQGMLVQPEMHLPHPTHPGLHPHQSG
SQ  GPLPNPAIYAAPPVSLSPGQPPPQQLLPPPFYPPPGVMTFGNTNYPYPAGGTLPPMYPNPQAQSQVYGGVTYYDTIQQQA
SQ  QPKRSPPRRSSNPVTVRPPPPEDQSRKAAEEIRS
//
ID  O14253;
PN  Nuclear cap-binding protein subunit 1;
GN  cbc1;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P34160}. Nucleus {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14253;
DR  Pfam: PF02854;
DR  Pfam: PF09088;
DR  Pfam: PF09090;
DE  Function: Component of the CBC complex, which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. {ECO:0000250|UniProtKB:P34160}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005845;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0000340;
GO  GO:0000339;
GO  GO:0045292;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSYRGSTRPRKRTREGENYGFRPHRGNSQELLAARIKKDITFLADPRGNSVAADDINYVAMSLSREANDPETISTILDC
SQ  IQTTAFIIPVKIPHLATLIIRASLRVPLILEKAAAYFCLQYFTNLNSFLYYEAKVDLRMLICMSFALQPGTLKPLFSLLA
SQ  DAISKETKPSVWGDNFLRIILINLPYFIAANNDLGKKDFANEILDQCEIYVRHRKSSITLSNPLSIHDNLSEEELDLLYK
SQ  QLILSRENDFTFPYISQPWKFFESDFVHIVPVSPSIPEWTFQPTPQQNELPSFKRFFELFNNFEIRTTPDASDVAASIFR
SQ  DISVDVINHLEFNRVEAAQVLTDLDVYFTYKTFALRGTPVNELPNLDPSESRWKAEDIIVEAVLGELLGSQNTTYKPVYY
SQ  HSLLIECCRIAPKILAPTFGRVIRLMYTMSSDLPLQTLDRFIDWFSHHLSNFNFHWKWNEWIPDVELDDLHPKKVFMRET
SQ  ITRELILSYYTRISDSLPEELRCLLGEQPSGPNFVYENETHPLYQQSSQIIEALRLHKPLEELDIILQSEEIQNSETSAV
SQ  RLVMSCAYSLGSRSFSHALNVFEKHLNTLKHFSRKSLDSEIEVVDELFSFWKLQPFNAVMWLDKMLNYSIISITSIIEWL
SQ  IKQDVTIWSRSYTWSLVNTTFNKLAARLRRSVSNKEDSSLINEANEEKEIVTNLLLSALRALISENAENIWVSHWLNLML
SQ  KYVESNFLSVKKDTIEEANEPVQENTSEEQEDTKMQPVDAVDEQPSENNQTAADATNEEK
//
ID  G0S2G1;
PN  Protein ELYS;
GN  ELYS;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WYP5}.
DR  UNIPROT: G0S2G1;
DR  UNIPROT: G0ZGV2;
DR  Pfam: PF13934;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC). {ECO:0000250|UniProtKB:Q8WYP5}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLDFTHFPEVFPTDGPRPYDQHFVRQTETFRKSLDGVLFIDRVLGALGLPDAAKAYPPRGDAGLRALHQQVCSAKVSAHA
SQ  KLSVLYYLLLDHDEHRGSRSQLADALAEEVGLPANYQILMRGLWHMDRKEFKFALEHLAHPSLPAEFADEIITVLVRDGH
SQ  TTGDYSLPLAYYHAVRPVLQTSSALENLFAALARTSVTDALAFSRTYPDHGARQLLFERLVASVLEEHGSGQVAGRSASR
SQ  AKELVSLPLTGVEEKWLNDYLSTGEGRKSRSAKAVVQMRQVVTGRQKELGAVVGVRAGR
//
ID  P0CA01;
PN  p150;
GN  Ken;
OS  561445;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250}. [p34]: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250}. [p14]: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250}. [p37]: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000250}. Host nucleus {ECO:0000250}. Note=Nuclear at early stages of infection. Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (By similarity). {ECO:0000250}. [p150]: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (By similarity). {ECO:0000250}.
DR  UNIPROT: P0CA01;
DE  Function: Polyprotein pp220 is essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope (By similarity). {ECO:0000250}. The structural protein p34 is a component of the virus core shell. {ECO:0000250}. The structural protein p14 is a component of the virus core shell. {ECO:0000250}. The structural protein p37 is a component of the virus core shell. {ECO:0000250}. The structural protein p150 is a component of the virus core shell. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0019012;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNRGSSTSSRPPLSSEANLYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIKAISKI
SQ  GFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETICKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLSDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFID
SQ  NILTPTQKELDKLKTDEVDIIKILNDTNSVLGTKNFGKVLSYTLCNLGIAATVANKINKALQRVGLKVEQYLHSKNWAEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENNCAKKGGDGEKTPLDKRMEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGMKLVKEIALTPNITKLRDALSRINDMGTIALDLSLIGFYNNAAAREERETFLIQLTLVKNVLEELAKT
SQ  DPNFKNLYDSCFRLLQIIDFYTDIVQKKYGGGEDCECTKVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEVDWKATISAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRGVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQTVPMSPLQIYKTLLEYIQHS
SQ  ALSVGLKNLNQTQIGGQRVALAQTAEEASQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAGLYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRVIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEAVKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFIGPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVS
SQ  YQELIQQATNELKKEHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNTFRNNIKALDLDTIQKS
SQ  IIEWLRETQAANVNRANLIDWLGRRHGDISEIRNPGLVIKANDARLSEVYPDPTTDATAPLDRNLVTETLFAWFTRFVGI
SQ  PADGAVRPEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKLVQVRFPETSTAHVHLDFTGLISLIDSLMADTKYFLDLLR
SQ  PHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYILLTKPYNVLQLRGGAQRG
SQ  NAANIQINNNPEFSERYEQYGRVFSRLVFYDALIENSGLRVEQVALGDFRLSNLIRTNNAQEENALSFWTAVAPRAYANV
SQ  NDAANNLRRYRLYGSDYGIRNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINTFANGNFSQAVMELGYAHPDLARDNT
SQ  AFGHRGDPTEQSVLLLSLGLMLQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQY
SQ  TKVQLARPNLTALLGANNDSIIYYNNNNVPNTGLTVGQAALRGIGSVFRPDITLMPLGNAQNNTNDVVRKRLIAVINGII
SQ  RGSLTLANSAMEVLHELTDHPIYFETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFK
SQ  ILYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYIHAIQALRFIINIRSFKTVMTYNENTFGGVNL
SQ  IGEDRDDKPIITEGIGMNAVYSLRKTLQDVISFVESSYQEEQINNIHKIVSPRSQTRSLGSNRERERIFNLFDMNIMPIN
SQ  VNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLDTAAPQPDVAQVLNIPNRPPMNTREFMLKLLINPYVTVSITQ
SQ  YGNELLFRGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPGLAAGIQRGREQWGQPLSDYINQ
SQ  ALHELVRTIRIIPQNIRVLRNIMVKNQLIADLAAIREQLVRMRREVENMVQTPEIQNNPTPEVIAAAQTWTQQYRARVDF
SQ  LINFIGNAQQPNSLIQLIQNITPLTVRAQLTTVFIRHGLPVPDPDQALQTDDEATQWFMTNIINQPITMIIPFTDLADDL
SQ  RIFLETMERYVFNVPRWLGPSTGRVARVPVNMAPGNIRYRTSYTENNVLTYIAEQNQEEGPWSIVKQVGVGIQKPALIQI
SQ  GKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPNHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  Q9H7C4;
PN  Syncoilin;
GN  SYNC;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPM5}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern (By similarity). {ECO:0000250|UniProtKB:Q9EPM5}.
DR  UNIPROT: Q9H7C4;
DR  UNIPROT: B4DNK8;
DR  UNIPROT: B4DY58;
DR  UNIPROT: C9IY41;
DR  Pfam: PF00038;
DR  PROSITE: PS51842;
DR  OMIM: 611750;
DE  Function: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000250|UniProtKB:Q9EPM5}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TDR0-2; IntAct: EBI-11285923,EBI-11946508; Score: 0.37
DE  Interaction: P61604; IntAct: EBI-711483,EBI-11285923; Score: 0.40
GO  GO:0005829;
GO  GO:0005882;
GO  GO:0031594;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0030018;
GO  GO:0045103;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASPEPRRGGDGAAQAARKTRVEANSPLPKNSGSLNEAEALNPEVTLSSEGSLNLEDILYLEDTGDLDETLYVQETEKAE
SQ  EALYIEEAMQPDEALHVEEPGNPEETVCVEETTEPDRIQFVEGPVEPGKPTSPEHVVYEGETVTRAEKSNPEESLRAEQS
SQ  PSMEENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIR
SQ  LVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQE
SQ  SRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVR
SQ  QKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQG
SQ  AV
//
ID  Q54ED3;
PN  DnaJ homolog subfamily A member 1 homolog;
GN  dnaja1;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: Q54ED3;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for Hsp70 family members. Plays a role in protein transport into mitochondria and in the regulation of apoptosis via its role as co-chaperone (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0031072;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0006457;
GO  GO:0009408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKEKEYYERLGVKPDCTEDELKKAYRKMAVKYHPDKNQGPGKDAAEAKFKDISEAYEVLSDPEKRKMYDSYGSEGMKES
SQ  GFHASSAEDLFSHFFGAGGGGGGFSFGGGGGDDFGGFSFGNMGGMGGMGGMGGGHKKRRKGEDIEHEMNRSLEELYNGKL
SQ  VKISISRDEVCKTCKGSGSNKPGVTTTCPTCNGSRYVFQKKQVGPGMIQQVQTACHTCHGTGEKIKEEDKCKECKGKRVI
SQ  QGKKIVQFQVEKGTRDGERIMLQGQGSEYPGVPPGDVIITIREKPNVNFKRNGDNLIYTKRLKLLDSIAGSQFIINTLDQ
SQ  RKLWVNHEKGDIIKQGDMRYIENEGMPIKGTSRKGKLIIAFDIEYPSNLTNDDIEKLSKILPKAATPSVSKSDCKSVGLS
SQ  KVNFNTNEQSSHGGAGGAYQQHGGAYGHQKQQQQGFNPADFGAQFGGGGPQQAQQCQQQ
//
ID  A8XA40;
PN  Calnexin;
GN  cnx;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
DR  UNIPROT: A8XA40;
DR  Pfam: PF00262;
DR  PROSITE: PS00803;
DR  PROSITE: PS00804;
DR  PROSITE: PS00805;
DE  Function: Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death (By similarity). {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0051082;
GO  GO:0030968;
GO  GO:0007275;
GO  GO:0006457;
GO  GO:0009408;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLNRKWSFVFLTFLLVISVNANDDVFEDEDEASESGVEKDEFVPSNFVAPKLADTSKPNFFDYFPVGSKIGQTWIKSLAK
SQ  KDDVDSEIAKYNGEWSIGAPTKVSIEGDYGLIVKTKARHHAIAAKLETPFVFGSNKFIAQYDVKFEEGQECGGGYLKLLS
SQ  EGAEKDLASFQDKTPYTIMFGPDKCGASGQVHLIFRYKNPVNGTVSEYHAKQPASIGTAYWDDHNTHLFTLVVKPTGEYS
SQ  VSVDGKSLYYGNMLSDISPSLTPPKEIFDETDLKPEDWDEREQIEDETASKPDDWDENEPQNVVDESATKPYDWNEEENE
SQ  LIPDPEAQKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKPPTIKNPKYRGKWVRPKIANPAYKGKWSPRLIDNPNYFE
SQ  PKPFDGLAPISAVGIELWTMSENILFDNILITSSEQDASEIAKQTFYIKQQEEYRLAAATGSSNGIFQQIVDATNEKPWL
SQ  WAVYILCILLPLIAIGVFCFGKGSKPAPNFAKKSDTYSPDDDRVPNLVDDQEEEIIAEDEEDNQPGPSGTQNQPPIDEDE
SQ  QDEVEQQPSSSKTASSESSSAAEEEDNDHVVHENEPVQPTEEVAKKSPRVTGGAKRRTARRGD
//
ID  Q5RI56;
PN  Optineurin;
GN  optn;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
DR  UNIPROT: Q5RI56;
DR  UNIPROT: Q6P3H5;
DR  UNIPROT: Q7SXF4;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0007409;
GO  GO:0043122;
GO  GO:0051648;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGDISHPRGSGPGNLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLN
SQ  TMDVENEALKNQVKELEKSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKD
SQ  LSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEV
SQ  KNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKT
SQ  QDEKNNLNQLKDAYTKLFEDYSELQEEKKKRESCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISV
SQ  FQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQRRHVPRGANPQGPTAPNNLPG
SQ  GRGEWQQQNIPDHACPKCGEVLPDLDSLQIHIMDCII
//
ID  Q5RCJ3;
PN  Cullin-7;
GN  CUL7;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RCJ3;
DR  Pfam: PF03256;
DR  Pfam: PF11515;
DR  Pfam: PF00888;
DR  PROSITE: PS50069;
DR  PROSITE: PS51284;
DE  Function: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin- protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial- mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0031467;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0001837;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0000281;
GO  GO:0001890;
GO  GO:0050775;
GO  GO:0016567;
GO  GO:0007088;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHK
SQ  MLGEDGQVIGPSQESTGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDP
SQ  RVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGEGQCGEEGKAGEELGRLRDSQDTVAGASDLIRTRTQILLSLSQQEA
SQ  IEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEEWSGE
SQ  RGQLELEFSMAMGTLISELVQAIRWDQASDRPRSSARSPGSIFQPQLADVSPGLPATQAQPSFRRSRHFRPRSEFASGNT
SQ  YALYVRDTLQPGMRVRMLDEYEEISAGDEGEFRQSNNGVPPVQVLWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQG
SQ  AVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDSEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDE
SQ  ILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNPAYPSLLEAQEDVLLEAQAQAKDSEDAAKVEA
SQ  KEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRI
SQ  LKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELA
SQ  QELRDMVFKCEKHAHLYRELITNILGGCIQMVLGQIEDHRRTHRPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSN
SQ  PHRASKLTDRNPKTYWESNGSAGSRYITLHMRQGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSA
SQ  SRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLETLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLH
SQ  LSSRLNGALRQEQNFADRFLPDNEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAF
SQ  FSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCRRAVVEKQVNNFLTSSWRDDDFV
SQ  PRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCL
SQ  QAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQE
SQ  LLKLEDTEKKIQVGHGASGKEHKSEKEEEAGAAAAVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHCWPVASICHTLN
SQ  PRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLA
SQ  LSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEEGRNLEKRRNLLNC
SQ  LIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVP
SQ  VTVMEPHTESLNPGSSGPNPPLTFHTVQIRSRGVPYASCTATQSFSTFR
//
ID  Q08CK7;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  igf2bp1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
DR  UNIPROT: Q08CK7;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta- actin/ACTB mRNA translation in polarized cells, a crucial process for cell migration and neurite outgrowth. Promotes the directed movement of cells by fine-tuning intracellular signaling networks and enhances the velocity of cell migration (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070937;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003730;
GO  GO:0051028;
GO  GO:0003407;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNEKVTAEDLVKTFEDYKIPYSGQFLMKTGYASVDCPDDQWAMKAIETFSGKVELHGKRIEVEHSVPKKQRT
SQ  RKLQIRNIPPHLQWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYGTREQARQAIQKLNGYQFDNNALRVSYIPDENSE
SQ  VDSQRGPDNGRRPGYGPRGTSRQMSPGSGIPSKHQHADIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENA
SQ  GAAEKPISIHSTPEGCSAACRMILEIMNQEAKDTKTADEVPLKVLAHNNFVGRLIGKEGRNLKKVEQDTDTKITISPLQD
SQ  LTLYNPERTITVKGSIEACCLAEQEIMKKVREAYDNDIAAMNQQTHLIPGLNLGAIGLFPPSSAMPPPALGNSVPGPPYG
SQ  PMGASEQETVHVYIPAQAVGALIGKKGQHIKQLSRFAGASIKIAPAEAPDSKMRMVIVTGPPEAQFKAQGRIYGKLKEEN
SQ  FFGPKEEVKLETHIKVAAAAAGRVIGKGGKTVNELQNLTAAEVVVPREQTPDEHDQVIVKIIGHFYASQLAQRKIRDILT
SQ  QVKQQQKGGGMGTPQGPHPQGMTELGSPQGLAQEPRRK
//
ID  A7Z035;
PN  Clathrin interactor 1;
GN  CLINT1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans- Golgi network (By similarity). {ECO:0000250}.
DR  UNIPROT: A7Z035;
DR  Pfam: PF01417;
DR  PROSITE: PS50942;
DE  Function: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030136;
GO  GO:0005798;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030276;
GO  GO:0008289;
GO  GO:0006897;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVY
SQ  KSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYV
SQ  GVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKA
SQ  RRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSLKTSVPSS
SQ  KSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGNFPSQVTATSGNGDFGDWSAFNQAPSVPVAASGELFGSASQPA
SQ  VELVSSSQPALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQPLQNVSTVLQKPNPLYNQNT
SQ  DMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNMMTQSFGAVNLSSPSNMLPVRPQTN
SQ  PLMGGPMPMSMPNVMTGTMGMAPLGNSPMMNQSMMGMNMNIGMSTTGMGLTGTMGMGMPNLAMTSGTMQPKQDAFANFAN
SQ  FSK
//
ID  Q9EST1;
PN  Gasdermin-A;
GN  Gsdma;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P57764}. Cell membrane {ECO:0000250|UniProtKB:P57764}.
DR  UNIPROT: Q9EST1;
DR  UNIPROT: A3KFN3;
DR  Pfam: PF04598;
DR  Pfam: PF17708;
DE  Function: May promote pyroptosis. Upon cleavage in vitro of genetically engineered GSDMA, the released N-terminal moiety binds to some types of lipids, such as possibly phosphatidylinositol (4,5)-bisphosphate. Homooligomerizes within the membrane and forms pores of 10 -15 nanometers (nm) of inner diameter, triggering cell death. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q96QA5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0006915;
GO  GO:0042742;
GO  GO:0070269;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVHTDYTLLDVLEPGSSPSDPTDSGNFS
SQ  FKNMLDARVEGDVDVPKTVKVKGTAGLSRSSTLEVQTLSVAPTALENLHKERKLSADHPFLKEMRERGENLYVVMEVVET
SQ  LQEVTLERAGKAEGCFSLPFFAPLGLQGSVNHKEAVTIPKGCVLAYRVRQLMVNGKDEWGIPHICNDSMQTFPPGEKPGE
SQ  GKFILIQASDVGEMHEDFKTLKEEVQRETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQTLEGALDKGHEVTLEALP
SQ  KDVLLSKDAMDAILYFLGALTVLSEAQQKLLVKSLEKKILPVQLKLVESTMEKNFLQDKEGVFPLQPDLLSSLGEEELIL
SQ  TEALVGLSGLEVQRSGPQYTWDPDTLPHLCALYAGLSLLQLLSKNS
//
ID  O62275;
PN  Argonaute protein wago-4;
GN  wago;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}. Cytoplasmic granule {ECO:0000269|PubMed:29769721}. Cytoplasm {ECO:0000269|PubMed:29791857}. Note=Co-localizes with znfx-1 in P-granules in germline blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with znfx-1 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to cytoplasmic P- granules in germline blastomeres. {ECO:0000269|PubMed:29769721}.
