ID A0A024B7W1; PN RNA-directed RNA polymerase NS5; GN POLG; OS 2043570; 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:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; 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:P17763}; 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:P17763}; 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 {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000250|UniProtKB:P17763}. 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: A0A024B7W1; DR PDB: 5GOZ; DR PDB: 5GP1; DR PDB: 5H30; DR PDB: 5H32; DR PDB: 5H37; DR PDB: 5IRE; DR PDB: 5IZ7; DR PDB: 5JMT; DR PDB: 5KQR; DR PDB: 5KQS; DR PDB: 5KVE; DR PDB: 5LBS; DR PDB: 5LBV; DR PDB: 5LCV; DR PDB: 5M5B; DR PDB: 5MRK; DR PDB: 5NJU; DR PDB: 5NJV; DR PDB: 5U4W; DR PDB: 5UHY; DR PDB: 5ULP; DR PDB: 5Y0A; DR PDB: 5Y6M; DR PDB: 5Y6N; DR PDB: 6CO8; DR PDB: 6I7P; DR PDB: 6JFH; DR PDB: 6JFI; DR PDB: 6NIP; DR PDB: 6NIU; 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 the 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. {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 pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. 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. {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 ande forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could 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. 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. Antagonizes the complement function. Binds to the host macrophages and dendritic cells. Inhibits the 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 (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:Q32ZE1}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}. [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 (By similarity). Leads to translation arrest when expressed ex vivo (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:28592527}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). Leads to translation arrest when expressed ex vivo (PubMed:28592527). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527}. [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 (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}. [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 a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway. Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway. {ECO:0000250|UniProtKB:Q32ZE1}. 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:0051539; GO GO:0005524; GO GO:0003725; GO GO:0005525; 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:0039574; GO GO:0039502; GO GO:0039694; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEI SQ IKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQI SQ MDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREY SQ TKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC SQ VTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGK SQ GSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDC SQ EPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALA SQ GALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQ SQ TLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWD SQ FGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSV SQ DFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQL SQ TVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTS SQ VWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKS SQ LAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAK SQ DGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDL SQ AKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFAL SQ AWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINV SQ VGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVT SQ GNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGET SQ TDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLL SQ AVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVEC SQ FEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIV SQ DLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEV SQ EVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANF SQ KADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIY SQ LQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPA SQ EVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPY SQ KAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIP SQ EPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFIT SQ PAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAA SQ ARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSP SQ NKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEA SQ RRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYG SQ WNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQR SQ RYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGN SQ RIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKV SQ DTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKER SQ EHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVL SQ EEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQ SQ RGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHAL SQ RFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSY SQ AQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPY SQ LGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL // ID A0A072VMJ3; PN Protein CNGC15c; GN CNGC15C; 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: A0A072VMJ3; DR Pfam: PF00520; DR PROSITE: PS50042; DR PROSITE: PS50096; 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:0044325; GO GO:0005249; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MGFDNPRSERFEDDPEISKIPTTSGVKVKYHIDGTQIPEQSSKKSRKNETRNKFLKTRVLSRVFSEDYERVKKRVLVLDP SQ RGQLIHRWNKIFLVACLVSLFVDPLFFYLPVVREEVCIDIGKTLEVILTVVRSFGDLFYIVQICMKFRTAYVAPSSKVFG SQ RGELVLTYSKIALRYFSKGFWLDFIAALPLPQVLIWIIIPTLRGSTMANTKNVLRFFIIFQYIPRLYLIFPLSSQIVKAT SQ GVVTETAWAGAAYNLMLYMLASHILGACWYLLSIERQEACWKSVCNMEKSNCQYGFFNCHSIKDAPRVAWFIASNVTNLC SQ SPNAGFYPFGIYADAMTSKVTSSPFFNKYFYCLWWGLRNLSSLGQGLLTSTFIGEIMVAIVVATLGLVLFALLIGNMQTY SQ LQSITVRLEEWRVKRTDTEQWMHHRQLPPELRESIRKYNQYKWVATRGVEEEDLLKGLPLDLRREIKRHLCLELVRGVPL SQ FDQMDERMLDAICERLKPALCTEGTYLVREGDPVNEMLFIIRGHLDSYTTNGGRDGFFNSCRIGPGDFCGEELLTWALDP SQ RPSVILPSSTRTVKAFSEVEAFALIAEDLKFVASQFRRLHSKQLRHKFRFYSHQWRTWAACFIQAAWRRHKKRKEAAELR SQ AKENLVAASEAENEIAKKYGKGFVVYGTRVARSTRKGVNMHSGTNSGVVSSLQKPTEPDFSDE // 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 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 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 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 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 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 A0JM59; PN Ubiquitin carboxyl-terminal hydrolase 20; GN usp20; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. DR UNIPROT: A0JM59; DR Pfam: PF06337; DR Pfam: PF00443; DR Pfam: PF02148; DR PROSITE: PS51283; DR PROSITE: PS00972; DR PROSITE: PS00973; DR PROSITE: PS50235; DR PROSITE: PS50271; DE Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination 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. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005813; GO GO:0005737; GO GO:0048471; GO GO:0004197; GO GO:0004843; GO GO:0036459; GO GO:0008270; GO GO:0006897; GO GO:0016579; GO GO:0071108; GO GO:0070536; GO GO:0008277; GO GO:0006511; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MGDAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYVDHSTLHAQAKKHNLTVNLTTFR SQ VWCYACEKEVFLDPRGPPASQTTSPRLSHRDFPTSAHPLKSVPIAVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAAL SQ QALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLM SQ DQLHEELKEPVPLETQEREEEDRDDQREGERGGTVEEDFLSCDSGGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEK SQ LKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYVHCSSRSCSPHPVESISKHSSTPPRSSPLRTSHSYVLKKAQVL SQ SGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQDLSLPIPGKEDLAKLHSTIHQSAVSKAGTCGDSYAAQ SQ GWLSFFMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFR SQ HEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVICHHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHET SQ VVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISREWLNKFNTFAEPGPISNQSFLCSHGGIPPNKYHYID SQ DLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRRKTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEA SQ FVKAKDSDPPGPIDNSKVALTKSSGQVQLKQGADYGQISEETWNYLLNVYGGGPEIAIRQTVAQYQEAEHLHGEQKIEAE SQ TRAG // ID A0JMU8; PN Protein CASC3; GN casc3; OS 8355; 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: A0JMU8; DR UNIPROT: B7ZRY2; 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: No; 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 MADRRRRRRRASQDSEGEEEEEESGSDSVGSGGESGAPVRQERSEQGNRKAEPPREGKESECESEDGIEGDAVLSDYESA SQ DESEIVPTKEVEEAHYNEEEPLKATLKQENNVEEAPAARDQKPKSKGTVTGERQSGDGQESNEPEEDKTIQKSQKQLDDD SQ EDRKNPAYIPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWVHDRFHEDEQAPKSREELISIYGYDIRSSKNPEE SQ IRPRRPRKPRFSSPSRREENNEKASWPLNRYQDSGDAQPLRPYTNRSAPPSNKVVPSRTYSRQGGYKENRASYQSEEEAS SQ LHTYERRQVYGGHRARSSEQGPPPPREFSPEADPIVKEEAVIEKQAAEPSPPPPDRPVEKKSYSRARRSRIKVGDTGKSM SQ EDTTAAELPPPPLMPPAVAAEFTPAPLNVKQGNWEPPAEGGMSGIDEELSQMNLTEQSWNQGQPAYISPRGIPNPMHMGN SQ GPPQYSRMEGMAVQGGRVKRYSSQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYTHGDSSSSMPPQGMIVPPEMHLSHP SQ GMHPHPSPATMSTPNLYPAPVSLPPGQQPPQQLLPPPYFPAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGG SQ VTYYNPVQQQVQPKPSPPRRTSQPVTIKPPPPEENRHLKMNEKINS // ID A0PJ23; PN RING finger protein Z; GN Z; OS 192848; 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: A0PJ23; 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 MGLRYSREVKQRYGEKELEGRIPITLDMPQTLYGRYNCKSCWFANKGLIKCSNHYLCLKCLTAMLSRSDYCGICGGILPK SQ KLVFETTPSAPPYTP // 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 A1A5P9; PN Melanoma-associated antigen E1; GN Magee1; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane (By similarity). {ECO:0000250}. DR UNIPROT: A1A5P9; DR Pfam: PF01454; DR PROSITE: PS50838; DE Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0030425; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0045211; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSLVSQNSRRRRGGRANGRKNSGKGRPAAVPGPAVPRDRSDPQILQGLGATEGPGTSVLPTPRGGSSTSVPPTASEGSSA SQ PGQLITSEGRNTSQLPTSRKGRGTRRPPAVSAGLNAAASITASEGASTPVLPTAPKGSKASEHLTISEGASISEQPQSHE SQ GPNVQPTLGEGSGTSVPPTFSEESGISEPLPSGEGLSISVSPTISEGAGINEPSPASKAPSTSVPPTASNGLGINLPPTS SQ SEGLSISVLFSASEESDISVPPPSAEGLSTSMPPPSGEVQSTWVPPIILEGCSVKVRSTSRKGRRTPVRSAACESPSPSA SQ ECLSTSLSSISAEGFCSSLAPCAEGSDTCELLPCGEGPSTSGLHDLEEESSISQMPLAAEGPSASGSSIEDENPEEALSC SQ GASVGMNLCKCTSLALQKADDPSVRPKRAEGFLDFQVLRDSENSNSITIMGLGTAHVALTLKPQDPMEQNVAELLQFLLL SQ KDQTKYPIKESEMREFIVQEYRNQFPEILRRAAAHLECIFRFELKELDPEEHTYILLNKLGPVPFEGLEDIPNGPKMGLL SQ MMILGQIFLNGNQAREADIWEMLWRFGVQRERRLSVFGNPKRLLSVEFVWQRYLDYRPITDCVPVEYEFYWGPRSHVETT SQ KMKILKFMARIYNKDPMDWPAQYNEALEEEAERDVPNNWRAVPHFRRPLFQEVSPELLASDSDAPGCPSKYSPHSWPESR SQ LESKSRKLVQLFLLMDSTKLPIPKKGILYYIGRECSKVFPDLLNRAARTLNHVYGTELVVLDPRNHSYTLYNRREMEDME SQ EIMDSPNRPGNNFLMQVLSFIFIMGNHARESAVWAFLRGLGVQNGRKHVITCRYLSQRYIDSLRVPDSDPVQYDFVWGPR SQ ARLETSKMKALRYVARIHRKEPQDWPDQYREALEDEANRAEAGRRPLVVRNLR // 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 A1CYG5; PN ATP-dependent RNA helicase dbp5; GN dbp5; OS 331117; 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: A1CYG5; 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: No; GO GO:0005934; GO GO:0010494; GO GO:0031965; GO GO:0044614; GO GO:0005844; GO GO:0005524; GO GO:0000822; GO GO:0003723; GO GO:0003724; GO GO:0008186; GO GO:0016973; GO GO:0006415; GO GO:0006409; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MASEQPVEAAPTGGSLADRITKPDESNTSETPAPAADQTDGAPAQLGGSDLHEPEYNVEVKLSDLQADPNNPLYSVKNFE SQ DLGLDPRILKGLSNMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPT SQ RELARQILGVVQVMGQFVDGLIIGAAVPTDRDSRPKRLECSIVVGTPGTVGDMIKRRTFIPNKLKVLVLDEADNMLDQQG SQ LGDQCIRVKALLPRDIQVVLFSATFPEHVHQYASKFAPNANEITLQHEELTVEGIKQLYLDCADGEDKYKTLVQLYGLLT SQ VGSSIIFVQTRAAAQEIEKRMTAEGHTVVSLTGERDPSVRDAIIDQFRRGEAKVLIATNVLARGIDVSTVSMVINYDIPE SQ LHQPSVPGRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQTYFNCEIQRVDTKDWDEVEDIIKKTIKNSRA SQ NPKFAGGKE // ID A1L3G9; PN Nuclear envelope integral membrane protein 1b; GN nemp1b; OS 8355; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with lamins and banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. DR UNIPROT: A1L3G9; DR UNIPROT: B9X188; DR Pfam: PF10225; DE Function: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. DE Reference Proteome: No; GO GO:0016021; GO GO:0005635; GO GO:0005637; GO GO:0043621; GO GO:0001654; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINST SQ KMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCG SQ LLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYL SQ IVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIK SQ LKRAKPGPPRLLTEEEYRKQADVETRKALEELRECCSSPDFAAWKTISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGL SQ GGSFLEDELFGEDSDVEEEMEIEPPLYPIPRSVF // 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 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 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 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 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 A2A5R2; PN Brefeldin A-inhibited guanine nucleotide-exchange protein 2; GN Arfgef2; OS 10090; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes (By similarity). {ECO:0000250}. DR UNIPROT: A2A5R2; 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 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; DE Interaction: Q8BP00; IntAct: EBI-4282243,EBI-4283806; Score: 0.35 GO GO:0032279; GO GO:0005879; GO GO:0030054; GO GO:0005737; GO GO:0031410; GO GO:0005829; GO GO:0043197; GO GO:0000139; GO GO:0016020; GO GO:0005815; GO GO:0048471; GO GO:0055037; GO GO:0032280; GO GO:0005802; GO GO:0005086; GO GO:0050811; GO GO:0005085; GO GO:0017022; GO GO:0034237; GO GO:0010256; GO GO:0007032; GO GO:0006887; GO GO:0006893; GO GO:0035556; GO GO:0032760; GO GO:0015031; GO GO:0001881; GO GO:0032012; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKS SQ PRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTIL SQ QTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQS SQ KPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEP SQ DRALGALECQECAVPPGVDENSQTNGIADDRQSLSSADNLEPDVQGHQVAARFSHILQKDAFLVFRSLCKLSMKPLGEGP SQ PDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQ SQ IEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTP SQ LQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIQDD SQ PEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVD SQ QLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMT SQ KEQYIKMNRGINDSKDLPEEYLSSIYDEIEGKKIAMKETKEHTIATKSTKQSVASEKQRRLLYNVEMEQMAKTAKALMEA SQ VSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSL SQ LTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGE SQ EFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSL SQ QKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKK SQ NRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKC SQ LSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLT SQ VMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQ SQ WCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFKTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLS SQ SIDRNASERGQSQLSNPTDDSWKGAPYAHQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDAEI SQ HIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDE SQ NRRDSWDEIQQRLLRVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKISDEKFKAHASMYYPYLCEIMQFDLIPELRA SQ VLRKFFLRIGLVYKIWIPEEPSQVPAALSSTW // ID A2A6M5; PN Calcium-binding and coiled-coil domain-containing protein 2; GN Calcoco2; OS 10090; 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: A2A6M5; DR UNIPROT: Q3TK36; DR UNIPROT: Q3TKZ6; DR UNIPROT: Q3TL30; DR UNIPROT: Q9CWE3; DR Pfam: PF17751; 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:0005737; GO GO:0031410; GO GO:0005856; GO GO:0048471; GO GO:0016605; GO GO:1901098; GO GO:0098792; TP Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305}; SQ MDQCPIPTLLEHGNFSQVLFNNVEKFYAPRGDIMCYYTLTEKFIPRRKDWIGIFKVGWKTTQEYYTFMWAPLPKDQNKDS SQ ATQQEIQFKAYYLPKDVERYQFCYVDEDGLVRGTSVPFQFCPDPDEDIMVVINKEKVEEMEQLSEELYQQNQELKDKYAD SQ LHEQLQRKQVALEATQRVNKTLEHKVEEKASWEKEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKAS SQ WEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEKEKASWEEEKASWEKEKAPWEVEKAPWKE SQ VKAYWWNDLHR // ID A2AI05; PN NADPH-dependent diflavin oxidoreductase 1; GN Ndor1; OS 10090; 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: A2AI05; DR UNIPROT: Q3TQZ6; DR UNIPROT: Q80WC5; 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: Yes; GO GO:0005737; GO GO:0005829; GO GO:0045111; GO GO:0005654; GO GO:0048471; GO GO:0050660; GO GO:0010181; GO GO:0050661; GO GO:0003958; GO GO:0016491; GO GO:0016709; GO GO:0008219; GO GO:0036245; GO GO:0016226; GO GO:0055114; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRK SQ SLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVP SQ LDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNI SQ SFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACL SQ SQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQIL SQ VAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG SQ NFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDV SQ SEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA // ID A2CEI4; PN Nucleoporin 88; GN nup88; OS 7955; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}. DR UNIPROT: A2CEI4; DR UNIPROT: A0A2R8QUY6; DR UNIPROT: Q501Y6; DR Pfam: PF10168; DE Function: Component of the nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}. DE Reference Proteome: Yes; GO GO:0005643; GO GO:0017056; GO GO:0006406; GO GO:0006611; GO GO:0006606; GO GO:0000055; GO GO:0000056; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MASLAGDRWREALKNHDIFNNLQERLHLEPQGTSKRIAKNLTFCLNGDLFIWDSVESVFYTTNLRQLNSDGEPDTSRYQT SQ LLCINPPLFEVCQVLVSPSQYHVALIGQRGATVLELPQRWGKKSEFEGGRIQINCKTIPVAERFFTSSASVTLRQAVWYP SQ SETEEPHLVLLTSDNTIRFYNLKEPQSPARVLSVSQMDDDSSVHTRSRSYAASLGETAVAFDFGPLADSPHLSSLRMKAE SQ LVVYPLYILYGNGETFLNYISLSHSVGSLGKPMGPLPMYPAAEDNYGYDACAVLCLPCVPNILVIATESGMLYHCVVLEA SQ EEEEDGGAVERWSRGSETAPSLYVFECVELELTLKLPAGEEEEITESDFTCPIRLHRDPLCQHRYHCTHEAGVHSVGLTW SQ FKKLHKFLESDEEDKDSLQELAAEQRCIVEHILCTRPLANSLPAPVRGFWIVSDLSLGATMICITSTYECLLLPLLSSIR SQ PASPPLLCSHPGAGSDSSPLRGLAEDSFEQHIRNILARSSTNPLMLRSGDKDSSPPPSECLQLLSRATQVFREEYILKLG SQ LAHEEMQRRVKLLSGQKNKQLEDLALCREDRKSLTEAAERLADKYEDAKYRQEAIMNRVKRVLGSLRSQLPVLSDSEKDM SQ RKELQTINDQLRHLDNGIKQVNMKKDYQKKQMNAGASPAHSSLTLNAHQRKCLQGVLKEQGEHIAGMMKQIKDIKNHFSF // 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 A2VE78; PN F-box/LRR-repeat protein 5; GN FBXL5; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: A2VE78; 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. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; GO GO:0019005; GO GO:0005506; GO GO:0055072; GO GO:1903364; GO GO:0016567; GO GO:0031146; GO GO:0006511; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAPFPEEVDVFTAPHWRMKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVH SQ SDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTKDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCS SQ QKDTAELLRGLSLWNQAEERQKFFKYSVDEKSDKEAEVSEQSTGITHLPPEVMVSIFSYLNPQELCRCSQVSTKWSQLAK SQ TGSLWKHLYPVHWARGDWYSGPAAELDTEPDEEWVKSRRDESRAFQEWDEDADIDESEESGEESIAISIAQMEKRLLHGL SQ IHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVA SQ LEKISRALGILTTHESGLLKTSTSKVTSTTWKNKDITMQSFKQSACLHDVTNKDIGEEVDNEHPWTKPISSDDFTSPYVW SQ MLDAEDLADIEDAVEWRHRNVESLCVMETASNFSCPSSACYSKDIVGLRTSVCWQQHCASPAFAYCGHSYCCTGTALRTM SQ SALPESSALCRKAPRTRLLREKDLIYSGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTVT SQ GAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE // ID A3GFS1; PN Nuclear protein localization protein 4; GN NPL4; OS 322104; 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: A3GFS1; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSVTLRFRSREGTFRVAANPDADFLLVLEQLLSKISIEDVQNLYLSDKPNSKGELANGLCGKTVTELGLKNGDMLYASYE SQ AATGSNPDSTTNITTSTNNHNSGSISIGHISIPTTTSGPRKVTQLPVDDVLEKDEGLIKRPLTKFCRHGAKGMCEFCSPL SQ PPWDANYRKENAIKHMSYHAYLKELNELKNSKHNSSSYIAPLEEPNYSILLNCNEGHQPYPKGICSKCQPPPITLQLQKF SQ RMVDHVEFATSSIMNNFIDVWRHTGVQRFGVMYGRYEPFDKVPLGIKAVVEAIYEPPQSGELDGITMLPWENEAEVDAIA SQ SELGIYKVGVVFTDLTDSGQKNGTVLCKRHKDSYFLSNLEILMAARNQIQHANITKFSSSGQFSSKFVTCVISGGLNGEI SQ EPRSYQVSTSAEALVRADIITGSTQPSRLYVNSSNDRRYVPDVAYSELNEYGLEVKSNAKPTFPVDFLLVSLTDSFPVNP SQ TPMFDTDSNFVIENRDFFNELQNLHAVSKYLNADTSGKGTSLCNFHFLVYLKRTNILGAQEFDLLLRFVRERQYEDYLHL SQ VESPGWMTLITILEQST // 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 A3KPL7; PN Transmembrane protein 170A; GN tmem170a; OS 7955; SL Nucleus Position: SL-0178; SL Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}. DR UNIPROT: A3KPL7; DR UNIPROT: Q6PCR5; DR Pfam: PF10190; DE Function: May regulate membrane morphogenesis in the endoplasmic reticulum (ER) by promoting ER sheet formation at the expense of ER tubules. {ECO:0000250|UniProtKB:Q8WVE7}. DE Reference Proteome: Yes; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0071786; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MIEALIVGEMQDVQIGFVKQILSLNLVPRSNNTTCGNNTSLCDFSEMWYGVFLWAVVSSLIFHLPAALLALATLRRHKVA SQ RFFPLGILLMGIIGPLFGGVLTSAAIAGVYKAAGKSMFSLEALVFGVGQSLFIFIISFLRILATL // ID A3KPP3; PN Ran guanine nucleotide release factor; GN rangrf; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}. DR UNIPROT: A3KPP3; DR UNIPROT: A7E2J7; DR Pfam: PF04603; DE Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate (PubMed:26903377). {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:26903377}. DE Reference Proteome: Yes; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0005085; GO GO:0060047; GO GO:0001947; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HD47}; SQ MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWE SQ VRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAI SQ PWTLQDFQGVLQSLRLLDSGVFG // ID A4FUC9; PN Rhophilin-2; GN RHPN2; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: A4FUC9; DR Pfam: PF03097; DR Pfam: PF02185; DR PROSITE: PS51180; DR PROSITE: PS50106; DR PROSITE: PS51860; DE Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; GO GO:0007165; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MTDTLLPAAPQPLEKEGNCYFRKGCNPLAQTGRSKLQNQRAALNQQILKAMRMRTGAENLLKAATNQKVREQVRLELSFL SQ NSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFSVALKDFILEHYSEDSYLYEDEIADLMDLRQACRT SQ PSRNEAGVELLMSYFMQLGFVESRFFPPTRQMGILFTWYDSLTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTEA SQ GLESTVDAFQRAAGVLNYLKETFTHTPSYDMSPAMLSVLVKMMLAQAQESTFEKVCLPGLQNEFFLLVKVAQEAAKVGEV SQ YRQLHTAMNQEPVKENIPYSWASLACVKAHHYEALAHYFTATLLIDHQLKPGEDEDHQEKCLSQLYSHMPEGLTPLATLK SQ NVHQRQLLGKSHLCQAVTHHEESMREASLCKKLRNIDVLQEVLSAAHDRSQLKYTQLREDDDLLNLTDAPDIVSKTEREV SQ EIIVPQFSKVTVTDFFQKLGPLSVFSANKRWTAPRSIHFTAEEGDLGFTLRGNSPVQVHFLDPYCSAAAAGTKEGDYIVS SQ IQDVDCKWLTLSEVMKMLKSFGQDDIEMKVVSLLDATSTMHSKCATYSVGMQKTYSMICLGIDVDDKTDKTKKVSKKLSF SQ LSWGTNKNRQKSASTLCLPSVGVTMPPVKKKLSSPFSLLNTDSSLY // 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 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 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 A4IG66; PN Transmembrane protein 201; GN tmem201; OS 7955; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000305}. DR UNIPROT: A4IG66; DR Pfam: PF10476; DR Pfam: PF09779; DE Function: May be involved in actin-dependent nuclear movement. May be involved in the organization of the nuclear envelope. May recruit Ran GTPase to the nuclear periphery. {ECO:0000250|UniProtKB:A2A8U2, ECO:0000250|UniProtKB:Q5SNT2}. DE Reference Proteome: Yes; GO GO:0005639; GO GO:0031965; GO GO:0051015; GO GO:0005521; GO GO:0030473; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MEALNQILIEYPPLVVGGVGATAVAAGGALIYRIATRKKPTHLQVNCWFCNQDTVVPYGNRNCWDCPYCEQYNGFQENGD SQ YNKPIPAQYMEHLNHGVSAGVPETPKTLQWVNCQMLLCKKCNNNQTLKIKQLASFIPREDENYDEEIEVYKHHLEQTYKL SQ CRPCQTAVEYYIKHQNRQLRALLFNHQLRRTRDADKAFIKNTYSLSTPAWLILLRILTFLACAFLVAVALSGYVDESPSV SQ TQTLSGGVVPPKRVLQNENESKTDEGSLMWDDLMGLLPEKAVENARLFWQSGSDHQMAVASVGLLTCITGVLMAGPVRLR SQ RIDAVASVLWLLVICFYLAECYLKTDVPSWLEMVKFGITSVCCLVGFAAAVATRKSTSQRRARGRRYLSGGSPGEFFCNH SQ GPLLSAPVSESSTFIPTPPPNLSQLLIRQQSQRTRKASPSSLPGRLNRALSLGTIPSLARADSGFLFSGSRPSSQCKDSP SQ PSDYYSLKSGSRPSSPGPSPTPSVAGSVTSTSSSARQRRPLISPARLNISGQKLRLFSSPLEPFSLASPPPFLSEHNPMH SQ SRGFLPDVPHFHLQNHGSVIDEGSVFEHLEKPMGSSSSSSNCHVDTTTGNNIESKPGWKGFLGMTLWPGLLFASLTINLS SQ FICIYVYYNWR // ID A4IHT0; PN Fidgetin-like protein 1; GN fignl1; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. DR UNIPROT: A4IHT0; DR Pfam: PF00004; DR Pfam: PF17862; DR Pfam: PF09336; DR PROSITE: PS00674; DE Function: May be involved in DNA double-strand break (DBS) repair via homologous recombination (HR). May regulate osteoblast proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}. DE Reference Proteome: Yes; 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:0031122; GO GO:0010569; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MQVPESSLAHLSEWQRDAFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAIIDSDKLEIGL SQ NNYADSILTLAKCQRNESDKWQSSLTTNNVLKLKSVQDMAVAGRRTQLSKSSADASVRVGNGINTSGYSAGLGNNVLRNS SQ GYTVPHAALSDCQMPGGSANFLQKPKISAFTIANTTSVANTSSNTLINNSISMTSSLMQSNEDKDPASFSGHMFLPTTSV SQ HSGKRKAYSALGNESSDIKPNPLVQRQLTNKEATCESGFKTAKEQLWVDQQKKYSNQPQRNPSPLYGGAKKSLGAARSRG SQ LHGKFVPPVPRQEDVQDSNRKVYGQGNSEMNAPSDERLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVV SQ WPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIF SQ IDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSDDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVV SQ SLMAKEHCSLAEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITPEQVRPIAYIDFQSAFLVVRPSVSQK SQ DLELYENWNKTFGCGR // ID A4RN19; PN Nuclear protein localization protein 4; GN NPL4; OS 242507; 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: A4RN19; DR UNIPROT: G4MZE9; DR UNIPROT: G4MZF0; 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:0005829; GO GO:0005783; GO GO:0005789; GO GO:0031965; GO GO:0042175; GO GO:0005634; GO GO:0048471; GO GO:0051028; GO GO:0015031; GO GO:0030433; GO GO:0006511; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MLLRLRGPDGMLRIELDPKDTFNKLGQELMGKLPPTVDPATITVSNAPGSQGDKKLLKDIAKYKVEAIGLKHGDLIFVDY SQ KHQGAEADGTANSDGASQPLTSTTNRLNGQPVLPTEDLPIDPLPTPAPGATIKNPWEVVRQSPLDDRLDKKDGKIPRKRD SQ AMCRHGPKGMCDYCQPLDPFDAKFLAEKKIKYLSMHAHLRKINSATNKPELGSSFIPPLSEPYFRVKHDCPSGHPQWPEG SQ ICSKCQPSAITLQPQPFRMVDHVEFASPSIVDSFINTWRRTGGQRYGIMYGKYSEYEEVPLGIKAVVQAIYEPPQVDEVD SQ GVSLNSWDNEKDVNQVARLCGLEPVGAIWTDLLDAGAGDGSVVCKRHADSYFLSSLEVCFAARLQAQHPKPSKWSDTGRF SQ GSNFVTCIISGNEQGEIAISSYQVSNEAVEMVRADIMEPSADPTVMLVREEEEDDGSTSRTRYIPDVFYRRINEYGANVQ SQ ENAKPSFPVEYLFVTLTHGFPDVAKPMFSDEGAFPIENREYMGESQEHSAAAKALKVHEKASSGSSKDGMKVSNFHLLCF SQ LHQMSVLSKDEESLLCRVATQHDLADAFQLRSTTGWQTLMAILQSTGERIPKRSRQTDVLAADPAASSYPGRRGIDDSDE SQ RLAKRFASVRLNARGDGRNGRDRPSAHET // ID A5D7F8; PN E3 ubiquitin-protein ligase SH3RF1; GN SH3RF1; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. 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: A5D7F8; DR Pfam: PF00018; DR Pfam: PF07653; 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. 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. 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. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}. DE Reference Proteome: Yes; 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: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 MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRP SQ WKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI SQ IVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG SQ MLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQ SQ RHSMEISPPVLISSSNPAAAARIGELAGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPAEAPYPAALATLNPPLP SQ PPPLQAATPTGTAVAAAAGMGPRPTAGPTDQTTHPRPQPRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGT SQ SMHTSKIGVFPGNYVAPVTRAVTSASQGKVPMLTTGPASRGGVLANPPSTGGPAQKPPGNGVAGGPGVPTAVVSAAHVQT SQ SPQAKVLLHASGQMTVNQARSAARTVSAHSQERPTAAVTPIQVQSTPGQSHHPLVSPQPPAPLGPPAHAAASGLGRVGGP SQ LACATAPASIPAASLEPEPSSRPATLLPGTPTSPDSGSAARPDKDGKKEKKGLLKLLSGASTKRKPRGSPPASPTLDAEL SQ GAELSCGPPGPPCACPGPCDGDTMAPGPQRRASSLDSAPVAPPPRQPCSSLGPAASEVRPAVCERHRVVVSYPPQSEAEL SQ ELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI // 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 A5D8S5; PN E3 ubiquitin-protein ligase SH3RF1; GN sh3rf1; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. DR UNIPROT: A5D8S5; DR Pfam: PF14604; DR Pfam: PF13445; 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. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}. DE Reference Proteome: Yes; GO GO:0005794; GO GO:0030027; GO GO:0048471; GO GO:0005078; GO GO:0046872; GO GO:0061630; GO GO:0006915; GO GO:0001764; GO GO:0046330; GO GO:0051865; GO GO:0043370; GO GO:2000564; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRP SQ RRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIII SQ LRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGML SQ GDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPP SQ PQRHSMEISGPVLISSSNPTAAARIGELSGGLSSSAPSQVHICTTGLIVTPPPSSPVTTATVFTFPPETSYASIPVDALP SQ PPPPPPPQSQSSVVGAAALNAGQRPSPAAGDQSGRQRPTVYVAMFPYSPRKEDELELRKGEMFLVLERCQDGWFKGTSMH SQ TGKIGVFPGNYMSPVSRTVSGSSQPKVPLTLCSQAGRGVTIVSPSSALGSMDLSKPLPVCPNATPSCSLPAAVVTAAHLP SQ TGQHPKVLMHVTSQMTVNQARNAVRTAVSHSQDRPTAAVTPIQSHNPVAYLPSTAVVLQASPVLNSSSGCSSARVGVALG SQ CAAASLTPPNVSAASLDTDAMRPVPMVALPVNAGSTKPLGAASNHGVACRLDKDCKREKKGLLKLLSNKKKLRPSPPSSP SQ TLEAEQSVSMELPQGAVGPEMALSGSAGHNGRIGACPMDSELSMSSSSSNTDAVTHRSSPQDNTAPIAPPPRQPCSSLLS SQ MQHDGRPIVCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGRTGLFPGSFVDSI // ID A5DBC9; PN Nuclear protein localization protein 4; GN NPL4; OS 294746; 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: A5DBC9; DR Pfam: PF05021; DR Pfam: PF11543; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MCYFCDFASLRVSYFIINFKFQLTQIIRFRTPSGMLRVNATPETAFNDLLNDLGNQMGESDLSSFTFSDKPNDKGSSANT SQ FHGKSVADLGLKHGDMLYVTRTATSSSPAVTASVNEPKSGSAVVTKPINTAGIIPIHGPTKVKQLEVDDVLDTQDGMIKR SQ KKSNLCRHGEKGMCEYCSPLPSWDKGYREENGIKHMSFHAYVNQINEQKNNRNNSTSYMSPLEEPDYNVNLNCPSGHAPY SQ PKGICSKCQPPVITLQQQQFRMVDHVEFADSGILNDFIDVWRQTGVQRFGFMFGRYEVFDKVPLGIKAVVEAIYEPPQAG SQ ETDGITLLPWENQELVLKVAEKLNLYPVGIAFTDLTDSGARNGTVLCKRHKDTYFLSCLEVLMAARFQIEHPNITKHSNS SQ GRFSSKFVTCVVSGGLEGEIEPRSFQVSTNAEALVRADIITGSTQPSMLYINSSQGKRYVPDVFYSKINEYGLEVKTNAK SQ PAFPVDFLLVTLSDAFPLNPTPRFTNGFTIENRDFMGNLQDLRAAYRYINSDPGNGSCLSNFHFIVYLVTLGILGDSELQ SQ MVFD // 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 A5DX93; PN Nuclear protein localization protein 4; GN NPL4; OS 379508; 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: A5DX93; DR Pfam: PF05021; DR Pfam: PF11543; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSLILRFRSKDGMFRVNTDSSSTFQTVVDQLSLKLPTTDYDQITVSDKPNNKNDLGSQAKTLLSILHQTISELQLKNGDL SQ LFLNYSNAIPQGTLASTSSTKLQSGSIAINSSGGSSGPATASGANASTIRVSPTTHGPVKVSQLPIDDELDSQDGILSRP SQ ISSMCRHGAKGMCEYCSPLPPWDENYRKEHAIKHISYHAYLKQQMAKFNKKELSSSYIAPLENPNYAINLNCNEGHQSYP SQ RGICSKCQPLPITLQLQKFRMVDHLEYASHTILNDFINVWRSTGVQRFGYLYGRYEKFDKVPMGIKAVVEAIYEPPQHDE SQ LDGLTLLDWEDEPIVDAIAAKLGLQKVGIVFTDLTDSGNRDGTVLCKRHKDSYFLTNLEIIMAAKFQIKNPNITKYANLG SQ EFSSKFVTCVISGGLQGEIEPRSYQVSSSAEGLVKADIITGSTQPSQIYVNGNNDTRYVPDIQYSKINEYGLEVKSNAKP SQ TFPGEFLLVSLTDSFPIDPKPLFTSKISYVIENREFLGHGDIDGLDHLQNLSSVAKFIKLNDSELFDFHWLVHVAKMGIL SQ SEEELSLLCKYVKEKKYDDYLQLMESGGWMTFLTILEQST // ID A5DXE2; PN Protein transport protein SEC13; GN SEC13; OS 379508; 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: A5DXE2; 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:0005789; GO GO:0000139; GO GO:0031080; GO GO:0035859; GO GO:0005198; GO GO:0090114; GO GO:0051028; GO GO:0031081; GO GO:0043547; GO GO:1904263; GO GO:0045893; GO GO:0015031; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MVTIGNAHEDLIHDAVLDYYGKRLATCSSDKTIKIYDIEGTENYKLTATLTGHEGPIWQVAWAHPKFGSILASCSYDGKV SQ LIWKEQQDTQQWSIIAEHTIHQASVNSVSWAPHELGAVLLCTSSDGKVSVVDFNDDGTTSHVIFDAHAIGVNSASWAPFT SQ AASSTSSKDANTLKQHRRFVTCGSDNLVKIWKYDTALETYAEEAKLEGHTDWVRDVAWSPSNLVRPYIATASQDCTVLIW SQ TQDKDGKWQSQPLTEEKFPDVCWRCSWSLSGNILAVSGGDNKVTLWKENLQGKWESAGEVELIK // ID A5DZX2; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 379508; 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: A5DZX2; 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:0005737; GO GO:0031965; GO GO:0005643; GO GO:0005524; GO GO:0003723; GO GO:0003724; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSNTKDVDADASNLLASLSVSKEKKEDTSNILAGLSLNGDESNKKEGSGVKDTESDKQKGNGKVEKVEKDENKDKSQSEA SQ KDDSKRETNLIENRYEVEVKLDDIQADPNSPLYSVKSFEELGLKPELLKGLYAMKFNKPSKIQERALPLLISNPPKNMIG SQ QSQSGTGKTAAFSLTMLSRVDESIKAPQCICLAPTRELARQTLEVVETMGKYSNITYQLVVPDSVPRGQAISAQVLVGTP SQ GIVHDLINRKAINVAKVKVFVLDEADNMLDAQGLADTCLRVKKRLPRDCQLVLFSATFPTEVRKYAEKFVPNANSLALKQ SQ EELNVKGIKQLYMDCKNQEHKFEVLCELYGLLTIGSSIIFVEQKATADSLYLRMKEEGHTVSILHGGLEVADRDRLIDDF SQ REGRSKVLITTNVLARGIDIATVSMVVNYDLPRTKEGRPDPSTYLHRIGRTGRFGRVGVSVSFVANEKDYQTLKYIAEYF SQ GIEDQMTVVPTDDWDEVEKIVTRVIKEKKMT // 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 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 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 A6NFY4; PN Nuclear envelope integral membrane protein 2; GN NEMP2; 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:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. DR UNIPROT: A6NFY4; DR UNIPROT: B4DYG6; DR Pfam: PF10225; DR OMIM: 616497; DR DisGeNET: 100131211; DE Function: DE Reference Proteome: Yes; DE Interaction: P62826; IntAct: EBI-286642,EBI-21557397; Score: 0.35 GO GO:0016021; GO GO:0005635; GO GO:0005637; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MGPRQGRWWLLLWLPPLATLPVRGEAAAAALSVRRCKALKEKDLIRTSESDCYCYNQNSQVEWKYIWSTMQVKITSPGLF SQ RIVYIAERHNCQYPENILSFIKCVIHNFWIPKESNEITIIINPYRETVCFSVEPVKKIFNYMIHVNRNIMDFKLFLVFVA SQ GVFLFFYARTLSQSPTFYYSSGTVLGVLMTLVFVLLLVKRFIPKYSTFWALMVGCWFASVYIVCQLMEDLKWLWYENRIY SQ VLGYVLIVGFFSFVVCYKHGPLADDRSRSLLMWMLRLLSLVLVYAGVAVPQFAYAAIILLMSSWSLHYPLRACSYMRWKM SQ EQWFTSKELVVKYLTEDEYREQADAETNSALEELRRACRKPDFPSWLVVSRLHTPSKFADFVLGGSHLSPEEISLHEEQY SQ GLGGAFLEEQLFNPSTA // 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 A6RC50; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 339724; 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: A6RC50; 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:0005934; GO GO:0010494; GO GO:0031965; GO GO:0044614; GO GO:0005844; GO GO:0005524; GO GO:0000822; GO GO:0003723; GO GO:0003724; GO GO:0008186; GO GO:0016973; GO GO:0006415; GO GO:0006409; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MATETPAGGPLEARISRAEPKTDASATSEPATGDTTETPAATKPSAADGQTDGASEGFGGSQLQEPEYSVNVKLSDLQAD SQ PNNPLYSIKSFEELGLHPSILQGLHSMSFRRPSKIQEKALPLLLNNPPANMIGQSQSGTGKTAAFVLNILSRLDLSPQME SQ LAPQALVLAPSRELARQIVGVIQVMGSYVDKLKVATAVPMESNRNQKVEAPVVVGTPGTVMDLIRKRLFNPQHLKVIVLD SQ EADNMLDQQGLGDQCIRVKGLLPKNIQVVLFSATFPDHVVRYANKFAPNANQITLKHEELTVEGIKQLYLDCDSDEHKFD SQ ILVKFYGLLTIGSSIIFVKTRASAVEIERRMVAEGHTVVSLTGGVEGQKRDEIIDKFRQGDAKVLITTNVLARGIDVQTV SQ SMVINYDIPELHAPKATKRIADAQTYLHRIGRTGRFGRVGVAVSFVASKEEWQMLQDIKTYFNTEIQRVNTQDWDEVEEV SQ VKTIIRSSRAGSNFQRS // ID A6SBT4; PN ATP-dependent RNA helicase dbp5; GN dbp5; OS 332648; 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: A6SBT4; DR Pfam: PF00270; DR Pfam: PF00271; 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: No; GO GO:0005737; GO GO:0031965; GO GO:0005643; GO GO:0005524; GO GO:0003723; GO GO:0003724; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MAESKSTSWADEVASPTIEKNEGNPLEEAQLDGATEPLGGGTLQDGQYEVEVKLSDIQGDETSPLYSVETFEQLGIDASI SQ LKGLYAMNFKKPSKIQEKALPLLLRNPPTNMIAQSQSGTGKTAAFVITILSRLDFSKPTTPQALCLAPSRELARQIEGVI SQ RSIGQFVDGLTVQAAIPGAVERNAKVNAMVVVGTPGTVMDLIKRRSIDASQMKILCLDEADNMLDQQGLGDQCMRVKSMI SQ RVEQILLFSATFPDEVYGFAQDFSPRANEIKLKRDELTVSGIKQMFMDCPNEVGKYEILVKLYGLMTIGSSIIFVKRRDT SQ ASNIAERLTKEGHKVAAVHGAFEGSERDQVLEDFRQGKAKVLITTNVLARGIDVQSVSMVINYDVPMKGRSDSDPPPETY SQ LHRIGRTGRFGRVGVSISFVFDRKSYDALNQIANHYNIDLIKLNQDDWDETEEIVKKVIKSSRAGTNLQS // 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 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 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 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 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 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 A7EGK5; PN Nuclear protein localization protein 4; GN npl4; OS 665079; 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: A7EGK5; 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 MLLRFRGPDGTVRIAVEANETFGQLGDKLLKLLPENLDPRTLTLSNAPSGGEVKLLMEIARAKVSQIGLKNGDMVFINYK SQ LLDNLPNGNSTTSTSTTHSSHLTSSTNRLNGSAVLPESIPVNVPAQAVTSPSEKIKNPWEVVQQSDLDNRLDKKDGKIPR SQ KRDTKMCRHGEKGMCDYCMPLEPFNAQYLAEKKIKNLSFHSYLRKINSATNKPELGSSFMPPLTEPYYRVKKNCPSGHPQ SQ WPEGICTKCQPSAITLQPQEFRMVDHVEFAQASLVENLLVFWRSTGAQRFGYLYGRYEEYTEVPLGVKAVVEAIYEPPQV SQ DELDGITLNKWESEKDVDEMARLCGMERVGVIWTDLLDSGAGDGTVICKRHIDSYYLSSLEIAFAARLQAKHPKPTKWSD SQ TGKFGSNFVTCVVTADETGGIAISAYQVSNTAVEMVRADIVEPSADPAVMIVRSEGDDDSDTSARYIPEVFYRKINEYGR SQ SVQENAKPSFPVEYLLVTLTHGFPSDPKPAFMAKNSFTIENRLVIGQEQDIKDVGKQLGLDKNGQLTQSSDGVLAVSDFH SQ LLCYIYSMGILSKEEMALLCRVATQHDLADGYQLIATPGWANFLAILQSTG // 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 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 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 A7RVK7; PN Probable trafficking protein particle complex subunit 2; GN v1g94938; OS 45351; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. DR UNIPROT: A7RVK7; DR Pfam: PF04628; DE Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005794; GO GO:0048471; GO GO:0006888; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MLGNYYFAIVGHYDNPVYEKEFNQQMKMDSNDHRHLNQFIVHAALDLVDESMWGTTGMYLKSVDKFNEWFVSAFDPPLSW SQ IIDPQFFLDLTSWMRFMMLHDVKNDDGIKNFFSDVYETFIKVLMNPFYEINSKIKSANFDKKVLLAAKKHILP // 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 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 A7TTC4; PN Nuclear protein localization protein 4; GN NPL4; OS 436907; 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: A7TTC4; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MLLRFRSKIGMNRVSCEATDLFGDVVENWVKEVGLNVDPGTVVVGNDPGSAKEPVSNIAGRSVEEMGLKHGDIVYIEYSD SQ SSGSNEGQSVPVNAVGAGSAVISELPVDVLLEKEDGLIKRTRSSLCKHGDKGMCEYCSPLPPWDKEYHAENKLKHISFHS SQ YLKKLNEATNKKSSGSSYIPPLSQPDYKINKRCNNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEIQQSDLINQFIES SQ WRATGMQRFGYLYGSYEKYDSTPLGVKAVVHAIYEPPQHDEQDGLTMDLEQVEEEMQKVDQIAMSMGLLRVGLIFSDLTD SQ TGNGNGTVFCKRHKDSFFLSSLEIIMAAKHQLAFPNASRFSEQGKFSSKFVTCVVSGNLDSEIDITSYQVSIEAEALVDA SQ KMISGSTHPSMAYINETNEEVYVPEIFYMKTNEYGLTVKENAKPAFPVDYLLVSLTHGFITEDSKNQIKFHSTGGFPWAN SQ RQAMGLSQDYQELKNYLYSAATGGDYNLLHEKISNFHLLLYIKSLEIFNEKDWSLLITSAISENWEQPLIQLTTTESFNS SQ LVLIMEMI // 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 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 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 A8E5V9; PN Stimulator of interferon genes protein; GN sting1; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; 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. {ECO:0000269|PubMed:30842662}. DR UNIPROT: A8E5V9; DR Pfam: PF15009; DE Function: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Exhibits guanine base- specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling (PubMed:26300263). {ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:30842662}. DE Reference Proteome: Yes; GO GO:0005776; GO GO:0000421; GO GO:0005737; GO GO:0031410; GO GO:0005789; GO GO:0033116; GO GO:0016021; GO GO:0048471; GO GO:0035438; GO GO:0061507; GO GO:0042803; GO GO:0002218; GO GO:0000045; GO GO:0051607; GO GO:0045087; GO GO:0032608; GO GO:0016239; GO GO:0032481; GO GO:0061709; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFV SQ TAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKES SQ IQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCI SQ VEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQ SQ QHSEEYSML // ID A8QFF6; PN Probable spastin homolog Bm1_53365; GN Bm1_53365; OS 6279; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: A8QFF6; 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:0048471; GO GO:0005524; GO GO:0016853; GO GO:0008568; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MLHPQKLEQQNYETFNKAYLKSKQLVTEGVSIDEISSNNDEQRKRIAMEKYRMGIEYFEKALKISPDKVYPEKRSEVITH SQ REAMKRNLEATKGRLSDLEKMFPSKGNRNLQHRPVQFVSPSISKPQTAQLSSRPISSEKKNINYSNARTRSNLLKGVDDK SQ FGGPLLNEILNQDDVKMSDIIGAETAKRALEETVILPTVNPSLFSGLRQPAQGILLFGPPGNGKTLLARAVAGECGSTMF SQ LNVSAASLTSKWVGDAEKIVRALFQIARNGQPTIIFIDEIDSILCERNEKETEVSRRMKTEFLIQMDGMLSSKDDRLLVI SQ GATNRPEELDSAILRRFPKRILIDVPNAAARLKLIMSLLEKTKTSFDLGLTQRQILAEWTHGYSNSDLVALCREAAMVPI SQ RDLSRKDIKNLVSTELRPITLRDFEIAMKAIKPSTNERMLQKLRKYAATAGQSD // 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 A8WUP2; PN Zygote defective protein 12; GN zyg; OS 6238; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to the minus end of microtubules, proximal to the centrosome. Centrosomal localization requires sun-1 and microtubules. {ECO:0000250}. DR UNIPROT: A8WUP2; DR Pfam: PF05622; DR PROSITE: PS50021; DE Function: Cytoskeletal linker protein, which is essential for attachment of the centrosome to the nucleus. Required for dynein localization to the nuclear envelope (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005813; GO GO:0005737; GO GO:0016021; GO GO:0005874; GO GO:0031965; GO GO:0051959; GO GO:0008017; GO GO:0031122; GO GO:0030705; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLDLTNQESDSSENGNSKYADSTDGRGIGTSRRLDDEDLDERRKDLADLVFWMSGLKATTLPLDDHTSLCNGRAFAEILH SQ EIDRSFFDERWLETMPEMRTSSNLVVKRSNLRKLWRKMSDYIQVLNRKVVSTRWTEIGDRLDGLDETDIPVAADLAMAVV SQ SLAFIGKTQEKYIQYSQELPAGEHQHMMANVARLVQIVMEELPEVPTFHEISELDGSQNELNSSHVESSVITNGNGSAER SQ RSTLSANDQVLVEAQLEIDELRSERDNLIKDVERLTKALESSQLDTSTCSEPNELSILEKQNEELRVKRRQAEERVLELE SQ ASMEHFQAIVVKLTDENDTLQSGQKELNMLKTHLDTAQSDVEEWRTIANKYQSDAEMLKKREKEVKELQGQVKSLTSRLE SQ HHVKTATIDEDNKAGIVQLRSQIGTLTANNVELNVGLESKKRIVEQLELQLIQYKEKVKELEDRKEDLIAERNELENKLL SQ FKESVTPRSLHESMFEAGHLSFDDKTKLPLEIENKRLTERIQELESLEPLKGEIIKMKSQNGVLEEEKLVITKQMEELER SQ QVADLQEKLTKNQQHASGDVVELKVQLEKANVEVERMRETEMRTEAKLAGVEELLRKRNVEKEANETALQKAKAVIDELE SQ SRNRPVGEDNKTSVQDFKELKTENELLRQKNEALETALNTTTQSLEQENRLITSAAHQQILDRSSDSMMIMRAQAGSDHP SQ QTLLDTQKMTRALPWRFGISSMLIIFMVWFFINTFCEVNAPPKA // 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 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 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 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 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 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 B0BLK0; PN RING finger protein Z; GN Z; OS 144752; 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: B0BLK0; 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 MGLRYSKEVRDRHGDKDIEGRVPMTLNLPQGLYGRFNCKSCWFVNKGLIACGDHYLCLGCLTRMLSRTDFCEICSKPLPK SQ KIIFEDSPSAPPYEP // ID B0BLK7; PN RING finger protein Z; GN Z; OS 42764; 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: B0BLK7; 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 MGSKSSKSSGFENVPSLGLSHTNQPRVSLIREARPSLYGRYNCKCCWFQNKNLVECSDHYLCLKCISSMLRRGQNCEICG SQ KPIPTHIAVTTAPTAPPEP // ID B0BLK9; PN RING finger protein Z; GN Z; OS 208899; 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: B0BLK9; 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 MGNCRSKQESHPICPNTQTPEPTEAEFRRAAVNSLYGRYNCKCCWFADRNLINCSDHYLCLRCLNVMLRTSNLCNICWKP SQ LPTRISVPTEPTAPSE // ID B0F9W3; PN G-protein coupled estrogen receptor 1; GN gper1; OS 29154; 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:0000269|PubMed:18420744}; Multi-pass membrane protein {ECO:0000269|PubMed:18420744}. 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=Colocalized with cadherin at the plasma membrane. DR UNIPROT: B0F9W3; DR Pfam: PF00001; DR PROSITE: PS00237; DR PROSITE: PS50262; DE Function: Membrane 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. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}. DE Reference Proteome: No; GO GO:0030424; GO GO:0016323; GO GO:0030054; GO GO:0030659; GO GO:0005856; GO GO:0032591; GO GO:0005769; GO GO:0005789; GO GO:0000139; GO GO:0016021; GO GO:0031966; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0014069; GO GO:0045211; GO GO:0055037; GO GO:0004930; GO GO:0005496; GO GO:1990239; GO GO:0007189; GO GO:0006915; GO GO:0007049; GO GO:0030154; GO GO:0071392; GO GO:0071371; GO GO:0051447; GO GO:1900194; GO GO:0007399; GO GO:0043401; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPD SQ LYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAK SQ LSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQ SQ KALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKL SQ RLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV // 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 B0V3F8; PN Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog; GN prkra; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: B0V3F8; DR UNIPROT: A4IGC9; DR Pfam: PF00035; DR Pfam: PF16482; DR PROSITE: PS50137; DR PROSITE: PS50835; 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 (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0048471; GO GO:0003725; GO GO:0008047; GO GO:0030422; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAPQRSQDKTPIQLLHEYGIKISSAPKYELIHADGDAHQPSFMFSVTIGEVTCKGRGSTKKAAKHEAAEAALKLLKRDSQ SQ IIDQRDNNGLSPEAGEASNPVGILQELAMQRVWCLPEYVVFMETGPGHMKEFTIACRLEGLEETGSGSSKKLARRAAAEN SQ MIAKLQSLSGSSEITWSPPSRVYVESLRNSTGEKVSLLKRTPLSLPNTDYIQMLLEISLELGFQVTYIDIDELTVNGQYQ SQ CLVELSTRPVTVCHGSGVTSSNAHNAAAHNALQYIKMVASKH // ID B0WRR9; PN Cryptochrome-1; GN cry; OS 7176; 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: B0WRR9; DR Pfam: PF03441; DR PROSITE: PS00394; 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 MTDKVRNRVQCWPALAQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQESSCVDFIPARQGA SQ TCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQHTVNIIGEPPRPVGAPSFEFVEFGRLPSILSTELKLFQRAPVPED SQ FGIYYEGNADIARQRWTGGEAKALELLGRRLKQEEEAFREGYYLPTQARPDFLAPPSSMSAALRFGCLSVRMFYWCVHDL SQ FARVQANNQLKHPGGHHITGQLIWREYFYTMSVHNPHYAVMELNPICLNIPWYEAKDDSLDRWKEGRTGFPLIDAAMRQL SQ MAEGWLHHILRNITATFLTRGGLWISWEAGVQHFLKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPVALARRLDPK SQ GEYVKRYLPELEKFPALYVHEPWKAPPELQEQYGCVIGKDYPAPMVNLAEVNKCNANKMNAIRQKLLDQGGSTPAHCRPS SQ DMDEVRQFFWLPEDVAAES // 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 B2C4J2; PN RING finger protein Z; GN Z; OS 499556; 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: B2C4J2; 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: Yes; 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 MGNTKTKDRQYQSNSSQPTNTSAPVLLRRQAEPSLYGRHNCRCCWFADTNLVNCSNHYLCLKCLNTMLRRSNLCDICGEE SQ LPTTIIVPVEPSAPLPGQ // 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 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 B2RYN7; PN Spastin; GN Spast; OS 10116; 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: B2RYN7; 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 (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}. DE Reference Proteome: Yes; DE Interaction: P15127; IntAct: EBI-7472166,EBI-21297133; Score: 0.35 GO GO:1904115; GO GO:0005813; GO GO:0005737; GO GO:0031410; GO GO:0005829; GO GO:0071782; GO GO:0005768; GO GO:0016021; GO GO:0005874; GO GO:0015630; GO GO:0030496; GO GO:0031965; GO GO:0005654; 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:0032467; GO GO:0031117; GO GO:0034214; GO GO:0051260; TP Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021}; SQ MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRF SQ SRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVI SQ VTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMV SQ SGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQ SQ EIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQP SQ SIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRL SQ LLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRS SQ VSPQTLEAYIRWNKDFGDTTV // 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 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 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 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 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 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 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 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 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 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 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 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 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 C5H431; PN RNA-directed RNA polymerase NS5; GN POLG; OS 164416; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [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:P17763}; 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:P17763}; 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:P17763}. 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: C5H431; 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. {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 immune response. {ECO:0000250|UniProtKB:P17763}. [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. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [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. {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 (By similarity). 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. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}. 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:0005525; 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: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 MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKN SQ IRNIVTNLMKGLAGRKKKRSLTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCED SQ YVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGSRRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKW SQ IMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTWVSVVLEQGSCVTLIADNKPS SQ VDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFS SQ CTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGT SQ DAWLVNKQWVHDITLPWQSGTGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTC SQ KAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIKVTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEV SQ LVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGSTGGFFSSIAKAVHTVFGAAFH SQ AIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFS SQ KYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSE SQ LKYGWKTWGKNIIFNPSRKNGTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKG SQ SVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSHTLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWH SQ NVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGCWYSMEVRPKHTNEAHLVKSW SQ VVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLA SQ LLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCL SQ LTPLTVAEIQRAVMFVCSIVIFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAV SQ GLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGLVIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEP SQ APWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLEDGVYTINQNSFLGLAQKGVGV SQ VKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKN SQ GKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPG SQ AGKTRIYLPQILKECEKLKLKTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVT SQ NWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSATPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRR SQ PTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGANLKVERVIDCRTAYKPILVDD SQ ATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTT SQ TSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWV SQ DTRVCSDNASLIDFIKFAEGRRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVM SQ LAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGGMNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLV SQ GVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGNPMLHHWIKIDYGNISLSGIT SQ QNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDG SQ NPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGN SQ YYATIGLAYNGWLAKQTRRGKAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAK SQ IRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSD SQ TLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYY SQ ISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPY SQ RTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAW SQ LFQHLARKKKPRICTREEFVAKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREK SQ KPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSRENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDT SQ RITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQRGSGQVVTYALNTVTNLKVQL SQ IRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPS SQ QGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMAN SQ AINSTVPVDWVPTGRTTWSIHGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRA SQ SWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGPGEVLW // ID C8XPA8; PN RNA-directed RNA polymerase NS5; GN POLG; OS 38837; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [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:P17763}; 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:P17763}; 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:P17763}. 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: C8XPA8; 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. {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 immune response. {ECO:0000250|UniProtKB:P17763}. [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. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [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. {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 (By similarity). 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. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}. 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:0005525; 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: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 MVNPKGVNVMAARVKRAAQKTKKKAVQVSRGLRGFVLFVLTQLFMGRKLTPNVRRLWKSSDKNSLIHVLTKIKKIVGNLL SQ MGVSRRKKRRSATTSGTVFMAMLGLTLAASVARHAHHTLINITKDDAHKLLTLRNGNCTVVATDIGNWCPDNVEYDCVTL SQ QDNEDPDDVDCWCYRVNNVRVTYGRCKDGNTPRRSKRAVVITAHLDQGLTTKKETWLGSSHFETQVQKVEKWIIRNPTYA SQ IAAILMSWYIGNSLKQRVVLLLLTLALGPAYATHCVGIPKRDFVQGVQGTTWVNLVLEQGGCVTIMAEGKPSVDVWMDNI SQ KFTSPTLVRRISHTATISDTKIATACPSNGEAKLDEEHIKEYACKRLYSDRGWGNGCGLFGKGSLVACAKYESTGHMDVY SQ EMDMTKVEYTVKTQVHSGAKSGDLSGVKTVSFAPTSGSQPVEFSGYGNMGLQCMIQSNVDFSTHYLVVMGNDAWLVHKAW SQ VEDITLPWKHGEGGTWKDKQYMVEFGEPHATTVKVLALGPQEGALRNALAGAMIVTYESSGKTFKLHGGHVTCKATVSGL SQ ALKGTTYTNCRGGLSFVKTPTDTGHGTVVMQVKVAKSAPCRLTAIAADDASGHVNRGTLVTSNPIAASNNDEVMIEINPP SQ YGTSYLIVGVGDDKLVYQWKKSGSTIGSLFSETVKGAQRMAIVGSSSWDFSSTSGFFSSVGKAIHTVFGTAFHGIFGGLS SQ WMTRILIGVLLVWLGLNSRNGTATTLMMLTGFIILFLSLGVGAEVGCSVNWGQKELKCGDGIFVYNDVDDWMHKYKYHPE SQ DPKVMAGLIAKAWEKGACGLTSVSELEHVMWVKIASEINAILEENEIDLTVVVHENKSVYRRGSRRFPRVETELTYGWES SQ WGKNFITDGKVSNNTFHVDGKEDQCASKNRVWNSLEIEEFGFGVFHTNVFLRQKADKTNSCDTTLMGAAVKGNVAAHADP SQ GFWMESQENNGTWEIQSIEFTAYRECEWPVSHTVHGTQVMESDMFMPKGIGGPVSHLNRMQGYKVQTNGAWAYGKTVVQR SQ ELCPDTSVVVDSSCSDRGKSIRSTTTEGKVIKEWCCRSCTLPPVSYWTSEGCWYAMEVRPMKTPEKHLVRSWVTAGDSYP SQ AWSIGLVAMFLFVDIMARSRPTRKMMIGGTMLLLAIMIMGELSYLDLLRYIIVVGEHFIERENGGDVAYMAIMAASHLRP SQ GLMAMVFAKSMWSPKQRVLLALGCAILQPFLTAQASALVWEWADSIGLVLLIVQGMVRNKEKNWALVLLALCSPVSMPVI SQ RKASMIIGTGGLLLSLWKGGGSSMRKGLPLFAASAARVLGLTKAHLSVLFILLITKNGKRTWPISECLAAVGIFGAAFGT SQ MFSEDETLLGPLALVGVVLIVYTMFTQSDGLELVKAADISWSDEAVVSGEARRFDVALNDSGEFKLLDEPPVSWLNVSFL SQ VVAIVASSLHPIALVVTLVAWTYWRTEKRSGVLWDVPLAPKVEACEHLEDGVFRIIQKGLFGSSQVGIGVAKDGVFHTMW SQ HVTRGAFLMHSGKQLTPTWGSVRKDLVCYGGTWKLDGAWNGVDEVQLIAVPPGKPATNVQTKPGTFVLPTGDEAGAVLLD SQ FPSGTSGSPIIDRHGNILGLYGNGIVLENGAYASAISQAQPGSVAEVETPGLDKMLRKGEFTMLDYHPGAGKTRKHLPNI SQ LKECERKRLRTLVLAPTRVVLSEMKEALTSVQAKFHTQAFNSTTTGREIIDVMCHATFVHRMLEGLRSGNWEVIIMDEAH SQ FLDPTSIAARGWAHHKSKTKESAVIFMTATPPGTSNEFPESNAEIEDVKKEIPSEPWSKGHEWILEDRRPTVWFLPSIKA SQ ANVMAACLRKAERSVVVLNRSTFENVYPTIKTKKPDFILATDIAEMGANLPVERVIDCRTAYKPVLVDERVALKGPLRIA SQ AAAAAQRRGRVGRNPDRDGDTYVYSEDTCEQNDHLVCWTEGSMLLDNMQVKGGFVAPLYEEEASKTTMTPGECRLRDDQR SQ KVFRTLIRKHDMPVWLSWQVAKSGLAADDRKWCFDGEDDNAILGDNGEVIKARSPGGQRKELKPRWSDARIASDNTSLMN SQ FIAFAEGRRSLPLSILWSVPNQLSEKLVQSIDTLTILLRSEEGSRAHKLALQQAPEAVSTLLLLGMMAICTLGLVILLMK SQ PKATDKMSMAMVTMAITGYLLKLGGMTHAQVGGILLVFFIMMVVIIPESGTQRSINDNKLAYVIILVGLVIGGVACNELG SQ WLEKTKADLFGNNMTHAQTVVLPTINWNWLDFRPGAAWSLYVGMATFLTPVFVHWIKNEYGNASLTGITPTAGILGALNQ SQ GVPFVKLNTSVGVLLLSVWNNFTTSSMLAAMVMLACHCLFVLPGVRAQCLREAQIRVFHGVAKNPMVDGNPTVDLEKEND SQ MPDLYEKKLALVALGMAAVLNAAMVRTALTTAEMVVLGSAAVGPLLEGNTSAFWNGPLAVAVAGVMRGNHYALIGIVYNL SQ WLLKTARRGGSSALTYGEVWKRQLNLLGKQEFMNYKVSDILEVDRSHAREVLNSGNDAVGVAVSRGSSKLNWLIERGYLR SQ PTGRVVDLGCGRGGWSYTCAAERQVTSVKAYTLGKEGHEKPRLIQSLGWNIIKFKDKSDITRMTPHASDTLLCDIGESSS SQ NPEVEKERTLRVIEAVEKWMSPTTVSFCFKVLAPYKPDVIEALERFQLKHGGGIIRNPYSRNSTHEMYYVSGVRNNILHM SQ VNSTSRMLMRRMSRPSGRSTVVPDLIYPTGTRSVASEAGPLDLEKVKARINRLKEEQESTWFVDSDHPYRTWHYHGSYVA SQ KQSGTAASMINGVVKLLSGPWDRIEEVTNMAMTDTTPFGQQRVFKEKVDTRAPEPPQGTREIMKVVNQWLFDYLGRTKQP SQ RICTKEEFINKVRSHAALGGILTEQEGWSSAAEAVADPRFWSLVDKERQAHLEGRCETCIYNMMGKREKKPSEFGRAKGS SQ RAIWYMWLGARFLEFEALGFLNEDHWLGRENSKAGVEGIGLQYLGYVVEEVARKGNGLVYADDTAGWDTRITEADLEDEQ SQ YIMKRMSAEHRQLAWAVMELTYRNKVVKVPRPGPGGKILMDVISRRDQRGSGQVVTYPLNTATNMKVQLIRMAEAENVIT SQ RNDVEKVSLITLKELQLWLEVNGVNRLERMAVSGDDCIVAPVDESFAGALHHLNAMSKTRKDISEWENSRGWTDWESVPF SQ CSHHFHTLYLKDGRTIIAPCRCQDELIGRARISPGNGWMIKETAGLSKAYTQMWTLMYFHRRDLRLMANAICSAVPIDWV SQ PTGRTTWSIHATGEWMSSDDMLEVWNKVWIQDNPHVKDKTPIFAWRDVPYIQKGQDRACGSLVGTSLRASWAESIMTSVH SQ RVRMLIGNERYVNYMESMDRYATQRCSAYGELL // ID C8XPB2; PN RNA-directed RNA polymerase NS5; GN POLG; OS 64296; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {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}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [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:P17763}; 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:P17763}; 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:P17763}. 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: C8XPB2; 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. {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 immune response. {ECO:0000250|UniProtKB:P17763}. [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. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [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. {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 (By similarity). 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. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}. 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:0005525; 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: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 MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLK SQ GIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSD SQ SMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIER SQ WMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKP SQ SVDIWLDSIFISSPVLVRRVSHTATISDTKVQTACPTNGEAKLEEEASAEYECKKTYSDRGWGNGCGLFGKGSIVACAKY SQ TSTGHMDVYEIDSTKIEYVTKAQVHAGMKHDDTTMVKEVKFEPTTGSMDVEFTGYGTLGLECHVQTMVDMANYYLVVMGQ SQ EAWLVHKQWVEDITLPWKIGEGGFWRDKHYMVEFTEPHATTMTVMVLGAQEGALRTALAGAMVVTYTDSSGTKKFSLKGG SQ HVSCKARMNGLVLKGSTYTMCKGGFSFVKTPTDTGHGTAVMQVKVSKGTPCRIPVQAVDSSNGGTNRATLITANPIAATT SQ EDEVMIELSPPYGESYIMIGTGDDKLTYHWHKSGSTIGSLFTETYKGAQRMAIIGDDAWDFSSSSNFFNSIGKALHTVFG SQ NVFHSIFGGLSWITKIILGGMFLWLGVNSRNQTMCMVLMAVGGILLFMTLGVSGEVGCSLDIKRRELKCGDGLFLFNDVN SQ DWTHKYKFHPEDPKLLASLIKKSHQEGRCGLSSVNEVEHRMWNSIKTEINAMFEENGVDLSVVVKDSKLHYKMGSHAFPK SQ VEEGLSLGWKNWGKSLVFEPKQSNVSFIIDGTSEDCPFTNRIWNAFVVEEFGIGMFTTNVFLTHKVDFTKQCDASLLGAG SQ VKGDVAVHGDPTLWMESRKENGTWQLHTIQMNGLRECFWPQTHTIHGSSVMESAMFLPKQYGGPVSHHNHYTGYAVQTAG SQ PWNVQPLIVKRETCPGTQVRVDEQCRDRGNSVRSTTSEGKIIPEWCCRSCTLPPVSFWGPDSCWYAMEIRPQNVHEEHLV SQ RSWASAGTGMAESSLGLVALFLFTDIFARKRMTRKFMVIGCLGVLSVMIVGGFTALDLIRYIIVVGQHFASMNHGGDVAY SQ LAIIAVGKLRPGLLMMYSFKAAWSPKERVMVALGLLVFQAVLGDFVHTGLWEWADAAGMCILIIQGMATRKEKTYIMPIL SQ ALLTPLSMEIIRKTGIFACVGLLGLSLWRGGDTTMRKGMPLLAGAATAASGLTRASLSVVFILCATAASRRSWPIGEIMA SQ IVGIVGTGFGMAVNDQASLAGPMLVFGLIMIVYATLGRADGLTLKRVGDITWEEEAVHSGSSTRYDVTLNEAGEFKLVHE SQ EPVVWSHVVFLVVALIAASVHPIALVVVTIIWTYGKKHLRGGVLWDIPIAPPVEEAEPLEDGVYAILQSGLMGKAQAGVG SQ VAQEGVFHTMWHVTRGGFLMVGGKRLTPHWASVKRDLICYGGNWKLDGKWDGVEEVQLIAVAPGKAPTNVQTKPGVFRMA SQ DGTEIGAVALDYPSGTSGSPIVNEKGQVIGLYGNGIVIGGSGYVSSIAQIAGGEGVTEEPLLDTATMLRKGKLTVLDYHP SQ GAGKTRIFLPYILKECVRRKLRTLVLAPTRVVLSEMREALRDVAVKYHTQAFQAAGTGRELVDAMCHATLSHRMLESSRS SQ VNWEVIIMDEAHYMDPTSIAARGWAAHKANNHESAVIFMTATPPGSANEFPESNGEIEDLRRDIPTEPWNKGHEWILEDR SQ RPTVWFLPSIRAANNIAACLRRSERSVVVLNRQTFETVYPTIKTKKPDFILATDIAEMGANLGVERVIDCRTSYKPVLTT SQ DGRVVIKGPLRIPASAAAQRRGRVGRCKDRDTDSYVYSEETSEDNGHYVCWTEASMLLDNMEVKGGMVAPLYDVEAQKTE SQ MVPGEARLRDDQRKVFRTLIKRYDLPVWVSWQVAKSGLMLEDRKWCFDGDDENTILNDNGEKILARSPGGQRKFLCPRWN SQ DSRLYYDNASLMSFLAFAEGRRSYLGVWHAVQMAPLKLGEKLTESLDTMVMLMRSEEGTRAYKLASTNAPEAVTILLMTG SQ IVVACTLGVGLAFMWPKGVDKMSMGMITMSIAGYLMLQGGLTPVQVASVLLIFFIFMVVLIPEAGTQRSINDNKTLYVLL SQ GVALLIGAITANEMGYLEKTKRDLLGERVQNEWKLELPMFDLRPGAAWSIYVGLATLVMPVLDHWIRTEYGSLSLTGIAQ SQ QASILQAMDKGVPFFKLNMSVIVLLVSVWNNFSMLSVLCGVGLLGVHCAFVLPGLRAQAAKQAQRRVYHGVAKNPVVDGQ SQ TTAEIETAPEMPPLYEKKLALVLLGVVAIANGVMVRSAFSMAETVVLLSAAVGPLLEGNTSAIWNGPMAVAMAGIMRGNY SQ YAGIGLAYNLWILQSPKRGRSTTMTLGELWKRQLNLMGKREFELYKITDIHEVDRSQAQAVMKAGIDNVGISVSRGTSKL SQ KWMVDRNYVEPLGRVVDLGCGRGGWSYLCAASKRVSSVKAYTLGITGHEKPVNVQSLGWNIIKFKDKTDVFKMEPHACET SQ LLCDIGESSSNPLVEMERTLKVIDNVERWMSPTTESYCFKVLAPYRPEVIERLERFQLKYGGGIVRVPFSRNSTHEMYYV SQ SGVKNNLTHMVSCVSRLLLRRMTHPDGRCKVEADVVFPTGTRNVASDLGPMDLSKVKDRVNRLRSEQGTWFQDDSHPYRT SQ WHYLGSYVAKQSGSAATMVNGVVKMLSMPWDRIENVTQLAMTDTTPYGQQRVFKEKVDTRAPPPPPGTRAIMEVVNKWMF SQ DFLAREKAPRICTKEEFINKVRSNAALGNMLEEQDGWKDAATAVQDPRFWALVDRERQVHLEGRCETCIYNMMGKREKKP SQ AEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSLAGVEGVGLQYLGYVVKNVWEKSNGIMYADDTAGWDTRV SQ TEADLDDEQYLLSKMEGYHKKLASAVMNMTYKYKVVKVPRPGPGGKVFMDVIARQDQRGSGQVVTYPLNTGTNMKVQLIR SQ MAEGEGVISRHDIERVTIKTLNALRVWLAENGAERLSRMAVSGDDCVVAPLDERFGLALHHLNAMSKIRKDIDDWTESIP SQ WRSWESVPFCSHHFHQLFLKDGRSIVVPCRDQDELVGRARVSPGNGWKLKETACLSKAYAQMWLLMYFHKRDLRLMGNAI SQ CSSVPAHWVPTGRTTWSIHAHNEWISSERMLDVWNKVWIVDNPHMPDKTCIDDWRDVPYLPKSQDRLCGSLIGITARASW SQ AENIRAVVNKIRGMIGNEVYSDHLSVMGRYTYSVQEVGTVL // 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 D3ZVF4; PN Trafficking protein particle complex subunit 2; GN Trappc2; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}. DR UNIPROT: D3ZVF4; DR Pfam: PF04628; DE Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005793; GO GO:0005634; GO GO:0048471; GO GO:0006888; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSGSFYFVIVGHHDNPVFEMEFLPAGKTESKDEHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH SQ MRLIMLHDVRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSTAFERKVQFLGKKHLLS // 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 D7RF80; PN RNA-directed RNA polymerase NS5; GN POLG; OS 33743; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [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: D7RF80; DR UNIPROT: B1PMU9; DR UNIPROT: H8Y6L3; DR UNIPROT: H8Y6L4; DR UNIPROT: H8Y6L5; DR UNIPROT: Q14F58; 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. {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 immune response. {ECO:0000250|UniProtKB:P17763}. [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}. [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:P17763}. 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: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 MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRK SQ TVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCD SQ DSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEG SQ WVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKP SQ SVDVWLDDIHQENPAKTREYCLHAKLANSKVAARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKF SQ SCEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVV SQ LELDKTAEHLPKAWQVHRDWFEDLSLPWRHGGAQEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGS SQ KYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLIT SQ PNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGMLSSVGKALHT SQ AFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWR SQ EVTDWYDGYAFHPESPSVLAASLKEAYEEGICGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDKRDPSDYRGGKV SQ GTLRRSGKEMKTSWKGWSQSFVWSVPEAPRRFMVGVEGAGECPLDKRRTGVFTVAEFGMGMRTKVFLDLRETASSDCDTG SQ VMGAAVKSGHAVHTDQSLWMRSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPAGLAGPRSHYNHIPGYA SQ EQVKGPWSQTPLRVVREPCPGTAVKIDQSCDKRGASLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQ SQ GGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGSSVVWCGMVVLGLVVTGLVTIEGLCRYVVAVGILMSME SQ LGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVATYFLLLVLELGFPEASLSNIWKWADSLAMGALILQACGQEGR SQ TRVGYLLAAMMTQKDMVIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLAGLLGGEGVGLRLLAFRKLAERRNRR SQ SFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLTAEWCGEVEWNPDLVNEGGEVNLKVRQDAM SQ GNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAVWTLFEMLGSGRRSELVFSGQETRTERNRPFEIKDGAYRIYS SQ PGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVDEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQE SQ THQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPEIPLSVQGTGWM SQ SKGQITVLDMHPGSGKTHRVLPELVRQCADRGMRTLVLAPTRVVLKEMERALAGKKVRFHSPAVEGQTTAGAIVDVMCHA SQ TYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGE SQ WREGFDWITEYEGRTAWFVPSISKGGAVARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVI SQ DGRTNIKPEEVDGKVELTGTRKVTTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVAT SQ FYGPEQVKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEENAIDGADGDLVRFKTPGG SQ SERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAP SQ EAFLTIVEVAVLGVATLGILWCFVARASVSRMFLGTVVLFAALFLLWIGGVDYGHMAGIALIFYTLLTVLQPEPGKQRSS SQ DDNRLAYFLLGLFSLAGLVTANEMGMLDKTKADLAGLVWRGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQL SQ QTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPMSLGLGVALAAFHLAIVASGLEAELTQRAHRV SQ FFSAMVKNPMVDGDVINPFPDGETKPALYERRMSLILAIALCMGSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTM SQ PMACGMAGLVRGSFWGLLPMGHRLWLRTTGTRRGGAEGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDKARELLKRG SQ ETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFR SQ TGMDVYSLEAHRADTILCDIGESSPDPLAEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGL SQ VRVPFSRNSTHEMYFSTAISGNIINSVNTQSRKLLARFGDQRGPTKVPEVDLGTGTRCVVLAEDKVREADVAERIAALKT SQ QYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEP SQ QVGTKIIMRAVNDWIFERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWPNAREAVEDPEFWRLVDEERERHLGGR SQ CAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGTSLNYLGWHLKKLSELE SQ GGLFYADDTAGWDTRITNADLEDEEQILRYLEGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVV SQ TYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEHGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAK SQ VRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSY SQ FHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMGDKGKVREWRDIPYLPKSQDGL SQ CSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII // 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 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 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 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 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 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 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 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 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 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 F1M391; PN Stimulator of interferon genes protein; GN Sting1; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, 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}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; 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: F1M391; DR PDB: 5GRM; DR PDB: 5GS5; 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:26669264). 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 (By similarity). 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:26669264). 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 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 (By similarity). 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:26669264). 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) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:26669264}. DE Reference Proteome: Yes; 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 MPYSNLHPSIPRPRSYRFKLAAFVLLVGSLMSLWMTGEPPSHTLHYLALHVASQQLGLLLKKLCCLAEELCHVQSRYQGS SQ YWKAVRACVGSPICFMALILLSFYFYCSLENTSDLRLAWHLGILVLSKSLSMTLDLQSLAPAEVSAVCEEKNFNVAHGLA SQ WSYYIGYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAY SQ SNSVYELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLEEILADVPESRNHCRLIVYQESEEG SQ NSFSLSQEVLRHIRQEEKEEVTMSGPPTSVAPRPSLLSQEPRLLISGMEQPLPLRTDLI // 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 F1N3B8; PN 2'-5'-oligoadenylate synthase 2; GN OAS2; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. DR UNIPROT: F1N3B8; DR UNIPROT: Q53AV7; DR Pfam: PF01909; DR Pfam: PF10421; DR PROSITE: PS00833; DR PROSITE: PS50152; DE Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. 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. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000250|UniProtKB:P29728}. DE Reference Proteome: Yes; 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 MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVF SQ FGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLW SQ SYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCG SQ AEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNW SQ LRSLRQNESPGPSWNVLPASLYITPGHLLDKFVKDFLQPNQTFQDQIKKALKIICSFLEENCFRHSTTKIQVIQGGSTVK SQ GTALKTGSDASLVVFANSLKSYTSPKNERYNIIKEIHEQLEACRQEKDFEVKFEISKWKPPWVLSFTLKSKVLNESVDFD SQ VLPAFNALGELKSGSTPSPRTYTELIHLYKPSDVFLEGEFSACFTKLQRNFVRSLPLKLKDLIRLLKHWYCGCEKKLKQK SQ GSLPPKYALELLSIYAWEKGSGAQDFDMAEGFRTVLELVIQYQHLCVFWTVNYSFDDEILRNFLLGQIRRTRPVILDPAD SQ PTGDVGGGHRWCWHLLAKEATEWLSSLCFKDKSGCPIQPWNVPKKRVQTPGSCGAGIYSMVNEMHLLRSHRFLD // 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 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 F1QNV4; PN Nuclear pore complex protein Nup133; GN nup133; OS 7955; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}. DR UNIPROT: F1QNV4; DR UNIPROT: Q7SZE9; DR Pfam: PF03177; DR Pfam: PF08801; DE Function: Involved in poly(A)+ RNA transport (By similarity). Involved in nephrogenesis (PubMed:30427554). {ECO:0000250|UniProtKB:Q8WUM0, ECO:0000269|PubMed:30427554}. DE Reference Proteome: Yes; GO GO:0000777; 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 MFSPRGTPGSGRRQAPRTGGRRSVSAVQPGLLFSPRRSAVTARSTPTRVQSHAVVESYNFDVQTFGSSLPVKVMEALTMA SQ DVDDQISVKVEASGWAWMVCGERLIVWKVSQTSVAKLSVCKDLQLPSSEFAYSADLVSISSSGPLDLAPIQSISVLAVSP SQ DGLVRFWPSLAHEGSYTEISLDLSGHLSNYVAAVKGGSFIVSSYRGHLLRLSADSSGKLHHRPVQQGQGMLSGIGRRVSS SQ LFGIRGQPADLSVFSVLWVKASSCLYSLSSCGLSKWEVDENSETQVLSWSTNQIITDSITDAIWDSESNYSEIKKGVNVL SQ YLDMQPSNAGLVVLAAAWYPGDTPCVAYFCLVTLAESIVPSPDLLTVEVTKYNPPFQSEEELLKTRLVLPDPSSPAAYLY SQ NEELVFACSTGAGRGGLAEEKILFSSPGDRVRGGGVCADLPVFFSQNSGLVAVLARETASLLPETMEDSLCTSVAGPGPE SQ GTPLETPPKIDMVAQEDKTKLLKQAFLQFCRHDLVGAQSMVDELFPSDGEGSADLDTVVTQIDLDLVDDYPACDPRWAES SQ VPDEGAGFTLTSLILLHQLEDKMKAHRCLMDFLLQTGLLDRLTSTKVRSCPMATRLLLCEHAEKLSAAIVLKNHHAKHPE SQ LVNTAIQTALKKNSTDTPTNLTPADVFFREVSQISSIFECLLDEEEKALKEHPDAARWGEVVLSVNDIIKDMLQAAAQYR SQ ETKASLYRAPENCSPEPEYIPWTASGGVGGVRSVISRQHELILRAAYPHADAELRSVLCEQLVALLDSLLSGYVAQLTSL SQ RRGGQQERYDTLENEYTQKRSELLKPLLELGQHQWVAALAEKYCDFDILVQLCERTDNQSRLQQYMVKFADQNFADFLFR SQ WYMEKGKRGKLLSQPMATHQQLASFLQAHDHLSWLHDIHVQDYQRAHRTLYNQANMETRYFSKKKTLLALSKLTALASDM SQ PEPVHRRQLNDIVEQERFLLHQETLPKQLLEEKQLNPDSMPLLSPQNLISLYICDENRGANEYDFKKALDLLEYFEEENG SQ IDVDALKREIFSKALKKDWKESWSSSDDNDDPLEAARDSTFVKILQKLIQERVSLQTYLPDIKDLLQEDELESLKSKPYF SQ EFLLRANYEHYLKVQI // 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 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 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 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 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 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 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 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 F4I8I0; PN SUN domain-containing protein 4; GN SUN4; 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: F4I8I0; DR UNIPROT: Q0WQI7; DR UNIPROT: Q9C9H3; 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:0043621; GO GO:0006997; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MQRSRRALLVRRRVSETTSNGRNRFYKVSLSLVFLIWGLVFLSTLWISHVDGDKGRSLVDSVEKGEPDDERADETAESVD SQ ATSLESTSVHSNPGLSSDVDIAAAGESKGSETILKQLEVDNTIVIVGNVTESKDNVPMKQSEINNNTVPGNDTETTGSKL SQ DQLSRAVPLGLDEFKSRASNSRDKSLSGQVTGVIHRMEPGGKEYNYAAASKGAKVLSSNKEAKGASSIICRDKDKYLRNP SQ CSTEGKFVVIELSEETLVNTIKIANFEHYSSNLKDFEILGTLVYPTDTWVHLGNFTALNMKHEQNFTFADPKWVRYLKLN SQ LLSHYGSEFYCTLSLLEVYGVDAVERMLEDLISIQDKNILKLQEGDTEQKEKKTMQAKESFESDEDKSKQKEKEQEASPE SQ NAVVKDEVSLEKRKLPDPVEEIKHQPGSRMPGDTVLKILMQKIRSLDVSLSVLESYLEERSLKYGMIFKEMDLEASKREK SQ EVETMRLEVEGMKEREENTKKEAMEMRKWRMRVETELEKAENEKEKVKERLEQVLERLEWMEKKGVVVFTICVGFGTIAV SQ VAVVFGMGIVRAEKQGGLAWLLLLISSTFVMFILSL // 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 F4ID16; PN Nuclear pore complex protein NUP98B; GN NUP98B; OS 3702; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. DR UNIPROT: F4ID16; DR UNIPROT: Q9LQ50; DR Pfam: PF04096; DR PROSITE: PS51434; DE Function: DE Reference Proteome: Yes; GO GO:0005635; GO GO:0044614; GO GO:0008139; GO GO:0003723; GO GO:0017056; GO GO:0071456; GO GO:0051028; GO GO:0000973; GO GO:0006606; GO GO:0006405; GO GO:0034398; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MFGSSNNNPFGQSSISSPFGTQTHSLFGQTNNNASNNPFATKPFGTSTPFGAQTGSSMFGGTSTGVFGAPQTSSPFGASP SQ QAFGSSTQAFGASSTPSFGSSNSPFGGTSTFGQKSFGLSTPQSSPFGSTTQQSQPAFGNSTFGSSTPFGASTTPAFGASS SQ TPAFGVSNTSGFGATNTPGFGATNTTGFGGSSTPGFGASSTPAFGSTNTPAFGASSTPLFGSSSSPAFGASPAPAFGSSG SQ NAFGNNTFSSGGAFGSSSTPTFGASNTSAFGASSSPSFNFGSSPAFGQSTSAFGSSSFGSTQSSLGSTPSPFGAQGAQAS SQ TSTFGGQSTIGGQQGGSRVIPYAPTTDTASGTESKSERLQSISAMPAHKGKNMEELRWEDYQRGDKGGQRSTGQSPEGAG SQ FGVTNSQPSIFSTSPAFSQTPVNPTNPFSQTTPTSNTNFSPSFSQPTTPSFGQPTTPSFRSTVSNTTSVFGSSSSLTTNT SQ SQPLGSSIFGSTPAHGSTPGFSIGGFNNSQSSPLFGSNPSFAQNTTPAFSQTSPLFGQNTTPALGQSSSVFGQNTNPALV SQ QSNTFSTPSTGFGNTFSSSSSLTTSISPFGQITPAVTPFQSAQPTQPLGAFGFNNFGQTQIANTTDIAGAMGTFSQGNFK SQ QQPALGNSAVMQPTPVTNPFGTLPALPQISIAQGGNSPSIQYGISSMPVVDKPAPVRVSPLLTSRHLLQRRVRLPTRKYR SQ PSDDGPKVPFFSDEEENSSTPKADAFFIPRENPRALFIRPVERVKSEHPKDSPTPLQENGKRSNGVTNGANHETKDNGAI SQ REAPPVKVNQKQNGTHENHGGDKNGSHSSPSGADIESLMPKLHHSEYFTEPRIQELAAKERVEQGYCKRVKDFVVGRHGY SQ GSIKFLGETDVCRLDLEMVVQFKNREVNVYMDESKKPPVGQGLNKPAVVTLLNIKCMDKKTGTQVMEGERLDKYKEMLKR SQ KAGEQGAQFVSYDPVNGEWTFKVEHFSSYKLGDEYDV // 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 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 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 F4IZR5; PN Protein EXPORTIN 1B; GN XPO1B; OS 3702; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9TVM2}. Nucleus membrane {ECO:0000250|UniProtKB:Q9TVM2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TVM2}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9TVM2}. DR UNIPROT: F4IZR5; DR UNIPROT: Q0WV73; DR UNIPROT: Q94IV0; DR UNIPROT: Q94KD5; DR UNIPROT: Q9M9N0; 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). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (By similarity). Required for the maternal-to-embryonic transition and during gametophyte development (PubMed:18791220). {ECO:0000250|UniProtKB:Q9SMV6, ECO:0000269|PubMed:18791220}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0031965; GO GO:0005643; GO GO:0005634; GO GO:0009506; GO GO:0005049; GO GO:0008536; GO GO:0009553; GO GO:0051028; GO GO:0009555; GO GO:0009846; GO GO:0009860; GO GO:0046825; GO GO:0000055; GO GO:0000056; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9TVM2}; SQ MAAEKLRDLSQPIDVVLLDATVEAFYSTGSKEERASADNILRDLKANPDTWLQVVHILQNTSSTHTKFFALQVLEGVIKY SQ RWNALPVEQRDGMKNYISDVIVQLSRDEASFRTERLYVNKLNIILVQIVKQEWPAKWKSFIPDLVIAAKTSETICENCMA SQ ILKLLSEEVFDFSKGEMTQQKIKELKQSLNSEFQLIHELCLYVLSASQRQELIRATLSALHAYLSWIPLGYIFESPLLEI SQ LLKFFPVPAYRNLTLQCLSEVASLNFGDFYDMQYVKMYSIFMNQLQAILPLNLNIPEAYSTGSSEEQAFIQNLALFFTSF SQ FKLHIKILESAPENISLLLAGLGYLISISYVDDTEVFKVCLDYWNSLVLELFGTRHHACHPALTPSLFGLQMAFLPSTVD SQ GVKSEVTERQKLYSDPMSKLRGLMISRTAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHEDTEKQM SQ LSKLSKQLSGEEWAWNNLNTLCWAIGSISGSMVVEQENRFLVMVIRDLLSLCEVVKGKDNKAVIASNIMYVVGQYSRFLR SQ AHWKFLKTVVHKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGESEPFVSELLSGLATIVGDLQPHQIHTFYES SQ VGSMIQAESDPQKRGEYLQRLMALPNQKWAEIIGQARQSADILKEPDVIRTVLNILQTNTRVATSLGTFFLSQISLIFLD SQ MLNVYRMYSELVSSSIANGGPYASRTSLVKLLRSVKREILKLIETFLDKAENQPHIGKQFVPPMMDQVLGDYARNVPDAR SQ ESEVLSLFATIINKYKVVMRDEVPLIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFRALIQLSSEQLKLVMD SQ SVIWAFRHTERNIAETGLNLLLEMLKNFQKSDFCNKFYQTYFLQIEQEVFAVLTDTFHKPGFKLHVLVLQHLFSLVESGS SQ LAEPLWDAATVPHPYSNNVAFVLEYTTKLLSSSFPNMTTTEVTQFVNGLYESRNDVGRFKDNIRDFLIQSKEFSAQDNKD SQ LYAEEAAAQMERERQRMLSIPGLIAPSEIQDDMADS // 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 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 F4KF65; PN Importin subunit alpha-9; GN IMPA9; OS 3702; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}. DR UNIPROT: F4KF65; DR UNIPROT: Q9LYX8; DR Pfam: PF00514; DE Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}. DE Reference Proteome: Yes; DE Interaction: Q9M7Q7; IntAct: EBI-1810458,EBI-2131591; Score: 0.40 GO GO:0005829; GO GO:0005643; GO GO:0005654; GO GO:0061608; GO GO:0008139; GO GO:0006607; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MADDGSASNRRDPIKSSVGNVAGQRRRKQAVTVAKERRELLVRAKRLCRVGTNGDVEDALVENEMMVDEEQPILEAQASK SQ SVEELKSAVQYQGKGAMQKRVTALRELRRLLSKSEFPPVEAALRAGAIPLLVQCLSFGSPDEQLLESAWCLTNIAAGKPE SQ ETKALLPALPLLIAHLGEKSSAPVAEQCAWAIGNVAGEGEDLRNVLLSQGALPPLARMIFPDKGSTVRTAAWALSNLIKG SQ PESKAAAQLVKIDGILDAILRHLKKTDEETATEIAWIIVYLSALSDIATSMLLKGGILQLLIDRLATSSSLQLLIPVLRS SQ LGNFVAVDPKAVLTILIREQNTEESIIGVLAKCLRSEHRVLKKEAAWVLSNIAAGSIEHKRMIHSTEVMPLLLRILSTSP SQ FDIRKEVAYVLGNLCVESAEGDRKPRIIQEHLVSIVSGGCLRGFIELVRSPDIEAARLGLQFIELVLRGMPNGEGPKLVE SQ GEDGIDAMERFQFHENEELRVMANSLVDKYFGEDYGIDE // 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 F5H982; PN Nuclear egress protein 1; GN NEC1; OS 868565; 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, ECO:0000269|PubMed:23365436}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}. DR UNIPROT: F5H982; 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, ECO:0000269|PubMed:23365436}. 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 MPKSVSSHISLATSTGRSGPRDIRRCLSSRLRSVPPGARSASVSSKHRNGLRKFISDKVFFSILSHRHELGVDFLREMET SQ PICTSKTVMLPLDLSTVAPGRCVSLSPFGHSSNMGFQCALCPSTENPTVAQGSRPQTMVGDALKKNNELCSVALAFYHHA SQ DKVIQHKTFYLSLLSHSMDVVRQSFLQPGLLYANLVLKTFGHDPLPIFTTNNGMLTMCILFKTRALHLGETALRLLMDNL SQ PNYKISADCCRQSYVVKFVPTHPDTASIAVQVHTICEAVAALDCTDEMRDDIQKGTALVNAL // ID F5HA27; PN Nuclear egress protein 2; GN NEC2; OS 868565; 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:23365436, ECO:0000269|PubMed:23623980}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:23365436, ECO:0000269|PubMed:23623980}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}. DR UNIPROT: F5HA27; 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:23365436, ECO:0000269|PubMed:23623980}. 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 MSVVGKRVVDELCRVVSSYLGQSGQSLDLERCIDGAPVYAKGGATAICTVRMQHGCVYHLEFVYKFWAHLLEEMHYPFSP SQ CFVISNNGLSTTLKCFLCRPSDAVSQFGHVLPVESDVYLAKNTSVVLGQDDFTKFKASLVFSKNLGVYNSMVICRTYFTD SQ YRQVLQFLVVTPKSHKRLKSLLETVYCLAAPVADSAAQGGAGFPTNGRDARACTSDVTAVYWAGQGGRTVRILGAFQWSL SQ GRAVALVRRSWPWISAGIAFLCLGLVWMRPS // ID F5HDD0; PN Envelope glycoprotein M; GN gM; OS 868565; 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:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. 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, ECO:0000269|PubMed:12771417}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}. DR UNIPROT: F5HDD0; 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:12771417}. DE Reference Proteome: Yes; GO GO:0044175; GO GO:0044178; 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 MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVY SQ IFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCI SQ HFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDA SQ IFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIV SQ IRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI // 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 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 F6WXT2; PN Nucleoporin NUP188 homolog; GN nup188; OS 8364; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000305}. DR UNIPROT: F6WXT2; DR UNIPROT: A9JRJ6; DR Pfam: PF10487; DE Function: May function as a component of the nuclear pore complex (NPC). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0044611; GO GO:0017056; GO GO:0051028; GO GO:0006606; GO GO:0006405; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAAAGCLYRRTSRELWTILLGRSSMKDGHQIKAELDRYGDRLLQGLAYYRPPSTSSTGKVKANKNLSPALQELGLRLSKF SQ LGLDEEQSVELLQTYLLYDYRGTQESVKGVPQDERQSQALMLKASMVDYYYEERISLLRCVLYILNYFQDDKHPYSAEFS SQ KCVEMMEQKELFGKYLKQFESLCREEAPTWETHGNFMTERQVSRWFVQRLREQAMLLEIIFLYFACFAASPSDLLALTKL SQ FKEQGFGCRLQNRHLVEPSMDPLVERIGYFSVLIFLEALDIETLMTCSLSDKTEQHPFSSEEQVCKEMDSVLVTLGDAPH SQ HGPVLLAWALLRFALNADKVTPTVRKMGSTAIQLHIFQYLTRMLQSLRSGENNCTTSTACLCVYTFLTFVLTNLEEQVLQ SQ SQQDLVDTAFQVFAAPNLPDLFWNMEPTAGLGILLDSVVGMFPFHLSPLLKLFTALVSKSSAKKVYSFLDRMSSYTEHYR SQ HKPHDILSHEDETLWKRQTPKVLYALGLGQTNLRIPQGTIGQVMADEHGFLVRWEYSYSCWTLFTCEIEMLLHVVSTADV SQ IHQCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVMNPPMDFLSSCVDCLAALATRMPAKVWIDLRHTGF SQ LPFAANPVSGHIISTEGMNAGGYGSLFGIEQSQGEYSITLSFLRLVTTLVKGQLGSTQSQGLVPCILFVLREMLPNYHRW SQ RYNSHGVREQLGFQILSLIHAILNLSPEEEESTSTPNLQSLCIFSLTNTEAGQAVINIMGVGVDTLNAVMLTQAGSSGTE SQ GQGQMLMQTIKLAFSITNNVIRLKPLSSAISPLEHALTQHGAHGNNLIAVLAKYIYHKYDPSLPRLAIQLLKRLAMVAPM SQ SVYACLGSDAAAIRDAFLSRLRDNIEDMQIKIMILEFLTVAVETQPGLIELFLNLEVKDTNEGSKEYSLGEWSCLQVVLK SQ LIDSQDPESSWGAPLLHRSAIAFLHALWQDRRDSAMTVLRTKPNFWENLTSPLFGTLAFPSESSELSILETCAFIMKIIC SQ LEIYYAVRGSLGDSLKKILKKFSEEERFTYWSNYVHSLVCQVAESEGACNSLTEYQQLLSAWRMFLMVATHNADVMHLTN SQ PEVRQKLFKDVLGGTQALLLVPRSMTCLHLGSMLCTVMIILLRRWKSDLAAPEDILSSLTQILEGVLQKDQQLVEKTKAR SQ VFAALISALEIKPMKASEIPQYPQLVLNVCETLQEEVVFLVDHTRQEVPANDASEDKDSMETEDTGRIRQKDQRDGVCVL SQ GLHLAKGLCEADEEGDQWQQVLRKLPVLPMLFSALEVSLRIKQNLHFCEAILHFLFTLAKTHQGAAAMAGAGVTQTVCLP SQ LLSVYQLSSNGASTAQPALSLRKSLDAPSWPGVYRLTVSLMERLLKTLRYNFLTEALDFVGVHQERILQCLGAVRTVPSL SQ ACLEEADHTVGFLLQLSNFTKEWHFHLPQLIKDVQVNLCYLCQACTSLLHSRKMLQHYLQIKNGETMSSTATPRGQRTPQ SQ TPSKQPTAESEALELRQLRSVQHSLLKILGKTLATLRAFTPDLCQILQPLDLAQYNLLFALSFTTPAFDADVTPSFGTLL SQ ATVNVTLSMLGEMDKKKDHPLGQVLGETNSTVDNKNIKSLLLFIMENCFYLLISQAVRYLRDPSVHPRDKQRMKQELSSE SQ LSTLLSSLSRYFRRGGPSSPAGGLMPSPQPKGASAAKVVPEAQEPLIQLVQAFVRHVQR // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 G0SEA3; PN Nucleoporin GLE2; GN GLE2; 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:P40066}. Nucleus membrane {ECO:0000250|UniProtKB:P40066}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40066}; Cytoplasmic side {ECO:0000250|UniProtKB:P40066}. Nucleus membrane {ECO:0000250|UniProtKB:P40066}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40066}; Nucleoplasmic side {ECO:0000250|UniProtKB:P40066}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P40066}. DR UNIPROT: G0SEA3; DR UNIPROT: G0ZGV3; 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:0000250|UniProtKB:P40066}. DE Reference Proteome: Yes; GO GO:0005829; GO GO:0031965; GO GO:0034399; GO GO:0005643; GO GO:0016973; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40066}; SQ MAGLFGTTTSTTTSTLGDLKNDVELGSPPEDSITDLSFNPNPNDPKDFLAVSSWDKKVRVYEIAANGQNQGKVQMEHEGP SQ VFAVDFFKDGTKVISAGADKQAKVLDLASGQAMQVAAHDAPIRCVKYFEAGGTPMAVTGSWDKTIKYWDFRSATPAGTVQ SQ CQERVYTMDVKENLLVIGTADRYIDVINLKEPVKFYKTLQSPLKWQTRVVSCFTDSQGFAIGSIEGRCAIQYVEDKDQSM SQ NFSFKCHRDTPQNNVTNVHAVNAISFHPQHGTFSTAGSDGTFHFWDKDAKHRLKGYPNVGGSITATKFNRNGTIFAYAIS SQ YDWSKGYQGNTANYPTKVMLHPVLGDECKPRPSVKKR // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 K9N7C7; PN 2'-O-methyltransferase; GN rep; OS 1263720; 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: K9N7C7; DR PDB: 4WUR; DR PDB: 5HOL; DR PDB: 5KO3; 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]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:26311885}. [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, ECO:0000269|PubMed:25142582}. [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:0071108; GO GO:0070536; GO GO:0039503; GO GO:0039579; GO GO:0039644; GO GO:0039653; GO GO:0039604; GO GO:0039502; GO GO:0006351; GO GO:0019082; GO GO:0039694; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHT SQ RHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHY SQ ERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEG SQ FITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG SQ KESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKH SQ SVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQT SQ QHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYV SQ VLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFM SQ STIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKV SQ SWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQL SQ EQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYN SQ IHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFS SQ LHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIA SQ QVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVIT SQ ECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNIL SQ HVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSL SQ TFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPL SQ GYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLL SQ HWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGAD SQ ISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMT SQ LDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDV SQ VLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHY SQ VHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTY SQ SPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKG SQ KPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVS SQ FVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFAT SQ RTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVD SQ LSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRAN SQ SFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQ SQ TSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGK SQ RTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQP SQ FYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIA SQ TKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQIT SQ NESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSK SQ LRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGII SQ RDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCY SQ TPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRIT SQ RTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAF SQ LTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIV SQ PIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKY SQ FSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLD SQ NTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGA SQ AFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQV SQ HQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLY SQ TGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFP SQ LLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLV SQ IVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFP SQ EVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIK SQ VAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDI SQ FDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMY SQ KQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAG SQ ALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEP SQ VQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGS SQ NTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEH SQ PDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLKRVRGSIVNARIEPCS SQ SGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDF SQ FIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERV SQ RQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFN SQ KPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVV SQ SCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDF SQ VVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSA SQ GHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAAT SQ RGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQV SQ LSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFV SQ DKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKD SQ GDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDS SQ YSVMLCGDNSAKFWEEAFYRDLYSSPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVC SQ NAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPL SQ KLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVS SQ YKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSH SQ FAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADI SQ LVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVS SQ TVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTT SQ QTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQSQIVTGLFKDCS SQ RETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVE SQ GAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSD SQ TLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGN SQ LATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDI SQ GNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDG SQ GSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYM SQ EAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQGLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTT SQ LPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKF SQ MSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEK SQ DFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAV SQ CSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQASADWKPGHAMPSLFKVQNVNLERC SQ ELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVS SQ DADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMG SQ KFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKES SQ QINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR // 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 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 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 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 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 O02173; PN Probable trafficking protein particle complex subunit 2; GN sedl; OS 6239; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. DR UNIPROT: O02173; DR Pfam: PF04628; DE Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. Required for the systemic spread of the RNAi response. {ECO:0000269|PubMed:16862146}. DE Reference Proteome: Yes; DE Interaction: Q9NA81; IntAct: EBI-367817,EBI-367809; Score: 0.62 DE Interaction: P34605; IntAct: EBI-312149,EBI-367809; Score: 0.37 GO GO:0005783; GO GO:0005794; GO GO:0048471; GO GO:0006888; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MATKEFYFAIIGHCDQPIFEMDFPVGEKKTKESEGTRHLNHYIGHAALDIVDEHALTTSQMYLKMVDKFNEWYVSAFVTA SQ SRIRFIMLHTHRADEGIKQFFQEMYETYIKHAMNPFYEIDDVIESPAFEQKATLYGRKYLS // 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 O02824; PN Alpha-1A adrenergic receptor; GN ADRA1A; OS 9986; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}. DR UNIPROT: O02824; DR Pfam: PF00001; DR PROSITE: PS00237; DR PROSITE: PS50262; 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 (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005901; GO GO:0005737; GO GO:0016021; GO GO:0031965; GO GO:0005634; GO GO:0005886; GO GO:0004937; GO GO:0046982; GO GO:0007512; GO GO:0061049; GO GO:0010507; GO GO:0001985; GO GO:0150099; GO GO:0001994; GO GO:0007200; GO GO:0097195; GO GO:0010613; GO GO:0001996; GO GO:0043410; GO GO:1903997; GO GO:0045987; GO GO:0001997; GO GO:0055117; GO GO:0019229; TP Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250}; SQ MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL SQ PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVG SQ PLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN SQ APAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSC SQ INPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFF SQ SSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV // 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 O08684; PN Phospholipase D1; GN PLD1; OS 10029; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. DR UNIPROT: O08684; DR Pfam: PF00169; DR Pfam: PF00614; DR Pfam: PF13091; DR Pfam: PF00787; 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: No; GO GO:0005789; GO GO:0000139; GO GO:0031902; GO GO:0048471; GO GO:0070290; GO GO:0035091; GO GO:0004630; GO GO:0048017; GO GO:0016042; GO GO:0006654; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MSLKSEHRVNTSALQKIAADMSNLIDNLDTRELHFEGEEVEFDTSPGDPKAQEKYIPFSSIYNTQGFKEPNIQTYLSGCP SQ IKAQVLEVERFTSTTRVPSINLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREM SQ PSLPRSSENTIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGLNC SQ CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWG SQ GAIEEFIQKHGSDFLKDHRFGSYAAVHENMLAKWYVNAKGYFEDIANAMEEAAEEIFITDWWLSPEIFLKRPVVEGNRWR SQ LDCILKRKAQQGVRIFIMLYKEVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGI SQ DLAYGRWDDNEHRLTDVGSVKRVTSGLSMGSLAAATMESMESLSLKDNHRSHKNEPILKSVDDVDPKLKGVGKPRKFSKF SQ SLYRQLHRRHLHNSDSVSSIDSASNTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRIPW SQ HDIGSVLHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQSTAHELRYQVPGAVPAKVQLLRSAADWSAGIKHH SQ EESIHSAYINVIENSKHYIYIENQFFISCADDKVVFNKVGDAIAQRILKAHREGQRYRVYIVIPRLPGFEGDISTGGGNA SQ LQAIMHFNYRTMCRGENSILGQLKPELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRS SQ MLGKRDSEMAVIVQDTETVPSIMDGKEYQAGCFAQGLRLQCFRLVLGYLSDPSEDLQDPVSDKFFKEIWVSTAARNATIY SQ DKVFRCLPNDEVHNLMQLRDFISKPILAKDDPIRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT // 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 O09114; PN Prostaglandin-H2 D-isomerase; GN Ptgds; OS 10090; 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: O09114; DR UNIPROT: O09157; DR UNIPROT: O35091; DR UNIPROT: Q3V2G5; DR UNIPROT: Q62169; DR PDB: 2CZT; DR PDB: 2CZU; DR PDB: 2E4J; DR PDB: 2KTD; DR PDB: 2RQ0; DR Pfam: PF00061; DR PROSITE: PS00213; 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. {ECO:0000269|PubMed:10781097, ECO:0000269|PubMed:11751991, ECO:0000269|PubMed:12077186, ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210, ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}. DE Reference Proteome: Yes; GO GO:0005576; GO GO:0005615; GO GO:0005794; GO GO:0031965; GO GO:0048471; GO GO:0005791; GO GO:0005504; GO GO:0004667; GO GO:0005501; GO GO:2000255; GO GO:0001516; GO GO:0045187; GO GO:0051384; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLT SQ STFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELK SQ EKFTTFSKAQGLTEEDIVFLPQPDKCIQE // 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 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 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 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 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 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 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 O13864; PN Importin subunit beta-1; GN kap95; OS 284812; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}. DR UNIPROT: O13864; 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 clasical nuclear localization signal (cNLS) in cargo substrates. 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. At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo. 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. {ECO:0000250|UniProtKB:Q06142}. DE Reference Proteome: Yes; GO GO:0005737; 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:0008536; GO GO:0051028; GO GO:0006606; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLW SQ QSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICES SQ VSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGC SQ LVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAA SQ DILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVA SQ MLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCH SQ FAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQI SQ LDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPS SQ FVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQ SQ TYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSES SQ LTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA // 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 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 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 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 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 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 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 O14199; PN UDP-N-acetylglucosamine transferase subunit alg14; GN alg14; OS 284812; 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: O14199; 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:0005783; GO GO:0030176; GO GO:0031965; GO GO:0043541; GO GO:0006488; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNTYVLTAIAVLASLIILLVGRNAIKSSKKKPFQKHLLVFFGSGGHTGEMLNLLNALDDKLYSVRSYVAGSDDTMSVSKA SQ SLLSNSLPSVKSKIFKVPRARYVKQSWLTTPFTAFWSLLGSISVIFWNPFGIPDVILCNGPGTCVFICLLGYLAKFLGKN SQ VKIVYVESFARVKSLSLSGKILMPFVDRFLVQWPDLATKYKRAEYIGIVA // 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 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 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 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 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 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 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 O15027; PN Protein transport protein Sec16A; GN SEC16A; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:29300766}; Peripheral membrane protein {ECO:0000269|PubMed:17005010}. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9QAT4}. Cytoplasm, cytosol {ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384}. Microsome membrane {ECO:0000269|PubMed:17428803}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (PubMed:17192411). 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, PubMed:28442536, PubMed:19638414, PubMed:17428803, PubMed:22355596). Recruited to microsomal membrane in SAR1-dependent manner (PubMed:17428803). {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}. DR UNIPROT: O15027; DR UNIPROT: A1YCA4; DR UNIPROT: J3KNL6; DR UNIPROT: Q4G0D7; DR UNIPROT: Q5SXP0; DR UNIPROT: Q5SXP1; DR UNIPROT: Q8N347; DR UNIPROT: Q96HP1; DR Pfam: PF12932; DR Pfam: PF12931; DR OMIM: 612854; DR DisGeNET: 9919; 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:17192411, PubMed:17005010, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter- enriched vesicles delivery to the cell membrane in adipocytes (By similarity). {ECO:0000250|UniProtKB:E9QAT4, ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:29300766}. DE Reference Proteome: Yes; DE Interaction: O14976; IntAct: EBI-357515,EBI-714707; Score: 0.35 DE Interaction: Q5S007; IntAct: EBI-5323863,EBI-357515; Score: 0.65 DE Interaction: P08559; IntAct: EBI-715747,EBI-357515; Score: 0.35 DE Interaction: O14880; IntAct: EBI-724754,EBI-357515; Score: 0.35 DE Interaction: P25786; IntAct: EBI-359352,EBI-357515; Score: 0.46 DE Interaction: Q9HBL7; IntAct: EBI-714824,EBI-357515; Score: 0.35 DE Interaction: P62491; IntAct: EBI-745098,EBI-357515; Score: 0.35 DE Interaction: Q96I36; IntAct: EBI-6570698,EBI-357515; Score: 0.35 DE Interaction: Q9NWT8; IntAct: EBI-448665,EBI-357515; Score: 0.35 DE Interaction: Q6ZNJ1; IntAct: EBI-2862306,EBI-357515; Score: 0.64 DE Interaction: Q96N67; IntAct: EBI-357515,EBI-2433703; Score: 0.50 DE Interaction: Q08AM6; IntAct: EBI-2107455,EBI-357515; Score: 0.35 DE Interaction: Q12824; IntAct: EBI-358419,EBI-357515; Score: 0.46 DE Interaction: Q9Y2H1; IntAct: EBI-991501,EBI-357515; Score: 0.46 DE Interaction: Q9UPY3; IntAct: EBI-395506,EBI-357515; Score: 0.35 DE Interaction: Q9H4B6; IntAct: EBI-1017775,EBI-357515; Score: 0.60 DE Interaction: O15084; IntAct: EBI-359567,EBI-357515; Score: 0.35 DE Interaction: O95835; IntAct: EBI-444209,EBI-357515; Score: 0.35 DE Interaction: Q7TSJ6; IntAct: EBI-6305003,EBI-357515; Score: 0.35 DE Interaction: Q9H6Z9; IntAct: EBI-1175354,EBI-357515; Score: 0.35 DE Interaction: P57078; IntAct: EBI-4422308,EBI-357515; Score: 0.35 DE Interaction: Q9UBN7; IntAct: EBI-301697,EBI-357515; Score: 0.35 DE Interaction: Q9BY41; IntAct: EBI-6598095,EBI-357515; Score: 0.35 DE Interaction: Q96DB2; IntAct: EBI-301713,EBI-357515; Score: 0.35 DE Interaction: P29353; IntAct: EBI-78835,EBI-357515; Score: 0.35 DE Interaction: P01375; IntAct: EBI-359977,EBI-357515; Score: 0.40 DE Interaction: E9QKK1; IntAct: EBI-10967445,EBI-357515; Score: 0.35 DE Interaction: P60710; IntAct: EBI-353957,EBI-357515; Score: 0.35 DE Interaction: Q92614; IntAct: EBI-949059,EBI-357515; Score: 0.35 DE Interaction: Q91X51; IntAct: EBI-2553222,EBI-357515; Score: 0.35 DE Interaction: Q8VDD5; IntAct: EBI-400906,EBI-357515; Score: 0.35 DE Interaction: Q9WTI7; IntAct: EBI-777558,EBI-357515; Score: 0.35 DE Interaction: Q8CAF4; IntAct: EBI-11096298,EBI-357515; Score: 0.35 DE Interaction: P35579; IntAct: EBI-350338,EBI-357515; Score: 0.35 DE Interaction: Q9Z1Z0; IntAct: EBI-7597484,EBI-357515; Score: 0.35 DE Interaction: Q8N3V7; IntAct: EBI-352936,EBI-357515; Score: 0.35 DE Interaction: Q6ZRV2; IntAct: EBI-2556538,EBI-357515; Score: 0.35 DE Interaction: Q6PJG2; IntAct: EBI-2795569,EBI-357515; Score: 0.35 DE Interaction: P24941; IntAct: EBI-375096,EBI-357515; Score: 0.35 DE Interaction: Q96QS3; IntAct: EBI-11107474,EBI-357515; Score: 0.35 DE Interaction: P47755; IntAct: EBI-762451,EBI-357515; Score: 0.35 DE Interaction: Q15691; IntAct: EBI-1004115,EBI-357515; Score: 0.35 DE Interaction: P51617; IntAct: EBI-358664,EBI-357515; Score: 0.35 DE Interaction: Q92731; IntAct: EBI-78505,EBI-357515; Score: 0.35 DE Interaction: P03372; IntAct: EBI-78473,EBI-357515; Score: 0.35 DE Interaction: Q9DBR0; IntAct: EBI-4285802,EBI-357515; Score: 0.35 DE Interaction: Q9D7I8; IntAct: EBI-11048238,EBI-357515; Score: 0.35 DE Interaction: Q9Z2X1; IntAct: EBI-4283704,EBI-357515; Score: 0.35 DE Interaction: Q9UHB6; IntAct: EBI-351479,EBI-357515; Score: 0.35 DE Interaction: G3X972; IntAct: EBI-11079353,EBI-357515; Score: 0.35 DE Interaction: Q16643; IntAct: EBI-351394,EBI-357515; Score: 0.35 DE Interaction: P09497; IntAct: EBI-726598,EBI-357515; Score: 0.35 DE Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-357515; Score: 0.35 DE Interaction: Q13492; IntAct: EBI-2803688,EBI-357515; Score: 0.35 DE Interaction: Q00610; IntAct: EBI-354967,EBI-357515; Score: 0.35 DE Interaction: P50548; IntAct: EBI-357515,EBI-8465203; Score: 0.35 DE Interaction: P61978-2; IntAct: EBI-357515,EBI-7060731; Score: 0.35 DE Interaction: E9PC66; IntAct: EBI-357515,EBI-11042988; Score: 0.35 DE Interaction: Q9NX05; IntAct: EBI-357515,EBI-1210530; Score: 0.35 DE Interaction: P31942; IntAct: EBI-357515,EBI-711437; Score: 0.35 DE Interaction: P52272-2; IntAct: EBI-357515,EBI-11033003; Score: 0.35 DE Interaction: P48729; IntAct: EBI-357515,EBI-1383726; Score: 0.53 DE Interaction: Q8N0X7; IntAct: EBI-357515,EBI-2643803; Score: 0.35 DE Interaction: Q9ULX6; IntAct: EBI-357515,EBI-357530; Score: 0.35 DE Interaction: Q92540-2; IntAct: EBI-357515,EBI-11083612; Score: 0.35 DE Interaction: O95817; IntAct: EBI-357515,EBI-747185; Score: 0.35 DE Interaction: O95782-2; IntAct: EBI-357515,EBI-10965313; Score: 0.35 DE Interaction: P27708; IntAct: EBI-357515,EBI-355504; Score: 0.35 DE Interaction: P13861; IntAct: EBI-357515,EBI-2556122; Score: 0.35 DE Interaction: Q9BWF3; IntAct: EBI-357515,EBI-2856454; Score: 0.35 DE Interaction: P53675; IntAct: EBI-357515,EBI-358826; Score: 0.35 DE Interaction: Q15437; IntAct: EBI-357515,EBI-742673; Score: 0.35 DE Interaction: Q96I24; IntAct: EBI-357515,EBI-954200; Score: 0.35 DE Interaction: Q8TD26; IntAct: EBI-357515,EBI-1043681; Score: 0.35 DE Interaction: Q8N684-2; IntAct: EBI-357515,EBI-5280595; Score: 0.35 DE Interaction: Q32P28; IntAct: EBI-357515,EBI-396328; Score: 0.35 DE Interaction: P18206-2; IntAct: EBI-357515,EBI-11027067; Score: 0.35 DE Interaction: Q1KMD3; IntAct: EBI-357515,EBI-1059150; Score: 0.35 DE Interaction: Q14677-3; IntAct: EBI-357515,EBI-10983245; Score: 0.35 DE Interaction: Q9HAU0-4; IntAct: EBI-357515,EBI-10981101; Score: 0.35 DE Interaction: Q08379; IntAct: EBI-357515,EBI-618309; Score: 0.53 DE Interaction: Q9NZB2; IntAct: EBI-357515,EBI-1171960; Score: 0.35 DE Interaction: P15924; IntAct: EBI-357515,EBI-355041; Score: 0.35 DE Interaction: Q5JSZ5; IntAct: EBI-357515,EBI-744891; Score: 0.35 DE Interaction: Q9UHV9; IntAct: EBI-357515,EBI-359873; Score: 0.35 DE Interaction: Q00610-2; IntAct: EBI-357515,EBI-10963396; Score: 0.35 DE Interaction: O95487-2; IntAct: EBI-357515,EBI-11045289; Score: 0.35 DE Interaction: P09651-2; IntAct: EBI-357515,EBI-352677; Score: 0.35 DE Interaction: P05783; IntAct: EBI-357515,EBI-297888; Score: 0.35 DE Interaction: F5H365; IntAct: EBI-357515,EBI-11081771; Score: 0.35 DE Interaction: Q14134-2; IntAct: EBI-357515,EBI-10963880; Score: 0.35 DE Interaction: P42694; IntAct: EBI-357515,EBI-1210654; Score: 0.35 DE Interaction: O15460-2; IntAct: EBI-357515,EBI-10182841; Score: 0.35 DE Interaction: O95486; IntAct: EBI-357515,EBI-749911; Score: 0.35 DE Interaction: Q6UN15; IntAct: EBI-357515,EBI-1021914; Score: 0.35 DE Interaction: Q8N163; IntAct: EBI-357515,EBI-355410; Score: 0.35 DE Interaction: P09496-2; IntAct: EBI-357515,EBI-4401010; Score: 0.35 DE Interaction: Q8WUF5; IntAct: EBI-357515,EBI-5550163; Score: 0.35 DE Interaction: C9JE98; IntAct: EBI-357515,EBI-11041567; Score: 0.35 DE Interaction: P55735; IntAct: EBI-357515,EBI-1046596; Score: 0.35 DE Interaction: Q99959-2; IntAct: EBI-357515,EBI-10987518; Score: 0.35 DE Interaction: Q8IWZ3-6; IntAct: EBI-357515,EBI-10971452; Score: 0.35 DE Interaction: Q96MX6; IntAct: EBI-357515,EBI-2434101; Score: 0.35 DE Interaction: Q9UHF7; IntAct: EBI-357515,EBI-2556151; Score: 0.35 DE Interaction: Q9NRA8; IntAct: EBI-357515,EBI-301024; Score: 0.35 DE Interaction: Q9NWS0; IntAct: EBI-357515,EBI-357318; Score: 0.35 DE Interaction: Q14244; IntAct: EBI-357515,EBI-2211064; Score: 0.35 DE Interaction: Q86UY5; IntAct: EBI-357515,EBI-1384254; Score: 0.35 DE Interaction: Q14498; IntAct: EBI-357515,EBI-395290; Score: 0.35 DE Interaction: P12268; IntAct: EBI-357515,EBI-353389; Score: 0.35 DE Interaction: P53992; IntAct: EBI-357515,EBI-81134; Score: 0.35 DE Interaction: Q13470-2; IntAct: EBI-357515,EBI-11018037; Score: 0.35 DE Interaction: Q63ZY3-3; IntAct: EBI-357515,EBI-11026136; Score: 0.35 DE Interaction: O15379; IntAct: EBI-357515,EBI-607682; Score: 0.35 DE Interaction: Q9Y2F9-2; IntAct: EBI-357515,EBI-10989708; Score: 0.35 DE Interaction: Q5T0W9; IntAct: EBI-357515,EBI-2556565; Score: 0.35 DE Interaction: Q5T5P2; IntAct: EBI-357515,EBI-746898; Score: 0.35 DE Interaction: Q9Y446; IntAct: EBI-357515,EBI-2880227; Score: 0.35 DE Interaction: Q14671-2; IntAct: EBI-357515,EBI-11071389; Score: 0.35 DE Interaction: H0YH87; IntAct: EBI-357515,EBI-11035685; Score: 0.35 DE Interaction: P09497-2; IntAct: EBI-357515,EBI-10965328; Score: 0.35 DE Interaction: O00443; IntAct: EBI-357515,EBI-641094; Score: 0.35 DE Interaction: Q96PK6; IntAct: EBI-357515,EBI-954272; Score: 0.35 DE Interaction: Q9NSY1; IntAct: EBI-357515,EBI-1383367; Score: 0.35 DE Interaction: Q14203; IntAct: EBI-357515,EBI-724352; Score: 0.35 DE Interaction: P20839; IntAct: EBI-357515,EBI-2866691; Score: 0.35 DE Interaction: Q9C0J8; IntAct: EBI-357515,EBI-712637; Score: 0.35 DE Interaction: Q9H4H8; IntAct: EBI-357515,EBI-2556127; Score: 0.35 DE Interaction: O60763; IntAct: EBI-357515,EBI-356164; Score: 0.35 DE Interaction: P04003; IntAct: EBI-357515,EBI-978348; Score: 0.35 DE Interaction: Q9ERG0; IntAct: EBI-2693855,EBI-357515; Score: 0.35 DE Interaction: Q8K389; IntAct: EBI-11068840,EBI-357515; Score: 0.35 DE Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-357515; Score: 0.35 DE Interaction: Q96H55; IntAct: EBI-10983249,EBI-357515; Score: 0.35 DE Interaction: P62140; IntAct: EBI-352350,EBI-357515; Score: 0.35 DE Interaction: P46940; IntAct: EBI-297509,EBI-357515; Score: 0.35 DE Interaction: Q14134; IntAct: EBI-702370,EBI-357515; Score: 0.35 DE Interaction: P31323; IntAct: EBI-2930670,EBI-357515; Score: 0.35 DE Interaction: Q15075; IntAct: EBI-298113,EBI-357515; Score: 0.35 DE Interaction: P15311; IntAct: EBI-1056902,EBI-357515; Score: 0.35 DE Interaction: P22087; IntAct: EBI-358318,EBI-357515; Score: 0.35 DE Interaction: P49841; IntAct: EBI-373586,EBI-357515; Score: 0.46 DE Interaction: P02545; IntAct: EBI-351935,EBI-357515; Score: 0.35 DE Interaction: P20339; IntAct: EBI-399437,EBI-357515; Score: 0.35 DE Interaction: Q71U36; IntAct: EBI-302552,EBI-357515; Score: 0.35 DE Interaction: P23258; IntAct: EBI-302589,EBI-357515; Score: 0.35 DE Interaction: O43493; IntAct: EBI-1752146,EBI-357515; Score: 0.46 DE Interaction: O95831; IntAct: EBI-356440,EBI-357515; Score: 0.46 DE Interaction: Q9NS69; IntAct: EBI-1047508,EBI-357515; Score: 0.35 DE Interaction: Q96GD4; IntAct: EBI-624291,EBI-357515; Score: 0.46 DE Interaction: O15155; IntAct: EBI-749204,EBI-357515; Score: 0.46 DE Interaction: P50613; IntAct: EBI-1245958,EBI-357515; Score: 0.35 DE Interaction: P49336; IntAct: EBI-394377,EBI-357515; Score: 0.35 DE Interaction: P51151; IntAct: EBI-4401353,EBI-357515; Score: 0.35 DE Interaction: O75880; IntAct: EBI-6656171,EBI-357515; Score: 0.35 DE Interaction: P27824; IntAct: EBI-355947,EBI-357515; Score: 0.35 DE Interaction: P19367; IntAct: EBI-713162,EBI-357515; Score: 0.35 DE Interaction: Q9BVA0; IntAct: EBI-11147603,EBI-357515; Score: 0.35 DE Interaction: Q15051; IntAct: EBI-2805823,EBI-357515; Score: 0.35 DE Interaction: Q86VP6; IntAct: EBI-456077,EBI-357515; Score: 0.35 DE Interaction: Q13618; IntAct: EBI-456129,EBI-357515; Score: 0.35 DE Interaction: P49674; IntAct: EBI-749343,EBI-357515; Score: 0.35 DE Interaction: P11279; IntAct: EBI-2805407,EBI-357515; Score: 0.35 DE Interaction: Q9UQM7; IntAct: EBI-1383687,EBI-357515; Score: 0.35 DE Interaction: P28482; IntAct: EBI-959949,EBI-357515; Score: 0.35 DE Interaction: Q7Z5H3-2; IntAct: EBI-12084490,EBI-357515; Score: 0.35 DE Interaction: Q8N4T4-1; IntAct: EBI-25408274,EBI-357515; Score: 0.35 DE Interaction: P0DTC5; IntAct: EBI-25475853,EBI-357515; Score: 0.35 DE Interaction: P0DTC7; IntAct: EBI-25475903,EBI-357515; Score: 0.35 DE Interaction: P0DTC8; IntAct: EBI-25475900,EBI-357515; Score: 0.35 DE Interaction: A0A663DJA2; IntAct: EBI-25475906,EBI-357515; Score: 0.35 DE Interaction: Q8IZD9; IntAct: EBI-1752361,EBI-357515; Score: 0.35 DE Interaction: P55735-1; IntAct: EBI-357515,EBI-10045850; Score: 0.35 DE Interaction: Q9NZN9; IntAct: EBI-6557414,EBI-357515; Score: 0.51 DE Interaction: Q9NQH7; IntAct: EBI-1171467,EBI-357515; Score: 0.51 DE Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-357515; Score: 0.35 DE Interaction: Q9HC77; IntAct: EBI-946194,EBI-357515; Score: 0.35 DE Interaction: Q9BY84; IntAct: EBI-3443956,EBI-357515; Score: 0.35 DE Interaction: O14829; IntAct: EBI-2931238,EBI-357515; Score: 0.35 DE Interaction: C5E526; IntAct: EBI-12577179,EBI-357515; Score: 0.35 DE Interaction: C5E527; IntAct: EBI-12585275,EBI-357515; Score: 0.35 DE Interaction: Q1K9H5; IntAct: EBI-6050669,EBI-357515; Score: 0.35 DE Interaction: B4URF7; IntAct: EBI-6050648,EBI-357515; Score: 0.35 DE Interaction: P03428; IntAct: EBI-2547475,EBI-357515; Score: 0.35 DE Interaction: I6T1Z2; IntAct: EBI-12561553,EBI-357515; Score: 0.35 DE Interaction: Q5EP37; IntAct: EBI-12577201,EBI-357515; Score: 0.35 DE Interaction: P03431; IntAct: EBI-2547514,EBI-357515; Score: 0.35 DE Interaction: Q99759; IntAct: EBI-357515,EBI-307281; Score: 0.40 DE Interaction: D3DR86; IntAct: EBI-357515,EBI-307345; Score: 0.40 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; GO GO:0021762; TP Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305}; SQ MQPPPQTVPSGMAGPPPAGNPRSVFWASSPYRRRANNNAAVAPTTCPLQPVTDPFAFSRQALQSTPLGSSSKSSPPVLQG SQ PAPAGFSQHPGLLVPHTHARDSSQGPCEPLPGPLTQPRAHASPFSGALTPSAPPGPEMNRSAEVGPSSEPEVQTLPYLPH SQ YIPGVDPETSHGGHPHGNMPGLDRPLSRQNPHDGVVTPAASPSLPQPGLQMPGQWGPVQGGPQPSGQHRSPCPEGPVPSG SQ VPCATSVPHFPTPSILHQGPGHEQHSPLVAPPAALPSDGRDEVSHLQSGSHLANNSDPESTFRQNPRIVNHWASPELRQN SQ PGVKNEHRPASALVNPLARGDSPENRTHHPLGAGAGSGCAPLEADSGASGALAMFFQGGETENEENLSSEKAGLSGQADF SQ DDFCSSPGLGRPPAPTHVGAGSLCQALLPGPSNEAAGDVWGDTASTGVPDASGSQYENVENLEFVQNQEVLPSEPLNLDP SQ SSPSDQFRYGPLPGPAVPRHGAVCHTGAPDATLHTVHPDSVSSSYSSRSHGRLSGSARPQELVGTFIQQEVGKPEDEASG SQ SFFKQIDSSPVGGETDETTVSQNYRGSVSQPSTPSPPKPTGIFQTSANSSFEPVKSHLVGVKPFEADRANVVGEVRETCV SQ RQKQCRPAAALPDASPGNLEQPPDNMETLCAPQVCPLPLNSTTEAVHMLPHAGAPPLDTVYPAPEKRPSARTQGPVKCES SQ PATTLWAQSELPDFGGNVLLAPAAPALYVCAKPQPPVVQPPEEAMSGQQSRNPSSAAPVQSRGGIGASENLENPPKMGEE SQ EALQSQASSGYASLLSSPPTESLQNPPVLIAQPDHSYNLAQPINFSVSLSNSHEKNQSWREALVGDRPAVSSWALGGDSG SQ ENTSLSGIPTSSVLSLSLPSSVAQSNFPQGSGASEMVSNQPANLLVQPPSQPVPENLVPESQKDRKAGSALPGFANSPAG SQ STSVVLVPPAHGTLVPDGNKANHSSHQEDTYGALDFTLSRTLENPVNVYNPSHSDSLASQQSVASHPRQSGPGAPNLDRF SQ YQQVTKDAQGQPGLERAQQELVPPQQQASPPQLPKAMFSELSNPESLPAQGQAQNSAQSPASLVLVDAGQQLPPRPPQSS SQ SVSLVSSGSGQAAVPSEQPWPQPVPALAPGPPPQDLAAYYYYRPLYDAYQPQYSLPYPPEPGAASLYYQDVYSLYEPRYR SQ PYDGAASAYAQNYRYPEPERPSSRASHSSERPPPRQGYPEGYYSSKSGWSSQSDYYASYYSSQYDYGDPGHWDRYHYSAR SQ VRDPRTYDRRYWCDAEYDAYRREHSAFGDRPEKRDNNWRYDPRFTGSFDDDPDPHRDPYGEEVDRRSVHSEHSARSLHSA SQ HSLASRRSSLSSHSHQSQIYRSHNVAAGSYEAPLPPGSFHGDFAYGTYRSNFSSGPGFPEYGYPADTVWPAMEQVSSRPT SQ SPEKFSVPHVCARFGPGGQLIKVIPNLPSEGQPALVEVHSMEALLQHTSEQEEMRAFPGPLAKDDTHKVDVINFAQNKAM SQ KCLQNENLIDKESASLLWNFIVLLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNEAVEQVEEEESGEAQL SQ SFLTGGPAAAASSLERETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRFANSLPINDPLQTVYQ SQ LMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASRGLLDAAHFCYLMAQAGFGVYTKKTTKL SQ VLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAETCPLPSFQVFKFIYSCRLAEMGLATQAFHYCEAIAKSILTQPHLY SQ SPVLISQLVQMASQLRLFDPQLKEKPEEESLAAPTWLVHLQQVERQIKEGAGVWHQDGALPQQCPGTPSSEMEQLDRPGL SQ SQPGALGIANPLLAVPAPSPEHSSPSVRLLPSAPQTLPDGPLASPARVPMFPVPLPPGPLEPGPGCVTPGPALGFLEPSG SQ PGLPPGVPPLQERRHLLQEARSPDPGIVPQEAPVGNSLSELSEENFDGKFANLTPSRTVPDSEAPPGWDRADSGPTQPPL SQ SLSPAPETKRPGQAAKKETKEPKKGESWFFRWLPGKKKTEAYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSM SQ PKTVQAAPPALPGPPGAPVNMYSRRAAGTRARYVDVLNPSGTQRSEPALAPADFVAPLAPLPIPSNLFVPTPDAEEPQLP SQ DGTGREGPAAARGLANPEPAPEPKVLSSAASLPGSELPSSRPEGSQGGELSRCSSMSSLSREVSQHFNQAPGDLPAAGGP SQ PSGAMPFYNPAQLAQACATSGSSRLGRIGQRKHLVLN // 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 O15182; PN Centrin-3; GN CETN3; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9256449}. Nucleus, nucleolus {ECO:0000303|PubMed:22307388}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic cells (PubMed:9256449). Localizes to centriole distal lumen (PubMed:26337392). Localization at the nuclear pore complex requires NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}. DR UNIPROT: O15182; DR UNIPROT: Q53YD2; DR UNIPROT: Q9BS23; DR Pfam: PF13499; DR PROSITE: PS00018; DR PROSITE: PS50222; DR OMIM: 602907; DR DisGeNET: 1070; DE Function: Plays a fundamental role in microtubule-organizing center structure and function. 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: Q92844; IntAct: EBI-356349,EBI-712959; Score: 0.35 DE Interaction: Q2NKQ1-4; IntAct: EBI-10182463,EBI-712959; Score: 0.72 DE Interaction: Q8NA72; IntAct: EBI-712959,EBI-2561090; Score: 0.80 DE Interaction: P04792; IntAct: EBI-352682,EBI-712959; Score: 0.37 DE Interaction: Q9H0K1; IntAct: EBI-712959,EBI-1181664; Score: 0.27 DE Interaction: Q70CQ1; IntAct: EBI-2511022,EBI-712959; Score: 0.40 DE Interaction: Q9R1K9; IntAct: EBI-2553037,EBI-712959; Score: 0.40 DE Interaction: Q9Y4C4; IntAct: EBI-2864441,EBI-712959; Score: 0.44 DE Interaction: Q5S007; IntAct: EBI-5323863,EBI-712959; Score: 0.44 DE Interaction: O14874; IntAct: EBI-1046765,EBI-712959; Score: 0.35 DE Interaction: O95976; IntAct: EBI-2802079,EBI-712959; Score: 0.35 DE Interaction: Q01831; IntAct: EBI-372610,EBI-712959; Score: 0.35 DE Interaction: Q8NA72-3; IntAct: EBI-11751537,EBI-712959; Score: 0.77 DE Interaction: P18509; IntAct: EBI-8588930,EBI-712959; Score: 0.35 DE Interaction: Q5VW00; IntAct: EBI-3951747,EBI-712959; Score: 0.35 DE Interaction: O15273; IntAct: EBI-954089,EBI-712959; Score: 0.40 DE Interaction: Q15293; IntAct: EBI-948278,EBI-712959; Score: 0.56 DE Interaction: Q9Y6K9; IntAct: EBI-712959,EBI-81279; Score: 0.44 DE Interaction: Q9UQ80; IntAct: EBI-924893,EBI-712959; Score: 0.40 DE Interaction: O43679; IntAct: EBI-2865580,EBI-712959; Score: 0.56 DE Interaction: O00141; IntAct: EBI-1042854,EBI-712959; Score: 0.56 DE Interaction: O95994; IntAct: EBI-712648,EBI-712959; Score: 0.56 DE Interaction: P19237; IntAct: EBI-746692,EBI-712959; Score: 0.56 DE Interaction: P17540; IntAct: EBI-712973,EBI-712959; Score: 0.56 DE Interaction: Q96EV8-2; IntAct: EBI-16749183,EBI-712959; Score: 0.35 DE Interaction: Q8N490-2; IntAct: EBI-10769878,EBI-712959; Score: 0.35 DE Interaction: Q12798; IntAct: EBI-2512818,EBI-712959; Score: 0.35 DE Interaction: O00212; IntAct: EBI-3918631,EBI-712959; Score: 0.35 DE Interaction: O43924; IntAct: EBI-712685,EBI-712959; Score: 0.37 DE Interaction: Q5UIP0; IntAct: EBI-711331,EBI-712959; Score: 0.37 DE Interaction: Q13432; IntAct: EBI-711260,EBI-712959; Score: 0.37 GO GO:0005814; GO GO:0005813; GO GO:0005737; GO GO:0005815; GO GO:0044615; GO GO:0005730; GO GO:0070390; GO GO:0005509; GO GO:0008017; GO GO:0051301; GO GO:0007098; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGK SQ ITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFI SQ AIMTGDI // 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 O17213; PN Protein rogdi homolog; GN H14A12; OS 6239; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250}. DR UNIPROT: O17213; DR Pfam: PF10259; DE Function: DE Reference Proteome: Yes; GO GO:0005623; GO GO:0005635; GO GO:0005634; GO GO:0043291; GO GO:0032502; GO GO:0007035; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEVQSLTITTNYPPKPASPNPQDIRDTIRSNKTNENLWIQRKDVDTTLRSALEHLKACCIVLNLSAKCDERLNVAVSHGT SQ TEKYQLMSRTGSSDNLKAAVTLLDDNVIQAEVTVKYPKAGGGYYRAVAQPDVQWKLQQLQDLGNHISRVTITLCDLQHEV SQ NLLKGDGERDAFTLATGARILEELKLTMNEISLARNSIMLPRKRSLLELCYFPPTRKFVPPLPQDQLISFYISCCRLVCA SQ SYQMVPKTVHPQGLSVFMAESQLPHLDDVIKHLNTVMAILQKLINYLSATMS // ID O17482; PN Protein timeless; GN tim; OS 7244; 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 per is required for nuclear localization (By similarity). {ECO:0000250}. DR UNIPROT: O17482; DR UNIPROT: O44430; DR UNIPROT: O44785; 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 (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 MDWLLATPQLQSVFSSLGSLVGGTYVVSPNALAILEEINHKLTYEDQTLRTFRRAIGFGQNVRVDLIPLLENAKDDAVLE SQ SVIRILVNLTVPVECLFSVDLMYRTEVGRHTIFELNKLLYNSKEAFTDPKSTKSVVEYMKHILESDPKLSPHKCDQINNC SQ LLLLRNILHIPETHAHFLMPRLQPGSGHQVSMQNTILWNLFIQSIDKLLLYLMTCPQRSLWGVTMVQLIALIYKDQHVST SQ LQKLLNLWFEASLSESSDDNESNTTPPKQASGDSSPMLTSDPTSDSSDNGSGGKKESCEERRQALREGTDATLHEVSRKG SQ HEYQNAMASSNAANYILEGPCSAQQPWSDCEMQEYKQMTAVISEPLNLSQPADNVNYTTNANYARTTSTDILTKTTSLKH SQ EGFKPPAPRRNTLSAILSDNYAPLSFISAVKLGQKSPHAGQLQLIKGKCCPQKRECPSSQSEHSDCGYGTQMENPESIST SQ SSNDDDGPQGKPQHQKPPCSSKHRSKQRIFAVPQDTKDLRRKKLVKRSKSSLINMKGLVLHTPNDDDISNLLKEFTVDFL SQ LKGYNYLVEELHSQLLSNAKMPIDTSHFFWLVTFFLKFAAQLELDMEHIDTILTFDVLSFLTYEGVSLCEQLELNARQEG SQ ADLRPYLRRMHLVVTAIREFLQAIEAYNKVTHLSEDDRYRLRQLQLQISATTDLRCLFVLLLRRFNPSIHSKQYLQDLVV SQ TNHILLLILDNAAKLEGGQTIGLSEHISQFATLEVMHYYGILLEDFSNNGEYVNDCIFTMMHHIGGDLDQVGVLYQPIIL SQ KAYSRIWEADYDICDDWSDLIEYVIHKFLNTPPKSPMAIPTASLTELTKEQNQEHTACPWSQEDMDSLCWYFVQSKRQND SQ VIGNIAKLFSNNGNKIKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLATPTSLTTDSGIELKESAYGKPSDDVQ SQ VLLDLIRKENKSQHLVWLQKLLLECCYVKMMIKCGSCQTDVEPIMEPVVYHCMFKQKPIPVVQWNNEQSSTMLYQPFMLL SQ LHKLGIQLPADAGLIFARIPDFWTPETMYGLAKKLGPLDKLTLKFDPRDLEDAPPSRHHTGARNSLSSISSLEADFGDSE SQ GLALIPEVDPAVEKAAAAASAIPNNEIFALPRVKHCNSIIRYTPDPTPPVPSWLQLVMRTKCSKRRSPATDASDCTSTST SQ MIADDEIKSYASMAQASHTKLNSGYPTSTLVCMNKLSNCSFAAPPNENSSSSGCGGTASSMSMPNMPDGNSDALMKTSFE SQ RLAVTGARYLRPSNTDQDYSALVASVYENEFANSDNVSVASDLTRMYVSDEDEKHELQLQQVE // 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 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 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 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 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 O23523; PN RGG repeats nuclear RNA binding protein A; GN RGGA; OS 3702; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:25783413}. Nucleus {ECO:0000250|UniProtKB:Q9SQ56, ECO:0000255|PROSITE-ProRule:PRU00768}. DR UNIPROT: O23523; DR UNIPROT: A8MQG3; DR UNIPROT: A8MQJ5; DR Pfam: PF04774; DR Pfam: PF09598; DE Function: Binds RNA. Regulates responses to abscisic acid (ABA). Promotes stomata closure in drought conditions. Involved in resistance to salt and drought stresses via the accumulation of Pro. {ECO:0000269|PubMed:25783413}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005829; GO GO:0005634; GO GO:0048471; GO GO:0003729; GO GO:0009738; GO GO:0071470; GO GO:0071472; GO GO:0009787; GO GO:0009737; GO GO:0006970; GO GO:0009651; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLPPAQAVREARSDAPRGGGGRGGFNRGRG SQ GYNRDDGNNGYSGGYTKPSGEGDVSKSSYERRGGGGAPRGSFRGEGGGPGGGRRGGFSNEGGDGERPRRAFERRSGTGRG SQ SDFKRDGSGRGNWGTPGEEIAAETEAVAGVETEKDVGEKPAVDDVAADANKEDTVVEEKEPEDKEMTLDEYEKILEEKKK SQ ALQSLTTSERKVDTKVFESMQQLSNKKSNDEIFIKLGSDKDKRKDDKEEKAKKAVSINEFLKPAEGGNYYRGGRGGRGRG SQ GRGRGGVSSGESGGYRNEAAPAIGDAAQFPSLGGK // 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 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 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 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 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 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 O35744; PN Chitinase-like protein 3; GN Chil3; OS 10090; SL Nucleus Position: SL-0178; SL Comments: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages. DR UNIPROT: O35744; DR UNIPROT: P70201; DR UNIPROT: Q3U462; DR UNIPROT: Q3UV87; DR UNIPROT: Q61201; DR PDB: 1E9L; DR PDB: 1VF8; DR Pfam: PF00704; DR PROSITE: PS51910; DE Function: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0031410; GO GO:0005576; GO GO:0005635; GO GO:0048237; GO GO:0004563; GO GO:0030246; GO GO:0008061; GO GO:0102148; GO GO:0006032; GO GO:0006954; GO GO:0000272; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEAL SQ NGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVK SQ EMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSAD SQ LNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDA SQ PQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY // 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 O36388; PN Envelope glycoprotein M; GN gM; OS 654901; 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: O36388; 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 MKSSKKDIFILHIWLKLMGCYVFMFITSVVLPIAAMFPNLGFPCYYNTLVDYSKLNLREKNQAQHLTPTLFLEAPEMFFY SQ VTYSFIVDCCSLVYYALAAVAVVKAKKHAPGLMALSQWIMAVGSPTLLYMAVLKLWTIQLYIHTLSYKHIYLAAFVYCLH SQ WLLSMVYTECYITNVSSQWTSSELKKTIPENILLYRVVHVLKPIMMNVHLSVVALETLIFCLSFMMAIGNSFYVMVSDIV SQ FGAINLYLILPIIWYFVTEFWLSKYLPRQFGFYFGVLVASIILILPVVRYDKIFVAAQIHRAVSINIAMIPLCALVALLV SQ RACRVYTDRKKIAYTALPSKPQTIKYTKPIEPSTKQAPDSSIFLEEESDTDFEQ // ID O36417; PN Nuclear egress protein 2; GN NEC2; OS 654901; 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: O36417; 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 MASGKKLIDQLCSVVSSFLCPSISSLDIDRCAVGPHIFSRGSSQAICTVKLLHGEVYNLEFVYRYWAHILEKYNFPFSPT SQ FIICNNGLAVTLKCYVSEPRDLSSRYGQATSMALDVNLQRNSFVVLSQDDFIKFKTPLVFAKDLDITNSMVVCRTYLTSS SQ RNSLQFLVVKSKNPRRLENVLDMIKRAVEATGSNLPATREKPLPLEQTEQLESTLPSSGHLRVLQSTSLTGRCPSWGAAC SQ ALLLLSLAVGLMAILAAKLMQWP // ID O36420; PN Nuclear egress protein 1; GN NEC1; OS 654901; 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: O36420; 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 MHKIQKMSCTPSVRSRYTLKRKRLNSAKSATLKKKKVFLSNSEFFAGVSTNYELGKDFLREMDTPICTSNTVFLPVKFSD SQ VAPGRCLTLSPYGHSSVLGFHCQECKPDSSSGFTQAQQSAESNELLSVNLCFLNNVEKVVQHKAFYLSLLGHSMNTVKQS SQ LGQPSLLYCYTVLKKFYPQIFPIFTANGPMLTMYIIFTSLTLHVSEAVLRILTDNVENHNLSADCYKGHYILSIEPQALE SQ ESNLNVCVTKICDLVAQLDFSDELKQEYVNGSTLIANFLN // 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 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 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 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 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 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 O43709; PN Probable 18S rRNA (guanine-N(7))-methyltransferase; GN BUD23; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Cytoplasm {ECO:0000269|PubMed:24488492}. Note=Localized diffusely throughout the nucleus and the cytoplasm (PubMed:24488492). Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). Localization is not affected by glucocorticoid treatment (PubMed:24488492). {ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}. DR UNIPROT: O43709; DR UNIPROT: A8K501; DR UNIPROT: C9K060; DR UNIPROT: Q96P12; DR UNIPROT: Q9BQ58; DR UNIPROT: Q9HBP9; DR PDB: 6G4W; DR Pfam: PF08241; DR Pfam: PF12589; DR OMIM: 194050; DR OMIM: 615733; DR DisGeNET: 114049; DE Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity (PubMed:25851604). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity (PubMed:25851604). Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (PubMed:24086612). Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors (PubMed:24488492). Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements (PubMed:24488492). Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}. DE Disease: Note=BUD23 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 BUD23 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000305|PubMed:11978965}. DE Reference Proteome: Yes; DE Interaction: P01100; IntAct: EBI-852851,EBI-1044726; Score: 0.40 DE Interaction: Q6ZWV7; IntAct: EBI-2554199,EBI-1044726; Score: 0.35 DE Interaction: P06748; IntAct: EBI-78579,EBI-1044726; Score: 0.35 DE Interaction: Q9UI30; IntAct: EBI-1044726,EBI-373326; Score: 0.67 DE Interaction: Q9C0C9; IntAct: EBI-1044726,EBI-2339946; Score: 0.35 DE Interaction: Q8IUE6; IntAct: EBI-1044726,EBI-1642157; Score: 0.35 DE Interaction: Q13618; IntAct: EBI-456129,EBI-1044726; Score: 0.35 DE Interaction: P00973; IntAct: EBI-3932815,EBI-1044726; Score: 0.37 DE Interaction: Q16512; IntAct: EBI-602382,EBI-1044726; Score: 0.37 DE Interaction: P55072; IntAct: EBI-1044726,EBI-355164; Score: 0.37 DE Interaction: Q5NHY6; IntAct: EBI-1044726,EBI-2796153; Score: 0.37 DE Interaction: Q9Y478; IntAct: EBI-1044726,EBI-719769; Score: 0.40 GO GO:0005730; GO GO:0005654; GO GO:0048471; GO GO:0008168; GO GO:0046982; GO GO:0003723; GO GO:0016435; GO GO:0006325; GO GO:2000234; GO GO:0070476; GO GO:0031167; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVG SQ LDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAV SQ LQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMS SQ RRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF // 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 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 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 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 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 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 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 O55047; PN Serine/threonine-protein kinase tousled-like 2; GN Tlk2; OS 10090; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000269|PubMed:10455159}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. 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: O55047; DR UNIPROT: B1ASU7; DR UNIPROT: B1ASU8; DR UNIPROT: Q9D5Y5; DR Pfam: PF00069; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00108; 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 (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250}. Testis-specific isoforms may play a role in spermatogenesis. Highly expressed in embryos throughout development. {ECO:0000269|PubMed:10092119}. DE Reference Proteome: Yes; DE Interaction: P83510; IntAct: EBI-7280013,EBI-16733969; Score: 0.35 GO GO:0005882; GO GO:0005634; GO GO:0048471; GO GO:0005524; GO GO:0004674; GO GO:0007049; GO GO:0030154; GO GO:0006974; GO GO:0071480; GO GO:0006325; GO GO:0007059; GO GO:0035556; GO GO:0007275; GO GO:0032435; GO GO:0018105; GO GO:0006468; GO GO:0001672; GO GO:0007283; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPR SQ GHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTE SQ HSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKK SQ LLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQ SQ APPATNEQKQRKSKTNGAENETLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKD SQ HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS SQ LDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDF SQ GLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQEN SQ TILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN // 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 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 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 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 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 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 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 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 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 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 O60175; PN Protein OPI10 homolog; GN SPBC21H7; OS 284812; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. DR UNIPROT: O60175; DR Pfam: PF05603; DE Function: DE Reference Proteome: Yes; GO GO:0005829; GO GO:0005635; GO GO:0005634; GO GO:0061608; GO GO:0006606; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MFGAICAGRLVQTNLQQVADNQFVFQLDSAESLNHIVVFLLPNSPFPVGMGAKVYFQWPGKPFQFLGYLTNEKPSAIFRL SQ KNTIQTLSENENCVGITAMLGISVEPLTNFTETPAVSTSASNVIAKPLPPVTSVAQKILTNLYNFLASFATSQLPPNSIG SQ LGDLRPNDTFIPLRVFQDWHAKFLNKLSNNPNFLDSEDQI // 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 O60271; PN C-Jun-amino-terminal kinase-interacting protein 4; GN SPAG9; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q58A65}. Lysosome membrane {ECO:0000269|PubMed:29146937}. Note=Perinuclear distribution in response to stress signals such as UV radiation. {ECO:0000250|UniProtKB:Q58A65}. [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15693750}. Note=Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix. {ECO:0000269|PubMed:15693750}. DR UNIPROT: O60271; DR UNIPROT: A6H8U5; DR UNIPROT: A8MSX0; DR UNIPROT: B4DHH2; DR UNIPROT: O60905; DR UNIPROT: Q3KQU8; DR UNIPROT: Q3MKM7; DR UNIPROT: Q86WC7; DR UNIPROT: Q86WC8; DR UNIPROT: Q8IZX7; DR UNIPROT: Q96II0; DR UNIPROT: Q9H811; DR PDB: 2W83; DR Pfam: PF16471; DR Pfam: PF09744; DR PROSITE: PS51776; DR PROSITE: PS51777; DR OMIM: 605430; DR DisGeNET: 9043; 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 (PubMed:14743216). Isoform 5 may play a role in spermatozoa-egg- interaction (PubMed:15693750). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). {ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15693750, ECO:0000269|PubMed:29146937}. DE Reference Proteome: Yes; DE Interaction: P53350; IntAct: EBI-476768,EBI-1023301; Score: 0.64 DE Interaction: Q07832; IntAct: EBI-2552999,EBI-1023301; Score: 0.40 DE Interaction: P23771; IntAct: EBI-6664760,EBI-1023301; Score: 0.35 DE Interaction: A3KN83; IntAct: EBI-2855422,EBI-1023301; Score: 0.27 DE Interaction: Q9UQ88; IntAct: EBI-1023301,EBI-373024; Score: 0.27 DE Interaction: Q9UKN8; IntAct: EBI-1023301,EBI-1237240; Score: 0.27 DE Interaction: Q9UBC2; IntAct: EBI-1023301,EBI-2556746; Score: 0.27 DE Interaction: Q8WUA4; IntAct: EBI-1023301,EBI-1237062; Score: 0.27 DE Interaction: P11274; IntAct: EBI-1023301,EBI-712838; Score: 0.27 DE Interaction: Q00613; IntAct: EBI-719620,EBI-1023301; Score: 0.27 DE Interaction: Q06945; IntAct: EBI-6672525,EBI-1023301; Score: 0.27 DE Interaction: Q12955; IntAct: EBI-2691178,EBI-1023301; Score: 0.27 DE Interaction: Q14566; IntAct: EBI-374900,EBI-1023301; Score: 0.27 DE Interaction: Q14C86; IntAct: EBI-1049788,EBI-1023301; Score: 0.27 DE Interaction: Q14683; IntAct: EBI-80690,EBI-1023301; Score: 0.27 DE Interaction: P30291; IntAct: EBI-914695,EBI-1023301; Score: 0.27 DE Interaction: P33991; IntAct: EBI-374938,EBI-1023301; Score: 0.27 DE Interaction: P33993; IntAct: EBI-355924,EBI-1023301; Score: 0.27 DE Interaction: P49736; IntAct: EBI-374819,EBI-1023301; Score: 0.27 DE Interaction: Q8ZED8; IntAct: EBI-2840186,EBI-1023301; Score: 0.37 DE Interaction: Q14240; IntAct: EBI-73473,EBI-1023301; Score: 0.40 DE Interaction: P61026; IntAct: EBI-1023301,EBI-726075; Score: 0.40 DE Interaction: P61006; IntAct: EBI-1023301,EBI-722293; Score: 0.62 DE Interaction: Q96BY7; IntAct: EBI-2963262,EBI-1023301; Score: 0.27 DE Interaction: Q9NY27; IntAct: EBI-1048740,EBI-1023301; Score: 0.27 DE Interaction: Q9P260; IntAct: EBI-2831057,EBI-1023301; Score: 0.27 DE Interaction: Q6IN85; IntAct: EBI-1055598,EBI-1023301; Score: 0.27 DE Interaction: Q9UQE7; IntAct: EBI-80718,EBI-1023301; Score: 0.27 DE Interaction: Q9Y4E8; IntAct: EBI-1043104,EBI-1023301; Score: 0.27 DE Interaction: Q9Y6Y0; IntAct: EBI-715774,EBI-1023301; Score: 0.27 DE Interaction: P19838; IntAct: EBI-1023301,EBI-300010; Score: 0.56 GO GO:0001669; GO GO:0034451; GO GO:0005737; GO GO:0005829; GO GO:0070062; GO GO:0005765; GO GO:0048471; GO GO:0042802; GO GO:0008432; GO GO:0019894; GO GO:0005078; GO GO:0030159; GO GO:0007257; GO GO:0032418; GO GO:0030335; GO GO:0051149; GO GO:0045666; GO GO:0042147; GO GO:0051146; GO GO:0016192; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRD SQ DNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALH SQ QRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQP SQ RSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQ SQ VAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEG SQ ADLLGMGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEA SQ EDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLF SQ SSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKED SQ GRVQAFGWSLPQKYKQVTNGQGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLD SQ TEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGNILDSFTVCNSHVLCIASVPG SQ ARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLGGITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSE SQ VDENVPTAEEATEATEGNAGSAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVRE SQ EAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHL SQ LDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTY SQ QHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDK SQ VTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEPGSQTPLKSMLVISGGEGYID SQ FRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGNE // 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 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 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 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 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 O64629; PN Serine/threonine-protein kinase Aurora-3; GN AUR3; OS 3702; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region. Nucleus. Chromosome. Chromosome, centromere. Note=Cytoplasmic perinuclear region or in dots around the nucleolus and at the nuclear periphery in interphase cells, associated to centromeric regions of condensed chromosomes at metaphase and dispersed along the entire length of the chromosomes during anaphase (PubMed:16028112). Nucleus (PubMed:15722465). {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112}. DR UNIPROT: O64629; DR Pfam: PF00069; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00108; DE Function: Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph). Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. {ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:17087760}. DE Reference Proteome: Yes; GO GO:0032133; GO GO:0000775; GO GO:0000780; GO GO:0005634; GO GO:0048471; GO GO:0005819; GO GO:0005876; GO GO:0051233; GO GO:0005524; GO GO:0035175; GO GO:0044022; GO GO:0035174; GO GO:0007059; GO GO:0043987; GO GO:0043988; GO GO:0016572; GO GO:0007052; GO GO:0016310; GO GO:0032465; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHP SQ NILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLK SQ IADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTP SQ NVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI // ID O64740; PN Protein transport protein SEC13 homolog B; GN SEC13B; OS 3702; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Golgi apparatus {ECO:0000305|PubMed:24280388}. Endoplasmic reticulum {ECO:0000269|PubMed:21189294, ECO:0000305|PubMed:24280388}. Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. DR UNIPROT: O64740; DR UNIPROT: Q8LAX1; DR Pfam: PF00400; DR PROSITE: PS50082; DR PROSITE: PS50294; DE Function: Required for protein transport from the endoplasmic reticulum to the Golgi apparatus. {ECO:0000305|PubMed:24280388}. DE Reference Proteome: Yes; DE Interaction: Q9C9L2; IntAct: EBI-4426144,EBI-4454838; Score: 0.37 DE Interaction: Q8LAZ7; IntAct: EBI-4454838,EBI-531132; Score: 0.37 DE Interaction: O48847; IntAct: EBI-3387563,EBI-4454838; Score: 0.37 DE Interaction: Q9LT89; IntAct: EBI-4426178,EBI-4454838; Score: 0.37 GO GO:0030127; GO GO:0005829; GO GO:0005783; GO GO:0000139; GO GO:0005635; GO GO:0005643; GO GO:0031080; GO GO:0005730; GO GO:0005198; GO GO:0090114; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MPGQKIETGHEDIVHDVQMDYYGKRIATASSDCTIKITGVSNNGGSQQLATLTGHRGPVWEVAWAHPKYGSILASCSYDG SQ QVILWKEGNQNQWTQDHVFTDHKSSVNSIAWAPHDIGLSLACGSSDGNISVFTARADGGWDTSRIDQAHPVGVTSVSWAP SQ ATAPGALVSSGLLDPVYKLASGGCDNTVKVWKLANGSWKMDCFPALQKHTDWVRDVAWAPNLGLPKSTIASGSQDGKVII SQ WTVGKEGEQWEGKVLKDFMTPVWRVSWSLTGNLLAVSDGNNNVTVWKEAVDGEWEQVTAVEP // 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 O73557; PN RING finger protein Z; GN Z; OS 11622; 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: O73557; DR PDB: 2M1S; DR PDB: 5I72; 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, ECO:0000269|PubMed:12970458, ECO:0000269|PubMed:14990716}. DE Reference Proteome: Yes; 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 MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAA SQ PTAPPTGAADSIRPPPYSP // 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 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 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 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 O74525; PN Uncharacterized membrane protein C70.04c; GN SPCC70; 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: O74525; 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 MKQNNKKPLPSKTKEISLETDWIDVIETMRETNESPKSQNPSEEATTVNELSCEAKPKLLFTPTKSSLSIGNFPYKEFDP SQ VLKFPGIHYTYSRERLWGTCVILSTLFWSYYVLSNSELLEFEASEYSLLFILIIALDALLTVSLFGLFHHLMFLTTNYSY SQ TINSTLDISKGFFINVLSTMVQALVTVTIAFTKFVTIDFPIYVFSSLFLYHPLSRSRQLPTKMQLDGSGERKTDSSLVHQ SQ NPPN // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 O77059; PN Cryptochrome-1; GN cry; OS 7227; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Nucleus {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Note=Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per. {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. DR UNIPROT: O77059; DR UNIPROT: Q9TYA0; DR PDB: 4GU5; DR PDB: 4JZY; DR PDB: 4K03; DR Pfam: PF00875; DR Pfam: PF03441; 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. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing. {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:10233998, ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:16527739, ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:18641630, ECO:0000269|PubMed:9845369, ECO:0000269|PubMed:9845370}. DE Reference Proteome: Yes; DE Interaction: P18431; IntAct: EBI-242141,EBI-94117; Score: 0.40 DE Interaction: P49021; IntAct: EBI-266295,EBI-94117; Score: 0.27 DE Interaction: P07663; IntAct: EBI-496170,EBI-94117; Score: 0.27 GO GO:0005737; GO GO:0005829; GO GO:0005641; GO GO:0005654; GO GO:0005634; GO GO:0048471; GO GO:0032991; GO GO:0009882; GO GO:0071949; GO GO:0050660; GO GO:0008020; GO GO:0009881; GO GO:0009785; GO GO:0071482; GO GO:0048512; GO GO:0032922; GO GO:0007623; GO GO:0050980; GO GO:0009649; GO GO:0043153; GO GO:0042332; GO GO:0045475; GO GO:0050958; GO GO:0045892; GO GO:0007602; GO GO:0018298; GO GO:0042752; GO GO:0045187; GO GO:0009637; GO GO:0009416; GO GO:0071000; GO GO:0009588; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGR SQ LLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQM SQ FLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKV SQ EQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYT SQ MSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHG SQ LQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQ SQ EQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV // 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 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 O77737; PN Bcl-2-like protein 1; GN BCL2L1; OS 9823; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). {ECO:0000250}. DR UNIPROT: O77737; DR Pfam: PF00452; DR Pfam: PF02180; DR PROSITE: PS50062; DR PROSITE: PS01080; DR PROSITE: PS01258; DR PROSITE: PS01259; DR PROSITE: PS01260; DR PROSITE: PS50063; DE Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}. DE Reference Proteome: Yes; GO GO:0030054; GO GO:0005813; GO GO:0005737; GO GO:0005829; GO GO:0016021; GO GO:0005759; GO GO:0005741; GO GO:0031965; GO GO:0030672; GO GO:0046982; GO GO:0042803; GO GO:0006897; GO GO:0097192; GO GO:0008630; GO GO:0007093; GO GO:0043066; GO GO:1902236; GO GO:1900118; GO GO:2001243; GO GO:0032465; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV SQ IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ SQ VLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK // 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 O80480; PN Importin subunit alpha-4; GN IMPA4; OS 3702; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}. DR UNIPROT: O80480; DR UNIPROT: F4HZG6; DR UNIPROT: O49602; DR UNIPROT: Q94KD4; DR Pfam: PF00514; DR Pfam: PF16186; DR Pfam: PF01749; DR PROSITE: PS50176; DR PROSITE: PS51214; DE Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope. Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium and is essential for Agrobacterium-mediated root transformation. {ECO:0000269|PubMed:18836040}. DE Reference Proteome: Yes; DE Interaction: Q94CL9; IntAct: EBI-1773344,EBI-2131464; Score: 0.40 DE Interaction: F8RP38; IntAct: EBI-6368424,EBI-2131464; Score: 0.37 DE Interaction: Q9SZU7; IntAct: EBI-25519488,EBI-2131464; Score: 0.56 DE Interaction: Q9LUA3; IntAct: EBI-541107,EBI-2131464; Score: 0.37 DE Interaction: Q9SIC8; IntAct: EBI-4450726,EBI-2131464; Score: 0.37 DE Interaction: Q058P7; IntAct: EBI-2131464,EBI-4431752; Score: 0.53 DE Interaction: Q8GUP4; IntAct: EBI-4476287,EBI-2131464; Score: 0.37 DE Interaction: Q8GX29; IntAct: EBI-2131464,EBI-604376; Score: 0.37 GO GO:0005829; GO GO:0043657; GO GO:0005643; GO GO:0005654; GO GO:0061608; GO GO:0008139; GO GO:0080034; GO GO:0006607; GO GO:0030581; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSLRPSTRAELRKKIYKTGVDADEARRRREDNLVEIRKNKREDSLLKKRREGMMLQQQLPLGAGLDGPQTAAAVEKRLEG SQ IPMMVQGVYSDDPQAQLEATTQFRKLLSIERSPPIDEVIKAGVIPRFVEFLGRHDHPQLQFEAAWALTNVASGTSDHTRV SQ VIEQGAVPIFVKLLTSASDDVREQAVWALGNVAGDSPNCRNLVLNYGALEPLLAQLNENSKLSMLRNATWTLSNFCRGKP SQ PTPFEQVKPALPILRQLIYLNDEEVLTDACWALSYLSDGPNDKIQAVIEAGVCPRLVELLGHQSPTVLIPALRTVGNIVT SQ GDDSQTQFIIESGVLPHLYNLLTQNHKKSIKKEACWTISNITAGNKLQIEAVVGAGIILPLVHLLQNAEFDIKKEAAWAI SQ SNATSGGSHEQIQYLVTQGCIKPLCDLLICPDPRIVTVCLEGLENILKVGEADKEMGLNSGVNLYAQIIEESDGLDKVEN SQ LQSHDNNEIYEKAVKILERYWAEEEEEQILQDGGNDNSQQAFNFGNNPAAPVGGFKFA // 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 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 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 O94319; PN Protein transport protein sec13; GN sec13; OS 284812; 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: O94319; 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). Involved in septum formation. {ECO:0000250, ECO:0000269|PubMed:11821054}. DE Reference Proteome: Yes; DE Interaction: O13637; IntAct: EBI-21245957,EBI-21245929; Score: 0.37 GO GO:0030127; GO GO:0005737; GO GO:0005829; GO GO:0005789; GO GO:0000139; GO GO:0031080; GO GO:0005634; GO GO:0035859; GO GO:0005198; GO GO:0090114; GO GO:0006886; GO GO:0051028; GO GO:1904263; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MTTVDTQHDDMIHDAILDYYGKRLATCSSDQTIKVFSIENNQQTLLETLRGHSGPVWQLGWAHPKFGTILASASYDGHVI SQ VWRETGGVWSELMDHTAHQASVNAVSWAPHEYGALLACASSDGKVSVLEFKDDGSCDTRIFTAHEPGCNAVCWSPPSLSG SQ SVVGQSPAAGPKKLATAGCDNLVKIWAFDAGVNNWILEDTLAGHVDWTRDVAWAPSVGLTKTYLASASQDKNVFIWTKEG SQ DGPWQKTPLTEEKFPDIAWRVSWSLSGNILAVSCGDNKVYLFKESQNKWQLLNELSN // 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 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 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 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 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 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 O94569; PN Uncharacterized transcriptional regulatory protein C1773.12; 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}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. DR UNIPROT: O94569; 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:0005730; 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 MVPIKKISTACDLCRQRKLRCNGELPKCQNCVVYSETCKYNKRKRVKKPNVDKDDPHIVVGQPPVKKSTAGITREYTEMI SQ ELRNHIITLSKRSVNMESRIDDMLNLLNYDLSEKRETSNEIPSLVQQIQNCGFLIDEKMRRYPGIFQIHPKDYTMNDLFP SQ QSFPTWISVYRNVPEKAWANRCVEWYFRYINSCWPLFDLENFMDLFDNFYSDKEKTKGAWVVSFYAIMALAVSRSKRKDK SQ EKISKSLFSTSWFLVQKPGFFLTARLDKIQALTIMIQFCAHLSLYNLCKVLCGQMCLMVKDLDLHKEATNPNVDIEVDEL SQ NRRVFWTCYIFETTTSLIFGTPPELGDLEIDCQLPSMDVLPRFTESSQGGIVFCSEIQLTIIKNEIRKKIYKCLASASEE SQ VYKEAVLSIRGKLIVWERNLPDELKQYYDVIKLNGTIPKNVDFENQHIFTACVEIYLSYCITQLYFYDPLTNYETCLEIA SQ RKAADAIRSYFMVIEPIFKKICYLWLFLYCPFTPFQILFSNILKMEKGTSDEKIEDLDRMYSLYRFFVEMKEINGEFADK SQ LSRVALDCIDAAEHYLELKSSVGSNIFELESLLV // 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 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 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 O94901; PN SUN domain-containing protein 1; GN SUN1; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q9D666}. DR UNIPROT: O94901; DR UNIPROT: A5PL20; DR UNIPROT: B3KMV7; DR UNIPROT: B4DZF7; DR UNIPROT: B7WNY4; DR UNIPROT: B7WP53; DR UNIPROT: E9PDU4; DR UNIPROT: E9PF23; DR UNIPROT: F8WD13; DR UNIPROT: Q96CZ7; DR UNIPROT: Q9HA14; DR UNIPROT: Q9UH98; DR Pfam: PF09387; DR Pfam: PF07738; DR Pfam: PF18580; DR PROSITE: PS51469; DR OMIM: 607723; DR DisGeNET: 23353; 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:18039933, PubMed:18396275). 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). 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 (By similarity). 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 (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenenis (By similarity). May play a role in DNA repair by suppressing non- homologous end joining repair to facilitate the repair of DNA cross- links (PubMed:24375709). {ECO:0000250|UniProtKB:Q9D666, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:24375709}. DE Reference Proteome: Yes; DE Interaction: Self; IntAct: EBI-2796904,EBI-2796904; Score: 0.40 DE Interaction: Q5NFR9; IntAct: EBI-2796367,EBI-2796904; Score: 0.37 DE Interaction: Q6NUS6; IntAct: EBI-11278332,EBI-2796904; Score: 0.35 DE Interaction: Q8N6G5; IntAct: EBI-10267100,EBI-2796904; Score: 0.35 DE Interaction: P04578; IntAct: EBI-6163496,EBI-2796904; Score: 0.46 DE Interaction: Q8NF91; IntAct: EBI-928867,EBI-2796904; Score: 0.35 DE Interaction: Q8WXH0; IntAct: EBI-2372294,EBI-2796904; Score: 0.35 DE Interaction: Q8WXH0-1; IntAct: EBI-6170976,EBI-2796904; Score: 0.52 DE Interaction: Q8NF91-1; IntAct: EBI-6170938,EBI-2796904; Score: 0.52 DE Interaction: P50402; IntAct: EBI-489887,EBI-2796904; Score: 0.46 DE Interaction: P02545; IntAct: EBI-2796904,EBI-351935; Score: 0.40 DE Interaction: Q9P0N5; IntAct: EBI-721260,EBI-2796904; Score: 0.35 DE Interaction: Q401N2; IntAct: EBI-21749821,EBI-2796904; Score: 0.35 DE Interaction: Q86UE6; IntAct: EBI-9028422,EBI-2796904; Score: 0.35 DE Interaction: P16444; IntAct: EBI-749514,EBI-2796904; Score: 0.35 DE Interaction: Q9Y6Q1; IntAct: EBI-7183095,EBI-2796904; Score: 0.35 DE Interaction: Q8TCN5; IntAct: EBI-2796904,EBI-9661677; Score: 0.35 DE Interaction: Q15654; IntAct: EBI-2796904,EBI-742327; Score: 0.35 DE Interaction: A2RUC4; IntAct: EBI-2796904,EBI-21511702; Score: 0.35 DE Interaction: Q8WWF5; IntAct: EBI-2129267,EBI-2796904; Score: 0.35 DE Interaction: Q9BQ31; IntAct: EBI-6426177,EBI-2796904; Score: 0.35 DE Interaction: Q6AZY7-2; IntAct: EBI-21598366,EBI-2796904; Score: 0.35 DE Interaction: Q9NVF7; IntAct: EBI-740282,EBI-2796904; Score: 0.35 DE Interaction: Q53F39-2; IntAct: EBI-21694292,EBI-2796904; Score: 0.35 GO GO:0005623; GO GO:0005737; GO GO:0005639; GO GO:0043231; GO GO:0034993; GO GO:0005635; GO GO:0031965; 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 MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSA SQ VSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKG SQ GNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCDDCKGKRHLDAHPGRAGTLW SQ HIWACAGYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFL SQ VLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLS SQ GQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQ SQ KELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQL SQ LQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGM SQ VDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTL SQ EHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTC SQ LYRFRVHGEPVK // 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 O95248; PN Myotubularin-related protein 5; GN SBF1; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12668758}. DR UNIPROT: O95248; DR UNIPROT: A0A024R4Z9; DR UNIPROT: A6PVG9; DR UNIPROT: G5E933; DR UNIPROT: O60228; DR UNIPROT: Q5JXD8; DR UNIPROT: Q5PPM2; DR UNIPROT: Q96GR9; DR UNIPROT: Q9UGB8; 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; DR OMIM: 603560; DR OMIM: 615284; DR DisGeNET: 6305; DE Function: Acts as an adapter for the phosphatase MTMR2 to regulate MTMR2 catalytic activity and subcellular location (PubMed:12668758). May function as a guanine nucleotide exchange factor (GEF) activating RAB28 (PubMed:20937701). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:20937701). Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts (PubMed:9537414). {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9537414}. DE Disease: Charcot-Marie-Tooth disease 4B3 (CMT4B3) [MIM:615284]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. {ECO:0000269|PubMed:23749797}. Note=The disease is caused by mutations affecting the gene represented in this entry. DE Reference Proteome: Yes; DE Interaction: Q9NTG7; IntAct: EBI-724621,EBI-2322878; Score: 0.40 DE Interaction: P03372; IntAct: EBI-78473,EBI-2322878; Score: 0.35 DE Interaction: P04792; IntAct: EBI-352682,EBI-2322878; Score: 0.37 DE Interaction: P11279; IntAct: EBI-2805407,EBI-2322878; Score: 0.35 DE Interaction: Q7CJU1; IntAct: EBI-2322878,EBI-2855448; Score: 0.37 GO GO:0005737; GO GO:0005829; GO GO:0005789; GO GO:0016021; GO GO:0016604; GO GO:0048471; GO GO:0019208; GO GO:0008138; GO GO:0017112; GO GO:0006661; GO GO:0006470; GO GO:0043087; GO GO:0007283; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYC SQ ACLTFWEPAEPSQQETTRVEDATEREEEGDEGGQTHLSPTAPAPSAQLFAPKTLVLVSRLDHTEVFRNSLGLIYAIHVEG SQ LNVCLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLADSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFL SQ SRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTIPECVH SQ IPPLPEPLQSQTHSVLSMVLDPELELADLAFPPPTTSTSSLKMQDKELRAVFLRLFAQLLQGYRWCLHVVRIHPEPVIRF SQ HKAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRPTDLFDELVAHEVARMRADENHPQRVLRHVQELAEQLYKNEN SQ PYPAVAMHKVQRPGESSHLRRVPRPFPRLDEGTVQWIVDQAAAKMQGAPPAVKAERRTTVPSGPPMTAILERCSGLHVNS SQ ARRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAQELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLD SQ EHGIAAALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPTEDLAPAQEVGEAPSQED SQ ERSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNS SQ MAGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVQRESRRLPPI SQ QKPKLLRPRLLPGEECVLDGLRVYLLPDGREEGAGGSAGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVA SQ ALTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSAHTPGRPPR SQ VTKDKGPSLRTLSRNLVKNAKKTIGRQHVTRKKYNPPSWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMS SQ SLVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSVQDNALQRVSRCYRQNRFPVVCWRS SQ GRSKAVLLRSGGLHGKGVVGLFKAQNAPSPGQSQADSSSLEQEKYLQAVVSSMPRYADASGRNTLSGFSSAHMGSHGKWG SQ SVRTSGRSSGLGTDVGSRLAGRDALAPPQANGGPPDPGFLRPQRAALYILGDKAQLKGVRSDPLQQWELVPIEVFEARQV SQ KASFKKLLKACVPGCPAAEPSPASFLRSLEDSEWLIQIHKLLQVSVLVVELLDSGSSVLVGLEDGWDITTQVVSLVQLLS SQ DPFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHVSRR SQ FRTFLLDSDYERIELGLLYEEKGERRGQVPCRSVWEYVDRLSKRTPVFHNYMYAPEDAEVLRPYSNVSNLKVWDFYTEET SQ LAEGPPYDWELAQGPPEPPEEERSDGGAPQSRRRVVWPCYDSCPRAQPDAISRLLEELQRLETELGQPAERWKDTWDRVK SQ AAQRLEGRPDGRGTPSSLLVSTAPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSGSRQAARRSTSTLYSQFQTAES SQ ENRSYEGTLYKKGAFMKPWKARWFVLDKTKHQLRYYDHRVDTECKGVIDLAEVEAVAPGTPTMGAPKTVDEKAFFDVKTT SQ RRVYNFCAQDVPSAQQWVDRIQSCLSDA // 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 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 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 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 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 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 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 O96018; PN Amyloid-beta A4 precursor protein-binding family A member 3; GN APBA3; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}. DR UNIPROT: O96018; DR UNIPROT: O60483; DR UNIPROT: Q9UPZ2; DR PDB: 2YT7; DR PDB: 2YT8; DR PDB: 5UWS; DR Pfam: PF00595; DR Pfam: PF00640; DR PROSITE: PS50106; DR PROSITE: PS01179; DR OMIM: 604262; DR DisGeNET: 9546; DE Function: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}. DE Reference Proteome: Yes; DE Interaction: Q9NWT6; IntAct: EBI-745632,EBI-6115839; Score: 0.75 DE Interaction: Q9H6Z9; IntAct: EBI-1175354,EBI-6115839; Score: 0.35 DE Interaction: P16152; IntAct: EBI-351348,EBI-6115839; Score: 0.35 DE Interaction: P78552; IntAct: EBI-6115839,EBI-1391535; Score: 0.35 DE Interaction: Q9UHD2; IntAct: EBI-6115839,EBI-356402; Score: 0.35 DE Interaction: Q9NSD9; IntAct: EBI-6115839,EBI-353803; Score: 0.35 DE Interaction: Q9H6S1; IntAct: EBI-6115839,EBI-359973; Score: 0.35 DE Interaction: Q9BY42; IntAct: EBI-6115839,EBI-1045669; Score: 0.35 DE Interaction: Q9BSJ5-2; IntAct: EBI-6115839,EBI-21508079; Score: 0.35 DE Interaction: Q99590; IntAct: EBI-6115839,EBI-3934011; Score: 0.35 DE Interaction: Q99569-2; IntAct: EBI-6115839,EBI-4324902; Score: 0.35 DE Interaction: Q96P71-2; IntAct: EBI-6115839,EBI-15098952; Score: 0.60 DE Interaction: Q8TEU7-3; IntAct: EBI-6115839,EBI-21543860; Score: 0.35 DE Interaction: Q8TBX8; IntAct: EBI-6115839,EBI-1383637; Score: 0.35 DE Interaction: Q8N9R8-2; IntAct: EBI-6115839,EBI-21554215; Score: 0.35 DE Interaction: Q6PD62; IntAct: EBI-6115839,EBI-1019583; Score: 0.35 DE Interaction: Q6P5Z2; IntAct: EBI-6115839,EBI-1384335; Score: 0.35 DE Interaction: Q5JTD0-2; IntAct: EBI-6115839,EBI-10980237; Score: 0.35 DE Interaction: Q12986-2; IntAct: EBI-6115839,EBI-21604769; Score: 0.35 DE Interaction: Q08AH1; IntAct: EBI-6115839,EBI-2818055; Score: 0.35 DE Interaction: Q06481-2; IntAct: EBI-6115839,EBI-21531175; Score: 0.35 DE Interaction: P55789; IntAct: EBI-6115839,EBI-718281; Score: 0.35 DE Interaction: P29803; IntAct: EBI-6115839,EBI-2957428; Score: 0.35 DE Interaction: P17029; IntAct: EBI-6115839,EBI-10199654; Score: 0.35 DE Interaction: P05067-10; IntAct: EBI-6115839,EBI-21535835; Score: 0.35 DE Interaction: O94985-2; IntAct: EBI-6115839,EBI-16041593; Score: 0.35 DE Interaction: O75319; IntAct: EBI-6115839,EBI-719569; Score: 0.35 DE Interaction: Q96BW9; IntAct: EBI-6115839,EBI-13943422; Score: 0.35 DE Interaction: P32320; IntAct: EBI-9250559,EBI-6115839; Score: 0.35 DE Interaction: Q9QYP6; IntAct: EBI-6115874,EBI-6115839; Score: 0.50 DE Interaction: A7MCY6; IntAct: EBI-359969,EBI-6115839; Score: 0.50 DE Interaction: Q92844; IntAct: EBI-356349,EBI-6115839; Score: 0.50 DE Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-6115839; Score: 0.35 DE Interaction: Q86VW1; IntAct: EBI-21721937,EBI-6115839; Score: 0.35 DE Interaction: Q9BZB8-3; IntAct: EBI-21821945,EBI-6115839; Score: 0.35 GO GO:0005737; GO GO:0043197; GO GO:0048471; GO GO:0005886; GO GO:0045202; GO GO:0001540; GO GO:0019899; GO GO:0004857; GO GO:0007268; GO GO:0001701; GO GO:0043086; GO GO:0015031; GO GO:0010468; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAP SQ CPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASA SQ EQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTS SQ TRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQD SQ HGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKR SQ RGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHC SQ PPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPA SQ ATYRLLTGQEQPVYL // 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 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 P00533; PN Epidermal growth factor receptor; GN EGFR; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Cell membrane {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}; Single-pass type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27153536}; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:27153536}. Endosome membrane. Nucleus {ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:20674546}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:20674546). Endocytosed upon activation by ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055). {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}. [Isoform 2]: Secreted. DR UNIPROT: P00533; DR UNIPROT: O00688; DR UNIPROT: O00732; DR UNIPROT: P06268; DR UNIPROT: Q14225; DR UNIPROT: Q68GS5; DR UNIPROT: Q92795; DR UNIPROT: Q9BZS2; DR UNIPROT: Q9GZX1; DR UNIPROT: Q9H2C9; DR UNIPROT: Q9H3C9; DR UNIPROT: Q9UMD7; DR UNIPROT: Q9UMD8; DR UNIPROT: Q9UMG5; DR PDB: 1DNQ; DR PDB: 1DNR; DR PDB: 1IVO; DR PDB: 1M14; DR PDB: 1M17; DR PDB: 1MOX; DR PDB: 1NQL; DR PDB: 1XKK; DR PDB: 1YY9; DR PDB: 1Z9I; DR PDB: 2EB2; DR PDB: 2EB3; DR PDB: 2EXP; DR PDB: 2EXQ; DR PDB: 2GS2; DR PDB: 2GS6; DR PDB: 2GS7; DR PDB: 2ITN; DR PDB: 2ITO; DR PDB: 2ITP; DR PDB: 2ITQ; DR PDB: 2ITT; DR PDB: 2ITU; DR PDB: 2ITV; DR PDB: 2ITW; DR PDB: 2ITX; DR PDB: 2ITY; DR PDB: 2ITZ; DR PDB: 2J5E; DR PDB: 2J5F; DR PDB: 2J6M; DR PDB: 2JIT; DR PDB: 2JIU; DR PDB: 2JIV; DR PDB: 2KS1; DR PDB: 2M0B; DR PDB: 2M20; DR PDB: 2N5S; DR PDB: 2RF9; DR PDB: 2RFD; DR PDB: 2RFE; DR PDB: 2RGP; DR PDB: 3B2U; DR PDB: 3B2V; DR PDB: 3BEL; DR PDB: 3BUO; DR PDB: 3C09; DR PDB: 3G5V; DR PDB: 3G5Y; DR PDB: 3GOP; DR PDB: 3GT8; DR PDB: 3IKA; DR PDB: 3LZB; DR PDB: 3NJP; DR PDB: 3OB2; DR PDB: 3OP0; DR PDB: 3P0Y; DR PDB: 3PFV; DR PDB: 3POZ; DR PDB: 3QWQ; DR PDB: 3UG1; DR PDB: 3UG2; DR PDB: 3VJN; DR PDB: 3VJO; DR PDB: 3VRP; DR PDB: 3VRR; DR PDB: 3W2O; DR PDB: 3W2P; DR PDB: 3W2Q; DR PDB: 3W2R; DR PDB: 3W2S; DR PDB: 3W32; DR PDB: 3W33; DR PDB: 4G5J; DR PDB: 4G5P; DR PDB: 4HJO; DR PDB: 4I1Z; DR PDB: 4I20; DR PDB: 4I21; DR PDB: 4I22; DR PDB: 4I23; DR PDB: 4I24; DR PDB: 4JQ7; DR PDB: 4JQ8; DR PDB: 4JR3; DR PDB: 4JRV; DR PDB: 4KRL; DR PDB: 4KRM; DR PDB: 4KRO; DR PDB: 4KRP; DR PDB: 4LI5; DR PDB: 4LL0; DR PDB: 4LQM; DR PDB: 4LRM; DR PDB: 4R3P; DR PDB: 4R3R; DR PDB: 4R5S; DR PDB: 4RIW; DR PDB: 4RIX; DR PDB: 4RIY; DR PDB: 4RJ4; DR PDB: 4RJ5; DR PDB: 4RJ6; DR PDB: 4RJ7; DR PDB: 4RJ8; DR PDB: 4TKS; DR PDB: 4UIP; DR PDB: 4UV7; DR PDB: 4WD5; DR PDB: 4WKQ; DR PDB: 4WRG; DR PDB: 4ZAU; DR PDB: 4ZJV; DR PDB: 4ZSE; DR PDB: 5C8K; DR PDB: 5C8M; DR PDB: 5C8N; DR PDB: 5CAL; DR PDB: 5CAN; DR PDB: 5CAO; DR PDB: 5CAP; DR PDB: 5CAQ; DR PDB: 5CAS; DR PDB: 5CAU; DR PDB: 5CAV; DR PDB: 5CNN; DR PDB: 5CNO; DR PDB: 5CZH; DR PDB: 5CZI; DR PDB: 5D41; DR PDB: 5EDP; DR PDB: 5EDQ; DR PDB: 5EDR; DR PDB: 5EM5; DR PDB: 5EM6; DR PDB: 5EM7; DR PDB: 5EM8; DR PDB: 5FED; DR PDB: 5FEE; DR PDB: 5FEQ; DR PDB: 5GMP; DR PDB: 5GNK; DR PDB: 5GTY; DR PDB: 5GTZ; DR PDB: 5HCX; DR PDB: 5HCY; DR PDB: 5HCZ; DR PDB: 5HG5; DR PDB: 5HG7; DR PDB: 5HG8; DR PDB: 5HG9; DR PDB: 5HIB; DR PDB: 5HIC; DR PDB: 5J9Y; DR PDB: 5J9Z; DR PDB: 5JEB; DR PDB: 5LV6; DR PDB: 5SX4; DR PDB: 5SX5; DR PDB: 5U8L; DR PDB: 5UG8; DR PDB: 5UG9; DR PDB: 5UGA; DR PDB: 5UGB; DR PDB: 5UGC; DR PDB: 5UWD; DR PDB: 5WB7; DR PDB: 5WB8; DR PDB: 5X26; DR PDB: 5X27; DR PDB: 5X28; DR PDB: 5X2A; DR PDB: 5X2C; DR PDB: 5X2F; DR PDB: 5X2K; DR PDB: 5XDK; DR PDB: 5XDL; DR PDB: 5XGM; DR PDB: 5XGN; DR PDB: 5XWD; DR PDB: 5Y25; DR PDB: 5Y9T; DR PDB: 5YU9; DR PDB: 5ZTO; DR PDB: 5ZWJ; DR PDB: 6ARU; DR PDB: 6B3S; DR PDB: 6D8E; DR PDB: 6DUK; DR PDB: 6JZ0; DR PDB: 6P1D; DR PDB: 6P1L; DR PDB: 6P8Q; DR PDB: 6S89; DR PDB: 6S8A; DR PDB: 6S9B; DR PDB: 6S9C; DR PDB: 6S9D; DR Pfam: PF00757; DR Pfam: PF14843; DR Pfam: PF07714; DR Pfam: PF01030; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00109; DR OMIM: 131550; DR OMIM: 211980; DR OMIM: 616069; DR DisGeNET: 1956; DE Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin- binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK- ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146, ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11602604, ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15611079, ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:7679104, ECO:0000269|PubMed:8144591, ECO:0000269|PubMed:9419975}. Isoform 2 may act as an antagonist of EGF action. (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269|PubMed:21516087}. DE Disease: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:16672372}. Note=The gene represented in this entry is involved in disease pathogenesis. Inflammatory skin and bowel disease, neonatal, 2 (NISBD2) [MIM:616069]: A disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized. {ECO:0000269|PubMed:24691054}. Note=The disease is caused by mutations affecting the gene represented in this entry. DE Reference Proteome: Yes; DE Interaction: D4A631; IntAct: EBI-297353,EBI-6251168; Score: 0.35 DE Interaction: O60645; IntAct: EBI-1052278,EBI-297353; Score: 0.40 DE Interaction: O94875; IntAct: EBI-311323,EBI-297353; Score: 0.55 DE Interaction: P00519; IntAct: EBI-375543,EBI-297353; Score: 0.69 DE Interaction: Self; IntAct: EBI-297353,EBI-297353; Score: 0.98 DE Interaction: P42566; IntAct: EBI-297353,EBI-396684; Score: 0.35 DE Interaction: Q9UJ41; IntAct: EBI-297353,EBI-913954; Score: 0.60 DE Interaction: P23467; IntAct: EBI-297353,EBI-1265766; Score: 0.69 DE Interaction: Q12913; IntAct: EBI-297353,EBI-2264500; Score: 0.44 DE Interaction: P08575; IntAct: EBI-1341,EBI-297353; Score: 0.59 DE Interaction: P62157; IntAct: EBI-397403,EBI-297353; Score: 0.40 DE Interaction: Q29376; IntAct: EBI-297353,EBI-1256881; Score: 0.44 DE Interaction: P0DP23; IntAct: EBI-297353,EBI-397435; Score: 0.76 DE Interaction: P0DP28; IntAct: EBI-397460,EBI-297353; Score: 0.40 DE Interaction: P13866; IntAct: EBI-297353,EBI-1772443; Score: 0.52 DE Interaction: P23470; IntAct: EBI-297353,EBI-2258115; Score: 0.57 DE Interaction: Q9BZP6; IntAct: EBI-297353,EBI-14357960; Score: 0.40 DE Interaction: Q92731; IntAct: EBI-78505,EBI-297353; Score: 0.50 DE Interaction: Q6PK50; IntAct: EBI-297353,EBI-9356629; Score: 0.40 DE Interaction: Q16543; IntAct: EBI-297353,EBI-295634; Score: 0.71 DE Interaction: Q96BE0; IntAct: EBI-9356686,EBI-297353; Score: 0.40 DE Interaction: Q8K2C9; IntAct: EBI-8329978,EBI-297353; Score: 0.40 DE Interaction: Q53FC7; IntAct: EBI-297353,EBI-9356749; Score: 0.40 DE Interaction: Q9BPW0; IntAct: EBI-297353,EBI-9356778; Score: 0.40 DE Interaction: Q13451; IntAct: EBI-297353,EBI-306914; Score: 0.40 DE Interaction: Q8IVD9; IntAct: EBI-297353,EBI-744342; Score: 0.40 DE Interaction: P04626; IntAct: EBI-641062,EBI-297353; Score: 0.96 DE Interaction: P21860; IntAct: EBI-720706,EBI-297353; Score: 0.92 DE Interaction: O14965; IntAct: EBI-448680,EBI-297353; Score: 0.60 DE Interaction: P14618-1; IntAct: EBI-297353,EBI-4304679; Score: 0.44 DE Interaction: P97313; IntAct: EBI-2272005,EBI-297353; Score: 0.56 DE Interaction: P78527; IntAct: EBI-297353,EBI-352053; Score: 0.40 DE Interaction: P17936; IntAct: EBI-297353,EBI-715709; Score: 0.58 DE Interaction: P50281; IntAct: EBI-297353,EBI-992788; Score: 0.35 DE Interaction: P63010; IntAct: EBI-297353,EBI-432924; Score: 0.35 DE Interaction: Q8TF42; IntAct: EBI-297353,EBI-1380492; Score: 0.60 DE Interaction: Q9UBS4; IntAct: EBI-297353,EBI-713113; Score: 0.35 DE Interaction: O75223; IntAct: EBI-297353,EBI-6912130; Score: 0.35 DE Interaction: P62701; IntAct: EBI-297353,EBI-354303; Score: 0.35 DE Interaction: P11142; IntAct: EBI-297353,EBI-351896; Score: 0.80 DE Interaction: O95782; IntAct: EBI-297353,EBI-353552; Score: 0.53 DE Interaction: P62269; IntAct: EBI-297353,EBI-352451; Score: 0.35 DE Interaction: P34931; IntAct: EBI-297353,EBI-354912; Score: 0.35 DE Interaction: P54652; IntAct: EBI-297353,EBI-356991; Score: 0.35 DE Interaction: P01040; IntAct: EBI-297353,EBI-724303; Score: 0.35 DE Interaction: P62805; IntAct: EBI-297353,EBI-302023; Score: 0.35 DE Interaction: P29353; IntAct: EBI-297353,EBI-78835; Score: 0.97 DE Interaction: P11021; IntAct: EBI-297353,EBI-354921; Score: 0.53 DE Interaction: P08195; IntAct: EBI-297353,EBI-702356; Score: 0.64 DE Interaction: Q75V66; IntAct: EBI-297353,EBI-8769971; Score: 0.35 DE Interaction: P38646; IntAct: EBI-297353,EBI-354932; Score: 0.75 DE Interaction: O95155; IntAct: EBI-297353,EBI-1641720; Score: 0.35 DE Interaction: Q01469; IntAct: EBI-297353,EBI-1054073; Score: 0.35 DE Interaction: Q92832; IntAct: EBI-297353,EBI-947754; Score: 0.35 DE Interaction: Q6UWL2; IntAct: EBI-297353,EBI-2821581; Score: 0.35 DE Interaction: P25705; IntAct: EBI-297353,EBI-351437; Score: 0.35 DE Interaction: Q8N163; IntAct: EBI-297353,EBI-355410; Score: 0.35 DE Interaction: Q09666; IntAct: EBI-297353,EBI-2555881; Score: 0.67 DE Interaction: Q13098; IntAct: EBI-297353,EBI-725197; Score: 0.35 DE Interaction: P62993; IntAct: EBI-297353,EBI-401755; Score: 0.98 DE Interaction: Q9UJM3; IntAct: EBI-297353,EBI-2941912; Score: 0.83 DE Interaction: Q71U36; IntAct: EBI-297353,EBI-302552; Score: 0.75 DE Interaction: P49411; IntAct: EBI-297353,EBI-359097; Score: 0.35 DE Interaction: Q8WV24; IntAct: EBI-297353,EBI-738731; Score: 0.35 DE Interaction: P10586; IntAct: EBI-297353,EBI-7188069; Score: 0.55 DE Interaction: Q9BYJ9; IntAct: EBI-297353,EBI-1051237; Score: 0.35 DE Interaction: Q92522; IntAct: EBI-297353,EBI-876335; Score: 0.35 DE Interaction: P53680; IntAct: EBI-297353,EBI-297662; Score: 0.35 DE Interaction: P62841; IntAct: EBI-297353,EBI-372635; Score: 0.35 DE Interaction: Q96JX3; IntAct: EBI-297353,EBI-8770074; Score: 0.35 DE Interaction: O60716; IntAct: EBI-297353,EBI-701927; Score: 0.75 DE Interaction: P30711; IntAct: EBI-297353,EBI-8770084; Score: 0.35 DE Interaction: P48594; IntAct: EBI-297353,EBI-1055490; Score: 0.35 DE Interaction: Q96QV6; IntAct: EBI-297353,EBI-6286100; Score: 0.35 DE Interaction: P12830; IntAct: EBI-297353,EBI-727477; Score: 0.76 DE Interaction: P23634; IntAct: EBI-297353,EBI-1174388; Score: 0.35 DE Interaction: Q01650; IntAct: EBI-297353,EBI-6138761; Score: 0.35 DE Interaction: P35321; IntAct: EBI-297353,EBI-6149907; Score: 0.35 DE Interaction: P18621; IntAct: EBI-297353,EBI-726937; Score: 0.35 DE Interaction: P31943; IntAct: EBI-297353,EBI-351590; Score: 0.53 DE Interaction: P23246; IntAct: EBI-297353,EBI-355453; Score: 0.35 DE Interaction: P08581; IntAct: EBI-297353,EBI-1039152; Score: 0.80 DE Interaction: Q5JNZ5; IntAct: EBI-297353,EBI-8770070; Score: 0.35 DE Interaction: Q10567; IntAct: EBI-297353,EBI-1171303; Score: 0.35 DE Interaction: P26232; IntAct: EBI-297353,EBI-3953920; Score: 0.35 DE Interaction: O94973; IntAct: EBI-297353,EBI-1642835; Score: 0.35 DE Interaction: Q9H0D6; IntAct: EBI-297353,EBI-372110; Score: 0.53 DE Interaction: P23468; IntAct: EBI-297353,EBI-2682990; Score: 0.55 DE Interaction: Q9UMD9; IntAct: EBI-297353,EBI-2528742; Score: 0.35 DE Interaction: P16615; IntAct: EBI-297353,EBI-358933; Score: 0.53 DE Interaction: Q8IUR7; IntAct: EBI-297353,EBI-1049469; Score: 0.35 DE Interaction: P31947; IntAct: EBI-297353,EBI-476295; Score: 0.83 DE Interaction: P27824; IntAct: EBI-297353,EBI-355947; Score: 0.35 DE Interaction: P04114; IntAct: EBI-297353,EBI-3926040; Score: 0.35 DE Interaction: O95470; IntAct: EBI-297353,EBI-1046170; Score: 0.35 DE Interaction: Q9UQB8; IntAct: EBI-297353,EBI-525456; Score: 0.67 DE Interaction: P04792; IntAct: EBI-297353,EBI-352682; Score: 0.67 DE Interaction: P04083; IntAct: EBI-297353,EBI-354007; Score: 0.77 DE Interaction: Q96RL7; IntAct: EBI-297353,EBI-1752583; Score: 0.35 DE Interaction: P49756; IntAct: EBI-297353,EBI-2211856; Score: 0.35 DE Interaction: Q9UK59; IntAct: EBI-297353,EBI-2871803; Score: 0.35 DE Interaction: Q96CW1; IntAct: EBI-297353,EBI-297683; Score: 0.67 DE Interaction: P16144; IntAct: EBI-297353,EBI-948678; Score: 0.35 DE Interaction: P35221; IntAct: EBI-297353,EBI-701918; Score: 0.67 DE Interaction: P35222; IntAct: EBI-297353,EBI-491549; Score: 0.35 DE Interaction: P08238; IntAct: EBI-297353,EBI-352572; Score: 0.89 DE Interaction: P07900; IntAct: EBI-297353,EBI-296047; Score: 0.78 DE Interaction: P43307; IntAct: EBI-297353,EBI-714168; Score: 0.35 DE Interaction: P40763; IntAct: EBI-297353,EBI-518675; Score: 0.92 DE Interaction: Q00325; IntAct: EBI-297353,EBI-358549; Score: 0.53 DE Interaction: O95573; IntAct: EBI-297353,EBI-1190822; Score: 0.35 DE Interaction: O60884; IntAct: EBI-297353,EBI-352957; Score: 0.53 DE Interaction: P27348; IntAct: EBI-297353,EBI-359854; Score: 0.85 DE Interaction: P68366; IntAct: EBI-297353,EBI-351772; Score: 0.53 DE Interaction: Q8NFI3; IntAct: EBI-297353,EBI-2857825; Score: 0.35 DE Interaction: O00483; IntAct: EBI-297353,EBI-1049381; Score: 0.35 DE Interaction: A1L0T0; IntAct: EBI-297353,EBI-720553; Score: 0.35 DE Interaction: P16083; IntAct: EBI-297353,EBI-358466; Score: 0.35 DE Interaction: Q14457; IntAct: EBI-949378,EBI-297353; Score: 0.63 DE Interaction: Q92622; IntAct: EBI-297353,EBI-2952709; Score: 0.56 DE Interaction: Q13480; IntAct: EBI-517684,EBI-297353; Score: 0.67 DE Interaction: P16333; IntAct: EBI-297353,EBI-389883; Score: 0.77 DE Interaction: P29353-7; IntAct: EBI-297353,EBI-9691288; Score: 0.58 DE Interaction: P46108-1; IntAct: EBI-287556,EBI-297353; Score: 0.51 DE Interaction: P04406; IntAct: EBI-354056,EBI-297353; Score: 0.79 DE Interaction: Q68CZ2; IntAct: EBI-1220488,EBI-297353; Score: 0.68 DE Interaction: P15941; IntAct: EBI-2804728,EBI-297353; Score: 0.82 DE Interaction: P42224; IntAct: EBI-1057697,EBI-297353; Score: 0.77 DE Interaction: Q9Y2R2; IntAct: EBI-297353,EBI-1211241; Score: 0.63 DE Interaction: P17252; IntAct: EBI-297353,EBI-1383528; Score: 0.63 DE Interaction: P16885; IntAct: EBI-617403,EBI-297353; Score: 0.80 DE Interaction: Q8WUI4; IntAct: EBI-297353,EBI-1048378; Score: 0.63 DE Interaction: O75791; IntAct: EBI-297353,EBI-740418; Score: 0.63 DE Interaction: P09769; IntAct: EBI-297353,EBI-1383732; Score: 0.63 DE Interaction: Q92870; IntAct: EBI-79277,EBI-297353; Score: 0.74 DE Interaction: Q9NSE2; IntAct: EBI-617866,EBI-297353; Score: 0.74 DE Interaction: Q9BRG2; IntAct: EBI-2339271,EBI-297353; Score: 0.63 DE Interaction: P49069; IntAct: EBI-1748958,EBI-297353; Score: 0.63 DE Interaction: O00750; IntAct: EBI-641107,EBI-297353; Score: 0.81 DE Interaction: P04150; IntAct: EBI-493507,EBI-297353; Score: 0.63 DE Interaction: P16234; IntAct: EBI-2861522,EBI-297353; Score: 0.68 DE Interaction: Q13094; IntAct: EBI-346946,EBI-297353; Score: 0.63 DE Interaction: O43561; IntAct: EBI-297353,EBI-1222766; Score: 0.63 DE Interaction: Q6S5L8; IntAct: EBI-9453524,EBI-297353; Score: 0.63 DE Interaction: P10599; IntAct: EBI-297353,EBI-594644; Score: 0.79 DE Interaction: P18031; IntAct: EBI-297353,EBI-968788; Score: 0.86 DE Interaction: Q12933; IntAct: EBI-355744,EBI-297353; Score: 0.63 DE Interaction: Q12929; IntAct: EBI-375576,EBI-297353; Score: 0.63 DE Interaction: Q92625; IntAct: EBI-1048612,EBI-297353; Score: 0.74 DE Interaction: Q9UBN7; IntAct: EBI-297353,EBI-301697; Score: 0.81 DE Interaction: P42229; IntAct: EBI-749537,EBI-297353; Score: 0.63 DE Interaction: Q14247; IntAct: EBI-351886,EBI-297353; Score: 0.63 DE Interaction: Q9UNE7; IntAct: EBI-357085,EBI-297353; Score: 0.72 DE Interaction: Q38SD2; IntAct: EBI-1050422,EBI-297353; Score: 0.54 DE Interaction: P30307; IntAct: EBI-297353,EBI-974439; Score: 0.55 DE Interaction: P42685; IntAct: EBI-1383583,EBI-297353; Score: 0.55 DE Interaction: Q8WUM4; IntAct: EBI-310624,EBI-297353; Score: 0.68 DE Interaction: P45984; IntAct: EBI-713568,EBI-297353; Score: 0.55 DE Interaction: Q07954; IntAct: EBI-1046087,EBI-297353; Score: 0.55 DE Interaction: P32121; IntAct: EBI-297353,EBI-714559; Score: 0.55 DE Interaction: P34932; IntAct: EBI-356933,EBI-297353; Score: 0.67 DE Interaction: O60603; IntAct: EBI-297353,EBI-973722; Score: 0.68 DE Interaction: O00459; IntAct: EBI-346930,EBI-297353; Score: 0.69 DE Interaction: P52630; IntAct: EBI-1546963,EBI-297353; Score: 0.55 DE Interaction: O14543; IntAct: EBI-297353,EBI-714146; Score: 0.55 DE Interaction: O14544; IntAct: EBI-3929549,EBI-297353; Score: 0.55 DE Interaction: Q07890; IntAct: EBI-298181,EBI-297353; Score: 0.55 DE Interaction: P10636; IntAct: EBI-366182,EBI-297353; Score: 0.55 DE Interaction: Q9NRF2; IntAct: EBI-310491,EBI-297353; Score: 0.77 DE Interaction: Q8N5H7; IntAct: EBI-297353,EBI-745980; Score: 0.55 DE Interaction: P46109; IntAct: EBI-297353,EBI-910; Score: 0.77 DE Interaction: Q05397; IntAct: EBI-702142,EBI-297353; Score: 0.67 DE Interaction: O00401; IntAct: EBI-957615,EBI-297353; Score: 0.55 DE Interaction: P07948; IntAct: EBI-79452,EBI-297353; Score: 0.82 DE Interaction: Q9H6Q3; IntAct: EBI-297353,EBI-1222854; Score: 0.55 DE Interaction: P31946; IntAct: EBI-297353,EBI-359815; Score: 0.55 DE Interaction: Q99952; IntAct: EBI-297353,EBI-1384210; Score: 0.55 DE Interaction: Q14155; IntAct: EBI-717515,EBI-297353; Score: 0.55 DE Interaction: P46108; IntAct: EBI-886,EBI-297353; Score: 0.69 DE Interaction: P05067; IntAct: EBI-297353,EBI-77613; Score: 0.55 DE Interaction: P49798; IntAct: EBI-297353,EBI-9688865; Score: 0.55 DE Interaction: P49407; IntAct: EBI-743313,EBI-297353; Score: 0.55 DE Interaction: Q99704; IntAct: EBI-1384360,EBI-297353; Score: 0.55 DE Interaction: P51636; IntAct: EBI-297353,EBI-603607; Score: 0.67 DE Interaction: P14923; IntAct: EBI-702484,EBI-297353; Score: 0.55 DE Interaction: P26447; IntAct: EBI-717058,EBI-297353; Score: 0.74 DE Interaction: Q92569; IntAct: EBI-79893,EBI-297353; Score: 0.77 DE Interaction: P45983; IntAct: EBI-297353,EBI-286483; Score: 0.55 DE Interaction: Q9UPY6; IntAct: EBI-297353,EBI-3907133; Score: 0.55 DE Interaction: Q99962; IntAct: EBI-297353,EBI-77938; Score: 0.68 DE Interaction: Q99759; IntAct: EBI-297353,EBI-307281; Score: 0.55 DE Interaction: P51451; IntAct: EBI-2105445,EBI-297353; Score: 0.69 DE Interaction: Q13153; IntAct: EBI-297353,EBI-1307; Score: 0.55 DE Interaction: P15498; IntAct: EBI-297353,EBI-625518; Score: 0.55 DE Interaction: P63104; IntAct: EBI-297353,EBI-347088; Score: 0.77 DE Interaction: Q15750; IntAct: EBI-358643,EBI-297353; Score: 0.55 DE Interaction: Q02156; IntAct: EBI-706254,EBI-297353; Score: 0.55 DE Interaction: P08631; IntAct: EBI-297353,EBI-346340; Score: 0.68 DE Interaction: Q02297; IntAct: EBI-2460704,EBI-297353; Score: 0.55 DE Interaction: Q13387; IntAct: EBI-722813,EBI-297353; Score: 0.69 DE Interaction: Q13905; IntAct: EBI-297353,EBI-976876; Score: 0.55 DE Interaction: P42684; IntAct: EBI-1102694,EBI-297353; Score: 0.69 DE Interaction: Q13322; IntAct: EBI-297353,EBI-80275; Score: 0.73 DE Interaction: P12931; IntAct: EBI-297353,EBI-621482; Score: 0.90 DE Interaction: Q8TDI0; IntAct: EBI-1042816,EBI-297353; Score: 0.55 DE Interaction: P37840; IntAct: EBI-985879,EBI-297353; Score: 0.55 DE Interaction: O43639; IntAct: EBI-713635,EBI-297353; Score: 0.55 DE Interaction: Q9Y5X1; IntAct: EBI-297353,EBI-77848; Score: 0.55 DE Interaction: Q99963; IntAct: EBI-473910,EBI-297353; Score: 0.55 DE Interaction: Q03135; IntAct: EBI-297353,EBI-603614; Score: 0.81 DE Interaction: Q92918; IntAct: EBI-881,EBI-297353; Score: 0.55 DE Interaction: P06493; IntAct: EBI-444308,EBI-297353; Score: 0.67 DE Interaction: P43403; IntAct: EBI-1211276,EBI-297353; Score: 0.69 DE Interaction: P19438; IntAct: EBI-299451,EBI-297353; Score: 0.55 DE Interaction: Q9Y6K9; IntAct: EBI-81279,EBI-297353; Score: 0.55 DE Interaction: Q9NZM3; IntAct: EBI-297353,EBI-308689; Score: 0.55 DE Interaction: Q05513; IntAct: EBI-295351,EBI-297353; Score: 0.55 DE Interaction: P05107; IntAct: EBI-300173,EBI-297353; Score: 0.55 DE Interaction: Q13239; IntAct: EBI-726214,EBI-297353; Score: 0.69 DE Interaction: Q08881; IntAct: EBI-297353,EBI-968552; Score: 0.55 DE Interaction: P07949; IntAct: EBI-297353,EBI-2480756; Score: 0.55 DE Interaction: Q05209; IntAct: EBI-297353,EBI-2266035; Score: 0.81 DE Interaction: O43707; IntAct: EBI-351526,EBI-297353; Score: 0.55 DE Interaction: Q9UGK3; IntAct: EBI-297353,EBI-1553984; Score: 0.55 DE Interaction: P15311; IntAct: EBI-297353,EBI-1056902; Score: 0.55 DE Interaction: Q16620; IntAct: EBI-297353,EBI-3904881; Score: 0.55 DE Interaction: P01135; IntAct: EBI-1034374,EBI-297353; Score: 0.78 DE Interaction: P41240; IntAct: EBI-297353,EBI-1380630; Score: 0.68 DE Interaction: P31749; IntAct: EBI-297353,EBI-296087; Score: 0.55 DE Interaction: P04049; IntAct: EBI-365996,EBI-297353; Score: 0.55 DE Interaction: P11309; IntAct: EBI-297353,EBI-696621; Score: 0.55 DE Interaction: P23528; IntAct: EBI-352733,EBI-297353; Score: 0.67 DE Interaction: Q16539; IntAct: EBI-73946,EBI-297353; Score: 0.40 DE Interaction: P01133; IntAct: EBI-297353,EBI-640857; Score: 0.97 DE Interaction: P27986; IntAct: EBI-79464,EBI-297353; Score: 0.78 DE Interaction: P01100; IntAct: EBI-297353,EBI-852851; Score: 0.40 DE Interaction: Q8K424; IntAct: EBI-297353,EBI-2650739; Score: 0.40 DE Interaction: Q86VI4; IntAct: EBI-297353,EBI-3267258; Score: 0.60 DE Interaction: Q9UPT5; IntAct: EBI-297353,EBI-720048; Score: 0.46 DE Interaction: Q96A65; IntAct: EBI-355383,EBI-297353; Score: 0.50 DE Interaction: Q8IYI6; IntAct: EBI-742102,EBI-297353; Score: 0.40 DE Interaction: Q80U62; IntAct: EBI-3506572,EBI-297353; Score: 0.50 DE Interaction: O54921; IntAct: EBI-297353,EBI-1036795; Score: 0.35 DE Interaction: Q96KP1; IntAct: EBI-465715,EBI-297353; Score: 0.40 DE Interaction: P36895; IntAct: EBI-2551936,EBI-297353; Score: 0.35 DE Interaction: Q92889; IntAct: EBI-297353,EBI-2370770; Score: 0.35 DE Interaction: P19338; IntAct: EBI-297353,EBI-346967; Score: 0.35 DE Interaction: Q13263; IntAct: EBI-297353,EBI-78139; Score: 0.35 DE Interaction: P02545; IntAct: EBI-297353,EBI-351935; Score: 0.35 DE Interaction: P07992; IntAct: EBI-297353,EBI-750962; Score: 0.60 DE Interaction: Q12906; IntAct: EBI-297353,EBI-78756; Score: 0.35 DE Interaction: P33991; IntAct: EBI-297353,EBI-374938; Score: 0.35 DE Interaction: Q12905; IntAct: EBI-297353,EBI-357925; Score: 0.35 DE Interaction: P11387; IntAct: EBI-297353,EBI-876302; Score: 0.35 DE Interaction: P35637; IntAct: EBI-297353,EBI-400434; Score: 0.35 DE Interaction: P06748; IntAct: EBI-297353,EBI-78579; Score: 0.35 DE Interaction: P09874; IntAct: EBI-297353,EBI-355676; Score: 0.35 DE Interaction: P27695; IntAct: EBI-297353,EBI-1048805; Score: 0.35 DE Interaction: Q9NXR7; IntAct: EBI-297353,EBI-949389; Score: 0.35 DE Interaction: Q08211; IntAct: EBI-297353,EBI-352022; Score: 0.35 DE Interaction: Q14566; IntAct: EBI-297353,EBI-374900; Score: 0.35 DE Interaction: P39748; IntAct: EBI-297353,EBI-707816; Score: 0.35 DE Interaction: P25205; IntAct: EBI-297353,EBI-355153; Score: 0.35 DE Interaction: P18074; IntAct: EBI-297353,EBI-6380590; Score: 0.35 DE Interaction: P30530; IntAct: EBI-2850927,EBI-297353; Score: 0.52 DE Interaction: Q15262-2; IntAct: EBI-21518251,EBI-297353; Score: 0.35 DE Interaction: P59665; IntAct: EBI-726336,EBI-297353; Score: 0.35 DE Interaction: Q92187; IntAct: EBI-21513582,EBI-297353; Score: 0.35 DE Interaction: Q15165-1; IntAct: EBI-16813978,EBI-297353; Score: 0.35 DE Interaction: P46940; IntAct: EBI-297353,EBI-297509; Score: 0.63 DE Interaction: P06396; IntAct: EBI-351506,EBI-297353; Score: 0.55 DE Interaction: O15511; IntAct: EBI-352975,EBI-297353; Score: 0.55 DE Interaction: O75368; IntAct: EBI-2854777,EBI-297353; Score: 0.68 DE Interaction: Q9H299; IntAct: EBI-297353,EBI-5234893; Score: 0.55 DE Interaction: Q15819; IntAct: EBI-714329,EBI-297353; Score: 0.55 DE Interaction: Q15005; IntAct: EBI-297353,EBI-1043352; Score: 0.55 DE Interaction: Q14204; IntAct: EBI-356015,EBI-297353; Score: 0.55 DE Interaction: Q12852; IntAct: EBI-297353,EBI-710223; Score: 0.62 DE Interaction: Q06830; IntAct: EBI-353193,EBI-297353; Score: 0.55 DE Interaction: Q02952; IntAct: EBI-297353,EBI-2562430; Score: 0.63 DE Interaction: Q02790; IntAct: EBI-297353,EBI-1047444; Score: 0.55 DE Interaction: Q02246; IntAct: EBI-297353,EBI-4397248; Score: 0.55 DE Interaction: P60520; IntAct: EBI-720116,EBI-297353; Score: 0.63 DE Interaction: P60174; IntAct: EBI-717475,EBI-297353; Score: 0.55 DE Interaction: P54368; IntAct: EBI-948441,EBI-297353; Score: 0.55 DE Interaction: P43243; IntAct: EBI-297353,EBI-352602; Score: 0.55 DE Interaction: P40925; IntAct: EBI-709625,EBI-297353; Score: 0.55 DE Interaction: P31948; IntAct: EBI-297353,EBI-1054052; Score: 0.63 DE Interaction: P31939; IntAct: EBI-297353,EBI-1048599; Score: 0.55 DE Interaction: P26641; IntAct: EBI-297353,EBI-351467; Score: 0.55 DE Interaction: P20336; IntAct: EBI-297353,EBI-1045943; Score: 0.55 DE Interaction: P17174; IntAct: EBI-297353,EBI-727329; Score: 0.55 DE Interaction: P16930; IntAct: EBI-4397076,EBI-297353; Score: 0.55 DE Interaction: P14625; IntAct: EBI-297353,EBI-359129; Score: 0.55 DE Interaction: P06132; IntAct: EBI-2871776,EBI-297353; Score: 0.55 DE Interaction: P04075; IntAct: EBI-709613,EBI-297353; Score: 0.55 DE Interaction: O95433; IntAct: EBI-448610,EBI-297353; Score: 0.55 DE Interaction: O94992; IntAct: EBI-2832510,EBI-297353; Score: 0.55 DE Interaction: O00170; IntAct: EBI-297353,EBI-704197; Score: 0.55 DE Interaction: Q9Y2H9; IntAct: EBI-297353,EBI-3385920; Score: 0.63 DE Interaction: Q9P0L0; IntAct: EBI-1059156,EBI-297353; Score: 0.63 DE Interaction: Q99784; IntAct: EBI-297353,EBI-1105073; Score: 0.55 DE Interaction: Q92733; IntAct: EBI-4397741,EBI-297353; Score: 0.55 DE Interaction: Q8N4S1; IntAct: EBI-1105197,EBI-297353; Score: 0.37 DE Interaction: Q8N111; IntAct: EBI-297353,EBI-946825; Score: 0.55 DE Interaction: A4FU49; IntAct: EBI-297353,EBI-4397635; Score: 0.55 DE Interaction: P17600; IntAct: EBI-297353,EBI-717274; Score: 0.55 DE Interaction: Q59GR8; IntAct: EBI-4397587,EBI-297353; Score: 0.55 DE Interaction: Q6UWJ1; IntAct: EBI-297353,EBI-4397667; Score: 0.55 DE Interaction: Q59EJ3; IntAct: EBI-4397543,EBI-297353; Score: 0.55 DE Interaction: P53041; IntAct: EBI-297353,EBI-716663; Score: 0.55 DE Interaction: Q16186; IntAct: EBI-954387,EBI-297353; Score: 0.55 DE Interaction: Q15120; IntAct: EBI-1383915,EBI-297353; Score: 0.55 DE Interaction: Q14318; IntAct: EBI-724839,EBI-297353; Score: 0.68 DE Interaction: Q14050; IntAct: EBI-2528281,EBI-297353; Score: 0.55 DE Interaction: Q13561; IntAct: EBI-297353,EBI-715074; Score: 0.55 DE Interaction: Q13491; IntAct: EBI-4397339,EBI-297353; Score: 0.55 DE Interaction: P62330; IntAct: EBI-297353,EBI-638181; Score: 0.55 DE Interaction: P55036; IntAct: EBI-297353,EBI-359318; Score: 0.55 DE Interaction: P49908; IntAct: EBI-297353,EBI-2623058; Score: 0.55 DE Interaction: P41222; IntAct: EBI-297353,EBI-948821; Score: 0.55 DE Interaction: P31321; IntAct: EBI-297353,EBI-2805516; Score: 0.55 DE Interaction: P16152; IntAct: EBI-351348,EBI-297353; Score: 0.55 DE Interaction: P21291; IntAct: EBI-3959636,EBI-297353; Score: 0.55 DE Interaction: P09936; IntAct: EBI-714860,EBI-297353; Score: 0.63 DE Interaction: O14818; IntAct: EBI-603272,EBI-297353; Score: 0.55 DE Interaction: O75095; IntAct: EBI-297353,EBI-947597; Score: 0.55 DE Interaction: Q9Y3A3; IntAct: EBI-297353,EBI-713935; Score: 0.55 DE Interaction: Q9Y237; IntAct: EBI-297353,EBI-714599; Score: 0.55 DE Interaction: Q96AD5; IntAct: EBI-716499,EBI-297353; Score: 0.55 DE Interaction: Q9NNZ3; IntAct: EBI-297353,EBI-4397791; Score: 0.55 DE Interaction: Q99608; IntAct: EBI-718177,EBI-297353; Score: 0.55 DE Interaction: Q8TDB4; IntAct: EBI-4397720,EBI-297353; Score: 0.55 DE Interaction: Q8N2Y8; IntAct: EBI-722486,EBI-297353; Score: 0.55 DE Interaction: Q7L273; IntAct: EBI-4397613,EBI-297353; Score: 0.55 DE Interaction: Q59G22; IntAct: EBI-297353,EBI-4397561; Score: 0.55 DE Interaction: Q53GZ6; IntAct: EBI-4397518,EBI-297353; Score: 0.55 DE Interaction: P60880; IntAct: EBI-297353,EBI-524785; Score: 0.55 DE Interaction: P52306; IntAct: EBI-746389,EBI-297353; Score: 0.55 DE Interaction: Q4KWH8; IntAct: EBI-297353,EBI-4397439; Score: 0.55 DE Interaction: P02751; IntAct: EBI-1220319,EBI-297353; Score: 0.40 DE Interaction: Q01973; IntAct: EBI-297353,EBI-6082337; Score: 0.58 DE Interaction: Q8ZE20; IntAct: EBI-2857666,EBI-297353; Score: 0.37 DE Interaction: Q81NA2; IntAct: EBI-2810080,EBI-297353; Score: 0.37 DE Interaction: Q5NEB4; IntAct: EBI-297353,EBI-2797653; Score: 0.37 DE Interaction: P05026; IntAct: EBI-297353,EBI-714630; Score: 0.35 DE Interaction: P53675; IntAct: EBI-297353,EBI-358826; Score: 0.35 DE Interaction: Q13740; IntAct: EBI-297353,EBI-1188108; Score: 0.35 DE Interaction: Q9NYD6; IntAct: EBI-297353,EBI-1188075; Score: 0.35 DE Interaction: P05362; IntAct: EBI-297353,EBI-1035358; Score: 0.35 DE Interaction: P55735; IntAct: EBI-297353,EBI-1046596; Score: 0.35 DE Interaction: P06702; IntAct: EBI-297353,EBI-1055001; Score: 0.35 DE Interaction: P05023; IntAct: EBI-297353,EBI-358778; Score: 0.35 DE Interaction: P09496; IntAct: EBI-297353,EBI-1171169; Score: 0.35 DE Interaction: Q9UQC2; IntAct: EBI-975200,EBI-297353; Score: 0.67 DE Interaction: O43147; IntAct: EBI-712398,EBI-297353; Score: 0.37 DE Interaction: P36542; IntAct: EBI-297353,EBI-711768; Score: 0.37 DE Interaction: O55156; IntAct: EBI-297353,EBI-349416; Score: 0.35 DE Interaction: Q00972; IntAct: EBI-297353,EBI-593839; Score: 0.35 DE Interaction: P15651; IntAct: EBI-297353,EBI-916589; Score: 0.35 DE Interaction: P62994; IntAct: EBI-297353,EBI-401775; Score: 0.56 DE Interaction: D3ZG10; IntAct: EBI-297353,EBI-22237528; Score: 0.35 DE Interaction: P32577; IntAct: EBI-297353,EBI-7482976; Score: 0.35 DE Interaction: Q6AZ23; IntAct: EBI-297353,EBI-22241493; Score: 0.35 DE Interaction: A0A0G2K064; IntAct: EBI-297353,EBI-22154492; Score: 0.35 DE Interaction: P24155; IntAct: EBI-297353,EBI-6372841; Score: 0.35 DE Interaction: P84083; IntAct: EBI-297353,EBI-916985; Score: 0.35 DE Interaction: Q5U2U2; IntAct: EBI-297353,EBI-976752; Score: 0.35 DE Interaction: D3ZYG0; IntAct: EBI-297353,EBI-22084151; Score: 0.35 DE Interaction: Q7TT49; IntAct: EBI-297353,EBI-692673; Score: 0.35 DE Interaction: Q62985; IntAct: EBI-297353,EBI-7395583; Score: 0.35 DE Interaction: A9CMB8; IntAct: EBI-297353,EBI-22241848; Score: 0.35 DE Interaction: P50116; IntAct: EBI-297353,EBI-22241807; Score: 0.35 DE Interaction: O15357; IntAct: EBI-297353,EBI-1384248; Score: 0.35 DE Interaction: Q9UKW4; IntAct: EBI-297353,EBI-297568; Score: 0.35 DE Interaction: Q63768; IntAct: EBI-297353,EBI-8423843; Score: 0.35 DE Interaction: P54100; IntAct: EBI-297353,EBI-22084104; Score: 0.35 DE Interaction: F1LWB1; IntAct: EBI-297353,EBI-22084199; Score: 0.35 DE Interaction: Q64725; IntAct: EBI-297353,EBI-2615512; Score: 0.35 DE Interaction: Q9WVR3; IntAct: EBI-297353,EBI-920167; Score: 0.35 DE Interaction: Q5RJK6; IntAct: EBI-297353,EBI-22084302; Score: 0.35 DE Interaction: F1LNG5; IntAct: EBI-297353,EBI-22085642; Score: 0.35 DE Interaction: G3V7X3; IntAct: EBI-297353,EBI-22085594; Score: 0.35 DE Interaction: Q9QZC5; IntAct: EBI-297353,EBI-22085551; Score: 0.50 DE Interaction: P50904; IntAct: EBI-297353,EBI-5747849; Score: 0.35 DE Interaction: P41499; IntAct: EBI-297353,EBI-7180604; Score: 0.35 DE Interaction: Q9WUD9-2; IntAct: EBI-297353,EBI-22179963; Score: 0.35 DE Interaction: Q9WUD9; IntAct: EBI-297353,EBI-7784541; Score: 0.35 DE Interaction: Q8CFN2; IntAct: EBI-297353,EBI-7023929; Score: 0.35 DE Interaction: A0A0G2K3B0; IntAct: EBI-297353,EBI-22180056; Score: 0.35 DE Interaction: A0A0G2JSR4; IntAct: EBI-297353,EBI-22156317; Score: 0.35 DE Interaction: Q5XI26; IntAct: EBI-297353,EBI-22150963; Score: 0.35 DE Interaction: F1M9D6; IntAct: EBI-297353,EBI-15667209; Score: 0.35 DE Interaction: Q8K4S7; IntAct: EBI-297353,EBI-8536678; Score: 0.35 DE Interaction: D3ZY64; IntAct: EBI-297353,EBI-22236644; Score: 0.35 DE Interaction: B2GV15; IntAct: EBI-297353,EBI-16219426; Score: 0.35 DE Interaction: D3ZV15; IntAct: EBI-297353,EBI-21998185; Score: 0.35 DE Interaction: P24135; IntAct: EBI-297353,EBI-22236548; Score: 0.35 DE Interaction: P10686; IntAct: EBI-297353,EBI-520788; Score: 0.35 DE Interaction: E9PT59; IntAct: EBI-297353,EBI-22237732; Score: 0.35 DE Interaction: D4A3T0; IntAct: EBI-297353,EBI-11702585; Score: 0.35 DE Interaction: P59622; IntAct: EBI-297353,EBI-22237808; Score: 0.35 DE Interaction: Q8R424; IntAct: EBI-297353,EBI-22237695; Score: 0.35 DE Interaction: F1M3E4; IntAct: EBI-297353,EBI-22237648; Score: 0.35 DE Interaction: Q920L0; IntAct: EBI-297353,EBI-22237619; Score: 0.35 DE Interaction: Q4KM68; IntAct: EBI-297353,EBI-22237548; Score: 0.35 DE Interaction: Q9EQH1; IntAct: EBI-297353,EBI-7620518; Score: 0.35 DE Interaction: P97573; IntAct: EBI-297353,EBI-8008869; Score: 0.35 DE Interaction: P85968; IntAct: EBI-297353,EBI-22237670; Score: 0.35 DE Interaction: D4A5Q1; IntAct: EBI-297353,EBI-22236396; Score: 0.35 DE Interaction: P52631; IntAct: EBI-297353,EBI-10764775; Score: 0.35 DE Interaction: Q63788; IntAct: EBI-297353,EBI-22237563; Score: 0.35 DE Interaction: P08461; IntAct: EBI-297353,EBI-916164; Score: 0.35 DE Interaction: A0A0R4J8U1; IntAct: EBI-297353,EBI-22236360; Score: 0.35 DE Interaction: Q63065; IntAct: EBI-297353,EBI-7383638; Score: 0.35 DE Interaction: Q5M824; IntAct: EBI-297353,EBI-7152521; Score: 0.35 DE Interaction: Q32PX8; IntAct: EBI-297353,EBI-22237992; Score: 0.35 DE Interaction: B5DFI9; IntAct: EBI-297353,EBI-22237955; Score: 0.35 DE Interaction: F1M9C0; IntAct: EBI-297353,EBI-22237909; Score: 0.35 DE Interaction: D3Z8I4; IntAct: EBI-297353,EBI-22237883; Score: 0.35 DE Interaction: P52632; IntAct: EBI-297353,EBI-15667283; Score: 0.35 DE Interaction: Q5BK11; IntAct: EBI-297353,EBI-22237117; Score: 0.35 DE Interaction: F1MAF2; IntAct: EBI-297353,EBI-22251970; Score: 0.35 DE Interaction: Q58FF7; IntAct: EBI-297353,EBI-9996483; Score: 0.35 DE Interaction: P09651; IntAct: EBI-297353,EBI-352662; Score: 0.35 DE Interaction: Q32P51; IntAct: EBI-297353,EBI-2556580; Score: 0.35 DE Interaction: P17844; IntAct: EBI-297353,EBI-351962; Score: 0.35 DE Interaction: P61221; IntAct: EBI-297353,EBI-2510446; Score: 0.35 DE Interaction: Q8IXB1; IntAct: EBI-297353,EBI-2949763; Score: 0.35 DE Interaction: P60709; IntAct: EBI-297353,EBI-353944; Score: 0.35 DE Interaction: Q15208; IntAct: EBI-297353,EBI-458376; Score: 0.35 DE Interaction: Q16875; IntAct: EBI-297353,EBI-764464; Score: 0.35 DE Interaction: Q9UHB6; IntAct: EBI-297353,EBI-351479; Score: 0.35 DE Interaction: Q9ULV4; IntAct: EBI-297353,EBI-351384; Score: 0.35 DE Interaction: Q9Y383; IntAct: EBI-297353,EBI-352851; Score: 0.35 DE Interaction: P23469; IntAct: EBI-2258070,EBI-297353; Score: 0.37 DE Interaction: Q6ZWB6; IntAct: EBI-6426198,EBI-297353; Score: 0.37 DE Interaction: Q14515; IntAct: EBI-2682673,EBI-297353; Score: 0.37 DE Interaction: P18433; IntAct: EBI-2609645,EBI-297353; Score: 0.63 DE Interaction: P0DMV8; IntAct: EBI-11052499,EBI-297353; Score: 0.37 DE Interaction: Q96JA1; IntAct: EBI-297353,EBI-2865191; Score: 0.74 DE Interaction: O14944; IntAct: EBI-17272224,EBI-297353; Score: 0.62 DE Interaction: Q6UW88; IntAct: EBI-15482510,EBI-297353; Score: 0.62 DE Interaction: Q99075; IntAct: EBI-7211558,EBI-297353; Score: 0.61 DE Interaction: P35070; IntAct: EBI-297353,EBI-25434897; Score: 0.44 DE Interaction: P15514; IntAct: EBI-297353,EBI-953674; Score: 0.44 DE Interaction: O94898; IntAct: EBI-297353,EBI-2830372; Score: 0.46 DE Interaction: P60033; IntAct: EBI-712921,EBI-297353; Score: 0.46 DE Interaction: P33992; IntAct: EBI-297353,EBI-359410; Score: 0.35 DE Interaction: P33993; IntAct: EBI-297353,EBI-355924; Score: 0.35 DE Interaction: P07948-1; IntAct: EBI-297353,EBI-6895930; Score: 0.54 DE Interaction: P07948-2; IntAct: EBI-297353,EBI-3951572; Score: 0.40 DE Interaction: Q8NBJ4; IntAct: EBI-712073,EBI-297353; Score: 0.64 DE Interaction: P62491; IntAct: EBI-745098,EBI-297353; Score: 0.40 DE Interaction: P46098-2; IntAct: EBI-21749217,EBI-297353; Score: 0.35 DE Interaction: Q13635-2; IntAct: EBI-21717270,EBI-297353; Score: 0.35 DE Interaction: Q6XE38; IntAct: EBI-21823017,EBI-297353; Score: 0.35 DE Interaction: Q9Y5F2; IntAct: EBI-21658546,EBI-297353; Score: 0.35 DE Interaction: Q15303; IntAct: EBI-80371,EBI-297353; Score: 0.40 DE Interaction: P02533; IntAct: EBI-297353,EBI-702178; Score: 0.35 DE Interaction: P10809; IntAct: EBI-297353,EBI-352528; Score: 0.35 DE Interaction: P31689; IntAct: EBI-297353,EBI-347834; Score: 0.35 DE Interaction: P68104; IntAct: EBI-297353,EBI-352162; Score: 0.35 DE Interaction: Q99959; IntAct: EBI-297353,EBI-702235; Score: 0.35 DE Interaction: Q04695; IntAct: EBI-297353,EBI-297873; Score: 0.35 DE Interaction: P13647; IntAct: EBI-297353,EBI-702187; Score: 0.35 DE Interaction: P05141; IntAct: EBI-297353,EBI-355133; Score: 0.35 DE Interaction: P22681; IntAct: EBI-297353,EBI-518228; Score: 0.96 DE Interaction: P10412; IntAct: EBI-297353,EBI-358163; Score: 0.35 DE Interaction: Q14289; IntAct: EBI-297353,EBI-298640; Score: 0.35 DE Interaction: P29317; IntAct: EBI-297353,EBI-702104; Score: 0.35 DE Interaction: Q9NR50; IntAct: EBI-297353,EBI-702257; Score: 0.35 DE Interaction: Q96EY1; IntAct: EBI-297353,EBI-356767; Score: 0.35 DE Interaction: P40855; IntAct: EBI-297353,EBI-594747; Score: 0.35 DE Interaction: P61978; IntAct: EBI-297353,EBI-304185; Score: 0.35 DE Interaction: P02538; IntAct: EBI-297353,EBI-702198; Score: 0.35 DE Interaction: P49023; IntAct: EBI-297353,EBI-702209; Score: 0.35 DE Interaction: P62807; IntAct: EBI-297353,EBI-354552; Score: 0.35 DE Interaction: P52597; IntAct: EBI-297353,EBI-352986; Score: 0.35 DE Interaction: P04264; IntAct: EBI-297353,EBI-298429; Score: 0.35 DE Interaction: Q14974; IntAct: EBI-297353,EBI-286758; Score: 0.35 DE Interaction: P98172; IntAct: EBI-297353,EBI-538287; Score: 0.35 DE Interaction: Q13191; IntAct: EBI-297353,EBI-744027; Score: 0.35 DE Interaction: P62258; IntAct: EBI-297353,EBI-356498; Score: 0.35 DE Interaction: Q14192; IntAct: EBI-297353,EBI-701903; Score: 0.35 DE Interaction: P31949; IntAct: EBI-297353,EBI-701862; Score: 0.35 DE Interaction: P07947; IntAct: EBI-297353,EBI-515331; Score: 0.56 DE Interaction: Q07065; IntAct: EBI-297353,EBI-702400; Score: 0.35 DE Interaction: Q9UBB4; IntAct: EBI-297353,EBI-702390; Score: 0.35 DE Interaction: Q14134; IntAct: EBI-297353,EBI-702370; Score: 0.35 DE Interaction: Q96AG4; IntAct: EBI-297353,EBI-358888; Score: 0.35 DE Interaction: Q9H5V8; IntAct: EBI-297353,EBI-1019736; Score: 0.35 DE Interaction: Q07912; IntAct: EBI-297353,EBI-603457; Score: 0.35 DE Interaction: O75815; IntAct: EBI-297353,EBI-702336; Score: 0.35 DE Interaction: Q969Z0; IntAct: EBI-297353,EBI-702328; Score: 0.35 DE Interaction: P06576; IntAct: EBI-297353,EBI-356231; Score: 0.35 DE Interaction: O43592; IntAct: EBI-297353,EBI-286683; Score: 0.35 DE Interaction: P54760; IntAct: EBI-297353,EBI-702121; Score: 0.35 DE Interaction: P0CG47; IntAct: EBI-297353,EBI-413034; Score: 0.35 DE Interaction: P55060; IntAct: EBI-297353,EBI-286709; Score: 0.35 DE Interaction: P56945; IntAct: EBI-297353,EBI-702093; Score: 0.35 DE Interaction: P07437; IntAct: EBI-297353,EBI-350864; Score: 0.35 DE Interaction: P22682; IntAct: EBI-640919,EBI-297353; Score: 0.50 DE Interaction: O00443; IntAct: EBI-297353,EBI-641094; Score: 0.35 DE Interaction: P68431; IntAct: EBI-297353,EBI-79722; Score: 0.27 DE Interaction: P13987; IntAct: EBI-297353,EBI-297972; Score: 0.44 DE Interaction: P98083; IntAct: EBI-297353,EBI-300201; Score: 0.40 DE Interaction: Q17R13; IntAct: EBI-457220,EBI-297353; Score: 0.35 GO GO:0016324; GO GO:0009925; GO GO:0016323; GO GO:0030054; GO GO:0009986; GO GO:0030665; GO GO:0005737; GO GO:0031901; GO GO:0030139; GO GO:0005789; GO GO:0005768; GO GO:0010008; GO GO:0005615; GO GO:0005925; GO GO:0000139; GO GO:0005887; GO GO:0016020; GO GO:0045121; GO GO:0097489; GO GO:0031965; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0032991; GO GO:0043235; GO GO:0070435; GO GO:0045202; GO GO:0051015; GO GO:0005524; GO GO:0051117; GO GO:0045296; GO GO:0005516; GO GO:0003682; GO GO:0003690; GO GO:0019899; GO GO:0048408; GO GO:0005006; GO GO:0042802; GO GO:0005178; GO GO:0004709; GO GO:0019901; GO GO:0019903; GO GO:0004713; GO GO:0004714; GO GO:0004888; GO GO:0031625; GO GO:0001618; GO GO:0043006; GO GO:0007202; GO GO:0048143; GO GO:0030154; GO GO:0007166; GO GO:0098609; GO GO:0071230; GO GO:0071276; GO GO:0071549; GO GO:0071364; GO GO:0071392; GO GO:0071260; GO GO:0034614; GO GO:0021795; GO GO:0007623; GO GO:0048546; GO GO:0016101; GO GO:0001892; GO GO:0007173; GO GO:0038128; GO GO:0061029; GO GO:0001942; GO GO:0042743; GO GO:0007611; GO GO:0097421; GO GO:0030324; GO GO:0010960; GO GO:0000165; GO GO:0061024; GO GO:0007494; GO GO:0060571; GO GO:0007275; GO GO:0043066; GO GO:1905208; GO GO:0042059; GO GO:1901185; GO GO:0045930; GO GO:0045746; GO GO:0042177; GO GO:0048812; GO GO:0001503; GO GO:0042698; GO GO:0038083; GO GO:0018108; GO GO:0097755; GO GO:0045780; GO GO:0090263; GO GO:0030307; GO GO:0030335; GO GO:0008284; GO GO:0045737; GO GO:0045739; GO GO:0045740; GO GO:0050679; GO GO:0070374; GO GO:0048146; GO GO:1900087; GO GO:0050729; GO GO:0033674; GO GO:0043406; GO GO:1901224; GO GO:0010750; GO GO:0033138; GO GO:0042327; GO GO:1903800; GO GO:1902722; GO GO:0051897; GO GO:1900020; GO GO:1903078; GO GO:0001934; GO GO:0048661; GO GO:0032930; GO GO:0051968; GO GO:0045944; GO GO:0045893; GO GO:0045907; GO GO:0046777; GO GO:0051205; GO GO:2000145; GO GO:0070372; GO GO:0046328; GO GO:0050999; GO GO:0050730; GO GO:0014066; GO GO:0006357; GO GO:0051592; GO GO:0033590; GO GO:0033594; GO GO:0006970; GO GO:0070141; GO GO:0007435; GO GO:0007165; GO GO:0043586; GO GO:0006412; GO GO:0007169; GO GO:0042060; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLK SQ TIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVE SQ SIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC SQ TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE SQ DGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKE SQ ITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL SQ FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHP SQ ECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNG SQ PKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS SQ GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLD SQ YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKW SQ MALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK SQ FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSA SQ TSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPS SQ RDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV SQ APQSSEFIGA // 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 P03084; PN Agnoprotein; GN AGNO; OS 1891767; 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:0000269|PubMed:6296448}. DR UNIPROT: P03084; 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, ECO:0000269|PubMed:3023658, ECO:0000269|PubMed:3023661, ECO:0000269|PubMed:6286139}. 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 MVLRRLSRQASVKVRRSWTESKKTAQRLFVFVLELLLQFCEGEDTVDGKRKKPERLTEKPES // ID P03086; PN Agnoprotein; GN AGNO; OS 10632; 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:0000269|PubMed:11517407, ECO:0000269|PubMed:15864296, ECO:0000269|PubMed:20300659}. DR UNIPROT: P03086; DR PDB: 2MJ2; DR PDB: 5NHQ; 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. {ECO:0000269|PubMed:11517407, ECO:0000269|PubMed:12165856, ECO:0000269|PubMed:20300659}. DE Reference Proteome: No; 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 MVLRQLSRKASVKVSKTWSGTKKRAQRILIFLLEFLLDFCTGEDSVDGKKRQRHSGLTEQTYSALPEPKAT // 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 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 P03246; PN E1B protein, small T-antigen; GN E1BS; OS 28285; SL Nucleus Position: SL-0415; SL Nucleus Position: SL-0416; SL Comments: Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. DR UNIPROT: P03246; 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. 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 MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKT SQ LDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRR SQ QEQSPWNPRAGLDPRE // 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 P03263; PN I-leader protein; GN LEAD; OS 10515; SL Nucleus Position: SL-0382; SL Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:3005631}. Note=Might be loosely associated with the nuclear membrane. DR UNIPROT: P03263; DR Pfam: PF03052; DE Function: DE Reference Proteome: Yes; GO GO:0044220; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MRADREELDLPPPVGGVAVDVVKVEVPATGRTLVLAFVKTCAVLAAVHGLYILHEVDLTTAHKEAEWEFEPLAWRVWLVV SQ FYFGCLSLTVWLLEGSYGGSDHHAARAQSPDVRARRSELDDNIAQMGAVHGLELPRRQVLRHRGT // 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 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 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 P04492; PN E1B protein, small T-antigen; GN E1BS; OS 28282; 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: P04492; 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: Yes; GO GO:0044203; GO GO:0020002; GO GO:0016020; GO GO:0019050; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MELETVLQSFQSVRQLLQYTSKNTSGFWRYLFGSTLSKVVNRVKEDYREEFENILADCPGLLASLDLCYHLVFQEKVVRS SQ LDFSSVGRTVASIAFLATILDKWSEKSHLSWDYMLDYMSMQLWRAWLKRRVCIYSLARPLTMPPLPTLQEEKEEERNPAV SQ VEK // 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 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 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 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 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 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 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 P06704; PN Cell division control protein 31; GN CDC31; OS 559292; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Spindle pole body, SPB half- bridge. DR UNIPROT: P06704; DR UNIPROT: D6W2V8; DR PDB: 2DOQ; DR PDB: 2GV5; DR PDB: 3FWB; DR PDB: 3FWC; DR PDB: 4MBE; DR Pfam: PF13499; DR PROSITE: PS00018; DR PROSITE: PS50222; DE Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity. {ECO:0000269|PubMed:11156974, ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:8070654, ECO:0000269|PubMed:8188750, ECO:0000269|PubMed:9813095}. DE Reference Proteome: Yes; DE Interaction: Q00684; IntAct: EBI-4192,EBI-4259; Score: 0.35 DE Interaction: P14832; IntAct: EBI-5463,EBI-4259; Score: 0.35 DE Interaction: P32472; IntAct: EBI-2883297,EBI-4259; Score: 0.35 DE Interaction: Q02959; IntAct: EBI-8484,EBI-4259; Score: 0.59 DE Interaction: P02293; IntAct: EBI-8088,EBI-4259; Score: 0.35 DE Interaction: Q02796; IntAct: EBI-30514,EBI-4259; Score: 0.35 DE Interaction: Q02206; IntAct: EBI-16204,EBI-4259; Score: 0.35 DE Interaction: P38890; IntAct: EBI-24263,EBI-4259; Score: 0.35 DE Interaction: P25302; IntAct: EBI-18626,EBI-4259; Score: 0.35 DE Interaction: P11484; IntAct: EBI-4259,EBI-8627; Score: 0.35 DE Interaction: P10591; IntAct: EBI-4259,EBI-8591; Score: 0.35 DE Interaction: Q06677; IntAct: EBI-4259,EBI-30084; Score: 0.35 DE Interaction: P32447; IntAct: EBI-3003,EBI-4259; Score: 0.35 DE Interaction: Q07457; IntAct: EBI-31563,EBI-4259; Score: 0.35 DE Interaction: P26448; IntAct: EBI-3824,EBI-4259; Score: 0.35 DE Interaction: P38915; IntAct: EBI-17964,EBI-4259; Score: 0.35 DE Interaction: Q12060; IntAct: EBI-8287,EBI-4259; Score: 0.35 DE Interaction: P39723; IntAct: EBI-20675,EBI-4259; Score: 0.35 DE Interaction: Q04477; IntAct: EBI-27228,EBI-4259; Score: 0.35 DE Interaction: P46675; IntAct: EBI-18471,EBI-4259; Score: 0.35 DE Interaction: P50102; IntAct: EBI-19863,EBI-4259; Score: 0.35 DE Interaction: Q6WNK7; IntAct: EBI-1251050,EBI-4259; Score: 0.76 DE Interaction: Q99181; IntAct: EBI-4259,EBI-8579; Score: 0.37 DE Interaction: P38305; IntAct: EBI-20939,EBI-4259; Score: 0.40 GO GO:0005737; GO GO:0005825; GO GO:0005815; GO GO:0044732; GO GO:0005643; GO GO:0070390; GO GO:0005509; GO GO:0042802; GO GO:0008017; GO GO:0051301; GO GO:0051028; GO GO:0043161; GO GO:0015031; GO GO:0043549; GO GO:0030474; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDD SQ FYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTD SQ S // 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 P07663; PN Period circadian protein; GN per; OS 7227; SL Nucleus Position: SL-0198; SL Comments: Nucleus. Cytoplasm, perinuclear region. 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. DR UNIPROT: P07663; DR UNIPROT: O17483; DR UNIPROT: O76882; DR UNIPROT: O76883; DR UNIPROT: O76884; DR UNIPROT: O76885; DR UNIPROT: Q24446; DR UNIPROT: Q24447; DR UNIPROT: Q24448; DR UNIPROT: Q24449; DR UNIPROT: Q6PVA3; DR UNIPROT: Q8MLY0; DR UNIPROT: Q9GN20; DR UNIPROT: Q9GN51; DR UNIPROT: Q9GQH9; DR UNIPROT: Q9GV48; DR UNIPROT: Q9GV53; DR UNIPROT: Q9GV54; DR UNIPROT: Q9GV55; DR UNIPROT: Q9W4X0; DR PDB: 1WA9; DR PDB: 3GEC; DR PDB: 3RTY; 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. Required for binding of cwo to the E box regions in the promoters of target genes of the transcriptional activator Clock, probably by binding to Clock-cycle heterodimers, reducing their affinity for E box binding and allowing cwo to bind instead (PubMed:27814361). {ECO:0000269|PubMed:27814361}. DE Reference Proteome: Yes; DE Interaction: O77059; IntAct: EBI-496170,EBI-94117; Score: 0.27 DE Interaction: Self; IntAct: EBI-496170,EBI-496170; Score: 0.27 DE Interaction: Q7JWQ7; IntAct: EBI-89424,EBI-496170; Score: 0.37 DE Interaction: Q26416; IntAct: EBI-176027,EBI-496170; Score: 0.37 DE Interaction: P49021; IntAct: EBI-266295,EBI-496170; Score: 0.50 DE Interaction: P49021-3; IntAct: EBI-266326,EBI-496170; Score: 0.37 DE Interaction: P33438; IntAct: EBI-496159,EBI-496170; Score: 0.37 DE Interaction: Q9VB55; IntAct: EBI-184355,EBI-496170; Score: 0.37 DE Interaction: Q9VXJ0; IntAct: EBI-85627,EBI-496170; Score: 0.37 DE Interaction: P11996; IntAct: EBI-124104,EBI-496170; Score: 0.37 DE Interaction: Q9VTW8; IntAct: EBI-131131,EBI-496170; Score: 0.37 DE Interaction: Q9VLX9; IntAct: EBI-179831,EBI-496170; Score: 0.37 DE Interaction: O61735; IntAct: EBI-496170,EBI-143834; Score: 0.27 DE Interaction: Q24533; IntAct: EBI-147892,EBI-496170; Score: 0.27 DE Interaction: O76324; IntAct: EBI-496170,EBI-189923; Score: 0.27 GO GO:0044297; GO GO:0005737; GO GO:0005829; GO GO:0005654; GO GO:0005634; GO GO:0048471; GO GO:0042802; GO GO:0046982; GO GO:0042803; GO GO:0003712; GO GO:0003714; GO GO:0001222; GO GO:0008134; GO GO:0000976; GO GO:0001306; GO GO:0048148; GO GO:0048512; GO GO:0032922; GO GO:0007623; GO GO:0042745; GO GO:0060086; GO GO:0007620; GO GO:0007619; GO GO:0008340; GO GO:0008062; GO GO:0009649; GO GO:0043153; GO GO:0045475; GO GO:0007616; GO GO:0045433; GO GO:0007617; GO GO:0000122; GO GO:2000678; GO GO:0045892; GO GO:0042752; GO GO:0045187; GO GO:1904059; GO GO:0001932; GO GO:0009416; GO GO:0006979; GO GO:0009266; GO GO:0007622; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEGGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKG SQ AGQGAGQAQTLISASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQAIEQLQQEEEEDQSGSESEADRVEG SQ VAKSEAAQSFPIPSPLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSF SQ CCVISMHDGIVLYTTPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRG SQ LKSGGFGVIGRPVSYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGI SQ ISHVDSAAVSALGYLPQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVN SQ PWSRKLEFVVGHHRVFQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFM SQ ETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPAELDP SQ PKTEPPEPRGTCVSGASGPMSPVHEGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGT SQ GTGTGTGTGTGTGTGTGTGTGTGNGTNSGTGTGTASSSKGGTAAIPPVTLTESLLNKHNDEMEKFMLKKHRESRGRTGEK SQ SKKSANDTLKMLEYSGPGHGIKRGGSHSWEGEANKPKQQLTLGTDAIKGAAGSAGGAVGTGGVGSGGAGVAGGGGSGTGV SQ AGTPEGRATTTSGTGTPGGAGGGGGAGAAAAAGASSSVGSSTPGPSSYPTCTQNINLWPPFSVGITPPVHSTHTAMAQSS SQ FSSAGLFPTFYYIPASLTPTSPTRSPRMHKHPHKGGTDMPTTSQQAAAAAAQAMPLQYMAGVMYPHPSLFYTHPAAAAAT SQ AMMYQPMPFPGMANALQIPERPLGSQSAYNKSVYTTTPASMTKKVPGAFHSVTTPAQVQRPSSQSASVKTEPGSSAAVSD SQ PCKKEVPDSSPIPSVMGDYNSDPPCSSSNPANNKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDPKHRKL SQ KSMSTSESKIMEHPEEDQTQHGDG // ID P07948; PN Tyrosine-protein kinase Lyn; GN LYN; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Membrane {ECO:0000305}; Lipid- anchor {ECO:0000305}. Note=Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts. DR UNIPROT: P07948; DR UNIPROT: A0AVQ5; DR PDB: 1W1F; DR PDB: 1WA7; DR PDB: 3A4O; DR PDB: 5XY1; DR PDB: 6NMW; 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: 165120; DR DisGeNET: 4067; DE Function: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3- kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-107'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity). {ECO:0000250|UniProtKB:P25911, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10891478, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15795233, ECO:0000269|PubMed:16467205, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829, ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:18577747, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19290919, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:7687428}. DE Disease: Note=Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells. DE Reference Proteome: Yes; DE Interaction: O92972; IntAct: EBI-79452,EBI-710506; Score: 0.59 DE Interaction: P00533; IntAct: EBI-79452,EBI-297353; Score: 0.82 DE Interaction: Self; IntAct: EBI-79452,EBI-79452; Score: 0.44 DE Interaction: P10275; IntAct: EBI-79452,EBI-608057; Score: 0.44 DE Interaction: Q13480; IntAct: EBI-79452,EBI-517684; Score: 0.44 DE Interaction: P10721; IntAct: EBI-79452,EBI-1379503; Score: 0.44 DE Interaction: P08581; IntAct: EBI-79452,EBI-1039152; Score: 0.44 DE Interaction: Q05397; IntAct: EBI-79452,EBI-702142; Score: 0.57 DE Interaction: P05556; IntAct: EBI-703066,EBI-79452; Score: 0.43 DE Interaction: P13612; IntAct: EBI-79452,EBI-703044; Score: 0.43 DE Interaction: P48023; IntAct: EBI-495538,EBI-79452; Score: 0.40 DE Interaction: Q80X56; IntAct: EBI-2553252,EBI-79452; Score: 0.40 DE Interaction: O95684; IntAct: EBI-1266334,EBI-79452; Score: 0.35 DE Interaction: P35579; IntAct: EBI-350338,EBI-79452; Score: 0.35 DE Interaction: Q86X19; IntAct: EBI-11343485,EBI-79452; Score: 0.35 DE Interaction: Q61879; IntAct: EBI-400918,EBI-79452; Score: 0.35 DE Interaction: Q9D620; IntAct: EBI-8399105,EBI-79452; Score: 0.35 DE Interaction: Q9NQW6; IntAct: EBI-2553589,EBI-79452; Score: 0.35 DE Interaction: Q9WUM4; IntAct: EBI-8316222,EBI-79452; Score: 0.35 DE Interaction: Q9UHB6; IntAct: EBI-351479,EBI-79452; Score: 0.35 DE Interaction: Q80X90; IntAct: EBI-688023,EBI-79452; Score: 0.35 DE Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-79452; Score: 0.35 DE Interaction: Q9H0B6; IntAct: EBI-726994,EBI-79452; Score: 0.35 DE Interaction: P11049; IntAct: EBI-6139068,EBI-79452; Score: 0.50 DE Interaction: P29350; IntAct: EBI-78260,EBI-79452; Score: 0.40 DE Interaction: P08238; IntAct: EBI-352572,EBI-79452; Score: 0.56 DE Interaction: A0A2S9PK33; IntAct: EBI-2865067,EBI-79452; Score: 0.37 DE Interaction: Q7CJG3; IntAct: EBI-79452,EBI-2844548; Score: 0.37 DE Interaction: P46527; IntAct: EBI-79452,EBI-519280; Score: 0.54 DE Interaction: Q8R5G7; IntAct: EBI-79452,EBI-621463; Score: 0.56 DE Interaction: Q9NRA0; IntAct: EBI-79452,EBI-985324; Score: 0.44 DE Interaction: Q8CI15; IntAct: EBI-79452,EBI-985291; Score: 0.40 DE Interaction: Q9JIA7; IntAct: EBI-985434,EBI-79452; Score: 0.40 DE Interaction: P11802; IntAct: EBI-79452,EBI-295644; Score: 0.40 DE Interaction: Q5U3Y8; IntAct: EBI-7618036,EBI-79452; Score: 0.40 DE Interaction: Q969Q1; IntAct: EBI-79452,EBI-5661333; Score: 0.37 DE Interaction: Q9BYV6; IntAct: EBI-79452,EBI-2341179; Score: 0.37 DE Interaction: O43172; IntAct: EBI-79452,EBI-718395; Score: 0.35 DE Interaction: P06493; IntAct: EBI-79452,EBI-444308; Score: 0.35 DE Interaction: P07900; IntAct: EBI-79452,EBI-296047; Score: 0.35 DE Interaction: P08631; IntAct: EBI-79452,EBI-346340; Score: 0.35 DE Interaction: P09769; IntAct: EBI-79452,EBI-1383732; Score: 0.35 DE Interaction: P15924; IntAct: EBI-79452,EBI-355041; Score: 0.35 DE Interaction: Q16543; IntAct: EBI-79452,EBI-295634; Score: 0.35 DE Interaction: Q8IX12; IntAct: EBI-79452,EBI-356265; Score: 0.35 DE Interaction: Q9NWB6; IntAct: EBI-79452,EBI-2808785; Score: 0.35 DE Interaction: Q9UQ35; IntAct: EBI-79452,EBI-1050142; Score: 0.35 DE Interaction: Q6P2Q9; IntAct: EBI-79452,EBI-538479; Score: 0.35 DE Interaction: Q9BUQ8; IntAct: EBI-79452,EBI-540096; Score: 0.35 DE Interaction: Q58FF7; IntAct: EBI-79452,EBI-9996483; Score: 0.35 DE Interaction: P29144; IntAct: EBI-79452,EBI-1044672; Score: 0.35 DE Interaction: P68400; IntAct: EBI-79452,EBI-347804; Score: 0.35 DE Interaction: Q8NEV1; IntAct: EBI-79452,EBI-21265922; Score: 0.35 DE Interaction: P84090; IntAct: EBI-79452,EBI-711389; Score: 0.35 DE Interaction: Q02413; IntAct: EBI-79452,EBI-1045757; Score: 0.35 DE Interaction: Q12874; IntAct: EBI-79452,EBI-1051880; Score: 0.35 DE Interaction: Q15029; IntAct: EBI-79452,EBI-357897; Score: 0.35 DE Interaction: Q15428; IntAct: EBI-79452,EBI-2462271; Score: 0.35 DE Interaction: Q15459; IntAct: EBI-79452,EBI-1054743; Score: 0.35 DE Interaction: Q8IWX8; IntAct: EBI-79452,EBI-2555370; Score: 0.35 DE Interaction: Q99873; IntAct: EBI-79452,EBI-78738; Score: 0.35 DE Interaction: Q9Y2W1; IntAct: EBI-79452,EBI-352039; Score: 0.35 DE Interaction: Q13115; IntAct: EBI-6591081,EBI-79452; Score: 0.35 DE Interaction: P33993; IntAct: EBI-355924,EBI-79452; Score: 0.50 DE Interaction: Q71U36; IntAct: EBI-302552,EBI-79452; Score: 0.35 DE Interaction: Q08857; IntAct: EBI-8346984,EBI-79452; Score: 0.50 DE Interaction: P16671; IntAct: EBI-2808214,EBI-79452; Score: 0.50 DE Interaction: Q9QWY8-1; IntAct: EBI-698517,EBI-79452; Score: 0.40 DE Interaction: Q9QWY8-2; IntAct: EBI-698524,EBI-79452; Score: 0.40 DE Interaction: P26660; IntAct: EBI-79452,EBI-706322; Score: 0.40 DE Interaction: P27958; IntAct: EBI-706378,EBI-79452; Score: 0.70 DE Interaction: Q913V3; IntAct: EBI-79452,EBI-10052968; Score: 0.40 DE Interaction: Q9WMX2; IntAct: EBI-710918,EBI-79452; Score: 0.67 DE Interaction: Q99759; IntAct: EBI-79452,EBI-307281; Score: 0.40 DE Interaction: P67870; IntAct: EBI-348169,EBI-79452; Score: 0.37 DE Interaction: P20273; IntAct: EBI-78277,EBI-79452; Score: 0.50 DE Interaction: Q9HCN6; IntAct: EBI-79452,EBI-515278; Score: 0.64 DE Interaction: Q07666; IntAct: EBI-1364,EBI-79452; Score: 0.61 GO GO:0005737; GO GO:0005829; GO GO:0070062; GO GO:0031234; GO GO:0098978; GO GO:0005794; GO GO:0034666; GO GO:0043231; GO GO:0042629; GO GO:0045121; GO GO:0030061; GO GO:0005758; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0014069; GO GO:0099091; GO GO:0005524; GO GO:0019899; GO GO:0046875; GO GO:0043015; GO GO:0043208; GO GO:0005178; GO GO:0044325; GO GO:0016301; GO GO:0004715; GO GO:0051219; GO GO:0140031; GO GO:0005161; GO GO:0004713; GO GO:0017124; GO GO:0005102; GO GO:0031625; GO GO:0002250; GO GO:0001782; GO GO:0050853; GO GO:0007596; GO GO:0030154; GO GO:0006974; GO GO:0031668; GO GO:0034605; GO GO:0071300; GO GO:0050663; GO GO:0097028; GO GO:0048013; GO GO:0030218; GO GO:0002774; GO GO:0002431; GO GO:0038095; GO GO:0038096; GO GO:0060397; GO GO:0002553; GO GO:0002768; GO GO:0045087; GO GO:0035556; GO GO:0050900; GO GO:0031663; GO GO:0030889; GO GO:0008285; GO GO:0070373; GO GO:0050777; GO GO:1902532; GO GO:0043407; GO GO:0070667; GO GO:0002762; GO GO:0001933; GO GO:0034136; GO GO:0034144; GO GO:0031175; GO GO:0014003; GO GO:0038083; GO GO:0018108; GO GO:0030168; GO GO:0002576; GO GO:1902961; GO GO:0030335; GO GO:0008284; GO GO:0051272; GO GO:2000670; GO GO:0060369; GO GO:0060252; GO GO:0070668; GO GO:0010976; GO GO:0070447; GO GO:0043552; GO GO:0014068; GO GO:0001934; GO GO:0046579; GO GO:0070304; GO GO:0042531; GO GO:0046777; GO GO:0006468; GO GO:0002902; GO GO:0050855; GO GO:0033628; GO GO:0042127; GO GO:0001817; GO GO:0050707; GO GO:0070372; GO GO:0045646; GO GO:0050727; GO GO:0033003; GO GO:0043304; GO GO:0090025; GO GO:0090330; GO GO:0001932; GO GO:0051279; GO GO:0043200; GO GO:0048678; GO GO:0009743; GO GO:0042493; GO GO:0009725; GO GO:0032868; GO GO:0014070; GO GO:0006991; GO GO:0009636; GO GO:0007165; GO GO:0002223; GO GO:0031295; GO GO:0002513; GO GO:0034142; GO GO:0007169; GO GO:0016032; TP Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18817770}; SQ MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPD SQ DLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESET SQ LKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAW SQ EIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITE SQ YMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAR SQ EGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCW SQ KEKAEERPTFDYLQSVLDDFYTATEGQYQQQP // ID P08325; PN Matrix protein; GN M; OS 11283; 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: P08325; DR PDB: 2W2R; 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 shutoff presumably inhibits 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: Yes; 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 MSSFKKILGLSSKSHKKSKKMGLPPPYDESCPMETQPSAPLSNDFFGMEDMDLYDKDSLRYEKFRFMLKMTVRSNKPFRS SQ YDDVTAAVSQWDNSYIGMVGKRPFYKIIAVIGSSHLQATPAVLADLNQPEYYATLTGRCFLPHRLGLIPPMFNVQETFRK SQ PFNIGLYKGTLDFTFTVSDDESNEKVPHVWDYMNPKYQSQIQQEGLKFGLILSKKATGTWVLDQLSPFK // 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 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 P09280; PN Nuclear egress protein 2; GN NEC2; 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_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: P09280; 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 MSRRTYVRSERRRGCGDNLLQRIRLVVPSALQCCDGDLPIFDPQRPPARCVFQFNGEDNVSEAFPVEYIMRLMANWAQVD SQ CDPYIKIQNTGVSVLFQGFFFRPTNAPVAEVSIDSNNVILSSTLSTGINLSALESIKRGGGIDRRPLQALMWVNCFVRMP SQ YVQLSFRFMGPEDPSRTIKLMARATDAYMYKETGNNLDEYIRWRPSFRSPPENGSPNTSVQMQSDIKPALPDTQTTRVWK SQ LALPVANVTYALFIVIVLVVVLGAVLFWK // 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 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 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 P09732; PN RNA-directed RNA polymerase NS5; GN POLG; OS 11081; 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: P09732; DR UNIPROT: A3EZ58; DR UNIPROT: Q88781; DR UNIPROT: Q88782; DR UNIPROT: Q88783; DR UNIPROT: Q88784; DR UNIPROT: Q88785; DR UNIPROT: Q88786; DR UNIPROT: Q88787; DR UNIPROT: Q88788; DR PDB: 4FG0; 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}. [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:0039563; GO GO:0039564; GO GO:0039502; GO GO:0039694; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSKKPGKPGRNRVVNMLKRGVSRVNPLTGLKRILGSLLDGRGPVRFILAILTFFRFTALQPTEALKRRWRAVDKRTALKH SQ LNGFKRDLGSMLDTINRRPSKKRGGTRSLLGLAALIGLASSLQLSTYQGKVLMSINKTDAQSAINIPSANGANTCIVRAL SQ DVGVMCKNDITYLCPVLSAGNDPEDIDCWCDVEEVWVHYGRCTRMGHSRRSRRSISVQHHGDSTLATKNTPWLDTVKTTK SQ YLTKVENWVLRNPGYALVALAIGWMLGSNNTQRVVFVIMLMLIAPAYSFNCLGTSNRDFVEGASGATWIDLVLEGGSCVT SQ VMAPEKPTLDFKVMKMEATELATVREYCYEATLDTLSTVARCPTTGEAHNTKRSDPTFVCKRDVVDRGWGNGCGLFGKGS SQ IDTCAKFTCKNKATGKTILRENIKYEVAIFVHGSTDSTSHGNYFEQIGKNQAARFTISPQAPSFTANMGEYGTVTIDCEA SQ RSGINTEDYYVFTVKEKSWLVNRDWFHDLNLPWTSPATTDWRNRETLVEFEEPHATKQTVVALGSQEGALHTALAGAIPA SQ TVSSSTLTLQSGHLKCRAKLDKVKIKGTTYGMCDSAFTFSKNPADTGHGTVIVELQYTGSNGPCRVPISVTANLMDLTPV SQ GRLVTVNPFISTGGANNKVMIEVEPPFGDSYIVVGRGTTQINYHWHKEGSSIGKALATTWKGAQRLAVLGDTAWDFGSIG SQ GVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLLGALLLWMGLQARDRSISLTLLAVGGILIFLATSVQADSGCAIDLQRR SQ ELKCGGGIFVYNDVEKWKSDYKYFPLTPTGLAHVIQEAHANGICGIRSTSRLEHLMWENIQRELNAIFEDNEIDLSVVVQ SQ EDPKYYKRAPRRLKKLEDELDYGWKKWGKTLFVEPRLGNNTFVVDGPETKECPTANRAWNSFKVEDFGFGMVFTRLWLTI SQ REENTTECDSAIIGTAIKGDRAVHSDLSYWIESKKNETWQLERAVMGEVKSCTWPETHTLWGDGVVESEMIIPVTLGGPK SQ SHHNKRNGYHTQTKGPWSEGEITLDFDYCPGTTVTVTEHCGNRGASLRTTTASGKLVTDWCCRSCSLPPLRYTTKDGCWY SQ GMEIRPVKEEEAKLVKSRVTAGVAGGMEPFQLGLLVAFIATQEVLKRRWTGKLTLTSLAVCLALLIFGNLTYMDLVRYLV SQ LVGTAFAEMNTGGDVIHLALVAVFKVQPAFLAGLFLRMQWSNQENILMVIGAAFLQMAANDLKLEVLPILNAMSIAWMLI SQ RAMKEGKVAMYALPILCALTPGMRMAGLDVIRCLLLIIGIVTLLNERRESVAKKKGGYLLAAALCQAGVCSPLIMMGGLI SQ LAHPNGKRSWPASEVLTGVGLMCALAGGLLEFEETSMVVPFAIAGLMYITYTVSGKAAEMWIEKAADITWEQNAEITGTS SQ PRLDVDLDSHGNFKLLNDPGAPVHLFALRFILLGLSARFHWFIPFGVLGFWLLGKHSKRGGALWDVPSPKVYPKCETKPG SQ IYRIMTRGILGTFQAGVGVMHEGVFHTMWHATEGAVLRNGEGRLDPYAGDVRNDLISYGGPWKLSATWDGTEEVQMIAVA SQ PGKPAINVQTTPGVFKTPFGTIGAVTLDFPKGTSGSPIINKKGEIIGLYGNGVLIGQGEYVSGIIQGERTEEPIPDAYNE SQ EMLRKRKLTVLELHPGAGKTRKVLPQIIKDCIQKRLRTAVLAPTRVVACEIAEALKGLPIRYLTPAVRNEHQGNEIVDVM SQ CHATLTQKLLTPTRVPNYQVYIMDEAHFIDPASIAARGYISTKVELGEAAAIFMTATPPGTNDPFPDSNSPILDVEAQVP SQ DKAWSTGYEWITNFTGRTVWFVPSVKSGNEIAICLQKAGKRVIQLNRKSFDTEYPKTKNNEWDFVVTTDISEMGANFGAH SQ RVIDSRKCVKPVILEDDDRVILNGPMAITSASAAQRRGRIGRNPSQIGDEYHYGGATNEDDHDLANWTEAKILLDNIYLP SQ NGLVAQMYQPERDKVFTMDGEFRLRGEERKNFVELMRNGDLPVWLAYKVASNGHSYQDRSWCFTGQTNNTILEDNNEVEV SQ FTKTGDRKILRPKWMDARVCCDYQALKSFKEFAAGKRSALGMMEVMGRMPNHFWEKTVAAADTLYLLGTSEANSRAHKEA SQ LAELPDSLETLLLIGMLCVMSMGTFIFLMNRKGVGKMGLGAFVMTLATALLWAAEVPGTQIAGVLLIVFLLMIVLIPEPE SQ KQRSQTDNQLAVFLICIMTLMGVVAANEMGLLEKTKSDIAKLFGSQPGSVGFATRTTPWDISLDIKPATAWALYAAATMV SQ MTPLIKHLITTQYVNFSLTAIASQAGVLLGLTNGMPFTAMDLSVPLLVLGCWNQMTLPSLAVAVMLLAIHYAFMIPGWQA SQ EAMRAAQRRTAAGIMKNAVVDGIVATDIPDLSPATPMTEKKMGQILLIAAAVLAVLVRPGICSIKEFGVLGSAALVTLIE SQ GTAGVVWNCTTAVGLCNLMRGGWLAGMSITWTVYKNVDKPKGKRGGGKGATLGEIWKSRLNQLTRAEFMAYRKDGIVEVD SQ RAPARKARREGRLTGGHPVSRGSAKLRWITERGFVKPMGKVVDLGCGRGGWSYYCATLKHVQEVKGFTKGGPGHEEPQLM SQ QSYGWNLVHMKSGVDVFHKPAEPADTVLCDIGESNPSCEVEEARTARVLDMVEEWLKKGATEFCIKVLCPYTPKIIEKLE SQ KLQRKYGGGLVRVPLSRNSTHEMYWVSGAAGNIIHAVSMTSQVLMGRMDKQNRSGPRYEEDVNLGSGTRSVGKLTEKPDL SQ RKVGERIRRLREEYQQTWTYDHNNPYRTWNYHGSYEVKPTGSASSMVNGVVRLLSKPWDMITNVTTMAMTDTTPFGQQRV SQ FKEKVDTKAPEPPLGVAQIMDVTTDWLWDFVAREKKPRVCTPEEFKAKVNSHAALGAMFEEQNQWSSAREAVEDPKFWEM SQ VDEEREAHLKGECHTCIYNMMGKREKKTGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRENSYGGVEGKGLQK SQ LGYILQEISQIPGGKMYADDTAGWDTRITKEDLKNEAKITKRMEERHRKLAEAIIDLTYRHKVVKVMRPGPDGKTYMDVI SQ SREDQRGSGQVVTYALNTFTNLAVQLIRCMEAEGVVDEDDITRVRLGRLAKAVEWLRKNGPERLSRMAVSGDDCVVKPID SQ DRFATALHFLNNMSKIRKDIQEWKPSTGWHNWQEVPFCSHHFNELMLKDGRTIVVPCRSQDELIGRARISPGAGWNVKET SQ ACLSKSYAQMWLLMYFHRRDLRMMANAICSAVPVNWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWIEENEYMKDKTPLA SQ AWNDIPYLGKREDIWCGSLIGTRTRATWAENIYAPIMQIRNLIGEEEYRDYM // ID P09866; PN RNA-directed RNA polymerase NS5; GN POLG; OS 408871; 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:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [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:P17763}; 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:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {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:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}. DR UNIPROT: P09866; DR UNIPROT: Q88661; DR UNIPROT: Q88662; DR UNIPROT: Q88663; DR UNIPROT: Q88664; DR UNIPROT: Q88665; DR UNIPROT: Q88666; DR UNIPROT: Q88667; DR UNIPROT: Q88668; DR UNIPROT: Q88669; DR UNIPROT: Q88670; DR UNIPROT: Q88671; DR UNIPROT: Q99BK4; DR UNIPROT: Q9DKQ5; DR UNIPROT: Q9DKQ6; DR UNIPROT: Q9DKQ7; DR PDB: 2H0P; DR PDB: 3UAJ; DR PDB: 3UC0; DR PDB: 3WE1; DR PDB: 4X42; DR PDB: 5B1C; 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}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:Q9Q6P4}. [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 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [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}. [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. {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:P17763}. DE Reference Proteome: No; GO GO:0005576; GO GO:0044167; GO GO:0033650; GO GO:0042025; GO GO:0044220; GO GO:0016021; GO GO:0044385; GO GO:0019028; GO GO:0019031; GO GO:0055036; GO GO:0005524; GO GO:0003725; GO GO:0005216; 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:0039707; GO GO:0051259; GO GO:0039545; GO GO:0039564; GO GO:0039574; GO GO:0039502; GO GO:0039694; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKIL SQ IGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFSLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCED SQ TVTYKCPLLVNTEPEDIDCWCNLTSTWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI SQ LRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL SQ DFELTKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDVVDRGWGNGCGLFGKGGVVTCAKFSC SQ SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTAMITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKM SQ KKKTWLVHKQWFLDLPLPWTAGADTSEVHWNYKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAG SQ HLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGAGAPCKVPIEIRDVNKEKVVGRIISSTPLAENT SQ NSVTNIELEPPFGDSYIVIGVGNSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLFTSLGKAVHQVFG SQ SVYTTMFGGVSWMIRILIGFLVLWIGTNSRNTSMAMTCIAVGGITLFLGFTVQADMGCVASWSGKELKCGSGIFVVDNVH SQ TWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLTKGKRALTP SQ PVSDLKYSWKTWGKAKIFTPEARNSTFLIDGPDTSECPNERRAWNSLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSA SQ AIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKSYAGPFSQHNYRQGYATQTVG SQ PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLSEKEENMV SQ KSQVTAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVITLCAIILGGLTWMDLLRALIMLGDTMSGRIGGQIHL SQ AIMAVFKMSPGYVLGVFLRKLTSRETALMVIGMAMTTVLSIPHDLMELIDGISLGLILLKIVTQFDNTQVGTLALSLTFI SQ RSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASRRSWPLNEGIMAVGLVSL SQ LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMIT SQ LLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAATKKAALSEGVYRIMQRGLFGKTQVGVGIHMEGVF SQ HTMWHVTRGSVICHETGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV SQ TLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS SQ IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA SQ HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGATDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK SQ AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILPDGPERVILAGP SQ IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLKNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLR SQ GEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPRWLDARVYADPMA SQ LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGRAYQHALNELPESLETLMLVALLGAMTAGI SQ FLFFMQGKGIGKLSMGLITIAVASGLLWVAEIQPQWIAASIILEFFLMVLLIPEPEKQRTPQDNQLIYVILTILTIIGLI SQ AANEMGLIEKTKTDFGFYQVKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG SQ WPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD SQ PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK SQ NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKHAVSRGSSKIRWIVERGMVKP SQ KGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN SQ PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGNLVRCPLSRNSTHEMYWVSGASGNIVSSVN SQ TTSKMLLNRFTTRHRKPTYEKDVDLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDQENPYRTWAYHGSYEAPS SQ TGSASSMVNGVVKLLTKPWDVIPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRMVMTTTANWLWALLGKKKNPRL SQ CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRA SQ IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEEIDKKDGDLMYADDTAGWDTRITEDDLQNEELI SQ TEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPRGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITQDD SQ MQNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFGTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH SQ FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR SQ TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMTDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIHTAITQVRN SQ LIGKEEYVDYMPVMKRYSAPSESEGVL // 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 P0C044; PN F protein; GN F; OS 11104; SL Nucleus Position: SL-0382; SL Comments: Host cytoplasm {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. DR UNIPROT: P0C044; DR Pfam: PF01543; DE Function: DE Reference Proteome: No; GO GO:0044220; GO GO:0019028; GO GO:0005198; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSTNPKPQKKKTNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRERLPSGRNLEVDVSLSPRLVGPRAGPGLSP SQ GTLGPSMAMRAAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWK SQ TA // ID P0C6U8; PN Non-structural protein 11; GN 1a; OS 694009; 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: P0C6U8; DR UNIPROT: P59641; DR PDB: 1P76; DR PDB: 1P9T; DR PDB: 1PA5; DR PDB: 1PUK; DR PDB: 1Q1X; DR PDB: 1Q2W; DR PDB: 1QZ8; DR PDB: 1UJ1; DR PDB: 1UK2; DR PDB: 1UK3; DR PDB: 1UK4; DR PDB: 1UW7; DR PDB: 1WOF; DR PDB: 1YSY; DR PDB: 1Z1I; DR PDB: 1Z1J; DR PDB: 2A5A; DR PDB: 2A5I; DR PDB: 2A5K; DR PDB: 2ACF; DR PDB: 2AHM; DR PDB: 2AJ5; DR PDB: 2ALV; DR PDB: 2AMD; DR PDB: 2AMQ; DR PDB: 2BX3; DR PDB: 2BX4; DR PDB: 2C3S; DR PDB: 2D2D; DR PDB: 2DUC; DR PDB: 2FAV; DR PDB: 2FE8; DR PDB: 2FYG; DR PDB: 2G9T; DR PDB: 2GA6; DR PDB: 2GDT; DR PDB: 2GRI; DR PDB: 2GT7; DR PDB: 2GT8; DR PDB: 2GTB; DR PDB: 2GX4; DR PDB: 2GZ7; DR PDB: 2GZ8; DR PDB: 2GZ9; DR PDB: 2H2Z; DR PDB: 2HOB; DR PDB: 2HSX; DR PDB: 2IDY; DR PDB: 2KAF; DR PDB: 2KQV; DR PDB: 2KQW; DR PDB: 2KYS; DR PDB: 2LIZ; DR PDB: 2OP9; DR PDB: 2PWX; DR PDB: 2W2G; DR PDB: 2WCT; DR PDB: 2Z3C; DR PDB: 2Z3D; DR PDB: 2Z3E; DR PDB: 2ZU4; DR PDB: 2ZU5; DR PDB: 3ATW; DR PDB: 3AVZ; DR PDB: 3AW0; DR PDB: 3AW1; DR PDB: 3E91; DR PDB: 3EA7; DR PDB: 3EA8; DR PDB: 3EA9; DR PDB: 3EAJ; DR PDB: 3EE7; DR PDB: 3F9E; DR PDB: 3F9F; DR PDB: 3F9G; DR PDB: 3F9H; DR PDB: 3FZD; DR PDB: 3IWM; DR PDB: 3M3S; DR PDB: 3M3T; DR PDB: 3M3V; DR PDB: 3MJ5; DR PDB: 3R24; DR PDB: 3SN8; DR PDB: 3SNA; DR PDB: 3SNB; DR PDB: 3SNC; DR PDB: 3SND; DR PDB: 3SNE; DR PDB: 3SZN; DR PDB: 3TIT; DR PDB: 3TIU; DR PDB: 3TNS; DR PDB: 3TNT; DR PDB: 3V3M; DR PDB: 3VB3; DR PDB: 3VB4; DR PDB: 3VB5; DR PDB: 3VB6; DR PDB: 3VB7; DR PDB: 4HI3; DR PDB: 4M0W; DR PDB: 4MDS; DR PDB: 4MM3; DR PDB: 4OVZ; DR PDB: 4OW0; DR PDB: 5F22; DR PDB: 5Y3E; DR PDB: 5Y3Q; DR PDB: 6NUR; DR PDB: 6NUS; DR PDB: 6Y7M; DR Pfam: PF16348; DR Pfam: PF12379; DR Pfam: PF01661; DR Pfam: PF16251; DR Pfam: PF11501; DR Pfam: PF09401; DR Pfam: PF12124; 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: [Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. [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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371). {ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}. [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:0000269|PubMed:19640993}. [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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF- kappa-B signaling. {ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:24622840, ECO:0000303|PubMed:24410069}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV. {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}. [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). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:16226257, ECO:0000269|PubMed:16271890}. [Non-structural protein 6]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). 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 (PubMed:24991833). {ECO:0000269|PubMed:24991833, ECO:0000303|PubMed:24410069}. [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:0000269|PubMed:22039154}. [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:0000269|PubMed:22039154}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000269|PubMed:19153232}. [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:0000269|PubMed:22635272}. DE Reference Proteome: Yes; GO GO:0039714; GO GO:0033644; GO GO:0044220; GO GO:0016021; GO GO:0004197; GO GO:0004519; 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 MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTN SQ HGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQN SQ WNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAW SQ FTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTL SQ MKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKG SQ GRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASF SQ SASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIP SQ DLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVE SQ FLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQC SQ IRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYC SQ ALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV SQ VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGL SQ PLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAAN SQ IHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQD SQ ILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQK SQ PVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSK SQ KAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEE SQ TRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAAR SQ CMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVE SQ FHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPS SQ DDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRAR SQ AGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGV SQ SIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPV SQ TDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQ SQ MTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSN SQ SFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENT SQ SITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFT SQ KSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYC SQ NGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGL SQ SAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVEC SQ TTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHL SQ YFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDS SQ TEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDL SQ EVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLT SQ CATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIIST SQ DDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLI SQ EYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEY SQ CRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYY SQ FMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAI SQ YVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDT SQ TSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPR SQ HVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNG SQ SPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTI SQ TLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRT SQ ILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAA SQ CAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDD SQ AARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVY SQ CFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMS SQ DVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQA SQ IASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRA SQ KVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVD SQ ADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLA SQ LLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPAN SQ STVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFC SQ DLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV // 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 P0C6V6; PN Non-structural protein 11; GN 1a; OS 229032; SL Nucleus Position: SL-0382; SL Comments: [Non-structural protein 1]: Host cytoplasm {ECO:0000269|PubMed:26773386}. Host nucleus {ECO:0000269|PubMed:26773386}. [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: P0C6V6; DR UNIPROT: Q91AV2; DR PDB: 5GWZ; 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 non-structural protein 1 (nsp1) protein plays a role in the inhibition of host interferon and pro-inflammatory cytokines production. Suppresses host RELA/p65 activation by blocking NFKBIA phosphorylation (PubMed:28715653). Targets also the RLR pathway downstream of the IRF3 activation by targeting host CREBBP to proteasomal degradation (PubMed:26773386). {ECO:0000269|PubMed:26773386, ECO:0000269|PubMed:28715653}. 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}. 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: No; GO GO:0030430; GO GO:0033644; GO GO:0042025; 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:0039644; GO GO:0019079; GO GO:0019082; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MASNHVTLAFANDAEISAFGFCTASEAVSYYSEAAASGFMQCRFVSLDLADTVEGLLPEDYVMVVIGTTKLSAYVDTFGS SQ RPRNICGWLLFSNCNYFLEELELTFGRRGGNIVPVDQYMCGADGKPVLQESEWEYTDFFADSEDGQLNIAGITYVKAWIV SQ ERSDVSYASQNLTSIKSITYCSTYEHTFLDGTAMKVARTPKIKKNVVLSEPLATIYREIGSPFVDNGSDARSIIRRPVFL SQ HAFVKCKCGSYHWTVGDWTSYVSTCCGFKCKPVLVASCSAMPGSVVVTRAGAGTGVKYYNNMFLRHVADIDGLAFWRILK SQ VQSKDDLACSGKFLEHHEEGFTDPCYFLNDSSLATKLKFDILSGKFSDEVKQAIIAGHVVVGSALVDIVDDALGQPWFIR SQ KLGDLASAPWEQLKAVVRGLGLLSDEVVLFGKRLSCATLSIVNGVFEFLADVPEKLAAAVTVFVNFLNEFFESACDCLKV SQ GGKTFNKVGSYVLFDNALVKLVKAKARGPRQAGICEVRYTSLVVGSTTKVVSKRVENANVNLVVVDEDVTLNTTGRTVVV SQ DGLAFFESDGFYRHLADADVVIEHPVYKSACELKPVFECDPIPDFPLPVAASVAELCVQTDLLLKNYNTPYKTYSCVVRG SQ DKCCITCTLQFKAPSYVEDAVNFVDLCTKNIGTAGFHEFYITAHEQQDLQGFLTTCCTMSGFECFMPTIPQCPAVLEEID SQ GGSIWRSFITGLNTMWDFCKRLKVSFGLDGIVVTVARKFKRLGALLAEMYNTYLSTVVENLVLAGVSFKYYATSVPKIVL SQ GGCFHSVKSVFASVFQIPVQAGIEKFKVFLNCVHPVVPRVIETSFVELEETTFKPPALNGGIAIVDGFAFYYDGTLYYPT SQ DGNSVVPICFKKKGGGDVKFSDEVSVKTIDPVYKVSLEFEFESETIMAVLNKAVGNRIKVTGGWDDVVEYINVAIEVLKD SQ HVEVPKYYIYDEEGGTDPNLPVMVSQWPLNDDTISQDLLDVEVVTDAPIDSEGDEVDSSAPEKVADVANSEPGDDGLPVA SQ PETNVESEVEEVAATLSFIKDTPSTVTKDPFAFDFVSYGGLKVLRQSHNNCWVTSTLVQLQLLGIVDDPAMELFSAGRVG SQ PMVRKCYESQKAILGSLGDVSACLESLTKDLHTLKITCSVVCGCGTGERIYEGCAFRMTPTLEPFPYGACAQCAQVLMHT SQ FKSIVGTGIFCRDTTALSLDSLVVKPLCAAAFIGKDSGHYVTNFYDAAMAIDGYGRHQIKYDTLNTICVKDVNWTAPLVP SQ AVDSVVEPVVKPFYSYKNVDFYQGDFSDLVKLPCDFVVNAANEKLSHGGGIAKAIDVYTKGMLQKCSNDYIKAHGPIKVG SQ RGVMLEALGLKVFNVVGPRKGKHAPELLVKAYKSVFANSGVALTPLISVGIFSVPLEESLSAFLACVGDRHCKCFCYGDK SQ EREAIIKYMDGLVDAIFKEALVDTTPVQEDVQQVSQKPVLPNFEPFRIEGAHAFYECNPEGLMSLGADKLVLFTNSNLDF SQ CSVGKCLNDVTSGALLEAINVFKKSNKTVPAGNCVTLDCANMISITMVVLPFDGDANYDKNYARAVVKVSKLKGKLVLAV SQ DDATLYSKLSHLSVLGFVSTPDDVERFYANKSVVIKVTEDTRSVKAVKVESTATYGQQIGPCLVNDTVVTDNKPVVADVV SQ AKVVPNANWDSHYGFDKAGEFHMLDHTGFTFPSEVVNGRRVIKTTDNNCWVNVTCLQLQFARFRFKSAGLQAMWESYCTG SQ DVAMFVHWLYWLTGVDKGQPSDSENALNMLSKYIVPAGSVTIERVTHDGCCCSKRVVTAPVVNASVLKLGVEDGLCPHGL SQ NYIGKVVVVKGTTIVVNVGKPVVAPSHLFLKGVSYTTFLDNGNGVVGHYTVFDHGTGMVHDGDAFVPGDLNVSPVTNVVV SQ SEQTAVVIKDPVKKAELDATKLLDTMNYASERFFSFGDFMSRNLITVFLYILSILGLCFRAFRKRDVKVLAGVPQRTGII SQ LRKSMRYNAKALGVFFKLKLYWFKVLGKFSLGIYALYALLFMTIRFTPIGSPVCDDVVAGYANSSFDKNEYCNSVICKVC SQ LYGYQELSDFSHTQVVWQHLRDPLIGNVMPFFYLAFLAIFGGVYVKAITLYFIFQYLNSLGVFLGLQQSIWFLQLVPFDV SQ FGDEIVVFFIVTRVLMFIKHVCLGCDKASCVACSKSARLKRVPVQTIFQGTSKSFYVHANGGSKFCKKHNFFCLNCDSYG SQ PGCTFINDVIATEVGNVVKLNVQPTGPATILIDKVEFSNGFYYLYSGDTFWKYNFDITDSKYTCKEALKNCSIITDFIVF SQ NNNGSNVNQVKNACVYFSQMLCKPVKLVDSALLASLSVDFGASLHSAFVSVLSNSFGKDLSSCNDMQDCKSTLGFDDVPL SQ DTFNAAVAEAHRYDVLLTDMSFNNFTTSYAKPEEKFPVHDIATCMRVGAKIVNHNVLVKDSIPVVWLVRDFIALSEETRK SQ YIIRTTKVKGITFMLTFNDCRMHTTIPTVCIANKKGAGLPSFSKVKKFFWFLCLFIVAAFFALSFLDFSTQVSSDSDYDF SQ KYIESGQLKTFDNPLSCVHNVFINFDQWHDAKFGFTPVNNPSCPIVVGVSDEARTVPGIPAGVYLAGKTLVFAINTIFGT SQ SGLCFDASGVADKGACIFNSACTTLSGLGGTAVYCYKNGLVEGAKLYSELAPHSYYKMVDGNAVSLPEIISRGFGIRTIR SQ TKAMTYCRVGQCVQSAEGVCFGADRFFVYNAESGSDFVCGTGLFTLLMNVISVFSKTVPVTVLSGQILFNCIIAFVAVAV SQ CFLFTKFKRMFGDMSVGVFTVGACTLLNNVSYIVTQNTLGMLGYATLYFLCTKGVRYMWIWHLGFLISYILIAPWWVLMV SQ YAFSAIFEFMPNLFKLKVSTQLFEGDKFVGSFENAAAGTFVLDMHAYERLANSISTEKLRQYASTYNKYKYYSGSASEAD SQ YRLACFAHLAKAMMDYASNHNDTLYTPPTVSYNSTLQAGLRKMAQPSGVVEKCIVRVCYGNMALNGLWLGDIVMCPRHVI SQ ASSTTSTIDYDYALSVLRLHNFSISSGNVFLGVVSATMRGALLQIKVNQNNVHTPKYTYRTVRPGESFNILACYDGAAAG SQ VYGVNMRSNYTIRGSFINGACGSPGYNINNGTVEFCYLHQLELGSGCHVGSDLDGVMYGGYEDQPTLQVEGASSLFTENV SQ LAFLYAALINGSTWWLSSSRIAVDRFNEWAVHNGMTTVGNTDCFSILAAKTGVDVQRLLASIQSLHKNFGGKQILGHTSL SQ TDEFTTGEVVRQMYGVNLQGGYVSRACRNVLLVGSFLTFFWSELVSYTKFFWVNPGYVTPMFACLSLLSSLLMFTLKHKT SQ LFFQVFLIPALIVTSCINLAFDVEVYNYLAEHFDYHVSLMGFNAQGLVNIFVCFVVTILHGTYTWRFFNTPASSVTYVVA SQ LLTAAYNYFYASDILSCAMTLFASVTGNWFVGAVCYKVAVYMALRFPTFVAIFGDIKSVMFCYLVLGYFTCCFYGILYWF SQ NRFFKVSVGVYDYTVSAAEFKYMVANGLRAPTGTLDSLLLSAKLIGIGGERNIKISSVQSKLTDIKCSNVVLLGCLSSMN SQ VSANSTEWAYCVDLHNKINLCNDPEKAQEMLLALLAFFLSKNSAFGLDDLLESYFNDNSMLQSVASTYVGLPSYVIYENA SQ RQQYEDAVNNGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAAAQMYKEARAVNRKSKVVSAMHSLLFGMLRRL SQ DMSSVDTILNLAKDGVVPLSVIPAVSATKLNIVTSDIDSYNRIQREGCVHYAGTIWNIIDIKDNDGKVVHVKEVTAQNAE SQ SLSWPLVLGCERIVKLQNNEIIPGKLKQRSIKAEGDGIVGEGKALYNNEGGRTFMYAFISDKPDLRVVKWEFDGGCNTIE SQ LEPPRKFLVDSPNGAQIKYLYFVRNLNTLRRGAVLGYIGATVRLQAGKQTEQAINSSLLTLCAFAVDPAKTYIDAVKSGH SQ KPVGNCVKMLANGSGNGQAVTNGVEASTNQDSYGGASVCLYCRAHVEHPSMDGFCRLKGKYVQVPLGTVDPIRFVLENDV SQ CKVCGCWLSNGCTCDRSIMQSTDMAYLNEYGALVQLD // 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 P0C6W1; PN 2'-O-methyltransferase; GN rep; OS 389230; 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: P0C6W1; DR UNIPROT: Q0Q4F3; 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, ECO:0000269|PubMed:19264783}. [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:0019082; GO GO:0039694; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLSKAGVTTQGARGKYRAELYNEKRSDHVACTVPLCDTEDMASKLTPWFEDGETAFNQVSSILKEKGKILFVPMHMQRAM SQ KFLPGPRVYLVERLTGGMLSKHFLVNQLAYKDHVGAAMMRTTLNVKPLGMFFPYDSSLETGEHTFLLRKNGLGGQLFRER SQ PWDRKETPYVEILDDLEADPTGKYSQNLLKKLIGGDCIPVDQYMCGKNGKPIADYAKIVAKEGLTTLADIEVDVKSRMDS SQ DRFIVLNKKLYRVVWNVTRRNVPYSKQTAFTVVSVIQCDDKESVPEHTFTIGSQILMVSPLKATNNKNFNLKQRLLHTFY SQ GKEAVQQPGYIYHSAYVDCNACGRGTWCTGNAIQGFACDCGANYSANDVDLQSSGLVPKNALFLANCPCANNGACSHNAA SQ QVYSILDGKACVEVGGKSFTLTFGGVVYAYMGCCDGTMYFVPRAKSCVSRIGDAIFTGCTGTWDKVVETANLFLEKAQHS SQ LNFCQQFALTEVVLAILSGTTSTFEELRDLCHNASYEKVRDHLVNHGFVVTIGDYIRDAINIGANGVCNATINAPFIAFT SQ GLGESFKKVAAIPWKICSNLKSALDYYCSNIMFRVFPYDIPCDVNDFVELLLDCGKLTVATSYFVLRYLDEKFDTVLGTV SQ SNACQTALSSFLNACVAASRATAGFISDMFKLFKVLMHKLYVYTSCGYVAVAEHSSKIVQQVLDIMSKAMKLLHTNVSWA SQ GTKLSAIIYEGREALLFNSGTYFCLSTKAKTLQDQMNLVLPGDYNKKTLGILDPVPNADTIDVTANSTVVDVVHGQLEPT SQ NEHGPSMIVGNYVLVSDKLFVRTDDEEFYPLCINGKVVSTLFRLKGGMPSKKVTFGDVNTVEVTAYRSVSITYDIHPVLD SQ ALLSSSKLATFTVEKDLLVEDFVDVIKDEVLTLLTPLLRGYDIDGFDVEDFIDVPCYVYNQDGDCAWSSNMTFSINPVED SQ VEEVEEFIEDDYLSDELPIADDEEAWTRAVEEVMPLDDILVAEIELEEDLPLETALESVEAEVGESISDELCVVETAKAQ SQ EPSVESTDSTPSTSTVVSENDLSVKPMSRVAETGDVLEVETAVVGGPVSDVTASVVTNDIVSVEQAQQCGVSSLPIQDEA SQ SENQVHQVPDLQCTSETKVEIVQPRQDLRPRRLRKSKVDLSKYKHTVINNSVTLVLGDAIQIASLLPKCVLVNAANRHLK SQ HGGGIAGAINKASGGDVQEESDEYISNSGPLHVGDSVLLKGYGLADAILRVVGPDARNNEDAALLKRCYKTFNKHTIVVT SQ PLISSGIFSVDPKVSFEYLLANVTTTTYVVVNNEDIYNTLATPSKPDGLVYSFEGWRGTVRTAKNYGFTCFICTEYSANV SQ KFLRTKGVDTTKKIQTVDGVSYYLYSARDALTDVIAAANGCPGICAMPFGYVTHGLDLAQSGNYVRQVKVPYVCLLASKE SQ QIPIMNSDVAIQTPETAFINNVTSNGGYHSWHLVSGDLIVKDVCYKKLLHWSGQTICYADNKFYVVKNDVALPFSDLEAC SQ RAYLTSRAAQQVNIEVLVTIDGVNFRTVILNDATTFRKQLGATFYKGVDISDALPTVKMGGESLFVADNLSESEEVVLKE SQ YYGTSDVTFLQRYYSLQPLVQQWKFVVHDGVKSLKLSNYNCYINATIMMIDMLHDIKFVVPALQNAYLRYKGGDPYDFLA SQ LIMAYGDCTFDNPDDEAKLLHTLLAKAELTVSAKMVWREWCTVCGIRDIEYTGMRACVYAGVNSMEELQSVFNETCVCGS SQ VKHRQLVEHSTPWLLVSGLNEVKVSTSTDPVYRAFNVFQGVETSVGHYVHVRVKDGLFYKYDSGSLTKTSDMKCKMTSVW SQ YPKVRYTADCNVVVYDLDGVTKVEVNPDLSNYYMKDGKYYTSKPTIKYSPATILPGSVYSNSCLVGVDGTPGSDTISKFF SQ NDLLGFDETKPISKKLTYSLLPNEDGDVLLSEFNNYNPVYKKGVMLKGKPILWVNNGVCDSALNKPNRASLRQLYDVAPI SQ VLDNKYTVLQDNTSQLIEPNVPVVEDVSITTRKLIEVKCKGLNKPFVKGNFSFVNDPNGVTVVDTLGLTELRALYVDINT SQ RYIVLRDNNWSSLFKLHTVESGDLQIVANGGSVTRRARVLLGASSLFASFAKITVTATTAACKTAGRSFCKFVVNYGVLQ SQ NMFLFLKMLFFLPFNYLWPKKQPTVDVGVSGLRTAGVVTTNIVKQCGTAAYYMLLGKFKRVDWKATLRLFLLLCTTILLL SQ SSIYHLVIFNQVLSSDVMLEDATGILAMYKEVRSYLGIRTLCDGLAVEYRNTSFDVVDFCSNRSVLCQWCLIGQDSLTRY SQ SALQMLQTHITSYVLNIDWIWFALEFFLAYVLYTSSFNVLLLVVTAQYFFAYTSAFVNWRAYNYIVSGLFFLVTHIPLHG SQ LVRVYNFLACLWFLRKFYSHVINGCKDTACLLCYKRNRLTRVEASTIVCGTKRTFYIAANGGTSYCCKHNWNCVECDTAG SQ VGNTFICTEVANDLTTTLRRLIKPTDQSHYYVDSVVVKDAVVELHYNRDGSSCYERYPLCYFTNLEKLKFKEVCKTPTGI SQ PEHNFLIYDTNDRGQENLARSACVYYSQVLCKPMLLVDVNLVTTVGDSREIAIKMLDSFINSFISLFSVSRDKLEKLINT SQ ARDCVRRGDDFQTVLKTFTDAARGHAGVESDVETTMVVDALQYAHKNDIQLTTECYNNYVPGYIKPDSINTLDLGCLIDL SQ KAASVNQTSMRNANGACVWNSGDYMKLSDSFKRQIRIACRKCNIPFRLTTSKLRAADNILSVKFSATKIVGGAPSWLLRV SQ RDLTVKGYCILTLFVFTVAVLSWFCLPSYSIATVNFNDDRILTYKVIENGIVRDIAPNDACFANKYGHFSKWFNENHGGV SQ YRNSVDCPITIAVIAGVAGARVANVPATLAWVGRQIVLFVSRVFANTNVCFTPTNEIPYDTFSDSGCVLSSECTLFRDAE SQ GNLNPFCYDPTVLPGASSYADMKPHVRYDMYDSDMYIKFPEVIFESTLRITKTLATQYCRFGSCEESAAGVCISTNGSWA SQ LYNQNYSTRPGIYCGDDYFDIVRRLAVSLFQPVTYFQLSTSLAMGLVLCVFLTAAFYYINKVKRALADYTQCAVVAVVAA SQ LLNSLCLCFIVANPLLVAPYTAMYYYATFYLTGEPAFIMHISWYVMFGTVVPIWMLASYTVGVMLRHLFWVLAYFSKKHV SQ DVFTDGKLNCSFQDAASNIFVIGKDTYVALRNAITQDSFVRYLSLFNKYKYYSGAMDTASYREACAAHLCKALQTYSETG SQ SDILYQPPNCSVTSSVLQSGLVKMSAPSGAVENCIVQVTCGSMTLNGLWLDNTVWCPRHIMCPADQLTDPNYDALLISKT SQ NHSFIVQKHIGAQANLRVVAHSMVGVLLKLTVDVANPSTPAYTFSTVKPGASFSVLACYNGKPTGVFTVNLRHNSTIKGS SQ FLCGSCGSVGYTENGGVLNFVYMHQMELSNGTHTGSSFDGVMYGAFEDKQTHQLQLTDKYCTINVVAWLYAAVLNGCKWF SQ VKPTRVGIVTYNEWALSNQFTEFVGTQSIDMLAHRTGVSVEQMLAAIQSLHAGFQGKTILGQSTLEDEFTPDDVNMQVMG SQ VVMQSGVKRISYGFMHWLMSTLVLAYVSVMQLTKFTMWTYLFETIPTQMTPLLFGFMACVMFTVKHKHTFLSLFLLPVAL SQ CLTYANIVYEPQTLVSSTLIAVANWLTPTSVYMRTTHLDFGLYISLSFVLAIIVRRLYRPSMSNLALALCSGVMWFYTYV SQ IGDHSSPITYLMFITTLTSDYTITVFATVNLAKFISGLVFLYAPHLGFILPEVKLVLLIYLCLGYMCTMYFGVFSLLNLK SQ LRVPLGVYDYSVSTQEFRFLTGNGLHAPRNSWEALILNFKLLGIGGTPCIKVATVQSKLTDLKCTSVVLLTVLQQLHLES SQ NSKAWSYCVKLHNEILAAVDPTEAFERFVCLFATLMSFSANVDLDALANDLFENSSVLQATLTEFSHLATYAELETAQSS SQ YQKALNSGDASPQVLKALQKAVNVAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDN SQ DVLNGVIANARNGCVPLSIVPLCASNKLRVVIPDISVWNKVVNWPSVSYAGSLWDVTVINNVDNEVVKPTDVVETNESLT SQ WPLVIECSRASSSAVKLQNNEIHPKGLKTMVVTAGIDQVNCSSSAVAYYEPVQGHRMVMGLLSENAHLKWAKVEGKDGFI SQ NIELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQLLGHIAATVRLQAGANTEFASNSTVLTLVAFAVDPAKAYLDYVG SQ SGGTPLSNYVKMLAPKTGTGVAISVKPEATADQETYGGASVCLYCRAHIEHPDVSGVCKYKTRFVQIPAHVRDPVGFLLK SQ NVPCNVCQYWVGYGCNCDALRNNTVPQSKDTNFLNRVRGSSVNARLEPCSSGLTTDVVYRAFDICNFKARVAGIGKYYKT SQ NTCRFVQVDDEGHKLDSYFIVKRHTMSNYELEKRCYDLLKDCDAVAIHDFFIFDVDKTKTPHIVRQSLTEYTMMDLVYAL SQ RHFDQNNCEVLKSILVKYGCCEQSYFDNKLWFDFVENPSVIGVYHKLGERIRQAMLNTVKMCDHMVKSGLVGVLTLDNQD SQ LNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCLAAETHKDCDFNKPLIEWLLLEYDYTDYKIGLFNKYFKHWD SQ QTYHPNCVNCGDDRCILHCANFNVLFSMVLPNTSFGPIVRKIFVDGVPFIVSCGYHYKELGLVMNMDVNIHRHRLALKEL SQ MMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVRPGNFNKDFYDFVVSRGFFKEGSSVTLKHFFFAQDGHAAIT SQ DYSYYAYNLPTMVDIKQMLFCMEVVDKYFDIYDGGCLNASEVIVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAVT SQ KRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVES SQ PHLMGWDYPKCDRAMPNMCRILASLILARKHSTCCTNSDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYAN SQ SVFNILQATTANVSALMSANGNTIIDREIKDMQFDLYINVYRKVVPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYA SQ AKGYVASIQNFKETLYYQNNVFMSEAKCWVETNLEKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTD SQ GTVMMERYVSLAIDAYPLTKHDDTEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDDSAKFWEEGFYRDLYSSPTTL SQ QAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATTHKMVLSVSPYVCNAPGCDVSDVTKLYLGGMSYYCNDHRPVC SQ SFPLCANGLVFGLYKNMCTGSSSIMEFNRLATCDWSDSGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVG SQ ERELILVWEVGKSKPPLNRNYVFTGYHLTKNSKVQLGEYVFERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLSAPT SQ IVNQERYLKITGIYPTITVPEEFANHVVNFQKAGFSKYVTVQGPPGTGKSHFAIGLAIYYPTARIVYTACSHAAVDALCA SQ KAFKYLNIAKCSRIIPAKARVECYDRFKVNDTNAQYLFSTVNALPEISVDILVVDEVSMCTNYDLSIINSRVKAKHIVYV SQ GDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSVCYRCPKEIVNTVSALVYNNKLSAKKDASGQCFKILFKGS SQ VTHDASSAINRPQLNFVKTFIAANPNWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNLN SQ RFNVAVTRAQKGILCVMTSQVLFDSLEFAELSLNNYKLQSQIVTGLFKDCSREDVGLPPAYAPTYLSVDAKYKTTDELCV SQ NLNITPNVTYSRVISRMGFKLDATIPGYPKLFITRDEAIRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQP SQ VGVVDTEWGSMLTTISARPPPGEQFKHLVPLMNKGATWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKI SQ GKEQRCCMCSRRASTFSSPLQSYACWSHSSGYDYVYNPFFVDVQQWGYVGNLATNHDRYCGIHAGAHVASSDAIMTRCLA SQ IYDCFIERVDWDVTYPYISHEQKLNSCCRTVERNVVRSAVLSGKFDKIYDIGNPKGIPIISEPVEWHFYDAQPLSNKVKK SQ LFYTDDVAKQFEDGLCLFWNCNVSKYPSNAVVCRFDTRVHSEFNLPGCNGGSLYVNKHAFHTPAYDINAFRDLKPLPFFY SQ YSTTPCEVHGSGNMLEDIDYVPLKSAVCITACNLGGAVCRKHAAEYRDYMEAYNIVSAAGFRLWVYKTFDIYNLWSTFVK SQ VQGLENIAFNVIKQGHFTGVDGELPVAVVNDKIFTKNGTDDVCIFKNETALPTNVAFELYAKRAVRSHPDLNLLRNLEVD SQ VCYNFVLWDYDRNNIYGTTTIGVCKYTDIDVNPNLNMCFDIRDKGSLERFMSMPNGVLISDRKIKNYPCIIGPKHAYFNG SQ AILRNIDAKQPITFYLYKKVNNEFVSFSDTFYTCGRTVNDFTALTPMEEDFLVLDSDVFIKKYSLEDYAFEHVVYGDFSH SQ TTLGGLHLLIGLYKKMRDGHILMEEMLKDRATVHNYFITDSNTASYKAVCSVIDLRLDDFVNIIKEMDLDVVSKVVKVPI SQ DLTMIEFMLWCKDGKVQTFYPRLQATNDWKPGLTMPSLFKVQQMNLEPCLLANYKQSIPMPNGVHMNVAKYMQLCQYLNT SQ CTLAVPANMRVIHFGAGCEKGVAPGTSVLRQWLPLDAVLIDNDLNEFVSDADITIFGDCVTVHVGQQVDLLISDMYDPCT SQ KAVGEVNQTKALFFVYLCNFIKNNLALGGSVAIKITEHSWSADLYKIMGRFAYWTVFCTNANASSSEGFLIGINFLGELK SQ EEIDGNVMHANYIFWRNSTPMNLSTYSLFDLSRFPLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLNVSTDVLV SQ NFRKRL // 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 P0C6W5; PN 2'-O-methyltransferase; GN rep; OS 694006; 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: P0C6W5; DR UNIPROT: A3EXG5; DR PDB: 5UTV; 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: 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, ECO:0000269|PubMed:19264783}. [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 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 NRVRGTSGVARLVPLGSGVQPDIVLRAFDICNTKVAGFGLHLKNNCCRYQELDADGTQLDSYFVVKRHTESNYLLEQRCY SQ EKLKDCGVVARHDFFKFNIEGVMTPHVSRERLTKYTMADLVYSLRHFDNNNCDTLKEILVLRGCCTADYFDRKDWYDPVE SQ NPDIIRVYHNLGETVRKAVLSAVKMADSMVEQGLIGVLTLDNQDLNGQWYDFGDFIEGPAGAGVAVMDTYYSLAMPVYTM SQ TNMLAAECHVDGDFSKPKRVWDICKYDYTQFKYSLFSKYFKYWDMQYHPNCVACADDRCILHCANFNILFSMVLPNTSFG SQ PLVQKIYVDGVPFVVSTGYHYRELGVVMNQDIRQHAQRLSLRELLVYAADPAMHVAASNALADKRTVCMSVAAMTTGVTF SQ QTVKPGQFNEDFYNFAVKCGFFKEGSTISFKHFFYAQDGNAAISDYDYYRYNLPTMCDIKQLLFSLEVVDKYFDCYDGGC SQ LQASQVVVANYDKSAGFPFNKFGKARLYYESLSYADQDELFAYTKRNVLPTITQMNLKYAISAKNRARTVAGVSIASTMT SQ NRQFHQKMLKSIAAARGASVVIGTTKFYGGWNRMLRTLCEGVENPHLMGWDYPKCDRAMPNLLRIFASLILARKHATCCN SQ ASERFYRLANECAQVLSEMVLCGGGFYVKPGGTSSGDSTTAYANSVFNICQAVSANLNTFLSIDGNKIYTTYVQELQRRL SQ YLGIYRSNTVDNELVLDYYNYLRKHFSMMILSDDGVVCYNADYAQKGYVADIQGFKELLYFQNNVFMSESKCWVEPDITK SQ GPHEFCSQHTMLVDMKGEQVYLPYPDPSRILGAGCFVDDLLKTDGTLMMERYVSLAIDAYPLTKHPDPEYQNVFWCYLQY SQ IKKLHEELTGHLLDTYSVMLASDNASKYWEVEFYENMYMESATLQSVGTCVVCNSQTSLRCGGCIRRPFLCCKCCYDHVV SQ STTHKLVLSVTPYVCNNPSCDVADVTQLYLGGMSYYCRDHRPPISFPLCANGQVFGLYKNICTGSPDVADFNSLATCDWS SQ NSKDYVLANTATERLKLFAAETLRATEENAKQAYASAVVKEVLSDRELVLSWETGKTRPPLNRNYVFTGFHITKNSKVQL SQ GEYIFEKGDYGDVVNYRSSTTYKLQVGDYFVLTSHSVQPLSSPTLLPQERYTKLVGLYPAMNVPESFASNVVHYQRVGMS SQ RYTTVQGPPGTGKSHLSIGLALYYPSAKIVYTACSHAAVDALCEKAHKNLPINRCSRIVPAKARVECFSKFKVNDVGAQY SQ VFSTINALPETTADILVVDEVSMCTNYDLSMINARVRAKHIVYVGDPAQLPAPRTLLTKGTLAPEHFNSVCRLMVAVGPD SQ IFLATCYRCPKEIVDTVSALVYDKKLKANKVTTGECYKCYYKGSVTHDSSSAINKPQLGLVKEFLIKNPKWQSAVFISPY SQ NSQNSVARRMLGLQTQTVDSSQGSEFDYVIYCQTSDTAHALNVNRFNVAITRAKKGILCVMSDSTLYESLEFTPLDVNDY SQ VKPKMQSEVTVGLFKDCAKAEPLGPAYAPTFVSVNDKFKLNESLCVHFDTTELQMPYNRLISKMGFKFDLNIPGYSKLFI SQ TREQAIREVRGWVGFDVEGAHACGPNIGTNLPLQIGFSTGVNFVVTPSGYIDTESGSRLANVVSKAPPGDQFKHLIPLMR SQ KGEPWSVVRKRIVEMLCDTLDGVSDTVTFVTWAHGFELTTLHYFAKVGPERKCFMCPRRATLFSSVYGAYSCWSHHRHIG SQ GADFVYNPFLVDVQQWGYVGNLQVNHDNVCDVHKGAHVASCDAIMTRCLAIHDCFCGEVNWDVEYPIIANELAINRACRS SQ VQRVVLKAAVKALHIETIYDIGNPKAIKVYGVNVNNWNFYDTNPVVEGVKQLHYVYDVHRDQFKDGLAMFWNCNVDCYPH SQ NALVCRFDTRVLSKLNLAGCNGGSLYVNQHAFHTDAFNKNAFVNLKPLPFFYYSDTACENATGVSTNYVSEVDYVPLKSN SQ VCITRCNLGGAVCKKHADEYRNFLESYNTMVSAGFTLWVDKTFDVFNLWSTFVKLQSLENVAYNVLKSGHFTAVAGELPV SQ AILNDRLYIKEDGADKLLFTNNTCLPTNVAFELWAKRSVNVVPEVKLLRNLGVTCTYNLVIWDYESNAPLVPNTVGICTY SQ TDLTKLDDQVVLVDGRQLDAYSKFCQLKNAIYFSPSKPKCVCTRGPTHASINGVVVEAPDRGTAFWYAMRKDGAFVQPTD SQ GYFTQSRTVDDFQPRTQLEIDFLDLEQSCFLDKYDLHDLGLEHIVYGQFDGTIGGLHLLIGAVRRKRTAHLVMETVLGTD SQ TVTSYAVIDQPTASSKQVCSVVDIILDDFIALIKAQDRSVVSKVVQCCLDFKVFRFMLWCKGGKISTFYPQLQAKQDWKP SQ GYSMPALYKVQNAVLEPCLLHNYGQAARLPSGTLMNVAKYTQLCQYLNTCSLAVPAKMRVMHFGAGSDKGVCPGTAVLKQ SQ WLPADAYLVDNDLCYCASDADSTYVGSCETFFSVNKWDFIFSDMYDARTKNTSGDNTSKEGFFTYLTGFIRSKLALGGSI SQ AIKITEHSWSADLYAIMGHFNWWTCFCTSVNSSSSEAFLIGVNYIGVGALLDGWQMHANYVFWRNSTVMQLSSYSLYDLQ SQ RFPLRLKGTPVMSLKEDQLNELVLNLIRAGRLIVRDAVDIGVRGVACSGV // ID P0C6X1; PN Putative 2'-O-methyl transferase; GN rep; OS 11137; 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: P0C6X1; DR UNIPROT: Q05002; DR UNIPROT: Q9DLN0; DR UNIPROT: Q9DLN1; DR PDB: 1P9S; DR PDB: 2J97; DR PDB: 2J98; DR PDB: 3EJG; DR PDB: 4RS4; DR PDB: 4S1T; 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. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). 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 MACNRVTLAVASDSEISANGCSTIAQAVRRYSEAASNGFRACRFVSLDLQDCIVGIADDTYVMGLHGNQTLFCNIMKFSD SQ RPFMLHGWLVFSNSNYLLEEFDVVFGKRGGGNVTYTDQYLCGADGKPVMSEDLWQFVDHFGENEEIIINGHTYVCAWLTK SQ RKPLDYKRQNNLAIEEIEYVHGDALHTLRNGSVLEMAKEVKTSSKVVLSDALDKLYKVFGSPVMTNGSNILEAFTKPVFI SQ SALVQCTCGTKSWSVGDWTGFKSSCCNVISNKLCVVPGNVKPGDAVITTQQAGAGIKYFCGMTLKFVANIEGVSVWRVIA SQ LQSVDCFVASSTFVEEEHVNRMDTFCFNVRNSVTDECRLAMLGAEMTSNVRRQVASGVIDISTGWFDVYDDIFAESKPWF SQ VRKAEDIFGPCWSALASALKQLKVTTGELVRFVKSICNSAVAVVGGTIQILASVPEKFLNAFDVFVTAIQTVFDCAVETC SQ TIAGKAFDKVFDYVLLDNALVKLVTTKLKGVRERGLNKVKYATVVVGSTEEVKSSRVERSTAVLTIANNYSKLFDEGYTV SQ VIGDVAYFVSDGYFRLMASPNSVLTTAVYKPLFAFNVNVMGTRPEKFPTTVTCENLESAVLFVNDKITEFQLDYSIDVID SQ NEIIVKPNISLCVPLYVRDYVDKWDDFCRQYSNESWFEDDYRAFISVLDITDAAVKAAESKAFVDTIVPPCPSILKVIDG SQ GKIWNGVIKNVNSVRDWLKSLKLNLTQQGLLGTCAKRFKRWLGILLEAYNAFLDTVVSTVKIGGLTFKTYAFDKPYIVIR SQ DIVCKVENKTEAEWIELFPHNDRIKSFSTFESAYMPIADPTHFDIEEVELLDAEFVEPGCGGILAVIDEHVFYKKDGVYY SQ PSNGTNILPVAFTKAAGGKVSFSDDVEVKDIEPVYRVKLCFEFEDEKLVDVCEKAIGKKIKHEGDWDSFCKTIQSALSVV SQ SCYVNLPTYYIYDEEGGNDLSLPVMISEWPLSVQQAQQEATLPDIAEDVVDQVEEVNSIFDIETVDVKHDVSPFEMPFEE SQ LNGLKILKQLDNNCWVNSVMLQIQLTGILDGDYAMQFFKMGRVAKMIERCYTAEQCIRGAMGDVGLCMYRLLKDLHTGFM SQ VMDYKCSCTSGRLEESGAVLFCTPTKKAFPYGTCLNCNAPRMCTIRQLQGTIIFVQQKPEPVNPVSFVVKPVCSSIFRGA SQ VSCGHYQTNIYSQNLCVDGFGVNKIQPWTNDALNTICIKDADYNAKVEISVTPIKNTVDTTPKEEFVVKEKLNAFLVHDN SQ VAFYQGDVDTVVNGVDFDFIVNAANENLAHGGGLAKALDVYTKGKLQRLSKEHIGLAGKVKVGTGVMVECDSLRIFNVVG SQ PRKGKHERDLLIKAYNTINNEQGTPLTPILSCGIFGIKLETSLEVLLDVCNTKEVKVFVYTDTEVCKVKDFVSGLVNVQK SQ VEQPKIEPKPVSVIKVAPKPYRVDGKFSYFTEDLLCVADDKPIVLFTDSMLTLDDRGLALDNALSGVLSAAIKDCVDINK SQ AIPSGNLIKFDIGSVVVYMCVVPSEKDKHLDNNVQRCTRKLNRLMCDIVCTIPADYILPLVLSSLTCNVSFVGELKAAEA SQ KVITIKVTEDGVNVHDVTVTTDKSFEQQVGVIADKDKDLSGAVPSDLNTSELLTKAIDVDWVEFYGFKDAVTFATVDHSA SQ FAYESAVVNGIRVLKTSDNNCWVNAVCIALQYSKPHFISQGLDAAWNKFVLGDVEIFVAFVYYVARLMKGDKGDAEDTLT SQ KLSKYLANEAQVQLEHYSSCVECDAKFKNSVASINSAIVCASVKRDGVQVGYCVHGIKYYSRVRSVRGRAIIVSVEQLEP SQ CAQSRLLSGVAYTAFSGPVDKGHYTVYDTAKKSMYDGDRFVKHDLSLLSVTSVVMVGGYVAPVNTVKPKPVINQLDEKAQ SQ KFFDFGDFLIHNFVIFFTWLLSMFTLCKTAVTTGDVKIMAKAPQRTGVVLKRSLKYNLKASAAVLKSKWWLLAKFTKLLL SQ LIYTLYSVVLLCVRFGPFNFCSETVNGYAKSNFVKDDYCDGSLGCKMCLFGYQELSQFSHLDVVWKHITDPLFSNMQPFI SQ VMVLLLIFGDNYLRCFLLYFVAQMISTVGVFLGYKETNWFLHFIPFDVICDELLVTVIVIKVISFVRHVLFGCENPDCIA SQ CSKSARLKRFPVNTIVNGVQRSFYVNANGGSKFCKKHRFFCVDCDSYGYGSTFITPEVSRELGNITKTNVQPTGPAYVMI SQ DKVEFENGFYRLYSCETFWRYNFDITESKYSCKEVFKNCNVLDDFIVFNNNGTNVTQVKNASVYFSQLLCRPIKLVDSEL SQ LSTLSVDFNGVLHKAYIDVLRNSFGKDLNANMSLAECKRALGLSISDHEFTSAISNAHRCDVLLSDLSFNNFVSSYAKPE SQ EKLSAYDLACCMRAGAKVVNANVLTKDQTPIVWHAKDFNSLSAEGRKYIVKTSKAKGLTFLLTINENQAVTQIPATSIVA SQ KQGAGDAGHSLTWLWLLCGLVCLIQFYLCFFMPYFMYDIVSSFEGYDFKYIENGQLKNFEAPLKCVRNVFENFEDWHYAK SQ FGFTPLNKQSCPIVVGVSEIVNTVAGIPSNVYLVGKTLIFTLQAAFGNAGVCYDIFGVTTPEKCIFTSACTRLEGLGGNN SQ VYCYNTALMEGSLPYSSIQANAYYKYDNGNFIKLPEVIAQGFGFRTVRTIATKYCRVGECVESNAGVCFGFDKWFVNDGR SQ VANGYVCGTGLWNLVFNILSMFSSSFSVAAMSGQILLNCALGAFAIFCCFLVTKFRRMFGDLSVGVCTVVVAVLLNNVSY SQ IVTQNLVTMIAYAILYFFATRSLRYAWIWCAAYLIAYISFAPWWLCAWYFLAMLTGLLPSLLKLKVSTNLFEGDKFVGTF SQ ESAAAGTFVIDMRSYEKLANSISPEKLKSYAASYNRYKYYSGNANEADYRCACYAYLAKAMLDFSRDHNDILYTPPTVSY SQ GSTLQAGLRKMAQPSGFVEKCVVRVCYGNTVLNGLWLGDIVYCPRHVIASNTTSAIDYDHEYSIMRLHNFSIISGTAFLG SQ VVGATMHGVTLKIKVSQTNMHTPRHSFRTLKSGEGFNILACYDGCAQGVFGVNMRTNWTIRGSFINGACGSPGYNLKNGE SQ VEFVYMHQIELGSGSHVGSSFDGVMYGGFEDQPNLQVESANQMLTVNVVAFLYAAILNGCTWWLKGEKLFVEHYNEWAQA SQ NGFTAMNGEDAFSILAAKTGVCVERLLHAIQVLNNGFGGKQILGYSSLNDEFSINEVVKQMFGVNLQSGKTTSMFKSISL SQ FAGFFVMFWAELFVYTTTIWVNPGFLTPFMILLVALSLCLTFVVKHKVLFLQVFLLPSIIVAAIQNCAWDYHVTKVLAEK SQ FDYNVSVMQMDIQGFVNIFICLFVALLHTWRFAKERCTHWCTYLFSLIAVLYTALYSYDYVSLLVMLLCAISNEWYIGAI SQ IFRICRFGVAFLPVEYVSYFDGVKTVLLFYMLLGFVSCMYYGLLYWINRFCKCTLGVYDFCVSPAEFKYMVANGLNAPNG SQ PFDALFLSFKLMGIGGPRTIKVSTVQSKLTDLKCTNVVLMGILSNMNIASNSKEWAYCVEMHNKINLCDDPETAQELLLA SQ LLAFFLSKHSDFGLGDLVDSYFENDSILQSVASSFVGMPSFVAYETARQEYENAVANGSSPQIIKQLKKAMNVAKAEFDR SQ ESSVQKKINRMAEQAAAAMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILNMARNGVVPLSVIPATSAARLVVV SQ VPDHDSFVKMMVDGFVHYAGVVWTLQEVKDNDGKNVHLKDVTKENQEILVWPLILTCERVVKLQNNEIMPGKMKVKATKG SQ EGDGGITSEGNALYNNEGGRAFMYAYVTTKPGMKYVKWEHDSGVVTVELEPPCRFVIDTPTGPQIKYLYFVKNLNNLRRG SQ AVLGYIGATVRLQAGKQTEFVSNSHLLTHCSFAVDPAAAYLDAVKQGAKPVGNCVKMLTNGSGSGQAITCTIDSNTTQDT SQ YGGASVCIYCRAHVAHPTMDGFCQYKGKWVQVPIGTNDPIRFCLENTVCKVCGCWLNHGCTCDRTAIQSFDNSYLNRVRG SQ SSAARLEPCNGTDIDYCVRAFDVYNKDASFIGKNLKSNCVRFKNVDKDDAFYIVKRCIKSVMDHEQSMYNLLKGCNAVAK SQ HDFFTWHEGRTIYGNVSRQDLTKYTMMDLCFALRNFDEKDCEVFKEILVLTGCCSTDYFEMKNWFDPIENEDIHRVYAAL SQ GKVVANAMLKCVAFCDEMVLKGVVGVLTLDNQDLNGNFYDFGDFVLCPPGMGIPYCTSYYSYMMPVMGMTNCLASECFMK SQ SDIFGQDFKTFDLLKYDFTEHKEVLFNKYFKYWGQDYHPDCVDCHDEMCILHCSNFNTLFATTIPNTAFGPLCRKVFIDG SQ VPVVATAGYHFKQLGLVWNKDVNTHSTRLTITELLQFVTDPTLIVASSPALVDKRTVCFSVAALSTGLTSQTVKPGHFNK SQ EFYDFLRSQGFFDEGSELTLKHFFFTQKGDAAIKDFDYYRYNRPTMLDIGQARVAYQVAARYFDCYEGGCITSREVVVTN SQ LNKSAGWPLNKFGKAGLYYESISYEEQDAIFSLTKRNILPTMTQLNLKYAISGKERARTVGGVSLLATMTTRQFHQKCLK SQ SIVATRNATVVIGTTKFYGGWDNMLKNLMADVDDPKLMGWDYPKCDRAMPSMIRMLSAMILGSKHVTCCTASDKFYRLSN SQ ELAQVLTEVVYSNGGFYFKPGGTTSGDATTAYANSVFNIFQAVSSNINCVLSVNSSNCNNFNVKKLQRQLYDNCYRNSNV SQ DESFVDDFYGYLQKHFSMMILSDDSVVCYNKTYAGLGYIADISAFKATLYYQNGVFMSTAKCWTEEDLSIGPHEFCSQHT SQ MQIVDENGKYYLPYPDPSRIISAGVFVDDITKTDAVILLERYVSLAIDAYPLSKHPKPEYRKVFYALLDWVKHLNKTLNE SQ GVLESFSVTLLDEHESKFWDESFYASMYEKSTVLQAAGLCVVCGSQTVLRCGDCLRRPMLCTKCAYDHVFGTDHKFILAI SQ TPYVCNTSGCNVNDVTKLYLGGLNYYCVDHKPHLSFPLCSAGNVFGLYKSSALGSMDIDVFNKLSTSDWSDIRDYKLAND SQ AKESLRLFAAETVKAKEESVKSSYAYATLKEIVGPKELLLLWESGKAKPPLNRNSVFTCFQITKDSKFQVGEFVFEKVDY SQ GSDTVTYKSTATTKLVPGMLFILTSHNVAPLRAPTMANQEKYSTIYKLHPSFNVSDAYANLVPYYQLIGKQRITTIQGPP SQ GSGKSHCSIGIGVYYPGARIVFTACSHAAVDSLCAKAVTAYSVDKCTRIIPARARVECYSGFKPNNNSAQYVFSTVNALP SQ EVNADIVVVDEVSMCTNYDLSVINQRISYKHIVYVGDPQQLPAPRVLISKGVMEPIDYNVVTQRMCAIGPDVFLHKCYRC SQ PAEIVNTVSELVYENKFVPVKEASKQCFKIFERGSVQVDNGSSINRRQLDVVKRFIHKNSTWSKAVFISPYNSQNYVAAR SQ LLGLQTQTVDSAQGSEYDYVIFAQTSDTAHACNANRFNVAITRAKKGIFCIMSDRTLFDALKFFEITMTDLQSESSCGLF SQ KDCARNPIDLPPSHATTYLSLSDRFKTSGDLAVQIGNNNVCTYEHVISYMGFRFDVSMPGSHSLFCTRDFAMRHVRGWLG SQ MDVEGAHVTGDNVGTNVPLQVGFSNGVDFVAQPEGCVLTNTGSVVKPVRARAPPGEQFTHIVPLLRKGQPWSVLRKRIVQ SQ MIADFLAGSSDVLVFVLWAGGLELTTMRYFVKIGAVKHCQCGTVATCYNSVSNDYCCFKHALGCDYVYNPYVIDIQQWGY SQ VGSLSTNHHAICNVHRNEHVASGDAIMTRCLAVYDCFVKNVDWSITYPMIANENAINKGGRTVQSHIMRAAIKLYNPKAI SQ HDIGNPKGIRCAVTDAKWYCYDKNPINSNVKTLEYDYMTHGQMDGLCLFWNCNVDMYPEFSIVCRFDTRTRSTLNLEGVN SQ GGSLYVNNHAFHTPAYDKRAMAKLKPAPFFYYDDGSCEVVHDQVNYVPLRATNCITKCNIGGAVCSKHANLYRAYVESYN SQ IFTQAGFNIWVPTTFDCYNLWQTFTEVNLQGLENIAFNVVNKGSFVGADGELPVAISGDKVFVRDGNTDNLVFVNKTSLP SQ TNIAFELFAKRKVGLTPPLSILKNLGVVATYKFVLWDYEAERPLTSFTKSVCGYTDFAEDVCTCYDNSIQGSYERFTLST SQ NAVLFSATAVKTGGKSLPAIKLNFGMLNGNAIATVKSEDGNIKNINWFVYVRKDGKPVDHYDGFYTQGRNLQDFLPRSTM SQ EEDFLNMDIGVFIQKYGLEDFNFEHVVYGDVSKTTLGGLHLLISQVRLSKMGILKAEEFVAASDITLKCCTVTYLNDPSS SQ KTVCTYMDLLLDDFVSVLKSLDLTVVSKVHEVIIDNKPWRWMLWCKDNAVATFYPQLQSAEWKCGYSMPGIYKTQRMCLE SQ PCNLYNYGAGLKLPSGIMFNVVKYTQLCQYFNSTTLCVPHNMRVLHLGAGSDYGVAPGTAVLKRWLPHDAIVVDNDVVDY SQ VSDADFSVTGDCATVYLEDKFDLLISDMYDGRTKAIDGENVSKEGFFTYINGFICEKLAIGGSIAIKVTEYSWNKKLYEL SQ VQRFSFWTMFCTSVNTSSSEAFVVGINYLGDFAQGPFIDGNIIHANYVFWRNSTVMSLSYNSVLDLSKFNCKHKATVVVQ SQ LKDSDINEMVLSLVRSGKLLVRGNGKCLSFSNHLVSTK // 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 P0C6X5; PN Putative 2'-O-methyl transferase; GN rep; OS 277944; 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: P0C6X5; DR UNIPROT: Q6Q1S3; DR PDB: 5NH0; DR PDB: 6FV1; DR PDB: 6FV2; 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. {ECO:0000269|PubMed:20181693}. 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. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). {ECO:0000269|PubMed:20181693}. 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: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 MFYNQVTLAVASDSEISGFGFAIPSVAVRTYSEAAAQGFQACRFVAFGLQDCVTGINDDDYVIALTGTNQLCAKILPFSD SQ RPLNLRGWLIFSNSNYVLQDFDVVFGHGAGSVVFVDKYMCGFDGKPVLPKNMWEFRDYFNNNTDSIVIGGVTYQLAWDVI SQ RKDLSYEQQNVLAIESIHYLGTTGHTLKSGCKLTNAKPPKYSSKVVLSGEWNAVYRAFGSPFITNGMSLLDIIVKPVFFN SQ AFVKCNCGSESWSVGAWDGYLSSCCGTPAKKLCVVPGNVVPGDVIITSTSAGCGVKYYAGLVVKHITNITGVSLWRVTAV SQ HSDGMFVASSSYDALLHRNSLDPFCFDVNTLLSNQLRLAFLGASVTEDVKFAASTGVIDISAGMFGLYDDILTNNKPWFV SQ RKASGLFDAIWDAFVAAIKLVPTTTGVLVRFVKSIASTVLTVSNGVIIMCADVPDAFQSVYRTFTQAICAAFDFSLDVFK SQ IGDVKFKRLGDYVLTENALVRLTTEVVRGVRDARIKKAMFTKVVVGPTTEVKFSVIELATVNLRLVDCAPVVCPKGKIVV SQ IAGQAFFYSGGFYRFMVDPTTVLNDPVFTGDLFYTIKFSGFKLDGFNHQFVTASSATDAIIAVELLLLDFKTAVFVYTCV SQ VDGCSVIVRRDATFATHVCFKDCYNVWEQFCIDNCGEPWFLTDYNAILQSNNPQCAIVQASESKVLLERFLPKCPEILLS SQ IDDGHLWNLFVEKFNFVTDWLKTLKLTLTSNGLLGNCAKRFRRVLVKLLDVYNGFLETVCSVAYTAGVCIKYYAVNVPYV SQ VISGFVSRVIRRERCDMTFPCVSCVTFFYEFLDTCFGVSKPNAIDVEHLELKETVFVEPKDGGQFFVSGDYLWYVVDDIY SQ YPASCNGVLPVAFTKLAGGKISFSDDVIVHDVEPTHKVKLIFEFEDDVVTSLCKKSFGKSIIYTGDWEGLHEVLTSAMNV SQ IGQHIKLPQFYIYDEEGGYDVSKPVMISQWPISNDSNGCVVEASTDFHQLECIVDDSVREEVDIIEQPFEEVEHVLSIKQ SQ PFSFSFRDELGVRVLDQSDNNCWISTTLVQLQLTKLLDDSIEMQLFKVGKVDSIVQKCYELSHLISGSLGDSGKLLSELL SQ KEKYTCSITFEMSCDCGKKFDDQVGCLFWIMPYTKLFQKGECCICHKMQTYKLVSMKGTGVFVQDPAPIDIDAFPVKPIC SQ SSVYLGVKGSGHYQTNLYSFNKAIDGFGVFDIKNSSVNTVCFVDVDFHSVEIEAGEVKPFAVYKNVKFYLGDISHLVNCV SQ SFDFVVNAANENLLHGGGVARAIDILTEGQLQSLSKDYISSNGPLKVGAGVMLECEKFNVFNVVGPRTGKHEHSLLVEAY SQ NSILFENGIPLMPLLSCGIFGVRIENSLKALFSCDINKPLQVFVYSSNEEQAVLKFLDGLDLTPVIDDVDVVKPFRVEGN SQ FSFFDCGVNALDGDIYLLFTNSILMLDKQGQLLDTKLNGILQQAALDYLATVKTVPAGNLVKLFVESCTIYMCVVPSIND SQ LSFDKNLGRCVRKLNRLKTCVIANVPAIDVLKKLLSSLTLTVKFVVESNVMDVNDCFKNDNVVLKITEDGINVKDVVVES SQ SKSLGKQLGVVSDGVDSFEGVLPINTDTVLSVAPEVDWVAFYGFEKAALFASLDVKPYGYPNDFVGGFRVLGTTDNNCWV SQ NATCIILQYLKPTFKSKGLNVLWNKFVTGDVGPFVSFIYFITMSSKGQKGDAEEALSKLSEYLISDSIVTLEQYSTCDIC SQ KSTVVEVKSAIVCASVLKDGCDVGFCPHRHKLRSRVKFVNGRVVITNVGEPIISQPSKLLNGIAYTTFSGSFDNGHYVVY SQ DAANNAVYDGARLFSSDLSTLAVTAIVVVGGCVTSNVPTIVSEKISVMDKLDTGAQKFFQFGDFVMNNIVLFLTWLLSMF SQ SLLRTSIMKHDIKVIAKAPKRTGVILTRSFKYNIRSALFVIKQKWCVIVTLFKFLLLLYAIYALVFMIVQFSPFNSLLCG SQ DIVSGYEKSTFNKDIYCGNSMVCKMCLFSYQEFNDLDHTSLVWKHIRDPILISLQPFVILVILLIFGNMYLRFGLLYFVA SQ QFISTFGSFLGFHQKQWFLHFVPFDVLCNEFLATFIVCKIVLFVRHIIVGCNNADCVACSKSARLKRVPLQTIINGMHKS SQ FYVNANGGTCFCNKHNFFCVNCDSFGPGNTFINGDIARELGNVVKTAVQPTAPAYVIIDKVDFVNGFYRLYSGDTFWRYD SQ FDITESKYSCKEVLKNCNVLENFIVYNNSGSNITQIKNACVYFSQLLCEPIKLVNSELLSTLSVDFNGVLHKAYVDVLCN SQ SFFKELTANMSMAECKATLGLTVSDDDFVSAVANAHRYDVLLSDLSFNNFFISYAKPEDKLSVYDIACCMRAGSKVVNHN SQ VLIKESIPIVWGVKDFNTLSQEGKKYLVKTTKAKGLTFLLTFNDNQAITQVPATSIVAKQGAGFKRTYNFLWYVCLFVVA SQ LFIGVSFIDYTTTVTSFHGYDFKYIENGQLKVFEAPLHCVRNVFDNFNQWHEAKFGVVTTNSDKCPIVVGVSERINVVPG SQ VPTNVYLVGKTLVFTLQAAFGNTGVCYDFDGVTTSDKCIFNSACTRLEGLGGDNVYCYNTDLIEGSKPYSTLQPNAYYKY SQ DAKNYVRFPEILARGFGLRTIRTLATRYCRVGECRDSHKGVCFGFDKWYVNDGRVDDGYICGDGLIDLLVNVLSIFSSSF SQ SVVAMSGHMLFNFLFAAFITFLCFLVTKFKRVFGDLSYGVFTVVCATLINNISYVVTQNLFFMLLYAILYFVFTRTVRYA SQ WIWHIAYIVAYFLLIPWWLLTWFSFAAFLELLPNVFKLKISTQLFEGDKFIGTFESAAAGTFVLDMRSYERLINTISPEK SQ LKNYAASYNKYKYYSGSASEADYRCACYAHLAKAMLDYAKDHNDMLYSPPTISYNSTLQSGLKKMAQPSGCVERCVVRVC SQ YGSTVLNGVWLGDTVTCPRHVIAPSTTVLIDYDHAYSTMRLHNFSVSHNGVFLGVVGVTMHGSVLRIKVSQSNVHTPKHV SQ FKTLKPGDSFNILACYEGIASGVFGVNLRTNFTIKGSFINGACGSPGYNVRNDGTVEFCYLHQIELGSGAHVGSDFTGSV SQ YGNFDDQPSLQVESANLMLSDNVVAFLYAALLNGCRWWLCSTRVNVDGFNEWAMANGYTSVSSVECYSILAAKTGVSVEQ SQ LLASIQHLHEGFGGKNILGYSSLCDEFTLAEVVKQMYGVNLQSGKVIFGLKTMFLFSVFFTMFWAELFIYTNTIWINPVI SQ LTPIFCLLLFLSLVLTMFLKHKFLFLQVFLLPTVIATALYNCVLDYYIVKFLADHFNYNVSVLQMDVQGLVNVLVCLFVV SQ FLHTWRFSKERFTHWFTYVCSLIAVAYTYFYSGDFLSLLVMFLCAISSDWYIGAIVFRLSRLIVFFSPESVFSVFGDVKL SQ TLVVYLICGYLVCTYWGILYWFNRFFKCTMGVYDFKVSAAEFKYMVANGLHAPHGPFDALWLSFKLLGIGGDRCIKISTV SQ QSKLTDLKCTNVVLLGCLSSMNIAANSSEWAYCVDLHNKINLCDDPEKAQSMLLALLAFFLSKHSDFGLDGLIDSYFDNS SQ STLQSVASSFVSMPSYIAYENARQAYEDAIANGSSSQLIKQLKRAMNIAKSEFDHEISVQKKINRMAEQAATQMYKEARS SQ VNRKSKVISAMHSLLFGMLRRLDMSSVETVLNLARDGVVPLSVIPATSASKLTIVSPDLESYSKIVCDGSVHYAGVVWTL SQ NDVKDNDGRPVHVKEITKENVETLTWPLILNCERVVKLQNNEIMPGKLKQKPMKAEGDGGVLGDGNALYNTEGGKTFMYA SQ YISNKADLKFVKWEYEGGCNTIELDSPCRFMVETPNGPQVKYLYFVKNLNTLRRGAVLGFIGATIRLQAGKQTELAVNSG SQ LLTACAFSVDPATTYLEAVKHGAKPVSNCIKMLSNGAGNGQAITTSVDANTNQDSYGGASICLYCRAHVPHPSMDGYCKF SQ KGKCVQVPIGCLDPIRFCLENNVCNVCGCWLGHGCACDRTTIQSVDISYLNRARGSSAARLEPCNGTDIDKCVRAFDIYN SQ KNVSFLGKCLKMNCVRFKNADLKDGYFVIKRCTKSVMEHEQSMYNLLNFSGALAEHDFFTWKDGRVIYGNVSRHNLTKYT SQ MMDLVYAMRNFDEQNCDVLKEVLVLTGCCDNSYFDSKGWYDPVENEDIHRVYASLGKIVARAMLKCVALCDAMVAKGVVG SQ VLTLDNQDLNGNFYDFGDFVVSLPNMGVPCCTSYYSYMMPIMGLTNCLASECFVKSDIFGSDFKTFDLLKYDFTEHKENL SQ FNKYFKHWSFDYHPNCSDCYDDMCVIHCANFNTLFATTIPGTAFGPLCRKVFIDGVPLVTTAGYHFKQLGLVWNKDVNTH SQ SVRLTITELLQFVTDPSLIIASSPALVDQRTICFSVAALSTGLTNQVVKPGHFNEEFYNFLRLRGFFDEGSELTLKHFFF SQ AQNGDAAVKDFDFYRYNKPTILDICQARVTYKIVSRYFDIYEGGCIKACEVVVTNLNKSAGWPLNKFGKASLYYESISYE SQ EQDALFALTKRNVLPTMTQLNLKYAISGKERARTVGGVSLLSTMTTRQYHQKHLKSIVNTRNATVVIGTTKFYGGWNNML SQ RTLIDGVENPMLMGWDYPKCDRALPNMIRMISAMVLGSKHVNCCTATDRFYRLGNELAQVLTEVVYSNGGFYFKPGGTTS SQ GDASTAYANSIFNIFQAVSSNINRLLSVPSDSCNNVNVRDLQRRLYDNCYRLTSVEESFIDDYYGYLRKHFSMMILSDDG SQ VVCYNKDYAELGYIADISAFKATLYYQNNVFMSTSKCWVEEDLTKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGV SQ FVDDVVKTDAVVLLERYVSLAIDAYPLSKHPNSEYRKVFYVLLDWVKHLNKNLNEGVLESFSVTLLDNQEDKFWCEDFYA SQ SMYENSTILQAAGLCVVCGSQTVLRCGDCLRKPMLCTKCAYDHVFGTDHKFILAITPYVCNASGCGVSDVKKLYLGGLNY SQ YCTNHKPQLSFPLCSAGNIFGLYKNSATGSLDVEVFNRLATSDWTDVRDYKLANDVKDTLRLFAAETIKAKEESVKSSYA SQ FATLKEVVGPKELLLSWESGKVKPPLNRNSVFTCFQISKDSKFQIGEFIFEKVEYGSDTVTYKSTVTTKLVPGMIFVLTS SQ HNVQPLRAPTIANQEKYSSIYKLHPAFNVSDAYANLVPYYQLIGKQKITTIQGPPGSGKSHCSIGLGLYYPGARIVFVAC SQ AHAAVDSLCAKAMTVYSIDKCTRIIPARARVECYSGFKPNNTSAQYIFSTVNALPECNADIVVVDEVSMCTNYDLSVINQ SQ RLSYKHIVYVGDPQQLPAPRVMITKGVMEPVDYNVVTQRMCAIGPDVFLHKCYRCPAEIVNTVSELVYENKFVPVKPASK SQ QCFKVFFKGNVQVDNGSSINRKQLEIVKLFLVKNPSWSKAVFISPYNSQNYVASRFLGLQIQTVDSSQGSEYDYVIYAQT SQ SDTAHACNVNRFNVAITRAKKGIFCVMCDKTLFDSLKFFEIKHADLHSSQVCGLFKNCTRTPLNLPPTHAHTFLSLSDQF SQ KTTGDLAVQIGSNNVCTYEHVISFMGFRFDISIPGSHSLFCTRDFAIRNVRGWLGMDVESAHVCGDNIGTNVPLQVGFSN SQ GVNFVVQTEGCVSTNFGDVIKPVCAKSPPGEQFRHLIPLLRKGQPWLIVRRRIVQMISDYLSNLSDILVFVLWAGSLELT SQ TMRYFVKIGPIKYCYCGNSATCYNSVSNEYCCFKHALGCDYVYNPYAFDIQQWGYVGSLSQNHHTFCNIHRNEHDASGDA SQ VMTRCLAVHDCFVKNVDWTVTYPFIANEKFINGCGRNVQGHVVRAALKLYKPSVIHDIGNPKGVRCAVTDAKWYCYDKQP SQ VNSNVKLLDYDYATHGQLDGLCLFWNCNVDMYPEFSIVCRFDTRTRSVFNLEGVNGGSLYVNKHAFHTPAYDKRAFVKLK SQ PMPFFYFDDSDCDVVQEQVNYVPLRASSCVTRCNIGGAVCSKHANLYQKYVEAYNTFTQAGFNIWVPHSFDVYNLWQIFI SQ ETNLQSLENIAFNVVKKGCFTGVDGELPVAVVNDKVFVRYGDVDNLVFTNKTTLPTNVAFELFAKRKMGLTPPLSILKNL SQ GVVATYKFVLWDYEAERPFTSYTKSVCKYTDFNEDVCVCFDNSIQGSYERFTLTTNAVLFSTVVIKNLTPIKLNFGMLNG SQ MPVSSIKGDKGVEKLVNWYIYVRKNGQFQDHYDGFYTQGRNLSDFTPRSDMEYDFLNMDMGVFINKYGLEDFNFEHVVYG SQ DVSKTTLGGLHLLISQFRLSKMGVLKADDFVTASDTTLRCCTVTYLNELSSKVVCTYMDLLLDDFVTILKSLDLGVISKV SQ HEVIIDNKPYRWMLWCKDNHLSTFYPQLQSAEWKCGYAMPQIYKLQRMCLEPCNLYNYGAGIKLPSGIMLNVVKYTQLCQ SQ YLNSTTMCVPHNMRVLHYGAGSDKGVAPGTTVLKRWLPPDAIIIDNDINDYVSDADFSITGDCATVYLEDKFDLLISDMY SQ DGRIKFCDGENVSKDGFFTYLNGVIREKLAIGGSVAIKITEYSWNKYLYELIQRFAFWTLFCTSVNTSSSEAFLIGINYL SQ GDFIQGPFIAGNTVHANYIFWRNSTIMSLSYNSVLDLSKFECKHKATVVVTLKDSDVNDMVLSLIKSGRLLLRNNGRFGG SQ FSNHLVSTK // ID P0C6X6; PN 2'-O-methyltransferase; GN rep; OS 31631; SL Nucleus Position: SL-0382; SL Comments: [Papain-like proteinase]: 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: P0C6X6; DR UNIPROT: Q4VID8; DR UNIPROT: Q4VIE7; DR UNIPROT: Q696Q1; DR UNIPROT: Q6TNG2; DR UNIPROT: Q9WAC3; 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; 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 MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDMICSTTAQKLETDGICPENHVMVDCRRLLKQECCVQSSLIREI SQ VMNASPYHLEVLLQDALQSREAVLVTTPLGMSLEACYVRGCNPKGWTMGLFRRRSVCNTGRCTVNKHVAYQLYMIDPAGV SQ CLGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKRGEKGAYNKDHGCGGFGHVYDFKVEDAYDQVHDEPKGKFSKKAYAL SQ IRGYRGVKPLLYVDQYGCDYTGSLADGLEAYADKTLQEMKALFPTWSQELPFDVIVAWHVVRDPRYVMRLQSAATICSVA SQ YVANPTEDLCDGSVVIKEPVHVYADDSIILRQYNLFDIMSHFYMEADTVVNAFYGVALKDCGFVMQFGYIDCEQDSCDFK SQ GWIPGNMIDGFACTTCGHVYEVGDLIAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI SQ PILKSSVKSYDSLVYTGVLGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLINRGVYKPLLENIDYF SQ NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKLCHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD SQ LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFQSVAKVVLDSLRV SQ TFIDGLSCFKIGRRRICLSGRKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL SQ TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDDHVGLLDQAWRVPCAGRRVTFKEQPTVKEIISMPKIIKVFYELD SQ NDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNPLFLFDEAGEEVFAPKLYCA SQ FTAPEDDDFLEESDVEEDDVEGEETDLTITSAGQPCVASEQEESSEVLEDTLDDGPSVETSDSQVEEDVEMSDFVDLESV SQ IQDYENVCFEFYTTEPEFVKVLGLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA SQ NIVLPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHICKCGESMVLIDVDVPFTAHFALKD SQ KLFCAFITKRIVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV SQ KGDIIKVSKLVKAEVVVNPANGHMVHGGGVAKAIAVAAGQQFVKETTNMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD SQ ARTQGKQSYVLLERVYKHFNNYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK SQ LAARLSFNVGRSIVYETDANKLILINDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVLPEGWRVVNKFYQINGV SQ RTVKYFECTGGIDICSQDKVFGYVQQGIFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN SQ VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCFKWQVVVNGKYFTFKQANNNCFVNVSCLML SQ QSLHLTFKIVQWQEAWLEFRSGRPARFVALVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG SQ LDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFIGDNVGHYVHVKCEQSYQL SQ YDASNVKKVTDVTGKLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY SQ TNFKLIGHTVCDSLNSKLGFDSSKEFVEYKITEWPTATGDVVLANDDLYVKRYERGCITFGKPVIWLSHEKASLNSLTYF SQ NRPLLVDDNKFDVLKVDDVDDSGDSSESGAKETKEINIIKLSGVKKPFKVEDSVIVNDDTSETKYVKSLSIVDVYDMWLT SQ GCKYVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPAVNVVKAVRNKTSACFNFIKWLFVLLFGWIKISA SQ DNKVIYTTEIASKLTCKLVALAFKNAFLTFKWSMVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW SQ IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY SQ TAWFYPLFALISIQILTTWLPELFMLSTLHWSFRLLVALANMLPAHVFMRFYIIIASFIKLFSLFKHVAYGCSKSGCLFC SQ YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT SQ DVKQVGCSMRLFYDRDGQRIYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK SQ NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQIYKVLDTFLSCARKSCSIDSDVDTKCLAD SQ SVMSAVSAGLELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQFSSDFQHKLKKAC SQ CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV SQ IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVIDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ SQ CYTPHSQISYSNFYASGCVLSSACTMFTMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR SQ VVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA SQ VIVVLVFYYLIKLKRAFGDYTSVVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT SQ IMPLWFCLLYIAVVVSNHAFWVFSYCRKLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS SQ GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCVVSVTYGNMTLNGLWLDD SQ KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMRGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV SQ LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP SQ IQDYIQSVNFLAWLYAAILNNCNWFIQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ SQ GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLFKGTVCWIMASTFLFSCIITAFVKWTMFMYVTTNMFSITFCALCV SQ ISLAMLLVKHKHLYLTMYITPVLFTLLYNNYLVVYKHTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLVGMVFVTLRSI SQ NHDLFSFIMFVGRLISVFSLWYKGSNLEEEILLMLASLFGTYTWTTVLSMAVAKVIAKWVAVNVLYFTDIPQIKIVLLCY SQ LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT SQ DVKCANVVLLNCLQHLHVASNSKLWHYCSTLHNEILATSDLSVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD SQ NTVLQALQSEFVNMASFVEYEVAKKNLDEARFSGSANQQQLKQLEKACNIAKSAYERDRAVAKKLERMADLALTNMYKEA SQ RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLNIIVPDKSVYDQIVDNIYVTYAGNVW SQ QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRYNEVSATVLQNNELMPAKLKIQVVNSGPDQTCNTPTQCYYNNSNNGKI SQ VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDAKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA SQ SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG SQ LCKLRGKFVQVPVGIKDPVSYVLTHDVCRVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGASVDARLVPCASGLSTDVQ SQ LRAFDIYNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMKCYERVKDCKFVAEHDFFTFDVEGSRV SQ PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE SQ FADKLVEVGLVGVLTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYIMPMLTMCHALDCELYVNNAYRLFDLVQYDF SQ TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM SQ NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFVLSKGLLKEGSSV SQ DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY SQ YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY SQ GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHETCCSQSDRFYRLANECAQVLSEIVMCGGCYYV SQ KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDKVDSTFVTEYYEFLNKHFSM SQ MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVEHDINNGPHEFCSQHTMLVKMDGDDVYLPYPNPS SQ RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLAYIKKLYNDLGNQILDSYSVILSTCDGQKF SQ TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL SQ YLGGMSYYCEDHKPQYSFKLVMNGLVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE SQ AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD SQ VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVFYCTARV SQ VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL SQ SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK SQ NESSLLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYV SQ IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTLDKVPQAVETKVQCSTNLFKDCSKSYSGYHPAH SQ APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLISLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATLDSI SQ GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGHRWDVVRPRIVQMFADHLIDLSDCV SQ VLVTWAANFELTCLRYFAKVGREISCNVCTKRATVYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC SQ SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVILKAAMLCNRYTLCYDIGNPKGIACV SQ KDFDFKFYDAQPIVKSVKTLLYSFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF SQ HTKPFARAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLESYNTATTAGF SQ TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVTKIDKEDVVIFINNTTYPTNVAVELFA SQ KRSVRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGAFEAFKRSNNGVYIST SQ TKVKSLSMIRGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLGVSSNQSPQGNLGSNGKPGNVGGNDALSI SQ STIFTQSRVISSFTCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVVQEFVS SQ YDSSIHSYFITDEKSGGSKSVCTVIDILLDDFVTLVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASD SQ WKPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAV SQ LRQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALG SQ GSVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLCKPKVEIDGNVMHANYLFWRNSTVWNGGAYSL SQ FDMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLIRDTNKEVFVGDSLVNVI // ID P0C6Y0; PN 2'-O-methyl transferase; GN rep; OS 11144; SL Nucleus Position: SL-0382; SL Comments: [Papain-like proteinase]: 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: P0C6Y0; DR UNIPROT: P19751; DR UNIPROT: P29982; DR UNIPROT: Q66194; DR UNIPROT: Q90045; 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; 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 MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVDCSRLPALECCVQSAIIRDI SQ FVDEDPQKVEASTMMALQFGSAVLVKPSKRLSVQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV SQ CLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPRGKYSCKAYA SQ LLRGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELSPVWRDSLDNEVVVAWHVDRDPRAVMRLQTLATVRSI SQ EYVGQPIEDMVDGDVVMREPAHLLAPNAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDTCGFRGW SQ VPGNMMDGFPCPGCCKSYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGGAAYWSPYPGMWLPVIWSS SQ VKSYSYLTYTGVVGCKAIVQETDAICRFLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE SQ FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSLMVNFSREVVDMCMDMALLFMHDVKVATKYVKKVTGKVAVRFKA SQ LGIAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGVITFIQEVPELVKNFVDKFKTFFKVLIDSMSVSILSGLT SQ VVKTASNRVCLAGSKVYEVVQKSLPAYIMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPSSFEKICIVDK SQ LYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVVFNDKPKVKEVPSTRKIKIIFALDATFDSVLSKACSEFEVDKDV SQ TLDELLDVVLDAVESTLSPCKEHGVIGTKVCALLERLVDDYVYLFDEGGEEVIASRMYCSFSAPDEDCVATDVVYADENQ SQ DDDADDPVVLVADTQEEDGVAREQVDSADSEICVAHTGGQEMTEPDVVGSQTPIASAEETEVGEACDREGIAEVKATVCA SQ DALDACPDQVEAFDIEKVEDSILSELQTELNAPADKTYEDVLAFDAIYSETLSAFYAVPSDETHFKVCGFYSPAIERTNC SQ WLRSTLIVMQSLPLEFKDLGMQKLWLSYKAGYDQCFVDKLVKSAPKSIILPQGGYVADFAYFFLSQCSFKVHANWRCLKC SQ GMELKLQGLDAVFFYGDVVSHMCKCGNSMTLLSADIPYTFDFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVDGKQ SQ IDGKVVTKFNGDKFDFMVGHGMTFSMSPFEIAQLYGSCITPNVCFVKGDVIKVLRRVGAEVIVNPANGRMAHGAGVAGAI SQ AKAAGKAFINETADMVKAQGVCQVGGCYESTGGKLCKKVLNIVGPDARGHGNECYSLLERAYQHINKCDNVVTTLISAGI SQ FSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSFQLAKNLCRDVKFVTNACSSLFSESSFVSSYD SQ VLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGEVFVSSQGKKFGYVQNGSFKEASVS SQ QIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIHKGKVFFQYSGLSAADLAAVKDAFGF SQ DEPQLLQYYSMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWRRPGNEFRSGKPLRFVSLVLAKGS SQ FKFNEPSDSTDFIRVELREADLSGATCDLEFICKCGVKQEQRKGVDAVMHFGTLDKSGLVKGYNIACTCGDKLVHCTQFN SQ VPFLICSNTPEGKKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVSKVSEAKGNFTDCLYLKNLKQTFSSVLTTY SQ YLDDVKCVAYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGHDIAEKLNAKLGFDCNSPFMEYKITEWPT SQ ATGDVVLASDDLYVSRYSGGCVTFGKPVIWRGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDRRPVPSAVLVTGA SQ ASGADASAISTEPGTAKEQKACASDSVEDQIVMEAQKKSSVTTVAVKEVKLNGVKKPVKWNCSVVVNDPTSETKVVKSLS SQ IVDVYDMFLTGCRYVVWTANELSRLINSPTVREYVKWGMSKLIIPANLLLLRDEKQEFVAPKVVKAKAIACYGAVKWFLL SQ YCFSWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPL SQ PMFVGQIVAWVKTTFGVLTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYESINVVQHVVDRRVSFDYISLFKLV SQ VELVIGYSLYTVCFYPLFVLVGMQLLTTWLPEFFMLGTMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMY SQ GCSKPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVN SQ PTDSAYYSVIEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLNAAVFYAQS SQ LYRPMLMVEKKLITTANTGLSVSRTMFDLYVYSLLRHLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFVGCARRKCAID SQ SDVETKSITKSVMAAVNAGVEVTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQSNVAKAANVACIWSVDAFNQLSA SQ DLQHRLRKACVKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRVLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLY SQ ASFKVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLVYYRNSKACPVVVAVIDQDIGHTLFNVPTKVLRYGFHVLHFI SQ THAFATDRVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGVMHNASLYSSLVPHVRYNLASSNGYIRF SQ PEVVSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNSSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVQPIDFFALT SQ ASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVM SQ HLQWLVMYGAIMPLWFCITYVAVVVSNHALWLFSYCRKIGTDVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYL SQ SLYNKYRYFSGKMDTATYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCVVSVTYGN SQ MTLNGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSDRMSLTVMSYQMQGSLLVLTVTLQNPNTPKYSFG SQ VVKPGETFTVLAAYNGRPQGAFHVVMRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGP SQ YRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLA SQ AIKRLHSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHM SQ LGVTLCALCFVIFAMLLIKHKHLYLTMYIMPVLCTLFYTNYLVVGYKQSFRGLAYAWLSYFVPAVDYTYMDEVLYGVVLL SQ VAMVFVTMRSINHDVFSTMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTD SQ IPQIKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPV SQ IEVSQIQSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSVAFDKLAQLLVVLFANPAAVDSKCLAS SQ IEEVSDDYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMA SQ DLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPPLTSNTLTIIVPDKQVFDQVVD SQ NVYVTYAPNVWHIQSIQDADGAVKQLNEIDVNSTWPLVISANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNIPTQ SQ CYYNTTGTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTV SQ RLQAGTATEYASNSAILSLCAFSVDPKKTYLDYIQQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYC SQ RSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNRVRGTSVNARLV SQ PCASGLDTDVQLRAFDICNANRAGIGLYYKVNCFRFQRVDEEGNKLDKFFVVKRTNLEVYNKEKECYELTKDCGVVAEHE SQ FFTFDVEGSRVPHIVRKDLSKFTMLDLCYALRHFDRNDCSTLKEILLTYAECDESYFQKKDWYDFVENPDIINVYKKLGP SQ IFNRALLNTANFADTLVEAGLVGVLTLDNQDLYGQWYDFGDFVKTVPCCGVAVADSYYSYMMPMLTMCHALDSELFVNGT SQ YREFDLVQYDFTDFKLELFNKYFKHWSMTYHPNTSECEDDRCIIHCANFNILFSMVLPKTCFGPLVRQIFVDGVPFVVSI SQ GYHYKELGVVMNMDVDTHRYRLSLKDLLLYAADPALHVASASALLDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYEFIL SQ SKGLLKEGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVVEVVNKYFEIYEGGCIPATQVIVNNYDKSAGY SQ PFNKFGKARLYYEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRG SQ VPVVIGTTKFYGGWDDMLRRLIKDVDSPVLMGWDYPKCDRAMPNILRIVSSLVLARKHDSCCSHTDRFYRLANECAQVLG SQ EIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCSLMACNGHKIEDLSIRELQKRLYSNVYRADHVDPAFVSE SQ YYEFLNKHFSMIILSDDGVVCYNSEFASKGYIANISDFQQVLYYQNNVFMSEAKCWVETDIEKGPHEFCSQHTMLVKMDG SQ DEVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENPEYQNVFRVYLEYIKKLYNDLGNQILDSIS SQ VILSTCDGQKFTDETFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCAYDHVMSTDHKYVLSVSPYVCNS SQ PGCDVNDVTKLYLGGMSYYCEAHKPQYSFKLVMNGMVFGLYKQSCTGSPYIEDFNKIASCKWTEVDDYVLANECTERLKL SQ FAAETQKATEEAFKQCYASATIREIVSDRELILSWEIGKVRPPLNKNYVFTGYHFTNNGKTVLGEYVFDKSELTNGVYYR SQ ATTTYKLSVGDVFILTSHAVSSLSAPTLVPQENYTSVRFASAYSVPETFQNNVPNYQHIGIKRYCTVQGPPGTGKSHLAI SQ GHAVYYCTARVVYTAASHAAVDALCEKAHKFLNINDCARIVPAKLRVDCYDKFNVNDTTRKYVFTTINALPELVTDIIVV SQ DEVSMLTNYELSVINSRVRAKHYVYIGDPAQLPAPRVLLNKGTLEPRYFNSVTKLMCCLGPDIFLGTCYRCPKEIVDTVS SQ ALVYNNKLKAKNDNSAMCFKVYYKGQTTHESSSAVNMQQIHLISKLLKANPSWSNAVFISPYNSQNYVAKRVLGLQTQTA SQ DSAQGSAYDFVIYSQTAQTAHSVNVNRFNVAITRAKKGILCVMSSMQLIGVFNFTTLTLDKINNPRLQCTTNLFKDCSKS SQ YVGIPPCAFLLAVDDKYKVSGNLAVCLNVADSAVTYSRLISLMGFKLDLTLDGYCKLFITRDEAIKRVRAWVGFDAEGAH SQ ATRDSIGTNFPLQLGFSTGIDFVVEATGMFAERDGYVFKKAAARAPPGEQFKHLVPLMSRGQKWDVVRIRIVQMLSDHLV SQ DLADSVVLVTWAASFELTCLRYFAKVGKEVVCSVCNKRATCFNSRTGYYGCWRHSYSCDYLYNPLIVDIQQWGYTGSLTS SQ NHDPICSVHKGAHVASSDAIMTRCLAVHDCFCKSVNWNLEYPIISNEVSVNTSCRLLQRVMFRAAMLCNRYDVCYDIGNP SQ KGLACVKGYDFKFYDASPVVKSVKQFVYKYEAHKDQFLDGLCMFWNCNVDKYPANAVVCRFDTRVLSKLNLPGCNGGSLY SQ VNKHAFHTNPFTRAAFENLKPMPFFYYSDTPCVYMEGMESKQVDYVPLRSATCITRCNLGGAVCLKHAEEYREYLESYNT SQ ATTAGFTFWVYKTFDFYNLWNTFTRLQSLENVVYNLVNAGHFDGRAGELPCAVIGEKVIAKIQNEDVVVFKNNTPFPTNV SQ AVELFAERSIRPHPELKLFRSSNIHVCWNHVLWDYAKDSVFCSSTYKVCKYTDLQCIESLNVLFDGRDNGALEAFKKCRN SQ GVYINTTKIKSLSMIKGPQRADLNGVVVEKVGDSDVEFWFAMRRDGDDVIFSRTGSLEPSHYRSPQGNPGGNRVGDLSGN SQ EALARGTIFTQSRFLSSFSPRSEMEKDFMDLDEDVFIAKYSLQDYAFEHVVYGSFNQKIIGGLHLLIGLARRPKKSNLVI SQ QEFVPYDSSIHSYFITDENSGSSESVCTVIDLLLDDFVDIVKSLNLKCVSKVVNVNVDFKDFQFMLWCNEEKVMTFYPRL SQ QAAADWKPGYVMPVLYKYLESPMERVNLWNYGKPITLPTGCMMNVAKYTQLCQYLSTTTLAVPANMRVLHLGAGSDKGVA SQ PGSAVLRQWLPSGSILVDNDMNPFVSDSVASYYGNCITLPFDCQWDLIISDMYDPLTKNIGEYNVSKDGFFTYLCHLIRD SQ KLALGGSVAIKITEFSWNAELYSLMGKFAFWTIFCTNVNASSSEGFLIGINWLNRTRNEIDGKTMHANYLFWRNSTMWNG SQ GAYSLFDMTKFPLKAAGTAVVSLKPDQINDLVLSLIEKGKLLVRDTRKEVFVGDSLVNVK // 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 P0C7N6; PN Nuclear protein localization protein 4; GN NPL4; OS 321614; 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: P0C7N6; DR UNIPROT: Q0UV64; 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 MILRFVSKEGQFRLTVQPDSTFPELLAQIAEKLPKSVDLQSVTVSNRPQGGDARKISELKGVSFKQVGLSHGAQLFLGFE SQ DQSTASNGHATAPTGANRLNGKVVEASDMPSVPLGSPTQVIKNPWEVVRQSPLDDKLDRQDGKIHRKRDARMCTHGPKGM SQ CDYCMPLEPYAAAYLAEKKIKHLSFHSYLRKVNSAKNRPELGSSYIPPLTEPYYRVRPDCPSGHKPFPAGICTKCQPGAI SQ SLKPQEYRMVDHVEFASIQVVDDLINFWRNTGCQRLGFLYGRYEEYTEVPLGTKAVVETIYEPPQVNELDGISLGDWDNE SQ KEIDEIAAQCGLQRVGVIFTDLLDADKGDGSVICKRHIDSYYLSSLEIAFAARYQAKYPRPTKWSETGKFGSNFVTCVIS SQ GDDQGQIGISSYQASNDAVEMVRADIIEPSAEPSVMLVQSEDDNEALNRARYIPEVFYRRINEHGANVQENAKPDFPVEY SQ LFVTLTHGFPTQPNPLFTGGKFPIENREIMGEMPDVSALGKSLNAKANGLALNTTSGLNAISNFHMLCFIHNLGILSKDE SQ ESLLFKVASTHDTSEGSALQHTGGWATLLTILKESGERPPKRSYASPSFSATGRGAAHPGEKNRLMRQPSHGSDSDSVQL SQ AKRLKGASLKGKE // ID P0C8N6; PN Nuclear envelope integral membrane protein 2; GN Nemp2; OS 10116; 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: P0C8N6; 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 MPPGSWWLVLWLPPLATLPAGAVPQEEAAMSVPRCKSLKETDLIKTSVSDCYCYNQHSQIEWTYMWSTVQVTVTSPGLLS SQ IVYITGRHTCQHTETILSFLKCVTHNFWTAEEAKEVTIVFSPYGETVCFSVKPVGSLLTYAVSVNRNVVDFRLFLVFATG SQ IFLFFYAKTLSQSPVFYYSSGTVLGILMTLVFVLLMTKKHIPKYSTFGALMIGCWFASVYVLCQLMENLKWLWCGNRIYV SQ LGYVLVVGLCSFSACYSRGPPADEGSRDLLMWALRFLSLVLVYTGMAISQFAYAVMILLLLSWTRHYLLRAFSCLRWKVR SQ QWFATRALVVRYLTDDEYREQAEAETASALEELRQACCRPDFPSWLAVSRLQAPKKFAEFVLGASHLSPEEVSTHEKQYG SQ LGGAFLEEQLFSLQTESLPAS // 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 P0CA05; PN p8; GN Ken; OS 561445; SL Nucleus Position: SL-0382; SL Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q65179}. [p35]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p15]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. DR UNIPROT: P0CA05; DE Function: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. DE Reference Proteome: No; GO GO:0044220; GO GO:0019012; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP SQ FYIPTPMEFTGEIGSYTGVKLEVEKKEANKVILKNGEAVLIPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN SQ DPPVSKHISPYTPRTRIAIEVEKAFDECMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP SQ YKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADTATKEVDVPICYSDPETVHSYANHVRTEI SQ LHHNMVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV SQ RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNDTQTGSQTSSLTDLVP SQ TRLHSFLNHNLSKLKILNRAQQTVKNILSNDCLNQLKHYVKHTGKNEILKLLQE // 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 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 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 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 P0CS50; PN Protein transport protein SEC13; GN SEC13; OS 214684; 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: P0CS50; DR UNIPROT: Q55MW6; DR UNIPROT: Q5KB95; 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 MCLWPLIQSAQASKPVPVETQHEDMIHDAQLDYYGKRLATCSSDRTIRIFNVIKGEAKGEPVILKGHTAAVWQVSWAHPS SQ FGSILASCSYDGRVFIWKEVGQGQGKGSGGELQDGWERIKEHTLHTASVNSIAWAPYDLGPILACASSDGKVSVLSFQND SQ GSIEVNIFPAHGTGANAISWAPSVLSTVSGVSRSQQPSNSLAPQKRFVTAGSDNLIRIWGFDEEQKKWTEEETIKGHEDW SQ VRDVAWAPNIGLPGMYIASASQDRTVLIHSRPSPSSSWTSAPLLPSLPQSQDPHFPDAVWRVSWSLAGNVLAVSCGDGKV SQ SLWKEGVGKGWECVSDFSS // ID P0CU06; PN UPF0742 protein SPAC750.04c; GN SPAC750; OS 284812; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Cytoplasm {ECO:0000255|UniProtKB:P0CU07}. Nucleus membrane {ECO:0000255|UniProtKB:P0CU07}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic dots and the nuclear envelope. {ECO:0000255|UniProtKB:P0CU07}. DR UNIPROT: P0CU06; DR UNIPROT: Q9P332; DR Pfam: PF09437; DE Function: DE Reference Proteome: Yes; GO GO:0005737; GO GO:0016021; GO GO:0031965; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVY SQ HNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR // 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 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 P0DTD1; PN 2'-O-methyltransferase; GN rep; 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}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0C6X7}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250|UniProtKB:P0C6X9}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. DR UNIPROT: P0DTD1; DR PDB: 5R7Y; DR PDB: 5R7Z; DR PDB: 5R80; DR PDB: 5R81; DR PDB: 5R82; DR PDB: 5R83; DR PDB: 5R84; DR PDB: 5RE4; DR PDB: 5RE5; DR PDB: 5RE6; DR PDB: 5RE7; DR PDB: 5RE8; DR PDB: 5RE9; DR PDB: 5REA; DR PDB: 5REB; DR PDB: 5REC; DR PDB: 5RED; DR PDB: 5REE; DR PDB: 5REF; DR PDB: 5REG; DR PDB: 5REH; DR PDB: 5REI; DR PDB: 5REJ; DR PDB: 5REK; DR PDB: 5REL; DR PDB: 5REM; DR PDB: 5REN; DR PDB: 5REO; DR PDB: 5REP; DR PDB: 5RER; DR PDB: 5RES; DR PDB: 5RET; DR PDB: 5REU; DR PDB: 5REV; DR PDB: 5REW; DR PDB: 5REX; DR PDB: 5REY; DR PDB: 5REZ; DR PDB: 5RF0; DR PDB: 5RF1; DR PDB: 5RF2; DR PDB: 5RF3; DR PDB: 5RF4; DR PDB: 5RF5; DR PDB: 5RF6; DR PDB: 5RF7; DR PDB: 5RF8; DR PDB: 5RF9; DR PDB: 5RFA; DR PDB: 5RFB; DR PDB: 5RFC; DR PDB: 5RFD; DR PDB: 5RFE; DR PDB: 5RFF; DR PDB: 5RFG; DR PDB: 5RFH; DR PDB: 5RFI; DR PDB: 5RFJ; DR PDB: 5RFK; DR PDB: 5RFL; DR PDB: 5RFM; DR PDB: 5RFN; DR PDB: 5RFO; DR PDB: 5RFP; DR PDB: 5RFQ; DR PDB: 5RFR; DR PDB: 5RFS; DR PDB: 5RFT; DR PDB: 5RFU; DR PDB: 5RFV; DR PDB: 5RFW; DR PDB: 5RFX; DR PDB: 5RFY; DR PDB: 5RFZ; DR PDB: 5RG0; DR PDB: 6LU7; DR PDB: 6M03; DR PDB: 6VWW; DR PDB: 6W01; DR PDB: 6W02; DR PDB: 6W61; DR PDB: 6W63; DR PDB: 6W6Y; DR PDB: 6W75; DR PDB: 6Y2E; DR PDB: 6Y2F; DR PDB: 6Y2G; DR PDB: 6Y84; DR PDB: 6YB7; DR Pfam: PF13604; DR Pfam: PF16348; DR Pfam: PF06478; DR Pfam: PF12379; DR Pfam: PF01661; DR Pfam: PF16251; DR Pfam: PF11501; DR Pfam: PF09401; DR Pfam: PF06471; DR Pfam: PF06460; DR Pfam: PF12124; DR Pfam: PF08716; DR Pfam: PF08717; DR Pfam: PF08710; DR Pfam: PF05409; DR Pfam: PF11633; DR Pfam: PF08715; DR PROSITE: PS00867; DR PROSITE: PS51653; DR PROSITE: PS00213; DR PROSITE: PS51442; DR PROSITE: PS51154; DR PROSITE: PS51124; DR PROSITE: PS51657; DR PROSITE: PS50507; DE Function: [Replicase polyprotein 1ab]: 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}. [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}. [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] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198291}. [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}. [Proofreading exoribonuclease]: 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. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens. {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; DE Interaction: O75569; IntAct: EBI-25475891,EBI-713955; Score: 0.35 DE Interaction: O95831; IntAct: EBI-25475880,EBI-356440; Score: 0.35 DE Interaction: P04406; IntAct: EBI-25475880,EBI-354056; Score: 0.35 DE Interaction: P31689; IntAct: EBI-25475871,EBI-347834; Score: 0.35 DE Interaction: P35658; IntAct: EBI-25475877,EBI-1222270; Score: 0.35 DE Interaction: P37198; IntAct: EBI-25475877,EBI-347978; Score: 0.35 DE Interaction: P49454; IntAct: EBI-25475888,EBI-968343; Score: 0.35 DE Interaction: P57088; IntAct: EBI-25475871,EBI-1048629; Score: 0.35 DE Interaction: P61026; IntAct: EBI-25475871,EBI-726075; Score: 0.35 DE Interaction: P61970; IntAct: EBI-25475891,EBI-591778; Score: 0.35 DE Interaction: P63244; IntAct: EBI-25475874,EBI-296739; Score: 0.35 DE Interaction: Q06787; IntAct: EBI-25492388,EBI-366305; Score: 0.35 DE Interaction: Q15056; IntAct: EBI-25475877,EBI-748492; Score: 0.35 DE Interaction: Q5JTV8; IntAct: EBI-25475871,EBI-2559665; Score: 0.35 DE Interaction: Q6ZRP7; IntAct: EBI-25475871,EBI-11127401; Score: 0.35 DE Interaction: Q7Z3B4; IntAct: EBI-25475877,EBI-741048; Score: 0.35 DE Interaction: Q86UE4; IntAct: EBI-25475891,EBI-1046588; Score: 0.35 DE Interaction: Q8NC51; IntAct: EBI-25475864,EBI-523558; Score: 0.35 DE Interaction: Q8TEM1; IntAct: EBI-25475862,EBI-372826; Score: 0.35 DE Interaction: Q99567; IntAct: EBI-25475877,EBI-726178; Score: 0.35 DE Interaction: Q99720; IntAct: EBI-25475868,EBI-3248663; Score: 0.35 DE Interaction: Q9BV73; IntAct: EBI-25475888,EBI-1053100; Score: 0.35 DE Interaction: Q9BVL2; IntAct: EBI-25475877,EBI-2811583; Score: 0.35 DE Interaction: Q9H7Z7; IntAct: EBI-25475871,EBI-681645; Score: 0.35 DE Interaction: Q9UM54; IntAct: EBI-25475864,EBI-350606; Score: 0.35 GO GO:0044172; GO GO:0033644; GO GO:0044220; GO GO:0016021; GO GO:0005524; GO GO:0003678; GO GO:0004519; GO GO:0004527; GO GO:0046872; GO GO:0008168; GO GO:0003723; GO GO:0003724; GO GO:0003968; GO GO:0036459; GO GO:0039595; GO GO:0039520; GO GO:0032259; GO GO:0039648; GO GO:0039579; GO GO:0039644; 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 NRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYN SQ LLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVEN SQ PDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLT SQ RALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGP SQ LVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQ SQ TVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCI SQ NANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTN SQ RQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSL SQ SHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLY SQ ECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKG SQ PHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYI SQ RKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVIS SQ TSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTN SQ AGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIG SQ EYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQK SQ YSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYV SQ FCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDM SQ FLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYN SQ SQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRN SQ VATLQAENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFIT SQ REEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYK SQ GLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDY SQ VYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHM SQ VVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPAN SQ SIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCIT SQ RCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQSLENVAFNVVNKGHFDGQQGEVPVSIIN SQ NTVYTKVDGVDVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVDIAANTVIWDYKRDAPAHISTIGVCSMTDIA SQ KKPTETICAPLTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPKQASLNGVTLIGEAVKTQFNYYKKVDGVVQQ SQ LPETYFTQSRNLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYGDFSHSQLGGLHLLIGLAKRFKESPFELEDF SQ IPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVVKVTIDYTEISFMLWCKDGHVETFYPKLQSS SQ QAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGT SQ AVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQKLA SQ LGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLSSY SQ SLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN // 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 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 P10215; PN Nuclear egress protein 1; GN NEC1; OS 10299; 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, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP- Rule:MF_04023}. DR UNIPROT: P10215; DR PDB: 4ZXS; 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, ECO:0000269|PubMed:15140953, ECO:0000269|PubMed:15140956, ECO:0000269|PubMed:24453362}. DE Reference Proteome: Yes; GO GO:0044201; GO GO:0016020; GO GO:0046872; GO GO:0046802; GO GO:0046765; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MYDTDPHRRGSRPGPYHGKERRRSRSSAAGGTLGVVRRASRKSLPPHARKQELCLHERQRYRGLFAALAQTPSEEIAIVR SQ SLSVPLVKTTPVSLPFCLDQTVADNCLTLSGMGYYLGIGGCCPACNAGDGRFAATSREALILAFVQQINTIFEHRAFLAS SQ LVVLADRHNAPLQDLLAGILGQPELFFVHTILRGGGACDPRLLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPG SQ YRFVAHVWQSTFVLVVRRNAEKPTDAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP // ID P10406; PN E1B protein, small T-antigen; GN E1BS; OS 28280; 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: P10406; 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 MEIWTVLEDFHKTRQLLENASNGVSHLWRFCFGGDLAKLVYRAKQDYREQFEDILRECPSLFDALNLGHQSHFNQRISRA SQ LDFTTPGRTTAAVAFFAFIFDKWSQETHFSRDYQLDFLAVALWRTWKCQRLNAIPATCRYSR // 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 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 P10544; PN E1B protein, small T-antigen; GN E1BS; OS 10524; 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: P10544; 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 MEFWSELQSYQSLRRLLELASARTSSCWRFIFGSTLTNVIYRAKEDYSSRFAELLSFNPGIFASLNLGHHSFFQEIVIKN SQ LDFSSPGRTVSGLAFICFILDQWSAQTHLSEGYTLDYMTMALWRTLLRRKRVLGCSPAQPPHGLDPVREEEEEEEEEENL SQ RAGLDPQTEL // 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 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 P10999; PN Lamin-L(III); GN LAML3; OS 8355; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. DR UNIPROT: P10999; DR UNIPROT: P23420; DR UNIPROT: Q6AZG7; 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:0005637; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MATSTPSRAREHASAAQSPGSPTRISRMQEKEDLRHLNDRLAAYIERVRSLEADKSLLKIQLEEREEVSSREVTNLRQLY SQ ETELADARKLLDQTANERARLQVELGKVREEYRQLQARNSKKENDLSLAQNQLRDLESKLNTKEAELATALSGKRGLEEQ SQ LQEQRAQIAGLESSLRDTTKQLHDEMLWRVDLENKMQTIREQLDFQKNIHTQEVKEIKKRHDTRIVEIDSGRRVEFESKL SQ AEALQELRRDHEQQILEYKEHLEKNFSAKLENAQLAAAKNSDYASATREEIMATKLRVDTLSSQLNHYQKQNSALEAKVR SQ DLQDMLDRAHDMHRRQMTEKDREVTEIRQTLQGQLEEYEQLLDVKLALDMEINAYRKMLEGEEQRLKLSPSPSQRSTVSR SQ ASTSQTSRLLRGKKRKLDETGRSVTKRSYKVVQQASSTGPVSVEDIDPEGNYVRLLNNTEEDFSLHGWVVKRMHMSLPEI SQ AFKLPCRFILKSSQRVTIWAAGAGAVHSPPTDLVWKSQKTWGTGDNIKITLLDSTGEECAERTLYRVIGEEGETDEDFVE SQ EEELERQFRSQSHQSVDPSCSIM // 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 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 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 P11317; PN Early E3 9.0 kDa glycoprotein; GN E311; OS 45659; SL Nucleus Position: SL-0415; SL Nucleus Position: SL-0418; SL Comments: Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. DR UNIPROT: P11317; DE Function: DE Reference Proteome: No; GO GO:0044200; GO GO:0016021; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MILFQSNTTTSYAYTNIQPKYAMQLEITILIVIGILILSVILYFIFCRQIPNVHRNSKRRPIYSPMISRPHMALNEI // ID P11936; PN Deoxyribonuclease-1; GN DNASE1; OS 9823; 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: P11936; DR UNIPROT: Q95KK2; 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:3782104). 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 (PubMed:3782104). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:3782104}. DE Reference Proteome: Yes; GO GO:0005576; GO GO:0005635; GO GO:0005634; GO GO:0003779; GO GO:0004536; GO GO:0004530; GO GO:0003677; GO GO:0006915; GO GO:0006308; GO GO:0000737; GO GO:0002283; GO GO:0002673; GO GO:0070948; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQD SQ DPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPS SQ DAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAG SQ PLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA // 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 P12349; PN Period circadian protein; GN per; OS 7244; 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: P12349; 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: No; GO GO:0005634; GO GO:0048471; GO GO:0006355; GO GO:0048511; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMAVKRNKDKSRKKKKAKSP SQ AQATAATTTTIKSLEQTEEPLLVKPNNGSCEQQLELQDAQQLGAPTPSDAHDAHGDKPQLDVDEQQDDPQAEQIQQLETA SQ TAATISPDTMSASVTVTIDGCTSMEKTCEWTDRPGRLEAHAACIGKQHVQQQQHDRVKEDSFCCVISMHDGVVLFTTANL SQ NEMLGYPREMWLGRSFIDFVHIKDRATFASQITTGIPIAESRCSQSKDARTTFCVMLRRYRGLASGGFGIIGRPVSYAPF SQ RLGLTFREAPEEVQPDGCTLSNATSMLLVISATPIKSCYKEPDEFLSPKGPKFAIQHTAAGIISHVDTAAVSALGYLPQD SQ LIGRSILDFYHHEDLSDIKDIYEKVVKKGQTVGATFCSKPFRFLIQNGCYILLETEWTSFVNPWSRKLEFVVGHHRVFQG SQ PKQCDVFEMSPNVTPNIPEDEQNRNACIKEDILKMMTETVTRPSDTVKQEVSRRCQALASFMETLMDEVARGDLKLDLPH SQ ETELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVDTDPPKMDSSYVSSAREDALSP SQ VHGFEGSGGSGSSGNLTTASNVRMSSVTNTSNTGTGTSGGENSASGSSNPLPVNMTLTEILLNKHNDEMEKCMLKKHRES SQ RGRTGDKTKKSVIEKMPEYSGPGHGQTMKRGGSHSWEGDANKPKQQLTLSAVVVAPTVSVSPAEDSQTTAKWQAPMTGSH SQ LFQSSYNFPQSINLWPPFSLGLTTPTVHTTHTSMAQKSFSPQHNLFPAFYYIPAPLATATAGSAAAQTSVSSASAAQHSP SQ KSSENPSTSQPEATAATAMPMPYMAGVMYPHPSLFYAYQPMPFPSVSGAVQMSVQSSGSQSNNNNKSIYTMAPASTTTQK SQ PGAFHSITPAELNKPDAPDTLLHTETSPKISVQEAPKKELSDLPSTSARRGSSSDQRNNSNNPKKYTDSNGNSDDMDGSS SQ FSSFYSSFIKTTDGSESPPDNEKETKVHKLKPIVEHPEEDQTQHGDG // ID P12478; PN C-terminal core protein; GN nef; OS 11683; 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 {ECO:0000250}. 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: P12478; DR PDB: 5EO0; DR PDB: 5EO1; 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, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. 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) (By similarity). {ECO:0000250}. 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. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity). {ECO:0000250}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000250}. DE Reference Proteome: No; 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 MGGRWSKSSIVGWPAIRERIRRTDPAADGVGAVSRDLEKHGAITSSNTRGTNADCAWLEAQEESEEVGFPVRPQVPLRPM SQ TYKGALDLSHFLKEKGG // 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 P12684; PN 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2; GN HMG2; OS 559292; SL Nucleus Position: SL-0178; SL Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope. DR UNIPROT: P12684; DR UNIPROT: D6VZ84; DR UNIPROT: E9P8X3; 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}. DE Reference Proteome: Yes; DE Interaction: P12683; IntAct: EBI-8377,EBI-8384; Score: 0.67 DE Interaction: Self; IntAct: EBI-8384,EBI-8384; Score: 0.55 DE Interaction: P38219; IntAct: EBI-8384,EBI-21409; Score: 0.35 DE Interaction: P16140; IntAct: EBI-8384,EBI-20254; Score: 0.35 DE Interaction: P09733; IntAct: EBI-8384,EBI-18976; Score: 0.35 DE Interaction: P36008; IntAct: EBI-8384,EBI-6329; Score: 0.35 DE Interaction: P02994; IntAct: EBI-8384,EBI-6314; Score: 0.35 DE Interaction: P11484; IntAct: EBI-8384,EBI-8627; Score: 0.35 DE Interaction: P33299; IntAct: EBI-8384,EBI-13910; Score: 0.35 DE Interaction: P40069; IntAct: EBI-8384,EBI-9166; Score: 0.35 DE Interaction: P30822; IntAct: EBI-8384,EBI-20589; Score: 0.35 DE Interaction: P00330; IntAct: EBI-8384,EBI-2218; Score: 0.35 DE Interaction: P40341; IntAct: EBI-8384,EBI-14858; Score: 0.35 DE Interaction: P16521; IntAct: EBI-8384,EBI-6338; Score: 0.35 DE Interaction: P10592; IntAct: EBI-8384,EBI-8603; Score: 0.35 DE Interaction: P26783; IntAct: EBI-8384,EBI-16150; Score: 0.35 DE Interaction: P32905; IntAct: EBI-8384,EBI-16032; Score: 0.35 DE Interaction: P26321; IntAct: EBI-8384,EBI-15398; Score: 0.35 DE Interaction: P41805; IntAct: EBI-8384,EBI-15270; Score: 0.35 DE Interaction: P41940; IntAct: EBI-8384,EBI-11191; Score: 0.35 DE Interaction: P12709; IntAct: EBI-8384,EBI-7238; Score: 0.35 DE Interaction: P06169; IntAct: EBI-8384,EBI-5687; Score: 0.35 DE Interaction: P04147; IntAct: EBI-8384,EBI-12823; Score: 0.35 DE Interaction: P15108; IntAct: EBI-8384,EBI-8666; Score: 0.35 DE Interaction: P39925; IntAct: EBI-8384,EBI-2317; Score: 0.35 DE Interaction: Q02159; IntAct: EBI-19749,EBI-8384; Score: 0.37 GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0034399; GO GO:0005778; GO GO:0000502; GO GO:0050662; GO GO:0004420; GO GO:0042282; GO GO:0015936; GO GO:0006696; GO GO:0008299; GO GO:0016126; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRS SQ PVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNS SQ NFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHS SQ LLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAI SQ YARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEINIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRS SQ NVAIILGKASVIGLLLLINLYVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIE SQ DSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDLVVQQKSATIEFSETRSMPAS SQ SGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNLVELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTR SQ AVLVRRKALSTLAESPILVSEKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRG SQ CKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRT SQ TTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSA SQ LVELNISKNLVGSAMAGSVGGFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTV SQ LEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHNRKTNKANELPQPSNKGPPCK SQ TSALL // 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 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 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 P14733; PN Lamin-B1; GN Lmnb1; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. DR UNIPROT: P14733; DR UNIPROT: Q61791; 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: Yes; DE Interaction: Q7TPH6; IntAct: EBI-1811542,EBI-445247; Score: 0.35 DE Interaction: Q80YT7; IntAct: EBI-16726361,EBI-445247; Score: 0.35 DE Interaction: P83510; IntAct: EBI-7280013,EBI-445247; Score: 0.35 DE Interaction: Q9Z0E3; IntAct: EBI-80858,EBI-445247; Score: 0.35 DE Interaction: Q01815; IntAct: EBI-644904,EBI-445247; Score: 0.35 DE Interaction: A2AKD7; IntAct: EBI-20565907,EBI-445247; Score: 0.35 DE Interaction: Q9D2G2; IntAct: EBI-773210,EBI-445247; Score: 0.35 DE Interaction: Q8K2B3; IntAct: EBI-1219461,EBI-445247; Score: 0.35 DE Interaction: Q60932; IntAct: EBI-299577,EBI-445247; Score: 0.35 DE Interaction: P08228; IntAct: EBI-1635090,EBI-445247; Score: 0.35 DE Interaction: Q01097; IntAct: EBI-400125,EBI-445247; Score: 0.35 DE Interaction: A3KGF7; IntAct: EBI-681172,EBI-445247; Score: 0.37 GO GO:0005737; GO GO:0005638; GO GO:0005635; GO GO:0005637; GO GO:0005652; GO GO:0016363; GO GO:0031965; GO GO:0005654; GO GO:0005634; GO GO:0003690; GO GO:0008432; GO GO:0043274; GO GO:1990837; GO GO:1904609; GO GO:0010971; GO GO:0046330; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLK SQ ALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSL SQ EGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYE SQ YKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE SQ RIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVT SQ VSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTS SQ VSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEE SQ EPIGVAVEEERFHQQGAPRASNKSCAIM // 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 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 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 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 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 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 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 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 P17592; PN Early E3 7.7 kDa protein; GN E311; OS 10519; SL Nucleus Position: SL-0415; SL Nucleus Position: SL-0418; SL Comments: Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. DR UNIPROT: P17592; DE Function: DE Reference Proteome: No; GO GO:0044200; GO GO:0016021; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MILFQSNTTNTINVQTTLNHDMENHTTSYAYINIQPKYAMHLKITILIVIGILILSVILYFLFSYD // 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 P17763; PN RNA-directed RNA polymerase NS5; GN POLG; OS 11059; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion. Host nucleus {ECO:0000269|PubMed:18420804}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}. [Peptide pr]: Secreted {ECO:0000269|PubMed:19759134}. [Small envelope protein M]: Virion membrane {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:26655246}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000305}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane protein {ECO:0000269|PubMed:23408612}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000269|PubMed:26072288}. [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:0000269|PubMed:17276984}; Multi-pass membrane protein {ECO:0000269|PubMed:17276984}. Host mitochondrion {ECO:0000269|PubMed:27252539}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000269|PubMed:17276984, ECO:0000269|PubMed:27252539}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000303|PubMed:28441781}. DR UNIPROT: P17763; DR UNIPROT: P27910; DR UNIPROT: P89313; DR UNIPROT: P89314; DR PDB: 3J8D; DR PDB: 3L6P; DR PDB: 3LKW; DR PDB: 4AL8; DR PDB: 4GSX; DR PDB: 4GT0; DR PDB: 4LCY; DR PDB: 4OIG; DR PDB: 5VIC; DR PDB: 5WJL; DR PDB: 5WKF; 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 (PubMed:11893341). 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 (PubMed:18420804, PubMed:21909430). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008). {ECO:0000269|PubMed:11893341, ECO:0000269|PubMed:18420804, ECO:0000269|PubMed:21909430, ECO:0000269|PubMed:23522008}. [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:0000269|PubMed:18369148, ECO:0000269|PubMed:19759134}. [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 (PubMed:9971841). prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:21388812). {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:25326389, ECO:0000269|PubMed:9971841, ECO:0000303|PubMed:21388812}. [Small envelope protein M]: May play a role in virus budding (PubMed:25326389). Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain (PubMed:13679613). May display a viroporin activity (PubMed:16007501). {ECO:0000269|PubMed:13679613, ECO:0000269|PubMed:16007501, ECO:0000269|PubMed:25326389}. [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 (PubMed:18369148). prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:11893341). {ECO:0000269|PubMed:11893341, ECO:0000269|PubMed:18369148}. [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 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000269|PubMed:27416066}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000269|PubMed:25392211}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (PubMed:26728778). {ECO:0000255|PROSITE- ProRule:PRU00859, ECO:0000269|PubMed:26728778}. [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}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27252539}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000269|PubMed:17276984}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of a cellular antiviral state by blocking the IFN- alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15956546}. [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:0000269|PubMed:17267492, ECO:0000269|PubMed:19279106, ECO:0000269|PubMed:19850911}. DE Reference Proteome: Yes; GO GO:0039714; GO GO:0005576; GO GO:0044167; GO GO:0033650; GO GO:0042025; GO GO:0044220; GO GO:0016021; GO GO:0044385; GO GO:0019028; GO GO:0019031; GO GO:0055036; GO GO:0005524; GO GO:0003725; GO GO:0005216; 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:0039707; GO GO:0051259; GO GO:0039545; GO GO:0039564; GO GO:0039574; GO GO:0039502; GO GO:0046762; GO GO:0039694; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis; SQ MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKV SQ LRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCE SQ DTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETW SQ ALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPT SQ LDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFK SQ CVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTTATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLT SQ MEKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFA SQ GHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVTD SQ KEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIF SQ GTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEV SQ HTWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVSGILAQGKKMIR SQ PQPMEHKYSWKSWGKAKIIGADVQNTTFIIDGPNTPECPDNQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQVCDHRLMS SQ AAIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCIWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTA SQ GPWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKTIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENL SQ VKSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLTMGQLTWNDLIRLCIMVGANASDKMGMGTT SQ YLALMATFRMRPMFAVGLLFRRLTSREVLLLTVGLSLVASVELPNSLEELGDGLAMGIMMLKLLTDFQSHQLWATLLSLT SQ FVKTTFSLHYAWKTMAMILSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLITENKIWGRKSWPLNEGIMAVGIVS SQ ILLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTL SQ TILLKATLLAISGVYPMSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRILQRGLLGRSQVGVGVFQEGV SQ FHTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNAGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGA SQ IALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYL SQ PAIVREAIRRNVRTLVLAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMD SQ EAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYDWITDFPGKTVWFVPS SQ IKSGNDIANCLRKNGKRVVQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILA SQ GPMPVTVASAAQRRGRIGRNQNKEGDQYIYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYR SQ LRGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEIWTKEGERKKLRPRWLDARTYSDP SQ LALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGKAYRHAMEELPDTIETLMLLALIAVLTG SQ GVTLFFLSGRGLGKTSIGLLCVIASSALLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMIL SQ TAAANEMGLLETTKKDLGIGHAAAENHHHAAMLDVDLHPASAWTLYAVATTIITPMMRHTIENTTANISLTAIANQAAIL SQ MGLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVFMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDL SQ DPVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGL SQ AFSLMKSLGGGRRGTGAQGETLGEKWKRQLNQLSKSEFNTYKRSGIIEVDRSEAKEGLKRGEPTKHAVSRGTAKLRWFVE SQ RNLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDI SQ GESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNI SQ VSAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKNGHKSTWHYDEDNPYKTWAYHGS SQ YEVKPSGSASSMVNGVVRLLTKPWDVIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRN SQ KKPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKA SQ KGSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQ SQ NEAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGI SQ FSPSELETPNLAERVLDWLKKHGTERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPF SQ CSHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWV SQ PTSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDRWCGSLIGLTARATWATNIQVAIN SQ QVRRLIGNENYLDFMTSMKRFKNESDPEGALW // 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 P18541; PN RING finger protein Z; GN Z; OS 11624; 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: P18541; DR UNIPROT: Q49K85; 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, ECO:0000269|PubMed:12050381}. DE Reference Proteome: Yes; 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 MGQGKSREEKGTNSTNRAEILPDTTYLGPLSCKSCWQKFDSLVRCHDHYLCRHCLNLLLSVSDRCPLCKYPLPTRLKIST SQ APSSPPPYEE // ID P18588; PN Interferon-induced GTP-binding protein Mx1; GN Mx1; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000269|PubMed:2173790}. Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}. DR UNIPROT: P18588; DR Pfam: PF01031; DR Pfam: PF00350; DR Pfam: PF02212; DR PROSITE: PS00410; DR PROSITE: PS51718; DR PROSITE: PS51388; DE Function: Interferon-induced dynamin-like GTPase which has antiviral activity against influenza A virus, (IAV) and Thogoto virus (THOV). Inhibits IAV by interefering with the process of primary transcription, probably by affecting the viral polymerase function (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0030424; GO GO:0005737; GO GO:0031410; GO GO:0043197; GO GO:0044327; GO GO:0005789; GO GO:0016020; GO GO:0015630; GO GO:0031966; GO GO:0005634; GO GO:0048471; 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:0051607; GO GO:0045087; GO GO:0061025; GO GO:0000266; GO GO:0048285; GO GO:0098884; GO GO:0031623; GO GO:0050803; GO GO:0009615; GO GO:0016185; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591}; SQ MKERTSACRHGTPQKHPDTSEESQAMESVDNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEA SQ LSGVALPRGSGIVTRCPLVLKLKQLKQGEKWSGKVIYKDTEIEISHPSLVEREINKAQNLIAGEGLKISSDLISLEVSSP SQ HVPDLTLIDLPGITRVAVGDQPADIEHKIKRLITEYIQKQETINLVVVPSNVDIATTEALKMAQEVDPQGDRTIGILTKP SQ DLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRVLLEDGKATVPCLAKRLTM SQ ELTSHICKSLPILENQINVNHQIASEELQKYGADIPEDDSKRLSFLMNKINVFNKDILSLVQAQENISWEESRLFTKLRN SQ EFLAWNDYIEEHFKKTLGSSEKHSQMEKFESHYRGRELPGFVDYKAFENIIKKEVKALEEPALNMLHRVTTMVKNAFTKV SQ SSNNFGDFLNLHSTAKSKIEDIRFNQEKEAEKLIRLHFQMEHIVYCQDQAYKKALQEIREKEAEKEKSTFGAFQHNSPRK SQ ELTTTEMTQHLNAYYQECGRNIGRQIPLIIQYSILQTFGQEMEKAMLQLLQDTSKCNWFLTEQSDSREKKKFLKRRLLRL SQ DEAQRKLAKFSN // 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 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 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 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 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 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 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 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 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 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 P21910; PN Lamin-L(II); GN LAML2; OS 8355; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. DR UNIPROT: P21910; 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:0005637; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MATTTPSRSTRSSMQSPARGTSTPLSPTRISRLQEKEELRHLNDRLAVYIDRVRALELENDRLMVKISEKEEVTTREVSG SQ IKNLYESELADARKVLDETARERARLQIELGKFRSDLDELNKNYKKKDADLSTAQGRIKDLEALFHRSEAELGTALGEKR SQ SLEAEVADLRAQLSKTEDAHRVAKKQLEKETLMRVDFENRMQSLQEEMDFRKNIYEEESRETRKRHERRIVEVDRGHHYD SQ YESKLAQALDELRKQHDEQVKMYKEELEQTYQAKLDNIKRSSDHNDKAANTALEELTERRMRIETLGYQLSGLQKQANAA SQ EERIRELEELLSSDRDKYRKLLDSKEREMAEMRDQMQQQLNEYQELLDVKLALDLEINAYRKLLEGEEERLKLSPSPESR SQ VTVSRATSSSSSATRTSRSKRRRVEEEYEEGGASTGFGAGHSLGSSRITASEGSSRTITSGQSSTTRFHLSQQASATGSI SQ SIEEIDLEGKYVHLKNNSDKDQSLGNWRLKRKIGEEEEIVYKFTPKYVLKAGQSVKIYSADAGVAHSPPSILVWKNQSSW SQ GTGSNIRTYLVNTEEEEVAVRTVTKSVLRNVEEEEDEDADFGEEDLFHQQGDPRTTSRGCSVM // 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 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 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 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 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 P27269; PN Protein V2; GN V2; OS 66366; SL Nucleus Position: SL-0382; SL Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11878881, ECO:0000269|PubMed:16979684}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery. DR UNIPROT: P27269; DR Pfam: PF01524; DR Pfam: PF03716; DE Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000269|PubMed:16979684, ECO:0000269|PubMed:18165314}. DE Reference Proteome: Yes; GO GO:0044220; GO GO:0019048; GO GO:0060967; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MWDPLLNEFPESVHGFRCMLAIKYLQSVEETYEPNTLGHDLIRDLISVVRARDYVEATRRYNHFHARLEGSPKAELRQPI SQ QQPCCCPHCPRHKQATIMDVQAHVPKAQNIQNVSKP // ID P27594; PN Interferon-induced GTP-binding protein Mx1; GN MX1; OS 9823; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:17203407, ECO:0000269|PubMed:19109387}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}. DR UNIPROT: P27594; DR UNIPROT: Q1AHC4; DR UNIPROT: Q75PY7; DR Pfam: PF01031; DR Pfam: PF00350; DR Pfam: PF02212; DR PROSITE: PS00410; DR PROSITE: PS51718; DR PROSITE: PS51388; DE Function: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV). Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. {ECO:0000269|PubMed:20167191}. DE Reference Proteome: Yes; GO GO:0030424; GO GO:0005737; GO GO:0031410; GO GO:0043197; GO GO:0044327; GO GO:0005789; GO GO:0016020; GO GO:0015630; GO GO:0031966; GO GO:0005634; GO GO:0048471; 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:0071357; GO GO:0051607; GO GO:0016197; GO GO:0061025; GO GO:0000266; GO GO:1901253; GO GO:0045071; GO GO:0048285; GO GO:0098884; GO GO:0031623; GO GO:0050803; GO GO:0016185; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591}; SQ MVYSSCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS SQ SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISH SQ ELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEG SQ DRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQEQLSLAKALQKEQAFFENHAHFRDLLEEGRAT SQ IPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEY SQ ECRLFTKMRNEFCRWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDL SQ VRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEAEEEKNRKSN SQ QYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDK SQ RKFLKERLMRLTQARRRLAKFPG // 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 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 P28865; PN Nuclear egress protein 1; GN NEC1; 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_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}. DR UNIPROT: P28865; DR UNIPROT: Q69060; 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 MTVHKSRIRRSRSLSVTHRIQKRPDHREKTKLYLQLKLHDLHTVFNLFPEYEQKFLAIIKLPITGKEPIDVPFSLSNHHQ SQ HTCLEFSPYANEQISKSACLHCESVSVPTSSDAMVAHLNQVNNVMQNRLYFYGFRKDMELIRMSAKQPTIFQIFYIVHNT SQ INNIFPIMFERKQKLGMHIVFQSRTLHIPCECIKQIVAVSSGYNVYLDILQESVILTVLCETLDTNTNIHIDIGMLQKKL SQ EEMDIPNEISDRLEKYKGHLIGFH // 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 P28951; PN Nuclear egress protein 1; GN NEC1; OS 31520; 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: P28951; DR UNIPROT: Q6DLI2; 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 MFDGRSDIYDSTSFAAELDDLYSCRSTGRENGRRSRVSTRGVHRDRCGSAAKRRSTKRRCELVARERDRYSLYLDYMASH SQ PSDEISAVRELVVPLIKTTSITLPFDLNQTVADNCLSLSGMGYYLGIGGCCPTCTVSGEPRLHRADRAALILAYVQQLNN SQ IYEYRGFLASVLAAAAQGDQAGVAASEGVQAERLLENVLAQPELFFAYHVLRDGGIQNVRVLFYRDLSVSGYMMYAVFPT SQ KSVHLHYRLIDRLLAACPGYKIIAHVWQTAFVLVVRRDEGQQTDMDIPTVSAGDIYCKMCDLSFDGELLLEYKKLYAVFD SQ DFLPPV // ID P28954; PN Nuclear egress protein 2; GN NEC2; OS 31520; 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: P28954; DR UNIPROT: Q6S6P5; 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 MDSYNYRDFAVGGGLLQRIRLVVSGSLHCGESDATLNDPKHLPARCVFQFSGPDNNSVTFPIEYVLRLMKNWARSQCDPY SQ IRIQNTGVSVLFQGFFFAPPNAPMASITSEHNNVILKSTHTTGLALSGIERVKRGGGLDLRPLQAMMQISCFTRMPVVQL SQ SFRFMGPEDASRTQRLLERATSFGAMELHQKRTVDSCDRSNGIVSPREHRECRERQKRRPTPKRCASEVFASLASISSAF SQ ASERVKRRPVRIAAAILAFVFVAVILAIATKGRLF // 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 P29728; PN 2'-5'-oligoadenylate synthase 2; GN OAS2; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:19923450}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}. DR UNIPROT: P29728; DR UNIPROT: A8K9T1; DR UNIPROT: Q6PJ33; DR UNIPROT: Q86XX8; DR Pfam: PF01909; DR Pfam: PF10421; DR PROSITE: PS00832; DR PROSITE: PS00833; DR PROSITE: PS50152; DR OMIM: 603350; DR DisGeNET: 4939; DE Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). 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:10464285, PubMed:9880569, PubMed:11682059). 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:10464285, PubMed:9880569). 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 (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}. DE Reference Proteome: Yes; DE Interaction: P49761; IntAct: EBI-10211452,EBI-745579; Score: 0.67 GO GO:0005737; GO GO:0005829; GO GO:0043231; 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:0060333; GO GO:0045071; GO GO:0006139; 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 - Experimental Evidence {ECO:0000269|PubMed:2211721}; SQ MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLF SQ FSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIY SQ RELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKD SQ NFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLT SQ SPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKG SQ TALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSF SQ DVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPK SQ GSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAE SQ PTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF // ID P30026; PN Non-structural protein 1; GN POLG; OS 31636; 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:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [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}. DR UNIPROT: P30026; DR UNIPROT: Q66450; DR Pfam: PF01003; DR Pfam: PF02832; DR Pfam: PF00869; DR Pfam: PF01004; DR Pfam: PF00948; DR Pfam: PF01570; 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 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. DE Reference Proteome: No; GO GO:0005576; GO GO:0044167; GO GO:0042025; GO GO:0044220; GO GO:0016021; GO GO:0019031; GO GO:0019013; GO GO:0055036; GO GO:0046983; GO GO:0005198; GO GO:0075512; GO GO:0039654; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNNQRKKARSTPFNMLRRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVALPRFLTIPPTAGILKRWGTIKKSKAIND SQ VRGCRKEIGRMLNILNRRRRTAGVIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAIDFGELCE SQ DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTRTTTGEHGREKRSVALVPHVGMGLETGTETWMSSDGAWKRACRMETW SQ ILRHPGFTIMAAILAYTIGTTHFQRGLILILQTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT SQ LDFELIKTEATQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT SQ CKKNMEGNIVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEIVLLQ SQ MEDKAWLVHRQWFLDLPLPWLPGADTQGSNRIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT SQ GHLKCRLRMDKLQLKGMSYSMCTGKFQIVKEIAETQHGTIVIRVQYEGDGSPCKIPLEIMDLEKRHVLGRLITVNPIVTE SQ KDSPVNIEAEPPFGDSYIIIGVEPGQLKLHWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF SQ GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGVITLYLGAMVQADSGCVVSWKNKELKCGSGIFITDNV SQ HTWTEQYNFQPESPSKLASAMRKAHEEGICGIRSVTRLENLMWKQITPELKHILSEIEVKLTIMTGDIKGIMQAGTRSLR SQ PQPTELKFSWETWRKAKMVPTEPHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKEDLCCDSKVMS SQ AASKDNRAVHDDMGYWIESALNDTWKMEKASFIEVKSCHWPKSHTLWINGGLESEMIIPKSFAGPVSQHNYRPGYYTQTA SQ GPRHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSSTIPPLRIKGEDGCWYGMEIRPLKEKEENL SQ VTSLVTA // 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 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 P31689; PN DnaJ homolog subfamily A member 1; GN DNAJA1; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Membrane {ECO:0000305|PubMed:10816573}; Lipid- anchor {ECO:0000305|PubMed:10816573}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}. Note=Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proportion is associated with nuclei. {ECO:0000250}. DR UNIPROT: P31689; DR UNIPROT: Q5T7Q0; DR UNIPROT: Q86TL9; DR PDB: 2LO1; DR PDB: 2M6Y; DR PDB: 6E8M; DR Pfam: PF00226; DR Pfam: PF01556; DR Pfam: PF00684; DR PROSITE: PS00636; DR PROSITE: PS50076; DR PROSITE: PS51188; DR OMIM: 602837; DR DisGeNET: 3301; DE Function: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co- chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}. DE Reference Proteome: Yes; DE Interaction: A0A142I5B9; IntAct: EBI-20625235,EBI-347834; Score: 0.35 DE Interaction: O43542; IntAct: EBI-2849976,EBI-347834; Score: 0.35 DE Interaction: O95831; IntAct: EBI-356440,EBI-347834; Score: 0.35 DE Interaction: P00533; IntAct: EBI-297353,EBI-347834; Score: 0.35 DE Interaction: P04626; IntAct: EBI-641062,EBI-347834; Score: 0.35 DE Interaction: P05129; IntAct: EBI-949799,EBI-347834; Score: 0.35 DE Interaction: P13569; IntAct: EBI-349854,EBI-347834; Score: 0.53 DE Interaction: Q9H9G7; IntAct: EBI-2267883,EBI-347834; Score: 0.35 DE Interaction: Q9HCK5; IntAct: EBI-2269696,EBI-347834; Score: 0.35 DE Interaction: Q5S007; IntAct: EBI-5323863,EBI-347834; Score: 0.53 DE Interaction: P09622; IntAct: EBI-353366,EBI-347834; Score: 0.35 DE Interaction: P08559; IntAct: EBI-715747,EBI-347834; Score: 0.35 DE Interaction: O00429; IntAct: EBI-724571,EBI-347834; Score: 0.35 DE Interaction: Q6ZNJ1; IntAct: EBI-2862306,EBI-347834; Score: 0.35 DE Interaction: Q15077; IntAct: EBI-10235794,EBI-347834; Score: 0.35 DE Interaction: P03427; IntAct: EBI-8430745,EBI-347834; Score: 0.35 DE Interaction: Q9Y251; IntAct: EBI-5453868,EBI-347834; Score: 0.35 DE Interaction: Q9HC29; IntAct: EBI-7445625,EBI-347834; Score: 0.35 DE Interaction: Q8WW22; IntAct: EBI-2555157,EBI-347834; Score: 0.35 DE Interaction: Q96BE0; IntAct: EBI-9356686,EBI-347834; Score: 0.35 DE Interaction: Q9Y266; IntAct: EBI-357298,EBI-347834; Score: 0.35 DE Interaction: P21860; IntAct: EBI-720706,EBI-347834; Score: 0.35 DE Interaction: Q13043; IntAct: EBI-367376,EBI-347834; Score: 0.35 DE Interaction: Q16659; IntAct: EBI-1384105,EBI-347834; Score: 0.35 DE Interaction: P57078; IntAct: EBI-4422308,EBI-347834; Score: 0.35 DE Interaction: Q92769; IntAct: EBI-301821,EBI-347834; Score: 0.35 DE Interaction: Q9UBN7; IntAct: EBI-301697,EBI-347834; Score: 0.53 DE Interaction: Q969S8; IntAct: EBI-301762,EBI-347834; Score: 0.35 DE Interaction: Q96DB2; IntAct: EBI-301713,EBI-347834; Score: 0.35 DE Interaction: Q9H492; IntAct: EBI-720768,EBI-347834; Score: 0.35 DE Interaction: O95166; IntAct: EBI-712001,EBI-347834; Score: 0.35 DE Interaction: P60520; IntAct: EBI-720116,EBI-347834; Score: 0.35 DE Interaction: P05213; IntAct: EBI-347834,EBI-2311600; Score: 0.40 DE Interaction: P99024; IntAct: EBI-350896,EBI-347834; Score: 0.40 DE Interaction: Q9Z1B5; IntAct: EBI-2552918,EBI-347834; Score: 0.40 DE Interaction: P83887; IntAct: EBI-2553410,EBI-347834; Score: 0.40 DE Interaction: P68372; IntAct: EBI-2553564,EBI-347834; Score: 0.40 DE Interaction: P05214; IntAct: EBI-10963854,EBI-347834; Score: 0.35 DE Interaction: O75665; IntAct: EBI-716327,EBI-347834; Score: 0.35 DE Interaction: Q15468; IntAct: EBI-7488405,EBI-347834; Score: 0.35 DE Interaction: P35550; IntAct: EBI-7817407,EBI-347834; Score: 0.35 DE Interaction: Q6ZMQ8; IntAct: EBI-2008380,EBI-347834; Score: 0.35 DE Interaction: P10398; IntAct: EBI-365961,EBI-347834; Score: 0.35 DE Interaction: Q13418; IntAct: EBI-747644,EBI-347834; Score: 0.35 DE Interaction: P51617; IntAct: EBI-358664,EBI-347834; Score: 0.35 DE Interaction: P53671; IntAct: EBI-1384350,EBI-347834; Score: 0.35 DE Interaction: P04049; IntAct: EBI-365996,EBI-347834; Score: 0.35 DE Interaction: Q96FW1; IntAct: EBI-1058491,EBI-347834; Score: 0.35 DE Interaction: P03372; IntAct: EBI-78473,EBI-347834; Score: 0.35 DE Interaction: Q9BQE3; IntAct: EBI-1103245,EBI-347834; Score: 0.35 DE Interaction: Q71U36; IntAct: EBI-302552,EBI-347834; Score: 0.60 DE Interaction: Q9H9B4; IntAct: EBI-355861,EBI-347834; Score: 0.35 DE Interaction: Q14684; IntAct: EBI-372051,EBI-347834; Score: 0.35 DE Interaction: Q15051; IntAct: EBI-2805823,EBI-347834; Score: 0.35 DE Interaction: P07900; IntAct: EBI-296047,EBI-347834; Score: 0.35 DE Interaction: P0DOE9; IntAct: EBI-6138585,EBI-347834; Score: 0.35 DE Interaction: Q8JPQ9; IntAct: EBI-6152703,EBI-347834; Score: 0.35 DE Interaction: Q13617; IntAct: EBI-456179,EBI-347834; Score: 0.35 DE Interaction: Q13620; IntAct: EBI-456067,EBI-347834; Score: 0.35 DE Interaction: Q13616; IntAct: EBI-359390,EBI-347834; Score: 0.35 DE Interaction: Q93034; IntAct: EBI-1057139,EBI-347834; Score: 0.35 DE Interaction: Q92905; IntAct: EBI-594661,EBI-347834; Score: 0.35 DE Interaction: Q13618; IntAct: EBI-456129,EBI-347834; Score: 0.35 DE Interaction: Q77M19; IntAct: EBI-6149376,EBI-347834; Score: 0.35 DE Interaction: P15822; IntAct: EBI-722264,EBI-347834; Score: 0.37 DE Interaction: Q13042; IntAct: EBI-347834,EBI-994830; Score: 0.37 DE Interaction: Q9Y2Q3; IntAct: EBI-347834,EBI-1053767; Score: 0.40 DE Interaction: O00422; IntAct: EBI-347834,EBI-1044156; Score: 0.40 DE Interaction: P01889; IntAct: EBI-347834,EBI-1046513; Score: 0.40 DE Interaction: P31930; IntAct: EBI-347834,EBI-1052596; Score: 0.40 DE Interaction: Q92956; IntAct: EBI-347834,EBI-1056653; Score: 0.40 DE Interaction: O75365; IntAct: EBI-347834,EBI-1043866; Score: 0.40 DE Interaction: Q9NPF4; IntAct: EBI-347834,EBI-1056510; Score: 0.40 DE Interaction: Q8IXH7; IntAct: EBI-347834,EBI-536725; Score: 0.37 DE Interaction: P49703; IntAct: EBI-347834,EBI-711726; Score: 0.37 DE Interaction: P19256; IntAct: EBI-347834,EBI-718785; Score: 0.37 DE Interaction: P30408; IntAct: EBI-347834,EBI-714256; Score: 0.37 DE Interaction: Q9UM11; IntAct: EBI-347834,EBI-724997; Score: 0.37 DE Interaction: Q16526; IntAct: EBI-741297,EBI-347834; Score: 0.35 DE Interaction: P30530; IntAct: EBI-2850927,EBI-347834; Score: 0.35 DE Interaction: P61586; IntAct: EBI-446668,EBI-347834; Score: 0.35 DE Interaction: P06239; IntAct: EBI-1348,EBI-347834; Score: 0.35 DE Interaction: P41743; IntAct: EBI-286199,EBI-347834; Score: 0.35 DE Interaction: Q05513; IntAct: EBI-295351,EBI-347834; Score: 0.35 DE Interaction: P36507; IntAct: EBI-1056930,EBI-347834; Score: 0.35 DE Interaction: Q9H1R3; IntAct: EBI-356910,EBI-347834; Score: 0.35 DE Interaction: Q13882; IntAct: EBI-1383632,EBI-347834; Score: 0.35 DE Interaction: P15498; IntAct: EBI-625518,EBI-347834; Score: 0.35 DE Interaction: O15524; IntAct: EBI-968198,EBI-347834; Score: 0.35 DE Interaction: Q13163; IntAct: EBI-307294,EBI-347834; Score: 0.35 DE Interaction: Q13164; IntAct: EBI-1213983,EBI-347834; Score: 0.35 DE Interaction: P19419; IntAct: EBI-726632,EBI-347834; Score: 0.35 DE Interaction: Q13153; IntAct: EBI-1307,EBI-347834; Score: 0.35 DE Interaction: P41240; IntAct: EBI-1380630,EBI-347834; Score: 0.35 DE Interaction: P46734; IntAct: EBI-602462,EBI-347834; Score: 0.35 DE Interaction: Q02156; IntAct: EBI-706254,EBI-347834; Score: 0.35 DE Interaction: P83110-1; IntAct: EBI-25469082,EBI-347834; Score: 0.35 DE Interaction: P0DTD1; IntAct: EBI-25475871,EBI-347834; Score: 0.35 DE Interaction: P0DTC5; IntAct: EBI-25475853,EBI-347834; Score: 0.35 DE Interaction: P0DTC3; IntAct: EBI-25475894,EBI-347834; Score: 0.35 DE Interaction: P0DTD8; IntAct: EBI-25475914,EBI-347834; Score: 0.35 DE Interaction: P0DTC8; IntAct: EBI-25475900,EBI-347834; Score: 0.35 DE Interaction: Q7Z6J6; IntAct: EBI-727282,EBI-347834; Score: 0.35 DE Interaction: Q15334; IntAct: EBI-299979,EBI-347834; Score: 0.35 DE Interaction: P35240; IntAct: EBI-1014472,EBI-347834; Score: 0.35 DE Interaction: Q13509; IntAct: EBI-350989,EBI-347834; Score: 0.35 DE Interaction: Q14CZ7; IntAct: EBI-10234819,EBI-347834; Score: 0.35 DE Interaction: Q92834; IntAct: EBI-6558417,EBI-347834; Score: 0.35 DE Interaction: Q9C0F1; IntAct: EBI-744115,EBI-347834; Score: 0.35 DE Interaction: Q9NXB0; IntAct: EBI-719269,EBI-347834; Score: 0.35 DE Interaction: O14829; IntAct: EBI-2931238,EBI-347834; Score: 0.35 DE Interaction: Q9Y2T4-3; IntAct: EBI-14013186,EBI-347834; Score: 0.46 DE Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-347834; Score: 0.35 DE Interaction: Q8IVT5; IntAct: EBI-486984,EBI-347834; Score: 0.35 DE Interaction: Q9BXB4; IntAct: EBI-347834,EBI-2514786; Score: 0.35 DE Interaction: Q96SU4-2; IntAct: EBI-347834,EBI-12519654; Score: 0.35 DE Interaction: Q14249; IntAct: EBI-347834,EBI-9369928; Score: 0.35 DE Interaction: O95714; IntAct: EBI-347834,EBI-1058922; Score: 0.35 DE Interaction: A0JLT2; IntAct: EBI-394430,EBI-347834; Score: 0.35 DE Interaction: Q9NX70; IntAct: EBI-394656,EBI-347834; Score: 0.35 DE Interaction: Q04206-2; IntAct: EBI-347834,EBI-289947; Score: 0.40 DE Interaction: Q13546; IntAct: EBI-347834,EBI-358507; Score: 0.40 DE Interaction: Q9Y572; IntAct: EBI-347834,EBI-298250; Score: 0.40 DE Interaction: Q15750; IntAct: EBI-347834,EBI-358643; Score: 0.40 DE Interaction: Q9NYJ8; IntAct: EBI-347834,EBI-358708; Score: 0.40 DE Interaction: O43318-2; IntAct: EBI-347834,EBI-358700; Score: 0.40 DE Interaction: P19438; IntAct: EBI-347834,EBI-299451; Score: 0.40 DE Interaction: P20333; IntAct: EBI-347834,EBI-358983; Score: 0.40 DE Interaction: Q13233; IntAct: EBI-347834,EBI-49776; Score: 0.40 DE Interaction: Q99759; IntAct: EBI-347834,EBI-307281; Score: 0.40 DE Interaction: Q00653; IntAct: EBI-347834,EBI-307326; Score: 0.40 DE Interaction: Q99558; IntAct: EBI-347834,EBI-358011; Score: 0.40 DE Interaction: Q15628; IntAct: EBI-347834,EBI-359215; Score: 0.40 DE Interaction: Q13077; IntAct: EBI-347834,EBI-359224; Score: 0.40 DE Interaction: Q12933; IntAct: EBI-347834,EBI-355744; Score: 0.40 DE Interaction: Q9Y4K3; IntAct: EBI-347834,EBI-359276; Score: 0.40 DE Interaction: Q9Y333; IntAct: EBI-347834,EBI-347416; Score: 0.55 GO GO:0098554; GO GO:0005829; GO GO:0070062; GO GO:0016020; GO GO:0015630; GO GO:0005739; GO GO:0005634; GO GO:0048471; GO GO:0005524; GO GO:0001671; GO GO:0055131; GO GO:0051087; GO GO:0001664; GO GO:0030544; GO GO:0050750; GO GO:0046872; GO GO:0030957; GO GO:0031625; GO GO:0051082; GO GO:0043066; GO GO:1903748; GO GO:0043508; GO GO:1905259; GO GO:0031397; GO GO:0043065; GO GO:0006457; GO GO:0070585; GO GO:0051223; GO GO:0009408; GO GO:0006986; TP Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:14752510,}; SQ MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGG SQ FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI SQ RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII SQ IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL SQ IIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS // 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 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 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 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 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 P33755; PN Nuclear protein localization protein 4; GN NPL4; OS 559292; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. DR UNIPROT: P33755; DR UNIPROT: D6VQG6; DR PDB: 6JWH; DR PDB: 6JWI; DR PDB: 6JWJ; DR PDB: 6OA9; DR PDB: 6OAA; DR Pfam: PF05021; DR Pfam: PF05020; DR PROSITE: PS50249; DE Function: Substrate-recruiting cofactor of the CDC48-NPL4-UFD1 segregase (PubMed:31249135). Assists CDC48 in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation (PubMed:11739805, PubMed:11740563, PubMed:11847109). Involved in the import of nuclear- targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus (PubMed:8930904, PubMed:11733065). Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1 (PubMed:11733065). Regulates ubiquitin-mediated mitochondria protein degradation (PubMed:31249135). Involved in spindle disassembly probably by promoting the degradation of spindle assemby factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562). {ECO:0000269|PubMed:11733065, ECO:0000269|PubMed:11739805, ECO:0000269|PubMed:11740563, ECO:0000269|PubMed:11847109, ECO:0000269|PubMed:14636562, ECO:0000269|PubMed:31249135, ECO:0000269|PubMed:8930904}. DE Reference Proteome: Yes; DE Interaction: P54860; IntAct: EBI-20003,EBI-12193; Score: 0.55 DE Interaction: P53044; IntAct: EBI-19997,EBI-12193; Score: 0.93 DE Interaction: Q04311; IntAct: EBI-784329,EBI-12193; Score: 0.40 DE Interaction: Q05468; IntAct: EBI-32961,EBI-12193; Score: 0.35 DE Interaction: Q12532; IntAct: EBI-33283,EBI-12193; Score: 0.35 DE Interaction: Q08109; IntAct: EBI-37613,EBI-12193; Score: 0.53 DE Interaction: P25694; IntAct: EBI-4308,EBI-12193; Score: 0.90 DE Interaction: Q04228; IntAct: EBI-12193,EBI-27730; Score: 0.74 DE Interaction: P32467; IntAct: EBI-8774,EBI-12193; Score: 0.35 DE Interaction: P16140; IntAct: EBI-12193,EBI-20254; Score: 0.35 DE Interaction: P02994; IntAct: EBI-12193,EBI-6314; Score: 0.35 DE Interaction: P06169; IntAct: EBI-12193,EBI-5687; Score: 0.35 DE Interaction: P41832; IntAct: EBI-3692,EBI-12193; Score: 0.27 DE Interaction: Q02159; IntAct: EBI-12193,EBI-19749; Score: 0.37 DE Interaction: P39081; IntAct: EBI-12193,EBI-12980; Score: 0.37 GO GO:0036266; GO GO:0005737; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0042175; GO GO:0005634; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0043130; GO GO:0031625; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0043161; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; GO GO:0006511; TP Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis; SQ MLIRFRSKNGTHRVSCQENDLFGTVIEKLVGNLDPNADVDTFTVCEKPGQGIHAVSELADRTVMDLGLKHGDMLILNYSD SQ KPANEKDGVNVEIGSVGIDSKGIRQHRYGPLRIKELAVDEELEKEDGLIPRQKSKLCKHGDRGMCEYCSPLPPWDKEYHE SQ KNKIKHISFHSYLKKLNENANKKENGSSYISPLSEPDFRINKRCHNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEFQ SQ KSEIINEFIQAWRYTGMQRFGYMYGSYSKYDNTPLGIKAVVEAIYEPPQHDEQDGLTMDVEQVKNEMLQIDRQAQEMGLS SQ RIGLIFTDLSDAGAGDGSVFCKRHKDSFFLSSLEVIMAARHQTRHPNVSKYSEQGFFSSKFVTCVISGNLEGEIDISSYQ SQ VSTEAEALVTADMISGSTFPSMAYINDTTDERYVPEIFYMKSNEYGITVKENAKPAFPVDYLLVTLTHGFPNTDTETNSK SQ FVSSTGFPWSNRQAMGQSQDYQELKKYLFNVASSGDFNLLHEKISNFHLLLYINSLQILSPDEWKLLIESAVKNEWEESL SQ LKLVSSAGWQTLVMILQESG // 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 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 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 P34349; PN MOB-like protein phocein; GN mob; OS 6239; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y3A3}. Membrane {ECO:0000250|UniProtKB:Q9Y3A3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y3A3}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9Y3A3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y3A3}. DR UNIPROT: P34349; DR Pfam: PF03637; DE Function: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250|UniProtKB:Q9QYW3}. DE Reference Proteome: Yes; GO GO:0032580; GO GO:0048471; GO GO:0046872; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Y3A3}; SQ MTAATENRTVRRNGPGTKRADWNNWSPLAFEEMDSALNIQQYIQQTIKANPADVATILTPPLDQDEGVWKYEHLRQFCIE SQ LNGLALLLQRECIPETCQQMTATEQWIFLCAAHKNPNECPAIDYTRHTLDGAATLLNSNKYFPSRVNIKEISISKLGSVA SQ RRVYRIFSHAFFHHRKLFDEFENETHLCKRFTTYVSKYNLMQQEHLIVPILPNQQQQQQTTVQ // 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 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 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 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 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 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 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 P35281; PN Ras-related protein Rab-10; GN Rab10; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:20576682}; Cytoplasmic side {ECO:0000305|PubMed:20576682}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium {ECO:0000269|PubMed:20576682}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61027}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4 storage vesicles (By similarity). Localizes to the base of the cilium (PubMed:20576682). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:20576682}. DR UNIPROT: P35281; 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 (By similarity). 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). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (By similarity). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Plays also a specific role in asymmetric protein transport to the plasma membrane (By similarity). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (PubMed:21856246). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (By similarity). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027, ECO:0000269|PubMed:21856246}. DE Reference Proteome: Yes; DE Interaction: P19357; IntAct: EBI-915426,EBI-917314; Score: 0.35 GO GO:0098993; GO GO:0005929; GO GO:0012505; GO GO:0005789; GO GO:0071782; GO GO:0005768; GO GO:0070382; GO GO:0005794; GO GO:0032593; GO GO:0016020; GO GO:0048471; GO GO:0030670; GO GO:0005886; GO GO:0055037; GO GO:0055038; GO GO:0008021; GO GO:0005802; GO GO:0019003; GO GO:0051021; GO GO:0005525; GO GO:0003924; GO GO:0031489; GO GO:0019882; GO GO:0007409; GO GO:0071236; GO GO:0032869; GO GO:0071786; GO GO:0016197; GO GO:0045200; GO GO:0097051; GO GO:0090150; GO GO:0043001; GO GO:0006893; GO GO:0006886; GO GO:0030859; GO GO:1903361; GO GO:0072659; GO GO:0009306; GO GO:0032482; GO GO:0045055; GO GO:0017157; GO GO:0006904; GO GO:0016192; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIEIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR SQ GAMGIMLVYDITNGKSFENISKWLRNIDQHANEDVERMLLRNKCDMDHKRVVPKGKGEQIAREHRIRFFETSAKANINIE SQ KAFLTLPEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC // 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 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 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 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 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 P35930; PN RNA-directed RNA polymerase; GN POL1; OS 12262; 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: P35930; DR UNIPROT: Q66182; 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 MYMLTFEPGLCVAGIIRQVRSNPFMHVVQAYARTTETYREDIEMTKSMLKLKADEPLLVMSIVAAAMDFQTMVMAPIEME SQ ASEFLYGFYAERMSYIVTNRGMSELHEYIQLQCQRHLLVKVEIDGQYLVQEHEYEAQGFNIKRVKELITDVATWVPKKVK SQ GMIGWSVDAVLDSFQEYFYKVITERIPMAMKVCSWVATVWDQIKTWIEDAMTAMSSFLQGCNELLTWGLATLAACCALNV SQ LERILIFMEFLDESIDIAGIFLRTGVVAAACYHFSSTAKGFTEMMSVLSVATTAVAAVVCANYFGGSKTKKVNAQGNPVD SQ LLERIAAGLSSISQDSLVSLGKSCSAINSIATSYGHLRNFAGRVLTMLRDFAWKILGLETRFLADAALVFGEDVDGWLQR SQ ISALREAYVSKAYSSQDEVFEMNVLLERGYKMRHLMATGSRVSPAIGNMLMQGLADLERLHRNAAVQGVKGVRKIPFTVF SQ AHGNSRCGKSLLIGKLISDFQEHKGLGEDTVYSRNTTETHWSGYRRQPIVVIDDFAAVESDISAEAQLINLVSSTPYSVV SQ MAAIEEKGMTFDSQFIFASTNFLEVSPNGKIRCDDAFRNRRHVLIDVKLKPEVEYQSDDFTANQSYNILEHSHGRYNVVA SQ TFDNYEELLAYCLTKHEQHEAEQEANLAKLRRTNKFESHFKKFEQVLQLSTYFSSSIERIKREALATTDGADDYHLLYVV SQ PRNGSYLHVAANKDFQIQQWYGPVEEVAEEDILRASERMLLGAYEFLLLSTELNVVVKNHLPELICTDNYDHNLEFCGVV SQ GDPVYHQQLLKNIRALKPWHRAVLFGIGTLMGAKNPTPWYKRMWEGIKDVLYKAYSTEISQWPVPLKITCGIVLVGIVGA SQ GFWKTVSVLTNAGNGAGLVGAAVNSFSVVSTAEAQSRKPNRFEVQQYRYKNVPLTRRSWGNAQMSLDQSTVSILNKCHAK SQ FIIASQHAQIVLVPGRRFIGYSHFFCNLKHPLMVQIETADRTYFHRYQPENMEYIEDSELCVYHSSCLEDISHSCWDLFC SQ WDPDKELPKKFSADFVSCKYNTWTKSVEPTWANVDAEVIKEDFTICDGEYRNTVSTSIRYEAPTVMSDCGSMIITNVGGK SQ TKIVGIHVAGRDNKIGMASLLPPLLPCAQAQGAEKYFNFYPIEYDAAEGIARVGELKPKLYIPLPKKTSLVKTPEEWHLG SQ TPCDKVPSILVKGDPRLADTVHADYDPCLSGLTKYSTPMSPLDSVLLGETCQEILDEWFDCLPEGFELGEVTINEALNGV SQ DGVDYMDRIPLATSEGFPHVMSREQGEKGKQRFVQGDGHIVSLIPGTSVHEAYETLSRTIATEVPTLVGIECPKDEKLPF SQ RKVFTKPKTRNFTILPMEYNILVRQYFLNFVRFIMKKRDVLPCQVGINPYSMEWSIVASRLKSQGNDILCCDYSSFDGLL SQ SKQIMEMMADMINRFCGGGTLICAKRKNLLMACCSRLAISRDSVWRIECGIPSGFPLTVICNSIFNEILVRYHYKLLLQE SQ HNAPNMYVQSFKNLISMVTYGDDNLISVNAVVKPYFDGTKLKQAMARNGIIITDGKDKTSATLEFRRLEDCDFLKRGFLK SQ RSSVLWDAPEEKASLWAQLHYVNVNNCEMQVAYMTNLVNVLRELYMHDPTEMVEFRRLALKSIPWLNTTDLPTLYQVKEF SQ YAEQRLRNIPDHNDSLDMLTSVDLLGPAILGEGVPQEALVLSELLEVRDLRYHTVPDNDNGKEVWILFNTMYPQKLLPSN SQ CHSFTWNCGQGRGGLPTQHWLATNVTRTDSKLNKLIRTAVAANKKIVLATKDNILPINVIAVLLAARNKVMPSLATNALL SQ TYVIGAAKKLNFLTSECQFAFFNV // 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 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 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 P36282; PN Protein V2; GN V2; OS 223353; SL Nucleus Position: SL-0382; SL Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. 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: P36282; DR Pfam: PF01524; DR Pfam: PF03716; DE Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0044220; GO GO:0019048; GO GO:0060967; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MWDPLVHEFPETVHGFRCMLANKYLLAVESKYAPDTLGYELIRDCIGVVRSRNYEQATSRYRDIYTRLQGATEAELQQSV SQ QERCCCPHCPRHKKADMGESAHVQKAHDVQAVQKP // ID P36312; PN RNA-directed RNA polymerase; GN POL1; OS 31716; 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: P36312; 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; SQ MKFFAGQTVMDVLQHVSSPTTNLRLLSYCNLKKEEDGKMMLAIKEQRHRRLLTLSYGAMCFQFSNSVGDEGIEVDDDELM SQ FEIFDALLRTKISNSKGMTHLYSWMRGVYLSTFKVEVQCDDYNSNLLEKDLAGEAQGLSQFVSGLADWIPSRVKTLAGYA SQ AEGIIEAFKKHFDKLLVEYCPMAVAACSWITTVWTTIKEWVQSAMDAMSWIMAGCTELISWGMCVIAGSCALSLLEKALV SQ AMGLISSSFDLAGIFVRSAVVGAFCLTVVNKRSRNCAELLQLVSLAVGAVSSATSSCFQSPVGQATDVSAESQSGGVEML SQ ESLAKNLTNFCDGTLVSIGKTCNAVNSINTAAGTIKNLVGRLLSMLSNFAYKLLGLESTFLRDASVVFSENVDGWLKQIS SQ WCQDQFLAKAYINQDELMVLRSLITRGEVMQREMIMGGMKVSPTVCGLINKGCTDLAKLMAGAVMHGTSGTRKIPFVVYA SQ HGASRVGKTMVINRLIEDFRKELELGEDCVYPRNVVDDYWSGYKRQPIVVIDDFGAVSSDPSAEAQLIPLISSAPYPLNM SQ ADLSEKGMHFDSAIVMCSSNFIECSPESKVRDEMAFRNRRHVLFTVSLDPNIPYDGDDITKNQIYEIKTWFHDSYHVEAT SQ FTSYGDLLAYCKNKWVEHNTEQEANLKQLGVKKESVAFQQFRSILDLAVFVNQDAENFKQRLETPDGRCHFVSCYDKSGI SQ LRHYTIDATGDVQEMEKVDSSLDDILLEKTNKMVLAAYKMIKYHKDTNLVIKTQLADLVDPTKYTADFQFDGVIGSPLFS SQ SQVMPSVKALPLWQRMVLYTVGQNLGRTHSSWYEGIKDKCMLALSKAYSTEIKDWPVALKIVVGVILATVAGKAFWRFYA SQ SMADAGNGGHFVGAVASAFAGSQAVVAQSRKPNRFDVAQYRYRNIPLRKRNWAEGQMSLDQSTMLIMEKCKANFVFSNIS SQ CQIVMLPGRQFLCYKHVFASLNSPMYVDIYTANKKYKLYYKPQNRVYFETDSEIMLYKDASLEDIPASCWDLFCFDAEKS SQ LPRGSFPAEILSCKLDRTTNQHIPEWADISARTVNQKLDVEFGEYQTIFYSYLQYDVSTKAEDCGSLIIATIDGRKKIIG SQ IHTAGRANRSGFASYMPQVEIPVQAQAAEKFFDFLEKEQHVTEGIGKVGNLKKGVWVPLPTKTNLVETPKEWHLGTEKTK SQ EPSILSSTDLRLGDKQYDPFVGGIQKYAEPMGILDDEVLRHVATDIVEEWFDCVDPQEDTFEEVDLQVAINGLEGMEYME SQ RVPMATSEGFPHILTRKSGEKGKGRFVYGDGEIFDLIPGTSVHEAYLTLEETCADTVPALVGIECPKDEKLPLRKIYEKP SQ KTRCFTVLPMEYNLVVRRKFLKFVVFIMKNRHRLSCQVGINPYGMEWSRLAMSLLEKGNNILCCDYSSFDGLLTKQVMHL SQ MSEMINELCGGSSRLKQQRTNLLMACCSRYALCKGEVWRVECGIPSGFPLTVICNSIFNELLVRYSYIKICQQARVPATI SQ TYGFSTFVKMVTYGDDNLLSVQSAITHVFDGTKLKEFLKLNGITITDGKDKTSPVLNFRNLEDCDFLKRGFKKESDVVWV SQ GPEEKESLWAQLHYVTTNNLEKHEAYLVNVVNVIRELYLHDPREAAELRRKAIQNVDFLKENPKDLPTMAAIKEFYNMQR SQ QQQFVDSNDNLDSLLNPDFLFVAPHRKMHEAEMELVPKWYLRDLGKAPINVLTGEADRICVLVNASIPDHLLPEKVVNIS SQ WPYGPGRGGLPTHGWAQANLYNPNSAVVKKLRTLVNQNPDDRVDICFRHDAVPVAIATIIFLVHLGKVKGRSANEYLTKI SQ IDSAKSLKFLPKECDIIF // 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 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 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 P38242; PN UDP-N-acetylglucosamine transferase subunit ALG14; GN ALG14; OS 559292; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:16100110, ECO:0000269|PubMed:17686769}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:15282802}; Single- pass membrane protein {ECO:0000255}. DR UNIPROT: P38242; DR UNIPROT: D6VQ69; 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. {ECO:0000269|PubMed:15615718, ECO:0000269|PubMed:16100110}. DE Reference Proteome: Yes; DE Interaction: P11484; IntAct: EBI-8627,EBI-21477; Score: 0.53 DE Interaction: P32589; IntAct: EBI-21477,EBI-8648; Score: 0.35 DE Interaction: P10591; IntAct: EBI-21477,EBI-8591; Score: 0.35 DE Interaction: P25294; IntAct: EBI-21477,EBI-17244; Score: 0.35 DE Interaction: P10592; IntAct: EBI-21477,EBI-8603; Score: 0.35 DE Interaction: P40069; IntAct: EBI-21477,EBI-9166; Score: 0.35 GO GO:0030176; GO GO:0031227; GO GO:0031965; GO GO:0042175; GO GO:0043541; GO GO:0043495; GO GO:0006488; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MKTAYLASLVLIVSTAYVIRLIAILPFFHTQAGTEKDTKDGVNLLKIRKSSKKPLKIFVFLGSGGHTGEMIRLLENYQDL SQ LLGKSIVYLGYSDEASRQRFAHFIKKFGHCKVKYYEFMKAREVKATLLQSVKTIIGTLVQSFVHVVRIRFAMCGSPHLFL SQ LNGPGTCCIISFWLKIMELLLPLLGSSHIVYVESLARINTPSLTGKILYWVVDEFIVQWQELRDNYLPRSKWFGILV // ID P38529; PN Heat shock factor protein 1; GN HSF1; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q00613}. Cytoplasm {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}. DR UNIPROT: P38529; DR UNIPROT: I7GGU6; DR Pfam: PF00447; DR Pfam: PF06546; DR PROSITE: PS00434; 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:8455593). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. 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. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. 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. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells. Plays a role in nuclear export of stress-induced mRNA. Plays a role in the regulation of mitotic progression. Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation. {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:8455593}. DE Reference Proteome: Yes; GO GO:0005813; GO GO:0101031; GO GO:0000777; GO GO:0005737; GO GO:0000776; GO GO:0097431; GO GO:0097165; GO GO:0005654; GO GO:0005634; GO GO:0048471; GO GO:0016605; GO GO:0031490; GO GO:0001046; GO GO:0003677; GO GO:0003700; GO GO:0031072; GO GO:1990841; GO GO:0042803; GO GO:0043621; GO GO:0000978; GO GO:0043565; GO GO:0071276; GO GO:0071480; GO GO:0034605; GO GO:0006281; GO GO:0000165; GO GO:0006397; GO GO:0051028; GO GO:2001033; GO GO:0031333; GO GO:0000122; GO GO:1902808; GO GO:1902751; GO GO:0008284; GO GO:0010628; GO GO:0045931; GO GO:1900365; GO GO:0045944; GO GO:0061408; GO GO:0070207; GO GO:0043618; GO GO:0009408; GO GO:0009416; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEGPGAAAAAVGAGPGGSNVSAFLTKLWTLVEDPETDPLICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNM SQ YGFRKVVHIEQGGLVKPEKDDTEFQHPYFIRGQEHLLENIKRKVTSVSSIKNEDIKVRQDNVTKLLTDIQVMKGKQESMD SQ SKLIAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSSSAHSMPKYSRQYSLEHVH SQ GSSPYAASSPAYSGSNIYSPDSSTNSGPIISDVTELAQSSPSASPSGSLDERSSPVVRIKEEPPSPSRSPKENEPSTTTA SQ AAGNSTEQPQPQEKCLSVACLDKNELNDHLDTIDSNLDNLQTMLSTHGFSVDTTALLDLFSPSMTVTDMNLPDLDSSLAS SQ IQDLLSSQEQQKPSEADAAAADTGKQLVHYTAQPLFLVDSSAVDVGSGDLPIFFELGEGSYFTDGDEYNEDPTISLLSGT SQ EQPKPKDPTVS // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 P49790; PN Nuclear pore complex protein Nup153; GN NUP153; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0185; SL Comments: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Tightly associated with the nuclear membrane and lamina (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000250}. DR UNIPROT: P49790; DR UNIPROT: B4DIK2; DR UNIPROT: E7EPX5; DR UNIPROT: F6QR24; DR UNIPROT: Q4LE47; DR UNIPROT: Q5T9I7; DR UNIPROT: Q7Z743; DR PDB: 2EBQ; DR PDB: 2EBR; DR PDB: 2EBV; DR PDB: 2GQE; DR PDB: 4U0C; DR PDB: 4U0D; DR PDB: 5TSV; DR PDB: 5TSX; DR PDB: 6AYA; DR Pfam: PF08604; DR Pfam: PF10599; DR Pfam: PF00641; DR PROSITE: PS01358; DR PROSITE: PS50199; DR OMIM: 603948; DR DisGeNET: 9972; 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. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}. DE Reference Proteome: Yes; DE Interaction: A8CG34; IntAct: EBI-286779,EBI-2880179; Score: 0.35 DE Interaction: O15504; IntAct: EBI-286779,EBI-2515057; Score: 0.35 DE Interaction: P02545; IntAct: EBI-351935,EBI-286779; Score: 0.49 DE Interaction: P12270; IntAct: EBI-286779,EBI-1048528; Score: 0.35 DE Interaction: P46060; IntAct: EBI-286779,EBI-396091; Score: 0.35 DE Interaction: Q9UPY3; IntAct: EBI-395506,EBI-286779; Score: 0.56 DE Interaction: Q92973; IntAct: EBI-286779,EBI-286693; Score: 0.53 DE Interaction: Q14974; IntAct: EBI-286779,EBI-286758; Score: 0.53 DE Interaction: Q8WUF5; IntAct: EBI-5550163,EBI-286779; Score: 0.35 DE Interaction: Q13625; IntAct: EBI-77642,EBI-286779; Score: 0.35 DE Interaction: P62826; IntAct: EBI-286642,EBI-286779; Score: 0.64 DE Interaction: Q96DB2; IntAct: EBI-301713,EBI-286779; Score: 0.35 DE Interaction: Q5S007; IntAct: EBI-5323863,EBI-286779; Score: 0.35 DE Interaction: P25054; IntAct: EBI-727707,EBI-286779; Score: 0.37 DE Interaction: Q9Y2K6; IntAct: EBI-2511991,EBI-286779; Score: 0.40 DE Interaction: Q8IY92; IntAct: EBI-2370740,EBI-286779; Score: 0.35 DE Interaction: P03372; IntAct: EBI-78473,EBI-286779; Score: 0.35 DE Interaction: Q9QWT9; IntAct: EBI-2552204,EBI-286779; Score: 0.40 DE Interaction: E9PVX6; IntAct: EBI-2553009,EBI-286779; Score: 0.40 DE Interaction: P51784; IntAct: EBI-306876,EBI-286779; Score: 0.40 DE Interaction: Q8BH74; IntAct: EBI-2554056,EBI-286779; Score: 0.35 DE Interaction: Q9ERU9; IntAct: EBI-643756,EBI-286779; Score: 0.35 DE Interaction: E9PUA5; IntAct: EBI-10972016,EBI-286779; Score: 0.35 DE Interaction: Q6PFD9; IntAct: EBI-646104,EBI-286779; Score: 0.35 DE Interaction: P57740; IntAct: EBI-295687,EBI-286779; Score: 0.35 DE Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-286779; Score: 0.35 DE Interaction: Q8VE37; IntAct: EBI-8006911,EBI-286779; Score: 0.35 DE Interaction: P63280; IntAct: EBI-80180,EBI-286779; Score: 0.35 DE Interaction: Q80U93; IntAct: EBI-2551193,EBI-286779; Score: 0.35 DE Interaction: Q96EE3; IntAct: EBI-922818,EBI-286779; Score: 0.35 DE Interaction: O14862; IntAct: EBI-6253193,EBI-286779; Score: 0.35 DE Interaction: P18754; IntAct: EBI-286779,EBI-992720; Score: 0.35 DE Interaction: O00629; IntAct: EBI-286779,EBI-396343; Score: 0.35 DE Interaction: Q8TEM1; IntAct: EBI-286779,EBI-372826; Score: 0.35 DE Interaction: Q9H9A5; IntAct: EBI-286779,EBI-1054261; Score: 0.35 DE Interaction: Q53GS7; IntAct: EBI-286779,EBI-1955541; Score: 0.35 DE Interaction: P78406; IntAct: EBI-286779,EBI-724495; Score: 0.35 DE Interaction: Q8NFH5; IntAct: EBI-286779,EBI-9050429; Score: 0.35 DE Interaction: Q8IXQ5-2; IntAct: EBI-286779,EBI-10981566; Score: 0.35 DE Interaction: Q9NXE4-2; IntAct: EBI-286779,EBI-10966436; Score: 0.35 DE Interaction: J3KMX2; IntAct: EBI-286779,EBI-11076792; Score: 0.35 DE Interaction: P52948-5; IntAct: EBI-286779,EBI-5280407; Score: 0.35 DE Interaction: P52292; IntAct: EBI-286779,EBI-349938; Score: 0.53 DE Interaction: P63165; IntAct: EBI-286779,EBI-80140; Score: 0.35 DE Interaction: Q8WUM0; IntAct: EBI-286779,EBI-295695; Score: 0.53 DE Interaction: Q9NRG9; IntAct: EBI-286779,EBI-3912901; Score: 0.35 DE Interaction: Q69YH5; IntAct: EBI-286779,EBI-6911908; Score: 0.35 DE Interaction: P61956-2; IntAct: EBI-286779,EBI-10966382; Score: 0.35 DE Interaction: Q96HA1; IntAct: EBI-286779,EBI-739990; Score: 0.35 DE Interaction: Q9UKX7; IntAct: EBI-286779,EBI-2371082; Score: 0.35 DE Interaction: P33991; IntAct: EBI-286779,EBI-374938; Score: 0.35 DE Interaction: P62136; IntAct: EBI-286779,EBI-357253; Score: 0.53 DE Interaction: O14715; IntAct: EBI-286779,EBI-2560912; Score: 0.35 DE Interaction: O00505; IntAct: EBI-286779,EBI-358297; Score: 0.35 DE Interaction: P63279; IntAct: EBI-286779,EBI-80168; Score: 0.35 DE Interaction: Q9BW27; IntAct: EBI-286779,EBI-716392; Score: 0.35 DE Interaction: Q03188; IntAct: EBI-286779,EBI-295799; Score: 0.35 DE Interaction: Q8NFH4; IntAct: EBI-286779,EBI-2563158; Score: 0.35 DE Interaction: P49792; IntAct: EBI-286779,EBI-973138; Score: 0.35 DE Interaction: Q8NFH3; IntAct: EBI-286779,EBI-1059321; Score: 0.35 DE Interaction: Q969G3; IntAct: EBI-286779,EBI-455078; Score: 0.35 DE Interaction: Q9UBU9; IntAct: EBI-286779,EBI-398874; Score: 0.76 DE Interaction: O60684; IntAct: EBI-286779,EBI-359923; Score: 0.35 DE Interaction: O95373; IntAct: EBI-286779,EBI-286735; Score: 0.35 DE Interaction: Q99567; IntAct: EBI-286779,EBI-726178; Score: 0.35 DE Interaction: Q86XI6; IntAct: EBI-286779,EBI-3918864; Score: 0.35 DE Interaction: Q9BTX1-2; IntAct: EBI-286779,EBI-10966386; Score: 0.35 DE Interaction: Q8N1F7; IntAct: EBI-286779,EBI-1042703; Score: 0.35 DE Interaction: Q9HC62; IntAct: EBI-286779,EBI-714881; Score: 0.35 DE Interaction: Q96SK2; IntAct: EBI-286779,EBI-10963859; Score: 0.35 DE Interaction: P52294; IntAct: EBI-286779,EBI-358383; Score: 0.35 DE Interaction: Q8TAQ2; IntAct: EBI-286779,EBI-357418; Score: 0.35 DE Interaction: Q96EE3-1; IntAct: EBI-286779,EBI-10966390; Score: 0.35 DE Interaction: Q92621; IntAct: EBI-286779,EBI-1045046; Score: 0.35 DE Interaction: Q9P0U3-2; IntAct: EBI-286779,EBI-10967520; Score: 0.35 DE Interaction: Q5SRE5; IntAct: EBI-286779,EBI-1049404; Score: 0.35 DE Interaction: Q12769; IntAct: EBI-286779,EBI-295715; Score: 0.35 DE Interaction: Q9BW19; IntAct: EBI-286779,EBI-2107279; Score: 0.35 DE Interaction: E9PF10; IntAct: EBI-286779,EBI-10966422; Score: 0.35 DE Interaction: Q6NUQ4; IntAct: EBI-286779,EBI-372318; Score: 0.35 DE Interaction: P35658-2; IntAct: EBI-286779,EBI-10969485; Score: 0.35 DE Interaction: Q9UN86-2; IntAct: EBI-11035716,EBI-286779; Score: 0.35 DE Interaction: Q05322; IntAct: EBI-6153153,EBI-286779; Score: 0.35 DE Interaction: Q13618; IntAct: EBI-456129,EBI-286779; Score: 0.35 DE Interaction: A0A0F7R9Q0; IntAct: EBI-2815990,EBI-286779; Score: 0.37 DE Interaction: A0A0F7RG11; IntAct: EBI-2815999,EBI-286779; Score: 0.37 DE Interaction: Q9ZC54; IntAct: EBI-2846248,EBI-286779; Score: 0.37 DE Interaction: P01106; IntAct: EBI-447544,EBI-286779; Score: 0.35 DE Interaction: Q8WUY9; IntAct: EBI-3924857,EBI-286779; Score: 0.35 DE Interaction: P36873-2; IntAct: EBI-3964623,EBI-286779; Score: 0.35 DE Interaction: Q9GZY0; IntAct: EBI-444173,EBI-286779; Score: 0.35 DE Interaction: Q8N9Q2; IntAct: EBI-10268630,EBI-286779; Score: 0.35 DE Interaction: Q2NL82; IntAct: EBI-358058,EBI-286779; Score: 0.35 DE Interaction: Q9UKX7-2; IntAct: EBI-10966378,EBI-286779; Score: 0.35 DE Interaction: Q9BXS6-2; IntAct: EBI-10969852,EBI-286779; Score: 0.35 GO GO:0005829; GO GO:0043657; GO GO:0016020; GO GO:0042405; GO GO:0031965; GO GO:0034399; GO GO:0005643; GO GO:0044613; GO GO:0044615; GO GO:0005730; GO GO:0005654; GO GO:0003677; GO GO:0042802; GO GO:0046872; GO GO:0008139; GO GO:0043495; GO GO:0017056; GO GO:0075733; GO GO:0006406; GO GO:0046832; GO GO:0051292; GO GO:0006606; GO GO:0016925; GO GO:1900034; GO GO:0060964; GO GO:0006110; GO GO:0006405; GO GO:0006409; GO GO:0046718; GO GO:0075732; GO GO:0016032; GO GO:0019083; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MASGAGGVGGGGGGKIRTRRCHQGPIKPYQQGRQQHQGILSRVTESVKNIVPGWLQRYFNKNEDVCSCSTDTSEVPRWPE SQ NKEDHLVYADEESSNITDGRITPEPAVSNTEEPSTTSTASNYPDVLTRPSLHRSHLNFSMLESPALHCQPSTSSAFPIGS SQ SGFSLVKEIKDSTSQHDDDNISTTSGFSSRASDKDITVSKNTSLPPLWSPEAERSHSLSQHTATSSKKPAFNLSAFGTLS SQ PSLGNSSILKTSQLGDSPFYPGKTTYGGAAAAVRQSKLRNTPYQAPVRRQMKAKQLSAQSYGVTSSTARRILQSLEKMSS SQ PLADAKRIPSIVSSPLNSPLDRSGIDITDFQAKREKVDSQYPPVQRLMTPKPVSIATNRSVYFKPSLTPSGEFRKTNQRI SQ DNKCSTGYEKNMTPGQNREQRESGFSYPNFSLPAANGLSSGVGGGGGKMRRERTRFVASKPLEEEEMEVPVLPKISLPIT SQ SSSLPTFNFSSPEITTSSPSPINSSQALTNKVQMTSPSSTGSPMFKFSSPIVKSTEANVLPPSSIGFTFSVPVAKTAELS SQ GSSSTLEPIISSSAHHVTTVNSTNCKKTPPEDCEGPFRPAEILKEGSVLDILKSPGFASPKIDSVAAQPTATSPVVYTRP SQ AISSFSSSGIGFGESLKAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFK SQ PVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECS SQ VCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG SQ TKSGFKGFDTSSSSSNSAASSSFKFGVSSSSSGPSQTLTSTGNFKFGDQGGFKIGVSSDSGSINPMSEGFKFSKPIGDFK SQ FGVSSESKPEEVKKDSKNDNFKFGLSSGLSNPVSLTPFQFGVSNLGQEEKKEELPKSSSAGFSFGTGVINSTPAPANTIV SQ TSENKSSFNLGTIETKSASVAPFTCKTSEAKKEEMPATKGGFSFGNVEPASLPSASVFVLGRTEEKQQEPVTSTSLVFGK SQ KADNEEPKCQPVFSFGNSEQTKDENSSKSTFSFSMTKPSEKESEQPAKATFAFGAQTSTTADQGAAKPVFSFLNNSSSSS SQ STPATSAGGGIFGSSTSSSNPPVATFVFGQSSNPVSSSAFGNTAESSTSQSLLFSQDSKLATTSSTGTAVTPFVFGPGAS SQ SNNTTTSGFGFGATTTSSSAGSSFVFGTGPSAPSASPAFGANQTPTFGQSQGASQPNPPGFGSISSSTALFPTGSQPAPP SQ TFGTVSSSSQPPVFGQQPSQSAFGSGTTPNSSSAFQFGSSTTNFNFTNNSPSGVFTFGANSSTPAASAQPSGSGGFPFNQ SQ SPAAFTVGSNGKNVFSSSGTSFSGRKIKTAVRRRK // 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 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 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 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 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 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 P52361; PN Nuclear egress protein 1; GN NEC1; OS 57278; 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: P52361; 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 MAIQSTRRLRRASSLLKKSKPYNKEKTNLSLSLSLKELHSVFKLFPEYELKFLNMMKLPITGKEPIKIPFDLSLHHQHTC SQ LDLSPYANEQVSKSACVNCGTTNIPTASDAMVAYMNQISNVMQNRLYYYGFQKKVELIRMSAKQPTLFQIFYILSSIASN SQ FLPIMFENNEKLNMYVVFQTRTLHIPCECINQIMTVSSGYTVLLDILHDSIVLHVLCKTIETSNIQIDINVLQRKIEEMD SQ VPDEIGDKFEKLKHILPFI // 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 P52371; PN Envelope glycoprotein M; GN gM; OS 82831; 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: P52371; 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 MKSSKSDLFIYKTWFKLLVLYFVMFVLSATVPIAASFPGLGFPCYYNALVNYSAINLTERNVAKHLTPTLYLEEPEMFAY SQ MTFTFLVDCFAAVYYFLGALAIMLAKRHFVVSLTTLSQWIAMVGTPTLILIGMWRMWTIQLFIQTLSYKHIYLSAFVYLI SQ HFLLSFLHTQCYISRNSQLWSLKVLEQGIPPNTLLDTVVFTIKPLLANCQLFCLGLEMLVFSLSFMMAIGNSFYVLVSDI SQ VFGAINLYLALVLFWVLLTELYLVKYMTFVMGFYLGGLIGCIFLLVPLWRYEQIFVAANLRSPILINILVIFFLCTLSAL SQ VRLLRMTWFSPTKPSYEPIQLKNIKHRRVKLQSPSGPSILEEGSSDEGSEDSEEEEEL // ID P52372; PN Envelope glycoprotein M; GN gM; OS 57278; 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: P52372; 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 MALSRVDVINMRIWVLSIICACLTYVNVTVHLVAVHFPNLGFPCAYYEINDMKAINLSIRNDIRSLTPQLYLNPIQLICY SQ VVFMDICFFFILVYYIVCCVKVFSSEKTPNINQSTRDITWMGDSLSCFQFVLTMDTYQFFVTCLSFRLVTLAAFTYCLFF SQ ICFTAFTLTMITQYQSSERSFFVLKRIHPKLKGTIKYKTIIINMIELMLGFSSMVFAITICLGLGNNFYIKSSTVAFASI SQ NTFFVMSFVYSLVIELILHQYVKVQFGLHFGILFGILGLTYPILKYDSLFKTEWTVKFIVNLAVITIVCLSFIICRLIRF SQ FMRKHHNYKKLPTTVEDLDVLEEANE // ID P52373; PN Envelope glycoprotein M; GN gM; OS 69156; 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: P52373; 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: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 MAKAGVMTLSHVDRMNLRTWTMAIACCLLSFVNIVVFSVAAHFPGIGFPCYYPRIIDFDNMNLTMYNAIHHLTPQLFLDP SQ VQLIVYVIFTELIFFCVLSYYIVCWVQIYFRSEHGTQVNQSTRDINFMGDSATCFTFVLTMDTFQIFLLSLSFRLPSMVA SQ FSKCMYFMCLTAFVVTLVTHYESRERSAFALSKIHPKLQGTIRYRTAVVNLTQLILGFATMVLAMSLALGFGNSFFVKTA SQ HVVFGAMVAFAIVACVYFSIIESVLSRYMKVQFGYHIGTILGVCGAMYPIIRYEALNASSYARDINIGITVLLLLCVAFS SQ VIRTVRFLLRRNKRYRALALDNEEIRALRSDAE // ID P52449; PN Envelope glycoprotein M; GN gM; OS 36351; 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: P52449; 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 MASSRVDTINLRIWLVSIICAALSFINVTVHLIAINFPNLGFPCAYFEINDLKAVNLSANNEIYQMTHQLYINPVQIICY SQ VLIMAILFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYSIFF SQ VCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLSELMLGYSTMFLGITTCLGVGNSIYIRSITVAFSSI SQ NTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLSVVAIISIGFIICRLVRY SQ LVKKKRRYKQLLNAESSSLMDENE // 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 P52466; PN Nuclear egress protein 2; GN NEC2; OS 57278; 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: P52466; 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 MLKEKMYDELILSTCRVLKLGPADFRVTDKNLFSKNPKFPLCDILLKLDFAYSLEYLLSLWEDLTKQEARFIFKNTGGAV SQ SMSCYLHAPIKQESQNIVKECNILNVNECLSVCLNDIEAIKPSSSGVLTKCIIRRNRDAAFIVEFVAFGPESESEYIALL SQ KAIILKKKFLERQDLEKHRAARHIKKPLRLQLKSVGEMTSFRSINYMGNTKDAAVFPVTVPIFARRNNILCGFLVAALLI SQ VCYVIFKEFALSADFSAV // ID P52497; PN Carbon catabolite-derepressing protein kinase; GN SNF1; OS 5476; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. DR UNIPROT: P52497; DR UNIPROT: Q00309; DR Pfam: PF16579; DR Pfam: PF00069; DR Pfam: PF08587; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00108; DE Function: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity). {ECO:0000250}. DE Reference Proteome: No; GO GO:0031965; GO GO:0005524; GO GO:0004674; GO GO:0005975; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSEQAQPQASADQQQHQHNHHHHHHHHHHNENQSQQQVPIDPAANPANRIGRYQILKTLGEGSFGKVKLAQHLGTGQKVA SQ LKIINRKTLAKSDMQGRVEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEFAGKELFDYIVQRGKMPEDEARRFFQQII SQ AAVEYCHRHKIVHRDLKPENLLLDDQLNVKIADFGLSNIMTDGNFLKTSCGSPNYMPAPEVISGKLYAGPEVDVWSAGVI SQ LYVMLCGRLPFDDEFIPALFKKISNGVYTLPNYLSAGAKHLLTRMLVVNPLNRITIHEIMEDDWFKQDMPDYLLPPDLSK SQ NKNSKIDVDEDVIRALSVTMGYDRDCKIVNVIEKANKQVAAGNSSSQQSKSSNEILDAYLLMKENHALVKDLKKSKSENI SQ ESFLSQSPPPSPFPNRGSTSSAPGVQQSLTYQTLATVPDLSTLPNSTIAILPTSLPSIHRAYMAETKQNGDPSQQHAPPP SQ TKKSKTRWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPTEEELWTIRVRWKYDTSAQFECGSAPNLMKMQIQLFQLEPN SQ NYLVSFKFSGWESAHGNAGTDSPQSHRQQDLDEVGSFSAYPFLHLATRLIMELAVNSQSG // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 P55735; PN Protein SEC13 homolog; GN SEC13; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein {ECO:0000269|PubMed:8972206}; Cytoplasmic side {ECO:0000269|PubMed:8972206}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein {ECO:0000269|PubMed:8972206}; Cytoplasmic side {ECO:0000269|PubMed:8972206}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:14517296, ECO:0000269|PubMed:18160040}. Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000269|PubMed:14517296}. DR UNIPROT: P55735; DR UNIPROT: A8MV37; DR UNIPROT: B4DXJ1; DR UNIPROT: Q5BJF0; DR UNIPROT: Q9BRM6; DR UNIPROT: Q9BUG7; DR PDB: 3BG0; DR PDB: 3BG1; DR PDB: 5A9Q; DR Pfam: PF00400; DR PROSITE: PS50082; DR PROSITE: PS50294; DR OMIM: 600152; DR DisGeNET: 6396; DE Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (PubMed:8972206). Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q9D1M0, ECO:0000269|PubMed:8972206}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1 (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}. DE Reference Proteome: Yes; DE Interaction: O14976; IntAct: EBI-714707,EBI-1046596; Score: 0.35 DE Interaction: O15027; IntAct: EBI-357515,EBI-1046596; Score: 0.35 DE Interaction: O15504; IntAct: EBI-2515057,EBI-1046596; Score: 0.37 DE Interaction: P00533; IntAct: EBI-297353,EBI-1046596; Score: 0.35 DE Interaction: P02545; IntAct: EBI-351935,EBI-1046596; Score: 0.35 DE Interaction: P35729; IntAct: EBI-11713,EBI-1046596; Score: 0.40 DE Interaction: P37198; IntAct: EBI-347978,EBI-1046596; Score: 0.49 DE Interaction: P49687; IntAct: EBI-1046596,EBI-11730; Score: 0.70 DE Interaction: Self; IntAct: EBI-1046596,EBI-1046596; Score: 0.63 DE Interaction: O94979; IntAct: EBI-1046596,EBI-1767898; Score: 0.44 DE Interaction: Q15436; IntAct: EBI-81088,EBI-1046596; Score: 0.51 DE Interaction: Q5T011; IntAct: EBI-10749411,EBI-1046596; Score: 0.35 DE Interaction: Q9NXC5; IntAct: EBI-2515122,EBI-1046596; Score: 0.64 DE Interaction: Q96S15; IntAct: EBI-746424,EBI-1046596; Score: 0.53 DE Interaction: Q6PJI9; IntAct: EBI-2515073,EBI-1046596; Score: 0.53 DE Interaction: P03372; IntAct: EBI-78473,EBI-1046596; Score: 0.35 DE Interaction: Q12824; IntAct: EBI-358419,EBI-1046596; Score: 0.46 DE Interaction: Q9Y2H1; IntAct: EBI-991501,EBI-1046596; Score: 0.46 DE Interaction: Q9UPY3; IntAct: EBI-395506,EBI-1046596; Score: 0.35 DE Interaction: O00463; IntAct: EBI-1046596,EBI-523498; Score: 0.56 DE Interaction: Q96JE7-2; IntAct: EBI-10215083,EBI-1046596; Score: 0.67 DE Interaction: P04792; IntAct: EBI-1046596,EBI-352682; Score: 0.37 DE Interaction: Q8WYP5; IntAct: EBI-396018,EBI-1046596; Score: 0.32 DE Interaction: Q9BW27; IntAct: EBI-716392,EBI-1046596; Score: 0.56 DE Interaction: P43351; IntAct: EBI-706448,EBI-1046596; Score: 0.35 DE Interaction: Q8BH74; IntAct: EBI-2554056,EBI-1046596; Score: 0.56 DE Interaction: Q6PFD9; IntAct: EBI-646104,EBI-1046596; Score: 0.56 DE Interaction: P56749; IntAct: EBI-1046596,EBI-723005; Score: 0.37 DE Interaction: Q9ERU9; IntAct: EBI-643756,EBI-1046596; Score: 0.35 DE Interaction: P57740; IntAct: EBI-295687,EBI-1046596; Score: 0.53 DE Interaction: Q9BPU9; IntAct: EBI-6958971,EBI-1046596; Score: 0.35 DE Interaction: P63280; IntAct: EBI-80180,EBI-1046596; Score: 0.35 DE Interaction: P21333; IntAct: EBI-350432,EBI-1046596; Score: 0.35 DE Interaction: Q91X51; IntAct: EBI-2553222,EBI-1046596; Score: 0.35 DE Interaction: P56377; IntAct: EBI-1054374,EBI-1046596; Score: 0.35 DE Interaction: Q9Z1Z0; IntAct: EBI-7597484,EBI-1046596; Score: 0.35 DE Interaction: Q96EE3; IntAct: EBI-922818,EBI-1046596; Score: 0.62 DE Interaction: P58043; IntAct: EBI-9638431,EBI-1046596; Score: 0.35 DE Interaction: Q92731; IntAct: EBI-78505,EBI-1046596; Score: 0.35 DE Interaction: G3X972; IntAct: EBI-11079353,EBI-1046596; Score: 0.35 DE Interaction: P09497; IntAct: EBI-726598,EBI-1046596; Score: 0.35 DE Interaction: Q9NYZ3; IntAct: EBI-2511327,EBI-1046596; Score: 0.35 DE Interaction: Q13492; IntAct: EBI-2803688,EBI-1046596; Score: 0.35 DE Interaction: Q00610; IntAct: EBI-354967,EBI-1046596; Score: 0.35 DE Interaction: Q9CWZ3; IntAct: EBI-1993805,EBI-1046596; Score: 0.35 DE Interaction: O43493; IntAct: EBI-1752146,EBI-1046596; Score: 0.35 DE Interaction: O15155; IntAct: EBI-749204,EBI-1046596; Score: 0.35 DE Interaction: P49336; IntAct: EBI-394377,EBI-1046596; Score: 0.35 DE Interaction: Q15075; IntAct: EBI-298113,EBI-1046596; Score: 0.35 DE Interaction: Q8NFH3; IntAct: EBI-1059321,EBI-1046596; Score: 0.35 DE Interaction: O94979-2; IntAct: EBI-17482477,EBI-1046596; Score: 0.35 DE Interaction: Q92734; IntAct: EBI-357061,EBI-1046596; Score: 0.35 DE Interaction: Q13618; IntAct: EBI-456129,EBI-1046596; Score: 0.35 DE Interaction: P48729; IntAct: EBI-1383726,EBI-1046596; Score: 0.35 DE Interaction: P49674; IntAct: EBI-749343,EBI-1046596; Score: 0.35 DE Interaction: A0A0F7RLQ7; IntAct: EBI-2814703,EBI-1046596; Score: 0.37 DE Interaction: A0A0H2W3Z6; IntAct: EBI-2841276,EBI-1046596; Score: 0.37 DE Interaction: P01889; IntAct: EBI-1046596,EBI-1046513; Score: 0.40 DE Interaction: P56537; IntAct: EBI-1046596,EBI-372243; Score: 0.40 DE Interaction: P78396; IntAct: EBI-1046596,EBI-375065; Score: 0.40 DE Interaction: P23508; IntAct: EBI-1046596,EBI-307531; Score: 0.40 DE Interaction: P62330; IntAct: EBI-638181,EBI-1046596; Score: 0.40 DE Interaction: Q96JE7; IntAct: EBI-749897,EBI-1046596; Score: 0.37 DE Interaction: Q8IZD9; IntAct: EBI-1752361,EBI-1046596; Score: 0.35 DE Interaction: Q8NFH4; IntAct: EBI-2563158,EBI-1046596; Score: 0.55 DE Interaction: Q96HA1; IntAct: EBI-739990,EBI-1046596; Score: 0.37 DE Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-1046596; Score: 0.35 DE Interaction: Q6IQ23; IntAct: EBI-2125301,EBI-1046596; Score: 0.35 DE Interaction: Q9BW85; IntAct: EBI-1046596,EBI-10300345; Score: 0.35 DE Interaction: Q96EA4; IntAct: EBI-1046596,EBI-715381; Score: 0.35 DE Interaction: Q96CP2; IntAct: EBI-1046596,EBI-9394506; Score: 0.35 DE Interaction: Q96BP3; IntAct: EBI-1046596,EBI-2827139; Score: 0.35 DE Interaction: Q8WUM0; IntAct: EBI-1046596,EBI-295695; Score: 0.35 DE Interaction: Q8NAV1; IntAct: EBI-1046596,EBI-715374; Score: 0.35 DE Interaction: Q12769; IntAct: EBI-1046596,EBI-295715; Score: 0.35 DE Interaction: Q03154; IntAct: EBI-1046596,EBI-742064; Score: 0.35 DE Interaction: P58004; IntAct: EBI-1046596,EBI-3939642; Score: 0.35 DE Interaction: P52948-5; IntAct: EBI-1046596,EBI-5280407; Score: 0.35 DE Interaction: P11274; IntAct: EBI-1046596,EBI-712838; Score: 0.35 DE Interaction: O15400-2; IntAct: EBI-1046596,EBI-11042829; Score: 0.35 DE Interaction: O15062; IntAct: EBI-1046596,EBI-722671; Score: 0.35 DE Interaction: O15027-2; IntAct: EBI-1046596,EBI-11079342; Score: 0.35 DE Interaction: Q9NYJ8; IntAct: EBI-1046596,EBI-358708; Score: 0.40 GO GO:0030127; GO GO:0005829; GO GO:0005789; GO GO:0012507; GO GO:0070062; GO GO:0061700; GO GO:0000139; GO GO:0043657; GO GO:0043231; GO GO:0005765; GO GO:0005635; GO GO:0031080; GO GO:0005654; GO GO:0042802; GO GO:0005198; GO GO:0019886; GO GO:0002474; GO GO:0048208; GO GO:0090114; GO GO:0090110; GO GO:0006886; GO GO:0075733; GO GO:0006406; GO GO:0032008; GO GO:1904263; GO GO:0032527; GO GO:1900034; GO GO:0060964; GO GO:0006110; GO GO:0006409; GO GO:0016032; GO GO:0019083; TP Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8972206}; SQ MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYD SQ RKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAP SQ AVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV SQ FIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQN SQ EQ // ID P55820; PN Synaptosomal-associated protein 25; GN SNAP25; OS 9986; 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: P55820; 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:0031201; GO GO:0045202; GO GO:0017075; GO GO:0005249; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879}; SQ MLQLVEESSKDAGIRXLVMLDEQGEQLERVVDEREQMAISGGFIRIMEKMLGSG // 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 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 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 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 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 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 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 P60321; PN Nanos homolog 2; GN NANOS2; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:19168545}. Cytoplasm, P-body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19168545}. Note=Localizes at P-bodies during gonocyte development (By similarity). More abundant in perinuclear region of the cytoplasm of the germ cells of the adult testis. {ECO:0000250}. DR UNIPROT: P60321; DR UNIPROT: Q17R30; DR UNIPROT: Q4G0P8; DR Pfam: PF05741; DR PROSITE: PS51522; DR OMIM: 608228; DR DisGeNET: 339345; DE Function: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; DE Interaction: O95273; IntAct: EBI-10216569,EBI-748961; Score: 0.67 DE Interaction: P43365; IntAct: EBI-749530,EBI-10216569; Score: 0.78 DE Interaction: Q9UIV1; IntAct: EBI-10216569,EBI-2105113; Score: 0.35 DE Interaction: Q9C0C2; IntAct: EBI-10216569,EBI-2104458; Score: 0.35 DE Interaction: Q9UKZ1; IntAct: EBI-10216569,EBI-2562014; Score: 0.35 DE Interaction: Q9UHA7; IntAct: EBI-10216569,EBI-13385196; Score: 0.35 DE Interaction: Q9UFF9; IntAct: EBI-10216569,EBI-742299; Score: 0.35 DE Interaction: Q9NZN8-4; IntAct: EBI-10216569,EBI-21546893; Score: 0.35 DE Interaction: Q9HC44; IntAct: EBI-10216569,EBI-746674; Score: 0.35 DE Interaction: Q9H9A5-2; IntAct: EBI-10216569,EBI-21502930; Score: 0.35 DE Interaction: Q9H2K2; IntAct: EBI-10216569,EBI-4398527; Score: 0.35 DE Interaction: Q96LI5; IntAct: EBI-10216569,EBI-1046635; Score: 0.35 DE Interaction: Q92600; IntAct: EBI-10216569,EBI-357079; Score: 0.35 DE Interaction: Q8N4C8-2; IntAct: EBI-10216569,EBI-10988882; Score: 0.35 DE Interaction: Q14201-2; IntAct: EBI-10216569,EBI-21547457; Score: 0.35 DE Interaction: Q14192; IntAct: EBI-10216569,EBI-701903; Score: 0.35 DE Interaction: Q14106; IntAct: EBI-10216569,EBI-2562000; Score: 0.35 DE Interaction: O95819-2; IntAct: EBI-10216569,EBI-21536929; Score: 0.35 DE Interaction: O75175; IntAct: EBI-10216569,EBI-743073; Score: 0.35 DE Interaction: D6R9H6; IntAct: EBI-10216569,EBI-21546884; Score: 0.35 DE Interaction: A5YKK6-2; IntAct: EBI-10216569,EBI-16057352; Score: 0.35 DE Interaction: P60903; IntAct: EBI-717048,EBI-10216569; Score: 0.56 GO GO:0005737; GO GO:0005634; GO GO:0000932; GO GO:0048471; GO GO:0003729; GO GO:0008270; GO GO:0030154; GO GO:0030718; GO GO:0006402; GO GO:0007275; GO GO:0045835; GO GO:0017148; GO GO:1900153; GO GO:0007283; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MQLPPFDMWKDYFNLSQVVWALIASRGQRLETQEIEEPSPGPPLGQDQGLGAPGANGGLGTLCNFCKHNGESRHVYSSHQ SQ LKTPDGVVVCPILRHYVCPVCGATGDQAHTLKYCPLNGGQQSLYRRSGRNSAGRRVKR // 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 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 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 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 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 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 P62833; PN Ras-related protein Rap-1A; GN RAP1A; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cell membrane; Lipid-anchor. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions. Colocalized with RAPGEF2 in the perinuclear region (By similarity). {ECO:0000250}. DR UNIPROT: P62833; DR UNIPROT: A4IFG1; DR UNIPROT: P10113; DR Pfam: PF00071; DR PROSITE: PS51421; DE Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)- induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0030054; GO GO:0005737; GO GO:0005769; GO GO:0098978; GO GO:0032045; GO GO:0005770; GO GO:0043005; GO GO:0048471; GO GO:0005886; GO GO:0019003; GO GO:0005525; GO GO:0003924; GO GO:0044877; GO GO:0017034; GO GO:0071320; GO GO:1990090; GO GO:0061028; GO GO:2000301; GO GO:0038180; GO GO:0070374; GO GO:0043547; GO GO:0010976; GO GO:0045860; GO GO:2001214; GO GO:0072659; GO GO:0032486; GO GO:1901888; GO GO:0098696; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFAL SQ VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYD SQ LVRQINRKTPVEKKKPKKKSCLLL // 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 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 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 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 P70600; PN Protein-tyrosine kinase 2-beta; GN Ptk2b; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000269|PubMed:9645946}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:9645946}; Peripheral membrane protein {ECO:0000269|PubMed:9645946}; Cytoplasmic side {ECO:0000269|PubMed:9645946}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery. Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts (By similarity). {ECO:0000250}. [Isoform 2]: Cell junction, focal adhesion. Note=Localizes to focal adhesions, but not isoform 1 and isoform 3. DR UNIPROT: P70600; DR UNIPROT: O88489; DR UNIPROT: Q3T1H4; DR UNIPROT: Q63201; DR Pfam: PF00373; DR Pfam: PF18038; DR Pfam: PF03623; DR Pfam: PF07714; DR PROSITE: PS50057; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00109; DE Function: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. 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 of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:7544443}. DE Reference Proteome: Yes; DE Interaction: Q9WUD9; IntAct: EBI-8651342,EBI-7784541; Score: 0.40 GO GO:0097440; GO GO:0030424; GO GO:0005623; GO GO:0044297; GO GO:0005938; GO GO:0042995; GO GO:0005856; GO GO:0030425; GO GO:0043197; GO GO:0031234; GO GO:0005925; GO GO:0098978; GO GO:0030426; GO GO:0030027; GO GO:0045121; GO GO:0043025; GO GO:0017146; GO GO:0005634; GO GO:0048471; GO GO:0098794; GO GO:0014069; GO GO:0043423; GO GO:0005524; GO GO:0004683; GO GO:0019899; GO GO:0004715; GO GO:0008022; GO GO:0004672; GO GO:0044877; GO GO:0031625; GO GO:0007015; GO GO:0090630; GO GO:0042976; GO GO:0002250; GO GO:0001525; GO GO:0043534; GO GO:0045453; GO GO:0007155; GO GO:0030154; GO GO:0007166; GO GO:0006968; GO GO:0071498; GO GO:0071300; GO GO:0070098; GO GO:0086100; GO GO:0007173; GO GO:0048041; GO GO:0014009; GO GO:0007229; GO GO:0035235; GO GO:0060292; GO GO:0060291; GO GO:0000165; GO GO:0002315; GO GO:0043066; GO GO:0030502; GO GO:0008285; GO GO:0010656; GO GO:0045638; GO GO:0043524; GO GO:0030279; GO GO:0043267; GO GO:0031175; GO GO:0001556; GO GO:0038083; GO GO:0018108; GO GO:0030838; GO GO:0045766; GO GO:2000538; GO GO:0030307; GO GO:0030335; GO GO:0008284; GO GO:0001954; GO GO:0032270; GO GO:0007204; GO GO:2000573; GO GO:0010595; GO GO:0070374; GO GO:2000463; GO GO:0046330; GO GO:0043507; GO GO:0010976; GO GO:0045429; GO GO:0051000; GO GO:0050731; GO GO:0043552; GO GO:0045860; GO GO:2000379; GO GO:0051968; GO GO:0045727; GO GO:2000060; GO GO:0006468; GO GO:2000249; GO GO:0050848; GO GO:0030155; GO GO:0008360; GO GO:0010752; GO GO:2000114; GO GO:0032960; GO GO:0010758; GO GO:0045428; GO GO:2000310; GO GO:0051279; GO GO:2000058; GO GO:0051592; GO GO:0051591; GO GO:0042220; GO GO:0042493; GO GO:0045471; GO GO:0009749; GO GO:0009725; GO GO:0042542; GO GO:0001666; GO GO:0035902; GO GO:0010226; GO GO:0009612; GO GO:0010243; GO GO:0006970; GO GO:0000302; GO GO:0007172; GO GO:0002040; GO GO:0043149; GO GO:0033209; GO GO:0048010; TP Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9645946}; SQ MSGVSEPLSRVKVGTLRPPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRI SQ GPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRN SQ DYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYAS SQ LREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVL SQ QLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIIHAKKDGEKRNSLPQIPTLNLESRRSHLSESCSIESD SQ IYAEIPDETLRRPGGPQYGVAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKN SQ LDHPHIVKLIGIIEEEPTWIVMELYPYGELGHYLERNKNSLKVPTLVLYALQICKAMAYLESINCVHRDIAVRNILVASP SQ ECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEK SQ GDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMERDIAIEQERNARYRPPKILEPTAFQEPPPKPSRP SQ KYKHPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAE SQ KIKMRQVLDRQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLV SQ YHNVMTLVEAVLELKNKLSQLPPEEYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMRLA SQ QQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE // 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 P83722; PN Nuclear pore complex protein Nup160; GN nup160; OS 8355; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11684705}. Cytoplasm {ECO:0000269|PubMed:11684705}. DR UNIPROT: P83722; DE Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:11684705). Involved in poly(A)+ RNA transport (PubMed:11684705). {ECO:0000269|PubMed:11684705, ECO:0000303|PubMed:11684705}. DE Reference Proteome: No; GO GO:0005737; GO GO:0031080; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ PVNIYVIMADQGPAHLPVSLAVHTDMLEYVPVSKDEYFQKLKKA // 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 P86172; PN NmrA-like family domain-containing protein 1; GN Nmral1; OS 10116; 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: P86172; 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; GO GO:0005634; GO GO:0048471; GO GO:0042802; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ KLVVVFGATGAQGGSVARTLLEDGTFRVRVVTRNPEQKLLADLAKRLGLHYVVYSGLENIKKLAAGHFDGKGEVEEYFRK SQ PEEYIGQNVGLSTCRTTPEEYEKLGFQGAQDLANMFRFYALKPDRNIDLTLRAQTLDQWLEQHKGDFAHL // ID P87170; PN CTP-dependent diacylglycerol kinase 1; GN ptp4; OS 284812; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12382}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12382}. Nucleus membrane {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12382}. DR UNIPROT: P87170; DE Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of ned1. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in pre-tRNA splicing. {ECO:0000250|UniProtKB:Q12382, ECO:0000269|PubMed:11955632}. DE Reference Proteome: Yes; GO GO:0005783; 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 MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRE SQ SEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYW SQ GLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM // 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 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 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 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 P91607; PN Period circadian protein; GN per; OS 46840; 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: P91607; 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 SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVEPSYVSSAREDAHRTLSPVQGFEGSGGTGSSGNFTTGSNLHM SQ SSVTNTSNAGTGTSGTGNSGGGGGGGGGGGPGNGAVTPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANDTL SQ KMVEYSGPGPGPGHGHGIKRGGSHSWEGEANKPKQLLTLNTGGMPPLLDIHTSSASLSKCQASGAGGGGSGSVGGTGNIG SQ SGGSNAQPSTNQYAQSGLSCTQNINLWPPFSVGITTPTSVLSTHTAVAQSSFSTQHNLFPTFYYIPASIAASSPSGTSPN SQ PRPHKHTLVHKSAEQPSTSQAAAATMPLQYMTGLMYPHPSLFYTHPAAAAATAMV // 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 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 Q01017; PN Envelope glycoprotein M; GN gM; OS 10383; 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: Q01017; 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 MMKASRSDTFMLRTWIQLLVLFVIMFIMSAILPIAASVEGLGFPCYFPNLVDYSLLNLTLRNAAKHLTPTLFLEAPELFV SQ YITWSVLVDLASAIYYVVGALAILQARKTHLTSMITLQTWINLVGSHTMLFIGIARMWTLQLFIHVLSYKHVMLAAFIYF SQ LHFCLSYMHTLSLVSRNSPKWSVLLMEQHIPKQSLLSTILDYGKPLCVNMYLSLLALEMLVFSLGFMMAIGNSFYILVSD SQ TVLASINLYFVLTTFWYMMTEMFLQDYLKLQFGFYLGVFSGSLILLLPVLRYEAVFVSANLHKTVAVNIAMIPAMCVIAM SQ MFRLFRYSQQVRKPENSYTPLPKRFKKRRQKQDQQLIMVETSDEEL // ID Q01041; PN Nuclear egress protein 1; GN NEC1; OS 10383; 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: Q01041; 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 MSSRSVKSRKSTKSRRHHPYVKLTDKMFFSAISSKKELGTDFLREMDAPICTSKTILLPLDLNSISPGRCIYLSPFGHSS SQ NMEFQCEKCTESKNKGSGDVSQNHDLYSVTLVFYKNVDKVVKHKAFYLSLLSHSMENLKKSFTQPELLYAYVVVKEAGHN SQ VFPIFFEKDDCLSICLTFKCQTLHIGESCLRMLMDNLPNYKISIDYIKDVYAMTFTQCFAIQRNISIAEDTICESVSTLD SQ CTDELREEIVKGINALQIKDI // ID Q01045; PN Nuclear egress protein 2; GN NEC2; OS 10383; 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: Q01045; 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 MNSTRLVYELCDIVNLYLCQPGVQIDVDRCASGPHVFTKGGTEAICTVKLSHGLVYNIEFVYKFWAHKLESVKYPFSPCF SQ IISNNGLATTLKCFLSRPRNVNHFGHVLNIDSDVYLTKNTSVILSQDDFVKFKTNLVFSKDLDVFHSMVVFRTYLIEHRQ SQ ALQFLVVKPRSSKRVNSILSSVAKTASQNFILDPPRRSEETRVCIKPWTLSKKNIWTIILSLVAVVAIILKWREL // 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 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 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 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 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 Q03252; PN Lamin-B2; GN LMNB2; OS 9606; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. DR UNIPROT: Q03252; DR UNIPROT: O75292; DR UNIPROT: Q14734; DR UNIPROT: Q96DF6; DR PDB: 2LLL; DR PDB: 5BNW; DR Pfam: PF00038; DR Pfam: PF00932; DR PROSITE: PS00226; DR PROSITE: PS51842; DR PROSITE: PS51841; DR OMIM: 150341; DR OMIM: 608709; DR OMIM: 616540; DR DisGeNET: 84823; 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 Disease: Partial acquired lipodystrophy (APLD) [MIM:608709]: A rare childhood disease characterized by loss of subcutaneous fat from the face and trunk. Fat deposition on the pelvic girdle and lower limbs is normal or excessive. Most frequently, onset between 5 and 15 years of age. Most affected subjects are females and some show no other abnormality, but many develop glomerulonephritis, diabetes mellitus, hyperlipidemia, and complement deficiency. Mental retardation in some cases. APLD is a sporadic disorder of unknown etiology. {ECO:0000269|PubMed:16826530, ECO:0000269|PubMed:22768673}. Note=The disease is caused by mutations affecting the gene represented in this entry. Epilepsy, progressive myoclonic 9 (EPM9) [MIM:616540]: An autosomal recessive form of progressive myoclonic epilepsy, a rare disease initially responsive to antiepileptic drugs which over time becomes refractory and can be associated with cognitive decline. EPM9 features include myoclonus, tonic-clonic seizures, ataxia, and delayed psychomotor development. {ECO:0000269|PubMed:25954030}. Note=The disease may be caused by mutations affecting the gene represented in this entry. DE Reference Proteome: Yes; DE Interaction: O75604; IntAct: EBI-2830427,EBI-743272; Score: 0.56 DE Interaction: P02545; IntAct: EBI-351935,EBI-2830427; Score: 0.62 DE Interaction: P20700; IntAct: EBI-968218,EBI-2830427; Score: 0.75 DE Interaction: P48678; IntAct: EBI-299212,EBI-2830427; Score: 0.35 DE Interaction: Self; IntAct: EBI-2830427,EBI-2830427; Score: 0.56 DE Interaction: Q5S007; IntAct: EBI-5323863,EBI-2830427; Score: 0.56 DE Interaction: Q7KZN9; IntAct: EBI-3248549,EBI-2830427; Score: 0.35 DE Interaction: P36957; IntAct: EBI-351007,EBI-2830427; Score: 0.35 DE Interaction: P00441; IntAct: EBI-990792,EBI-2830427; Score: 0.35 DE Interaction: P31040; IntAct: EBI-1057265,EBI-2830427; Score: 0.35 DE Interaction: Q8NDX5; IntAct: EBI-1223801,EBI-2830427; Score: 0.35 DE Interaction: Q8WVC0; IntAct: EBI-932432,EBI-2830427; Score: 0.35 DE Interaction: P23258; IntAct: EBI-302589,EBI-2830427; Score: 0.35 DE Interaction: Q7LBC6; IntAct: EBI-2511832,EBI-2830427; Score: 0.35 DE Interaction: P46013; IntAct: EBI-876367,EBI-2830427; Score: 0.35 DE Interaction: Q9UBB9; IntAct: EBI-1105213,EBI-2830427; Score: 0.56 DE Interaction: Q5JST6; IntAct: EBI-2349927,EBI-2830427; Score: 0.56 DE Interaction: P55081; IntAct: EBI-2830427,EBI-1048159; Score: 0.56 DE Interaction: Q4G0R1; IntAct: EBI-14066006,EBI-2830427; Score: 0.56 DE Interaction: O14753; IntAct: EBI-2830427,EBI-3917713; Score: 0.56 DE Interaction: Q81VE0; IntAct: EBI-2830427,EBI-2830418; Score: 0.37 DE Interaction: Q8ZIY9; IntAct: EBI-2846835,EBI-2830427; Score: 0.37 DE Interaction: Q9H1R3; IntAct: EBI-356910,EBI-2830427; Score: 0.35 DE Interaction: Q9H5J0; IntAct: EBI-7229473,EBI-2830427; Score: 0.40 DE Interaction: Q96P66; IntAct: EBI-2830427,EBI-17935713; Score: 0.40 DE Interaction: A8K8P3; IntAct: EBI-2830427,EBI-743371; Score: 0.40 DE Interaction: Q8NF50-3; IntAct: EBI-25409271,EBI-2830427; Score: 0.35 DE Interaction: A6NC98; IntAct: EBI-347573,EBI-2830427; Score: 0.56 DE Interaction: Q15911-2; IntAct: EBI-2830427,EBI-10237226; Score: 0.56 DE Interaction: P35219; IntAct: EBI-2830427,EBI-718700; Score: 0.56 DE Interaction: P14373; IntAct: EBI-719493,EBI-2830427; Score: 0.56 DE Interaction: Q08379; IntAct: EBI-618309,EBI-2830427; Score: 0.56 DE Interaction: Q96HB5; IntAct: EBI-744556,EBI-2830427; Score: 0.56 DE Interaction: Q9Y3C0; IntAct: EBI-2830427,EBI-712969; Score: 0.56 DE Interaction: Q16543; IntAct: EBI-2830427,EBI-295634; Score: 0.56 DE Interaction: Q9NVV9; IntAct: EBI-741515,EBI-2830427; Score: 0.56 DE Interaction: Q9Y250; IntAct: EBI-1216080,EBI-2830427; Score: 0.56 DE Interaction: P78424; IntAct: EBI-12029004,EBI-2830427; Score: 0.56 DE Interaction: Q53FD0-2; IntAct: EBI-14104088,EBI-2830427; Score: 0.56 DE Interaction: Q05BL1; IntAct: EBI-11952721,EBI-2830427; Score: 0.56 DE Interaction: Q9UJV3-2; IntAct: EBI-10172526,EBI-2830427; Score: 0.56 DE Interaction: Q96KQ4; IntAct: EBI-1105153,EBI-2830427; Score: 0.56 DE Interaction: Q3SY00; IntAct: EBI-2830427,EBI-10241197; Score: 0.56 DE Interaction: Q9Y2J4; IntAct: EBI-746752,EBI-2830427; Score: 0.56 DE Interaction: A2BDD9; IntAct: EBI-17286414,EBI-2830427; Score: 0.56 DE Interaction: P33993; IntAct: EBI-355924,EBI-2830427; Score: 0.35 DE Interaction: P07954; IntAct: EBI-1050358,EBI-2830427; Score: 0.56 DE Interaction: P49356; IntAct: EBI-602349,EBI-2830427; Score: 0.35 GO GO:0005638; GO GO:0005637; GO GO:0031965; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MSPPSPGRRREQRRPRAAATMATPLPGRAGGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISE SQ KEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSE SQ VELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERR SQ LVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQ SQ LSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEE SQ RLKLSPSPSSRVTVSRATSSSSGSLSATGRLGRSKRKRLEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVSIEEID SQ LEGKFVQLKNNSDKDQSLGNWRIKRQVLEGEEIAYKFTPKYILRAGQMVTVWAAGAGVAHSPPSTLVWKGQSSWGTGESF SQ RTVLVNADGEEVAMRTVKKSSVMRENENGEEEEEEAEFGEEDLFHQQGDPRTTSRGCYVM // 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 Q03296; PN Period circadian protein; GN per; OS 7257; 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: Q03296; 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 EGSGGSGSSGNFTTGSNIRMSSVTNTSNAGTGTGTGTGTGTATGTGTATGTGTSAGGTSAGGNASGNSGNPPPAFAITLT SQ ETLLNK // ID Q03297; PN Period circadian protein; GN per; OS 7260; 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: Q03297; DR UNIPROT: O18421; DR UNIPROT: O18422; DR UNIPROT: P91721; DR UNIPROT: P91722; 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: No; GO GO:0005634; GO GO:0048471; GO GO:0006355; GO GO:0048511; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ NKDKSRKKKKPKCIALATATAVSLEGTRESPLPASGSCEKVLQELQDTQQLGEPLVVTETQLSEQLLETEQNEDQNKSEQ SQ LAQFPLPTPIVTTLSPGIGPGHDCVGGASGGAVAGGCLVVGAGTDKTSELIPGKLESAGTKPSQERPKEESFCCVISMHD SQ GIVLYTTPSISDVLGFPRDMWLGRSFVDFVHHKDRATFASQITTGIPIAESRGCMPKDARSTFCVMLRRYRGLNSGGFGV SQ IGRAVNYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAA SQ VSALGYLPQDLIGRSIMDFYHHEDLSVMKDTYETVMKKGQTAGASFCSKPYRFLIQNGCFVLLETEWTSFVNPWSRKLEF SQ VVGHHRVFQGPKLCNVFETSVSAKPKISEEAQNRNARIKEDIVKLLAETVSRPSDTVKQEVSRRCQALANFMETLMDEIT SQ RADLKLDLPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYV SQ SSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLHMSSVTNTSNAGTGTSGTGNSGDGGGGGGADGTGSGAAPPVTLT SQ ESLLNKHNDEMEKFMLKKHRESRGRSGDKNKKSANEAMKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTGGG SQ GGGGGGGGGGGGGGLPLFLDVTHTSSSSQNKGPTGVAAGGAGGGVGGGGGSCSGLGGNGNVGSGNGNNSQPSTNQYTQSG SQ LPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFPTFYYIPASIAASSPSSTNTNPNRPHKHAHVHSSSEKP SQ STSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMVYQPVPFAGVANPMQLPEQASKNVYTTQPVMVAPPTATNKTQ SQ GAFHSITPAPPQRPSSQATSVKAETGSNVAPSDTSKKEVPDSPITPTMGDFTLDQPCNNNATTLKKYTDSNGNSDDMDGS SQ SFSSFYSSFIKTTDGSESPPENDKDAKHRKLKSLDQSDNKIVEHPEEDQTQHG // ID Q03427; PN Lamin-C; GN LamC; OS 7227; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0180; SL Comments: Nucleus {ECO:0000269|PubMed:7593280}. Nucleus lamina {ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:27402967}. Note=Nuclear periphery (PubMed:7593280). In premeiotic nuclei of primary spermatocytes, localization to the nuclear lamina depends on type-B lamin Lam. In spermatocytes, temporarily depleted between anaphase I and telophase I, and anaphase II and telophase II. {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280}. DR UNIPROT: Q03427; DR UNIPROT: Q24374; DR UNIPROT: Q9V729; 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 (By similarity). In spermatocytes, regulates cytokinesis during meiosis (PubMed:27402967). {ECO:0000250|UniProtKB:P08928, ECO:0000269|PubMed:27402967}. DE Reference Proteome: Yes; DE Interaction: O76417; IntAct: EBI-498761,EBI-498159; Score: 0.37 DE Interaction: Q8T0N1; IntAct: EBI-498761,EBI-499087; Score: 0.37 DE Interaction: Q9VJ29; IntAct: EBI-498761,EBI-153860; Score: 0.37 GO GO:0005638; GO GO:0016020; GO GO:0005635; GO GO:0005652; GO GO:0034399; GO GO:0070732; GO GO:0005200; GO GO:0006325; GO GO:0006342; GO GO:0007112; GO GO:0060415; GO GO:0031081; GO GO:0030833; GO GO:0035989; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSARRVTLNTRVSRASTSTPVGGASTSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNL SQ AQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVN SQ GKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSRRQIE SQ ISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAK SQ LQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEER SQ RLNIESPGRPTTDSGISSNGSHLTASASSRSGRVTPSGRRSATPGISGSSAVKRRRTVIDESEDRTLSEYSVNAAAKGDL SQ EIIEADVEGRFIKLHNKGTEEINLTGWQLTRIAGDEELAFKFSRGSKVLGGASVTIWSVDAGTAHDPPNNLVMKKKWPVA SQ NSMRSVLANADKEDVASYDRVRANVSSHTSRHRSSGTPSTGFTLGSGAGSTGVRSLFSLLF // 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 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 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 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 Q03963; PN Interferon-induced, double-stranded RNA-activated protein kinase; GN Eif2ak2; OS 10090; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q03963; DR UNIPROT: Q61742; DR UNIPROT: Q62026; DR PDB: 1X48; DR PDB: 1X49; DR Pfam: PF00035; DR Pfam: PF00069; DR PROSITE: PS50137; DR PROSITE: PS00107; DR PROSITE: PS50011; DR PROSITE: PS00108; 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 west nile virus (WNV), sindbis virus (SV), foot-and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic choriomeningitis virus (LCMV). 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 and IRS1. 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. Regulates proliferation, differentiation and survival of hematopoietic stem/progenitor cells, induction of cytokines and chemokines and plays a role in cortex-dependent memory consolidation. {ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19264662, ECO:0000269|PubMed:20038207, ECO:0000269|PubMed:20478537, ECO:0000269|PubMed:20585572, ECO:0000269|PubMed:20631127, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21994357, ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:23392680, ECO:0000269|PubMed:23401008, ECO:0000269|PubMed:23403623}. DE Reference Proteome: Yes; DE Interaction: P35569; IntAct: EBI-2603444,EBI-400825; Score: 0.40 DE Interaction: P35570; IntAct: EBI-520230,EBI-2603444; Score: 0.44 GO GO:0005737; GO GO:0005829; GO GO:0005634; GO GO:0048471; GO GO:0005524; GO GO:0003725; GO GO:0004694; GO GO:0042802; GO GO:0004715; GO GO:0004672; GO GO:0000186; GO GO:0034198; GO GO:0051607; GO GO:0030968; GO GO:0045087; GO GO:0043066; GO GO:0033689; GO GO:0017148; GO GO:0045071; GO GO:0043065; 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:0032496; GO GO:0009636; GO GO:0009615; GO GO:0033197; GO GO:0006412; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKV SQ DCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKL SQ LKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNS SQ DFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYK SQ TRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATA SQ LENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLK SQ KLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC // 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 Q04537; PN Period circadian protein; GN per; OS 7274; 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: Q04537; 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 EGSGGSGSSGHFTTGSNVHMSSVTNTSNGGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTASGTATGTASGT SQ ATGTANGTGTGKGTDTHTAGSGSGSGTGTGTGTGTTTTTTTGNNSSSSTPPVTLTESLLNK // ID Q04561; PN Non-structural protein 12; GN rep; OS 11049; SL Nucleus Position: SL-0382; SL Comments: [Nsp1]: Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm {ECO:0000269|PubMed:23287061}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. Host cytoplasm {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000269|PubMed:28648849}. 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 endoplasmic reticulum {ECO:0000269|PubMed:21799305}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Serine protease nsp4]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000269|PubMed:25449571}. Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase nsp10]: Host cytoplasm {ECO:0000269|PubMed:28648849}. Host cytoplasm, host perinuclear region {ECO:0000305}. [Non-structural protein 11]: Host cytoplasm {ECO:0000269|PubMed:29444948}. Host nucleus {ECO:0000269|PubMed:29444948}. [Non-structural protein 12]: Host cytoplasm {ECO:0000269|PubMed:29920289}. DR UNIPROT: Q04561; DR Pfam: PF16749; DR Pfam: PF14757; DR Pfam: PF14758; 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: [Replicase polyprotein 1ab]: 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-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:27881655}. [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis (PubMed:28235682). Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:28235682}. [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28}. [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000269|PubMed:25102331}. [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF- kappa-B essential modulator NEMO and mediates its cleavage (PubMed:25008936). Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria (PubMed:27329948). Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity (PubMed:30158128). {ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:23936003, ECO:0000269|PubMed:25008936, ECO:0000269|PubMed:27329948, ECO:0000269|PubMed:30158128}. [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000269|PubMed:21799305}. [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000269|PubMed:27881658}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000269|PubMed:25449571}. [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000269|PubMed:12127789}. [Non-structural protein 11]: Plays a role in the inhibition of the secretion of host IL-1beta by the NLRP3 inflammasome through its endonuclease activity (PubMed:26398903). Plays also a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO (PubMed:29444948). {ECO:0000269|PubMed:26398903, ECO:0000269|PubMed:29444948}. DE Reference Proteome: Yes; GO GO:0030430; GO GO:0044165; GO GO:0033644; GO GO:0042025; GO GO:0044220; GO GO:0016021; GO GO:0005524; GO GO:0004197; GO GO:0003678; GO GO:0004521; GO GO:0003723; GO GO:0003724; GO GO:0003968; GO GO:0004252; GO GO:0036459; GO GO:0008270; GO GO:0039520; GO GO:0039648; GO GO:0039579; GO GO:0039514; GO GO:0039545; GO GO:0039522; 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 MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSA SQ VFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLT SQ NSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVD SQ LADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRG SQ IRAVVDPDGPIHVEALSCPQSWIRHLTLDDDVTPGFVRLTSLRIVPNTEPTTSRIFRFGAHKWYGAAGKRARAKRAAKSE SQ KDSAPTPKVALPVPTCGITTYSPPTDGSCGWHVLAAIMNRMINGDFTSPLTQYNRPEDDWASDYDLVQAIQCLRLPATVV SQ RNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIAD SQ FLANPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFIYAVERMLKDCPSSKQAMALLAKIKVPSSKA SQ PSVSLDECFPTDVLADFEPASQERPQSSGAAVVLCSPDAKEFEEAAPEEVQESGHKAVHSALLAEGPNNEQVQVVAGEQL SQ KLGGCGLAVGNAHEGALVSAGLINLVGGNLSPSDPMKENMLNSREDEPLDLSQPAPASTTTLVREQTPDNPGSDAGALPV SQ TVREFVPTGPILCHVEHCGTESGDSSSPLDLSDAQTLDQPLNLSLAAWPVRATASDPGWVHGRREPVFVKPRNAFSDGDS SQ ALQFGELSESSSVIEFDRTKDAPVVDAPVDLTTSNEALSVVDPFEFAELKRPRFSAQALIDRGGPLADVHAKIKNRVYEQ SQ CLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVAQWD SQ RKLSVTPPPKPVGPVLDQIVPPPTDIQQEDVTPSDGPPHAPDFPSRVSTGGSWKGLMLSGTRLAGSISQRLMTWVFEVFS SQ HLPAFMLTLFSPRGSMAPGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVG SQ SSCDHDSPECHAELLALEQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRYLWHVLLRLCMLADLALSLVYVVSQGRCHKC SQ WGKCIRTAPAEVALNVFPFSRATRVSLVSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKMSAQ SQ TVVAVPYDPSQAIKCLKVLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRVVVDSDTFVAAVRCGYSTAQLVLG SQ RGNFAKLNQTPPRNSISTKTTGGASYTLAVAQVSAWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPTYGPGVVCSSR SQ LCVSADGVTLPLFSAVAQLSGREVGIFILVLVSLTALAHRMALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHP SQ LTMLWVHSFLVFCLPAAGILSLGITGLLWAIGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRT SQ LIFTPSAVGSLLEGAFRTHKPCLNTVNVVGSSLGSGGVFTIDGRRTVVTAAHVLNGDTARVTGDSYNRMHTFKTNGDYAW SQ SHADDWQGVAPVVKVAKGYRGRAYWQTSTGVEPGIIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPE SQ GETCTIKETKLSDLSRHFAGPSVPLGDIKLSPAIIPDVTSIPSDLASLLASVPVVEGGLSTVQLLCVFFLLWRMMGHAWT SQ PIVAVGFFLLNEILPAVLVRAVFSFALFVLAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGTFAGRLS SQ ELSQALSTYCFLPRVLAMTSCVPTIIIGGLHTLGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMN SQ NESLTAALACKLSQADLDFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQIDKMKGVLSKLEAFAETATP SQ SLDIGDVIVLLGQHPHGSILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRSEE SQ DDLKVERMKKHCVSLGFHNINGKVYCKIWDKSTGDTFYTDDSRYTQDHAFQDRSADYRDRDYEGVQTTPQQGFDPKSETP SQ VGTVVIGGITYNRYLIKGKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLKRIISQLQGLTTEQALNCLLAA SQ SGLTRCGRGGLVVTETAVKIIKYHSRTFTLGPLDLKVTSEVEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGL SQ DTIPGIQPGHGAGNMGVDGSIWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHKGRLINTRFGD SQ LPYKTPQDTKSAIHAACCLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQ SQ KYDLSTQGFVLPGVLRLVRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTP SQ CTLKKQYCSKPKTRTILGTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAI SQ VRWFVANLLYELAGCEEYLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSALKMGHEIGL SQ KFLEEQLKFEDLLEIQPMLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNR SQ DRILAALAYHMKAQNASEYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKK SQ FRHCGICDAKADYASACGLDLCLFHSHFHQHCPVTLSCGHHAGSKECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKV SQ GNKTTALDPGRYQSRRGLVAVKRGIAGNEVDLSDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQV SQ QDDDVIYTPTHQTMFDIVSALKVCRYSIPGASGLPFPPPARSGPWVRLIASGHVPGRVSYLDEAGYCNHLDILRLLSKTP SQ LVCLGDLQQLHPVGFDSYCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTRPVAFGQVLTPYHKD SQ RIGSAITIDSSQGATFDIVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLTPERTDCNLVFSRGDELVVL SQ NADNAVTTVAKALETGPSRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPTFAPLPKELAPHWPVVTHQ SQ NNRAWPDRLVASMRPIDARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAE SQ EEAAKELPHAFIGDVKGTTVGGCHHITSKYLPRSLPKDSVAVVGVSSPGRAAKAVCTLTDVYLPELRPYLQPETASKCWK SQ LKLDFRDVRLMVWKGATAYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQ SQ NILTTAWFEDLGPQWKILGLQPFRRAFGFENTEDWAILARRMNDGKDYTDYNWNCVRERPHAIYGRARDHTYHFAPGTEL SQ QVELGKPRLPPGQVP // 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 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 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 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 Q05B54; PN Transmembrane protein 134; GN TMEM134; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6X4}. DR UNIPROT: Q05B54; DR Pfam: PF05915; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0048471; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSASRPQFSIDDAFELSLEDTGPGLEPSGVARFGPLHFERRARFEVADEDKQSRLRYQNLENDEDGAQASPEPDGGVSSR SQ DSGQTSIRSSQWSFSSISSSTQRSYNACCSWTQHPLIQKNHRVVLASFLLLLLGLVLILTGVGLEVAPSPGVSSAIFFVP SQ GFLLLVPGVYHVIFIYCAVKGHRGFQFFYLPYFEK // 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 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 Q06151; PN m7GpppX diphosphatase; GN DCS1; OS 559292; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic. DR UNIPROT: Q06151; DR UNIPROT: D6VYR7; DR UNIPROT: Q6Q5L1; DR PDB: 5BV3; DR Pfam: PF05652; DR PROSITE: PS00892; DE Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7- methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulate the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity. {ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:14523240, ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:16260594, ECO:0000269|PubMed:16963086, ECO:0000269|PubMed:22985415}. DE Reference Proteome: Yes; DE Interaction: P25491; IntAct: EBI-10420,EBI-38973; Score: 0.35 DE Interaction: Self; IntAct: EBI-38973,EBI-38973; Score: 0.75 DE Interaction: P32356; IntAct: EBI-38973,EBI-19509; Score: 0.67 DE Interaction: Q12123; IntAct: EBI-38701,EBI-38973; Score: 0.87 DE Interaction: P53940; IntAct: EBI-2612341,EBI-38973; Score: 0.35 DE Interaction: P48363; IntAct: EBI-13239,EBI-38973; Score: 0.35 DE Interaction: P40150; IntAct: EBI-8632,EBI-38973; Score: 0.35 DE Interaction: P25303; IntAct: EBI-38973,EBI-16711; Score: 0.35 GO GO:0005737; GO GO:0005739; GO GO:0005634; GO GO:0000932; GO GO:0048471; GO GO:0044692; GO GO:0016818; GO GO:0042802; GO GO:0050072; GO GO:0046982; GO GO:0042803; GO GO:0000340; GO GO:0009267; GO GO:0000290; GO GO:0000288; GO GO:0031086; GO GO:1901919; GO GO:0090342; GO GO:0009408; GO GO:0007584; GO GO:0006970; GO GO:0006979; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSQLPTDFASLIKRFQFVSVLDSNPQTKVMSLLGTIDNKDAIITAEKTHFLFDETVRRPSQDGRSTPVLYNCENEYSCIN SQ GIQELKEITSNDIYYWGLSVIKQDMESNPTAKLNLIWPATPIHIKKYEQQNFHLVRETPEMYKRIVQPYIEEMCNNGRLK SQ WVNNILYEGAESERVVYKDFSEENKDDGFLILPDMKWDGMNLDSLYLVAIVYRTDIKTIRDLRYSDRQWLINLNNKIRSI SQ VPGCYNYAVHPDELRILVHYQPSYYHFHIHIVNIKHPGLGNSIAAGKAILLEDIIEMLNYLGPEGYMNKTITYAIGENHD SQ LWKRGLEEELTKQLERDGIPKIPKIVNGFK // 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 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 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 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 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 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 Q074N0; PN RNA-directed RNA polymerase NS5; GN POLG; OS 407141; SL Nucleus Position: SL-0382; SL Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [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:P17763}; 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:P17763}; 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:P17763}. 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: Q074N0; 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. {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 immune response. {ECO:0000250|UniProtKB:P17763}. [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. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [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. {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 (By similarity). 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. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}. 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:0005525; 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:0039564; GO GO:0039502; GO GO:0039694; GO GO:0019062; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSGRKAQGKTLGVNMVRRGARSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKLTTHLKRLWRMLDPRQGLAV SQ LRKVKRVVASLMIGLSSRKRRSNEMAMMPLLILSMVILAGGVTLVRKNRWLLLNVTAEDLGKTFSLGTGNCTTNILEAKY SQ WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGRCDAVGRSKRSRRAIDLPTHENHGLKTRQEKWMAGRMGERQLQ SQ KIERWLVRNPFFAITALAIAYLVGNNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQGKCVTVMA SQ PDKPSLDISLQTVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENDGDNACKRTYSDRGWGNGCGLFGKGSIVA SQ CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI SQ AEMEKDSWIVDRQWAQDLTLPWQSGSGGIWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDENDNNLYK SQ LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAVNKGILVTVNPI SQ ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH SQ TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAVNFGKRELKCGDGIFVF SQ RDSDDWLTKYSYYPEDPVKLASIIKASHEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISVVVQDPKNIYQRGTH SQ PFSRIRDGLQYGWKTWGKNLIFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGMGVFTTRVFMDAVFDYSVDCDGA SQ ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMVHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV SQ QTNGPWMQVPLEVRREPCPGTSVVLDTGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTHE SQ SHLVRSWVTAGEVHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGIILLGAMLVGQVTVLDLVKLIVAVGLHFHEINNGGD SQ AMYMALIASFSIRPGLLVGFGLRTLWSPRERLVMAFGAAMVEVALGGMMGGLWQYLNAVSLCVLTINAISSRKASNAVLP SQ LMALLTPVTMHEVRMATMLFCTVVIVGVLHQNAKDTSMQKTIPIVALTLTSYMGLTQPFLGLCAYMSTQVFGRRSIPVNE SQ ALAAAGLVGVLAGLAFQDMENFLGPIAVGGILMMLVSVAGKVDGLELKKLGEVSWEEEAEISGSSSRYDVALSEQGEFKL SQ LSEDKVPWDQIVMTSLALVGAAIHPFALLLVLGGWVLHIKGARRSGDVLWDIPTPKVIEECEYLEDGIYGIFQSTFLGAS SQ QRGVGVAQGGVFHTMWHVTRGAFLLRNGKKLVPSWASVKEDLVAYGGSWKLDGKWDGEEEVQLIAAVPGKAVVNVQTKPS SQ VFKVRNGGEIGAVALDYPSGTSGSPIVNRSGEVVGLYGNGILVGDNSFVSAISQTEVKEESKEELQEIPTMLKKGMTTIL SQ DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLE SQ PTRAVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWTSGHEWI SQ LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEKEYPTIKQKRPDFILATDIAEMGANLCVERVLDCRTAYKP SQ VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIE SQ GTKTPVSPGEMRLRDDQRRVFRELVRGCDLPVWLSWQVAKPGLKTNDRKWCFEGPEEHEILNDNGETVKCRSPGGAKKAL SQ RPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVVLTELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI SQ VMLFILAGLLTSGMVIFFMSPKGMSRMSMAMGTMAGSGYLMFLGGVKPTHISYVMLIFFVLMVVIIPEPGQQRTIQDNQV SQ AYLIIGILTLLSIVAANELGMLEKTKEDFFGRRNIATSGGTIPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYG SQ NLSLSGIAQSASVLSFMDKGIPFMKMNISVVILLVSGWNSITVIPLLCGVGGAMLHWTLILPGIKAQQSKLAQKRVFHGV SQ AKNPVVDGNPTADIEEAPEMPALYEKKLALYLLLALSLMSVAMCRTPFSLAEGIVLSSAALGPLIEGNTSLLWNGPMAVS SQ MTGVMRGNYYAFVGVMYNLWKMKTGRRGSASGKTLGEVWKRELNLLDKQQFELYKRTDITEVDRDMARRHLAEGKVDTGV SQ AVSRGTAKLRWFHERGYVKLEGRVMDLGCGRGGWCYYAAAQKEVSGVKGYTLGRDGHEKPMNVQSLGWNIVTFKDKTDIH SQ RLEPAKCETLLCDIGESSPSSVTEGERTLRVLETIEKWLACGVDNFCVKVLAPYMPDVIEKLELLQRRFGGTIIRNPLSR SQ NSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEPDVILPIGTRSVETDKGPLDRDAIEERVERIKTEYAATW SQ FYDNDNPYRTWHYCGSYITKTSGSAASMINGVIKILTFPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRK SQ IMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAVGAFLEEQEQWKTANEAVQDPKFWEMVDAERKLHQQGRCQSCVY SQ NMMGKREKKLSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIKDLSTKEGGGFYA SQ DDTAGWDTRITEADLDDEQEIMSYMNAEQRKLAWAVMEMTYKNKVVKVLRPAPGGKAFMDIISRRDQRGSGQVVTYALNT SQ ITNLKVQLIRMAEAEMVINHQHVNECDEGVLARLDAWLAENGCDRLARMAVSGDDCVVRPVDDRFGLALSHLNAMSKVRK SQ DISEWQPSKEWTDWENVPFCSHHFHELVLKDGRKVVVPCRDQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHK SQ RDMRLLSFAVSSAVPMAWVPSGRTTWSVHGKGEWMTTQDMLDVWNRVWVLNNPHMKDKTTVKEWRDVPYLTKRQDKLCGS SQ LIGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI // 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 Q07937; PN Nanos homolog 1; GN nanos1; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21195170}. Note=During early cleavage and blastula stages found close to the cell periphery in a germ plasm-like pattern. From gastrula stage on, detected predominantly in a perinuclear region. DR UNIPROT: Q07937; 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. Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival. {ECO:0000269|PubMed:21195170}. DE Reference Proteome: No; 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 MDGGLCFDSWSDYLGLSSLISRGLQPQREGERPRWDVLSPASAEPLPSNESVGHKGCGFCRSNREALSLYTSHRLRALDG SQ RVLCPVLRGYTCPLCGANGDWAHTMRYCPLRRLLRDPQSNSNNPKLRH // 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 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 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 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 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 Q08AE8; PN Protein spire homolog 1; GN SPIRE1; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11747823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11747823}. Cell membrane {ECO:0000269|PubMed:11747823}; Peripheral membrane protein {ECO:0000269|PubMed:11747823}; Cytoplasmic side {ECO:0000269|PubMed:11747823}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11 (By similarity). {ECO:0000250|UniProtKB:Q52KF3}. DR UNIPROT: Q08AE8; DR UNIPROT: A8K2B5; DR UNIPROT: J3KQ50; DR UNIPROT: J3KQR5; DR UNIPROT: Q1RMD4; DR UNIPROT: Q8NDP1; DR UNIPROT: Q9NQ71; DR UNIPROT: Q9ULT4; DR PDB: 2YLE; DR PDB: 2YLF; DR PDB: 3R7G; DR PDB: 3RBW; DR Pfam: PF16474; DR PROSITE: PS51377; DR OMIM: 609216; DR DisGeNET: 56907; DE Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament (PubMed:11747823, PubMed:21620703). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:11747823). Required for asymmetric spindle positioning and asymmetric cell division during meiosis (PubMed:21620703). Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703). 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 (PubMed:26287480). {ECO:0000269|PubMed:11747823, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:26287480}. DE Reference Proteome: Yes; DE Interaction: P31946-2; IntAct: EBI-10770173,EBI-1055655; Score: 0.35 DE Interaction: P61981; IntAct: EBI-359832,EBI-1055655; Score: 0.35 DE Interaction: Q04917; IntAct: EBI-306940,EBI-1055655; Score: 0.35 DE Interaction: P03372; IntAct: EBI-78473,EBI-1055655; Score: 0.35 DE Interaction: P63104; IntAct: EBI-347088,EBI-1055655; Score: 0.35 DE Interaction: P27348; IntAct: EBI-359854,EBI-1055655; Score: 0.56 DE Interaction: Q9Y3M2; IntAct: EBI-1055655,EBI-947308; Score: 0.27 DE Interaction: P68466; IntAct: EBI-6152154,EBI-1055655; Score: 0.35 DE Interaction: Q96RK4; IntAct: EBI-1805814,EBI-1055655; Score: 0.56 GO GO:0005623; GO GO:0005938; GO GO:0030659; GO GO:0005856; GO GO:0005829; GO GO:0031307; GO GO:0005654; GO GO:0048471; GO GO:0005886; GO GO:0003779; GO GO:0030036; GO GO:0030041; GO GO:0045010; GO GO:0036089; GO GO:0051295; GO GO:0070649; GO GO:0046907; GO GO:0040038; GO GO:2000781; GO GO:0090141; GO GO:0015031; GO GO:0016192; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q52KF3}; SQ MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRH SQ RVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHM SQ ANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKS SQ AKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTL SQ RKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRP SQ LSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSS SQ VSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTV SQ EEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFS SQ LGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSL SQ VLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI // ID Q08BY2; PN Myelin-associated neurite-outgrowth inhibitor; GN fam168b; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:D4AEP3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AEP3}. Cell projection, axon {ECO:0000250|UniProtKB:D4AEP3}. DR UNIPROT: Q08BY2; DR Pfam: PF14944; DE Function: Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. DE Reference Proteome: Yes; GO GO:0030424; GO GO:0016021; GO GO:0048471; GO GO:0005886; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNPVYSPASSGVPYANPKGIGYPAGFPVGYAAAAPAYSPSMYPGANPAFPSGYAPGTPFKMSCSPTTGAVPPYSSSPNPY SQ PAAVYPVRSPYPQQNPYAQQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPAAMYAPPIPPPRPNGVTMGMVGGTTMAMSAG SQ TLLTTHSPTPVAPHPSMPTYRQPATPTYSYVPPQW // 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 Q08CX1; PN Ras and EF-hand domain-containing protein; GN rasef; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q08CX1; DR Pfam: PF13499; DR Pfam: PF00071; DR PROSITE: PS50222; DR PROSITE: PS51419; DE Function: Binds predominantly GDP, and also GTP. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; GO GO:0005509; GO GO:0005525; GO GO:0003924; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEDKDELSRLRALFHTFDSKSSGRLEKGQFSALCAELKVSPSEAEDIFARLDSDKDSCITFEDFAMGFRGARGLHMPEGK SQ KDVEQGEPPKSPSTPDKEEKPEETSSPAWEDFQRRLADEVNYIPRREQASILYQNINIVEPLLIQQYEHVIRNFVREIRL SQ QSTEMENLAIAVKRAQDKAAIQLSELEEEMDQRIQAVEKRVKKEEKRKSEEALNDLKRQHESEVAELQVTIKKLKKLEEQ SQ SKNINLKEDVAVLRRRLHDLTMENQKLRKDLLEAQTSISFLQSELDALKSDYADQSLSSERDMDIIRGFTDERENLARQI SQ EILQTANRKLHDSNDGLRSALENSLMKYNRSLRTINTSPGSTISRNSPKLTRCTSPYDRSPRSSYLDEDYDSLAVCDPMQ SQ RMNCEVDSLPESCIDSGLSTLRDSNEYDSEAEYRPPRIFHRSRFPHENYGGDASDTDVPEIRDEESYAPDNGGNLDWKPS SQ NPVSRSSSGASSSRKCISALSANVTSAETVDKVHKYTHAEKAYKIVLAGDAAVGKSSFLMRLCKNEFRGNTSATLGVDFQ SQ MKTLVVDGEPTILQLWDTAGQERFRSIAKSYFRRADGVLLLYDVTCEKSFLNVREWIDMIEDATSEAIPIMMVGNKADLR SQ QLMAEQGHICVSTNYGEKLSRTYGALFCETSAKEGSNIVEAVLHLAREVRKRCDNEDDRGSVTNLSAAISKKPAQMKNCC SQ NV // ID Q08DH8; PN DNA repair protein XRCC3; GN XRCC3; OS 9913; 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: Q08DH8; 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:0005759; GO GO:0005634; GO GO:0048471; GO GO:0033065; GO GO:0005657; GO GO:0005524; GO GO:0003677; GO GO:0008094; GO GO:0000724; GO GO:0045003; GO GO:0090267; GO GO:0010824; GO GO:0071140; GO GO:0090656; GO GO:0000722; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MDLDRLDLNPRIVAAVKKAKLRSVKEVLHLSGPDLQRRTHLSSPDVQLLLRASASLLRGHGVCTALHLLRQEGPFPEQHQ SQ RLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQLPPRHGGLGAGAVYVCTEDAFPSRRLQQLIAQQQR SQ LRADVPGHVISKIRFGHQIFIEHAADVDTLLQCVREKVPVLLARGMARLVVIDSVAAPFRCEFDGAALALRAQRLLALGA SQ ELRRLSCAFRSPVLCVNQVTEAVEEQDLVAGPPGMSPALGITWANQLLVRLLADRQRPEEAPLTPPGRTLRVVFAPHLPA SQ SSCSYTIAAEGVRGMPGTACS // 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 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 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 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 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 Q09747; PN ATP-dependent RNA helicase dbp5; GN dbp5; OS 284812; 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: Q09747; DR PDB: 3FHO; 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:0005829; GO GO:0005635; GO GO:0031965; GO GO:0005643; GO GO:0005634; GO GO:0005524; GO GO:0003723; GO GO:0003724; GO GO:0002184; GO GO:0006406; GO GO:0016973; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQ SQ SENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQS SQ QSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGT SQ VMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEE SQ LSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRV SQ GTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQR SQ PITRVPTDDYEELEKVVKNALKM // 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 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 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 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 Q0CHM0; PN Protein transport protein sec13; GN sec13; OS 341663; 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: Q0CHM0; 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:0005789; GO GO:0000139; GO GO:0005643; 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 MAAAQVISNSGHEDMIHDAGLDYYGRRLATCSSDKTIKVFEIEGEAHRLVETLKGHEGAVWCVAWAHPKFGTILASSSYD SQ GKVLIWREQHQNTTSPAAGSAWTKVFDFSLHTASVNMVSWAPHESGCLLGCASSDGHVSVLEFQDNSWTHQIFHAHGMGV SQ NSISWAPAAAPGSLISANPGPGQQRRFVTGGSDNLLKIWDYNPETKTYNLSQTLEGHSDWVRDVAWSPSILSKSYIASAS SQ QDKTVRIWTSDASNPGQWTSQQLEFDSVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE // 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 Q0IHC4; PN Myelin-associated neurite-outgrowth inhibitor; GN fam168b; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:D4AEP3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AEP3}. Cell projection, axon {ECO:0000250|UniProtKB:D4AEP3}. DR UNIPROT: Q0IHC4; DR Pfam: PF14944; DE Function: Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. DE Reference Proteome: No; GO GO:0030424; GO GO:0016021; GO GO:0048471; GO GO:0005886; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQQELEHPAHVSSGVQMFMFGHAFSVARNGAI SQ PSGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPFYAAPPHVIHHTTVVQPNGMPA SQ TMYPAPIQSPRGNGVAMGMVAGTTMAMSAGTLLTSHYPSPVAPQVTMPTYRPPGTPTYSYVPPQW // 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 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 Q0P4G6; PN Solute carrier family 2, facilitated glucose transporter member 10; GN slc2a10; OS 8364; 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: Q0P4G6; DR Pfam: PF00083; DR PROSITE: PS50850; DR PROSITE: PS00216; DE Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}. DE Reference Proteome: Yes; GO GO:0012505; GO GO:0005887; GO GO:0048471; GO GO:0005351; GO GO:0046323; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MGLSSPTLILAATVSLLGGIVFGYELGIISGALLVLKTVYQLTCFEQEALVSAVLFGALLASLIGGIIIDRWGRRTAILA SQ SNLVVLAGSIILIATSTFWWLIVGRVTIGFAISISSMACCIYVSEIVRPHQRGMLVSLYETGITVGILISYAMNYFLSGV SQ NESWKYMFGLAIVPAAFQFISILFLPSKPHKLNFWEQDTDDGFIELEETGEAGEFKPDTYDRQYTFLDLFRSKDNMRTRT SQ LLGLGLVLFQQFTGQPNVLYYASTIFQSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAIT SQ GIGIVSFTVKMDSHRDCGSVTGRNMSSGESNVSQLLGIVHAETSTINTLDNSVHQLAMAIRSPSLANSASSNHKDLISQN SQ STVLPASPELPSNYTILNWITLLSMMAFVSAFSIGFGPMTWIVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLDVIA SQ SIGLSWTFLLYGVVGLLAIAFIYFFIPETKGQSLEEIDKQFSTKRILQKRETSKGVGKRPSSGPPYQRIGKASPS // 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 Q0UCB9; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 321614; 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: Q0UCB9; 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:0005934; GO GO:0010494; GO GO:0031965; GO GO:0044614; GO GO:0005634; GO GO:0005844; GO GO:0005524; GO GO:0000822; GO GO:0003723; GO GO:0003724; GO GO:0008186; GO GO:0016973; GO GO:0006415; GO GO:0006409; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSATEPTKEPAKEEVAEQSTVAQAQVDGSGEPANGSPLTETEYKVEVKLADMQADPNNPLYSAQSFEELQLSEELLKGVR SQ NMNFRKPSKIQEKALPLLLMNPPTNMIAQSQSGTGKTAAFSLNILSRIDLSRNEPQAIALAPSRELARQILGVITHMGQF SQ MEGLKTMAAIPDPTKRNQRLDAHVLVGTPGTVQEQLKRRLIKSDSIKILVLDEADNMLDQQGMGDQCTRVKSLLPKNIQT SQ VLFSATFPPAVINYANKFAPNSNVLTLAHEELTIEGIKQLYIDIDKDQDKYSTLLKFYGLMTQASSIIFVRTRRTAEELE SQ RRMVAEGHKVAQLSGALEGQDRDRVIDQFRSGEAKVLITTNVLARGIDVESVTMVINYDVPTMADGREADPETYLHRIGR SQ TGRFGRVGVALTFVHDKASWQQLHDIASYFKTDLHPIDTSDWDNVEEMIQKIIKSSRAGKSTKEMTEMITS // ID Q0UNA9; PN Protein transport protein SEC13; GN SEC13; OS 321614; 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: Q0UNA9; 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 MADNGQNVDLLSIEANEVQHDAVLDYYGRRLATCSSDKTIKIFEVEGDKHTLVETLRGHEGPVWCVAWAHPKYGNILASS SQ SYDGKVIIWREQSSTWQKIYEVALHTASVNIVAWAPHEVGCLLACASSDGNVSVLEFKDNAWSHVIFQACGSGVNSVSWA SQ PAVAPGQVVSASGNQAGAARRFVTGGSDCQVKLWDFSAETGSWQSTQILTGHTDWVRDVAWSPTVLSKSYIASASQDKTV SQ RIWTSSDLRDWKSTVLNVDAVAWRVSWSLSGNVLAVSTGDNRVSLWKERLSGGWECVKTIEE // ID Q0VBZ8; PN Proline-rich protein 14; GN PRR14; OS 9913; 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: Q0VBZ8; DR UNIPROT: Q58D02; 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. Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit. Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha. 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}. 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 MDLPGDSSTPGRQRLCRQPHAGALWGAKSPKRPKLQPLGAPSPLEKASRRVLAVVLEDVMAARMVPLEPQEESSTPRHHS SQ NHRDSVRSQPPASPPRQAMWSPQARPPDPLHLCREPLSRIRRPPSTPRRQSRTTPGPDEGPSQKVDQVHQPTLVVMLQDI SQ ASSRPRAEGFADEAPNFIIPARRAEPKVMVHQPKPPSRDLPAPSRPSALSANPLASPPPAPDPVLEPPSTPPPSSLLRPR SQ LSPWGLAPLFHSVRSKLESFADIFLTPNKAPRPPPPSPPMKLELKIAISEAGQPGASEGTVTVSPRPPIRQWRAQDQNPS SQ ATLTKPSLGRSHSCPDLGPPGPDPCSWPPVPAPSSRPRPRRHTVGGGEMAKAPPPPRPCLRKEVFPLGGVGASPPLVTSC SQ SSTASTSSFSEPAEPRLSSTKRKEPRAPEDQVLPDSETKTIGKVSRFRIRRTPARSQINLTPMGLPRPVRLNKKEFSLEE SQ IYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRTVEFRDSSLPRSRRPSRGARATAGRTLPPSLAPSPDVEPL SQ LQQRLQELDASLLEEEEEGDQDQPHRT // ID Q0VCW8; PN Phosducin-like protein 3; GN PDCL3; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}. DR UNIPROT: Q0VCW8; DR Pfam: PF02114; DE Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000250|UniProtKB:Q9H2J4}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0048471; GO GO:0001525; GO GO:0006915; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MQDPNADTEWNDILRKKGILPSKEDLKDLEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEFNEEDERAIEMYRQQRL SQ AEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYP SQ DRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIKTSLEENPKKPVEDVLLSAVRCSVPAKRDSDSEDD // 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 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 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 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 Q10099; PN Nucleoporin seh1; GN seh1; OS 284812; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasm. Nucleus, nuclear pore complex. DR UNIPROT: Q10099; 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. 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:0034399; GO GO:0005643; GO GO:0031080; GO GO:0005634; 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 MDDISATTIQTNHQDLVNDVTYDFYGRRMVSCSADQRVKVYDFNDDTETWAITSEWRAGDASLMRVAWAHPSFGQVLAVC SQ SLDRGVRIYEEQKKNFESKTWVEVAKLMDARSAVLDISFCPFQHGCKLAAVSADATLRIYEAMEPGNLTYWTLMNEIALM SQ PSPPSRNEQPAFCVNWCPSRWREQYIAVGCMNDAYIYKQNSHGKWKKVAELPGHTDLIRDICWAPSMGSSYYLIATACKD SQ GNVRIFKVETLCEEVFQEEEDAGNSMTEDSNFNLNSLKVELIGEYDNHKCQVWRCRFNVTGTILSSSGDDGCVRLWKASY SQ ANLFKCISVVSLEKKPEKL // 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 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 Q10283; PN 3-hydroxy-3-methylglutaryl-coenzyme A reductase; GN hmg1; OS 284812; SL Nucleus Position: SL-0178; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19486165}; Multi-pass membrane protein {ECO:0000269|PubMed:19486165}. Nucleus envelope {ECO:0000269|PubMed:19486165}. DR UNIPROT: Q10283; DR UNIPROT: O74425; DR Pfam: PF00368; DR Pfam: PF12349; DR PROSITE: PS00066; DR PROSITE: PS00318; DR PROSITE: PS50065; DR PROSITE: PS50156; DE Function: Catalyzes 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:19486165, ECO:0000269|PubMed:8896278}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0031965; GO GO:0042175; GO GO:0005778; GO GO:0050662; GO GO:0004420; GO GO:0042282; GO GO:0015936; GO GO:0006696; GO GO:0010142; GO GO:0019287; GO GO:0008299; GO GO:0016126; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQI SQ PAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDS SQ SSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVL SQ LSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRH SQ FSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGND SQ SSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAI SQ SSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPE SQ KKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDV SQ TRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTM SQ RGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRF SQ CTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTV SQ EDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGG SQ TVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPAT SQ DALKSVNSRVPGR // 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 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 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 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 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 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 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 Q12382; PN CTP-dependent diacylglycerol kinase 1; GN DGK1; OS 559292; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. DR UNIPROT: Q12382; DR UNIPROT: D6W310; DE Function: Involved in pre-tRNA splicing (By similarity). CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PAH1/SMP2. Involved in the resistance to nickel chloride and nalidixic acid. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:10407277, ECO:0000269|PubMed:11481671, ECO:0000269|PubMed:18458075}. DE Reference Proteome: Yes; DE Interaction: P11484; IntAct: EBI-8627,EBI-36644; Score: 0.35 DE Interaction: Q8N6L0; IntAct: EBI-749265,EBI-36644; Score: 0.56 DE Interaction: Q96BA8; IntAct: EBI-6942903,EBI-36644; Score: 0.56 GO GO:0005783; 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 MGTEDAIALPNSTLEPRTEAKQRLSSKSHQVSAKVTIPAKEEISSSDDDAHVPVTEIHLKSHEWFGDFITKHEIPRKVFH SQ SSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNMLYCRTVGALMRKKEIHTYNGVLWYILGLIFSFNF SQ FSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAYSYVNKPGEIQWSPET SQ SRLSLNMLSLLGGVVAALSEGIDLFNWDDNFTIPVLSSLFMNAVIKTFKK // 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 Q15004; PN PCNA-associated factor; GN PCLAF; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000269|PubMed:11313979, ECO:0000269|PubMed:16288740, ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21673012}. Note=Following DNA damage, localizes to DNA damage sites (PubMed:21628590). Colocalizes with centrosomes in perinuclear region (PubMed:21673012). DR UNIPROT: Q15004; DR UNIPROT: A6NNU5; DR UNIPROT: A8K3Y3; DR UNIPROT: G9G694; DR UNIPROT: G9G696; DR PDB: 4D2G; DR PDB: 6EHT; DR PDB: 6GWS; DR PDB: 6IIW; DR Pfam: PF15715; DR OMIM: 610696; DR DisGeNET: 9768; 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. {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}. DE Reference Proteome: Yes; DE Interaction: P38936; IntAct: EBI-375077,EBI-10971436; Score: 0.35 DE Interaction: P17918; IntAct: EBI-1173716,EBI-10971436; Score: 0.35 DE Interaction: P12004; IntAct: EBI-358311,EBI-10971436; Score: 0.74 DE Interaction: P54274-2; IntAct: EBI-711018,EBI-10971436; Score: 0.56 DE Interaction: Q8IYD8-2; IntAct: EBI-21821466,EBI-10971436; Score: 0.35 GO GO:0005813; GO GO:0005654; 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 MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKEN SQ QIPEEAGSSGLGKAKRKACPLQPDHTNDEKE // 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 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 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 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 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 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 Q17285; PN Period circadian protein; GN per; OS 34689; 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: Q17285; 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 SKSSTGTPPSYNQLNYNENLMRFFKSKPVTVGKEESMAVEQSYNDVELQRDPSPDQCCDYSGESGSAGNLSSGSNVQMEI SQ ITNGSNTGTGTSSGSFQPPLLTEALLN // 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 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 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 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 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 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 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 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 Q1DY54; PN Nuclear protein localization protein 4; GN NPL4; OS 246410; 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: Q1DY54; DR UNIPROT: J3KEP2; 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 MAPPKPLILRFESRNGQFRLTVEPAELFPALLPKILSNLPQNVDPTSIALSNQPIGTGGQERKLSLLDGVSIQQVGLKHG SQ DKLFIGYSEQSTLVNGKSSNTSAGNMQHISRRLNGAPVPEQDLPAPPQPSSPTALIKNPWEVVQQSALDDRLDKKDGKIP SQ RGRDLKMCRHGPKGMCDYCMPLEPYAPEYLADKKIKHLSFHSYLRKVNSSKNKPELGSSFMPPLTEPYYRVRKDCPSGHP SQ AWPEGICTKCQPSAITLQPQEFRMVDHVEFASPDLINSLLDFWRKSGSQRLGFLYGTYEEYSEVPLGVKAVVQAIYEPPQ SQ VDEVDGITLREWENERDVDEVAKLCGLEKVGVIFTDLLDSGLGDGTVICRRHIDSYYLSSLEVAFAARLQARYPKPSKWS SQ ETGRFGSNFVTCILSGDENGAISISAYQASNSAVEMVRADIVEPSADPSVMLVQRENELENADTGNARYIPEVFYRKVNE SQ YGANVQENAKPAFPVEYLFVTLTHGFPTEPSALFADTTFPIENREVIGESQDIRNVAKKLLSRSDPDEAIRAVSNFHLLC SQ FMHGLGILSKEEEALLCTVARTHDPADGVQLINTPGWATLVTILQESGEPPPKRSWPFQTESSSSNKNHTRHVPLYPKTL SQ TSDSDQLAKRFKGASLE // 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 Q1JPH6; PN Eukaryotic translation initiation factor 4H; GN EIF4H; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q1JPH6; DR UNIPROT: A5D959; DR Pfam: PF00076; DR PROSITE: PS50102; DE Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; GO GO:0005844; GO GO:0003743; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK SQ FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGFRDDFLGGRGGSRPGDRRTGPPM SQ GSRFRDGPPLRGPNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVHKEQE // ID Q1L911; PN Nurim; GN nrm; OS 7955; 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: Q1L911; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0005635; GO GO:0005637; GO GO:0031965; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MASVTFRDGFLCVSALITFVFVFVTGADFVRFVSFRAINHNLSGAAPLCRDSVPWSVALRDGVVQKAVAVDVLLLVVFSL SQ QHSLLAWTPVKRVCQSVFGVLSRSVYCFTTAAALQILMHYWRPVTSAPCLWSVSSAPWEIWFPLICFIVHFLCWAIICSI SQ LLIFDYPELLGIKQVYYECLGLGDPLLLKSERAQRLYSHLRHPVCVELLTVLWLLPSFPLDRLLLAVFLTVYLILAHSLD SQ KQDCAYLRHQLRNKLQLFSTPLEGSEQTNDNNKLE // 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 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 Q1RML2; PN 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1; GN PLCZ1; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. 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 pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}. DR UNIPROT: Q1RML2; DR UNIPROT: Q5IT24; 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:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:15744020, ECO:0000269|PubMed:18284699, ECO:0000305}. DE Reference Proteome: Yes; GO GO:0005623; 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:0007343; GO GO:0032959; GO GO:0016042; GO GO:0007275; GO GO:0048015; GO GO:0060470; GO GO:0051209; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MENKWFLLMVRDDFKGGKITLEKALKLLEKLDIQCNTIHVKYIFKDNDRLKQGRITIEEFRTIYRIITYREEIIEIFNTY SQ SENRKILLEKNLVEFLMREQYTLDFNKSIASEIIQKYEPIEEVKQAHQMSFEGFRRYMDSSECLLFDNKCDHVYQDMTHP SQ LTDYFISSSHNTYLISDQLWGPSDLWGYISALVKGCRCLEIDCWDGSQNEPVVYHGYTFTSKLLFKTVIQAINKYAFLAS SQ EYPVVLSLENHCSPSQQEVMADSLLATFGDALLSYTLDNFSDRLPSPEALKFKILVRNKKIGTLHETLERKGSDMHGKVE SQ EFEEEEEIEQEEDGSGAKEPEPVGDFQDDLAKEEQLKRVVGIPLFRKKKIKISMALSDLVIYTKVEKFKSFHHSHLYQQF SQ NESNSIGESQARKLTKLAAREFILHTRRFITRVYPKALRADSSNFNPQEFWNVGCQMVALNFQTPGVPMDLQNGKFLDNG SQ CSGYVLKPRFLRDKKTKFNPHKVQIDSNPLTLTIRLISGIQLPPSYQNKADTLVIVEIFGVPNDQMKQQSRVIKKNAFNP SQ RWNETFTFVIQVPELALIRFVAENQGLIAGNEFLGQYTLPVLCMNRGYRRVPLFSKMGESLEPASLFIYVWYIR // 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 Q1XHX8; PN Nurim; GN NRM; OS 9598; 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: Q1XHX8; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0005635; GO GO:0005637; GO GO:0031965; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLM SQ AAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFD SQ YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLR SQ YLRAQLQRKLHLLSRPQDGEAE // 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 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 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 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 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 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 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 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 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 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 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 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 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 Q25206; PN Period circadian protein; GN per; OS 7235; 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: Q25206; 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 SKSSTETPLSYNQLNYKENLQRFFNSKPVTAPTQLDPVNRDSSYASTSREDACSAISPDHGGECSGGSGSSGNCTTNSNI SQ RMSSFTNTSITGTGTSGCGNSGGKLSESGPVEVGGAAADAGPSLAADNSIPPISVTLTESLLN // ID Q25221; PN Period circadian protein; GN per; OS 34685; 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: Q25221; 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 SKSSTETPPSYNQLNYNENLQRFFNSKPITAPVDVDPHEVEQSYDASTDARSFRSPLRHFEGSGGSGSSGNFNSGSNLHI SQ GSITNTSNTGTGTSSGSVQLITLTESLLN // ID Q27J81; PN Inverted formin-2; GN INF2; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20023659}. DR UNIPROT: Q27J81; DR UNIPROT: Q27J83; DR UNIPROT: Q69YL8; DR UNIPROT: Q6P1X7; DR UNIPROT: Q6PK22; DR UNIPROT: Q86TR7; DR UNIPROT: Q9BRM1; DR UNIPROT: Q9H6N1; DR Pfam: PF06367; DR Pfam: PF06371; DR Pfam: PF02181; DR Pfam: PF02205; DR PROSITE: PS51444; DR PROSITE: PS51232; DR PROSITE: PS51082; DR OMIM: 610982; DR OMIM: 613237; DR OMIM: 614455; DR DisGeNET: 64423; DE Function: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}. DE Disease: Focal segmental glomerulosclerosis 5 (FSGS5) [MIM:613237]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:20023659, ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:22971997, ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188}. Note=The disease is caused by mutations affecting the gene represented in this entry. Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE) [MIM:614455]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type E is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Patients additionally manifest focal segmental glomerulonephritis, proteinuria, progression to end-stage renal disease, and a characteristic histologic pattern on renal biopsy. {ECO:0000269|PubMed:22187985, ECO:0000269|PubMed:24174593, ECO:0000269|PubMed:24750328, ECO:0000269|PubMed:25165188, ECO:0000269|PubMed:25676889}. Note=The disease is caused by mutations affecting the gene represented in this entry. DE Reference Proteome: Yes; DE Interaction: O14976; IntAct: EBI-714707,EBI-2557882; Score: 0.35 DE Interaction: Q14108; IntAct: EBI-1564650,EBI-2557882; Score: 0.35 DE Interaction: P84089; IntAct: EBI-2551866,EBI-2557882; Score: 0.40 DE Interaction: P35579; IntAct: EBI-350338,EBI-2557882; Score: 0.35 DE Interaction: Q9NQW6; IntAct: EBI-2553589,EBI-2557882; Score: 0.35 DE Interaction: Q9D6P8; IntAct: EBI-11062253,EBI-2557882; Score: 0.35 DE Interaction: P62140; IntAct: EBI-352350,EBI-2557882; Score: 0.35 DE Interaction: Q9P2B7; IntAct: EBI-2558932,EBI-2557882; Score: 0.35 DE Interaction: P36873; IntAct: EBI-356283,EBI-2557882; Score: 0.35 DE Interaction: Q15388; IntAct: EBI-711636,EBI-2557882; Score: 0.35 DE Interaction: Q9NS69; IntAct: EBI-1047508,EBI-2557882; Score: 0.35 DE Interaction: P27824; IntAct: EBI-355947,EBI-2557882; Score: 0.35 DE Interaction: A0A0F7RE19; IntAct: EBI-2557882,EBI-2809783; Score: 0.37 DE Interaction: A0A384KTM2; IntAct: EBI-2557882,EBI-2847147; Score: 0.37 GO GO:0048471; GO GO:0003779; GO GO:0017048; GO GO:0030036; GO GO:0090140; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSVKEGAQRKWAALKEKLGPQDSDPTEANLESADPELCIRLLQMPSVVNYSGLRKRLEGSDGGWMVQFLEQSGLDLLLEA SQ LARLSGRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHVL SQ TLDALDHYKTVCSQQYRFSIVMNELSGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARLRDLEDAD SQ LLIQLEAFEEAKAEDEEELLRVSGGVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLLWEALESLVN SQ RAVLLASDAQECTLEEVVERLLSVKGRPRPSPLVKAHKSVQANLDQSQRGSSPQNTTTPKPSVEGQQPAAAAACEPVDHA SQ QSESILKVSQPRALEQQASTPPPPPPPPLLPGSSAEPPPPPPPPPLPSVGAKALPTAPPPPPLPGLGAMAPPAPPLPPPL SQ PGSCEFLPPPPPPLPGLGCPPPPPPLLPGMGWGPPPPPPPLLPCTCSPPVAGGMEEVIVAQVDHGLGSAWVPSHRRVNPP SQ TLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPAAKPKEPTMVAPRARKEPKEITFLDAKKSLN SQ LNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIPCYQLRIEC SQ MLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTL SQ LHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQYTERLQASISAFRALD SQ ELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPV SQ RKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAASMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATT SQ ASESRGWDLVDAVTPGPQPTLEQLEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQ SQ PPAAGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKSFSEDAVTD SQ SSGSGTLPRARGRASKGTGKRRKKRPSRSQEEVPPDSDDNKTKKLCVIQ // 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 Q27YE6; PN RING finger protein Z; GN Z; OS 55097; 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: Q27YE6; 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 MGQKPSKPKAPPTTYESPRSSLTPDATGFGPEFCKSCWFERKGLIKCQNHYLCMTCLTLLLTVSNRCPVCKYPLPTKLRL SQ EKSPTAPPPEATNPPPYSP // ID Q28E95; PN E3 ubiquitin-protein ligase SH3RF1; GN sh3rf1; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. DR UNIPROT: Q28E95; 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. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q6NRD3, ECO:0000250|UniProtKB:Q7Z6J0}. DE Reference Proteome: Yes; GO GO:0005794; GO GO:0030027; GO GO:0048471; GO GO:0005078; GO GO:0046872; GO GO:0061630; GO GO:0006915; GO GO:0001764; GO GO:0046330; GO GO:0051865; GO GO:0043370; GO GO:2000564; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRNELRCPECRTLVECGVDELPSNILLVRLLDGIKQRP SQ RKAGVGGSAGNSTNVLRAQGSLTTNCGLNDAQNIHGGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIV SQ LRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGML SQ GDKIGIFPISYVEFNSAAKQLIELDKPSGVDTGEGSSGTTHSSNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSM SQ EISPPVLISSSNPTAAARISELTGLSCSAPSQVHISTTGLIVTPPPSSPVVSGPAFTFPPEVTYQAALGDLNPPLLPPPP SQ LATPVITSTSSGAAAAVQRSISGPAEQVTHLRTSTRPSVFVAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHT SQ SKIGVFPGNYVAPVTRALTTATPAKVAMATASSSNVVNLVTPTPPGAPCQKLQGNGAEFAKTVSTNGVPPAGIPGSHIQS SQ SPQAKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAAVTPIQAQIPSASVLPQQAATSQQMPPPLSGPAAYINAAMNISR SQ PSVPVASAASSSVSSAAFETECNWKSGSGLAACSFPENVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPH SQ SPTQELEQTNSEAALEGAVGPDILPVNGNGRVASCTVDCDLVSASALVQDNRKPASLDTNVPIAPPPRQPCSSLGTVLND SQ SRPCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI // ID Q28GF5; PN Transmembrane protein 18; GN tmem18; OS 8364; 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: Q28GF5; 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 MAEDPGLWTLLERAPIDWKEPWLIGLAVFHILCLIVTYVSFKSYPLQICHFLLMVVLVSCAEYINEFAAMHWRSYSKQQY SQ FDSSGMFISLAFSAPLLCNTIIIVVHWVYKTLCVMTELKTLQQKRKESREKRKKKE // 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 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 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 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 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 Q29RU2; PN Oncoprotein-induced transcript 3 protein; GN OIT3; OS 9913; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250}. Note=Can be secreted into blood. {ECO:0000250}. DR UNIPROT: Q29RU2; DR Pfam: PF00100; DR PROSITE: PS00010; DR PROSITE: PS01187; DR PROSITE: PS51034; DE Function: May be involved in hepatocellular function and development. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0031012; GO GO:0005635; GO GO:0032190; GO GO:0005509; GO GO:0007339; GO GO:0035803; GO GO:2000344; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MPQLLLLACLLIIVTRVAPRALDPCSAYISLNEPWRNTEHQFDESRGSPLCDNSVDGEWYRFTGMAGDAMPTFCIPENHC SQ GTHAPVWLNGSHPLEGDGIVQRQACASFNGNCCLWNTTVEVKSCPGGYYVYRLTKPSVCFHVYCGHFYDICDDDCHGSCL SQ GTSECTCAPGTVLGPDRQTCFDENECEQNNGGCSEICVNLKNSYRCECGIGRVLRSDGKTCEDIEGCHNNNGGCSHSCLT SQ SETGYQCECPRGLVLSEDNHTCQVPVFCKSNTIEVSIPRDLVGGLELFLTNTSCRGVSNGTHVNILFSLKTCGTVVDVVN SQ DKIVASNLVTGLPKQTPGSSGDIIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNTPLEIMSRSHGIFPFTLEIFKDHEFE SQ EPYREALPTLKLRDSLYFGIEPLVHVNGLESLVESCFATPTSKIDEIMKYYIIQDGCVSDDSVKQYTSRDHLAKHFQVPV SQ FKFVGKDHKEVFLHCRVLVCGMLDERSRCAQGCHRRVRREASTEGEDASGPRSQMLTGGPISIDWED // ID Q2KHS5; PN 2-acylglycerol O-acyltransferase 2-A; GN mogat2; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}. DR UNIPROT: Q2KHS5; DR Pfam: PF03982; DE Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250|UniProtKB:Q3SYC2}. DE Reference Proteome: No; GO GO:0005789; GO GO:0016021; GO GO:1990578; GO GO:0003846; GO GO:0006071; GO GO:0019432; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MKIQFAPHNVPFERRLQTAAVLQWVFSFLALAQTCILLFFVLLFTRFWIISVVYGVWWFLDWDTPSKGGRRGEWLRRHVI SQ WTYMKDYFPITLVKTADLDPQQNYVVGSHPHGVLVAGAFTNFCTEATGFHRLFPGITPYLLMLPLWFRAPFFRDYIMSGG SQ LIPSDKDSASYLLKNKAGGNAVVIAVGGAPESLDARPGAFTLLIKNRKGFVRLAILHGASLVPVFSFGENELFDQVDNPR SQ GSWLRKIQEKLQKMMGVALPLFHARGVFQYSFGLIPYRKPIATIVGKPIRVEENPNPSSEEVDKLHKIYMEELSKLFEEH SQ KTKYNVPADKHLTFV // ID Q2KIA2; PN Multifunctional methyltransferase subunit TRM112-like protein; GN TRMT112; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. {ECO:0000250|UniProtKB:Q9UI30}. DR UNIPROT: Q2KIA2; DR Pfam: PF03966; DE Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S- adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production. Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA. {ECO:0000250|UniProtKB:Q9UI30}. DE Reference Proteome: Yes; GO GO:0005654; GO GO:0048471; GO GO:0046982; GO GO:0018364; GO GO:2000234; GO GO:0070476; GO GO:0030488; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MRLLTHNLLSSHVRGVGPRGFPLRLQATEVRINPVEFNPDFIVRMIPKVEWAALLEAADHLHLIQVPKEPIQGYEHNEEF SQ LRKMHHVLLEVEVLEGTLQCPESGRVFPISRGIPNMLLSDEETET // 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 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 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 Q2T9R2; PN Protein KASH5; GN CCDC155; OS 9913; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0183; SL Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q80VJ8}. 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:0000250|UniProtKB:Q80VJ8}. DR UNIPROT: Q2T9R2; DR UNIPROT: F1N496; 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:0000250|UniProtKB:Q80VJ8}. DE Reference Proteome: Yes; GO GO:0000781; GO GO:0016021; GO GO:0034993; GO GO:0005640; GO GO:0051321; GO GO:0034397; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MDMPEDQAGGPTAKMYLWDQAEDRSLGTLLSLEEQILNSTFEACDPQRTGTVAVTHLLAYLEAVTGRGPQDARLQTLACS SQ LDPSGEGPQATVDLDTFLVVMRDWITACQLDGGLELEEETAFEGALTSQQLPSGCPEVEDPANLESFGGEDPRPELPATA SQ DLLSSLEDLELSNRRLAGENAKLQRSVETAEEGSARLGEEISALRKQLRSTQQALQLARGVDEELEDLKTLAKSLEEQNR SQ SLLAQARHTEKEQQRLVAEMETLQEENGKLLAERDGVKRRSEELASEKDILKRQLYECEHLICQRDAILSERTRHAESLT SQ KTLEEYRATTQELRLEISHLEEQLSQTQEGLDELSEGAQVRRVDCTNLLPPSLGVELQAIQQRNLQEESAHPQEGREEPS SQ TRLPRREEEDGAEIQVMVDLPLHPEDSHPGDILGNPPESSPSEPELQQALVPMVKELVPVRRPVWGQLCLWPLHLRRLRV SQ TRHLLIPAPLLGLLLLLLLSVLLLGQSPPPTWPHLQLCYLQPPPV // 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 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 Q2TLY2; PN Macoilin-1; GN Maco1a; 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:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. DR UNIPROT: Q2TLY2; DR UNIPROT: Q1L869; DR UNIPROT: Q2TLY0; 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: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 MKRRNADCSKLRRPLKRNRITEGIHSSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF SQ VCVAFTSDIICLLFIPKQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIG SQ YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQRQERETEEATSKGMSEADSVLVAQNGTAINK SQ KLPISLPELEYKEKGKDSAKDKKQQQHSIGINNNILQTVDAKLQDIEYMENHLNAKRLNNELGGSAENLFLKEEVGAGGG SQ SAPSKHYKNSSPRSHNSTNGSVPSSSSNRSDKKQKCTGKNLAPHRDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS SQ RQVEQDLRSQISSLSSAERSMRSELGQLRQENELLQNKLHNAVQAKQKDKQTIVQLEKRLKAEQEARAAVEKQLAEEKKR SQ KKMEEATAARAVALAAASRGECTDSLKSRIRELESECKKLTHDMKLKEEQIRELELKAQELHKYKENEKDTEVLMSALSA SQ MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKEQEIKELKQKIAEVMAVMPSITYSAETNNMTPVTPHY SQ SSKFMDTSPSSLDPNASVYQPLKK // ID Q2VRL0; PN 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1; GN PLCZ1; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. 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 pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}. DR UNIPROT: Q2VRL0; DR Pfam: PF00168; DR Pfam: PF09279; DR Pfam: PF00388; DR Pfam: PF00387; 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. 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:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:16049153, ECO:0000305}. DE Reference Proteome: Yes; GO GO:0005623; GO GO:0005829; GO GO:0005730; GO GO:0005654; GO GO:0005634; GO GO:0048471; GO GO:0045120; GO GO:0061827; GO GO:0004435; GO GO:0032266; GO GO:0005546; GO GO:0010314; GO GO:0032959; GO GO:0016042; GO GO:0007275; GO GO:0048015; GO GO:0060470; GO GO:0051209; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEENRWFLNIIQDGFMNGKIDFDSTVKLLEKLHMPFNLAHVKHVFKKTVDKRKIHTINIEDFRAIYRAIVHRNEFHEIFC SQ AYSENRKNLADTELTAFLKKEQFKTEGAETTALEVILKYEPIDEVRKRRQLSFEGFIRYMSSEDCTIFKKEHRTVYQDMN SQ HPLCDYFISSSHNTYLVSDQLIGPSDLNGYISALLKGCRCLEIDCWDGSNNDPVVYHGHTLTSKITFCSVIHVVDKYAFA SQ ASDYPVVLSLENHCSTKQQERIAQYLLNILGDKLLTSPIGDIEVTQLPSPEALKFKILVKNKKCGTIEETMLRKGRDSHG SQ ETGEVSEEEITSSDEETDEKTPLYPKSGSSKRKSEGRSSPPPRKKAKVKKMKIAMGLSDLVIYTKSEKFVSFEHSLAHQK SQ CYENNSIGELKAQKFVKHAANQFVSHTSRFITRIYPKGTRAGSSNYNPQEFWNVGCQMVALNFQTSGTPMELQNGKFLDN SQ GGCGYILKPEFLRNRNSTFNPHNVGRYSNPLSLSIRLISGHQLPPSNLSKSNKADPLVQLEIYGVPEDQAKRKSSVIKSN SQ ALSPRWDETFSFTVQVPELALIRFCVQDEISLVANDFLGQYTLPLLSLSKGYCTVPLFSKSGGKLEPASLFVYVWYY // 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 Q2YDQ5; PN F-box/LRR-repeat protein 5; GN fbxl5; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q2YDQ5; 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; GO GO:0006511; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAPFPDEVDVFTGPHWRMKQLVGLYSEKLSNTNFSNNRDFRSFLQSLLDTFTEFKKHEQIENECIMELLQERSHTVYHVH SQ ADNKLSDMLTLFQKGLRSVTSEFEQLNYAQQLKERLEAFTQDFIPHMKEEEEVYQPMLMEYFSYEELKAIKQQVMLQHCS SQ SQCQSSCSDTHTLLKGLSLWSHAELQKAFKYSDHEKTGDERVLERVSVSSLPQELLLRIFRFLGPQDLCRCAQVCSVWTQ SQ VTRTGSLWRHLYPVRWARGEYYSGPPGDLDLEPDDDWIKSLQDDGRAYQEWDEDADVDESEEASAERSSISALQREKLLL SQ NGIIQKLLPAVGSSVRSLSLAYSSTLSSKMVRQMLSLCPNLTHLDLTQTDVSDSAFDSWCALGACGTLQHLDLSGCDKIT SQ DRTLKILSVGLGDSSTPSPAHKLLQAPPSPIRIEEPRLQPMGRSCQDLIFKRRPGGRGSGCGPTHIWVLDPVKLADIEDA SQ ADWSRRGGVASQEIGCGGISEALSASCCCRRSQRRGFRTGLSSSPWQYGDALCGHSSCCSSDAAAIRTQSDLQATGGSAE SQ LRTKCWFEGQSCAEHHNRTDQSGAQRALRFLSLSGCHQITDLGLRCVCLRGGLPLLEHLNLSGCPLITGAGLQEVVSASP SQ ALNIEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE // ID Q32NG5; PN Solute carrier family 2, facilitated glucose transporter member 12; GN slc2a12; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; 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: Q32NG5; DR Pfam: PF00083; DR PROSITE: PS50850; DR PROSITE: PS00216; DE Function: Insulin-regulated facilitative glucose transporter. {ECO:0000250|UniProtKB:Q6NWF1}. DE Reference Proteome: No; GO GO:0012505; GO GO:0016021; GO GO:0048471; GO GO:0005886; GO GO:0022857; GO GO:0008643; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLAHSTAQDLILQQRSSDDHPQTNPRQTGCGAFIILSSVIAAISGLLVGYELGIISGALLQLQSLLELTCQQQEIVVSAL SQ LIGALVASLVGGCLIDLYGRRTTIIFTSILLVFANLLPVVVVSYGSLIAGRIFIGVSISLSAIATCVYIAELSPQDKRGM SQ LVSLNELMIVAGILLAYICNYLFASVNNGWKYMFGLITPLAALQAVAMFFLPRSPRFLIMKGYDDAAGKVLQKLRATTDI SQ NEELTAIKSSIKAEYQYKFLDLFCSRDNMRARLLIGLTLSFFVQITGQPNILFYASTVLKSVGFQSTEAASLASTGIGVV SQ KVVSTIPAIFLVDKIGSKTFLCIGSAVMAVSLVSVGLVSLQLDVNYNNICKVHTVQNHSLQDSFVYGPVALAKHNESLFE SQ ETGTWLESTKASYHSTSQNGTKLLHVSAPEDSSFGFTVKEPKVKSQSDEIPEYMKWLCLSSLLAFVAAFSIGLGPMAWLV SQ QSEIFPAGIKGRAFAITSSMNWGMNLLISLTFLTLTEMIGLPWMLFGYALMSIASLVFVIMFVPNTKGRPLEEISKELAN SQ RSYMCNAVCHRRRSKKKLTPVALIQSPA // ID Q32PE2; PN Ran guanine nucleotide release factor; GN RANGRF; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}. DR UNIPROT: Q32PE2; DR Pfam: PF04603; DE Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1. Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics. Enhances the expression of SCN5A at the cell membrane in cardiomyocytes. {ECO:0000250|UniProtKB:Q9HD47}. DE Reference Proteome: Yes; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0005085; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HD47}; SQ MEPTRDNPLFGGAFSATLPPGAIDVSDLRPVPDHQEVFCHRVTDQSLIVELLELQAHVQGEEAARYHFEDVGGVQEARAV SQ QVETVQPLVLEKLALRGCCQEAWILSGQQQVAKENQQVAKYVTLHQALLRLPQYQTDLLLTFNQPPPENRSSLGPENLSI SQ PPWSLGDFEQLVTSLTLHDPNIFGPE // 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 Q32ZD4; PN RNA-directed RNA polymerase NS5; GN POLG; OS 64315; 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: Q32ZD4; 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}. [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 MSKKPGGPAGRRVVNMLKRPASVSPIKGIKRLIGNLTDGRGPLRVVLAFIAFFRFAAIMPTQGLLRRWRVMNKSEALKHL SQ TSFKKEISNMLNIINRRKAKRGNGSVLLWIALVTGSMALRLGTYQGKVLMSINKTDVAEIIPIPTTKGDNLCTVRAMDVG SQ YMCQNDITYECPRLEPGMDPEDIDCWCDREAIYVHYGLCTKNHRERRGRRSVNIPSHGESQLENRGTPWLDTAKTTKYLT SQ KVENWMIRNPGYAIVAVAAAWMLGSNTSQKVIFTIMLLLIAPAYSINCLGVTNRDFVEGMSGGTWVDIVLEGDGCVTIMA SQ KDKPTLDIRLLKMEAKDLATVRSYCYHATVTSVSSEARCPTMGEAHNPKALDSNYLCKSTYVDRGWGNGCGLFGKGSLQT SQ CVKFGCTQKAMGMTIQRENLDYELAIYVHGPTSVAAHGNYTTQLGAKHAAKFSITPSSPSFTANLGEYGEATVDCEPRAA SQ LDIDNYYVMSMNNKHWLVNRDWFHDLDLPWTGPATDVWKYRESLVEFEEAHVTRQTVVALAAQEGELHIVLAGAIPVTVA SQ GTTLTLTSGHLKCRMKLDKLKIKGSTYLMCKDKFAFAKNPVDTGHGTIVTEVQYAGSDGPCRIPITMTENLHDLTPIGRL SQ VTVNPFVPSSETAQKILIELEPPFGTSFILVGTGPNQVKYQWHKSGSVIGSAFKTTIKGAQRMAVLGETAWDFGSVGGVF SQ NSIGKGIHGLFGGAFRTLFGGMSWVTQALMGALLLWLGVSSRERTVSITLLATGGILLFLAMNVHADTGCAIDITRRELK SQ CGSGIFIHNDVETWRDNYKYHPSTPKNFAKIIHKAYKEGICGVRSASRLEHEMWKHIAPELNAILEDNEVDLSVVVEEHK SQ GIYKKAPLRLENTSDEMHFGWKNWGKSFLFKTQMANSTFVVDGPETKECPTERRAWNSLEIEDFGVGIMSTKVFLKVNGD SQ KTEVCDSMVMGTAIKGNRAVHSDLGYWIESGKNTSWRLERAVLGEVRSCTWPESHTLWNEGVEDSDLIIPPTLGGPRTHH SQ NKREGYKTQLKGPWNEEGPIIIEFGECPGTKVTQEESCRNRAASARTTTASGKVIRDWCCKNCTMPPLRFTTKNGCWYGM SQ EIRPKHESEETLIKSKVTAGTGNDICRFQLGLLMAFVFTQEVLRKRWTARLALPTAALLLACFVLGAFTYSDMIRYFVLV SQ GCAFAESNSGGDVIHLALIAVFNIQPAALVSTFFRNRWTNRENLLLVIAAAMAQMAWSDVGIEIMPIMNAMALAWMILKA SQ VSIGTVSTIAMPILSGLAPPMEWFGLDVLRCLLLIVGVAALIKERKENLAKKKGALLISAGLALTGAFSPLVLQGALMLS SQ ECATKRGWPASEVLTAIGMTIALAGSVARLDSGTMAIPLATTSILFVSYVLSGKSTDMWIERCADVTWEEEAEITGTSPR SQ LDVELDDNGDFKMINDPGVPMWMWASRMGLMCMAAYNPVLIPVSVAGYWMTRKIHKRGGVLWDLPAPKQMGRSDMKPGVY SQ RVMTSGVLGSYQSGVGVMYDGVFHTMWHVTQGAALRNGEGRLNPTWGSVRDDLITYGGKWKLSATWDGTEEVQLIAAEPG SQ KPVKNFQTRPGVFKTPAGEVGAITLDFPKGTSGSPIVNKAGAVIGLYGNGLVLSHGAYVSAISQGERQEEEAPEAFTPEM SQ LRKRQLTILDLHPGAGKTRRVIPQIVREAVKQRLRTVILAPSRVVAAEIAEALRGLPVRFQTSAVKAEHSGTEIVDVMCH SQ ATLTQRLMTPMRVPNYNVFVMDEAHFTDPASIAARGYISTKVESGEAAAIFMTATPPGTIDPFPDSNSPIIDQEAEIPDR SQ AWNSGFEWITDYTGKTVWFVPSVRSGNEIAMCLTKAGKKVIQLNRKSYETEYQKCKGNDWDYVVTTDISEMGANFGAHRV SQ IDSRKCVKPVIINDGEGRVQLNGPLPITASSAAQRRGRVGRDPTQSGDEYYYGGPITNDDTGHAHWIEAKMLLDNIQLQN SQ GLVAQLYKPERDKVFATDGEYRLRGEQKKHFVELMRTGELPVWLSYKVAEAGINYTDRRWCFDGPHNNTILEDNTEVEIW SQ TRQGERKVLRPRWSDARVYSDNQALRAFKEFAAGKRSAGSMMDVMARMPDYFWTKTMNAADNLYVLATTEKGGRAHRAAL SQ EELPDTLETVLLIAMMSLASCGMLALMMQRKGIGKTGMGTAVLTAVTILLWMADVPAPKIAGVLLISFLLMIVLIPEPEK SQ QRSQTDNHLAVFLICALLLVSAVSANEMGWLDTTKRDLGKLFSGPSAVTTSRWEPLKLALALKPATAWAGYAGMTMLLTP SQ LFRHLITTQYISFSLTAITSQASALFGLNSGYPFVGVDLSVVFLLVGCYGQYNLPTTMATIGLLVGHYAFMIPGWQAEAM SQ RAAQRRTAAGVMKNAVVDGIVATDIPEMDTATPIVEKKMGQVMLLIISALAILLNPDTMTVVEGGVLITAALATLLEGNA SQ NTVWNSTVAVGVCHLMRGGWAAGPSIGWTIIRNLEAPKVKRGGIAAPTLGEIWKSRLNQLTREQFMEYRKDGIIEVDRTA SQ ARRARREGNRTGGHPVSRGTAKLRWLVERGFAKPLGKVVDLGCGRGGWSYYCATLRHVQEVRGYTKGGPGHEEPMLMQSY SQ GWNIVSMKSGIDVFYRPTEACDTVLCDIGESSPSPGVEEARTLRVLEMIEPWLRTANQYCVKVLCPYTPKVIERLEKLQR SQ KYGGGLVRVPLSRNSNHEMYWVSEASSNLINAVNATSQVLLQRLEKDHRKGPRYEEDVDLGSGTRSVARRSPFMDTRKIH SQ HRIERLKSEFSTTWHYDCEHPYRTWNYHGSYEVKPTGSASSMVNGVVKLMSKPWDSIQSVLTMAMTDTTPFGQQRVFKEK SQ VDTKAPEPAPGVKAVLDLTTDWLWAVLCRRKKPRMCTKEEFIAKVNSHAALGAIFEEQNQWASAREAVEDPGFWNFVDKE SQ RQAHLEGRCETCIYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRENSYGGVEGKGLQKLGYI SQ LQEISRKEGGHMFADDTAGWDTRVTLTDLENEAKITRWMEPEHRKLAEAMIELTYKNKVVKVTRPGKEGKTVMDIISRND SQ QRGSGQVVTYALNTYTNLAVQLIRCMEGEGLLEEEETMRISDAKRRAVQAWLDTNGTERLTPMAVSGDDCVVKPIDNRFA SQ TALHFLNGMSKVRKDIQEWKPSTGWTNWQEVPFCSHHFNELVMRDGRKIVVPCRAQDELIGRARVSPGSGWSLRETACLG SQ KAYAQMWLLMYFHRRDLRLMANAICSAVPIDWVPTGRTTWSIHGKGEWMTTEDMLAVWNRVWIFENEHMEDKTPVYSWTD SQ VPYIGKREDQWCGSLIGHRSRATWAENIYTPIMQVRNLIGAERYVDYMPAQTRFAHEAELQGGVL // ID Q32ZD5; PN RNA-directed RNA polymerase NS5; GN POLG; OS 44024; 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: Q32ZD5; DR PDB: 2V6I; DR PDB: 2V6J; 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 (PubMed:18004778). {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:18004778}. [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: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 MTKKPGRPGRNRAVNMLKRGASRALGPMIKLKRMLFGLLDGRGPLRMVLAILAFFRFTALKPTAGLLKRWGMMDKVHALS SQ LLKGFKKDLASMTDFVHLPKKKSGVSIIGRMLVFSFTAAVRVTLENGMSLMKIQKADVGKVITIRTDRGENRCIVQAMDV SQ GEDCEDTMKYLCPAIENPSEPDDIDCWCDKADAMVTYGRCSKTRHSRRSRRSTNIAGHADSRLDSRGSVWMDTKKATSYL SQ TKAESWALRNPGYALVAAVLGWSLGTSNAQKVIFTVMILLIAPAYSIRCVGVENRDFIEGVSGGTWVDVVLEHGGCVTIM SQ APDKPTIDLELTSTIAKSMAVTRTYCVQAQVSELSVETRCPTMGEAHNSKSSDAAYVCKKGFSDRGWGNGCGLFGKGSME SQ TCAKFSCQTKAEGRIIQRENLEYTIHMNVHASQETGHFMNDTIASENKHGAKISITATGPSRTADLGDYGMVTLDCEPRA SQ GLDFDNLYLLTLGRNSWLVNRDWFHDVNLPWIGGAEGHWKNRESLVEFGKTHATKREVLALGSQEGTLQVALAGAMIAKF SQ GSNVATINSGHLKCRLKLDKLKIKGTTYHMCKGSFAFTKTPSDTGHGTVLLELTYSGSDGPCRVPISMSVSLSNIEPVGR SQ MVTVNPIVLSSSPQKTIMIEVEPPFGDSFIIAGTGEPRAHYHWRKSGSSIGAAFATTIKGARRLAVIGDDAWDFGSVGGI SQ LNSVGKALHQIFGGMFRTLFGGMSWFTQIMIGALCCWLGINARDRTIAVTFLAVGGVLVFLATSVNADSGCALDLKRKEF SQ KCGNGIFVFNDAEAWSHSYRYHPSTPKKLAGSIVRAIEEGQCGVRSVGRLEHEMWRANAREINAILLENEKNLSVVVLES SQ EYYRKAKNLMPIGDEMPFGWKSWGKKFFEEPQLQNQTFVVDGRVGKECPEEKRSWNNFRIEDFGFGVFTTSVWMEQRTEY SQ TEDCDQKVIGAAVKGELAAHSDLGYWIESRSKNGSWELERAYLLESKSCSWPATHTLWNGGVEESELIIPKSRAGPVSHH SQ NTRKGYHNQIKGPWHLTPLEIRFESCPGTTVVTTEECGNRGPSLRTTTTSGKVISEWCCRSCTMPPLSFRTADGCWYGME SQ IRPLKEREETMVKSHVSAGRGDGVDNLSLGLLVLTIALQEVMRKRILGRHITWMVIAVFMAMILGGLSYRDLGRYLVLVG SQ AAFAERNSGGDLLHLVLVATFKVKPMALLGFVLGGRWCRRQSLLLSIGAVLVNFALEFQGGYFELVDSLALALLFVKAVV SQ QTDTTSVSLPLLAALAPAGCYTVLGTHRFIMLTLVLVTFLGCKKTASVKKAGTAAVGVVLGMVGMKTIPMLGMLMVTSRA SQ RRSWPLHEAMAAVGILCALFGALAETEVDLAGPLAAAGLIVMAYVISGRSNDLSIKKVEDVKWSDEAEVTGESVSYHVSL SQ DVRGDPTLTEDSGPGLEKVLLKVGLMAISGIYPVAIPFALGAWFFLEKRCKRAGALWDIPSPREAKPAKVEDGVYRIFSR SQ KLFGESQIGAGVMVKGTFHTMWHVTRGAVLKAGEGLLEPAWADVRKDLICYGGNWKLEEHWDGNEEVQLIALEPGKKVRH SQ IQTKPGIFKTSEGEIGALDLDCMAGTSGSPIVNKNGEVVGLYGNGVLIKGDRYVSAISQKENVGQEDGAEIEDNWFRKRE SQ LTVLDLHPGAGKTRRVLPQLVREAVKKRLRTVILAPTRVVASEMYEALRGEPIRYMTPAVQSERTGNEIVDFMCHSTFTM SQ KLFQGVRVPNYNLYIMDEAHFLDPASVAARGYIETRVSMGDAGAIFMTATPPGTTEAFPPSNSPIIDEETRIPDKAWNSG SQ YEWIIEFDGRTVWFVHSIKQGAEIGTCLQKAGKKVLYLNRKTFESEYPKCKSEKWDFVITTDISEMGANFKADRVIDPRK SQ TIKPILLDGRVSMQGPIAITPASAAQRRGRIGRNPEKLGDIYAYSGNVSSDNEGHVSWTEARMLLDNVHVQGGVVAQLYT SQ PEREKTEAYEGEFKLKTNQRKVFSELIRTGDLPVWLAFQVASANVEYHDRKWCFDGPNEHLLLENNQEIEVWTRQGQRRV SQ LKPRWLDGRITSDHLNLKSFKEFASGKRSALSILDLIAVLPSHLNLRLQEALDTAAILSRSEPGSRSYKAALENSPEMIE SQ TFLLCALVCLMTIGLVVVLVRGKGPGKLAFGMVSIGVMTWLLWSAGVDPGKIAAAVILVFLLLVVLIPEPEKQRSVQDNQ SQ LAMLMLLIATILGGVAANEMGWLEKTKADLSWVVRGRSSTTTPVVELDMKPATAWTLYALATTLLTPLFQHLIVTKYANI SQ SLMAIASQAGTLFSMDSGIPFSSIELSVPLLALGCWTQITPCSLILACVLLSTHYAILLPGMQAQAARDAQRRTAAGIMK SQ NAVVDGIVATDIPPLDGAGPLTEKKLGQLLLFAAAVTGVVITRSPRSWSELGVLGSAVGSTLIEGSAGKFWNATTVTAMC SQ NLFRGSYLAGVPLTYTIIRNSNPSNKRGGGIGETLGEKWKARLNQMNTLEFHRYRRSHIMEVDREPARAALKSGDFTRGA SQ AVSRGSAKLRWMHERGYIRLHDKVVDLGCGRGGWCYYSATVKEVKEVKGYTKGGRGHEEPVLTQSYGWNIVQMKSGVDVF SQ YKEAEPCDVVLCDIGECSSSPAVEADRSTKVLELAERWLERNDGADFCIKVLCPYMPEVVEKLSKLQLRYGGCLVRNPLS SQ RNSTHEMYWVSGYKGNLIGVINSTSALLLRRMEIKFAEPRYEEDVNLSCGTRAVSIAPPKFDYKKIGQRVERLKAEHMST SQ WHYDCEHPYRTWAYHGSYVVKPSGSASSQVNGVVKLLSKPWDVSSEVTGMSMTDTTPFGQQRVFKEKVDTKAPEPPAGAE SQ MASVIVSEWLWKRLNREKKPRLCTKEEFVRKVRGNAALGPVFEEENQWKDAAEAVQDPGFWNLVDMERKNHLEGKCETCV SQ YNMMGKREKKRGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRGNSGGGVEGLGIQKLGYVMREIGEKGGILYA SQ DDTAGWDTRITECDLRNEAHIMEYMENEHRKLARAIFELTYKHKVVKVMRPGKGVPLMDIISREDQRGSGQVVTYALNTF SQ TNLVVQLIRMAEAECVLTPEDLHEMSQSAKLRLLKWLKEEGWERLTRMAVSGDDCVVAAPDARFGAALTFLNAMSKIRKD SQ IKEWTPSKGWKNWEEVPFCSHHFHRLQMKDGRELVVPCRSQDELIGRARVTQGPGDLMSSACLAKAYAQMWQLLYFHRRD SQ LRLMGNAICSAVPVDWVPTGRTTWSIHGKGEWMTSENMLEVWNRVWIEENEHMEDKTPVREWTDIPYLGKREDPWCGSYI SQ GYRPRSTWAENIKVPVNVIRVKIGGNKYQDYLGTQKRYESEKRVEFRGVL // ID Q32ZE0; PN RNA-directed RNA polymerase NS5; GN POLG; OS 64304; 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: Q32ZE0; 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. {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}. [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 MARKPGRPGGNRVVNMLKRTAANAASPLGLAKRLLGDAFAGRGPLRVILAVVAFFRFTAIKMSPALLKKWGTVEKGAAIA SQ IMKSFKKEIGSMLDVVARRKTKNKGKRSVESSALLVLLTACLALGFKVVTGPEGPIMDVTKKDVGKALEIPFQNFNNTCW SQ VMAMDVGHPCEDTIEYECPSLDIGAEPNDIDCWCDTMPMRVRYGRCTKGSIPKRSRRNAVFPQHTENVLATRQETWMNTD SQ VIMKHLIKVETWALRNPGFALVAITLGWMLGSNRSQKIIFTILLLLVAPAYNMRCIGVENRDFVEGLSGGTWVDVVLEHG SQ GCVTVRVEGKPTLDFELVQTKATGLAAVRAYCYQAKVSDIQISAACPAVQLTENSKATDSNYLCRRGVTNRGWNNGCGLF SQ GKGDIHTCVKFKCEKKAAGFSIGKENLEYEVRASVHNSIGADKFSNELADGEPHTQKMKFSPLSPSAEKSFGDYGTLGMD SQ CEPQSGLDFGQLYLMTIESKSWLVNRDWYHDLHLPYTVGSGSQWNNREALVEFQEPHATKQEVLALGSQEGALHSALAGA SQ IMANRETSSPHALLLTAGHLKCRIKMDKMVIKGITYGQCSGTFKMEKHPADTGHGTVVLDVSYQGDDAPCKIPIVITSNL SQ AEVEPVGRLVSAHPVITAKNVRTMLEVEPPYGDSYIVIGVGDGRLKQHWFKKGSVIGGAFSTTMKGAKRLAVLGDAAWDF SQ GSVGGVFNSLGKAVHQLFGGIFRTLFGGMSWLSRLMIGALCLWIGINARDHSIAVTMLSVGGILIFLSINVSADTGCVVD SQ IERKELKCGSGIFIMNDIEAWRDEYAFHPSGPKALAASVVEAFSQGVCGVRSVNRLEHKMWESIADELNAILEENEREIT SQ IVVKDMENPAQKGKMRLRPVEKELKYGWKKWGASFFKRASRKNATFLVDGPSGEECPNSNRAWNSFFIEDFGFGVFKTSV SQ WLGLNEQMTEVCDTKMIGTGVKNDRAVHSDLGYWIESRKNLTWEISRARLIETKACIWPRSHTLWSDGIEETQLIIPKSL SQ GGPRSRHNMRSGYKTQINGPWDQIPLDIKFEECPGTSVTVTPNCGGRGPSARSTTASGKVIADWCCRDCILPPLTFRSGE SQ TCWYAMEIRPVSEREETLIRSKVSAGDGNEIDTFSLGLLVAMLVTQEGLRKRWATRHIMVASLTMLAAMVTGHITYRDLL SQ RYVVLLGATFAQINDGGDVMHLALVAVFKVQPGFLLGFLLRRRWTPRESMLLAISACFLHLVFSELSTDITTLAHNFSLA SQ LLILRAIIQTDVSSVTLPVLSMMAPSFQLSVLGTFRMAVAVYVIVNLMMSKRNDAVKKAAPSVVAAALGQFGMVNATAAL SQ GTLYVLEKHGKRSWPPSEIFSAVGVLCALVGALGNVQSTPLAGPMAACGLLIAAYVVTGKSTDIEIERAGLISWSEDAEV SQ SGSSPRVDVALDENGDFSLIDGQGPSLESVILKTALVAFSGLFPVSIPFCAAAWYLHGKSGRRAGALWDIPAPREVKKGS SQ TENGVYRILANRLFGKTQVGVGVMHEGVFHTMWHVTRGAALKSGEGRLDPYWGDVKKDLISYGGPWKLEGRWDGVSEVQL SQ IAVPPKEKAKNVQTTPGVFKTPHGEIGAIVLDFPAGSSGSPIINKLGEVIGLYGNGLMMGDAYASSIAQAEVEDEPDTPN SQ CLPPDVTHKKKLTVLDLHPGAGKTRKVLPKLLQEALEKRLRTVVLAPTRVVAAEMAEALKGMPIRYQTAAVTSSHSGNEI SQ IDLMCHATFTSRLMQPHRVPNYNLYIMDEAHFTDPASIAARGFIATKVSLGEAAAVFMTATPPGSDNPFPASNAPITDTE SQ AQIPDKAWSTGFDWITEYGGKTVWFVPSVRMGNEIAACLTKAKKKVIQLSRRTFNTEYPKCKQGDWDFVVTTDISEMGAN SQ FKATRVIDSRRAIKPSIMQDQEERVVLSGPTPISPASAAQRRGRVGRNPNQLGDEYVFSGLTQANDEGNACWTEARMLLD SQ NIHMQNGLIAQLYGPEQDKCFATDGEFKLREKERATFLEFLKADLPVWLSFKAASSGVQYHDRKWCFDGPDNNLVLEDNV SQ PVEIWTKSGERKKLKPRWSDARTYCDHGALTAFKEFAGGRRSVTTGLLEGVGRLPEHLGQRLKESIDTLYLAFTAEVGSR SQ PHREAMQEMPAALETVLVFFLLMIMTGCTFFLLMRHKGINKMGYGMVVMSAVGGLLWYGNVPAPKIAGILLLTFLLMVVL SQ IPNPEKQRSIQDNQLALVVLGCLMFLGGIAANEMGMLERTKQDLAGVFHKTERKSTEFTLLTPPDLRPATAWSIYAIGTT SQ LITPLIHHMITTHYANFSLMAMANQAGSLFGMQTGAPFSKMDWAVPAIVVGCWQQLTPATLMTALVLLAVHYIYMIPGWQ SQ AGAARAAQRRTAAGIMKNPVVDGLVVTDIPTLEEVDPLVEKKLGQYILLAVAIAAAVLRQDLQSWSECATLSAAAAATLW SQ EGSPGKIWNASTACSLVNIFRGHTLAAVPFMFTILRNTGNTGKRGGVEGETLGEKWKHLLNAMDKYEFSRYKVNGIFEVD SQ REPARMALANGLVTSGHAVSRGSAKLRWMVERAAVRPTGRVIDLGCGRGGWSYYCATLKQVQEVRGYTKGGPGHEEPRMV SQ QSYGWNIVTLKSGVDVFHRPAEVGDTILCDIGESSATPEVEEARTLKVLEMVEPWLKNKPEFCIKVLCPYRPKVIERLSA SQ LQRTYGGGLVRVPLSRNSTHEMYWTSGTAGNIINAVNLTSKVLLHRMEKKWIGPRYEKDVNLGSGTRAVIVKRKAPDMDK SQ IGNRVKRLKEEHIATWCYDDMNPYRTWNYHGSYEVKPTGSASSMINHVVKMLSKPWDTLNSVTSISMTDTTPFGQQRVFK SQ EKVDTKAPEPPTGVAEVMDIISDWTWRLLSRQKKPRLCTRDEFKAKVNNHAAMGSIFEEEHQWQTAKEAVEDPGFWALVD SQ REREAHLAGRCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWLSRENSYAGVEGLGLQRLG SQ YVLRDISRRPGGKMYADDTAGWDTRITEKDLDNEAKIIDQMEGEHKQLAKAIMELTYRHKVVKVMRPGPGGKTYMDIISR SQ EDQRGSGQVVTYALNTFTNMIVQLTRCAEAEGVLIPSMRERKLTPAEHRALLLWLDTEGVKRLKKMAISGDDCVVKGEDE SQ RFATALYFLNAMAKVRKDIQEWKPSSGWADWQEVPFCSHHFKELQLKDGRTIVVPCRHQDELVGRARVSPGAAWTVRESA SQ GLAKAYAQMWKLMYFHRRDLRLMANAICSAVPKDWVPTGRTTWSIHGKGEWMTNEDMLEVWNRVWIRENPHVEDKTEVAD SQ WKDVPYLGKREDQWCGSLIGSRTRATWAENIWVAVNQVRAKIGKEEYSDHLSSQQRFENWGEVRFSGVL // ID Q38942; PN Protein RAE1; GN RAE1; 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:0000269|PubMed:21189294}. DR UNIPROT: Q38942; DR UNIPROT: Q1LYY5; DR UNIPROT: Q9SAJ0; DR Pfam: PF00400; DR PROSITE: PS50082; DR PROSITE: PS50294; DE Function: DE Reference Proteome: Yes; DE Interaction: Q9M0V3; IntAct: EBI-1632780,EBI-1632807; Score: 0.37 GO GO:0080008; GO GO:0005829; GO GO:0005635; GO GO:0005643; GO GO:0003723; GO GO:0043130; GO GO:0051028; GO GO:0015031; GO GO:0006405; GO GO:0000972; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MATFGAPATANSNPNKSYEVTPSPADSISSLSFSPRADILVATSWDNQVRCWEISRSGASLASAPKASISHDQPVLCSAW SQ KDDGTTVFSGGCDKQAKMWPLLSGGQPVTVAMHEGPIAAMAWIPGMNLLATGSWDKTLKYWDTRQQNPVHTQQLPDKCYT SQ LSVKHPLMVVGTADRNLIVFNLQNPQTEFKRIQSPLKYQTRCVTAFPDQQGFLVGSIEGRVGVHHLDDSQQSKNFTFKCH SQ RDGNDIYSVNSLNFHPVHGTFATAGSDGAFNFWDKDSKQRLKAMSRCNQPIPCSSFNHDGSIYAYAACYDWSKGAENHNP SQ ATAKSSIFLHLPQESEVKAKPRVGATGRK // 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 Q3KP22; PN Membrane-anchored junction protein; GN MAJIN; 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:Q9D992}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D992}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9D992}. Note=In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}. DR UNIPROT: Q3KP22; DR UNIPROT: B3KS99; DR UNIPROT: E9PPE5; DR PDB: 6GNX; DR PDB: 6GNY; DR PDB: 6J08; DR Pfam: PF15077; DR OMIM: 617130; 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:0000250|UniProtKB:Q9D992}. DE Reference Proteome: Yes; DE Interaction: P53350; IntAct: EBI-21493388,EBI-476768; Score: 0.35 DE Interaction: P26998; IntAct: EBI-21493388,EBI-1965681; Score: 0.35 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 MSLKPFTYPFPETRFLHAGPNVYKFKIRYGKSIRGEEIENKEVITQELEVPVEKKAVGAVMRKRKHMDEPSSPSRPGLDR SQ AKIGTSSQGPSKKKPPVETRRNRERKTQQGLQETLASDITDVQKQDSEWGHSLPGRIVPPLQHNSPPPKERAATGFFGFL SQ SSLFPFRYFFRKSSHS // ID Q3KTM2; PN Glycerophosphodiester phosphodiesterase domain-containing protein 5; GN GDPD5; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Endomembrane system {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}. DR UNIPROT: Q3KTM2; DR Pfam: PF03009; DR PROSITE: PS51704; DE Function: Glycerophosphodiester phosphodiesterase that promotes cell cycle exit and drives spinal motor neuron differentiation (PubMed:16195461, PubMed:19766572, PubMed:23329048). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (PubMed:23329048). {ECO:0000269|PubMed:16195461, ECO:0000269|PubMed:19766572, ECO:0000269|PubMed:23329048}. DE Reference Proteome: Yes; DE Interaction: P0CB50; IntAct: EBI-2464239,EBI-2464223; Score: 0.59 DE Interaction: Q06830; IntAct: EBI-2464223,EBI-353193; Score: 0.40 DE Interaction: P35700; IntAct: EBI-444948,EBI-2464223; Score: 0.40 GO GO:0012505; GO GO:0030426; GO GO:0016021; GO GO:0048471; GO GO:0008889; GO GO:0004435; GO GO:0006629; GO GO:0045666; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MVKHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTKWERLWFLILTSSFFLTLVWFYFWWEVHNDYNEINWFLYNRM SQ GYWSDWSIPILVTTAAGFTYITVLLILALCHIAVGQQMNLHWLHKIGLMTTLITTVVTMSSIAQLWDDEWEMVFISLQAT SQ APFLHIGALAAVTALSWLIAGQFARMEKATSQMLMVTAYLAVVVALYLVPLTISSPCIMEKKALGPKPAIIGHRGAPMLA SQ PENTLMSFQKAVEQKIYGVQADVILSYDGVPFLMHDKTLRRTTNVEEVFPGRAYEHSSMFNWTDLEMLNAGEWFLRNDPF SQ WTAGSLSRSDYLEAANQSVCKLADMLEVIKDNTSLILNFQDLPPDHPYYTSYINITLKTILASGIQQQAVMWLPDTERQL SQ VRQIAPAFQQTSGLKLDAERLREKGIVKLNLRYTKVTNEDVRDYMAANLSVNLYTVNEPWLYSILWCTGVPSVTSDSSHV SQ LRKVPFPIWLMPPDEYRLIWITSDLISFIIIVGVFIFQNYHNDQWRLGSIRTYNPEQIMLSAAVRRSSRDVKIMKEKLIF SQ SEINNGVETTDELSLCSENGYANEMVTPTDHRDTRLRMN // 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 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 Q3SYC2; PN 2-acylglycerol O-acyltransferase 2; GN MOGAT2; OS 9606; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000269|PubMed:12621063}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}. DR UNIPROT: Q3SYC2; DR UNIPROT: A8K7I3; DR UNIPROT: Q3SYC1; DR UNIPROT: Q6ZQZ2; DR UNIPROT: Q86UH6; DR UNIPROT: Q9H630; DR Pfam: PF03982; DR OMIM: 610270; DR DisGeNET: 80168; DE Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:1990578; GO GO:0003846; GO GO:0016407; GO GO:0006651; GO GO:0006071; GO GO:0050892; GO GO:0019432; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIW SQ KYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFANLCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGL SQ VTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG SQ SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHK SQ LKFNIPADQHLEFC // 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 Q3T0A9; PN Protein shisa-5; GN SHISA5; OS 9913; 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 {ECO:0000250}. DR UNIPROT: Q3T0A9; DR Pfam: PF13908; DE Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0031965; GO GO:0042771; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MAAPAPAPRILVLLLLLLPAPEGAQSELCMISHGRKVDPWVCPDFCCGNCNDQYCCSDVLKQVMWIEEDCHAPEASILTD SQ DFDSGFDSDPVARFGTVIAIGVTLFVIAVVTVIVCCTCSCCCLYKMCRRPQPVVTTTMATTVTHTPYLQPPSYPGPTYQG SQ YHSVVPQPGMPTAPYPTQPTGPPAYHETMAGGAALPYPASQPPYNPAYMEPPKAVP // 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 Q3TA38; PN Transmembrane protein 120B; GN Tmem120b; 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:26024229}; Multi-pass membrane protein {ECO:0000255}. DR UNIPROT: Q3TA38; DR UNIPROT: Q14BK6; DR UNIPROT: Q8R243; DR Pfam: PF07851; DE Function: Necessary for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229}. DE Reference Proteome: Yes; GO GO:0016021; GO GO:0005637; GO GO:0045444; GO GO:0051291; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELTSLQTLCSTSISKQKRHLKDLKHTLQRYKRHSSHEEAALIQQMT SQ ANIKERQNVFFDMEAYLPKKNGLYLNLVLGNVSVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVF SQ NFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGLIYQKFRNQFLAFSIFQSCVQFLQYYYQRGC SQ LYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSTHEECKEWQVFVLALTFLILFLGNFLT SQ TLKVVHAKLHKNRNKTKQP // 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 Q3TUD9; PN Transmembrane protein 18; GN Tmem18; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96B42}. Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}. DR UNIPROT: Q3TUD9; DR UNIPROT: Q8CID7; DR Pfam: PF14770; DE Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0016021; GO GO:0031965; GO GO:0003677; GO GO:0016477; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MSSAYSVRSFPVSIPAVIMETDWTEPWLLGLLAFHLLCLLLTCFSSQRYKLQIGHFLCLVVLVYSAEYINEVAAVNWRLF SQ SKYQYFDSRGMFISLVFSAPLLFNAMLIVIMWVRKTLTVMTDLKTLQEERKERRRRRKEE // 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 Q3U5C7; PN Prickle-like protein 1; GN Prickle1; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}. DR UNIPROT: Q3U5C7; DR Pfam: PF00412; DR Pfam: PF06297; DR PROSITE: PS00478; DR PROSITE: PS50023; DR PROSITE: PS51303; DE Function: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure (By similarity). Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005829; GO GO:0031965; GO GO:0005634; GO GO:0008134; GO GO:0008270; GO GO:0035904; GO GO:0060976; GO GO:0090090; GO GO:2000691; GO GO:0045892; GO GO:0001843; GO GO:0032436; GO GO:0031398; GO GO:0006606; TP Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250}; SQ MPLEMEPKMSKLVFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHD SQ NEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAVMHAVCEQCGLQMNGGEVAVFASRAGPGVCWHPSCFVCFT SQ CNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCC SQ GCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDIHASDSSDS SQ AFQSARSRDSRRSVRMGRSSRSADQCRQSLLLSPALNYKFPGLSGNADDTLSRKLDDVSLASRQGAGFANEEFWKARVEQ SQ EASEDPEEWAEHEDYMTQLLLKFGDKNLFQQQSSEVDPRASEHWIPDNMVTNKPEVKPNHQGLASKKYQSDMYWAQSQDG SQ LGDSAYGSHPGPASSRRLQELDLDHGAAGYTHDQSQWYEDSLECLSDLKPEQSIRDSMDSLALSNITGASVDGESKPRPS SQ LYSLQNFEEIEAEDCEKMSNMGTLNSSMLHRSAESLQSLNSGLCPEKILPEEKPAHLPVLRRSKSQSRPQQVKFSDDVID SQ NGSYDIEIRQPPMSERTRRRAYHFEERGSRPHHHRHRRSRKSRSDNALNLVTERKYSAKDRLRLYTPDNYEKFIQNKSAR SQ ELQAYMQNANLYSQYAHATSDYALQNPGMNRFLGLCGEDDDSWCSSSTSSSDSEEEGYFLGQPIPQPRPQRFTYYTDDLS SQ SPASALPTPQFTQRTTKSKKKKGHKGKNCIIS // 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 Q3U9G9; PN Delta(14)-sterol reductase LBR; GN Lbr; 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:18785926}; 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: Q3U9G9; DR UNIPROT: Q3TSW2; DR UNIPROT: Q811V8; DR UNIPROT: Q811V9; DR UNIPROT: Q8BST3; DR UNIPROT: Q8K2Y8; DR UNIPROT: Q8VDM0; DR UNIPROT: Q91YS5; DR UNIPROT: Q91Z27; 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 (PubMed:18785926). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (PubMed:22140257). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (PubMed:22140257). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000269|PubMed:18785926, ECO:0000269|PubMed:22140257}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0005637; GO GO:0005652; GO GO:0031965; GO GO:0005643; GO GO:0005634; GO GO:0051087; GO GO:0070087; GO GO:0050613; GO GO:0003677; GO GO:0070402; GO GO:0008139; GO GO:0016627; GO GO:0006695; GO GO:0030223; GO GO:0016126; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MPSRKFVEGEVVRGRWPGSSLYYEVEILSHDNKSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSISSSPSRRRGSRS SQ RSRSRSRSRSPGRAPKGSRRSVSASHEGDVKEKKEKEMRREILQVKLTPLVLKPFGNSVSVYNGEPEHMEKNATPYKDKQ SQ ERIILSTEDRYIVTQYSLRPRREEVKAKEIESEEQNLVTKGPAPLGTFQVTTPQRKDLEFGGVPGAVLIMLGLPACVLLL SQ LLQCRQKDPGLLHFPPPLPALHELWEPRVCGVYLLWFFVQALFHLLPVGKVAEGTPLVDGRRLQYRLNGLYAFILTSAAL SQ GAAVFWGVELCYLYTHFLQLALAATGFSVLLSAYLYVRSLRAPREELSPASSGNAVYDFFIGRELNPRLGAFDLKFFCEL SQ RPGLIGWVVINLVMLLMEMKIQERAAPSLAMILVNSFQLLYVVDALWNEEALLTSMDIMHDGFGFMLAFGDLVWVPFTYS SQ LQAFYLVSHPHDLSWPLASVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIHTSTGKSLLVSGWWGFVRHPNYL SQ GDLIMALAWSLPCGFNHLLPYFYIIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY // 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 Q3UJ81; PN Nuclear envelope phosphatase-regulatory subunit 1; GN Cnep1r1; OS 10090; 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}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}. DR UNIPROT: Q3UJ81; DR UNIPROT: A7E1Z4; DR UNIPROT: Q8VEG8; DR UNIPROT: Q9D3Q4; DR Pfam: PF09771; DE Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which 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 (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005829; GO GO:0016021; GO GO:0071595; GO GO:0031965; GO GO:0006629; GO GO:0035307; GO GO:0010867; GO GO:0034504; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL SQ FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ // ID Q3UY34; PN Protein CUSTOS; GN Custos; OS 10090; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. DR UNIPROT: Q3UY34; DR UNIPROT: Q3TX98; DR UNIPROT: Q8K0K9; DR UNIPROT: Q9CVB7; DE Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. DE Reference Proteome: Yes; GO GO:0005635; GO GO:0007275; GO GO:0030178; GO GO:0060061; GO GO:0016055; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MVAPSGAMSDSENSSSSSSDAEELARCREAATPAWGLEQRPGAAERPEAGAADKQAPTPQPSRRHEVNQHEEDGNDLRTT SQ PEFRAHVAKKLGALLDSSIAIAEVWKKSQKAKMQQVAKEEDGFRLFFTSIPGGHKKEASPRPCRKRQPPSSSEDSDEELQ SQ RCREAAVSASDILQESAIHCPAKAEEKKKLKKKAKKKVDNADLAAAPGLEQVKEAGVVNGDPVSLGIQKKRKKKAKKSRE SQ APLCPPAECAAAKPEN // ID Q3V2A7; PN Glutamine-rich protein 2; GN Qrich2; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane {ECO:0000269|PubMed:30683861}. Nucleus {ECO:0000269|PubMed:30683861}. Cytoplasm {ECO:0000269|PubMed:30683861}. 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:0000269|PubMed:30683861}. DR UNIPROT: Q3V2A7; DR UNIPROT: B9EKM0; DR Pfam: PF16043; 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 Reference Proteome: Yes; GO GO:0005737; GO GO:0031965; GO GO:0005634; GO GO:0036126; GO GO:0030031; GO GO:0030317; GO GO:2000059; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MENSVSEASLYLQDQLDKLRTIIESMLGSSSTLLSMSITPHKSTACLVPGQIDPEATCPACSLDVSHQVSLLVQRYEQLQ SQ DMVSGLAASRPSKKAKLQGQDEELLGHVQSAILQVQGDCEKLNITTSNLIEDHRQKQKDIEVLYQGIERLDKEKANREHL SQ EMEIDEKADKSALASKVSRIQFDATTEQLNHMMQELVAKMSGQEQDWQKLLDKLLAEMDSKLDRLELDPLKQMLEDRWKS SQ LRQQLKERPPLYQADEAAAMRRQLLAHFHCLSCDRPLETTVTGQVISVTPIISSMPGHRSVRPYTVFELEQIRQQSRNLK SQ LGSSFPRVDMSQMERSVGRLHSMHSRMLMDMEKVQVHFGGSVKASSQMIRELLHTQCLSHPCYKRGADTADYSYSTVSRR SQ CGGSHTLTYPYRRNRPQHLSPLEEIQIAMKHDEVDILGLDGHIYKGRMDTRLPGILGKDAPGVTKHNKAKLQQLQQLQQL SQ QQLQQLQQLQQAQHARPHAHRQPSLGNMISPPSRPQSAQMIADSKAVPSGQKKDRPVSSEGRLLQSNVSHSSIPTDIASL SQ QGSQQGLNMHIDVPPGEGLEEPTRGPRSTAAH // 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 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 Q3ZC61; PN MORF4 family-associated protein 1; GN MRFAP1; OS 9913; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}. DR UNIPROT: Q3ZC61; DR Pfam: PF15155; DE Function: DE Reference Proteome: Yes; GO GO:0005634; GO GO:0048471; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MRPLDIVELAEPEEVEVLEPEEDFEQFLLPVINEMREDIAALSREHGRAYLRNRSKLWEMDNMLIQIKTQVEASEESALN SQ HLQNPDDGAEGRGTKRCEKAEEKAKEIAKMAEMLVELVRRIEKSESS // 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 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 Q4HY71; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 229533; 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: Q4HY71; DR UNIPROT: A0A0E0RW04; DR UNIPROT: V6RQB4; 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:0005737; GO GO:0031965; GO GO:0005643; GO GO:0005524; GO GO:0003723; GO GO:0003724; GO GO:0051028; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MADLASRITKPDEVAAETPAETPAETAPAASGELGQADGNIEDLGGSGLQEPEWDVEVSLSELQNNEATPFHSATTWQDL SQ GLREDLLKGLLSLNFLKPSKVQGKSLPLMLSDPPRNMLAQSQSGTGKTAAFVTAILSRVDFSKPDQPQALALAPSRELAR SQ QIEGVINAIGRFVENKKVAAAIPGVLPRGEPVRASVIVGTPGTVMDIIRRRQLDISQLRVLVLDEADNMLDQQGLGDQCL SQ KVKNMLPKEIQVLLFSATFPENVMKYAGKFAPNAHSLKLQRSELTVKGISQMFIDCPDDNMKYDILCKLYGLMTIGQSVI SQ FVKTRDSASEIERRMVADGHKVSALHAAFDGAERDNLLTKFRQGENKVLITTNVLARGIDVSSVSMVINYDIPMKGRGDT SQ EPDAETYLHRIGRTGRFGRVGVSISFVYDKKSFDALSKIAEMYGIDLVKLDTEDWDEAEERVKEVIKKNRAQASYAPSAT SQ EPKAAAGA // ID Q4P7Z8; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 237631; 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: Q4P7Z8; DR UNIPROT: A0A0D1E0C9; 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 MSESKDKTTAPAADSNVNEIASGISGLLSSKDVAESNLRESSHEVQVTLADQQADPNSPLYSAKSFEALGLHENLLKGIY SQ AMKYQKPSKIQEKALPLLLQNPPKNMIGQSQSGTGKTAAFILTMLSRIDYDLQKPQAIALAPSRELARQIMDVARTMSKF SQ TNVTTCLCLPDEVKRGEKITAQLIIGTPGKTFDMIKSKGIDTAAIKVFVLDEADNMLDQQSLGEQSIRVKNTMPKSCQLV SQ LFSATFPTNVYDFAVRIAPGANEIRLKQEELSVEGIKQFYMDCKDEDHKYEVLVELYNLLTIGQSIIFCAKRETADRIAQ SQ KMTQEGHKVDSLHGRLETADRDRTIDAFRDGKSKVLISTNVIARGIDIQQVTLVINYDMPLTQTGEADAETYLHRIGRTG SQ RFGRKGVSINFVHDQQSWSYMDQIEKALKCQITRVATNDLEEMEYTIKEALKQIGK // 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 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 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 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 Q4R914; PN Calcium-binding and coiled-coil domain-containing protein 2; GN CALCOCO2; OS 9541; 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: Q4R914; 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 MEKTIEDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCRYTFTQNFIPRQKDWIGIFRVGWKTVREYYTFMWVTLPID SQ LNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELK SQ DSCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETEQLEHLKKENGHLFLSLTEQRKDQKKLEQTVEE SQ MKQNETTAMKKQQELMDENFDLSRRLSEKKMIYNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGA SQ GQNPGLVYGNPYSGIQESSSPSQLSIKKCPICKADDICDHTLEQQQMQALCLNCPICDKIFPATEKQIFEDHVFCHSL // ID Q4V882; PN Epsin-3; GN Epn3; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus {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: Q4V882; DR Pfam: PF01417; 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: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 IGSGQLGFSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAEKGGRSWKGDDFPVANGAEPAG SQ QRRRDREPEREERKEEEKLKTSQSSILDLADVFAPAPALPSTHCSADPWDIPGLRPNTEPSGSSWGPSADPWSPVPSGNA SQ LSRSQPWDLLPTLSSSEPWGRTPVLPSGPPITDPWAPSSPTPKLPSTGVDPWGASVETSNTSALGGASPFDPFAKPLEST SQ EPMESRDSAQALPKGKSPSPVELDPFGDSSPSCKQNGVKETEALDLGVLGEALTQQPGKEARPCRTPESFLGPSASSLVN SQ LDSLVKAPLAARTRNPFLTGLSAPSPTNPFGAGEQGRPTLNQMRTGSPALGLPPGGPVGVPLGSMTYSASLPLPLSSVPV SQ GATLPASVSVFPQAGAFAPPPASLPQPLLPTSDPVGPLPPQAGTNPFL // ID Q4V9F0; PN Diacylglycerol O-acyltransferase 2; GN dgat2; OS 7955; 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: Q4V9F0; 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 (By similarity). {ECO:0000250|UniProtKB:Q96PD7}. DE Reference Proteome: Yes; GO GO:0005789; GO GO:0016021; GO GO:0005811; GO GO:1990578; GO GO:0004144; GO GO:0006071; GO GO:0055088; GO GO:1905897; GO GO:0061959; GO GO:0019432; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MKTILAAYSGVKKGSGSSILSALHDLPTVPWLTRSKMVKHLQVISVLQFIMTFLTMGIACSLLLMYMFCTDFWVISVLYV SQ AWLIYDWNTPGQGGRRSTWVRDWTVWKYMRDYFPIRLIKTHNLLPSRNYIFGYHPHGILCFGAFCNFGTEATGFTKVFPG SQ IKPSLATLAGNFRLPMFREYLMCGGICPVNRNSIDYLLSSNGTGNAVVIVIGGAAESLDCAPGRNSVMLKKRKGFVKLAL SQ KQGADLVPVYSFGENEVYKQLIFEEGSWWRTIQRKLQKFLGFAPCLFHGCGLFFPESWGLVPYCKPITTVVGEPITVPKI SQ EEPTQDVIDMYHAMYIRSLKSLFDNYKTRFGLNESDTLIIH // ID Q4VBT2; PN Nucleolar complex protein 4 homolog; GN noc4l; OS 7955; 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: Q4VBT2; DR Pfam: PF03914; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0030692; GO GO:0031965; GO GO:0005730; GO GO:0032040; GO GO:0042254; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MAPSGDSNVKEHNNQVSYKKAINTKTDLILQNKKHANDIFDVIEYLQSEKEKEIIFATNACSKIFCELIERGDLFVGELP SQ KEEDLAQGDRSAEEKYHIFMRHRYNSCVELMLENVSHESFQVKETSLCAVMKFVATEGKHPLQNLDWSEHYNFPRELIQA SQ LVEHLLSEKEDMSLLISRFQEFMEKDDVRYYVMSSVRYSTATVMERNKKAVIPVFQNNVFNLLTTINIPNQASEMTNFLV SQ QQQSKHDDWKAAKLKEHKRAFEQMWLLFLRYKLPGSMYKKILVILHESILPQMSDPKLMMDFLSAAYDIGGAISLSALNG SQ LFVPIHEHNLDYPDFYKKLYNLLDPSIFHVKYRARFFHLANIFLSSTHLPVYLVAAFVKRLARLSLTAPPTALLILLPFI SQ CNLIRRHPSCRVLIHRPSAADEPCDDPYVMEEEDPAQCHALESSLWEIKTLQNHHHPDVSKAATMINEPLSAQEEDISEL SQ LELTTFELMERELKGEKKTVPLEFDMATDLLKSSREVLGVHFTLE // 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 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 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 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 Q54C85; PN Importin-13 homolog A; GN ipo13A; OS 44689; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. DR UNIPROT: Q54C85; DE Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005635; GO GO:0008536; GO GO:0006606; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MYNNNGFHEETNIDESQFTVEKVETVLKSLYFPQNNDYSALPQIQQWLIQFQKSFSSWSIAPLLLMSNIKEIQYFGASTI SQ ENKIKNNWLSLSQDMKKEFLDNLLLFLKTQITKCSTVVITRLCLAVSVIACHSTTDLWANPILDVLQLSFQDINNLDCFN SQ PNLVNLTLELLTIFPEELTNADYITQEKRNKVGLQFNKHNSKVFEILCKIMSLPQNQQTLIFMKSSLKCFKSWILFDCSP SQ REYLIDSDLILKCFEAVSNNPKLVEDFLMVLDEMFTFMGGKIFRSYTSAFSLVLSRILMIFPSFYILALQEENQIFNQIF SQ LLFSHIAENHIKTLLKNPELSNNFFKALIQMALKGDFETCELLSPVITEIAALHELHSTSSTTEATTTTIATTTTPTTTS SQ DCDISGWYQYLGEMVEVFRLKSMYPLDKDISDLYEEDAEKFFAFRVIAGDSVLEVYNILEGKILQQLLNSLWSDIQSFPT SQ TKCWQSIEATIYLLSCLSESITEDTEFVPQLFSILGQLPIQSTPLIKSTMTLAGNYSNLIDKSTIFLEKIVKDFFPAFEN SQ PDLKSVASQSFLSISKNSKCASILSNSITQLISLCAPILSNNNKILDDPSNFNILEALLYIISTLPSDSQVLNYSTQLLY SQ PFILFIKNYYTNQLQQQQQQQQQQQTELRLLLSSINLLTKFCKIYDDEQVNEYGTTQQENNNNNNNNNNNNNNNNNNNNN SQ NNNNNIKPVFEIINNIIPIYGELLSLNTLESSIIEAISIFYKKAIMINNNHQNITNIPEINRQLTLAFLKHKPLSLVLST SQ LSISIVNLPKEQHLDFLADSLSSISSKMIQIWSEKSNQNNKKNNKKINNNIDIDNDNENNNNNNQIQFENNELNEFKNLK SQ ISIYPDITKEYFTMITQYIRYNAVSIPQGVISHLFSIILVNITKIHDKVTARACFSFMALIITKSKEMKSQIKWEPLLNE SQ INGWLSIHGELFIKQILYSAGGGIPRSVVQFISEVIASLVSSYPDVFRISALKCLSVDGFPSSNITKEQKEKFLNSLMLY SQ RSKKLPLKIVTDFSLVSLGIATNQ // 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 Q54DS8; PN Protein SEC13 homolog; GN sec13; OS 44689; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. DR UNIPROT: Q54DS8; 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. {ECO:0000250|UniProtKB:P55735}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. DE Reference Proteome: Yes; GO GO:0030127; GO GO:0005829; GO GO:0005789; GO GO:0000139; GO GO:0005765; GO GO:0005643; GO GO:0031080; GO GO:0005198; GO GO:0090114; GO GO:0006888; GO GO:0051028; GO GO:1904263; GO GO:0015031; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735}; SQ MATQNVDSGHEDMVHDAQFDYYGKFLATCSSDKMIKIFDVGGENPQHLVDLRGHEGPVWQVAWAHPKFGKILASASYDRK SQ VIVWKEVGNNSWSIIHQYAGHELSVNSISWAPHEFGLSLACASSDGSVTIHNYNNNVWEAPQKIQVSQIGVNSVSWSPAA SQ IPTSLVNSANTIIPAPIKRIVTGSCDNLIKIFKNVEDKWILDKQLEDHKDWVRDVAWAPNIGLPYSKIASCSQDRSVIVW SQ TQDENGVWSGKPLPKFDDIVWRVSWSVIGNILAVSCGDNQVTLWKEGVDSEWKLISHVENN // 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 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 Q54EV7; PN Exportin-1; GN xpo1; OS 44689; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. DR UNIPROT: Q54EV7; DR Pfam: PF08767; DR Pfam: PF18777; DR Pfam: PF18784; DR Pfam: PF18787; DR Pfam: PF03810; DR Pfam: PF08389; DR PROSITE: PS50166; DE Function: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES). DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005634; GO GO:0048471; GO GO:0005049; GO GO:0008536; GO GO:0006611; GO GO:0046825; GO GO:0000055; GO GO:0000056; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MENILNFNEPLDINLLDQIVSVLYNPLSNKNDIKAAQMVLGKFQEHPDAWSKVDTILETSKIVQTKFIALVIMDSLIKYR SQ WKSLPREQCEGIKNYIVSLIIRLSSDPQTSSREKLLVNKLNLVFVQILKQEWTTNWSTFIPEIISSSKTNESLCENNMVI SQ LRLLSEEIFNFSEEQMTQTKIQTLKITFEKEFSLINDLCFYILENATRASLIKATLETLQRFLNWVPLHYIIEVNGGIAE SQ PSKLVKLLLHKYFPEPLFRNSTLKCLTEIGNLNLGNQQYDAVFIAIIDKFMNQIKFIKPDPSKIPQDYEDGDQGERSFIH SQ TVSLFLTGFFKSHLKIMENSLNIPYLTLAHEILVNISNIDELELFKICLEYWNFLSSNLYSDIATFTTTLLSTPPRLQLY SQ KSVLSKVRVVLIDHMAKPEEVIVVEDENGNIVRETTKDTDSLTLYESMRETLIFLTHLDSENTQHIMLEKLQTLISGREF SQ TFQRLNTLCWAIGSISGAQNKEQEKRFLVTVIKDLLELCQNKKGKDNKAVIASDIMYIVGQYPRFLKDHWKFLKTVVNKL SQ FEFMHESHPGVQDMACDTFLKISKQCKRKFVVLQVEESQPFINELLNQLSTTIAHLEQSQIHTFYEAVGYMIASSSDAAF SQ REKLVNKFMELPNHSWLQIMGAASVKVESLLTVEVARDILNLIKTNNRAAMSLENCYITQISKIYLDLLNVYRTYSDHIS SQ RNPNIYRETLGQAMRSVKKETLKLLETFIEKSSDKQVIYSNFLQPLLEAVLGDYRTNIPETRDPEVLSLMTAIITSLKQL SQ VHPEVPKILEAVFETTLSMITKNFEDYPYHRINFFNLIRAINSNAFTVFHNLHPQQFKLLIDCVVWAFKHTERNISETGL SQ HILKELIENVSKNSDVANVFFKTYLVSLLNDILYILTDSFHKSGFALECDILRMMFQVVENGVVKIPLFDPQQANFPSNS SQ EYVKEIVVTFLSASPNVSRPQIQAFVTRLFNLANINNNDFKSATRDFLITLKEWKSHENADLYSDEKNIEKALALKKQSM SQ IPGMVRPNDVNLEMNDL // 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 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 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 Q54RV6; PN Trafficking protein particle complex subunit 2; GN trappc2; OS 44689; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. DR UNIPROT: Q54RV6; DR Pfam: PF04628; DE Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005794; GO GO:0048471; GO GO:0006888; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSTFTFLIIGKNDNPLYEIEFPITVQKKETYVLQYIAHGSLDIVEEHVWKSNNMYLKIIDKFNKVQISSFVTAGHIKFLL SQ LHEKKDEDAIKNFFVEVHDLYLKILLNPFYEYNKPITSTAFDAKVRKIGTKYF // 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 Q54VZ8; PN Exocyst complex component 8; GN exoc8; OS 44689; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. DR UNIPROT: Q54VZ8; DR Pfam: PF16528; 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:0042995; GO GO:0000145; GO GO:0048471; GO GO:0006887; GO GO:0006893; GO GO:0008104; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MKKGVTYPLKIDTNLSTVSSSVNYNDIECVDIKSNGHYIVKFMYREWVGPLNLMTTQKTSIKISIDLKEQTVTCTHTDKK SQ KTVYRWGEFPNKKETEQNKKEDNPVQYETFLSSNFNSEKYVNDLFTHKTDQQATVHLQYLENRKLGCIDHLKKDVYKNHL SQ IFIGASKEIANSEVDMLDFRNLISDYGNVMSSLQNISISWDHYKVKKSGKIDFEPLSPATEPIQWLTTAPNELSVSIEQR SQ EFEVAVGLVEKINKIYESNPKVEIVMQTHPLKDQIENKVKILTDKLMNELRSPLLKANQIKDTISLLVRLSQNDKAKSIF SQ LESRSHSINQAIKKIVFSGDLNRFIGELARVIFNSINSTCNDFTNSFPSYMNSGLVSWIIEELVLISDIFNRQVFILDNF SQ YSISQAIRIIESHCEMMDQTGLSIGFYWNLLLQPHVEQLIVNYEIKIRDSMLHQLMDEKWNGVSNWDYEVKSQLNSLPSS SQ LKNSGTPNSGGSGISNNNSNNNNNYQSPIINNNFNSGGGNKKIGLTFQQMHQDNLNNMEDIDQGRLKLTSSTIFLNTIIQ SQ KFAIDICQIITIDLIPVISQSLGSIFKDYMSYLKNEIQKEYLSDTQCLAIISDSVYIVDDLVSRIATRFEDATGEKLNNL SQ TQLSSLLYSYFESIRDQYSTRKALELVDNSMNWEEQEYQVEEELDPFPKNFIVLSEALDRLAESIQTNVNVESVLPIASR SQ IISEIVNIISNRFESTSNLVFGYGGLQHFILEMKYLATFAGKYPVEDSTFELINTMIRNHKEIYLNNTSDPKPLKTEEYF SQ TSIIDNLVYQKAVYN // ID Q54WT9; PN Importin-13 homolog B; GN ipo13B; OS 44689; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. DR UNIPROT: Q54WT9; DR Pfam: PF03810; DE Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005635; GO GO:0008536; GO GO:0006606; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MNTNAMDQYENCPSYGSFDVKSFSDSPIPFTNNNNNNNNNNNNNSICVMPSNYNNKNNNNNNNEKLEPEATLDVLTHALH SQ TLYKSNDSNQRKLAEKWLILFQKQPIAWEFCPRLLLETNIFELQYFGASTLESKLKNEWNECNVEMKSKILNTIVSIIQN SQ STKLPICCVTRVSVTLTIAVMYTFPEIWRNAIFDIIHLSIKQDINTLSLHDPSQNHFNTDRLLMVLEFLSILPDELKKQD SQ LALCKYSEIQKELKLIIDKIYKFLLSVLFLPINENFEFIKISYKALSAWLKYMLPSNGTMLQSCFEISFTVGQQKVSNNS SQ NGNGNGNNNNNNNRNSIGYPLIDSLALVLEGSSLSIEGQSNGSCYIEAFRYAIEQSLTIFPTFYNEATVMNQDDSKAKPI SQ FNVFVQFISSNNSQLFTTDLIHRCLNLLISFIEIGSRETISLLFYLIDDFKTHTMLVQQDQNILKFFFLKLLNRFLDVSM SQ YPNGKDYCPIENGTNPLSTSQNAQFNGVLCETNIETLLDDDIEQFRSCSSDCLMNIQENDIIPKSTFLKFLIEKLNAFIN SQ EKCPHWEQYESILYYIYAFSGGSQDGQLEYVPILLNIIPLIPIKSIPLVRTSIKLIGRYSSFLKTNTDYLAKVVSDLLPA SQ LSHAELIGSAASSLLSICVSDKCSTMLWPHFNQILDQIEPILLGPQKSNPSIVLVYKSLLHILHKAPIHELSPLFTRLIS SQ PVIPNITDHIPRVKSKDHYNQLLVQLSILYSVNEIIEYDEFATMGANGEFTSPSKHPLYPFFQTTIPIQGQLLKHYKSEF SQ EIIDCITTFYRYMMLYFREIANDFVDEILQQATQSFNQYPIASLLQIISSIIIPKLQPLTITNIKNSISLISNTFINTLK SQ SVILATNNNNKNNDNTNNNDDNNNKNDNNNNNNNNDNDKSNFILDFTITPDITKDYLILITKILKTSPQCIEPNIISTIC SQ IYIIYNLTDLTKDKPTTGNCCLFLTNCLSLNNGKLQISDPNGNKVLEQIKNEMNALFESDPKHSYVLVYNILMNICWTPT SQ SIQVTQHFSDVLLSFAIGYPNLLKLHATNILNDPNFIKDKQINPHDKQSFLTNILKSNSTQVDYRSSVRTFSFICNDKE // 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 Q557F4; PN Probable importin subunit alpha-A; GN DDB_G0273595; OS 44689; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. DR UNIPROT: Q557F4; DR UNIPROT: Q869V5; DR Pfam: PF00514; DR Pfam: PF16186; DR Pfam: PF01749; DR PROSITE: PS50176; DR PROSITE: PS51214; DE Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005829; GO GO:0005643; GO GO:0005654; GO GO:0061608; GO GO:0008139; GO GO:0006607; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMEN SQ KIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQ SQ TQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIG SQ LIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLE SQ YPDSIVFTPALRAVGNIVTGESSQTQIVIDNNGVELITRLLAVQKKSIRKESCWALSNITAGEPSQIDVVVSNPKTVTTL SQ ISLLSHSEHDIKREACWALSNSTNNSSTKSIQTLVRHNILKHFIDLLNSQDLVILKIVLEGLINIIKEGEKTKTKTGVNP SQ YVNLISEMQGESIIYDLQEHQSKDVYKKAFELIEFFESSDYSDSENSEPNINQNGQYEFSSNYNSNSINI // 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 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 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 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 Q55DA6; PN Probable 18S rRNA (guanine-N(7))-methyltransferase; GN DDB_G0269722; OS 44689; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. DR UNIPROT: Q55DA6; DR Pfam: PF08241; DR Pfam: PF12589; DE Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity). {ECO:0000250}. 