DR  UNIPROT: O62275;
DR  Pfam: PF02170;
DR  Pfam: PF02171;
DR  PROSITE: PS50821;
DR  PROSITE: PS50822;
DE  Function: Argonaute protein which is involved in the endogenous small interfering RNA (endo-siRNA) pathway and is required for RNA-mediated gene silencing (RNAi) in the germline (PubMed:17110334, PubMed:29791857, PubMed:30728462). Interacts with secondary 22G-RNAs, which are RNA-dependent RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length with a 5'guanosine residue (PubMed:29791857). Also interacts with the mRNA targets of 22G-RNAs (PubMed:29791857). Associates with znfx-1 to mediate small RNA-directed transgenerational epigenetic inheritance of both germline- and soma-expressed genes (PubMed:29791857, PubMed:29769721). {ECO:0000269|PubMed:17110334, ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XVJ3; IntAct: EBI-2418617,EBI-326728; Score: 0.49
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0031048;
GO  GO:0060966;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPALPPVYTPSGAPSSVHAPPAVPPVPVPTQPLRSEYQTSNDACIKRLEELNIAPAAKLYPTPTEPGKCGVEAEIQTNVF
SQ  GIEMHQDSLFYQYSVNITTELKNGKEVTFTKKGKDDFVVTERHDKCCAILFRALGDYEEFFKTSDSCLIYDGQSILFSNV
SQ  DLFQGFREGAVKTKYMQLDGGEMDHKDLKSLPCIKLEVFPTKNPAVKFTREAVARRATDSNLDSVSLAYQQILELALTQP
SQ  CLRNTARYVVFDHGKMFFIDPLGEGFEKCDVVDVGDGKQVVPGLKKTINFIEGPYGRGRSNPSVVIDGMKVAFHKNQPIL
SQ  DKLKEITTQPVEHGLKGLEKDRCAAVIKGLDCYSTYGGRERHHKIEGIHHEGARNARFELNDGGSCTVAQYFEDVYNITL
SQ  RYPDTNLIVSKERGNINFYPMELLKISSHQRVQIPQLTSAQSQKTTKESAVLPDVRQRLILTGKNAAQISSDNEVLGKMG
SQ  VSVCEDPLMVKGRSIPAVKLANAEIGANPINVKDNKWRANRFTRPATAPNVWAMYVVGTASTRITLDTLKKFADEFAAMC
SQ  KSKGVNMPAPADISLIHMDAIESRLYDATKANCTFVFIITDDSITTLHQRYKMIEKDTKMIVQDMKLSKALSVINAGKRL
SQ  TLENVINKTNVKLGGSNYVFVDAKKQLDSHLIIGVGISAPPAGTKYAMENKGVLNPNVIGYAYNAQHNQEFSGDFVLNSA
SQ  SQDTLAPIEDIVMHSLNEYQKFHDGGLPRRVIVYRTGTSEGNHGSIMAYEIPLARAAMRDFSPDIQLVYIVVSKDHSFRF
SQ  FKPDLASLASRPQATSSTASRHSAMPAAPKAWDLNIAPGILVDSIVTNPACKQFFLNSHITLQGTAKTPLYTVLADDAKV
SQ  SMTALEDITYKLCHLHQIVGLPTSLPTPLYVANEYAKRGRNLWNEAVALNNVPTVSGPEADRLKELTKSICYKASGDLTG
SQ  RRVNA
//
ID  Q7Z6J2;
PN  General receptor for phosphoinositides 1-associated scaffold protein;
GN  GRASP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=Localized at postsynaptic membranes. {ECO:0000250}.
DR  UNIPROT: Q7Z6J2;
DR  UNIPROT: Q6PIF8;
DR  UNIPROT: Q7Z741;
DR  PDB: 2PNT;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DR  OMIM: 612027;
DR  DisGeNET: 160622;
DE  Function: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NHN0; IntAct: EBI-2801077,EBI-2806496; Score: 0.37
GO  GO:0030054;
GO  GO:0098978;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098685;
GO  GO:0030306;
GO  GO:0042802;
GO  GO:0030165;
GO  GO:0008104;
GO  GO:0099152;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTLRRLRKLQQKEEAAATPDPAARTPDSEVAPAAPVPTPGPPAAAATPGPPADELYAALEDYHPAELYRALAVSGGTLPR
SQ  RKGSGFRWKNLSQSPEQQRKVLTLEKEDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNG
SQ  LNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTL
SQ  ESVRSCLYGAGLLPGSLPFGPLLAVPGRPRGGARRARGDADDAVYHTCFFGDSEPPALPPPPPPARAFGPGPAETPAVGP
SQ  GPGPRAALSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGPGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL
//
ID  D3ZZ07;
PN  Cathepsin 7;
GN  Cts7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endosome {ECO:0000250|UniProtKB:Q91ZF2}. Lysosome {ECO:0000250|UniProtKB:Q91ZF2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q91ZF2}. Golgi apparatus {ECO:0000250|UniProtKB:Q91ZF2}. Nucleus {ECO:0000250|UniProtKB:Q91ZF2}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q91ZF2}.
DR  UNIPROT: D3ZZ07;
DR  Pfam: PF08246;
DR  Pfam: PF00112;
DR  PROSITE: PS00139;
DR  PROSITE: PS00639;
DE  Function: Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression (By similarity). {ECO:0000250|UniProtKB:Q91ZF2}.
DE  Reference Proteome: Yes;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005764;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004197;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0045930;
GO  GO:0051603;
GO  GO:0060707;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVAVFLAILCLRAALAAPRPDYSLDAEWEEWKRNNAKTYSPEEEKQRRAVWEENVKMIKWHTMQNGLWMNNFTIEMNEF
SQ  GDMTGEEMRMMTDSSALTLRNGKHIQKRNVKIPKTLDWRDTGCVAPVRSQGGCGACWAFSVAASIESQLFKKTGKLIPLS
SQ  VQNLIDCTVTYGNNDCSGGKPYTAFQYVKNNGGLEAEATYPYEAKLRHCRYRPERSVVKIARFFVVPRNEEALMQALVTY
SQ  GPIAVAIDGSHASFKRYRGGIYHEPKCRRDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGEQWGERGYMKLPRDQNNYC
SQ  GIASYAMYPLL
//
ID  Q810M5;
PN  Palmitoyltransferase ZDHHC19;
GN  Zdhhc19;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WVZ1}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8WVZ1}.
DR  UNIPROT: Q810M5;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that mediates palmitoylation of STAT3 and RRAS. Palmitoylation of STAT3 induces the homodimerization and transcriptional activation of STAT3, thereby, promoting inflammation and cancer. Palmitoylation of RRAS is linked to cell viability. May be involved in S-stearoylation of STAT3. {ECO:0000250|UniProtKB:Q8WVZ1}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0019706;
GO  GO:0018230;
GO  GO:0045944;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFLKDAVTLVKEPQQLPSIPLSWFPSSVFAAFNVTLLLFLSGLFFGFPCRWLVQNGEWAFPAITGPLFILTFFSLVSLN
SQ  FSDPGILHRGSTKEDPMTVHVVRVNQRAFRLEWCPKCLFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRLFMLL
SQ  VLSLCLYSGALLVTCLTFLFRTRHLPFSLDKGMAILVAVPAAGFLIPLFLLLLIQALSVSRAESSYESKCRYHPEYNPFD
SQ  QGFAKNWYLAMFAPLGPNYMSEVVCLQRPVGTAWIQEKTKPSPPRRPKHCRPGPPGPQHQPRRVPGKGPPGSGEAAALQE
SQ  MRRLPASVEKSPGGPRQPTAEPAAGDP
//
ID  P42674;
PN  Blastula protease 10;
GN  BP10;
OS  7656;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Secreted, extracellular space. Note=First detected in a perinuclear region, then in an apical and submembranous position just before its secretion into the perivitelline space.
DR  UNIPROT: P42674;
DR  Pfam: PF01400;
DR  Pfam: PF00431;
DR  PROSITE: PS51864;
DR  PROSITE: PS01180;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS00142;
DE  Function: Could be involved in the differentiation of ectodermal lineages and subsequent patterning of the embryo.
DE  Reference Proteome: No;
GO  GO:0005938;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0004222;
GO  GO:0008270;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLILFLSGLVSLVLCTLAAPTGDQKEIHTETPPPKKPSETTTPGALKTPQPEPKDEEPTPGAFQGDMMLTEDQQRESKE
SQ  AIDDEMTGRKKRKATIYESQRWPYKVIPYVISPSSSGQSSLIRNAMDHWEQNTCLRFEPRTSSHSRQLGHNAYLSFFRGS
SQ  GCWSYVGKAFNGEQQISIGNGCAYFGTIVHEIGHAIGFHHEQSRPDRDDYINVLYQNIQSGRQHNFAKYTWGRVTSRNVE
SQ  YDVGSIMHYGGYGFSSNGRPTITTRDPRLNSRLGQRIALSPADIELANLIYECDDIEDCAGANECLNGGYHDTECNCVCP
SQ  SGYNGDLCEDAVTTTRPDCSERFTEMTGVITSPNWPGRYEDNMACVYQIEGPPGSTIELTFTEMNIENHAACRYDAVEVR
SQ  KDDINSDGEKFCGNTLPAVQISSGNQMLISFTSDPSITGRGFRATYRIVILTTTQIPDTTTISTTTPVPTTTQATTDETV
SQ  VGSCGGSFGGTQGRVATPNYPNNYDNDLECVYVIEVEIGRRVELDFIDFVLEDETNCRWDSLSINLGDGIKIDMKMCGRE
SQ  YPAASLVSIGNNMELTLISDRSVTDRGFMADYRAIDL
//
ID  A9C3N6;
PN  Protein CUSTOS;
GN  custos;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:P0DPK0}.
DR  UNIPROT: A9C3N6;
DR  UNIPROT: A3KNH5;
DR  UNIPROT: A8WGJ3;
DE  Function: Essential for Spemann-Mangold organizer formation and subsequent anterior head development in the embryo. Inhibits canonical Wnt signaling pathway by antagonizing nuclear import of beta-catenin (ctnnb1) during embryogenesis. {ECO:0000269|PubMed:25157132}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0097065;
GO  GO:0007275;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSESSSEDENTARLKEAVWSFKPEDVKINGKENNGRQSHRADVSKHEHDGNELGTTPEFRSHVAKKLGTYLDGCISEVCS
SQ  DTVEPAQSENREDEEGFRLFSSSTPGKWMEQSPPPPPKRRPVPSSSDSDSEMEMRFREAAVSLSDILGPVAQNLSEKTEE
SQ  KSTKEETEDTVTKMKKKKKRKTSSEESQDKVNHQTEKQSNVEGNQEQTTAGERLKKKKKKKKKKRKKLEKDIKKDE
//
ID  O94490;
PN  Uncharacterized transcriptional regulatory protein C417.09c;
GN  SPCC417;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: O94490;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
GO  GO:0006351;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHARMQPHEDRSRSGMSRSEAMELEDQLEEEERGGNVVVGSSSANANASTAETGKKSAGGSKPKRRRGERIPPSKRIRKA
SQ  IAYVNKYASGCFGRVERRLVCTRSISRHSNQKLLDFCVECKKHKIKCVGNFPCGRCLKKGLECVIETPPRLLMNKDEISL
SQ  NLQRLSHMETILSKLMPSMSLDLPSLEAKIAELSESLQTYPDKVLTDIELGSYQQVTLNETQTYYEDAGSNESFVARVHE
SQ  IICQGREFQVQHKLTNKGNKTFEDILDPADNTVASLIHALPPKDITFYLLMTFWQFSSDNNHFYYNTKLFAAKVHHLFDD
SQ  PTSFQSKDGGFVCMLLLSMAMGSLFSYIRHPEFLSDENHDRWTYPGSQFYQNAKLLFPKVISESSLETVQSFFLAGMYLS
SQ  PTLAHEVVYMYFGIAMRAAVANGMHKKSANAQFSGDVAELRKRLFWSVYCMERKIGISLGRPESLVRSEIDIHFPEYRES
SQ  LDSQNFIASFRTFTLAIKISLLTNKVYDMWYSSLHGKANLKAATIKEIVNEIEAWRQQLSPDLEIQNIGPDSRSYRGIVH
SQ  LHLAYHIVRIAMGRPFLLHRLRERTMNSKTDEGARLLTDKLISYCYSSALHIVDLLVLLRMHKFLSVYSFMDYHSCHAAS
SQ  FIILVHLLINPSEQTIEQLNTAIDILNFVTDRFPLLKGSTDVITNLRAFAEQSEVYQSRLNATEPAYSTQVPFFPRDADY
SQ  HNQINLQNLWNDENINASLEALFNDAKGFGFLLPADNFIFPSDDGDM
//
ID  Q29RU0;
PN  E3 ubiquitin-protein ligase RNF128;
GN  RNF128;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}.
DR  UNIPROT: Q29RU0;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. {ECO:0000250|UniProtKB:Q8TEB7}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGQLPGAGVFCRGGCGFSRLLAWCFLLVLSPQTPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPV
SQ  AGVLVPPDGPGALNACNPHTNFTVPTVPGDWGSSVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIP
SQ  MSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNA
SQ  RAQSRKQRQLKADAKKAIGRLQLRTQKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHVFHKTCVDPWLLEHRTCPMC
SQ  KCDILKALGIEVDVEDGSVSLQVPVSNETSSNASPHEEDNRSETASSGYASVQGADEPPLEEHAHSANENLQLVNHEANS
SQ  MAVDVVPHVDNPTFEEDESPDQETTVREIKS
//
ID  O13760;
PN  Uncharacterized membrane protein C17A2.10c;
GN  SPAC17A2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13760;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTCVNVCFFLFPPCHRNKITEADKSLVDLLIPSLCCSLAVFPSIPLINTHSNLCLFSNFSHSCFLFCTHPDTLPTSLSIN
SQ  PKKLSLSFSFPLSQKRPFPNFLHPFTGSELSLFRCLLLFFFFLLFFLSFSFSFSFLFFLSQIFIVYFSSFPILHFLFFFF
SQ  LCVCVFLSFLFSLSHLLSLAILFLPLLLRVFSTLSRLPRLFCLCLQKKRRVLIPFAFTSFRKIASLPCVC
//
ID  Q1LYM3;
PN  Protein spire homolog 1;
GN  spire1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q52KF3}. Cleavage furrow {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}.
DR  UNIPROT: Q1LYM3;
DR  UNIPROT: Q08BK5;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Also acts in the nucleus: together with fmn2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. {ECO:0000250|UniProtKB:Q52KF3}.
DE  Reference Proteome: Yes;
GO  GO:0032154;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0045010;
GO  GO:0070649;
GO  GO:2000781;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q52KF3};
SQ  MTDGGMLISPSALQDPGDGARPEDIAMDCTDGEEELCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKHRRKETGVSPPG
SQ  RIAGPGDVRIRKDGNVKLYQPSNPDKHTPPSSSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETD
SQ  CPDEGYEATEEEDEGEEENAEVSNVRGYRDIISLCLSHLPSPSDAPNHYQAVCRALYAETKELRTFLEKIKSAKENLRKM
SQ  EGETEEPVRDLNELQNADWARFWVQVMRDLRHGVKLKKVQERQYNPLAIEYQLTPYEMLMDDIRSKRYKLRKVMVNGDIP
SQ  PRLKKSAHEIILEFIRSRPPLNPVSARKLKPHAPQPPTLHERILEEIRSERKLRPVSPDMIRRSRLGAGKSISTPQDLFR
SQ  SSDIPDGPRKLAISTLSLANGTSPARSPVNGVAGGHSLSQRKRLLKAPTLAELDSSDSEEEQSTRKSDSSSSISTSLVED
SQ  TSPESVMGKKPPPQFLPISSTPQPDKRIAPQRRHSIEKEAPTNIRHFLPPSRQNSKSLAHALGSGHAEEFCFPVECLTLT
SQ  VEEVMHIRQVLVKAELEKFQQYKDIYNALKKGKLCFSCRSKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPIS
SQ  SLGPSILPKKEPGASSAPTDKTSSTSSHKKNSLQRSLSRSSKHGDRSSSKDELELPEQFTEDWSTMEVCVDCKKFINDII
SQ  SNSRRNLSTKRARLHRRTHSVYSSSTSSSNYKPTERTIKEV
//
ID  O60131;
PN  Uncharacterized transcriptional regulatory protein C16G5.17;
GN  SPBC16G5;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O60131;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVGKSKNRAHKNIRARSCLRCRRRKVKCDRQYPCSRCKESEESCTYGVNEQAVQLLEEPLSRPITRETDSSAHQETRTRL
SQ  EENNLPKTQKFGFVDWKTILKSSAEFQGIVQRDPESRLREALETDPKLKKRLECILETIPPWDVCESLLKVYANTFNVTN
SQ  YILDFEQADKLLSDLKNSNHVFATSIILIVTAIAVALSLESFPSNIERYFSAVNHSAIELSDALNSKIDDFLNEEVIFRL
SQ  WRNIDRIRLHAIRAQLCMRNQFRSMNTDLCYAIHYACFVNPIFQNTDTEYEANMEVWLSICEIDALECVLRSCQPWVQHD
SQ  IYGKLLSQRKMGSDVISYEFHSLLGQLLTCGLEIYKAIHTSTVNEFVNSIQFYESQLSLVLMEIESKFSNIDGSDIHFRY
SQ  LFLKTVFWTVRKNLYQGFITVSRTLVPNYPDIVQKLGQTSIQLSRLISNSMDCFEKYGWLKAMLILVTHTFLIIHVCSER
SQ  GYDVPKDFWNVTASVQATLEEKKYPGIVWERIHYVLNIYTTINSVEPELSEDHGDLDDQNLFQVFTDIFDFNFNFPLPNL
//
ID  P85091;
PN  Cytoplasmic FMR1-interacting protein 1;
GN  CYFIP1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
DR  UNIPROT: P85091;
DE  Function: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E- FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q7L576, ECO:0000250|UniProtKB:Q7TMB8}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0030027;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0045202;
GO  GO:0051015;
GO  GO:0048365;
GO  GO:0048675;
GO  GO:0030032;
GO  GO:0008360;
GO  GO:0031529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYLTPSEKRINLSKVHPTDKLADQIFAYYKEGERDGKDEIIKNVPLKRIRK
//
ID  Q8VDR9;
PN  Dedicator of cytokinesis protein 6;
GN  Dock6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly located near the cell surface. {ECO:0000250}.
DR  UNIPROT: Q8VDR9;
DR  UNIPROT: E9QKQ0;
DR  UNIPROT: Q3UM59;
DR  UNIPROT: Q6PFY0;
DR  UNIPROT: Q8BJS1;
DR  UNIPROT: Q9D461;
DR  Pfam: PF06920;
DR  Pfam: PF14429;
DR  Pfam: PF11878;
DR  PROSITE: PS51650;
DR  PROSITE: PS51651;
DE  Function: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases (By similarity). Through its activation of CDC42 and RAC1, regulates neurite outgrowth in an vitro differentiation system. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005085;
GO  GO:0007264;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRSSSSLGVPLTEVIEPLDFEDVLLSRPPEVEPGPLRDLIEFPV
SQ  DDLELLKQPRECRTTESGVPEDGQLDAQVRAAVEMYSEDWVIVRRRYQHLSTAYSPITTETQREWQKGLTCQVFEQDTPG
SQ  DERTGPEDVDDPQHCSGSPEDTPRSSGASGIFSLRNLAADSLLPTLLEQAAPEDVDRRNEALRRQHRAPTLLTLYPAPDE
SQ  DEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGTLALYDVREKKKISENFYFDLNSDSVKGLLRAHGTHPAIST
SQ  LARSAIFSVTYPSPDIFLVVKLEKVLQQGDISECCEPYMVMKEADTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVH
SQ  LANIVSRPQDRDSDSEGERRPTWAERRRRGPQDRGYSGDDACSFSSFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRP
SQ  SSLLRRLRPVTAQLKLDISPAPENLHFCLSPDLLHVKPYPDPRGRPTKEILEFPAREVYAPHSCYRNLLFVYPHSLNFSS
SQ  RQGSVRNLAVRIQYMAGEDQSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLRLPACVTENHHLFFTFYHVSC
SQ  QPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDP
SQ  HLDKFFTLVHVLEEGIFPFRLKETVLSEGTMEQELRASLAALRLASPEPLVAFSHLVLDKLVRLVVRPPIICGQMVNLGR
SQ  GAFEAMAHVASLVHRNLEAVQDSRGHCPLLASYVHYAFRLPGGDLSLPGEAPPATVQAATLARGSGRPASLYLARSKSIS
SQ  SSNPDLAVVPGSVDDEVSRILASKGVDRSHSWVNSAYAPGGSKAVLRRVPPYCGADPRQLLHEELALQWVVSGSAVRELV
SQ  LQHAWFFFQLMVKSMELHLLLGQRLDTPRKLRFPGRFLDDIAALVASVGLEVITRVHKDMKLAERLNASLAFFLSDLLSI
SQ  ADRGYIFSLVRAHYKQVATRLQSAPNPTALLTLRMDFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQ
SQ  APDPKVTSMFELSGPFRQQHFLSGLLLTELALALDPEAEGASLLHKKAISAVHSLLCSHDVDSRYAEATVKAKVAELYLP
SQ  LLSLARDTLPQLHGFAEGSGQRSRLASMLDSDTEGEGDIGSTINPSVAMAIAGGPLAPGSRTSISQGPSTAARSGCPLSA
SQ  ESSRTLLVCVLWVLKNAEPTLLQRWAADLALPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILG
SQ  TIGARQEMVRRSRERSPFGNQENVRWRKSATHWRQTSDRVDKTKDEMEHEALVDGNLATEASLVVLDTLETIVQTVMLSE
SQ  ARESILSAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRMHASASLYL
SQ  LMRQNFEIGHNFARVKMLVTMSLSSLVGTTQNFSEEHLRKSLKTILTYAEEDIGLRDSTFAEQVQDLMFNLHMILTDTVK
SQ  MKEHQEDPEMLMDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDSRHLPVGCVSF
SQ  QNVSSNVLEESAISDDILSPDEEGFCSGKNFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVH
SQ  GKLQEAFTKIMHQSSGWERVFGTYFRVGFYGTRFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNP
SQ  VDKSKLDPQKAYIQITYVEPHFDTYELKDRVTYFDRNYGLRAFLFCTPFTPDGRAHGELAEQHKRKTLLSTEHAFPYIKT
SQ  RIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLSEIPEDPKLFRHH
SQ  NKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERHYSRLREALQPLLTQRLPQLLAPSSTSLRSSMNRSSFRKADL
//
ID  O56860;
PN  p3;
GN  gag;
OS  53182;
SL  Nucleus Position: SL-0382;
SL  Comments: [Gag protein]: Virion {ECO:0000250}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal (By similarity). In the late phases of infection, Gag proteins assemble in the cytoplasm to form the virion's capsids. {ECO:0000250}. [p3]: Virion. Host cytoplasm, host perinuclear region. Note=Gag proteins assemble in the cytoplasm to form the capsids. {ECO:0000250}.
DR  UNIPROT: O56860;
DR  Pfam: PF03276;
DE  Function: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044163;
GO  GO:0019013;
GO  GO:0003677;
GO  GO:0003723;
GO  GO:0075521;
GO  GO:0046718;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARELNPLQLQQLYINNGLQPNPGHGDIIAVRFTGGPWGPGDRWARVTIRLQDNTGQPLQVPGYDLEPGIINLREDILIA
SQ  GPYNLIRTAFLDLEPARGPERHGPFGDGRLQPGDGLSEGFQPITDEEIQAEVGTIGAARNEIRLLREALQRLQAGGVGRP
SQ  IPGAVLQPQPVIGPVIPINHLRSVIGNTPPNPRDVALWLGRSTAAIEGVFPIVDQVTRMRVVNALVASHPGLTLTENEAG
SQ  SWNAAISALWRKAHGAAAQHELAGVLSDINKKEGIQTAFNLGMQFTDGNWSLVWGIIRTLLPGQALVTNAQSQFDLMGDD
SQ  IQRAENFPRVINNLYTMLGLNIHGQSIRPRVQTQPLQTRPRNPGRSQQGQLNQPRPQNRANQSYRPPRQQQQHSDVPEQR
SQ  DQRGPSQPPRGSGGGYNFRRNPQQPQRYGQGPPGPNPYRRFGDGGNPQQQGPPPNRGPDQGPRPGGNPRGGGRGQGPRNG
SQ  GGSAAAVHTVKASENETKNGSAEAVDGGKKGGKD
//
ID  Q06BI3;
PN  Calcium-binding protein 8;
GN  Caln1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:19458041}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19458041}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
DR  UNIPROT: Q06BI3;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000269|PubMed:19458041}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAII
SQ  MQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINE
SQ  EESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME
//
ID  A6ZZB9;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: A6ZZB9;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  A9ULB4;
PN  TP53-regulated inhibitor of apoptosis 1;
GN  triap1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43715}. Mitochondrion {ECO:0000250|UniProtKB:O43715}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}.
DR  UNIPROT: A9ULB4;
DR  Pfam: PF05254;
DR  PROSITE: PS51808;
DE  Function: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. The triap1:prelid1 complex probably functions as a phosphatidic acid (PA) transporter across the mitochondrion intermembrane space to provide PA for cardiolipin CL synthesis in the inner membrane. Likewise, the triap1:prelid3a complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (By similarity). Required for pronephros development; probably involved at an early stage in the formation of pronephric components derived from the somatic layer (PubMed:18472403). {ECO:0000250|UniProtKB:O43715, ECO:0000269|PubMed:18472403}.
DE  Reference Proteome: Yes;
GO  GO:0005758;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0006915;
GO  GO:1902166;
GO  GO:0015914;
GO  GO:0048793;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSVGEECTDMKREYDQCFNRWFAEKFLKGECSGDPCTELFRRYRDCVQKAIKDKDIPVDGVDFMGPSKSKTESDGSS
//
ID  Q9H4I8;
PN  Serine hydrolase-like protein 2;
GN  SERHL2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Peroxisome {ECO:0000250}. Note=Concentrated in perinuclear vesicles. May be located in peroxisomes. {ECO:0000250}.
DR  UNIPROT: Q9H4I8;
DR  UNIPROT: B1AHE9;
DR  UNIPROT: B1AHF0;
DR  UNIPROT: Q0VDJ1;
DR  UNIPROT: Q5H973;
DR  UNIPROT: Q9BR29;
DR  UNIPROT: Q9BR30;
DR  UNIPROT: Q9Y3I9;
DR  Pfam: PF00561;
DR  OMIM: 607979;
DR  DisGeNET: 253190;
DE  Function: Probable serine hydrolase. May be related to cell muscle hypertrophy.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TDZ2; IntAct: EBI-12846282,EBI-7153876; Score: 0.35
DE  Interaction: Q9Y6M4-2; IntAct: EBI-12846282,EBI-16399650; Score: 0.35
DE  Interaction: Q9Y4D1-2; IntAct: EBI-12846282,EBI-21582910; Score: 0.35
DE  Interaction: Q9NWQ8; IntAct: EBI-12846282,EBI-2828115; Score: 0.35
DE  Interaction: Q9HAV0; IntAct: EBI-12846282,EBI-358539; Score: 0.35
DE  Interaction: Q05086-2; IntAct: EBI-12846282,EBI-10175863; Score: 0.35
GO  GO:0031410;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0016787;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSENAAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVP
SQ  YYLQTFVSEIRRVVAALKWNRFSILGHSFGGVVGGMFFCTFPEMVDKLILLDTPLFLLESDEMENLLTYKRRAIEHVLQV
SQ  EASQEPSHVFSLKQLLQRLLKSNSHLSEECGELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHV
SQ  LLIKAVHGYFDSRQNYSEKESLSFMIDTMKSTLKEQFQFVEVPGNHCVHMSEPQHVASIISSFLQCTHMLPAQL
//
ID  Q5RDB1;
PN  MOB-like protein phocein;
GN  MOB4;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: Q5RDB1;
DR  UNIPROT: Q5R8K8;
DR  Pfam: PF03637;
DE  Function: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0048471;
GO  GO:0019900;
GO  GO:0046872;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLE
SQ  LNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVC
SQ  RRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
//
ID  Q2KIC8;
PN  Transmembrane protein 100;
GN  TMEM100;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9CQG9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CQG9}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}.
DR  UNIPROT: Q2KIC8;
DR  Pfam: PF16311;
DE  Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor- dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. {ECO:0000250|UniProtKB:Q9CQG9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001525;
GO  GO:0060842;
GO  GO:0030509;
GO  GO:0071773;
GO  GO:0003198;
GO  GO:0001701;
GO  GO:0007219;
GO  GO:0045603;
GO  GO:2001214;
GO  GO:0043491;
GO  GO:0050848;
GO  GO:0051930;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTDEPIKEILGTPKSPKPVAMEKNANGEVVVTLVPLVSEIQLAAATGGAELSCYRCVIPFAVVVLITGTVVTAVAYSFNS
SQ  HGSIISILGLVLLSLGLFLLASSALCWKVRQRSKKAKRRESQTTLVVNQRGWFA
//
ID  Q641M3;
PN  Transmembrane protein 18;
GN  tmem18;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q641M3;
DR  Pfam: PF14770;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTASNTKNASAIPIDKFSNVRITSIWTFLQSVDWSEPWLMALLAFHVFCFAFTLLSCKYYRIQICHFLLMVAMVYSAEYL
SQ  NELAAMNWRSFSKFQYFDSKGMFISLVYSVPLLLNTVIIVAVWVWRTFSTMTELKILQLKRKAARENHKKTQ
//
ID  Q8CGZ0;
PN  Calcium homeostasis endoplasmic reticulum protein;
GN  Cherp;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region. Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}.
DR  UNIPROT: Q8CGZ0;
DR  UNIPROT: Q8K291;
DR  UNIPROT: Q8VCD2;
DR  Pfam: PF04818;
DR  Pfam: PF01585;
DR  Pfam: PF01805;
DR  PROSITE: PS51391;
DR  PROSITE: PS50174;
DR  PROSITE: PS50128;
DE  Function: Involved in calcium homeostasis, growth and proliferation. {ECO:0000250|UniProtKB:Q8IWX8}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13131; IntAct: EBI-1181405,EBI-2366446; Score: 0.37
DE  Interaction: Q15637; IntAct: EBI-2366446,EBI-744603; Score: 0.37
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0033017;
GO  GO:0044325;
GO  GO:0003723;
GO  GO:0006874;
GO  GO:0008285;
GO  GO:0070886;
GO  GO:0051209;
GO  GO:0006396;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMPMPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQAPELEPTS
SQ  AMPPLPQPPLAPTASLTPAQGTPSMDELIQQSQWSLQQQEQHLLALRQEQVTTAVAHAVEQQMQKLLEETQLDMSEFDNL
SQ  LQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKV
SQ  VVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQSLKTQ
SQ  HEEFVSSLAQQQQQQQQQQQQQPQPQPQPQIQLPQMEADVKATPPPPAPPPASAPAPTIPPTTQPDDNKPPIQMPGSSEY
SQ  DTSAGVQDPAAAGPRGPGPHEQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPG
SQ  WNGQRDAPWNNQPDPNWNNQFEGPWNNQHEPPPWGGAQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRF
SQ  MQDDFPPRHPFERPPYPHRFDYPQGDFPADMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGP
SQ  PHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQN
SQ  GLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSSSRSSKSSRSSSRSHSRSRSRSSSRSRSRSRSRSRSSR
SQ  SRSRSRSRSRSKSYSPGRRRRSRSRSPTPPSAAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPI
SQ  KGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDEFSTFGTRKEEKED
//
ID  B3P100;
PN  Protein asunder;
GN  asun;
OS  7220;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B3P100;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGGGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWSHSTQNMSHVMNAMVMVGVPSRNVATSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTD
SQ  ELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNALAAPPAKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMVPLKVKDPSAPPLARRLPRYFPLTTSSSILFHLQRHINWLPH
SQ  FLHILVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRSYTESPLSPERLEPITSGSASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPDFGNKDKDSVVTAASITPNVKEESVRS
//
ID  Q29KT5;
PN  Protein spire;
GN  spir;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Punctate spots in perinuclear region and cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q29KT5;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DR  PROSITE: PS51082;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003779;
GO  GO:0045010;
GO  GO:0007275;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTEHHMDVQADATQSASESKAMAAPKGKFSEAEEGFLSTSPDSANGDAQQAHTHTHIISHTHSKGAAKTQTQTQNGNGTL
SQ  GMGLGAPMLPGGSRQLLRQAFYQCSCPEQCVTLNNILDSFKAPLSEDQAWALIYQFGSLYYKVAAQAHKSGGDYEADLPS
SQ  RFELHFHRDGNVHFSGAERLPELVESQEQEASQQEQQQKQPQMDDSATSSVDSNAALDRAFDNNNHEHHHHHHHQHHHPV
SQ  DSNAALDRAHHTPLVVSHRKIISEMAEIVYTALDYNLPEDEECQMSQELENLFNFMTADETDEDCIDEGIDEGDKRWDDE
SQ  AEEERNDTKELEHIIETCRNHLQKPALADNHYKAVCRALATETIELRVFLQQVLNNGAEKLIKAAESSPTTQKELAKLGF
SQ  NDWARFWVQVIDELRRGVRLKKSNFERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRP
SQ  PLKKASERQLGPPRMCTPTPREQLMESIRQGKELKQITPPEAPPLRQRMLPSANSTLSRSRQRLIKVDFSQLQDDELFFD
SQ  DSSMSSSHSTAATHQHHQQHQPHHAHLAELHRCSQPKMPPYPFGGYMVPSQARQECQATATQLRPRRTMDTSAPRQTLPQ
SQ  PQAQARPPPPAEPSFTEDEYHRFFDNALESYDLATQCESRRASLRRHTIVGCQSNLEETHSMPPTRPESRQSDDAGSQSQ
SQ  SGASSEAPGIRKSPLMEGDHSQTTDGPPRLDEAHSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELE
SQ  GLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTP
SQ  SPSHHAHQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGAGASTSAAPGHAV
SQ  EALHDQAAMSASYSSAMRPSGVMQHHQKHHYNNAMSRSMEGPRSLPVHSPAYRPLSNSSTLERKSRFSRGFALFSSGSHL
SQ  AQTQDQKENLRGEQVPVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK
//
ID  F1MAD2;
PN  InaD-like protein;
GN  Patj;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to tight junctions in epithelial cells. Also found at the apical plasma membrane (By similarity). Localized in the paranodal region of myelinating Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DR  UNIPROT: F1MAD2;
DR  PDB: 3UIT;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DE  Function: Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0048471;
GO  GO:0032991;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NI35};
SQ  MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRK
SQ  GLLVFTDGSITNGNAHRPCSSITASESLPWTQRSGNEDFTSVIQQMAQGRHIEYIDIERPSTGGLGFSVVALRSQSLGLI
SQ  DIFVKEVHPGSVADRDQRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQSRTSTSSADTTLPET
SQ  VRWGHTEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGSTNVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPVGEIAVTPPTPASLPVALPVVATRTLGSDSSPFETYNVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSI
SQ  IPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEQPSSREAVAEPPEVPELT
SQ  GSLKPETNSRMEAEEIGERLDNLRKDTVQALEKPDVYPEDIPGCPENELKSRWENLLGPDYEVMVATLDTQIADDEELQK
SQ  YSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRR
SQ  LFDDEASVDEPRTVEPSLLEAEVDRSVDVSTEDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPMRSVIVIRSL
SQ  VADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEEEKEEKEEHFIFHSNNNGDNSESP
SQ  ETVHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDMDSSSEAWEMHEFLSPRLERRGEEREMLVDEEYEI
SQ  YQDRLRDMEAHPPPPHIREPTSASPRLDLQAGPQWLHADLSGGEILECHDTESMMTAYPQEMQDYSFSTTDMMKETFGLD
SQ  SRPPMPSSEGNGQHGRFDDLEHLHSLVSHGLDLGMMTPSDLQGPGVLVDLPAVTQRREQEELPLYRLPSARVVTKPSSHV
SQ  GMVSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSP
SQ  AGKTKALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPSVNNKGKTPPQNQDQNTQEKKAKRH
SQ  GTAPPPMKLPPPYRAPSADTEESEEDSALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPD
SQ  GPAAADGRMRVGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVNQMAVAPFPVPSHSPSPVEDLGGTEPV
SQ  SSEEDSSVDAKPLPERESSKPEDLTQAVDDSMVAEQEKASESPDSAARQMKQPGYSAQVSSSSQEIPSAPAPLCQSTHAD
SQ  VTGSGNFQAPLSVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGD
SQ  QILEVNGVDLRSSSHEEAITALRQTPQKVRLVIYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIV
SQ  KGGAADLDGRLIRGDQILSVNGEDVRQASQETVATILKCVQGLVQLEIGRLRAGSWASSRKTSQNSQGDQHSAHSSCRPS
SQ  FAPVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGVSIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGD
SQ  RIVSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEMMSAGSQLGSPTADRHPQDPEELLQRTAD
//
ID  P42001;
PN  Protection of telomeres homolog 1;
GN  pot;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:23390606, ECO:0000269|PubMed:24297748, ECO:0000305|PubMed:18329362}. Nucleus envelope {ECO:0000269|PubMed:24297748}. Chromosome, telomere {ECO:0000269|PubMed:23390606, ECO:0000305|PubMed:18329362}. Note=More highly expressed in meiotic pachytene nuclei than in diakinesis-stage oocyte nuclei (PubMed:23390606). Also expressed in mitotic nuclei (PubMed:23390606). {ECO:0000269|PubMed:23390606}.
DR  UNIPROT: P42001;
DR  UNIPROT: A0A2K5ATS5;
DR  UNIPROT: A0A2K5ATS9;
DR  UNIPROT: A0A2K5ATU9;
DE  Function: Telomeric DNA-binding protein, which binds to single-stranded C-rich repeat sequences, with high specificity to the 5'-GCCTAA-3' sequence (PubMed:18329362, PubMed:23390606). Repeat sequence binding can be at the 5' or 3' telomeric end (PubMed:18329362). May have a role in protecting the 5' end of the C-rich strand of the telomere (PubMed:23390606). Acts redundantly with pot-2 to negatively regulate telomerase-mediated telomere extension (PubMed:18329362, PubMed:23390606, PubMed:24297748). Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres) (PubMed:23390606, PubMed:22547822, PubMed:24297748). Through sun-1, anchors telomeres to the nuclear envelope in embryos (PubMed:24297748). {ECO:0000269|PubMed:18329362, ECO:0000269|PubMed:22547822, ECO:0000269|PubMed:23390606, ECO:0000269|PubMed:24297748}.
DE  Reference Proteome: Yes;
GO  GO:0000784;
GO  GO:0005635;
GO  GO:0043047;
GO  GO:1904357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQYTYQHIQDLVPGPTPQNFYGKIIFIKKKINQIVVLIKDETQSIYLRVIPKEDQELEFQLRQVVRVHRCKIQSILNSKE
SQ  GIAQIGLFGCHLIAWSQSGKVDNPVIISSRSWTKSDEDSERLQTLRKLGKSRRKSGRKTSVDTMANKLIERREAMFADTF
SQ  IKSLFNKIALSRKEHLSRNARELFYHRPGDIVETQNLLEIDDSWFNDENSEQFVQYVLNCTTCHVEYNHVEYAQNNIPTN
SQ  CRFCQEAMESFHAAFRIRISIETYGVFLTIPLELIKTELDICEDWDSESNIVEEEEKVTRFKKNIQEKVRDASIVHIKGI
SQ  SSLLLIIMLNINSISLVNNITENKRILLQKSNVPSSLQLKILITPFVIVVVRFFGITWIYSGSSCIEEVLNLIDNCSRRR
//
ID  Q9VE34;
PN  Ectopic P granules protein 5 homolog;
GN  Epg5;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}.
DR  UNIPROT: Q9VE34;
DR  UNIPROT: Q8MT53;
DE  Function: Involved in autophagy. Plays a role in late steps of autophagy. {ECO:0000269|PubMed:26917586}.
DE  Reference Proteome: Yes;
DE  Interaction: O61307; IntAct: EBI-118556,EBI-3409606; Score: 0.35
GO  GO:0005737;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0097352;
GO  GO:0006914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLEKPKKEKSKKSRNRVPIEKEEEEPAELSTSEEQRPAENVSLLEEFERVATLASSSSGEAIISHECCISSDVGVTSQ
SQ  EPEGTQEPTETEAQPSAPSAPPSTTVHVVQYPNLQPMQLSNAQVEEHSAKIVYRQAESPTGFALARSHIKLLSTEELRQI
SQ  YDCPELELAKQFELEFLMNSLLETSEADPLYAAVMEYYELQGKITSNLHDVEKLRKGCAESQKQIWVRQPVTRTFSGTCG
SQ  DGNVVQECVTYDVIQVDPIKLEVAKTSLTGLYDLVCHAYTNNSITAKITKVKVDQIINDLLTYPNLDGHSVVSLHHTQSG
SQ  EALQCVSQLRRAISILFSFVRRPSPNANFDKDLKEWLRKLIALQLLLATREDHWFLLFNILRCPNGVGSWAAQFLQLPGT
SQ  RAVRRGSQQNELPLDLNSPELNHCMAVLQILLMPVKKRNEYLKSQAQAHRELSDTPGATDRWIVVDSDGEDSHTPAGECV
SQ  GLKESDLVALLNQMPFEKIFTSALRIEKFLDDYIIEPDMITAQQMLAVVVFFSQLVKTIGEGLLTYNNERYKQLAKRLGR
SQ  LVRHTLQYVFDYNELFINNNLYKSSEMYERIQVELQALLVRACGYIYRTRNLGTWQYFSTLPFGTLDAEVIWHLFYYLNV
SQ  GFPTDLANDLVSNAEAAFQAEDFWRKFDLANADVAPEDMYYLLQTFFEMANERNRSKDGSLVKAICLHIFHIGYIHKSTR
SQ  EICYKTARDMLANLMDEDLFGCVLVQLKMRYGEVDQAAYLFKALPLENWHPSMDTFEVLSNWLLHFDYQSSESQLARLII
SQ  SHLNWGLDCEGRLFLPHNIHVRMAHLVNEALNKYAPEVIGASGISESVRQVSSLIDSTQSSREQFTNWCWRMVSVLRLHL
SQ  MDQGVESVRRTLQHPTEPLLFIPELERMEMIFQGVNENRPLALYVGMLVSLHGHSIPLICQHGFILLQQLLLDHRHAATI
SQ  RCLELIVPLFLETPETLANCESFQRLITTLLNADRTYLKLAKDMVYANSIGPILELLDNMLHHQIISYTSYGLCSPLNLL
SQ  NIWLNCFTTLPGWSQNSNLLYLLDRMLRISYQFPDCRAQAVEFFYNYYKDCTEWKSAPKGSALKAFFGGQSVSRIPLISP
SQ  QNCWLNLVILEIEFRLVDTRIFPELLRQISAQPVEAALKKTISLSKTSAFPASQLVIFKYAQLLASMESTHALFPIVCQK
SQ  FFELYLWRVPTENESLNFSHNFGVSDKFYEYNVPLMKSIKSQLKSAESYYSALATKNANDDAMAHFYRNCCKLMQNCALW
SQ  LEDTQINRFTSDAEHLPAQYNSEKLRELLSGHVNHWTEFLCLASLRKEQRHQADQWGRKVMRLSNQKAPRTPVQPKQRQP
SQ  PAQHIKSLLKSYEKIVENPLHIRVEPIKTPPIDGVIVAQIQKKMTTLNSTANNYHYKTSELNSLDLNYLERVPTLYSMIP
SQ  YEETRRKECTSLLFKRNCTAPAQIKLTPEHIRINDVISRKQAQNRERHDKIIEDILLAMSVESFAQAIEELGVCIGALLV
SQ  APLESSVTQIGVRVFYDIVDNLNEVTMKFQPTHDLYFQVLEKLGVFLEADQAAQGLAILRLALKRPDLLELLAGVFVPSR
SQ  TDVDHFLSMYEFLIDSHLKHCDTQTLFVLFSKFDLLGWMEAYQPKLSEINRLLLLVLQGLEAWSQPDSSLLQDLFRRHLV
SQ  HIFGYDFPQHYGEVMQLVLDRTSDQKLMPVVLLDLLNALFVRSNCAELSLQQSEVRVHELALDFARRQKLFTLKAATDTL
SQ  LLLSRHFQKERLHHGLHGLYPKHKDYCQALVLWFTSFGHTLLASAICSYQELLADQISDIVFGSIVETYSPWLIPYTEET
SQ  VSGVAHWIRQLTPGQSKVLLPWSEQHVSSCKLMIRSFVATIIQVLQYLPSSNKILEHVFAWYVHHFAQSSTTGHVLAPIH
SQ  EGLAQLPWERFLPPAQHVELLYDSLQKFLPESHAMLGHIFIRIEWNNWFAQMPQPVSILSRLFTIFVKIAFEPNIHIHPN
SQ  TSKILEDAIRYPWHLVECSELEQLLKWFVASVEPAIALKIPAESNYADRAVLELLRLACAMLPERSAQDAVVLGTAKRML
SQ  YTRSMVRMQRACGAKHQKLLATKEGERAFSNAFLELLDSIDGAISSCSEHRTMEEQRREALNLMLELVAPTQTQSQEVSN
SQ  IHIKALVWWQQRCSPGNLVMCSTLPAIGHLNTYIASIYSLLEASIENYFRTSPEIASWHAPSWQGLMEALSMSLPKLDLM
SQ  PIMQGSYFFSLHVFVLYKMEEIATDGDKVTFLQDLSQLLENLKTSPQTEPRMALVWGVIIARGCQIAQVNQQVKKPLHML
SQ  ARHLQIASTKAEGWGDGLLGVIGLKSEVITNRRKVLTRCLACVIFSLFPANRDLRIPSEEYESALRELSMLLANKKFTDI
SQ  KPLIVRAVSLLKESTFPDIRAVPHMVCRLISIFYEESYLTTIPEVWDFEFKLMAT
//
ID  A1YER2;
PN  Oxidoreductase HTATIP2;
GN  HTATIP2;
OS  9595;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: A1YER2;
DR  Pfam: PF13460;
DE  Function: Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0016491;
GO  GO:0004674;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
GO  GO:0051170;
GO  GO:0043068;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0045765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYAS
SQ  AFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSKFLYLQVKGEVEAKVEELKFD
SQ  RYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSL
SQ  KP
//
ID  Q5ZKD9;
PN  Kelch-like protein 20;
GN  KLHL20;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q5ZKD9;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. It also specifically mediates 'Lys-33'-linked ubiquitination (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGKPMRRCTSTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTSLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWV
SQ  KYSIQERRPQLPQVLQHVRLPLLSTKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEV
SQ  LFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPT
SQ  STCRTSVGVAVLGGYLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVER
SQ  YNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAV
SQ  GGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q54B27;
PN  Exocyst complex component 6;
GN  exoc6;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}.
DR  UNIPROT: Q54B27;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0017137;
GO  GO:0070177;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0015031;
GO  GO:0006904;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKKQKEEINTAGGSVILKTMVRDKDKEQKEEKREKKEKKRLEKKEAENVKKEKKKEKKELKKIGKAGRSGSITSDSST
SQ  HSGAQEFDSYGNDSNGGGGGLSASIDSNGLSSSGQPMQTRHLEKEVGEKQGIYSLSSQDRSSSLPHSSQDDQAKPLITES
SQ  EIFSSESFLIAVSDTDHLGPAIKSVFENNKEKEVIKILNAYIAQKDLDIEKICGENHEGFINSVTAFLGLKGENLDLKQD
SQ  VINLNYELQEIGRKYVTKAEELFAYKQIKDNIKRTKEVLNNCQYAILLGMKVDEYVQQKKYYQAIKNMDQLHNVYLKKLS
SQ  DFQFARNMDYNIPVLKEKIKKLVKDEFNQWMVEIKEKSAVIGKLGMIQTSKKLLKEREINPLKIKTTFGENEQIWDKILD
SQ  IPPIINSSSIGSLALYPTLNSPVTAPIYSPNSGKTPSSFGFNKQINEKDLKEDINQFSPFDESDIQFHPLYQCLFIHASI
SQ  GQLEEFQAYYTLNRLLQFQLVIQPKESGQVWELFLQQILGYFMVESKVIDSTEPFLSKTTINDSWNSALVKVTSVLQELF
SQ  THCVDTQPLIAFKKFVLIFTNTMSFYSYHVQPLYYFLDTMKEKYCQFSIKEAVERFTIILERDSHCSLIIESLEEYKSLI
SQ  LANKLDILERQQLRQLQNSLNNNQFQFGDKNLNNNNNNDDDDDYFDEDENEDDKISKRLPKSFLFSKMVPQFYTLIKKFI
SQ  SEFYEFSDQLTENENFIIRSTDTLIKKINEVLYSYLTQSQAVPQVIQLVINLQHLISGCSFFKDYLNSLILGEDYQKNQS
SQ  IVNETNKVILNSQNLLYTTKSHGEKLIIKLCEQKIEDLMSSAANIEWFPQNAIDDRPRDYIIDVCTFLEVTLPFISPLSQ
SQ  NLKEEFITKAFKNISESLFSLIYDDQLKKLNLQGVKSFDADLKYIETYVKEKANEKERTTTTSRNMVGYFVELRQLTNFL
SQ  LSDNPEDFVDPKIKAKHYNLITNIPQLLNILNKYKEESKGFTTSKEIKDRNKKIADAIKKIKDSL
//
ID  Q8K2T1;
PN  NmrA-like family domain-containing protein 1;
GN  Nmral1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8K2T1;
DR  UNIPROT: Q8BVF0;
DR  UNIPROT: Q9CZP2;
DR  Pfam: PF05368;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3UHD9; IntAct: EBI-771911,EBI-9989325; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-912574,EBI-9989325; Score: 0.35
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRKLVVVFGATGAQGGSVARALLEDGTFRIRVVTRNPEQRAAKELKQQGAEVVRGDQDDAASMELALAGAHATFIVTN
SQ  YWETCSQDREVQQPHQWDQVFKQGKLLADLAKRLGLHYVVYSGLENIRKLTAGKLAAGHFDGKGEVEEYFRDIGVPMTSV
SQ  RLPCYFENLLSYFLPQKAADGKSFLLDLPMGDVPMDGMSVSDLGPVVLSLLKKPEEYVGQNIGLSTCRHTAEEYAALLSK
SQ  HTGKAVHHAKTTPEDYEKLGFQGAQDLANMFRFYTLKPDRNIHLTLRLNPKAQTLDQWLEQHKGDFAQL
//
ID  B2RZ50;
PN  Cyclin-dependent kinase inhibitor 3;
GN  Cdkn3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}.
DR  UNIPROT: B2RZ50;
DR  Pfam: PF05706;
DR  PROSITE: PS50056;
DE  Function: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q16667}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0004722;
GO  GO:0004725;
GO  GO:0007050;
GO  GO:0060271;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPPISIQASEFDSSDEEPADDEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSSGIQDVFVFCT
SQ  RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD
SQ  SISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR
//
ID  G0S2X1;
PN  Nucleoporin NUP37;
GN  NUP37;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH4}.
DR  UNIPROT: G0S2X1;
DR  UNIPROT: G0ZGV1;
DR  PROSITE: PS00678;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALQPVPRMRRTLQNTQHTYSLGRRIYDVKTYPVQSPQGATILIYGHENGATVVWRGGRRLKPPKPQTNEKRNGTKPEDA
SQ  VMIIDSDDETGPTFVDKPEFEDSPSVADGSVAEIIQTLDLALGTAVNHIAVLPMPPCAAEDASWNGANILKTKIVFAVTC
SQ  ATNDVYVITLPLTPPSHEAKARPELRKSLLAGNAGKGVWGETLTLLTGPSRSCNGVAISLVKHRSSSRSRSSERSAAQAA
SQ  PITRVVVAAHSREASGTLRLWDVPLEAKPGTINRVEPFQTEYLPSPLTSISFNPVNLTQLLTVASPHAVRIYDYATASLP
SQ  SDDTSEGPFPSQGSWLISLYPPFARGPAMSTSRKPIVAAEWIARGRAILTLLADGQWGIWDLDGASPTAAGGGSNLFSKT
SQ  SAGLRGTAITAFSVTGHLEGTSPLRNPTTQKASSSSSGEFVPMTPHTRRDAIATAFGGSPEKLAAVRGGITVAQLPSTLT
SQ  SGAGDESAVLFLGGADPIVCVIPVLSKFWDSQLRRAAGGGVNLWSGAQPTRMIRLTDLSAGLLGERCTGAVAITKAVRAN
SQ  ASTNGILKEDDNSGSQGLPIEVLLQGESRLVIVHENGDAPTSSLTSRLLGARKKQRDEFKSVNAIVAYPPLEKPSVSFNL
SQ  NLTQRPEKPGTLFAPRSRHSKSLFEQSIDTIPSTDAGDEETIPATSAPSSQQGFMFATDLELAADLPDDEADAEGRDVEQ
SQ  ELLDIMEIDRELEQLEQARERGRKRVFFEEG
//
ID  A7MB43;
PN  Myotubularin-related protein 9;
GN  MTMR9;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96QG7}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96QG7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96QG7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QG7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96QG7}. Note=Localizes to ruffles during EGF- induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region. Partially localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000250|UniProtKB:Q9Z2D0}.
DR  UNIPROT: A7MB43;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DE  Function: Acts as an adapter for myotubularin-related phosphatases. Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding affinity for phosphorylated phosphatidylinositols (By similarity). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3-phosphate. The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels. Stabilizes MTMR8 protein levels. Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles. Negatively regulates autophagy, in part via its association with MTMR8. Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6. Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000250|UniProtKB:Q9Z2D0}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0030234;
GO  GO:0019903;
GO  GO:0010507;
GO  GO:0010922;
GO  GO:0050821;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96QG7};
SQ  MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGPLGTIIIKCKDFRIIQ
SQ  LDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSTISEWRLSYVNKEFSVCPSYPP
SQ  AVIVPKAIDDDALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRPLN
SQ  IAQQARAKGGGFEQEAHYPQWRRIHKSIDRYHILQESLIKLVESCNDQTQNMDRWLSKLEASNWLTHIKEILTTACLAAQ
SQ  CLDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNSKQKWESPVFLLF
SQ  LDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPSELSKFTNPLFEANNL
SQ  VIWPSVAPQSLQLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNLLRRQLAELETEDGVQESP
//
ID  P54217;
PN  Spermatocyte protein spe-11;
GN  spe;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:8565851}. Note=Localized to the perinuclear region of sperm.
DR  UNIPROT: P54217;
DE  Function: Paternally sperm-supplied factor required for embryogenesis (PubMed:8565851, PubMed:20971008). Plays a role in preventing polyspermy possibly by promoting the formation of a continuous and cohesive eggshell chitin layer (PubMed:20971008). {ECO:0000269|PubMed:20971008, ECO:0000269|PubMed:8565851}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030703;
GO  GO:0007275;
GO  GO:0060468;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDEEIDISTALNNKTTPKKKSLKRNSNSQEGYESPEEREIVYPSVFGAIGTPMAKSDNAKEWDEWKEKERKKDKAEWKR
SQ  YLRSKWDMTQGHLPLVSDSEFLKGRKEHKEYNSKARMDILDGLDEVNEGFFNCGKGAAMNIRYNDKNVSKKGAKKFVATV
SQ  ETAMKKAGNPTMEQMMTDDLDEDEARAEAEWERQREQRKLASRAYDAAMDEREDDAKYVPWDEYCQEMEELGKELKIGEK
SQ  HYKKWLEKKMDENKVTHKFNAYQLDLKCLDEDAFSNKKSLKSVVRNVQKFYRKMREPKK
//
ID  Q17902;
PN  Egalitarian protein homolog;
GN  egal;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:20005871}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}.
DR  UNIPROT: Q17902;
DR  UNIPROT: Q65ZH5;
DR  Pfam: PF01612;
DE  Function: Part of a complex with bicd-1 and dlc-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells. {ECO:0000269|PubMed:20005871}.
DE  Reference Proteome: Yes;
DE  Interaction: Q22799; IntAct: EBI-328330,EBI-328324; Score: 0.75
DE  Interaction: V6CJ04; IntAct: EBI-2006416,EBI-328330; Score: 0.51
GO  GO:0005635;
GO  GO:0008408;
GO  GO:0003676;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEAKNMALLFFMDHLMQKNGRRTIHDLSCQFGARGFSEEMRNAVGTTQEGLTEFLQGHPSLFTVEGDQVILNGHNDLNA
SQ  KNNPLLQSGIRSRNYEKEAVDFFVTKLTKFGPELQIKSLLGHRSQAAPEVRLVSGRHLKEFCEFLQSQVDYFVVEGDRVR
SQ  LKNMPEPDENAIEMDDEGRPLAGVKAKQAAVEYLKSVLEQNEDQPIPLDQFYQNFCQRFSHTIRQDVATNPKELLQFLKL
SQ  NRGLFFIRSNKVSLVKNRLNEDGSENGSDEGEETNNNGMFPLDQSALTRIHFVKALKPAQDLISRLWQDINNMEKKVVGL
SQ  DLKTVTVGVDGEIFLSLGVIATTSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDT
SQ  QVAHSLLQHEKFNKSLNEMRPISFINLQRVYYPQSIMLSDVTPRKMSMCPNWGVRPITEEFQLTIVEEAHCLLSALYQSL
SQ  SNLIPVHLRGVFEDKCIEVNHPEVLLASPNRPPPQPFISSPYRASTRRDVRNGGSIMQSFSPAPYAAAPRPQMSDACTQT
SQ  FSTGDIEVLNVFYE
//
ID  O60100;
PN  Probable importin subunit beta-4;
GN  kap123;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus. Nucleus envelope.
DR  UNIPROT: O60100;
DR  UNIPROT: Q9US72;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import, its predominant substrate seems to be ribosomal proteins. Binds to nucleoporins and the GTP-bound form of gsp1 (Ran) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0008536;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDAQFTLELTQLLFQSIAPDTTQITEATRALETKYLKEPGSLLSLFHIMGTCENPQVRQLAAIEARKLCHKYWSSVDADV
SQ  QNQIRSNLLDITLKEPESIVRHAFGRVIAALAKLDLPEGKWNELSAFLVQATMDQNDSIREMAVYVLYSIAETVDLDNKL
SQ  LLDFVNLFSQTITDSSRTVRVTSVQGLGAIAEVLESDDKKLLHAYRATLPGMLLVLQDVVQVGDVDASKQVFDVFNTFLI
SQ  ASGAIISKALGNIIEIITGIANSKQVDDEIRCMALSFIISCIRFKSRKLQALKLGKPLVLTLMEVATEETTDDIDEDCPA
SQ  RLALRSIDLLSTHLSPSQVFYPMFEAACAFSQSPQASYRKAALLSIGVAVEGSSESVAGNLPNIFPIIINGLCDNDMDVR
SQ  QAALLALSQIAVEIPTEVSKHHAQLLPLVFELMSTQGVKVGKSACNCIDALLEGLDKSEISGYLPMLMERLVGLLEFSDT
SQ  PDIKSCVAAAIGSAAFAAQDDFIPYFERTMASLSQCLHTTDDDEGYELRGTVMDTLGAIANAVGKQAFLPYTEQLIQLAY
SQ  EGIQIDHSRLRECSFCFYAVLARVYKEEFAPFLEHIVPALFKSIDQDESDILSERIGAPTAEEISQLLDSVETNEEENDE
SQ  ELEKAMGVNSAIAMEKEIAADALGEICMYVGAPFTPYLEPTVEKLVACTTHFYEGVRKSALSSLWRCATTYYKVCNVPQW
SQ  QPGLPLKVPVPDTVKNIFEAVRKCTFDTLEEEYEKTVATDILRNFAESIKTCGPVVLGDDYEKLCEVVMEVLQKQHIVQA
SQ  GDVFDDDFEEEDIVSNEEVDDTEQDALLIDSACDVVIALAVALGGSFADSFKVFYPQIVKYYMSKNGNERAMAVACVGEV
SQ  AGGIESAITPFTRDVFSLFMAALEDSEGEVRSNAAYSMGLLCQFSTEDLSSEYLNILQKLQPFFTQEVFRTALDNAIGCI
SQ  SRLILHNQNAIPVDQVLPIVFSKLPLKEDYLENAPLYHMILALYRQQNPCLVQHLGELIPVFASVLTGSPEQLNDELRSE
SQ  LLSMVKEIAPQYESVVSNYPQLVALLQ
//
ID  K7NAJ3;
PN  Interferon alpha/beta receptor 1b;
GN  ifnar1b;
OS  8022;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:24244163}. Note=Mainly detected in perinuclear regions, when overexpressed in RTG-2 cell line. {ECO:0000269|PubMed:24244163}.
DR  UNIPROT: K7NAJ3;
DR  Pfam: PF09294;
DR  Pfam: PF01108;
DE  Function: Involved in antiviral response. Associates with IFNAR2 to form the type I interferon receptor. In the presence of intracellular IFNAR1 (IFNAR1B) and IFNA1 (iIFN1b isoform), may mediate STAT1 and STAT2 phosphorylation and induction of EIF2AK2, MX1 and RSAD2. {ECO:0000269|PubMed:24244163}.
DE  Reference Proteome: No;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004905;
GO  GO:0001934;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLAELPQPQNLTLLTLNTQYVLTWDWDQTTTGNSVSFTVEYMAKYKMKMKKKNWSRVCERTTRTRCDLTGSDLHYLGMYV
SQ  LRVRASADGVDSDWVNKDFCPDIDASLGPPSRAELAPVGNLLDVTISDPLTSTQHSMKEHVLFLYYRILYWSRSDDPQGL
SQ  KPKVLDSSNNLVTPPELEAWAWYCVMIQSRYDYYNKTSSYTEPQCMQTEGDTPYGQIFLYFLVSMMVCFLLVLLSSYAFF
SQ  RFYRGLKNTFYPSIQLPAHIQEYLCDSSPGSDMPRLITADSEAELCCDKLTICPEVVLLEIHVPPPLTAPPSELEQDSGR
SQ  HIRQDSGDSGIYSTEGGSAQQGRSGGEPIRRDQEVDSWQTLEQVKMEEMGRELADERDLDEGVVDVCV
//
ID  O77691;
PN  Protein S100-A6;
GN  S100A6;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: O77691;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0042803;
GO  GO:0044548;
GO  GO:0005523;
GO  GO:0008270;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MACPLDQAISLLVAIFHKYSSREGDKNTLSKGELKELIQKELTIGAELEDSEIAKLLDDLDQNKDQVVNFQEYVTFLGAL
SQ  AMIYNEVLKACS
//
ID  A7WNB1;
PN  Matrix protein;
GN  M;
OS  666363;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: A7WNB1;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MNKMNQLVRFVKDTVAVRKPQSEDKSYLPIPSTIGGHEVNSPFAEPTAPSLGIIQPKCKRADWLIKSHLTITTNYEIKEW
SQ  ETWDRAISDILDLYDGNPVFKPILLFVYYVLAYNARKIPGPSNGVRYGAYFDELTTVWHAIPELMNQEIDYSYNHRVLHR
SQ  KIQYVISFKIQMSSTKRRTSPIESFIEVTSEGLKHTPQFTTILDRARFVYSLTGGRYVIHPF
//
ID  Q6NRG5;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  ndor1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}.
DR  UNIPROT: Q6NRG5;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DE  Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Transfers electrons from NADPH to the Fe/S cluster of ciapin1. {ECO:0000255|HAMAP-Rule:MF_03178}.
DE  Reference Proteome: No;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0003958;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPQQNLLILYGSQTGTAEDLAGRLSREAKRHHFNCRTEALDEYRVANLINEHLVIFVCATTGQGDPPDNMKNFWRFIFRR
SQ  NLPHNALCQMDYAVLGLGDSSYPKFNFIAKKLHKRLNQLGACPLLPAALGDDQHELGPDAVVDPWLKDLWSKVLSMFPLR
SQ  PGLEIISEDVLLPPKYSLRLLEEKVGQSELSGDAYERDFISNNTTPPSEIHPFLAPVLSNERVSAHDHFQDVRLIEFNIT
SQ  GSAIQFYPGDVVMVQPRNSLLHVEQFCSLLHLDPLNKVVVEPSDPESPVPMHLAALCSVQQLVERYLDICSIPRRSFFQL
SQ  FCHFSPDEMEREKLKEFSCAAGQEELYSYCNRPRRTILEVLVDFPHTTRCIPATFLLELIPQIRPRAFSIASSMEALPNT
SQ  IQILMAVVQYKTKLIEPRRGLCSTWLASLPPHGTERVPIWVKKGSMKFPCDPDTPVVMVGPGTGVAPFRAAIQERVANGR
SQ  PGNCLFFGCRGKSKDFYFEKEWEDLGNRGYLTLFTAFSRDQEDKIYVQHRIKENSKLLWDLIGTKQGYVYIAGNAKLMPN
SQ  EVTDALKWVLQLEGGMSAPDAEQYLASMEKSCRFQSETWS
//
ID  D8V072;
PN  Matrix protein;
GN  M;
OS  1559361;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: D8V072;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MLSRIKQGIKTKRSSSSSSSRSKTGDEDSSLMLRWVYDNDPPLKQTDTFQYLMAPTAPTDKASSSYIATTYKVDCKVEII
SQ  SRASIRNFDELINIASCLIDSYDGQLLIKPWIITVYLTIITHLVKEPDTHGVRSSVNRYHNGFNEILTLYINKNFAPENK
SQ  KYSFKKNLSTTHKGNQCNIIISIDLLPTDRKGKSIKDVYEVKMPDNREIPNFQQMLKPYNLKVKEKNGKYLISHKMSSSD
SQ  DSIDVSDSDENEF
//
ID  Q6FSC7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q6FSC7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEAQLHELQEEITRSSDLVLTEQDKRLQGTLREIDQSIRKLIETSDYLKLSGDADSLIDIKQLEVKSRELDSLMDLLRKL
SQ  YWREESLDLFLKYTINSDAEQVPVFSDTDPKYQSLQDEVSHLRDDVMTVKNQEIDQITGEILQVAHEITEKQDQVNMLYL
SQ  ETTNELDKCWELLDEWQRLQDDQRITKNEDNSNRKDTELNAMEECYEEWKTLEELAVLNDNLQKQIDELEKVDNKAINST
SQ  QLAEESIVNTVQLNDLIDMWKRRIIASIHEDISEIVLYPYSRKLQLRVANRYTIIIQLDKHQTHDGKSTIHDIDLFTEQD
SQ  SRIIPMRELRKQVLQECKGHSNILQALKNIINRVINNDN
//
ID  A7TFD7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  436907;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: A7TFD7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000778;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  METQAVKTIRDELRELENTVAQASDMVLSEQDHRNASAIREMTQSVIAMSKENSLISVSNEIDYNEEIGNLAIDPSLIDE
SQ  KIKQSNNFVELLKLTHLEQEALDYFLRYTISSTNTLELESTSDPKFVSLENEVTELENKTLTEHRDKIQEAKKDISDKSK
SQ  DLANKQDQINELCLGAANSVDECWKMLNELEDIHSQRDNDVKETLSQDTTTTSDLIEETYKEWSSLQTSLTELNNSKDEL
SQ  DQLIAFKNEKHKDNDSTKIRNANIKNKTITENVKMLKLLINFWESNFIVPGSKKSKLSNLEVYPQTKKFQFKCAEQYTVI
SQ  IQLNQNGGSIKSIEIFENDGKSVQENKNLSSLILNKYKNPLSSYPIFQVINDIVEELK
//
ID  P03248;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  10519;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P03248;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEVWAILEDLRQTRLLLENASDGVSGLWRFWFGGDLARLVFRIKQDYREEFEKLLDDIPGLFEALNLGHQAHFKEKVLSV
SQ  LDFSTPGRTAAAVAFLTFILDKWIRQTHFSKGYVLDFIAAALWRTWKARRMRTILDYWPVQPLGVAGILRHPPTMPAVLQ
SQ  EEQQEDNPRAGLDPPVEE
//
ID  O18737;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  CALCOCO2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: O18737;
DR  Pfam: PF17751;
DR  Pfam: PF18112;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEETVDDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDITCYYTLTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPVD
SQ  LNSESAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQSEVEEIEQHNKELCKENRELK
SQ  DSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQ
SQ  GREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMII
SQ  HDVLQREKEKMEKENDYLKRENNRLLSYMGLDCDSLSYQVPTSNQGGTRQDPGLVFGNPYSGIQESSAPSLLSIKKCPTC
SQ  KSDFAADVFDHNLALEQHLQTLSLNCPICDKTFPAKEKQIFEDHVFCHTL
//
ID  A8T6P4;
PN  Rab effector MyRIP;
GN  myrip;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}.
DR  UNIPROT: A8T6P4;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DE  Function: May link secretory vesicles to actin filaments (By similarity). May function as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030864;
GO  GO:0048471;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0017137;
GO  GO:0006886;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLSNNEAEHVLRVVQRDMQLRKKEEERLSEMKQELEEEGSRCLLLSKQQKFNEHCCIRCCSPFTFLLNPKRQ
SQ  CLDCHYNICKSCCSYSQSERGYICAACQKSRHLRTQSLEWFYNNVKSRFKRFGSAKVLKTLYRKHIIERGALSELPEVSA
SQ  HEGSNDNGSICDGSDSTLYKQSEGHSMADTLTVALRVAEEAIEEAIAKAENYKDSLEKQNEARYLHEHKEELIEELATTI
SQ  VQKIIQRGKRPEIQEEYEFVWPQNQKSELPSPTSTQNPLATQNSHSTSQPGAVAQSDISKRSRSAYSSDDSPEKGPEVGM
SQ  APGVPKSTEVETDIQNYSSLRRESRALSLPGWKSVDRLENSSASSVLQSPDGNWIALQSSQHSRPSLLTKRKSLVFSVLE
SQ  KESGVVSAYDEMGSDSDPEDQGGWGAALLQFRRRLSDETYYTDSQHDPEWTFTQHPPITSPSSGQYTNTETLNSDSETSP
SQ  SPSTRARRAPVMKKGPPETHLYPYYRHPADIVALPQLKPDVLDVNFNPHLGGDSSDGEERSEQVKRSRRRRKSKRETSEH
SQ  SRAHNALYSAATAENSTVLLNAMMMRRQQSQENTVPLNHQTPDSVTSPDILTFNNMSPEPEYQNTLAHNSSAASLPLLSQ
SQ  LGSNNPGFAPQDPLLRAFPVNETLEEELKYKLSELIGQVSERDVKSSDFEPISEVGNKQEDRVSEKDSGKLRPKERRESK
SQ  RESKLREMEKQSERQTVKLMDTSDAVRQINIERQMKKERERQRDIERQVERERERQRELEKQIEKDRERRREIEMQVEKK
SQ  QERQKEMEKQLKQEQERQSEIERDLEKKRKSIRMEKRN
//
ID  A4IF89;
PN  Exocyst complex component 8;
GN  EXOC8;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: A4IF89;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0035091;
GO  GO:0017160;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0022617;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYL
SQ  ESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGGGGAGGRDQLRGQTGFFPSPGGASRDGSGPGEEGKQR
SQ  TLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDGLAVVN
SQ  VKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSEKRRREQEEAAAPRGPPQVTPKASNPFEDEDDDEP
SQ  TVPEIEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRARVDERVRQLTEVLVFELSP
SQ  DRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAG
SQ  TDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVRVAKEHCQQLGDIGLDLTFIVHALLVKDIQGALHSYKE
SQ  IIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELH
SQ  MVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPES
SQ  TTSVV
//
ID  Q6CV05;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q6CV05;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTHYHSEYYSEVEKFEYQVTHVTEQILQEQDRLRGSTLHEYNQTILQLVSDYEMFNSNGQCDPSEINLPLEKLESWTNSL
SQ  KQIHLELESIDNFLRYAIPSDQTILNLSKFNESKYETLQAEVSELRDINVVQLQKEIESLQQQITTKSDENLLISEKIKE
SQ  SCLEASQDIDQCWKLLEQLEAYENANPSTEVITTTDPAFSTYNQWKWNQLAESELKHINQQLITLRATKEKLDKVFSKRS
SQ  ELETSPKSIETFTSYQLLSQLWRSKFIRQLLPDIANLEVYPQSGKLKFEVGIMQVIMQIESGIIKSVSLFSYELSYDRIE
SQ  TIKEDILGRIEHQKSLFKVLVVITDYIVNSL
//
ID  Q751U7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q751U7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSTKDTSGQSGYANDIRKLGEQTAHVSEQVLVQQERQRLGALEELHQSIIQIAEENSFVTPIKKDAANVHIDPRGIAVSV
SQ  QQFKQLAEVLKVTHLEQETLDNFLRYTISDNDQLLDIKSVADSRYARLAEEVCQLEQEELRHLENEIISLNGNITEQTTK
SQ  VIDANEKVKEECLEVSNGIERCWGLLNELETLRSTTDEGNVELGPLEETYQKWKSVDHFLQQKLHLKEQLRVLEDTRKSL
SQ  SEVTKSSGNRAPDLDASEKFVTYRLLDSMWKKQFVDTTKIRDLELYPRTGKIQFQVADTIYVLAISGDQISNIQLFNDKL
SQ  PAADLENNTQDLNKRFLGTSDVRRVVDFITHQQAVPQAQVH
//
ID  C5DK07;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C5DK07;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADDPTINGLELQLNAAEEHATALTEEALQNQDLHYKEVVEQLKRSVEQLVEDNESLFTAVDLPPEVDPTCISGRILDLA
SQ  QLTQQLKSTHLQQETLDNFLRYTISSTDILQLESESDERYASVSRAVSQLQDNDIIQLDSEVDQIKQDIRKAGQTIADQR
SQ  EALNELCLETGNLADECHTLLSELEEATRTREMVEKQAAVEVTNDHPVEEMYASWQSLKEELQQESHLRRHLNQLKQSKA
SQ  SLEAILGTKNGNEHKDTNVMQEYASYDAFIRFWISKFTNKEMENLEVFPRSNKFQFTHRGTDVVISLGPRGISRVELYGK
SQ  GIPLEKIAAARKDVNEEASRGEELYMSINRIIDKIKEHTTVS
//
ID  Q6NRQ2;
PN  Nucleolar complex protein 4 homolog A;
GN  noc4l;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q6NRQ2;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARKTKHACRIQDKRSDAERQDLDTKLAAVLESRGNANAVFDILEHLESKKEEVVQAAIRTASKLFEVMLEKRELYIGD
SQ  LPAENGTLPDTYSAEDKYKMWMRHRYNSCAACILDLLQHSSFSNQELALCTLMKFIQLEGKFPLENSEWKDSYRFPRELL
SQ  KFVIDNLLQEEADCTLLITRFQEYLEYDDVRYYTMTVTNDCVSRVQQKNKLVLPPVFQTNVFCLLSSINIPVEESALGNF
SQ  LVTKNVNNEDWKPSKLKDHKRVFERVWMIFLKHQLSVSLYKKVLLILHESILPHMSKPTLMIDFLTAAYDVGGAISLLAL
SQ  NGLFILIHQHNLEYPDFYKKLYSLLEPSIFHVKYRARFFHLANMFLSSTHLPVYLVAAFAKRLARLALTAPPQVLLMIIP
SQ  FICNLIRRHPACRVLIHRPSAGDLATDPYIMEEQDPAKSQALESSLWELEVLQQHYHGDVVRAANVISRPLSAQESDISG
SQ  LLEISSCELYDKEMKKKKFKSVPLEYEPVRGLLGLKSDITAQHFTF
//
ID  Q9Y7P8;
PN  Putative uncharacterized membrane protein C191.04c;
GN  SPCC191;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9Y7P8;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHSVCSIFLSCSHRVIQAKHPPFPLFHSYFHIPDFLSFVFPFVASPPLAFARRKLDHVPKKFARSIGPFLLIVFLFFNLF
SQ  PTFFFLPFFPDTTKRPNLAD
//
ID  Q9FYP9;
PN  Importin subunit alpha-2;
GN  P0011G08;
OS  39947;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region.
DR  UNIPROT: Q9FYP9;
DR  UNIPROT: O80332;
DR  UNIPROT: Q0JQJ0;
DR  Pfam: PF00514;
DE  Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. {ECO:0000269|PubMed:11124253}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADDSASPSPSSASPLQHHREALKSSVRNTAASRRREQAIAIGKERREALIRAKRVCRAPISGSDEAEMEEGDMVVDEEK
SQ  ACLEAKTAHAVEELKSALSIQGKGVQKKKIEALRDLRRLLSQPEVPLVDTAIKAGAVPLLVQYLSFGSSDEQLLEAAWCL
SQ  TNIAAGEPEETKSLLPALPLLIAHLGEKSSTLVAEQCAWAIGNVAGEGAELRSTLLAQGALRPLTRLMFSSKGSTARTAA
SQ  WAMSNLIKGPDPKAANELITIDGVLNAIIASLEKEDEELATEVAWVVVYLSALSDRGISLIVRSSVPQLLIGRLFSSENL
SQ  QLLIPVLRGLGNLIAADDYMVDSVLTVGHNIIDQALSGLIKCLKSDNRVLRKESSWALSNIAAGSFEHKKLIFASEATPV
SQ  LIRLVTSMQFDIRREAAYTLGNLCVVPTGNCELPKIIVEHLVAIVDGGALPGFIHLVRSADVDTAGLGLQFLELVMRGYP
SQ  NKQGPKLVEMEDGIEAMERFQFHENEQMRNMANGLVDEYFGEDYGLDE
//
ID  P11017;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
GN  GNB2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P11017;
DR  UNIPROT: A5D7A9;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Reference Proteome: Yes;
GO  GO:0005834;
GO  GO:0048471;
GO  GO:0003924;
GO  GO:0051020;
GO  GO:0044877;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI
SQ  IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITS
SQ  SGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
SQ  FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGV
SQ  TDDGMAVATGSWDSFLKIWN
//
ID  C5DZ48;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C5DZ48;
DR  UNIPROT: B2G406;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000777;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKSDLDGYEVRIKSLENQTAHYSEQALLEQEQRVLASLREITQNVIAMGQENSLVEIKGELESKEESELVIDPSGFQEKI
SQ  DTFVELVELLKVTHLEQETLDNFLRYTISSSNLLQINSVQDAKYVELESQVKELEQGTLESHKREIEATKGQIKNLCQEL
SQ  SMAQDSINETFLDTSNALEECDALLNELTQLRMEKQTSEEADTIEDDPVSQTYEDWESLQKSKLELRLLEEETSRLQSRV
SQ  ESYEDYQKRSRQLSNNDPRMLQNHKALELLVELWMTKFLPQPGISHLELFPQSRKFQFDVEPTFTVVITLADQTTFQNVQ
SQ  VYRKDAKSLVMDHGLNDEIKNSYLGTNNIYNGLNDIIHTLQRRVQAKGSN
//
ID  P52297;
PN  Importin subunit beta;
GN  kpnb1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14974}. Nucleus envelope {ECO:0000250|UniProtKB:Q14974}.
DR  UNIPROT: P52297;
DR  UNIPROT: B0LM40;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000269|PubMed:7878057}.
DE  Reference Proteome: No;
DE  Interaction: P20676; IntAct: EBI-618940,EBI-12392; Score: 0.44
DE  Interaction: A5XAW2; IntAct: EBI-3511040,EBI-618940; Score: 0.35
DE  Interaction: A0A1L8G4G8; IntAct: EBI-3645294,EBI-618940; Score: 0.35
DE  Interaction: Q6PAY1; IntAct: EBI-6285025,EBI-618940; Score: 0.35
DE  Interaction: Q91349; IntAct: EBI-6285043,EBI-618940; Score: 0.35
DE  Interaction: Q6DCP4; IntAct: EBI-619012,EBI-618940; Score: 0.44
DE  Interaction: P62826; IntAct: EBI-286642,EBI-618940; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0008536;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELVTILEKTVSPDRNELEAAQKFLEQAAVENLPTFVVELSKVLANPANSQVARVAAGLQIKNPLTSRDPDVKAQYQQRW
SQ  LAIDASARGEIKTYVLRTLGTESYRPSSASQCVAGIACAEITVNQWPQLIPQLVANVTDPNSTERMKESTLEAIGYICQD
SQ  IDPEQLQHKSNEILTAIIQGMRKEEPSNNVRLAATNALLNSLEFTKANFDKESERHYIMQVVCEATQCPDTRVRVAALQN
SQ  LVKIMSLYYQYMETYMGPALFAITVEAMKNEIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQ
SQ  YLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPESC
SQ  QLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLGAEPRVASNVCWAFSSLAEA
SQ  AYEAADVADDQEEPSSYCLSSSFEVIVQKLLETTDRPDGHQNNLRSAAYEALMEIVKNSAKDCYPAVQKTTLVIMERLQQ
SQ  VLQVESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLG
SQ  AEFLKYMEAFKPFLTIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEMMQFLLENLGNENVHRSVKPQILSVFGDV
SQ  ALAIGGEFKKYLDVVLNTLQQASQAQVDKSDYDMVDYLNELREGCIEAYTGIIQGLKGDQENVHPDVMLVQPRVEFILSF
SQ  IDHIAGDEDHTDSVVACGAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKTKTLATWATKELRKLKNQA
//
ID  P11048;
PN  Lamin-A;
GN  lmna;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus. Nucleus envelope {ECO:0000269|PubMed:25157132}.
DR  UNIPROT: P11048;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
DE  Reference Proteome: No;
GO  GO:0005882;
GO  GO:0005635;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  METPGQKRATRSTHTPLSPTRITRLQEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVISREVTGIKSAYETE
SQ  LADARKTLDSVAKERARLQLELSKIREEHKELKARNAKKESDLLTAQARLKDLEALLNSKDAALTTALGEKRNLENEIRE
SQ  LKAHIAKLEASLADTKKQLQDEMLRRVDTENRNQTLKEELEFQKSIYNEEMRETKRRHETRLVEVDNGRQREFESKLADA
SQ  LHELRAQHEGQIGLYKEELGKTYNAKLENAKQSAERNSSLVGEAQEEIQQSRIRIDSLSAQLSQLQKQLAAREAKLRDLE
SQ  DAYARERDSSRRLLADKDREMAEMRARMQQQLDEYQELLDIKLALDMEINAYRKLLEGEEERLRLSPSPNTQKRSARTIA
SQ  SHSGAHISSSASKRRRLEEGESRSSSFTQHARTTGKVSVEEVDPEGKYVRLRNKSNEDQSLGNWQIKRQIGDETPIVYKF
SQ  PPRLTLKAGQTVTIWASGAGATNSPPSDLVWKAQSSWGTGDSIRTALLTSSNEEVAMRKLVRTVVINDEDDEDNDDMEHH
SQ  HHHHHHHHDGQNSSGDPGEYNLRSRTIVCTSCGRPAEKSVLASQGSGLVTGSSGSSSSSVTLTRTYRSTGGTSGGSGLGE
SQ  SPVTRNFIVGNGQRAQVAPQNCSIM
//
ID  A6ZXN8;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A6ZXN8;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEVEIFFQLRKWIPTN
SQ  FMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  A3KNS9;
PN  All-trans retinoic acid-induced differentiation factor;
GN  atraid;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}.
DR  UNIPROT: A3KNS9;
DR  UNIPROT: Q502E7;
DR  UNIPROT: Q5RID6;
DR  PROSITE: PS00022;
DE  Function: Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030154;
GO  GO:1903363;
GO  GO:0033689;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSN
SQ  CSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTV
SQ  QMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT
//
ID  P52302;
PN  Protein lethal(3)malignant blood neoplasm 1;
GN  l;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:8174791}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8174791}. Note=Mainly around the nucleus.
DR  UNIPROT: P52302;
DR  UNIPROT: Q59E19;
DR  UNIPROT: Q8MS87;
DR  UNIPROT: Q9VRU6;
DR  Pfam: PF00379;
DR  PROSITE: PS51155;
DE  Function: Required for differentiation of the phagocytic blood-cell type, the plasmatocyte. {ECO:0000269|PubMed:8174791}.
DE  Reference Proteome: Yes;
GO  GO:0062129;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0008010;
GO  GO:0040003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLKLMAFVCALLLLCTLTHVLSAATTVRPYKFGFTIDEQQHRAEKRDERGIIMGEFGFITADGIYHVTVYATDEEGKFR
SQ  IISMKSYPYAGPVGSKSVPVTTTPKVLLPAAPVALPKYNFNSEACSGCFLKKSPPKTEIRTLSQPLAPVQPGKPDGSSDI
SQ  GLNVQLPFRESIAQTVASRLGLLQDTLQTSNTNTNAPNTKTIELGLNIAMSTYYTTKNAVTGHVSTQTSNSQTPSANTKI
SQ  DYNVGVVEKASPPVYRPLNIRLNEDVMRQAITYGNTIPGHVPLPNQPLVETSLLPASQVKIFALDGNAKVPLASNIQSVA
SQ  QHPNAGLNAKVPLASNIQSVAQHPNAGLNAKVPLASNIQSVAQHPNAGLKNINRSGVSSAKTLANTKTRPPHTFNPHQTP
SQ  LLSSATAPGISGVTANTPTGNVPSNGGGIAAGKAPGNPQAGGSGGIIGAGAPGGRKVSAGGIGSGSAIGGVSGGSKASGN
SQ  GGAIGSGSAIGGGATGSKASGFGFGSNIGGGVSGSKPSGFGSESKIGGPDSGSKALGFGSGSKIGGGITGTKASGFGGEI
SQ  GSGRGSASSATGDLYKFKYILDYNGHEETGGRNGDKQGSYFAIGEDAVQRTIEYIANEFGFQPHVSWRKLDAKEALPEEN
SQ  SLKHYEFKWFNQE
//
ID  Q9LTY1;
PN  Mitotic spindle checkpoint protein MAD1;
GN  MAD1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:22457071}. Note=The nucleus envelope association requires the presence of NUA. {ECO:0000269|PubMed:22457071}.
DR  UNIPROT: Q9LTY1;
DR  Pfam: PF05557;
DE  Function: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. Required for anchoring MAD2 to the nuclear envelope. {ECO:0000269|PubMed:22457071}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007094;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MILRTPQPKRLRSDAGESPFPTGATGSGNQLIIYEDSPLPAPAPLQTSHDHSADQHLCTYQCRQMVKADVLDALSTAEKQ
SQ  VEESKTKLQTLNANFTEADAERKHFRDKFLYSEQELAAAKAREKMLQEQLLMEINNSQERYTKELQSCHELEVKLQNEMN
SQ  LRKKAESSAATAEEKAKLLEDKLTQLSGSVDREKKRLNNDIAQLGKEAKLSVARIGADLERMQCRAQNAETESNLLRSQL
SQ  EHLKLIFDECLQEKTEVDKKLSSFTSEAASSSDNSVLVKHLQEELKRYEAEVREARKLKSRHLDAELLNVNLLEEQSRRE
SQ  RAESELSKFHDLQLSMEKLENELSSWKSLLNDIPGVSCPDDIVMRFSVLQNEVVQSTMKIGEASTRIKQLEETLEAIQLG
SQ  RQNAVSEAALAKEKSEALKTDVKRIEVMLTLVTEEKEQLKAVVNELRKSNSEGSVSGAADGALIQGFESSLAKKENYIKD
SQ  LEQDLNQLKDVNNRQRTEIELLNEKLVDEARRNKSLERDSDRLRSEISLLESKLGHGDYSAANTRVLRMVNTLGVENEAK
SQ  QTIEALQAELQKTKERLQAVEELKSQSGDAGKLVDSHITGKIAQLKEQNATLEKREERYKTVFADRISVFRRACCELFGY
SQ  KIVMDEHQRPNGIPVTRFTLQSIYAQSDDEKLEFEYESGNTSILNNEYASQGDIAKQIEIFIRKFNSIPAFTANLTMESF
SQ  NRRTLY
//
ID  Q99P25;
PN  Translin-associated factor X-interacting protein 1;
GN  Tsnaxip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12036294}.
DR  UNIPROT: Q99P25;
DR  UNIPROT: Q9DA98;
DR  Pfam: PF15739;
DE  Function: Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007275;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANLQERKSFSKPRISIQASGGTPEAKGIEKRKLSQKRRTLPLQLSLGGHLSPWPTYTSGQTVLHNRKPCSDDSRNRANS
SQ  CQQQSMSISKPKYLEQLENYLRKELLLLDLSTDSAQELRLQPYREIFEFFIEDFKTYKPLLSSIKNAYEVMLAHQKERIR
SQ  SLEPLKAKIVTMNEDCSERVLAMRAEERYEISVLKKEKMNLLKLIDKKNEEKISLQSEVAKLRRSLAEEYLRYLTERDAR
SQ  KILIGDLNELRYQQEDMSLAQTPGVWGEDPVKLTLALKMTRQDLTRTQMELNTMKANSGDVVPRRDLEMQEKTNMELQEQ
SQ  LESLKADYEEVQKEHELLLQLHMSTLKERDQFYNELQEIQRTSTPRPDWTKCESIIAGGPERWLVLAEGKNSDQLVDVLL
SQ  EEIGMGLLREKDFFPGLGFGDAIPPFLRFDGPVKNKKPSKKEVVNLLKDAWKERIAEEQKEPFPDFFFNFLERRFGVNDA
SQ  MAWAYTIFENIKLFRSSEIMNQFYAVLMGKNLESVYINQKKTLSHLLKELLSVDTQNEGSITMEQFSTILKTTFPLKKEE
SQ  QIQELMEAVGWGPDSSNTDMLNYRSLFNEDEEGQSEPFVQRLWEQYESDKEAYLEELKQELDLDPLEDVTLLKMRGTLMN
SQ  IDPTMDKQTLSAYLSQAYQIPAIDVPLEDEEKQGIISIKVETALDRLRMADTKRVGPREPDPAS
//
ID  Q9VVE2;
PN  Protein rogdi;
GN  rogdi;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Cell junction, synapse, presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q9VVE2;
DR  UNIPROT: Q32KF2;
DR  UNIPROT: Q8IQP4;
DR  UNIPROT: Q95T16;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P42287; IntAct: EBI-147361,EBI-122571; Score: 0.37
DE  Interaction: P62152; IntAct: EBI-182924,EBI-147361; Score: 0.37
DE  Interaction: P10734; IntAct: EBI-170297,EBI-147361; Score: 0.37
DE  Interaction: Q7K4Z4; IntAct: EBI-147361,EBI-159623; Score: 0.37
DE  Interaction: P11929; IntAct: EBI-147361,EBI-99597; Score: 0.37
DE  Interaction: Q9VU23; IntAct: EBI-147361,EBI-131541; Score: 0.37
DE  Interaction: Q9VYV9; IntAct: EBI-147361,EBI-199701; Score: 0.37
DE  Interaction: Q9VY61; IntAct: EBI-109208,EBI-147361; Score: 0.37
DE  Interaction: Q0E8K5; IntAct: EBI-147361,EBI-90335; Score: 0.37
DE  Interaction: Q9VCH1; IntAct: EBI-147361,EBI-136479; Score: 0.37
DE  Interaction: Q9VVC2; IntAct: EBI-147361,EBI-141024; Score: 0.37
GO  GO:0030424;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0048149;
GO  GO:0032502;
GO  GO:0007035;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKMLADTEREEALNLQIEFEWVLRQEVHAILKQLRSILVECAHRFPVPLYENEGKKTEKFILTVSPDQLKAVLTLTGDAI
SQ  TQADISFKLCKAPSQTQRTSITHDSPWKLQQVQDAANHLQTAINHIDDVDDSYHFKTSDEVLHVIGNILDALQRGRNSLL
SQ  VPKKKPIDELIKGRNMKSLVPNLPEDLAVSFYLQSHKLIIAVYQLLNNQGTMRFDSRQAEASVQWLNDVLLLLMNGQKLC
SQ  QQLKDKISVFSVYKDFTVGSRSPSALSY
//
ID  Q9QXY4;
PN  Opioid growth factor receptor;
GN  Ogfr;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11890982}. Nucleus {ECO:0000269|PubMed:11890982}. Note=The OGF/OGFR complex is probably translocated to the nucleus. Colocalized with OGF in the perinuclear region.
DR  UNIPROT: Q9QXY4;
DR  Pfam: PF04664;
DE  Function: Receptor for opioid growth factor (OGF), also known as Met- enkephalin. Seems to be involved in growth regulation.
DE  Reference Proteome: Yes;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004985;
GO  GO:0040008;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDPDCDSTWEEESEEDGEDGQADDTTDEDTGDDDGDAEEARPSLFQSRMTGYRNWRAMQDMQRYRHNYPDLTDQDCNGD
SQ  MCNLSFYKNEICFQPNGALIEDILQNWKDNYDLLEENHSYIQWLFPLREPGVNWHAKPLTLKEVEAFKSSKEVRERLVRA
SQ  YELMLGFYGFHLEDRGTGAVCRAQNFQPRFHNLNSHSHNNLRITRILKSLGELGLEHYQAPLVRFFLEETLVQHKLPSVR
SQ  QSALDYFLFAVRCRHQRRELVYFAWEHFKPRREFVWGPRDKLRRFKPQTIPQPLTGPGQADKDEGSRDPSQEAGTQGRTC
SQ  GSGRDLSGDSGTAEDPSLLNTKPSDGGTLDGNQRDEAKSLSPKESKKRKLEGNRQEQVPGEADPQGVSEVEKIALNLEEC
SQ  ALSPISQEPREAEPPCPVARVANEVRKRRKVEEGAEGDGVVSNTQMQASALPPTPSECPEAQKDGNGPEDSNSQVGAEDS
SQ  KSQVGPEDPNSQVGLEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVVGPEQAASKSPVEDPDSDTMGT
SQ  SVDESEELARIEASAEPPKP
//
ID  F4HYD7;
PN  Ran-binding protein M homolog;
GN  RANBPM;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:22676313}. Nucleus {ECO:0000269|PubMed:22676313}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
DR  UNIPROT: F4HYD7;
DR  UNIPROT: Q8VYQ8;
DR  UNIPROT: Q9C8P9;
DR  Pfam: PF10607;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50897;
DR  PROSITE: PS50896;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSSPPPANSANGDTTNNGENGQDLNLNFLDKIRLSAKRDAKEDEGEELPTELNTINSAGGFLVVSPDKLSVKYTNTNLH
SQ  GHDVGVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKF
SQ  TKDDAVGGGINYASQEFFFTKNGTIVGKIPKDIRGHLFPTVAVHSQNEEVLVNFGKKKFAFDIKGYEASERNKQQLAIEK
SQ  ISIPPNIGYGLVKTYLLHYGYEETLDAFNLATKNTVPPIHIDQENAIDEDDSSYALKQRKNLRQLVRNGEIDTALAELQK
SQ  LYPQIVQDDKSVVCFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGLTGFQDIVEDCFALLAYEKPEESSVWYFLEDSQ
SQ  RELVADAVNAAILSTNPNKKDVQRSCHLQSHLEKLLRQLTVCCLERRSLNGDQGETFRLRHVLNNNR
//
ID  A7TH24;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  436907;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A7TH24;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043007;
GO  GO:0007096;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNGLDDENQIDERDHYTDDGDYEIDIDSMNMFKSLYYEMMAYFSDLQMHLGEHLMAIDWDMKCKSIAEPVGNCLTALFYI
SQ  IRLLQDTLLSNYKDVYVSTEAFDLSKSTTLQEFPFLIRFVEVSKTKNLQNAKYIKKKTFMFYFDKLLLFLMILILSTNAY
SQ  ISWTFIWRNFKTYSLLYVVDRPNSKNVTKCSRTDLDQSYMENVSYGSYWTMLSYYIRNFRKKDDLEDEITTVKQKTPNVN
SQ  EKDYYYQLKKWSPSKFLTSLFCSFSPTCLVFLILSDVSFTTSIAVILHQFIFKYVVFEGYESRINDESIIHSAMISEINQ
SQ  KFVEPRLSKKVQDAKIDATPEGKVYRTEFFPSLTNCKSNLFNRHDLKGRSITESYNDRIKEFEIVTNTNNETHNVIKVVK
SQ  K
//
ID  Q759K4;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q759K4;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043007;
GO  GO:0007096;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPKHHTFATKLEDLVLTSMSFRMSKHQAHPIEPEDVIREESEDFYSDEEEYKETWSRWALQLLSSSPYDLYLIVNENFES
SQ  INWDLKAKTLARPLGGTMTFLFFTVRLLQDNVIKPNYHKINRTTDGFDFSRSATLREYDYFSKYQHGASWSSANWRVNSL
SQ  SILDTLLKCLYILLLVSNSVLTYKFLFGYFLKYSLFHSAQPPASNNLTKKSLHDLAYRSATDVSRGSLWTLIRYTFFQRG
SQ  RVQEEKPTDEFYYEIKKWCPSSFLTALFASFPPISVWFMAFSDITFVSLLPVILTQYLFWYVIFDCYEDRIKDELAIFKG
SQ  MAAEYNNKVMKPKLSAQTQDAMVDATMYGQEFVQFYPSYSTARSGVFITHSLCGDVIKEKYNQRTKAFEDIPTGSHSQNI
SQ  IRYSRNERLYHSVFPQNPLKKINGAAMSVNPMSFNRSPTYGGRYGTPPSRSHGSGQTYSSTSAPTSPMLKNRRAIPTDHS
SQ  TGGNISGGNYVEYTSNDVHGEPPRRHSTSPLKRDITSSAGREDNHLAFGVNSPNIRSRTVDVKKNLHTHTTVVCPKSDLD
SQ  TSQLSSKQSSISPFKLSRRGSIESRPPFR
//
ID  Q9C112;
PN  Uncharacterized membrane protein C27F1.10;
GN  SPAC27F1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane {ECO:0000305}; Multi- pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9C112;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQLTGSIYPWFTAYALLKSTLMELINSFIPYKSQTGKAPKCLVPYWLSIRLSLLYFKLTEAISFTEKCEKYNISLFDSTF
SQ  VFGYIVNCFFIIHLNTFLTSQ
//
ID  Q17DK5;
PN  Cryptochrome-1;
GN  cry;
OS  7159;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O77059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates after the perception of a light signal. {ECO:0000250}.
DR  UNIPROT: Q17DK5;
DR  Pfam: PF00875;
DR  Pfam: PF03441;
DR  PROSITE: PS00394;
DR  PROSITE: PS51645;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005641;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0050660;
GO  GO:0045892;
GO  GO:0018298;
GO  GO:0042752;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVNNILWFRHGLRLHDNPSLLEALRNDGTGSESVRLYPIFIFDGESAGTKLVGFNRMKFLLESLADLDRQLREIGGQLY
SQ  VFKGNAVNVMRRLFEELNIRKLCFEQDCEPIWKARDDAIQNLCRMMDVKCVEKVSHTLWDPQQIIRTNGGIPPLTYQMFL
SQ  HTVDIIGKPPRPVAAPSFEFVEFGSIPSILAQEVKLQQVRNLSPEDFGIYYEGNPDISHQQWMGGETKALECLGHRLKQE
SQ  EEAFLGGYFLPTQAKPEFLVPPTSMSAALRFGCLSVRMFYWCVHDLYEKVQANNQYRNPGGQHITGQLIWREYFYTMSVH
SQ  NPHYAEMEANPICLNIPWYEPKDDSLDRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGALWISWEAGVQHF
SQ  LKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPIALARRLDPKGEYVRRYLPELKNLPTLYVHEPWKAPLDVQKECG
SQ  CIVGRDYPAPMIDLAAASRANANTMNSIRQKLMERGGSTPPHCRPSDVEEIRNFFWLPEDVVADC
//
ID  O74907;
PN  Protein bcp1;
GN  bcp1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74907;
DR  Pfam: PF13862;
DE  Function: Involved in nuclear export, actin cytoskeleton organization and vesicular transport. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0097431;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0019207;
GO  GO:0015631;
GO  GO:0006974;
GO  GO:0000132;
GO  GO:0034453;
GO  GO:0090307;
GO  GO:0007052;
GO  GO:0000079;
GO  GO:0000055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAKRHAEENEDTVMSESLKVVDTDFINVDFEFFDPQPIDFHAFKNLLKQLLGYDHTNVNLSALADLILSQPLLGSTVKVD
SQ  GNNSDPYAMLSVINLNTRRDEPVIKQLTSYIISRLAKSNSRLENELQKLLEPNSGSQVGLIVNERLINMPVQVIPPMYNM
SQ  LLEEMQWAINENEPYNFTHYLLLSRTYTEIESKLMDDERPSKKGKKSKKTSGEEVMFFHPEDEQFREVAIDIADYPFANQ
SQ  DFNPDANRVFQDAGIKPQGELLLMTNEDFKNLVPKLMEIYSA
//
ID  Q6P752;
PN  Torsin-1A-interacting protein 2;
GN  Tor1aip2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q6P752;
DR  Pfam: PF05609;
DE  Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0007029;
GO  GO:0032781;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQTLKSQDTNMSDSGYRDPVEDSQNVLGNDPSVNSQAQDPIVTPSNTVEAQTLHPTSDLKEDHHEIGAKGQEHADTGDR
SQ  AESSEEPALEKPPLDKAELERSPSSQDTEQRHHPYSEHVGGDTLVLDPNYSQSDLGGRADAHLESSSAAPTEGAGEGGEA
SQ  GAHLESSCAALPVGADEGGRANAHLESSSAAPTEGAGEGGEADVHLESSSAVPPEEAHLESSSAAPSEGAGEGGEADAHL
SQ  ESSSAAPSEGAGEGGETAQNLLAVDSTDAQSPCHSSAGPGSQDSLRRRLPVTEAERHEEETQLVTEKEEVAQETLRKTEK
SQ  KSLWTYGSMFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFSQLREKFPGQSAFLWQRGRKFLQKHLNASNPSE
SQ  PATVIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSYGFENGHKAAVVHHFESLPA
SQ  GSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPRETEEKVRDLLWAKFTDSGTPSSFSHMDSDKLSGLWSRISH
SQ  LVLPVQPVKNIEERGCLL
//
ID  Q5R8I2;
PN  RNA transcription, translation and transport factor protein;
GN  RTRAF;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=May localize at the centrosome during mitosis. Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. {ECO:0000250|UniProtKB:Q9Y224}.
DR  UNIPROT: Q5R8I2;
DR  Pfam: PF10036;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex and is required for tRNA ligation. May be required for RNA transport. {ECO:0000250|UniProtKB:Q9Y224}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0042802;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAI
SQ  DWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILV
SQ  QERLTQDAVAKANQTKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLG
SQ  KVGR
//
ID  Q6DFT4;
PN  Trafficking regulator of GLUT4 1;
GN  trarg1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Endomembrane system {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8C838}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
DR  UNIPROT: Q6DFT4;
DR  Pfam: PF04505;
DE  Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. {ECO:0000250|UniProtKB:Q8C838}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032869;
GO  GO:0099638;
GO  GO:0044381;
GO  GO:0072659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAINTDTQYEKALGGSGNPLPADSHETEKLLTNASENKEENGMKKSFSVTMSSEKSMGDLEQNGHNLPYKSVSAGQLESA
SQ  PLSPSRVSLARASSTATTAQEQGRPTDYLVLAIFSCFCPVWPVNIVALVFSIMSRNSLQQGDLDGARRLGRLARLLSVVS
SQ  ILLGLVIIVLCILSLTIFH
//
ID  Q6PEE2;
PN  CBP80/20-dependent translation initiation factor;
GN  Ctif;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q6PEE2;
DR  UNIPROT: Q6A069;
DR  Pfam: PF02854;
DE  Function: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0000184;
GO  GO:0006446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLTDKTEGDGESQRTQSHISQWTADCREQLDGSCSFSRGRA
SQ  PPQQNGNKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGISLND
SQ  IEKVLPTWQGYHPMPHEAEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSGPHPSGRPT
SQ  HHGYSQNRRWHHGNMKHPPGDKGEAGSHRNAKETVTVENPKLEDGPGDTGHSGLEPPCSPDTLTPAASERPTPQLPGGPE
SQ  AEIKHKDTVLPERLRERPKITLLQSSKDRLRRRLKEKDRDEVAVETSSPQPSKMDRLMEILNIMRNNSSDVDAKLTSFME
SQ  EAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFI
SQ  TFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPS
SQ  ESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA
//
ID  A8XV40;
PN  Probable spastin homolog spas-1;
GN  spas;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized to the perinuclear region of the cytoplasm in early embryos. Present in the cytoskeletal fraction. {ECO:0000250}.
DR  UNIPROT: A8XV40;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  PROSITE: PS00674;
DE  Function: Severs microtubules, probably in an ATP-dependent fashion. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016853;
GO  GO:0008568;
GO  GO:0031122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFAFSKAPAGCSTYERVTQKFQDGSNKLRAAIEMDELTKQNGTINEKLQTAELYKQARQMLKEANEFNIMDIPESKRSEV
SQ  REKREKTLNLEKSAQDRLIKICNEVDPNMKRASTAADPCRAARITPRNTRATVPGDKKVSKVKQTEKAPHVCSRGDRCGA
SQ  HQPPPEKKSTPLKPVNQIRTRVKENKNPIGVQQQVFSFILSCCMRRNCRRPHYLFPCMISLKMNYFKFQATLPNQLNTVN
SQ  RSNLLKGVDKAIGERLLDEILDSTGVRMDDVAGCHSAKATLEEAVILPALNPNLFSGLRQPVKGILLFGPPGNGKTLLAK
SQ  AVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNGQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGAT
SQ  SSPDDRILVIGATNRPYELDDAVLRRFPKRIMLNLPDTEARKELITNTLKKHDMMDGLSSSDIRYIASNTSGFSNSDLVA
SQ  LCKEAAMVPVREIHRSKLSVTDGDKIRKIRASDFDTALRTIRPSTSDRILSKLSDFSRNFGC
//
ID  Q4R599;
PN  Translin-associated protein X;
GN  TSNAX;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q4R599;
DR  Pfam: PF01997;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0043565;
GO  GO:0030154;
GO  GO:0007275;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTDDNG
SQ  KENKTPSSDTQDEQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVSSVKTEMIDQEEGIS
//
ID  Q54BP6;
PN  Exocyst complex component 3;
GN  exoc3;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q62825}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q62825}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q62825}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}.
DR  UNIPROT: Q54BP6;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METVSLVPLEGLDDLSAQSAAIKKIEQNFSNIDSLASVTNHKISLIQQKKTIEAQIKNEVHSELEKSKKGLETLYKSYNR
SQ  INRMDESFSDTVELCSETSNLIGHYQLIKKVNTVRVNLINILKEVDRLLTIPEKAAEIEQLLSDDLNLLEIHSKLRELER
SQ  LHQKALKQFESNFEELEAIKEMFSSVPELSHRFENKIWNIVSNSIDIAQIKPAVLVKVAQIIEREKLHEQKQKEKKSQNS
SQ  LISSEGIHDDDDDDDDTEVNLNNSNKQQNNENENSSSNNNNNYDINNEDEGYDRNRSNYGDRFLEVLIQSISGKFEPMFL
SQ  NSHNDLVQTLKDVNKMVDELFIVMDIVQECYPPSYDLFNFYVDQYHTKFYSLFGSFSNLMESSHVNNNYQVVVTKNIPSA
SQ  HILMLVEWVVKNYSRDLSRLGIQDISPPLLDSLDPLIKIYKMHIKQLMREWCDNIINNDNQNKPEVVDGQYCSLAPIQLF
SQ  ESVASQLDIAAATKCQKLVVGVMEEVVSALMYFQVQSITLLQERNHEIKLENVIAYVNNNSKCYDHTQTIVDKVSNILDS
SQ  EHMGYLDFDPVLEGFLNVSKVATQAISSVIFRDLDECIHKFYTVEWYQEDLMQPIINTFEDYVTNDIQKYILENYLKRLA
SQ  LLLLDTLIEQLLAQLIGGKNKFNENTYKILSNDCDKLLDFFKKYLRLSVVTAKVQILEDFKQMITSSIDMVPVYFRSVIN
SQ  FHKDINERVVELVLYQRTDISKSEITEVLGQIKTIVETVHTDPTNPPTGIFSRMNIYQRGWFS
//
ID  Q6UY62;
PN  RING finger protein Z;
GN  Z;
OS  2169992;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6UY62;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019012;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNSKSKSKLSANQYEQQTVNSTKQVAILKRQAEPSLYGRHNCRCCWFANTNLIKCSDHYICLKCLNIMLGKSSFCDICG
SQ  EELPTSIVVPIEPSAPPPED
//
ID  Q6CKY2;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6CKY2;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAFWRNRHESPAISQERSPSPDRFQNSEDIREDNNNYNEDEKLGWFASFMGMFSLPYDWYLSINEDIAVIDWDSKSNSVA
SQ  WPLGNVLTFLFFSVRLLQDNVIAPNINKLTHSDDAFDFSKSKNLQKYDYFQQYGGSASSSENLYYKMLRQLHRLFYLLTV
SQ  LLLITNISVTYRYLFAHFQTYSIFYWKTVPKSKNVTKKSLHDLNHTYVEDAKRDSLWGMIKYLLFNGSHDDETNRAHYYE
SQ  LRKWTPSRFLTSFFVSFSPIAFCFLWMTDVTFKTLIPIIIHQYVLWFIVIDRYEQKLKDEQILSMSSVAELNSKVIQPKM
SQ  NVLKQDAMVDATPYNDGIVYFYPAYTTTRSHVFATHTLSGKLSKEKYNPRTDSFEDANSQRTENYVRFSYHHPKSINGAY
SQ  VRESYPSRQHSPRLSPSRYSHLQSGNTPSAPSTPLLIPSQQPHFDHSMLANASRNHNISERRNSHSPIKQHFANRLLNYP
SQ  DETNDSIPDVSDDRFRMDDRFRRGRQGYFNRSPDINSGTLHYDDGDDDDNRISKSPFRNSSSSPFR
//
ID  O23593;
PN  RGG repeats nuclear RNA binding protein B;
GN  RGGB;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9SQ56}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}.
DR  UNIPROT: O23593;
DR  UNIPROT: Q8LB56;
DR  Pfam: PF04774;
DR  Pfam: PF09598;
DE  Function: Binds RNA. {ECO:0000250|UniProtKB:Q9SQ56}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0003729;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASVNPFDLLDDDAEDPSQIVASKPLKVVAPVQTAKSGKMPTKPPPPSQAVREARNAPGGGRGAGRGGSYGRGGRGGNNR
SQ  DSRNNDGPANENGYGGGYRRSEEGDGARRGGPVGGYRGDRRGSYSNGGDSGDSERPRKNYDRHSRTAYGNEDKRDGAGRA
SQ  NWGTTQDDITPVTEESTAVVDKNLTVEKQDGEGEATDAKNETPAEKAEEKPEDKEMTLEEYEKVLEEKKKALQATKVEER
SQ  KVDTKAFEAMQQLSSKKSNNDEVFIKLGTEKDKRITEREEKTRKSLSINEFLKPADGKSYYRPRGGYQGGREGRGPREGN
SQ  QRDGGRNLREGGRNQRDGGAAAQAPTPAIGDSAQFPTLGK
//
ID  O94418;
PN  Meiotically up-regulated gene 87 protein;
GN  mug87;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94418;
DR  Pfam: PF04097;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051321;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0010389;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTW
SQ  KKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRV
SQ  SFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIIS
SQ  KAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEI
SQ  IQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPY
SQ  KYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFL
SQ  LMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQE
SQ  LSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAK
SQ  QADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNL
SQ  LLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQK
SQ  SSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT
//
ID  C5DQ18;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C5DQ18;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLRISKDVSVSVNTADLLPEDDGFDRVDGDNRGWFSVFLGLFNTHPSDWNIALNEAIETIDWDSKSITLAQPLGNFFTF
SQ  AFYVVRLLQLSLIKPNLSRINEKTDHFDLSKSEMLKKYEYLYHFTNDKNQSVGNVYYRFLGRLGKFFDICIVLLTFTNGF
SQ  ITYKFFWGNFKMYCLFYLKKGPHLRNVTKASLQKLGQDDDDGSLWSSLRYFWNGTKDKEGSTDDRDDDDGDIHYKLFKWT
SQ  PSQFITMLFVSFAPTAVVFLLFTEVSFLTLIAVIVHQWVLHRLVIDCYGNRLVHESVIASANLAEVEAKFVKPRMSKKVQ
SQ  DVAIDCTPHGDGMVKFYPALTTNRSHIFQTHSLTGELITETFNPSTKEFEDLQTEGTTHNVIRTAPYAAGDLLHRDPYWY
SQ  QRNMIMRDVAHRPYFHSREVSPTRYHPSRISPRPGQYSPLVSSTSGMSTPLMRPDRSPFLNTRPSLGEREELFHRGNSRS
SQ  PLRQPIENFKSLDRSSDSQSPIRRHNGDSDA
//
ID  O13671;
PN  Importin-alpha re-exporter;
GN  kap109;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13671;
DR  UNIPROT: Q9USC9;
DR  Pfam: PF03378;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Export receptor for importin alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005525;
GO  GO:0005049;
GO  GO:0008536;
GO  GO:0006611;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDE
SQ  VAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSD
SQ  ALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFT
SQ  YTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRK
SQ  HAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHI
SQ  NANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVF
SQ  TFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKL
SQ  AENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLP
SQ  VFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFV
SQ  EPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGP
SQ  DNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQ
SQ  AQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVL
SQ  QSYGYVI
//
ID  A5YVF1;
PN  Protein SUPPRESSOR OF GENE SILENCING 3;
GN  SGS3;
OS  4081;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18165314}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: A5YVF1;
DR  Pfam: PF03468;
DR  Pfam: PF03470;
DE  Function: Required for post-transcriptional gene silencing and natural virus resistance.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0031047;
GO  GO:0050688;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFSKWGGKPSNSSEKQKASSTPTVEEINRGVGDIGLNSEQNEGWEVYARKPKNKGGSSAGKQWAPQNPSPKAWGNQNTK
SQ  AWGHPDVGKKSGTRNNAGSGRGSGNNWSTPSDPQKLARPHLYDGGFPSSAPVPPALKNGWDWSSRVASAHPKDNSQVAAA
SQ  ADDDKASEHDAEDNELDFLDESDDDLHSDDFDSDVGEMSYETRKKNPWFNQLFHSLDSLTVTEINEPERQWHCPACKGGP
SQ  GAIEWFTGLQSLMTHAKTKGLRVKIHRELAELLEEDLRQRGTSVVPPGEVYGRWGGMEFKDKEIVWPPMVIIMNTRLDKD
SQ  ENDKWIGMGNQELLEYFSSYAAVKARHSYGPQGHRGMSLLIFEASAVGYIEADRLSEHFSENGRNRDAWERRSARFYPGG
SQ  KRLLYGYMADKKDIDNFNQHSAGKSKLKFEMRSYKEAVWNPAKQMREDNQQLIWFKNKAAKHQMQAKALEESLSLVSEKH
SQ  RQTLEENKIVRLKTKMHHEQIKEEMEFQEQFFKDQIKIIHDARTAREDNFEKTQQEQREMVKQSNANTASVEDHRVRAEK
SQ  VAKFIKLQDKEMEEFVEERENLMRTHDDRIAALRRKYWEEEVELERKFDLELSKLMEKYSPKQSDEVNSSGTM
//
ID  O74889;
PN  SAC3 family protein 1;
GN  SPCC576;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74889;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0006406;
GO  GO:0042274;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKRNETGNNRLKRSNNRGKSKKDWKDASVETTPRETSVDEDNTSVFEDVEAQDSRQKRFSSTLEGNRFEELRSLREKER
SQ  EVAIQNGLIDDPTKPRQLDEAVTFVGTCPDMCPEYEREQREYQNNLERWEINPETGRVDKNLAVKAFHRPAAGNEQALPS
SQ  DVRPPPVLKKSLDYLVDKIVCGPDPLENTHFFVRDRTRSIRQDFTLQNCRDLDAVACHERIARYHILCIHQLCEKKQFSA
SQ  QQEVEQLRKGILQSLCEFYDDLRKVKIRCPNEPEFRSYAIITHLRDPDVVRQSQILPIEIFDDQRVQLALRLSALAQKNN
SQ  ERVGHILPRNTEACPNLYTRFFKLVQSPAVTYLMACLLESHFMSIRKGALKAMRKAFMSAHANFPCGDLKRILHFDTVEQ
SQ  AASFSRYYGLEVSDDNGELSINLNKTAFFNDSKPDFRQLFSQTLVESKLQNRSFADIINGSRYNIDRVSPNTAFSTNIPL
SQ  SLPFANKEPQPIAGFKKNTPETSVVSKNLSTFNGKFNVNAPVFTPRSFPTKPFSATDISSVQPTNLPNGSTNGTETFIPP
SQ  VQNSITSNKEAVKPIKNKPKPISFESLSAVGNLIISDSLSRIVRQILQNLYTEWVHEKTNLVFATMFRTIFREVLLDGIA
SQ  SEVYLKSLKKHAISQISVRAHHSWVKKQEKMMLEMREKNRQEKYFSVLNSVVKAESSNITRLPIKRTFYGDTRNLDKASE
SQ  KLRAEHDRTRRLWKPVLMDSLFSNLQKFPVYEDWHLLIFNASTSSMMKTWLCAKFSLKETNKTSFWHSSYNLFNRQYHVD
SQ  MPDNVSDLPQTRLCYGACVYNVGLLDEEKRKDLANSDLNSSPKLIQGNDSRSAHESSANKLFSFVHDISRLTITKLPLLL
SQ  IFWSDSNLDMQGITQKYRFLELITSTWSAISSIHVLTITNDRDMDLEHSLKVLLDNVTVEKSPFAQLEELEVVRKKREAE
SQ  IEASSKTVKRLASNNKFLTDSNVEGLLEAPTSLENSLVEDDKWASLRQKIKAARDLLKKVETFY
//
ID  Q3ZBU9;
PN  UBX domain-containing protein 4;
GN  UBXN4;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}.
DR  UNIPROT: Q3ZBU9;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q92575};
SQ  MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSTQMAASWEDEKVTEASSNSFVAIKIDTRSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSISADELVTRIHKVRQMHSLKGEASLANGSQSEGSVSTPSASFEHNNTSENCQSRNVELCETPST
SQ  SDTKSDSATGGESSGQTTVSQEPSGCSNQRPTEDLTVRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKR
SQ  KQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEIKRETSTKERSTVA
SQ  RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVLLPAGRPT
SQ  TSMVHSSSGDFWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSVRAASLETSNLASSSNSEKREPVRKRVLEKRGEDFKK
SQ  EGKIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  Q4VKV5;
PN  Matrix protein;
GN  M;
OS  1560034;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: Q4VKV5;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MLRWFSFGSNEGSEVAGNGWSVKPIGNMSIKKDDPVGFPQGYQCLLKVIIQLEKKDPTKSDVSELIAGWVKRYSGPHLLE
SQ  RLIKALIILTVPKLSRENIDNHVKLGGLFEGQVTFHFSSRDLIPTKYLSYATSIRTTVKGIYSYLSIEAELNPSSHQGTS
SQ  VAKLLRASDVAKYYDNTLQSIFSQFEIKNVTITDDQIIFN
//
ID  U3H0P2;
PN  Uncharacterized protein wtf25;
GN  wtf25;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: U3H0P2;
DR  Pfam: PF03303;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0075297;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPLNTHRENHSYGTTDNSSPLLIILLIS
SQ  FTSIILFNAPAFCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWSKACGKGIKHFLKNWRNMIFAFCKSS
SQ  LFCLVLLKAENKLSSHLGDQRWGWKCSASAFTFMAVSSILIFIAETVEPGSCSTDLVKRTLAFYGYEIRQHVNEDATILL
SQ  REMNPESEA
//
ID  P34454;
PN  Uncharacterized protein F54F2.9;
GN  F54F2;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00624}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: P34454;
DR  Pfam: PF00226;
DR  Pfam: PF00249;
DR  PROSITE: PS50076;
DR  PROSITE: PS50090;
DR  PROSITE: PS51293;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRVILLLAFLISLTECQWTSEDLALYDLVEEVGVNFYEWFDIPRDASSNQVKKAYRKLTLEWHPDRNSAPDATEKFRQVA
SQ  GIYEVLKTTELREKYDNVLENGLPSWRHPMYYYRRMRKLAWYEGILVLLFIGTIAHYLMMWAAYFEKTLVYKQNVKKSRK
SQ  SKKEDPAEAEKLMKQALEEYLPKYSELLPIILARGTVTLFKNLALTAKDAMTPKEVEPEEPTEEELAQQRRQQRAAAAPQ
SQ  QLEFKFEVAQGMKAVSTNDPEMEKKYAAENEVVAQKQSGATWTPDELASLVRLSTEKYPAGTPNRWEQMGRVLNRSAEDV
SQ  IAMAGKMKQMKQEDYTKLLMTTIQQSVPVEEKSEDDWSQAEQKAFETALQKYPKGTDERWERISEEIGSKTKKQVMVRFK
SQ  QLAEMIRKKKTNDT
//
ID  Q148F6;
PN  Protein rogdi homolog;
GN  ROGDI;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Cell junction, synapse, presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q148F6;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005623;
GO  GO:0030054;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0032502;
GO  GO:0007035;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATVMAATAAERAVLEEEFRWLLHDEVHAVLRQLQDILKEASLRFTLPGSGTEGPTKQENFILGSCGTDQVKGVLTLQGD
SQ  ALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFRTGAEVLKLMDAVMLQLTRARNRL
SQ  TTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHTLQPNSTKNFRPAGGAVLHSPGAMFEWGTQRLE
SQ  VSHVHKVESVIPWLNDALVFFTVSLQLCQQLKDKISVFSSYWSCRPF
//
ID  Q27YE2;
PN  RING finger protein Z;
GN  Z;
OS  55096;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q27YE2;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019012;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGQNQSRDKQKAIQNQPKDTGNRADIIPDATGMGPEFCKSCWFERRSLVACNNHYLCMNCLTLLLSVSERCPICKLPLPQ
SQ  KLKLTSSPSAPPSPSPPPYSP
//
ID  P91697;
PN  Period circadian protein;
GN  per;
OS  46793;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91697;
DR  UNIPROT: P91692;
DR  UNIPROT: P91693;
DR  UNIPROT: P91694;
DR  UNIPROT: P91695;
DR  UNIPROT: P91696;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGANGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANEA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTIGGGGGGGVGGGMPLFLDITHASSSSQNKGLAGVGVGGAG
SQ  GVVGGGGSGTGLGGNGNVGSGNGNNNQPSTNQYTQSRLPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFP
SQ  TFYYIPASIAASSPSSTNTNPNRPHKHAHVHNSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  Q5ZM35;
PN  Twinfilin-2;
GN  TWF2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q5ZM35;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005884;
GO  GO:0005623;
GO  GO:0005737;
GO  GO:0030016;
GO  GO:0048471;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0030042;
GO  GO:0051016;
GO  GO:0010976;
GO  GO:0010591;
GO  GO:0042989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTHQTGIHATTELRDFFAKARNGSVRLIKVIIEEEQLVLGAHKELARRWDVDYDAFVLPLLDEQQPCYVLYRLDSQNAQG
SQ  YEWLFISWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDEMFGTVKEDVSLSGYQKHVSSCSAPAPLTAAEQELQQIRIN
SQ  EVKTEISVESKHQTLQGLAFPLQLDAQQAIQTLKQKKINYIQLKLDLERETIDLVHTSPTDISDLPKRIPQDSARYHFFL
SQ  YKHSHEGDYLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDTVEQEFCLEIAKKIEIDDGAELTAEFLYDEVHPKQHAFK
SQ  QAFAKPKGPVGKRGQKRLIKGPGENGEDS
//
ID  O55653;
PN  Early E3A 11.6 kDa glycoprotein;
GN  E311;
OS  10534;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: O55653;
DR  Pfam: PF05393;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGSTIAPTTDYRNTTATGLKSALNLPQVHAFVNDWASLGMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNP
SQ  HNEKIHRLDGLKPCSLLLQYD
//
ID  Q66KV4;
PN  Barrier-to-autointegration factor B;
GN  banf1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Chromosome {ECO:0000250}. Note=Colocalizes with nemp1a and nemp1b at the nuclear envelope. {ECO:0000269|PubMed:19167377}.
DR  UNIPROT: Q66KV4;
DR  Pfam: PF02961;
DE  Function: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non- specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005694;
GO  GO:0005635;
GO  GO:0003677;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSTSQKHRDFVAEPMGEKSVQCLAGIGDTLGRRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDACSANAKQSRDCYG
SQ  CLKEWCDAFL
//
ID  C0HAC0;
PN  F-box/LRR-repeat protein 5;
GN  fbxl5;
OS  8030;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: C0HAC0;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDVFTGPHWRMKQLVGLYCEKLSQTNFSNNNDFRSFLQSLCATFKEFKMHEQIENEYIIGLLQQRSCNVYNVH
SQ  SDNKLSEMLSLFEKGLRSVKSENEQLNYAQQLKERLEAFTQDFLPHMKEEEEVFQPMLMQYFTYEELKDIKKQVIAQHSS
SQ  QQRWDCAAEVLKGLSLWSQAEELHKAFKYADHEKTDDELEKELCSTHISQLPTEILLCLFRYLGPEDLCHCGQVCSAWSD
SQ  LAKTGSLWRHLYPVRWARGDYYRGPPDDVNQEPDEEWVKSLQDEGKAYQEWDEDADVDESDASCEDSLAISAAQREKKLL
SQ  NGMIQNLLPAVGSSVRSIVLAYSSTVSSKMVRQILSLCPNLTHLDLTQTDVTDSAFDSWSSLWACLSLEHLDLSGCEKLT
SQ  DRTLKKLSLGLGDLASPTCSEKRSDRRAKLLKSPPSPISLLDKRSLRPTGHSRQVLIFKQWPGKLGSAPCSPTRVWVLDA
SQ  SELADIEDAAEWNRRRGVSTPEVRGFVETQPGGLSCCCRRRRGGFRTGFSTSYWQQQYGLGEAGCGHSTCCTGETALRTL
SQ  GGLQYESYTTRGSAGAEFRTKCSSGGQLCLECDNRTDPSDGRRSLRFLSLSGCYQVTDLGLRALSQRGGLPLLEHLNLSG
SQ  CLLITEVGLQELVSACPALNDEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE
//
ID  Q55CQ7;
PN  Transportin;
GN  tnpo;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q55CQ7;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Mediates docking of the substrate-importin complex to distinct nucleoporins (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0008536;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEWVPNQDGLKQLVYVLNLSNSTSREVHDQIREELDKFHSVPDYNNYLTLIFKSNELQPHIRSVAGLVLKTNIKQYFEK
SQ  MPREVQNYIKREILPVLSDPDASVRHTVGNIITNLIKKSCFSEWPELLPALNLALDSNSQDLIEGSLYTLSLLCEDSTKK
SQ  LDSDDSGRALNQLIPKLIMFFKCNNADFRKKALVSISYFIISMPGALLINMEAFLKGIFSMSEDPSEAVRTNVCKTLVTL
SQ  VETKIEFLLPYIKDVIQYMLHATKDKSEEVALEACEFWTAISQAEGCRDLLRDYLPVLVPILLNGMVYTEQDYEYLDQGD
SQ  DSMTPDRPQDIKPFIASTKSHGSGSSGGGQDTGFVNPDNNNNSNNNNSSNNNSSNNNNNNNNEDDEEYNDDDDDDDDDGF
SQ  EDEAWTIRKSSAFAIDVLSGIFPDAEYLSVTLPLIEQRMNEQNPWPVRESAILALGAIADGSKNGLAPHLSKVIPYLINT
SQ  LNDPKPLVRSITCWTLSRYSYWIAQADGRDYLHPLVVNLLNRIVDNNKKVQEAACSAFATLEEEADLLLIPYLQMILVTF
SQ  VNAFGKYQAKNLLILYDAISTLAKVVGNELNKPELINILVPPLLQKFNALDDSNKNLLPLLGCLNQVCSSIGAGLQNLIS
SQ  LFFNRSIKLIEGSLQAHYKYNNQDQKGSSSSSDQDFIVAALDLLQGLSEGIGTSIESLIPNSNLPHLLLQCMNLRGSDVL
SQ  QSSFALLGDMSKFCLIHFKQYIPDYLNILTNNLYPEYLSVCNNASWAIGEIAIRMPDEVKPFVVAIRDRLISNINKVNLN
SQ  RGVLENTAVTIGRLGIVSPADISPFVDKFIQCWCMAIRRKTDDIEKDSAFRGMWLIINNNPNGALRHLVYICDAVASWDK
SQ  MQPDLYEAYFKLLHMYKTSMGGVWAQFYNQFPEQLREILNEKFKLNQDISQ
//
ID  Q6FL09;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6FL09;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFSWLIPDIPELFLTISVWFRLQGWEDNTKLGFIIGNTLTTIFYILRLAQDTLLAGVSRKLIRDYELFDLSKSETLLSDP
SQ  AFSSYHDVLFNKHHSTANASSYNKRVRKVTSTVYWSTYFLLLLSCYTCYRLFNTYKVYRIYYLKDLNLDKHPSLKKIEPD
SQ  YEVDEKLLKTSLKSKLLSRFIRLLQLQDEVETELPKVTEHYTLNKWDPSKLIISLSTSFSPTIIICLMYTNVTFLTVIPI
SQ  IIHQGIFYFMIWNRYEERFKDDALLMRENYLQYDTKYVKPLKQIMYQDVMTDTATISDGGFTKFFPVSKSTLFKHHEMSG
SQ  DVIIERYNKKSREFENVTDIIKPHHHINNTVKILPPTIRKDHKTNRYDHRQQSILKDRKFNIDSNEPQIINALTTAIPSR
SQ  SFFNNNPSGSNDDNCSGIKVRSSPTRETFFPATPLRKK
//
ID  O13746;
PN  Uncharacterized protein C16E8.18;
GN  SPAC16E8;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13746;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVTSFILNATFKEFACFGNNYLIILPGIMLERNVFRHLNYSTNSICSHYQFFGGHYESFELLVVIVYYFSHVGSFSLAE
SQ  IYRITWDKRIVLYGTTTTLVYCSEGSD
//
ID  A5WW21;
PN  Ras and EF-hand domain-containing protein;
GN  rasef;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: A5WW21;
DR  UNIPROT: A4QP53;
DR  Pfam: PF13499;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds predominantly GDP, and also GTP. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0032482;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHAELRRLFAACDGNQSGRVEYEDFTTVCRELNVPADDIRTLFNKFDLDGDGYINFNDFSSSFQEVSEALNLASLGNCL
SQ  HSQRRAWDEFENTLDGDVAFYLGRQWDALSELYEGIHSTSDELLLQQFEDLIRALVTEIREHRMESEQLETSLRRTEEVS
SQ  SSQLAEMEEDLQQQLIHTERRVREEEQKKLDESIAMLQIKHENELADLQTTIERLTKQYQEESKLNTPREDSVKLRAQIK
SQ  DLMEENEELRASLMKAQMNVSILQVELDKLKNAFTDQKRQHERESDDLKKMVMEFQSYSSHIEMLQEMNKSLYDSNDGLR
SQ  SALSQENASTKRQLSPRNEVLPRKMKPIRQSTMNQSSFTNEEDTLALVKCWAEKYLDSGVSVQSEMDAMSGIDYDSDDSH
SQ  HSVETVHHSYSCVPSELEVSEVKPEALRSVARSTVGSISSSLRRRLSAFPVKQNEEDLLDTQDLAPVYRLVLAGDAGSGK
SQ  SSFLLRLSLNEFRGDIQTTLGVDFQIKKMLVDGEKTNLQIWDTAGQERFRSIARSYFRKAHGVLLLYDVTSESSFLNVRE
SQ  WVEQIRESTDEDIPMCIIGNKVDLRAARPEGSCVSSIHGEKLAMNYNALFCEASAKEGTNVIEAVLHLAREVKKHVKLGR
SQ  RSESQVKLSLHKRRKTLSNCCGV
//
ID  C5E3S7;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C5E3S7;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTFRLSRFESPLIEDDGESRASLLGYSPENELYTDVDENRESRFRRFMSFISSSPYDMFLAINEHVESIDWDSKASTIAG
SQ  PLGNFFTCSLYTARLLQDSLIRPNQQKLDKKRDSFDLSRSEILRKFEYLSQVPKSGVVVTHLNWYWKFLTFLNVALQITV
SQ  GFLILINLFVAYKFLIGHFQVYSLFYTKTSPRSKNVTKRSLSDLSFKSLEEVTNSSLWTMIRYMFVRKRLIIKDAPKGKY
SQ  YYQLRKWTPGKFYTALFSAFSPISVIFLLVTEVSFKTALAVIGHQYILFLVLFKRYESRLDDEACLAKAHFEEINEKVIK
SQ  PKTTIKTQDAMVDATTYGGGAAFFPSFTTTRSHIFQTHAVTGDIITERYNPETRNFEDVENTGRAKNYISQIQGVSHGQQ
SQ  VVSRSKAMNGATARPQFFSRQPSPSKIGTPSIILNYRTSPFSAPTTPTLKPVNGVQNGQSIFRNSPDPSKANSLNCDTSH
SQ  LSRNNTLSRLRRNSVSPTKSGNYCSASGMRAIHKSNFGADSSVSYSMEAPSNELPFEEVARRGRHPFEITASRDLPAGRS
SQ  SAVSSRHSSISPFKGNTSFAGRESLDSRPPFR
//
ID  O59809;
PN  Probable importin c550.11;
GN  SPCC550;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O59809;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Active in protein import into the nucleus. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0005049;
GO  GO:0061608;
GO  GO:0008536;
GO  GO:0006406;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIP
SQ  EEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLD
SQ  DRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESL
SQ  MSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSP
SQ  RVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVK
SQ  LASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGY
SQ  LRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEV
SQ  DIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENT
SQ  VDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITY
SQ  GGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVF
SQ  LLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMI
SQ  TLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNY
SQ  LLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT
//
ID  Q08926;
PN  ULP1-interacting protein 4;
GN  UIP4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16407407}; Peripheral membrane protein {ECO:0000269|PubMed:16407407}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}. Nucleus envelope {ECO:0000269|PubMed:16407407}.
DR  UNIPROT: Q08926;
DR  UNIPROT: D6W3I3;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q07549; IntAct: EBI-2044051,EBI-22078; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0005635;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16407407};
SQ  MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDE
SQ  HSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKE
SQ  RKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTD
SQ  MSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS
//
ID  Q9Y820;
PN  PCI domain-containing protein C1105.07c;
GN  SPBC1105;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9Y820;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0000346;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0071033;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLNDFLQTLSNAVGEKNSNTLEKCIILDPSEPSFQQLSKTLFLDRKGKNKLNGTIQKEFGRIRGWKELVTTYFEYVENA
SQ  ASSPDQRKWELLQNLYSNLTTCFSHIDGAWLCTIVKRVSKLYVKLSLQLDTSTPTLEDSFDGNGFIQRKYVSDASRNVLR
SQ  TFNSILSDRQQNINPSKKDAIFCIANLLCLLYFRLKQIRLCQTIQANVISSGADISRATMAELVTFRYYLGRCHLYQRKI
SQ  HQAKDHLLFSFLQCPDECYHQKRLSLIYLTTCLLILGKSPTKGLLEKYKLTAAFEPLIKALKSGDIKSFRLSLEDNSRRK
SQ  WFIKRGIYLTLLDRCEIILWRNLFRKVFLFTFEQSQKTPHVSGSYLLTAARLSTNDNSYDMDDVECICVSLIDQGYIKGY
SQ  IIHASSTLVLKKDPSFGFSVIESLMPIARNDHAEKEFFHANA
//
ID  Q32PZ3;
PN  Protein unc-45 homolog A;
GN  Unc45a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the perinuclear region. Little protein in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q32PZ3;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q68CZ2; IntAct: EBI-1220488,EBI-22265203; Score: 0.35
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVSGPGTPEPRPSDPGASSAEELRKEGNELFKCGDYEGALTAYTQALSLGATPQDQAILHRNRAACHLKLEDYSKAESE
SQ  ASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLKRCVSLEPKNKVFQESLRNIGGQIQEKVRYMSSTDAKVEQMFQIL
SQ  LDPKEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDTGETDLMLAALRTLVGICSEHQSRTVATLSVLGTR
SQ  RVVSILGVENQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLELLTEIGVSGQGRDNALTLLI
SQ  KMVPRKSPKDPNNSLTLWVIDQGLKKILEVGGSVPEAAGELTVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIR
SQ  SWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVA
SQ  LLKDLYKGSERDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADV
SQ  KEEFVEDEAALKALFQLSRSEERSVLFAVGSALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLL
SQ  AAGVVSAMTCMVKTESPVLTNSCRELLSRVFLALVEEVEDRGTVVAQGGGKALLPLALEGTDVGQTKAAQALAKLTITSN
SQ  PEMTFPGERIYEVVRPLVSLLHLSCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMC
SQ  NLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLRRAAAGGLAMLTSMRPSLCSRIPQVTTHWLEILQALLLSPNPELQH
SQ  RGTVVVLNMMESSKEIASTLMESEVLEILSVLAKGEESPVTRAAAACLEKAVEYRLIQPNQDGE
//
ID  D3Z5T1;
PN  Coiled-coil domain-containing protein 78;
GN  Ccdc78;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm (By similarity). {ECO:0000250}.
DR  UNIPROT: D3Z5T1;
DR  Pfam: PF14739;
DE  Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0098536;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030030;
GO  GO:0098535;
GO  GO:0003009;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIA
SQ  THHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQ
SQ  QALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASS
SQ  TNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPREN
SQ  EYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQ
SQ  HLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL
//
ID  Q6P2B1;
PN  Transportin-3;
GN  Tnpo3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9Y5L0}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y5L0}. Note=Localizes to the nuclear envelope and annulate lamellae, which consists in stacks of endoplasmic reticulum membranes containing a high density of nuclear pores. {ECO:0000250|UniProtKB:Q9Y5L0}.
DR  UNIPROT: Q6P2B1;
DR  UNIPROT: Q7TSL6;
DR  UNIPROT: Q8BKX4;
DR  UNIPROT: Q8BP42;
DR  Pfam: PF08389;
DE  Function: Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation. The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively. Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus. {ECO:0000250|UniProtKB:Q9Y5L0}.
DE  Reference Proteome: Yes;
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0008536;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPT
SQ  DSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLR
SQ  IGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN
SQ  LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGD
SQ  LRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHSIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFR
SQ  MRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVHLPETVHTAVRYT
SQ  SIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIAHSLDSFMLSPEAAVG
SQ  LLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQE
SQ  IWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG
SQ  LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANSSVMRFLR
SQ  DLIHTGVANDHEEDFELRKELIGQVMSQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLP
SQ  KETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
//
ID  Q5RBN6;
PN  Protein NDRG2;
GN  NDRG2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RBN6;
DR  UNIPROT: Q5R695;
DR  UNIPROT: Q5R6V9;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQ
SQ  PLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHP
SQ  DTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNR
SQ  RDLNFERGGDITLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASS
SQ  CMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q99J23;
PN  GH3 domain-containing protein;
GN  Ghdc;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000269|PubMed:11735219}. Nucleus envelope {ECO:0000269|PubMed:11735219}.
DR  UNIPROT: Q99J23;
DR  UNIPROT: A2A5D7;
DR  UNIPROT: Q99J92;
DR  Pfam: PF03321;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0016881;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLLLWLLLLLLLLVPLLAILWQQRSRGARPCWLISLQHRVAWGMLGWAAAWQQWRLDRSTLNVGQSQQQALMWCLKKAQG
SQ  SCCLPREDTDMRTFRNHLPLTQTSHTQEQESEETLPSPASPQYHGDASLQATLLGLITLNKAYPEALAPGSTACVTPTSP
SQ  WPCSVPWLGHALGRVSPDGAKDPRTLLLEALISPGLRVLEARTAVELLDVFVGLEADGEELAEAIAAGILGTLLPKRAAE
SQ  LKEALEQGPRGLARRLWPKLQVVVTLDSGGQAEAVAALRVLWCQGLAFFSPAYAASGGVVALNLWPERPQGSYLLPPGVP
SQ  FIELLPIKEGTQEEAASTLLLTDAQREKEYELVLTNHTSLTRCRLGDVVQVVGTYNQCPVVRFTCRLGQTLNVRGEVTDE
SQ  TVFSVALAQAVGQWPGAKLLDHVCVESRVLDSCEGSAPHYEVFVELRGLRNLSEENRDKLDNCLQEASAQYKSLRFRGSV
SQ  GPAKVHLVRPGSFRVLREALAAFSSSSCRPPEMPRVIRLRHLAQLLQKRVIS
//
ID  Q6DF48;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  calcoco2;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q6DF48;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting galectin-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0003676;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MASDAPPTSMLQPEERNYSQVVFSRVEQSYVPGIDIICYFTYTSGFHPAKKDWVGIFKVSWKTTREYYTWVSADCEEQGL
SQ  EKRVTFKAYYLPKESDDYYQFCYVDQKGEVRGVSIPFQLCRKIQDEGEEDILLVTTEEEAQGMKEKQRVLEEKVAALEKD
SQ  KCTLQDECTQLALEQKNKAALIESLQAQQLECAKKNEELDQQNQELERQLEEEKCKNGSLHLKVVSAEEERERVQNDIRS
SQ  LQLEQNQLKEENMELHKHTNDMEFSLKKYSEEAKNQEEEVQELKDKLWDAEAKHHLLQVQLQDIQMEKKKDKYSIELLTK
SQ  EAEKVADLRQNLEKKDKTMETMEKQLAQLQRENATVLRQMEDLSYTLELRKAEISDMQQQRVRDGAEIEHLNRLLTEQSS
SQ  STPRNQGLFFQNPYESESLISFANEPQPGEAPGGSSVRHVQMQCPECGSEFENFQVFQDHIFCHDLESTE
//
ID  P12348;
PN  Period circadian protein;
GN  per;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P12348;
DR  UNIPROT: Q29I05;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0006355;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGESTESTQNTKVSDSAYSNSCSNSQSQRSGSSKSMLSGSHSSGSSGYGGKPSIQTSSSDMAIKRNKEKSRKKKKAKCT
SQ  QAQATISSSLEGAEEQPHSSGTTCDQKILHVLATTQQLGDQPSSLDHKLGEQLEARHNCGVGKAEQPQSFSLPCPLSVST
SQ  LMPGIGVCHGGNAPGGKWEKTFESCKLDTGPAKTERVKEDSFCCVISMHDGIVLYTTPSITDVLGFPRDMWLGRSFIDFV
SQ  HTKDRATFASQITTGIPIAESRCSMPKDARSTFCVMLRQYRGLQTSGYGVIGRSVNYEPFRLGMSFREAPEEERSDNYMV
SQ  ANSSNMLLVICATPIKSSYRVPEEIHSQRSPKFAIRHTAAGIISHVDSAAVSALGYLPQDLMGRSIMDLYHHDDLPVIKE
SQ  IYESVMKKGQTAGASFCSKPYRFLIQNGCYILLETEWSSFVNPWSRKLEFVVGHHRVFQGPKICNVFETPPNSEPKIAEE
SQ  LQNKNTRIKEEIVNLLAEKVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPH
SQ  HDYYDSKSSIETPPSYNQLNYNENLLRFFNSKPVTAPVEVDPPKVGSSDVSSTREDARSTLSPLNGFEGSGASGSSGHLT
SQ  SGSNIHMSSATNTSNAGTGTGTVTGTGTIIATSGTGTVTCASGNMDANTSAAFNIAANTSAADNFGADTSAADTSGADTS
SQ  AADNYAVDNYGPGNFGAENSCADNSGAENSCADNSGVDNSRPGNSGADNSAADNFGADNSGPDNSGADNSGPDNTGPDNS
SQ  GAENSRAENSRADNSRPDHPRPDISGASNSRPDKTGPDKSGAENSASGSGSGTSGNEGPSSGGQDTRTTAGTPDSPPVSL
SQ  TESLLNKHNDEMEKFMLKKHRESRGDRRTVEKNKNKTTNTIDSLKILEYSSTGPGHGTKRGGSYSWEGEGNKPKQQPTLN
SQ  SVGVGTGAPEAPIPPVHPTHTTHTAIAQSSFSAQQSLFPTFYYIPATPLAASTPAPGALSPTPRNQKHHHHAHQHAPKVP
SQ  DQASTSQQAAGPAAIPLQYVTGVMYPHPSLFYTHPAAAAATAMMYQPMPFPGIANAMQLPEQPSTSQSNYSKTVFSVIVA
SQ  PPTITTTTATTTPKTQGAFHSITPAQLQRPSSQDTSVKTEPASNATPSHSSNKKKANSSIASGIGDYNSNQACSRNRANV
SQ  KKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDNDKEAKHRKLKNITRLSSKIMEHPEEDQTQHGDG
//
ID  Q6AZL2;
PN  PCNA-associated factor;
GN  pclaf;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q6AZL2;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with pcna is disrupted, facilitating the interaction between monoubiquitinated pcna and the translesion DNA synthesis DNA polymerase eta (polh) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKADSAGSSASSGSYRKAVAARAPRKTFGSSSSGSNHVTSPTGKKSESKYAGGNPVCVRPTPTWQKGIGEFFGSPST
SQ  SQPEKENRIPSDDEEAGGSGAGKAPRKSRPLPPDPSEEAADSDDE
//