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. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA- modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. {ECO:0000250, ECO:0000250|UniProtKB:O43709}. DE Reference Proteome: Yes; GO GO:0005730; GO GO:0005654; GO GO:0048471; GO GO:0016435; GO GO:0070476; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSRPEHIAPPEIFYDDVESKKYSSNSRIIEIQTKMAERAYELLAIPETAEGLMLLDIGCGSGISGDVITDAGHYWIGCDI SQ SQHMLDVAIDREVEGDVMLRDIGQGFPFRAGSFDAAISISAIQWLCNAEKSHHNPRKRLHTFFQSLFNVLTRGGKAILQF SQ YPENSAQIEMITASALRCGFSGGLLIDFPNSSKAKKYFLVLFTGNNNIMPSAKGVEGEEYEQQEEEDSNEVKYSNRKRDR SQ RRVTKSKGSAQHKTKEWIMNKKDRQRKQGREIKNDSKFSGRKRGPKF // 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 Q567X9; PN Inositol 1,4,5-trisphosphate receptor-interacting protein; GN itprip; OS 7955; 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: Q567X9; 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; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MQGAIARVCMVVVAAILNHPLLFPNENTTVPEQDEDLLARMKEHQEKLEAEQKRLEQEISQNETSVIGDQDGYGWYFWSA SQ LCLVIFFTIEVCRQDLISAEIPDPAEDEDGDCSTGYHSAKSIALDRGTLNNFCKTRFFPYTNESGRVREFIEGFADDLLE SQ ALRSICDLKADLEVEDFAGIGSMFESWRVSKPPTCDLIVPFSPPQPLRFQFELWCDPSTEIPLDLQGCGRIQLIKPGGNG SQ TDCLCGSIDLGDDMLCLLHNRNECEVLEDDALPELLCARDTTYLSKGQIMRWFQISVSKAWGKISHKYDFELAFRNLDFP SQ GALKIKFPSGKTVVLNLTPAVQFENTDAYLISHFPSDTSNSSDTHWQLSLSVYEKNLLKHLAKSLPTNSCHIHCLQIVAF SQ LHKKQTTLTGRSAFCNYHIKTALLHLLLSKRPAMWQPQNLDSRLRDLLSFLQQSLEEKKLYHALVGNPRIPVEILVPKII SQ RTAEPINLYRPLVLQRHVYAKMEEHFEEMVRNTSVLVQEYTPHFSNGHVRHEFSSAEQI // 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 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 Q5A5N6; PN UDP-N-acetylglucosamine transferase subunit ALG14; GN ALG14; OS 237561; 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: Q5A5N6; DR UNIPROT: A0A1D8PIT0; 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 MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWI SQ YTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILF SQ LYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI // ID Q5AA50; PN Nuclear protein localization protein 4; GN NPL4; OS 237561; 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: Q5AA50; DR UNIPROT: A0A1D8PDQ6; DR UNIPROT: Q5AAD8; 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 MSSIILRFRSKDGMFRITTDSSSNFTLVLEQLIEKLSQSGNNGNGNGNNNKIDLQSLTIANKPQDKGKSSYEFQNQTVNE SQ LGLKNGDMLYVNYESVTNDSGPTTTATNTTTNTASGNTIPITGPVPSIPINSVVTSHGPLKVEELPIDQELDKEDGLITR SQ PLSSMCRHGPKGMCEYCSPLPPWDENYRKDHAIKHISFHAYLKQQLEKLKSSGGSYFPPLDPVDYSIDLTCNQGHKPYPN SQ GICSKCQPSPITLQLQKFRMVDHLEFADSFILNDFINVWRVSGVQRFGYLYGRYAKSEKTPLGIKAIVETIIEPPQHDEL SQ DGITLLDWDQQEEKMVDQVANKFGLYKVGIIFTDLTDAGTKNGKVLCKRHKDSYFLTNLEIIMAAKFQLKYPNISKYSTA SQ KNNGQFSSKFVTCVISGGLNGEIEPRSYQVSTSAEALVKADIITGCTQPSQIYVNESNNHRYVPDIQYSKINKYGLEVKS SQ NAKPTFPGEFLLVSLTDSFPLQPTPIFTNSYVIENREFLGDENHDIQSLKTLHNYLKSNNDQIFNFHFILHLIKTHILND SQ QEIDLLIEYIKSKNLEDYLKLVESNGWMTLMTILEQSV // ID Q5AJD0; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 237561; 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: Q5AJD0; DR UNIPROT: A0A1D8PJB3; 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 MSSEKVKRVEADATDLLASLSIDKSGEKLEEIKKGSTPDPSDLLGGLSLKEGDSKKPEEKKEVVEEPENKEINDDKKDED SQ KKDESKDEVKDGDGAKEETKEEVKEESKEEPKEPKEPKEPATNLIKSSYEVKVKLADIQADPNSPLYSVKSFEELGLSPE SQ LLKGLYAMKFNKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFSLTMLSRVDPTIKMPQCLCLSPTRELARQTLEVI SQ TTMGKFTNITTQLVVPNAIPRGSSVNAQVLVGTPGIAIDLIRRRQLNLSKMKVFVLDEADNMLEAQGLGDQAIRVKKALP SQ RGVQLVLFSATFPTEVREYAERLVPDANSLELKQEELNVDGIKQLYMDCRSEQHKFEVLCELYGLLTIGSSIIFVEKKET SQ ADVLYGKMKKEGHTVSVLHGGLDNTDRDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDMPTDKYGKPDPSTYLH SQ RIGRTGRFGRVGVSISFIHDRRSYDILMAIKAYFGNVEMTRVPTDDWDEVEKIVKKVIKS // ID Q5EE04; PN Nucleoprotein TPR; GN tpr; OS 8355; 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, ECO:0000269|PubMed:9531546}. Nucleus envelope {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9024684}. 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=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Localized to the nuclear periphery and in intranuclear spheroidal structures. Localized at NPC- attached intranuclear filament bundles projecting into the nuclear interior (PubMed:9024684). Colocalized with nup153 at the nuclear pore complex (PubMed:9531546). {ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9531546}. DR UNIPROT: Q5EE04; DR UNIPROT: P79992; 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. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters. May play a limited role in the regulation of nuclear protein export. May be involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, may act as a spatial regulator of the spindle-assembly checkpoint (SAC) response (By similarity). {ECO:0000250}. DE Reference Proteome: No; GO GO:0005737; GO GO:0005868; GO GO:0019898; GO GO:0000776; GO GO:0072686; GO GO:0042405; GO GO:0031965; GO GO:0034399; GO GO:0005643; GO GO:0044615; GO GO:0003682; GO GO:0031072; GO GO:0051019; GO GO:0003729; GO GO:0042803; GO GO:0017056; GO GO:0051301; GO GO:0034605; GO GO:0007094; GO GO:0031990; GO GO:0046832; GO GO:0000122; GO GO:0045947; GO GO:0031453; GO GO:0090316; GO GO:0090267; GO GO:0046827; GO GO:0042307; GO GO:0006606; GO GO:0010965; GO GO:1901673; GO GO:0070849; GO GO:0006405; GO GO:0006404; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270}; SQ QEQHSQLEAAKTQVEKDMGEKISNLERELENANDLLCSTKRKGVMLSEEELTAMSPTAAAVAKVVKPGMKLTELYNAYVE SQ TQDKLLMEKQENKRITKYLDEIVKEVEAKSPILKRQREEYERMQKTVASLSAKLEQAMREIQRMQDETDKANKCSSVLER SQ ENQRLELQIKDLSQQIRVLLMELEEARGNFVQRDDVSSANISSSSEVITQHLVTYRNIEELQQQNQRLLVALRELGEAKE SQ REEQESTSSRVSELEKELENALSELQQLREARSHQMTLVESIVRQRDMYRILLSQTTGVVLPAQDETALTSTPRKSPGVS SQ LDGSTSTPAAVVVSDSTEAAEARAALKQLQEVFENYRKEKAENDRMLNEQHDKLQEQVTELRSQNTKISTQLEFASKRYE SQ MLQDNVEGYRREITALQEKTQKLSATTQKQEQIINTLTHDLRAANEKLAVAEVRAENLKREKELLKMSEVRLTQERESLV SQ AEQRGQNLLLTNLQTIQVTLERSETEIKQRYNNQIEKLEQELAQTKKKLEHEIEQRHLLGKNQDVQVLELKKQYEMELNL SQ HNNTKELLKNSHKEISVLKQQLNSFELQLASRSSQQAANRDKDVNIEDVEEIKTKLRQSEELVNDLKERLKTATSNVEQY SQ RSVVLNLEESLNKEKQVTEEVRKTIEVRLKESSEYQSQLEKKMMESEKEKQELRDEKHKTVEQMEQQVTQLRQSLSSLQA SQ EVQQALQRATTSASNEQKAKQDCQEQARIAAEAQNKYERELMLHAADVEALQAAKKQLTSASAIRHKCEETAQKAGSQLL SQ ESRASWEERERMLKEEVSQIQSRCKDLEKQNGLLHEQIESLSKKMVTSVQEGALNMSFGEEGKSQEQVMEILRFVRREKE SQ IAEARFEVAQVECLRYRQRIEHMERELHELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVLIESNKILREENEKQEQ SQ ELQQLQAKIRKLESNILPLQESNAELSEKSGMLQAEKKLLEEDVRRWRARTQHLLSQQKDTDAEEYKKLLSEREVNTKRI SQ QQLTEETGKLKTEVARTNASLNTCQSQLQSVKDDLTKIKAEKEKLQKELDAKILDIQEKIKTITQVKKIGRRYKTQYEEL SQ KVTHDKMVAEASSAKADQLQEQASQKEVQELKDSLQRSEAKVTTMQTTVDNMQKTLDDKDNEIKEHQEQISRMQAELSHL SQ HKDLQDKTAQEEQMRQQINEKEEKTKKTLLVVRQKLAQNNGAKEQLTRENEDLKQKNANLEQQKEELEVRMSALRSQYDG SQ RISRLERELREQQERHHEQRDEPQETTRIPQQRQITLQPTTAAGERGSANTSEPPTANIKPTPSKVTTAAVPVNKSTPRA SQ SIRPMVTPAAVSTPTSTPTATVMPTTQVDQQEVQSEGQMEHVPVFGSASGSVRSTSPNVQSSLPQPILTLQQQTQTTAFV SQ QPTQQSHATIESPTQETPVEIVQSSPVERPTTSSTFGTYSATPSSSIPKRPREEEEDSTIETPEQIADDTDQQRTKKRKE SQ EDIEEKTETEAVINTEDALHILTQCSNMEFPLEEEIVESPIQTSQVIESQAPEQLQNVQSTQDSLQDTPPKKTHNLVIVI SQ SDEENEDEQEGYEEEEQEDEEEDEDDAGIGEGDDSNEETGSADGNEDYEGDDAEEADGTDPDTETEDSMTAGEGNQRAAD SQ SQNIGDSGVVTAESTFSQETREQPSSASDRQGPRPPQSPRRQAHPPRLTILAPPQELGPPPAQRIPVARRQSVGRGLQLT SQ PGVGGMQHFFDEEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQASSSHSDLGQLASQGGLGMYDTP SQ LFLAHEEESGGRSVPTTPLQVAAPVSVFAENPAADTSDHASQSVPMVTTSTGNVPTSVDSGAADEGDEVFVEAESEGIGA SQ ESTLEMDTQQEEPVQPSEADLPSTSQDPPSSSIADTSSSKPKPRRVWLQPQPGGRPFKRSRGGSDFRGRGGINRSNI // ID Q5F334; PN Leucine-rich repeat-containing protein 59; GN LRRC59; OS 9031; SL Nucleus Position: SL-0178; SL Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery. {ECO:0000250}. DR UNIPROT: Q5F334; DR Pfam: PF13855; DE Function: Required for nuclear import of FGF1. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005789; GO GO:0016021; GO GO:0005635; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MARGGGKSGSLKDKLDGNELDLSLCGLSEVPVRELAALPKATVLDLSCNSLVSLPSDFCSLTHLVKLDLSKNRLQQLPVD SQ FGRLVSLQHLDLLNNRLVTLPVSFAQLKLSLHHSPVEILSRLLGTPSSLLVFHSFHSWENQNLKWLDLKDNPLDPVLAKV SQ AGDCLDEKQCKQAAVRVLQHMKVIQSEQDRERQRKLQAEREMEKKREAEQRAREAQERELRKREKAEEKERRRREYDAQR SQ AAKQEMEKKTKKETVQTRKLASSSRPPQPARHKHSWSRSVLRALLLVLLCILCTLAVCKLTELQHQPLCVSVNTLYEDVV SQ AAVQNHKTLQNMLQQNSQQ // ID Q5F410; PN Transmembrane protein 18; GN TMEM18; OS 9031; 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: Q5F410; 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 MRSVAVAMEQPLHGPPGLSTILARTDWAEPWLLGLAGFHVLCFLLTCFSFQHYRVQIGHFLCMVCLVYCAEYINELAAMN SQ WRLFSKYQYFDSRGMFISLVFSAPLLVNTIIIVVNWVYRTLNVMTELKTLQQRIKAEKDKKK // ID Q5F452; PN Myotubularin-related protein 8; GN MTMR8; OS 9031; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}. DR UNIPROT: Q5F452; DR Pfam: PF06602; DR PROSITE: PS51339; DR PROSITE: PS00383; DE Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (By similarity). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96EF0}. DE Reference Proteome: Yes; GO GO:0005635; GO GO:0052629; GO GO:0004438; GO GO:0004725; GO GO:0046856; GO GO:0010506; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEHITTPKVENVKLLDRYTNRKAASGTLYLTATHLIYVDASAEVRKETWILHHHIATVEKLPLTTAGCPLLIHCKNFHVA SQ HFVIGQERDCHEVYTSLLKLSQPVKPEELYAFSYNPKMSKDNREIGWKLIDLKVDYQRMGIPNDYWEITDLNKDYEVCNT SQ YPPEIVVPRAASKATVIGSSRFRSRGRIPVLSYLYKENNAAICRCSQPLSGFSARCLEDEQMLQAIREANPGSPFMYVVD SQ TRPKLNAMANRAAGKGYENEDNYDNIRFKFIGIENIHVMRSSLQKLLEVCETKSPSMSDFLTGLENSGWLRHIKAVMDAS SQ VFLAKAVKDEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRAFKGFMVLIEKEWIAMGHKFSHRCGHLDGDPKEVSPVFT SQ QFIECVWQLMQQFPCTFEFNEHFLLEIHDHVYSCQFGNFLGTCHKEREDLKIFEKTHSLWPFLLQKKQELRNPLYRGFTA SQ YKELQPNTLPFSFQFWCGMYNRFDKGMHPKQCVLDHLLSCMNQKIKLEDNASELENKLPFLDGPLPNEACFLSKVGCAAS SQ KTPMLNTPQDYEGEAPPVLTNGISVGDINVTSDVDQRNKENLANHRDLHLNDSVDVLNSEAKDGKPQHH // ID Q5FVB0; PN Ataxin-10; GN atxn10; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q5FVB0; DR Pfam: PF09759; DE Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAAPVERLAGVCAELEQWLGEESGQRNDWAEGEGIVWRLSELFREAQYRELAEPRIFRLILQILSRVSCEIKVATLPAGA SQ FTDTHCQLPAECFRCLRNACVQCASNQDSVRNVGLIEESVRLIQIFGAPHVLQEPALVAFRCGLQFLGNTAAGNRDSQNA SQ VWACAFPDLFLSCLVHDDEKVVTYSSMVLFTCINREKVSTLQDPSKLDVALSVVTAYSKYPDAEWMYLIVMDHFLLCPDL SQ VKAVYLSQSSPERVTLLELILGKISQKEPLSAEESEALQAIAAFLSDCFQTQCKTILKLTSPSACDEEEPIVVTRLLDIL SQ CEVTSKNEHLSCLQTCPGLLEAAVDILRLTHLAGKQSMNVFTAAHTMSMGQDLTHAAVGFKAHLIRLIGNLCYQNKENQE SQ KVYQLDGIALILDNCSIDDNNPFLNQWAVFAIRNLTENNDKNQELIASMERQGLADSSLLKSMGLQAEERDGKLLLKSVK SQ KSPAL // ID Q5FVJ3; PN Inactive phospholipid phosphatase 7; GN Plpp7; OS 10116; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm. {ECO:0000250}. DR UNIPROT: Q5FVJ3; DR Pfam: PF01569; DE Function: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0016311; GO GO:0010832; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MPVSQSRARARDRNNVLNRAEFLSLNQPPKGTQEPRSSGRKASGPSTQPPPSSDGARERRQSQQLPEEDCMQLNPSFKGI SQ AFNSLLAIDICMSKRLGVCAGRAASWASARSMVKLIGITSHGIPWIGGTILCLVRSSTLAGQEVLMNLLLALLLDIMTVA SQ GVQKLIKRRGPYETSPGLLDYLTMDIYAFPAGHASRAAMVSKFFLSHLVLAVPLRVLLVLWAFCVGLSRVMIGRHHITDV SQ ISGFIIGYFQFRLVELVWMSSNTCQMLISAW // 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 Q5FW14; PN Charged multivesicular body protein 7; GN chmp7; OS 8364; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}. DR UNIPROT: Q5FW14; DR Pfam: PF03357; DE Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}. DE Reference Proteome: Yes; GO GO:0000815; GO GO:0005635; GO GO:0010458; GO GO:0045324; GO GO:0031468; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIV SQ IQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRAL SQ PLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERL SQ QSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLA SQ LKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWET SQ DQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ // ID Q5FW52; PN Muscular LMNA-interacting protein; GN Mlip; OS 10090; SL Nucleus Position: SL-0178; SL Comments: Nucleus {ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}. Nucleus envelope {ECO:0000269|PubMed:21498514}. Nucleus, PML body {ECO:0000269|PubMed:21498514}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26359501}; Peripheral membrane protein {ECO:0000269|PubMed:26359501}; Cytoplasmic side {ECO:0000269|PubMed:26359501}. DR UNIPROT: Q5FW52; DR UNIPROT: Q9D6X9; 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:26359501, PubMed:22343712, PubMed:26436652). Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD (PubMed:22343712). {ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26359501, 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; TP Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:26359501}; SQ MEFGKHEPGSSLKRNKNLEEGVTFEYSDHMTFSSESKQERVQRILDYPSEVSGRNSQQKEFNTKEPQGMQKGDLFKAEYV SQ FIVDSDGEDEATCRQGEQGPPGGPGNIATRPKSLAISSSLASDVVRPKVRGADLKTSSHPEIPHGIAPQQKHGLALDEPA SQ RTESNSKASVLDLPVEHSSDSPSRPPQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTASESQLTKPGVIRPVPVKSK SQ LLLRKDEEVYEPNPFSKYLEDNSGLFSEQ // ID Q5H8A5; PN Ion channel POLLUX; GN POLLUX; OS 34305; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Nucleus membrane {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}; Multi-pass membrane protein {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}. Note=The chloroplastic localization proposed by PubMed:15616514 is probably an overexpression artifact. DR UNIPROT: Q5H8A5; DR Pfam: PF06241; DE Function: Ion channel with permeability for potassium. Involved in perinuclear calcium spiking but not in cytosolic calcium influx. Required for early signal transduction events leading to endosymbiosis. Acts early in a signal transduction chain leading from the perception of Nod factor to the activation of calcium spiking. Also involved in fungal entry into root epidermal cells during the establishment of the arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:16903357, ECO:0000269|PubMed:19106374}. DE Reference Proteome: No; GO GO:0016021; GO GO:0031965; GO GO:0006811; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MIPLPVAAANSNSNSNSNSNDEESPNLSTVIKPPLKKTKTLLPPPSSSSSNRPLHLRVSIDNNNNNNAPPPPADFSDHQW SQ NYPSFLGTTTRKRRPSSVKPPSTSNLRFDTIPKTKTKTKTNTNTNTNTNTNTNTNTDLPPPPVPSSSPVARPQHHNHRSP SQ PIFYLLIITCIIFVPYSSYLQYKLAKLEDHKLHLCRQSQIHFSSGHGNGKISIPIHDASFSYILSRKAALYIVLFTLILP SQ FLLYKYLDYLPQIINFLRRTHNNKEDVPLKKRIAYMLDVFFSIYPYAKLLALLFATLFLIGFGGLALYAVTGGSLAEALW SQ HSWTYVADSGNHAETQGTGQRVVSVSISSGGMLIFAMMLGLVSDAISEKVDSLRKGKCEVIERNHILILGWSDKLGSLLK SQ QLAIANKSVGGGVIVVLAEKEKEEMEMDITKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDAR SQ ALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIK SQ RWPELDGLSFKDILISFPDAIPCGVKVAADGGKIVINPDDSYVMRDGDEVLVIAEDDDTYSPGSLPEVLKGFFPRIPDAP SQ KYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKEREKKLAAGGLDVFGLENIKLVHREGNAVIRRHLESLPL SQ ETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYKDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDS SQ RTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEQGNEMCIKPAEFYLFDQEELCFYDIMIRGRARQEII SQ IGYRLANQERAIINPSEKLVARKWSLGDVFVVIASGD // ID Q5HZ92; PN Ceramide-1-phosphate transfer protein; GN cptp; OS 8355; 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: Q5HZ92; 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 and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}. DE Reference Proteome: No; GO GO:0005829; GO GO:0010008; GO GO:0005794; GO GO:0005640; GO GO:0005886; GO GO:1902387; GO GO:1902388; GO GO:0005543; GO GO:1902389; 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 MSSTEEKFSLKEVLVSFKACLIDDDKDVILEHYVNGWKGLVRFMSSLGTIFSFVSKDAVSKIQIMESYLAGPNGERYRTL SQ QSMVEYELSSDLVDLTKRSDHTDSGCRTLLRLHRALRWLQLFLEKLRVSNEDSKTSTLCTEAYNDSLANFHPWIVRKAAT SQ VSFIALPYRNTFFEIMNVGTTEEVVAMLGESMPYVTKVYDFTQEVYSQHNLLELP // ID Q5I034; PN Protein CUSTOS; GN Custos; OS 10116; SL Nucleus Position: SL-0178; SL Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. DR UNIPROT: Q5I034; DE Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. DE Reference Proteome: Yes; GO GO:0005635; GO GO:0007275; GO GO:0030178; GO GO:0060061; GO GO:0016055; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MVAPSGAMSDSESSSSDSSDAEELARCREAATPAWGLEQRPREAERPAAGTADTQAPAPQPSRRREVNQHDEDGNELQTT SQ PEFRAYVAKKLGALLDSSIAIAEVWKKTQQARLQQEAKEQQEAKEQQAAKEEQAAKKEEDGFRLFFTSVPGGHEKEASPR SQ PCRKRQPPSSSEDSDEELQRCREAAVSASDILQESAIHCPAKVEKEAEKKKLKKKAKKKADADLAAATGLEQVKEAGSVN SQ GDPVLSGTKKKKKKKAKKAREASLCPPAECAAAEPKN // ID Q5I0I8; PN Nucleolar complex protein 4 homolog; GN Noc4l; OS 10116; 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: Q5I0I8; DR Pfam: PF03914; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0030692; GO GO:0031965; GO GO:0005730; GO GO:0005654; GO GO:0032040; GO GO:0042254; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MERQPASTGSRQELGRLLEAVLSNRGRANAVFDILAVLQSEDPEEIKEGVRTCSRLFGTLLEREELFVGSLPCEDMALAG SQ SQGATYKYKVWMRHRYHSCCNRLEELLTHPSFQVKELALETLMKFVQLEGAKPLEKPQWESHYLFPRTLFRAVVGGLLTP SQ EDDHSLLISQFCEYLEYDDIRYHAMQVATSILARATSRQPEVSLTFWNNAFTLLSAVNLPLQEHELTNFYVKHAQTSSKW SQ KVVHLKEQRKAFQEMWLGFLKHKLPLSLYKKVLVAMHDSILPHLAQPTLMIDFLTSACDVGGAISLLALNGLFILIHKHN SQ LEYPDFYQRLYGLLDPSIFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPLICNLLRRHPA SQ CRVMVHRPQGPELDADPYDPTEKDPARSRALESCLWELQTLQQHYHPEVSRAASVINQALSVPEVSIAPLLELTAYEIFE SQ QDLKKMMPESVPLEFIPAKGLLGRQDDLCTQFFCLS // 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 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 Q5M7B7; PN Optineurin; GN optn; OS 8355; 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: Q5M7B7; 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: No; GO GO:0005776; GO GO:0005794; GO GO:0048471; GO GO:0055037; GO GO:0070530; GO GO:0046872; GO GO:0006914; GO GO:0016192; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MENELLNHPHNNNMVNGHQDAPYDALSMKNDAEMLEQIKQLLMENNNLKETMKQMNQEMKERLEELLKRHNQHLLDLNSA SQ NEVLRKELQSLKEKIATSNQGSAVCSTSEEASENKQLKNQLTRLQAEKADLLGLISELQLKLGSFSEDSFVEIGFSERES SQ GEIVNEEKANKILSDHNISYRTNSIKEEGGGTEPEEVAISRLLRSLREETQKVERLEKELFSANKRLAELEKQTSEFCDK SQ GVQTEQESEQSQSEVIISSEVDILKEKVKSLNKELQETNDKLNEAKQFKNSLQEKCILLDKRLQENQVDLEEKQSLRYSI SQ KKLELQVESQESEIKLEQNKTEAEKNQLGILQVSYDKLNSEYQELRIREIEKVSKVEFNELLEKLDVCEKALAKKQFEID SQ EMREMDTKHEEDKETIELLRAQVDVYCADFHAERSARENIHQEKEQLATRLAYMIQEYEKLKEEMMGKQSIEQLQRRHGA SQ TSLLDASEGPYLVARGAANMEQPSITVYTCPKCNLTVPDMDTLQIHVMDCIT // ID Q5M7F4; PN 2-acylglycerol O-acyltransferase 2-B; GN mogat2; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}. DR UNIPROT: Q5M7F4; DR Pfam: PF03982; DE Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250|UniProtKB:Q3SYC2}. DE Reference Proteome: No; GO GO:0005789; GO GO:0016021; GO GO:1990578; GO GO:0003846; GO GO:0006071; GO GO:0019432; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MWIHFAPLRIPFSRRLQTVAVLQWAVSFLAMAQCCIALYILLLFSRYWFLALLYGVWLYLDWDTPSKGGRRSNWVRSWIV SQ WKYFAEYFPIKLLCTAPLDPKYNYIMGFHPHGVLVVGAFGNFCTEGTGFSRLFPGLTPHLLMLPAWFRVPFFREYIMSGS SQ LVSSDRSSAHYLLSQKSGGQALVIAVGGPPEALDAKPGELTLQLLNRTGFIKMALTHGAHLVPVLSFGENDLYNQVNNPR SQ GSLLRTTQEKLQKVLGIALPLFHGRGVFQYSWGLLPHRRPIYTVVGSPIPVAKTPCPTQEQISSLHALYVAKLRELYTTH SQ KGNYGIPRDRSLVLC // 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 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 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 Q5NVE2; PN Serum response factor-binding protein 1; GN SRFBP1; OS 9601; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}. DR UNIPROT: Q5NVE2; DR Pfam: PF09073; DE Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}. DE Reference Proteome: Yes; GO GO:0048471; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAQPGTLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGTEDALLKNQRRAQRLLEEIHAMKELKPDMVTKSALGD SQ DINFEKICKKPDSTATERAIARLAVHPLLKKKIDVLKAAVQAFKEARQNVTEVESSKNASEDNHSKNTLYSNDNGSNLQR SQ EGTVISEQEVKETKILAKKPIHNSKEKIAKMEHGPKAVTIANSPSKPSEKDSVISLESQKTPADPKLKTLSQTKKNKESD SQ SSLSGNSDGGEELCEEEKEYFDDSTEERFYKQSSMSEDSDSGDDFFIGKVRRTRKKESSCHSSVKEQKRLEKVFLKEDTG SQ ETHGDTRNDKTKPSTETRKLESVFFHSLSGSKSSRRNFKEQAPKTRSLDFPQNEPQFKNQFNKKLSRRLENTKQQLQLPL SQ HPSWEASRRRKEQQSNIAVFQGKKITFDD // ID Q5R414; PN Cytoplasmic FMR1-interacting protein 2; GN CYFIP2; OS 9601; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96F07}. Nucleus {ECO:0000250|UniProtKB:Q96F07}. 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). {ECO:0000250|UniProtKB:Q5SQX6}. DR UNIPROT: Q5R414; DR UNIPROT: Q5R6T9; DR Pfam: PF07159; DR Pfam: PF05994; DE Function: Involved in T-cell adhesion and p53-dependent induction of apoptosis. Does not bind RNA (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000250|UniProtKB:Q96F07}. DE Reference Proteome: Yes; GO GO:0030054; GO GO:0005737; GO GO:0043005; GO GO:0005634; GO GO:0048471; GO GO:0045202; GO GO:0006915; GO GO:0098609; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYA SQ VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLT SQ LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLAD SQ IVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIE SQ TSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLL SQ SKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIY SQ AALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYM SQ VRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIE SQ MSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSV SQ LLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWL SQ LEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPA SQ NIQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVESLLQGTILQYVKTLIEVMPKICR SQ LPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGE SQ RLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHV SQ DECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPL SQ KKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC // 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 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 Q5R812; PN Charged multivesicular body protein 7; GN CHMP7; OS 9601; SL Nucleus Position: SL-0178; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}. DR UNIPROT: Q5R812; DR Pfam: PF03357; DE Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}. DE Reference Proteome: Yes; GO GO:0000815; GO GO:0005635; GO GO:0010458; GO GO:0045324; GO GO:0031468; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEA SQ FQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKA SQ EEVYRLYQSSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVG SQ VYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQM SQ VFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPD SQ NPRDRHFTNSVPNPRISDAGLEAELEKLSLSEGGLVPSGKSPKRQLEPTLKPL // 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 Q5R923; PN Optineurin; GN OPTN; OS 9601; 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: Q5R923; 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:0005794; GO GO:0048471; GO GO:0055037; GO GO:0005802; GO GO:0070530; GO GO:0046872; GO GO:0006914; GO GO:0034620; GO GO:0090161; GO GO:0016192; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MSHQPLSCLTEKEDSPTESTGNGPPYLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQK SQ EERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGI SQ VSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTSRALSKYRSRSAEGAKNYLEHEELTVSQLLLCL SQ REGNQKVERLEIALKEAKERVSDFEKKASNRSEIETQTEGSTEKENDEEKGLETVGSEVEALNLQVTSLFKELQEAHTKL SQ SEAELMKKRLQEKSKLTVLQMTHNKLLREHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEQALASKQLQMDEMKQT SQ IAKQEEDLETMTVLRAQMEVYCSDFHAERAAREKIHEQKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSGADQ SQ QAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII // ID Q5R9G4; PN Exportin-7; GN XPO7; OS 9601; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. DR UNIPROT: Q5R9G4; DR UNIPROT: Q5RCM4; DR Pfam: PF03810; DR PROSITE: PS50166; DE Function: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export 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}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005643; GO GO:0008536; GO GO:0006886; GO GO:0051028; GO GO:0051169; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MADHVQSLAQLENLCKQLYETTDTTTRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKLVSRTNNPLPL SQ EQRIDIRNYVLNYLATRPKLATFVTQALIQLYARITKLGWFDCQKDDYVFRNAITDVTRFLQDSVEYCIIGVTILSQLTN SQ EINQADTTHPLTKHRKIASSFRDSSLFDIFTLSCNLLKQASGKNLNLNDESQHGLLMQLLKLTHNCLNFDFIGTSTDESS SQ DDLCTVQIPTSWRSAFLDSSTLQLFFDLYHSIPPSFSPLVLSCLVQIASVRRSLFNNAERAKFLSHLVDGVKRILENPQS SQ LSDPNNYHEFCRLLARLKSNYQLGELVKVENYPEVIRLIANFTVTSLQHWEFAPNSVHYLLSLWQRLAASVPYVKATEPH SQ MLETYTPEVTKAYITSRLESVHIILRDGLEDPLEDTGLVQQQLDQLSTIGRCEYEKTCALLVQLFDQSAQSYQELLQSAS SQ ASPMDIAVQEGRLTWLVYIIGAVIGGRVSFASTDEQDAMDGELVCRVLQLMNLTDSRLAQAGNEKLELAMLSFFEQFRKI SQ YIGDQVQKSSKLYRRLSEVLGLNDETMVLSVFIGKIITNLKYWGRCEPITSRTLQLLNDLSIGYSSVRKLVKLSAVQFML SQ NNHTSEHFSFLGINNQSNLTDMRCRTTFYTALGRLLMVDLGEDEDQYEQFMLPLTAAFEAVAQMFSTNSFNEQEAKRTLV SQ GLVRDLRGIAFAFNAKTSFMMLFEWIYPSYMPILQRAIELWYHDPACTTPVLKLMAELVHNRSRRLQFDVSSPNGILLFR SQ ETSKMITMYGNRILTLGEVPKDQVYALKLKGISICFSMLKAALSGSYVNFGVFRLYGDDALDNALQTFIKLLLSIPHSDL SQ LDYPKLSQSYYSLLEVLTQDHMNFIASLEPHVIMYILSSISEGLTALDTMVCTGCCSCLDHIVTYLFKQLSRSTKKRTTP SQ LNQESDRFLHIMQQHPEMIQQMLSTVLNIIIFEDCRNQWSMSRPLLGLILLNEKYFSDLRNSIVNSQPPEKQQAMHLCFE SQ NLMEGIERNLLTKNRDRFTQNLSAFRREVNDSMKNSTYGVNSNDMMS // 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 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 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 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 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 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 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 Q5RE06; PN Ataxin-10; GN ATXN10; OS 9601; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q5RE06; DR Pfam: PF09759; DE Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0048471; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAAPRLPPARALSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQ SQ LITECFRCLRNACIECSVNQNSIRNLDAIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFP SQ ELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLN SQ NQERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTEL SQ LGYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIP SQ LILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP // 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 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 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 Q5RJR8; PN Leucine-rich repeat-containing protein 59, N-terminally processed; GN Lrrc59; OS 10116; SL Nucleus Position: SL-0178; SL Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. {ECO:0000250}. DR UNIPROT: Q5RJR8; DR UNIPROT: Q63742; DR Pfam: PF13855; DR PROSITE: PS51450; DE Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; DE Interaction: P11362; IntAct: EBI-1028277,EBI-22243518; Score: 0.35 GO GO:0005789; GO GO:0016021; GO GO:0042645; GO GO:0005635; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MTKTGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATVLDLSCNKLSTLPSDFCGLTHLVKLDLSKNKLQQLPAD SQ FGRLVNLQHLDLLNNRLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQ SQ RRLEVEREAEKKREAKQQAKEAKERELRKREKAEEKERRRKEYDAQKASKREQEKKPKKETNQAPKSKSGSRPRKPPPRK SQ HNRSWAVLKGLLLLLLLCVAGGLVVCRVTGLQQQPLCTSVNAIYDNAVQGLRHHEILQWVLQTDSQQ // 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 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 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 Q5TZ18; PN Neuron navigator 3; GN nav3; OS 7955; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0183; SL Comments: Nucleus outer membrane {ECO:0000250}. DR UNIPROT: Q5TZ18; DR Pfam: PF00004; DR Pfam: PF00307; DR PROSITE: PS50021; DE Function: May be involved in neuron regeneration. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0030175; GO GO:0005794; GO GO:0030027; GO GO:0005640; GO GO:0003779; GO GO:0005524; GO GO:0072576; GO GO:0007399; GO GO:0022008; GO GO:0031016; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAHGLAPRSSELRVTESPMLSCQLSFKTEIHDRRTNLVPAPAATLARSSREAEESKICKIYTDWANHYLAKSGCPRLIKD SQ LTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLSAEEVCNGNLKSILGLFFILSRY SQ KQQQQHQQQYLQSLVELQQHVTHQTTGAAQLSQHKTQDMQSSLTARYTSPPGHSGIAAPQKKNTRLPGPSRVPAAGSGSN SQ SSKGSSNLNRRSQSFNSIDKSKPLQYASGNDRGSMNGSGSVPSSTSGQQLASAIPSPTAGKTWRSKSMNMKHSATSSMLA SQ TKPPSPTSSPTPPSSSDRLRPPITDASKSAPGNQRSMLEKFRILNPRATSRTSPSVAEMALQEEDDLSEFGDEGTFSPTP SQ PCGISKQQGKPSASAFAPPSKSNNCKNHNNKSLPQPKDKEDKNKTKNKASTPPKEEPVIVETSKKGSKIASLIPKGSKTS SQ AASVKKESAIPASSSIPKPGLKAPTATSKPAGTQSCVPATTGGEKTKLNKGSQSIYMQRSLGGLENRKTSMVLSTSTSAL SQ SASTTSGLGGGCALGGNGAVQLPQQQQHNHPNTATVAPFMYRTYSENDCTTVVPPEPCLSPTKELVYGKTAKQCLEEISG SQ EDPETRRMRTVKNIADLRQNLEETMSSLRGTQITHSTLETTFDTTVTTEVNGRGLPALSSRSSPMSWRLGQGSSPRLQAG SQ DAPSYTPPRSSAGSTTVRYGEPSRLLYTAPLRRAAASGARGAEPGEKGGISEVGPEVDVTGYGSDGDILAKNVHADDISG SQ YHTDGGIYSRNVDLYSRNVGRPAEMTPAREVVQKGVKEMQGEDSWDDSSSVSSGLSDTLDNISTDDLNPAPYSGISSRKS SQ KAAQSNKETHRHIEQDASSWAGAEDLKKVDEEMEPGMDPSCKWKTSSPSSSCQGEDISQKTGLPMSQTGSWRRGMSAQVG SQ ITPPRTKGTSTSLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGAL SQ ITASGATLTSGSATLGKVPKSACIGKSTGISNGRKTSLDGAQHQDDAVLLGCGGSEVPLQYRSLPRPAKSSSGGSSVVSR SQ SGHRSSSSSIDSNVSGKSAGGSGVAVGTPTSTKRRDTGKVGSGRSSPVTINQTDKEKVAGSDQEGTGLPTSPKSSPTSTQ SQ SGLRQPGSKYPDIASPTFRRLFGSKASSKPSSPGTPDSGKCPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQSGGSSP SQ LYGKTPDLGTDSPASSPASGLSLPSNARPWPPNLSSSSAGSKDTLSCHSMTSLHTSSESIDLPLPHHHGPKVTRTGSVKS SQ TLSEGMPLDRNTLPKKGLRQTSHEEGKEWLRSHSTGGLQDTGSPLSPPGTTCANAGKYHYSNLLSPTSMSQYNIPSTSMS SQ RSNSIPAQDSFELYGEGHPLGGSATSLEERPRGMSRSGSFRDSTDEVHGSSLSLVSSTSSLYSAQIRKLRRELDASQEKV SQ ATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELRETIEALKTQNTDAQTAIQVALNGPDHVHRDLRIR SQ RQHSSESMSSINSAASHSSLGSAKDAEDKKKKKKSWLRSSFKQAFSKKKTNKPQSSHDEIEEMTDSSLPSSPKLLHISRQ SQ ASSPQPLLSSPSTTELCECTEAEAEIILQLKNELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIELLKAENDRLK SQ SSGNTTPAATPAKTARPPSETSSTSSSSSRQSLGLSLNNLNITDTIMSDILLDDGYEGNLRKEGRSVRIVVTINSDSNKT SQ KAMQKKQYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRVDPLTSLGMNSDSIVCYRMGDVVRSHASEVPELLPCGYLVGD SQ NNVITVTLKGVKEGSIDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFILSKTGREVTDTNLATF SQ NVDQKSSKDLRQYLSSLAEQCNTEECEIELPTVVILDNLHHIGSLSDIFNGFLNCKYHKCPYVIGTMNQGVSSSPNLELH SQ HNFRWVLCANHTEPVKGFLGRFLRRKLIETEIDKNMRSNDLIKIIDWIPKIWQHLNSFLEAHSSSDVTIGPRLFLSCPMD SQ ADGSRVWFTDLWNYSLVPYLLEAVREGLQHEGQSLLQLRPEDVGYDGYSSSKDGAASKQVSQSDTEGDPLMNMLMRLQEA SQ ANYSSAQSCDSDSASHHEDLLDSSLESAL // ID Q5U247; PN Exocyst complex component 8; GN exoc8; OS 8355; 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}. DR UNIPROT: Q5U247; 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: No; GO GO:0000145; GO GO:0030426; GO GO:0048471; GO GO:0006887; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAEGGGSVQRLRRQLESNSFQAEQYVKLLSQQSDGDRDLQEHRQRIQSLADETAQSLKRNVYQNYRQFIETAKEISYLEG SQ EMYQLSHILTEQKSIMESVTQALLYTDRSEAARELQTAFPKEAEEGKVRNLTTLLEKVEGCKNLLETPGRYLVYNGDLTE SQ FDVDNMALIQKVHAFLMNDCLLIATSVPNRRGIYKYNALHNLDDLAVVNVKENPPMKDMFKILMFPESRIFQAENAKIKK SQ EWLEILEQTKKNKALNEKQKQEETTPQLPVVPEIPANPFIDEDGTFDEVEVDLTIDWIQELPEDLDVCIAQRNFEGAVDL SQ LDKLNSYLEDKPLTHPVKELKSKVDERVRQLTDVLVFELSPDRSLRGGPKATRRAVSQLVRLGQSTKACELFLKNQAAAV SQ QTAIRQLRIEGATLLYIHKLCNVFFTSLLETAKEFEMDFAENHGCYSAFIVWSRLALKMFVDAFSKQVFDSKESLSTVAE SQ CVKVAKEHCKQLSEIGLDLTFILHTLLVKDIKAALQSYKDIVIEATKHRNSEEMWRRMNLMTPEVLGKLREEMRNCGINN SQ FDQYTGDDCWVNISYTIVAFTKQTMAFLEEALKLYFPELHMVLLECLMEIILVAIQHVDYSLRCEQESEKKAFIRQNASF SQ LYENVLVVVEKRFEEGVGKPAKQLQELRNSSRLVRVNPESTTSVV // 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 Q5U2W6; PN Prostate tumor-overexpressed gene 1 protein homolog; GN Ptov1; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from the cytoplasm to the nucleus at the onset of S- phase. Also localizes to lipid rafts. {ECO:0000250}. DR UNIPROT: Q5U2W6; DR Pfam: PF11232; DE Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0044798; GO GO:0005654; GO GO:0048471; GO GO:0005886; GO GO:0045944; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MVRPRRAPHRSGAGGPLGGRGRPPRPLVVRAVRSRSWPAGPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGG SQ LAVNEHRLSNKLLAWSGVLEWQEKRRPFSDSAAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNS SQ QLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNAIRQVITTRKQAV SQ GPGGVHSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTDQWPRRLFMQLIPQQLLTTLVPLFR SQ NSRLVQFHFTKDMETLKSLCRIMDNGFAGCVHFSYKASCEVRVLMLLYSSEKKIFIGLIPHDQSNFVNGIRRVIANQQQV SQ LQRSLEQEQQQRGMGG // 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 Q5U395; PN CTD nuclear envelope phosphatase 1A; GN ctdnep1a; OS 7955; 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: Q5U395; DR Pfam: PF03031; DR PROSITE: PS50969; DE Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. Lipins 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 (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0005789; GO GO:0016021; GO GO:0071595; GO GO:0005635; GO GO:0031965; GO GO:0004721; GO GO:0004722; GO GO:0006998; GO GO:0010867; GO GO:0006470; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLKTRQCLLGIRTFLGVTSRIWSFFLYILRKHLRTIIQYQTVRYDILPLSPISRNRLNAVKRKILVLDLDETLIHSHHDG SQ VLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGILKRRYYRQ SQ HCTLDLGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTSDVRSVLSRNLH SQ QHRLW // 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 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 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 Q5XGC9; PN Serum response factor-binding protein 1; GN srfbp1; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}. DR UNIPROT: Q5XGC9; DR UNIPROT: Q28EI0; DR Pfam: PF09073; DE Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}. DE Reference Proteome: Yes; GO GO:0030686; GO GO:0005634; GO GO:0048471; GO GO:0030490; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEPVLNLNNEVVKLRKDVKKVKVLIIRKLTRHIAKLKSKKGTEELILKNQRRAQRLLEEIHSVKELKPDDVTKTALRKEI SQ SFEKVCKKPNSTAEERALARLATHPLLKQKITAIKEAIKAFKDARKTAAEGEREREKDEPEQVTKIKETKKPVQAKLNKN SQ TEEIKSAKEHVKEEKCKNLLEDSDKGTEKALELPYVQENLPEQTAENKEQPKAQDVERPAVERPAVERPAVERPAVERPA SQ VERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPA SQ VERPVVESPAVERPPVESPPKKKACLEQELGCELSDIEDSDKEKEYFDDSTEERFYKHSSSFEDSDSGSDNDFFIGKIRR SQ TKKKKSDKDGSKQKEEKVPPTKEKAQTSEVQKEIPTAKSMKLKSVFCKSLSQTKPKPSFTKRETNFRQERNKRPVMPQAS SQ PLAKKPLQSKATSVRQPGRKLEAQPLHPSWEASRKRKEQQAQITKFQGKKIVFDD // 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 Q5XHG1; PN Sphingomyelin phosphodiesterase 4; GN smpd4; OS 8355; SL Nucleus Position: SL-0178; SL Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZPR5}. DR UNIPROT: Q5XHG1; DR UNIPROT: Q4V7Y8; DR Pfam: PF14724; DE Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000250}. DE Reference Proteome: No; GO GO:0005789; GO GO:0000139; GO GO:0016021; GO GO:0005635; GO GO:0046872; GO GO:0004767; GO GO:0050290; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLLAGGSPQPSFLLGSLKADCVTKPFLQRCQDLVRVIEDFPAKELHAIFPWLIETVFGSLDGSILGWNLRGLHERINPLE SQ FHTALEFLDPSGAMMKLVYKLQAEEYKYDFPVSFLPGPVRASIQERVLPECPLYHNKIQFPASGGVSFNLALNSFEYFMF SQ HFAFCLLKQRNYPQGLHFSTADSAYYILVDKYLKWFLPVEGNVPPPHSPNTGGTVPSPAPRSPSLSFTSYGSHTSLLKRH SQ ISHQHLVNADPAAQEIWRTETLLQVFVEIWLHHYSLEMYQKMQSPNAKLEALHNRLSVSSAPPIYPALPGSLHSYQELFQ SQ PTEEHVLVVRLLVKHLHTFSNSIRPEQVSPSTHSHTASPLEELKRVVVPRFIQQKLYIFLQHCFGHWPLDASFRAVLEMW SQ LSYVQPWRYVLERSSPVSGEMQNRNVPEKWSTFVQENLLFYTKLFLRFLSRALRTDLVNPKNALMVFRAAKVFSQLNLPE SQ MILNGEQLFLKPEHVIPHRQHRLLLTPNLGGSFLSSWQPPITDTSLKVKSHVFSLEGQDCQYMQMFGPEARNLVLRLAQM SQ ISQAKQTAKSISNHSPDSSANQSFLSWFGLGSPDFNGSYNGSDLDEAGYDTIRKTDEHLEKALDYFCQIFRLNPTQLGQL SQ TANVDSSQDDDGKNKLPDCIQSEDGVVLTSLGRYQIINGLRKFDIEYQGDPELQPIRSYENAMLVRYLYRLSSVINKRFA SQ NSMGALCARKDFLGKLCRHHLTSSSRKCKKSPITSVSPSEPAAPHIRLRFLASYRTLAFLFIFYILGSLLSLGPLICTFL SQ LLIGCMFYAIVQTLLSEEQKPHNN // 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 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 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 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 Q5ZI22; PN Nucleoporin NUP42; GN NUP42; OS 9031; 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}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. DR UNIPROT: Q5ZI22; 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}; SQ MTICQFFLQGRCRFGDRCWNEHPRGGGGRPHSAGPVRGAGGGWGAASQRYANVIQPPIFKHSTWGGSGDGGGFSGASDFG SQ SPGNKSAVFSQNRFSALSSAHPADGFSDEEQRLLDCVAKDMATWESSGQWMFSCYSPEAGKPNVSGFREFSAEEVRLEYY SQ NCSANNNTENYINSVNQLVQERRNRLQELKALNASGKESLLSQLKNAVTQPLPSLGFGGQQASSFGFPSFPVSSSSGAAS SQ FSFKANPSVPPGNAAAVGSSAAASNPPTFGVTSSPSVPNPVGSGNSSAPSAASFSFKTSGTTSGCGTSGLSGFGSSAAAN SQ SSSTAPLPVSATPSAATGTSQSGASSASAAQTAGASGHNVTSAPSAVPNGIASDKLYTPRSELTAEELEQFEAKRFTLGK SQ IPLKPPPIDLLYL // ID Q5ZIA2; PN Ensconsin; GN MAP7; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. DR UNIPROT: Q5ZIA2; DR Pfam: PF05672; DE Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. DE Reference Proteome: Yes; GO GO:0005874; GO GO:0015630; GO GO:0048471; GO GO:0000226; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAEAAGRSGGRRRRAAEGSKTQDKKVASGQSNTGTKPDHPPILKVDDRQRLARERREEREKQLAARETVWLEREERARQH SQ YEKHLEERKKKLEEQRLKEEGRRAAVEEKRRQRIEEDKERHEAVVRRTIERSQKPKQKQNRWSWGGALHSRINNSDPDRR SQ SVSTMNLSKHVDPVINKRLSSSSATLLNSSDRARRLQLSPWESSIVSRLLTPTHSFLARSKSTAALSGDAASCSPISPLS SQ YKTMSCRNSADRAKLFASTDAVGRRRTHLAGTDKKEKERDHLSSNFSANLKGGHFSSNPKARSPAPSPVWHASKSLPSLA SQ GTLKQITSPPGSSKVPSTQARPPSPGNIRPVKKDTKPENEKKRAEKEAEKANEERTEGSKETSAGTGESANQEELAVQAE SQ DAQAASPSLPPAPPALSPPPAPMKTSAGTTDPEEATRLLSEKRRLAREQREREEQERREREELERQKKEELSQRIAEERA SQ RREEEEARRQEAERKRKDAEEEREKEERLRRQAEEREQKEREEMERIQKQKEEEARLREEAERIRLEREKHFQREEQERL SQ ERKKRLEEIMKRTRRVEAVDKKPNDQQNGHISKANNTGEAVITSPAPPMEPSGGPQLQHATQSPHSGKPVTCTHTIVSHQ SQ PPMNMDSNLNPEKNTEENGMSMQNDNFEEIINLPIGSKPSRLDALNNDGSDSPGIPLNPILAFEDKGTLLPQVDSVQTHQ SQ TAEVI // ID Q5ZID0; PN NmrA-like family domain-containing protein 1; GN NMRAL1; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. DR UNIPROT: Q5ZID0; DR Pfam: PF05368; DE Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005634; GO GO:0048471; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MTSKKLIVVFGATGAQGGSVARALLEDGAFAVRAVTRSPGRKEAAELRRRGAELMRADQDDERSLEEALTGAHGAFVVTN SQ FWEHCSKEKEVAQGRRLADLSKRLGLQHVVYSGLENVKQLTKGRLEVLHFDGKGEVEEYFRAVNVPTTTIRLPFYYENFL SQ SSFKPQKAPQGDKLLLGLPMGDTPMDGMAVEDLGPIVLSLLKSPEQYIGQVIGLSAGKLTVAEYAAAFSQQTGKTVEDSK SQ ITPEEYEKLGFPGAKELADMFRFYALKPDRNVELTMKLNPKARTFQQWLADNKAAF // ID Q5ZIS9; PN Protein shisa-5; GN Shisa5; OS 9031; 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 {ECO:0000250}. DR UNIPROT: Q5ZIS9; DR Pfam: PF13908; DE Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0031965; GO GO:0006915; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MGFGTLVAIGVIVFAVVVITIILCLTCSCCCLYKACRRPQPVVTTTTATTVVHAPYPQQQGVPPSYPAAPYQGYQPVAIQ SQ PQPGMPVAPYPAQYPPPYPMQPPDPPAYHETVAAGAGAPYPISQPPYNPAYMDPQKPTY // ID Q5ZJC7; PN Nucleolar complex protein 4 homolog; GN NOC4L; OS 9031; 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: Q5ZJC7; DR Pfam: PF03914; DE Function: DE Reference Proteome: Yes; GO GO:0016021; GO GO:0030692; GO GO:0031965; GO GO:0005730; GO GO:0032040; GO GO:0042254; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MARPALAASLEAVLGDRGNANRVFEILELLAAKEEEDVLCAARTCRRLFAALLRRGELFAGSLPAEEDALRGNYSAEEKY SQ KIWMRHRYNDCVESLSELLGHDSFQVKESSLCTLMKFVELEAECPLVAEQWKGSIAFPRHLLKVVVNGLIPIHEDASLLI SQ SRFQEYMEYEDVRYFVMKVVTESIGQVMQKIKERPLPFYQQNVFSLISPINMPNKERDMVKFMMKQDNREEWKVSKLQAH SQ KQAFERMWLTFLKHQLPSGLYKKVLVILHDSILPYMNEPTLMIDFLTVAYGVGGAISLLALNGLFILIHQHNLEYPDFYK SQ KLYSLLDPSIYHVKYRARFFHLADLFLSSSHLPAYLVAAFIKRLSRLALTAPPEALLMVIPFICNLFRRHPACKVLMHRP SQ NGPQDLSEDPYIMEQEEPSESRALESSLWELQSLQNHYHPDVAQAAAILNQSLSEIEDDISGLLELSASELFDKEIKKTS SQ ANVPLEFEQVRGLFGKKNDIIAEHFALD // 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 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 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 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 Q60490; PN 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase; GN EBP; OS 10141; SL Nucleus Position: SL-0178; SL Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7961902}; Multi-pass membrane protein {ECO:0000305|PubMed:7961902}. 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: Q60490; DR UNIPROT: Q9QV23; DR Pfam: PF05241; DR PROSITE: PS51751; DE Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000250|UniProtKB:Q15125}. DE Reference Proteome: Yes; GO GO:0031410; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0005635; GO GO:0000247; GO GO:0047750; GO GO:0004769; GO GO:0006695; GO GO:0030097; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MATTSTGPLHPYWPRHLRLDHFVPNDLSAWYIVTVLFTVFGALVVTMWLLSSRASVVPLGTWRRLSVCWFAVCAFVHLVI SQ EGWFVLYQKAILGDQAFLSQLWKEYAKGDSRYIIEDNFIICMESITVVLWGPLSLWAVIAFLRQHPSRYVLQFVISLGQI SQ YGDLLYFLTEYRDGFQHGEMGHPIYFWFYFFFMNVLWLVIPGVLFFDSVKQFYGAQNALDTKVMKSKGK // ID Q60664; PN Processed lymphoid-restricted membrane protein; GN Lrmp; OS 10090; SL Nucleus Position: SL-0178; SL Comments: [Processed lymphoid-restricted membrane protein]: Cytoplasm. 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. DR UNIPROT: Q60664; DR UNIPROT: Q7TMU8; DR Pfam: PF05781; 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. {ECO:0000269|PubMed:9314557}. DE Reference Proteome: Yes; DE Interaction: E9Q401; IntAct: EBI-643628,EBI-688116; Score: 0.35 DE Interaction: A3KGF7; IntAct: EBI-688116,EBI-681172; Score: 0.37 GO GO:0005694; GO GO:0005783; GO GO:0005789; GO GO:0030176; GO GO:0005815; GO GO:0005635; GO GO:0000922; GO GO:0002376; GO GO:0007338; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MLCVKGPPEQEPEDGALDVTRGCQCPLPTEDSILGQELLDCTRMNEDQSTDENGAGHFYSESPSQLREYLTQPSSEQTSS SQ SESTVTSSESGSDILHMASGDLDCKPLCEKEEEARAASAMQGTSLAPAAYGDYTSVGVAKAASQLEAGEELRTTENGGKG SQ SAPGETEISMPPKASVKLVNFQQSENTSANEKEVEAEFLRLSLGLKCDWFTLEKRVKLEERSRDLAEENLKKEITNCLKL SQ LESLTPLCEEDNQAQEIVKKLEKSIVLLSQCTARVASRAEMLGAINQESRVSRAVEVMIQHVENLKRMYAKEHAELEDLK SQ QALLQNDRSFNSLPDEDDCQIKKRSSSLNSKPSSLRRVTIASLPRNLGNVGLVSGMENNDRFSRRSSSWRILGTKQGEHR SQ PSLHRFISTYSWADAEDERSDVKARDAPEPQGEEAVERTRKPSLSERRSSTLAWDRGTICSSVASWVTHLQASFRRANRA SQ LWLTGLIIILIAALMSFLTGQLFQTAVEAAPTQEGDSWLSLEHILWPFTRLGHDGPPPV // ID Q60819; PN Soluble interleukin-15 receptor subunit alpha; GN Il15ra; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Membrane {ECO:0000250|UniProtKB:Q13261}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Nucleus membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Cell surface {ECO:0000250|UniProtKB:Q13261}. [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space {ECO:0000250}. DR UNIPROT: Q60819; DR UNIPROT: A2AP35; DR UNIPROT: A2AP36; DR UNIPROT: A2AP37; DR UNIPROT: Q80Z90; DR UNIPROT: Q80Z91; DR UNIPROT: Q80Z92; DR UNIPROT: Q8R5E4; DR PDB: 2PSM; DR Pfam: PF00084; DR PROSITE: PS50923; DE Function: High-affinity receptor for interleukin-15 (PubMed:17947230). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (PubMed:17947230). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (By similarity). In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q13261, ECO:0000269|PubMed:17947230}. DE Reference Proteome: Yes; GO GO:0009986; GO GO:0031410; GO GO:0005615; GO GO:0016021; GO GO:0031965; GO GO:0005886; GO GO:0042010; GO GO:0019901; GO GO:0035723; GO GO:0010977; GO GO:0032825; GO GO:0050766; GO GO:0007259; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MASPQLRGYGVQAIPVLLLLLLLLLLPLRVTPGTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVI SQ NKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTS SQ AGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTKVAISTSVLLVGAGVVMAFLAWYIKSRQPSQPCRVE SQ VETMETVPMTVRASSKEDEDTGA // 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 Q619T5; PN Ras and EF-hand domain-containing protein homolog; GN rsef; OS 6238; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}. DR UNIPROT: Q619T5; DR UNIPROT: A8XJC9; DR Pfam: PF00071; DR PROSITE: PS00018; DR PROSITE: PS50222; DR PROSITE: PS51419; DE Function: Binds GTP and GDP. Plays a role in uterine seam cell development. {ECO:0000250|UniProtKB:Q22908, ECO:0000250|UniProtKB:Q8IZ41}. 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 MANPDVENLFSLCDSESKGFLTMEDLKKVCPQLDDNDLRFIFNELDRDGSGKIEKMEFLQGFQETVQHGESRGLNGMQRR SQ ASVAFDDGGPVFRRDELVFESESDSSSRPAIRVYDEEHYHSESDTNINIDFSVPCQEEVLVLYEQLQSSGVPALLRKFER SQ VVGSFHKELSEKKHENERLQRIYASEREMYNRRMEEMESEVDQQLELIEMKARQEERERLTKEKEEMRERMSEEMSEMRT SQ NIERLQRMEKVLERENERLNHQKDLSDKLKVVNEENNDLRQNLAENHLELAMIKSELAQVRADFDQKQDELSARRDQASH SQ ATEESESVRKQLQLLFDANRKLHETNESLRDALDSRASVLRQFNLRTPSPGLINSNRNSVENFQTSTNMFKSVPLHAISD SQ EEPDPETSLILDDAHSLQGMDIAEGLVGLNDANGPAERTFRIVMCGDAAVGKSSFVMRVIRRQFTNQLPSTLGVDFHVKT SQ VNVDGRNVALQLWDTAGQERFRSLCKSYFRRADGAILVYDVCAEHSFLRVRDWIETIKESTERSIPIILVGNKVDMRLQT SQ PGAVAKTDGASMAAAMGVLFMETSALDGSNIDNAMLALTRELMAVEDVEIRSTGVVLNPAATKKGGCFSKCRGS // 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 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 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 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 Q63663; PN Guanylate-binding protein 1; GN Gbp2; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:P32456}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane {ECO:0000250|UniProtKB:P32456}; Lipid-anchor {ECO:0000250|UniProtKB:P32456}. Note=GBP2-GBP5 dimers localize to the Golgi apparatus. {ECO:0000250|UniProtKB:P32456}. DR UNIPROT: Q63663; DR Pfam: PF02263; DR Pfam: PF02841; DR PROSITE: PS51715; DE Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (By similarity). Exhibits antiviral activity against influenza virus. Promotes oxidative killing and delivers antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:P32456}. DE Reference Proteome: Yes; GO GO:0005737; GO GO:0031410; GO GO:0005794; GO GO:0000139; GO GO:0005634; GO GO:0048471; GO GO:0020005; GO GO:0005525; GO GO:0003924; GO GO:0042803; GO GO:0044406; GO GO:0035458; GO GO:0071346; GO GO:0071347; GO GO:0071222; GO GO:0071356; GO GO:0050830; GO GO:0042832; GO GO:0034504; GO GO:0009617; TP Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8148370}; SQ MASEIHMLQPMCLIENTEAHLVINQEALRILSAINQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWM SQ WCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFVYNSMGTINQQAMDQLHYVTELTDLIKSKSSPDQ SQ SGIDDSANFVGFFPTFVWALRDFSLELEVNGKLVTPDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPA SQ LRKQLCKLETLGEEELCSEFVEQVAEFTSYIFSYSAVKTLSGGIIVNGPRLKSLVQTYVGAISSGSLPCMESAVLTLAQI SQ ENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRLIEREAIEIFLKNSFKDVDQKFQTELGNLLISKRDAFIKKNSDV SQ SSAHCSDLIEDIFGPLEEEVKQGTFSKPGGYFLFLQMRQELEKKYNQAPGKGLEAEAVLKKYFESKEDIVETLLKTDQSL SQ TEAAKEIEVERIKAETAEAANRELAEKQEKFELMMQQKEESYQEHVRQLTEKMKEEQKKLIEEQDNIIALKLREQEKFLR SQ EGYENESKKLLREIENMKRRQSPGKCTIL // 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 Q63ZR5; PN Rhophilin-2-B; GN rhpn2; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q63ZR5; DR Pfam: PF03097; DR Pfam: PF02185; DR Pfam: PF00595; DR PROSITE: PS51180; DR PROSITE: PS50106; DR PROSITE: PS51860; DE Function: Binds specifically to GTP-Rho. {ECO:0000250}. DE Reference Proteome: No; GO GO:0048471; GO GO:0007165; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MTDALLPANLNAKRLSEQNYFRKGKSIAQTGRSKLQNQRAILNQQILKAMRMRAGAENLLRATANNKIREQVLLELSFVN SQ SNLQRLKEELERLNISVEVYQHTEQASNIPLIPLGLKETKDVDFTTAFKDFILEHYSEDASEYENELADLMDLRQACRTP SQ SRDEAGVELLVSYFQQLGYLENRFFPPSRNIGILFTWYDSFTGVPVSQPNISLEKASILFNIAALYSQIGTRCNRQTKIG SQ LEEAVTTFQKAAGVLNYLKETFTHTPSYDMSPAMLGALIKMLLAEAHECYFEKMILSGIQNEFCTLLKAAQEAAKVSEVH SQ MQVYTLMNQAPIKENVPYSWSVMVQVKAEHYKALANYFVAITLIDYQLNLSDDEDKQEKAISQLYDSMPEGLTAQTILKD SQ QQQRTLLGKAHLSKAIRSHEEAIRFSTLCSTLRQIDVLQLILSAFHQRSLLKFSQHQKPDDFLDLLSAPDIVSKTEYQAE SQ TIPPQLSKDKVTDIFQRLGPLSIFSVKQRWSAPRKMCITKEDGDFGFVLKGDCPVQVISLDPLCPAATEGLKEGDYIVSV SQ AGKDCKWCSTSQVMDMLQETGQDSIEIQVISIQDQTNSLANKSATYYAGMQKTYSLVCLTMDNDKNTKTQKATKKLSFLS SQ WGFKNRQKAASTICLPSEVKGKPKTDMVFSFPDNSLSTESALY // 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 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 Q641G3; PN Cell division cycle and apoptosis regulator protein 1; GN ccar1; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IX12}. DR UNIPROT: Q641G3; DR Pfam: PF14443; DR Pfam: PF14444; DR Pfam: PF02037; DR PROSITE: PS50800; DE Function: Transcriptional coactivator for nuclear receptors which may play an important role in regulating cell growth and apoptosis. {ECO:0000250|UniProtKB:Q8IX12}. DE Reference Proteome: No; DE Interaction: Q6P5F9; IntAct: EBI-2550236,EBI-11609103; Score: 0.35 GO GO:0048471; GO GO:0007049; GO GO:0006355; GO GO:0006417; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAQFGGQKNPPPWATQFTATAVSQPGPLAVQQSSLLGASPTIYTQQSALAAAGLASPSPANYQLSQTAALQQQAAAAAAA SQ AAAALQQQYTQPQQTIYSVQQQLQPPPQAILTQPAVALPTSLALSTPQQAAQITVSYPTPRSNQQQTQPQKQRVFTGVVT SQ KLHETFGFVDEDVFFQLTAVKGKSPQAGDRVLVEATYNPNMPFKWNAQRIQTLPNQNPASAQSLIKNPAAVMQPVAQPTA SQ YAVQTQPPPQAQTLLQAQISAATLTPLLQTQTSPLLQQPQQKAGLLQTPVRIVSQPQPVRRIEPPSRFSVRNDRGDSILS SQ RKDDRNRERERERRRSRDRSPQRKRSRERSPRRERERSPRRPRRVVPRYTVQISKFCLDCPGCDTMELRRRYQNLYIPSD SQ FFDAQFTWVDAFPISRPFQLGNYSNFYIMHKEVDPLEKNTAIVDPPDADHTYSAKVMLLASPSLEELYHKSCALAEDPIE SQ VREGFQHPARLIKFLVGMKGKDEAMAIGGHWSPSLDGPNPDKDPSVLIRTAVRCCKALTGIELSLCTQWYRFAEIRYHRP SQ EETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWENLCHGYKQQLVDKLQGDRKEADGEQEEEDKEDGDAKEISTPTHWSK SQ LDPKIMKVNDLRKELESRTLSSKGLKSQLIARLTKQLRIEEQKEEQKELEKCEKEEEEEEERKSEDDKEEEERKRQEELE SQ RQRREKRYMLPDEPAIIVHPNWSAKNGKFDCSIMSLSVLLDYRIEDNKEHSFEVSLFAELFNEMLQRDFGVRIYRELLAL SQ PEKEEKKDKEKKCKKEDKRERKEDKDDDDEPKPKRRKSSDDKIKLEEKEERKRDDRRKEDYREEDDPDYENQDDYEPIAA SQ EEDDGDYDDREDDDDDSSSKDKREDKRDGNRYSKERQSKDKEKDKKQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILY SQ TLGLHLSRAQVKKLFTKILLKESLLYRKLTDTATEDGSHEETDPLHNDILGNCSLLPSKAVRTGLSTVEDKGGLIVYKGA SQ MVDVGSLLQKLEKSEKTRTELEHRLQTLESKTEEDEKTISQLEASNRNLSEELKQTKDDVGHLKDSLKAAEDTRSLYEDQ SQ LTNTIKNLSAAMGEIQVVLNKNPSTTEDQKSKENGSS // 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 Q645J3; PN Sigma non-opioid intracellular receptor 1; GN SIGMAR1; OS 8321; 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:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. 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 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}. DR UNIPROT: Q645J3; DR Pfam: PF04622; DE Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}. DE Reference Proteome: No; GO GO:0031410; GO GO:0005789; GO GO:0016021; GO GO:0005637; GO GO:0005640; GO GO:0006869; TP Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720}; SQ MAVLSSRAMRAALGLAVLAVVIQLLRTWLSSKSYLFNQKDIAELAKQHAGMDFEVAFSKIIVELRKKHPGHILPDEDLQW SQ IFVNAGGWMGSMCLLHASLTEYILLFGTAIDTGGHSGRYWADISDTVITGTFRQWKEGTTKSEVFYPGDTIVHVAGEATS SQ VHWSGGTWMVEYGRGFIPSTMGFALADTIFSTQDFCTLFYTFRIYARCLLLETHTYLSELGLS // 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 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 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 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 Q66H19; PN Serum response factor-binding protein 1; GN Srfbp1; OS 10116; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}. DR UNIPROT: Q66H19; DR Pfam: PF09073; DE Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}. DE Reference Proteome: Yes; GO GO:0030686; GO GO:0005634; GO GO:0048471; GO GO:0030490; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MAADPSPPSAMAQPRPLNLNNEVVKMRKEVKRIRVLVIRKLVRSVSRLKSKKGSEDALLKNQRRAQRLLQEIHAMKELKP SQ DVITKSALNDDINFEKTCKKPDSTATERAIARLAVHPLLKRKVDALKAAIQAFKDARQNAPEAESSKSASKESQCEDIPR SQ SQAEASESQHPERTVVGEQKGKDKDPTTAKKAGSGSKEKLAKGKQGPKAVATPHSPGKPSEKGAGINSERQGAPTPGNHS SQ QGKASTRTTEDSVCEPDDNSISKEEVSEEEKEYFDDSTEERFYKQSSASEDSDSGDDFFIGKVRRTRKKECAVPSSAKEQ SQ KPLPKVSSKTNTLETHWDIRNDKHKLIPEARKLESVFFHSLSGPKSSRRDPREQAPKNKAPDIPENEPPIQNKFTKSARR SQ GFESAKQPSYAPLHPSWEASRRRKEQQSKIAVFQGKKITFDD // ID Q66H96; PN Calcium-binding protein 7; GN Cabp7; 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: Q66H96; 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. {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 MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQR SQ LDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEES SQ HLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK // 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 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 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 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 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 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 Q68FJ0; PN Nuclear pore complex protein Nup85; GN nup85; 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:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. DR UNIPROT: Q68FJ0; DR Pfam: PF07575; DE Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (By similarity). {ECO:0000250|UniProtKB:Q6DK84, ECO:0000250|UniProtKB:Q9BW27}. DE Reference Proteome: No; GO GO:0031965; GO GO:0031080; GO GO:0051028; GO GO:0072006; GO GO:0015031; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEELDVDPAETPIPGLGQQNRHIGFSWGPGDLLLYETLYQKQGNSETAARCPFMYLVRSDEDIYSPVLRKLFNESHSIFV SQ GLQKSAEEASGKSRKAQLVQVSRNYRSVLRACMEEMHTLSESTRETAQKYISQISILSAMELSWNLCEILFIESAPAGPL SQ LILLLEWVRLHVCEVDNIVQDVLRSEKPTEHEKFWDGVTGYVLQGRMNEARQLLAKEASTSASARSMCRVLDDLLKKMPM SQ LHTGGTQTLTEFELKWQHWREECERHLQNGTFSSNVHMEAVCRVLLGDEEVLLEKRDLMTTWYHFLVSRLLFKHPTVKPT SQ ELHFYAQSSLDMFLAGDSCPEPLDNILLAAFEFDIHQVIKEFSIVSSNWWFVAHLTDLLDHCQLFQAHNLYFGANMREFL SQ LLDYASGLFSHHSLWQLGVDYFDYCPNLGREYLKLHMERIPLSTEKKALKALRICEQRQMTEQVRSICKTMAMQSLCNRR SQ LGSALSWSIRAKDAAFATLISDRFLKEYCERGNFTDLDLIDNLGSAMLLSDRLTFLGKYREFHRMYSQEQFSEAASLLLS SQ LMTARIAPCSFWLTLLLDALPLLEQKQVIFSAEQTYELMRCLEDRMAAKLESTSPDEIQKQDSSIDNTKVEMLRLALARN SQ LARAIVTEGALQE // ID Q68G38; PN Torsin-1A; GN Tor1a; OS 10116; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Comments: Endoplasmic reticulum lumen. Nucleus inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus envelope is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface. DR UNIPROT: Q68G38; DR UNIPROT: Q8K3L8; DR Pfam: PF06309; DE Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). {ECO:0000250}. DE Reference Proteome: Yes; GO GO:0005623; GO GO:0030054; GO GO:0005737; GO GO:0030659; GO GO:0005783; GO GO:0005788; GO GO:0042406; GO GO:0030426; GO GO:0043231; GO GO:0016020; GO GO:0043005; GO GO:0005635; GO GO:0005637; GO GO:0005634; GO GO:0030141; GO GO:0008021; GO GO:0005524; GO GO:0016887; GO GO:0008092; GO GO:0042802; GO GO:0019894; GO GO:0051787; GO GO:0051082; GO GO:0007155; GO GO:0051085; GO GO:0061077; GO GO:0072321; GO GO:0071712; GO GO:0045104; GO GO:0031175; GO GO:0006998; GO GO:0071763; GO GO:0006996; GO GO:1900244; GO GO:0000338; GO GO:0051260; GO GO:0034504; GO GO:0051584; GO GO:2000008; GO GO:0006979; GO GO:0048489; GO GO:0044319; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MKLGRATLALLLLVPCVVRAVEPISLGLALAGVLTGYISYPRLYCLFAECCGQKRSLSREALQKDLDNKLFGQHLAKRVI SQ LNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQMWIRGNV SQ SACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFLSNAGAERITDVALDFWRSGKQREEIKLRDMEHA SQ LAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEEDEDIINKVAEEMTFFPKEEKVFSDKGC SQ KTVFTKLDYYLDD // 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 Q6AX31; PN Nucleoporin NDC1; GN ndc1; OS 8355; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0185; SL Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16600873}. Nucleus membrane {ECO:0000269|PubMed:16600873}; Multi-pass membrane protein {ECO:0000269|PubMed:16600873}. Note=Central core structure of the nuclear pore complex. DR UNIPROT: Q6AX31; 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. {ECO:0000269|PubMed:16600873}. DE Reference Proteome: No; 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 MTMLGERLVLRWRVAASFAWSVILMPVCCALFIVLSRIQILHPIQWLTDSISDLTSSYTIFCLLLICAILGLQCTFLMEY SQ YTVVPSIPCSRLALIGNLLLPHRILHSLAHVAMGVLASWCYAVLSKGKYQLLVVSCTLQSEDEADKPSHCLNESHLFQLL SQ CGAFFGYSYSLQYFVHNMNYLSFPSIQQYKYLQFRRFLPLIIKQSVFQSLYFIRSYAILYFCLGNIPRTWIQTALNLHMD SQ RQQPSLDTLRGFLNLSLFYQIWLSGTFLLATWYMVWILFRIYTTEARIFPVQTSFAEEAEKCLPFILNSNTLPLVKYLAM SQ QDLVLLSQYSPSRRQEVFSLSQPGGHPHNWTSISKECLNLMSSLTSRLIAHQEAAANNGRMRVPSSPKQIRKSSSSSGTS SQ LIEDSAEQTQNLSTIPRIGIPSLLKTASLKSSLDIGSPFATPGVKQMSESLDPNTPCHGSVQSPQVTRRGAKLWTSDSDV SQ QKNGSEVSPVMHRPVCNGAKQGILHTWFQHKLVQIKNVLSKRGLIMYLFSKHPEASSQDVFADAQIHIWALEALSHLVAA SQ SFSEDRMGVVQTSLSSVLAILLTLQEAVEKHFKLPHASSKPARNPGSLLDSSCKTLRFSLRAALKTAIYRITTTFGEHLH SQ AVPVSSEHKKKLQQFLDFKE // 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 // 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 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 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 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 Q6BRJ9; PN Nuclear protein localization protein 4; GN NPL4; OS 284592; 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: Q6BRJ9; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MFRINVDAGSDFLLVLEELVGKLSTNDIQSIYISDKPNSKGEQANSLCGRSVNDLGFKNGDLLFVTYESTGEPPKTESSA SQ PLTTAKTTNGANVSINMNDISIPINKGPGPLKVDQLPVDGLLDKEEGMIMRPRSDLCRHGDKGMCEYCSPLPPWDKDYRK SQ EKGFKHMSYHAHLNEINESKNNRNNATSYMAPLEEPNYNINLNCPSGSHAPYPKGICSKCQPPVITLQQQQFRMVDHVEY SQ ADSTILNKFIDSWRTTGVQRFGILYGRYEQFDKVPLGIKAVVEAIYEPPQSGELDGLTLLPWENERQVDEIAASLGLYKV SQ GMTFTDLTDSGAKNGTVLCKRHKNSYFLSCLEVIMAAKYQVSNPNITKHSNSGRFSSKFVTCVISGGMNGEIEPRSYQVS SQ NSAEALIKADIITGSTQPSMLYINDSEGKRYVPDVFYSKINEYGLEVKTNAKPAFPVEFLLVSLSDSFPLDPSPMFRENF SQ PIENRDFMGDLQDLKSAYNYLNADPGDGSQLFDFHFLTYIAKTGILSHDELKLVLSYVRNKDQTDYLQLVESPGWMTFIT SQ ILEQSV // ID Q6BZX5; PN Protein transport protein SEC13; GN SEC13; OS 284591; 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: Q6BZX5; 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 MVTIGNTHDDLIHDAVLDYYGKRLATCSSDKTIKIFEIDGDNHKLVETLRGHEGPVWQVSWAHPKFGSIIASASYDGKVF SQ IWREENGRWTNIAQHQHNASVNSVVWAPQEYGPLLLCASSDGNVSVVEFKEGGNCEATTFAAHDVGANSASWAPPAVSGS SQ LIQPINGKASNNIRIVTGGCDNLVKIWKYDPSSKTYVIEETLSGHKDWVRDVAWSSSVLSKSYIASASQDKTVIVWTQEG SQ NQPWKKKLLQDIPFPDVVWKVSWSLSGNVLAVSGGDNKVTLWKENLTGEWESAGVVEE // ID Q6C3X7; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 284591; 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: Q6C3X7; 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 MSDQVSDMLEKLELQKEKNQAAATEAKVEEVKEDDKKDVKEELNEDDKKVAKEDDKKEDAKEESKEDAEENNLIQTEYEV SQ RVKLADLQADPNSPLYSAKRFEDLGLDENLLKGLYAMKFNKPSKIQEKALPLLLSDPPHNMIGQSQSGTGKTGAFSLTML SQ SRVDPNLKAVQCICLAPSRELARQTLDVVDEMKKFTDITTHLIVPESTERGQKVTSQILVGTPGSVAGLLQKKQIDAKHV SQ KVFVLDEADNMVDSSMGSTCARIKKYLPSSTQVVLFSATFPESVLDLAGKMCPNPNEIRLKANELNVDAITQLYMDCEDG SQ EEKFKMLEELYSMLTIASSVIFVAQRSTANALYQRMSKNGHKVSLLHSDLSVDERDRLMDDFRFGRSKVLISTNVIARGI SQ DIATVSMVVNYDLPTDKNGKPDPETYLHRIGRTGRFGRSGVSISFVHDEASFEVLDSIQQSLGMTLTQVPTDDIDEVEEI SQ IKKAIKGK // ID Q6C619; PN Nuclear protein localization protein 4; GN NPL4; OS 284591; 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: Q6C619; 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 MILRFRSKKGTLRAEAQPTDLFDVAFKKLTEDLPDIDPATITLATSPTGKQEPASRLLGKTVQKLGLNHGDMLFVSYTDS SQ APRAAVEAVTAETAPQMTAAHIRDATKQLPVDDYLEKQDGKIKRQLSALQQRKFGSRGMGEDTLPVDPWDEEYLKEQKIK SQ HMSYHAYVKKLNSQANKKNGGGYIAPLNVSDFGVSKSCTGAHAPWPEGICSRCQPSAITLQSQPFRMVDHVEFAESGMIN SQ SFIEPWRQSGTQRIGWMYGHYEPYELVPLGIKAVVEAIYEPAQSGEYDGITITEITQADGQPQPPHIATAEACGLVPLGV SQ IFTDLVDAGNGDGSVICKRHADSYFLSSLEVAFAGAMQARFPNKSRWSPTSEFSSKFVTAVISGNPKGEIDVSCYQVSEQ SQ CEAMARADLIEPSINPSVLLVKEATKTRYVPDVFYKKNNEYGRTVLQGANPQLPVDYMLVTLTHGFPQDPRPLFSSGLSS SQ FPVENRELIGVTQSPQALGKALDSGSAGGAVSNFHLLSYIQSMGVLSAEEFQLLAKVATEKKDEDVSRLVASEGWNNLLL SQ IIQ // 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 Q6CF02; PN UDP-N-acetylglucosamine transferase subunit ALG14; GN ALG14; OS 284591; 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: Q6CF02; DR Pfam: PF08660; DE Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (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 MVTTILIAASAILVLLLLRLLFVLPASNRFGFLYRPKHSNPKLMVMMGSGGHTGEMLRMLKTLKLQSYAKRVYVSSSGDV SQ DSLEKVKVLESTTKTDIKTMVLENIPRARKVGQSYPSSVITSAVSFAVAVKLVHKHKPHVIVCNGPATCVMLCYAAFLLR SQ FMALIDTRIIYVESLARVNRLSLSGLILLPFCDRFLVQWPQLAEKYPRAEYHGILV // 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 Q6CJG3; PN UDP-N-acetylglucosamine transferase subunit ALG14; GN ALG14; OS 284590; 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: Q6CJG3; 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 MLLTTAWCLLIWSVTLLLVRICLVIPIFHSSREAGPLTKDKDNVGGRMKNLVLFIFLGSGGHTGEMLRLIEHYQGMLLES SQ AVTIHVGYSDDDSIIKFKNKIHQISVSNTLRAKVIYHRFDKARDVGSSLAGSIKSIIKTAIRSMVLTYRIKSSMRGHPNL SQ TLLNGPGTCCIITFWLKLYHIFLWQPSKIVYVESLARTNRLSLTGMILYPLADEFVVQWADLLPIYPKAKYYGVLV // 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 Q6CLY1; PN Nuclear protein localization protein 4; GN NPL4; OS 284590; 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: Q6CLY1; DR Pfam: PF05021; DR Pfam: PF11543; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MLLRLRSKLGIHRVSCEGNDNFGSVIEKWANQLRLNVDPDSVSVSTQPGVSKLMTEIAHQGVESLGLRHGDMVTVEFKVL SQ DTEEKNVSEKEMTNMTVSASTTSVPISSSHNKGSIRGKVKESALDIELEGETGLIPRSRSSLCRHGEKGMCEYCSPLPPW SQ DKGYQDEHSIKHISFHAYLKQLDEVTNKKSSGSSYIPPLSEPNYEINLNCAGGHEPWPKGICSKCQPSAITLQQQSFRMV SQ DHVEFQESELINQFIDSWRTTGMQRFGYLYGYYKRYDNVPLGIKAVVEAIWEPPQHDEQDGLTMDMDQVVKEVEDTDKLA SQ REMGLERIGMIFTDLTDTGLGDGSVYCKRHKDSFFLSSLEVIMAAKHQLRHPNVSKFSETGLFSSRFVTCCISGNLNQEI SQ DIATYQVSIEAEGLVEADLISGSTHPSQAYINETNDKRYVPEIFYTRKNEYNLTVKQNAKPAFPVDYLLVSLTHGFPKET SQ DDDSTTTANTTTVFKTVAGFPWTNRQAMGQSQDYTELKRYVYKACTGNDLAELQAKLSNFHFLLYLHSIEVLNQQEWSLL SQ IRTVTAPTLHEATEPLLNLINSPGWQTFVMILEQSM // 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 Q6CSZ5; PN Protein transport protein SEC13; GN SEC13; OS 284590; 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: Q6CSZ5; 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:0005789; GO GO:0000139; GO GO:0031080; GO GO:0035859; GO GO:0005198; GO GO:0090114; GO GO:0051028; GO GO:0031081; GO GO:0043547; GO GO:1904263; GO GO:0045893; GO GO:0015031; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MVTINNAHSELIHDAVLDYYGKRLATCSSDHTVKIFEVEGETHKLVDTLQGHEGPVWQVDWAHPKFGVILASCSYDGKVL SQ IWKEVNGRWSQIAAHEVHSASVNSIQWAPHEYGPLLLAASSDGKVSVVEFKENGTTSPIIIDAHSIGANTACWAPATLQQ SQ QSNQGTSGSASPQQVRRFVTGGADNLVKIWKYNSDAATYLLEHTLEGHSDWVRDVAWSPTVLSRSYLASVSQDRTCIIWT SQ QDSKEDTWKKTLLKEDKFPDVLWRASWSLSGNILALSCGDNTVTLWKENLEGKWEPAGQVTE // 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 Q6DBQ8; PN Ceramide-1-phosphate transfer protein; GN cptp; OS 7955; 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: Q6DBQ8; 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 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 MADAFSLQRVLETFRSSLSENKEVYIKYYIAGWQELVSFMNSLGNVFSFISKDVVSKIQILENFLSGENGSNYVTIQSMV SQ KYELENDLVDLTKRGSHPESGCRTLLRLHRALRWLELFLERLRTSTEDSKTSVMCSDAYNESLANHHPWLIRKAVGVAFC SQ ALPGRETFFDVMNAGDHTQVVALLGESLPLIAEVYQITEDLYAKNNLLELP // ID Q6DBY0; PN Nuclear pore complex protein Nup85; GN nup85; 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:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. DR UNIPROT: Q6DBY0; DR Pfam: PF07575; DE Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (By similarity). {ECO:0000250|UniProtKB:Q6DK84, ECO:0000250|UniProtKB:Q9BW27}. DE Reference Proteome: Yes; GO GO:0031965; GO GO:0031080; GO GO:0017056; GO GO:0006406; GO GO:0072006; GO GO:0045893; GO GO:0006606; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEELDVEPSTTLVPAAGVLQKHLGFEWGPGDLLVYETNYKLRGSSSAGSPLVHVVRKDEDICSPILRKLFNESHLIFMGL SQ QKIKEDAPSKNKKTQFVSISRNYRSVIRACMEELQQNAVTAQDGSLASQYGDQVSILLAIELIWNLCEVLFIEAAPAGSL SQ LLHLLNWVRLHKSDVDTRAREVLQSENPTQHPAYWDVVTSLVLQGRMDEARQILSKQASLRMESSSVFKRMDTLLQTMPI SQ FNPAGAQTLTEFDVKWRHWHEECDRCLQDHTFASSAELETLCKILLGDEDVILEQKDLMSTWYHFLVSRLLFTHPTIKPP SQ DLHYYAQSSMNMFLGPRATPEPLDIILLSAFEFDLHQVIKDCSIALNNWWFVAHLTDLLDHCKLLQSHNLHFGSNLREFL SQ VLEYASGLFTHHSLWQLAVDYLDHCPEFGRVYLELQIERVPLDTERKANKVLRICEDRQMSEQVRSICKIMAKRALRNNR SQ LGSALSWSIRAKDAALATLISERFLQDYSNKGSFTDLDVLDNLGPAMLLSDRLTFLGKYREFHRLYGENRFSDAAKLLLS SQ LMMAKIAPRSLWMTLLTDALPLLEQEEVIFTVDQTYELMSCLEELNSGTKDSNQMEQEEDLESTKTELLRVALARNLATA SQ IVKEGTIET // 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 Q6DFQ5; PN Sigma intracellular receptor 2; GN tmem97; OS 8364; 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: Q6DFQ5; 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:0000250|UniProtKB:Q5BJF2}. 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 MAVCARLLEWIFFFYFFSHIPITLLVDLQAVLPPSLYPQELLDLMKWYTVAFKDHLMANPPPWFKSFVYCEAILQLPFFP SQ VAAYAFFKGGCKWIRIPAIVYSAHVATTVIAIIGHILFGEFPKSDVIAPLTQKDRLTLVSIYAPYLLVPVLLLLTMLFSP SQ RYRQEEKRKRK // 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 Q6DGE9; PN Protein unc-45 homolog B; GN unc45b; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. DR UNIPROT: Q6DGE9; DR UNIPROT: Q8UVX6; DR Pfam: PF11701; DR PROSITE: PS50293; DE Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain (By similarity). Plays a role in sarcomere formation during muscle cell development. Required for myoseptal integrity, myofiber attachment, motility and craniofacial development (PubMed:17189627, PubMed:17586488, PubMed:20440001, PubMed:20849610). Is necessary for normal early lens development (PubMed:24549050). {ECO:0000250|UniProtKB:Q8CGY6, ECO:0000269|PubMed:17189627, ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:20440001, ECO:0000269|PubMed:20849610, ECO:0000269|PubMed:24549050}. DE Reference Proteome: Yes; GO GO:0031672; GO GO:0005737; GO GO:0048471; GO GO:0030018; GO GO:0051879; GO GO:0048738; GO GO:0061077; GO GO:0002088; GO GO:0048747; GO GO:0030239; GO GO:0060538; GO GO:0007519; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MTMGEIGDSVQLKEEGNKHFQAGEIDQAIDCYTKAIKTCKKEDKKALAVIYRNRSACFLKKENYSNAASDATKAIDVDAA SQ DIKALYRRCQAFEKLGKLDMAFKDVQRCATIEPKNKTFLETLRRLGAEIQQKLKTTFSTDSRVQNMFDILFSDEPDKEKR SQ EKAANNLIVLAREDAGAERIFQNNGVPLLMQLIDTGKPEMILAAIRTLSGMCTGHRARATAIIHSVGISKLCSIMAVDNE SQ EIALATANLFQCVNDSLSGGDKRNYGKEEALVLDSSKDLKDILLALLEMIASKNVSGHGRDQALNLLTKNVPRQNKKSTD SQ NSKCLFTIDHGLKKILKVCGQVPDLPDQLPMTENTQLIASVLLSKLYDDLRCDPERDQFRDICDDYIKSKFDPNDMDKNI SQ HAINTLSGILQGPFDLGNVLAGRQGVMEMMVALCGSEREVDQLVAVEALIHASTKTSKASFFISNGVSLLKEMYKKTKNE SQ KIKIRALVGLCKLGSAGGDDYSMRQFAEGSTEKLAKQCRKWLCNPTLDVRTRKWAIEGLAYLTNDADVKDDFAEDEPAMR SQ AMFELTKSNDKTILYAVACTLVNCTNSYDKKEIIPEMVQLAKFSKQHVPEQHPKDKKDFIVRRVKRLLKAGVTSALAVMV SQ KADNSILTDQTKEMLARVFLALTEDVKDRGIIVAQGGGKALIPLALEGTDKGKIKASHALAKIAAVSNPEIAFPGERIYE SQ VVRPLVSLLGTDRDGMENFEALRGLTNLAGLNDKLRVKILKEKALPEIENYMFEDHEQIRQAATECMCNLVCCKEVQDRY SQ LEDGNDKLKLLVLLCGEDEEKLQRAAAGALAMLTAAQKKLAVKMTKVTEQWLEILQRLCIHDNPEIQHRGLVTVFNMLDA SQ DDQLAKKLVESDMLEILTYVAKLEDNPKKQNAIDAARACLSKAMDNGLIKPFSN // ID Q6DRB1; PN Nucleoporin GLE1; GN gle1; OS 7955; 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}. DR UNIPROT: Q6DRB1; DR UNIPROT: Q502U5; 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:0005576; GO GO:0044614; GO GO:0000822; GO GO:0005543; GO GO:0031369; GO GO:0060287; GO GO:0006406; GO GO:0048666; GO GO:0016973; GO GO:0060296; GO GO:0006446; GO GO:0006449; GO GO:0014044; GO GO:0014037; GO GO:0014010; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MPSENLRWETLEALKNSPKGKLKYSPDWVEKGEDVLAGCVEVPSLSPLSGQILKRMSPRMLLKNCSRSSSVRDTSPGLSE SQ EAAVCRSAPISPRLKRSSCSLPAVSIQTEEEEEKEEEEKAEVVVEAPAVSPEASVSTPPAVSVLSPRATQISGCIRMCEQ SQ KHKAKAKMELSLRQEQQERLVATVANHESEQLKRFEEFMELKQRQEHQSIRDTNEKEAQESLGRQEKLREEHRHRMKILN SQ LRLREMEQQRLREVELERQRQVEGRERHRAINAIQEEVLQLNRLLQPQQSTHAEVEHAPYITRGNQLCSQLSEVVPAAAD SQ DQFPSVEDLSVAERALQEMRSLVRSLQEAVSQAAERKKKKEQEEEEEKRRQEQLKAQQEEQKKSAALSAKEKAKKEGLQT SQ GADDSTLKWYNSLQDLANQCAQAFDDLNKAKDTQTKKLKMELQKAATTPVSQIANSSGAPLKEAFEKIDKLLSRRPVTSA SQ GKTVSTSQHPQGLEFASYRLAEKFVKQGEEEVASNHSAAFPIGAVASGIWELHPKIGDLILAHLHKKCPYAVPHYPPMES SQ GTSVEDYQKILGYRVDEGKVEGQDSFLKRMSGMIRLYAAIIQMRWPYSSKQGLHLHGMNHGWRWMAQILNMEPLADITAT SQ ILFDFLEVCGNALMKQYRVQFWKLILIINEEYFPRYLCFASILHFTCIHWLQNIE // 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 Q6FJI2; PN Nuclear protein localization protein 4; GN NPL4; OS 284593; 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: Q6FJI2; DR Pfam: PF05021; DR Pfam: PF11543; 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:0036266; GO GO:0000837; GO GO:0000839; GO GO:0031965; GO GO:0048471; GO GO:0030894; GO GO:1990112; GO GO:0034098; GO GO:0071629; GO GO:0006274; GO GO:0071712; GO GO:0072671; GO GO:0051228; GO GO:0051028; GO GO:0051974; GO GO:0070651; GO GO:1900182; GO GO:0072665; GO GO:0030970; GO GO:1990116; GO GO:0030433; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MIIRFRSPVGMHRVRCEGSETLGQVLPQLQTILNEHGITPRAIELGKEANGKDKTNVESLLEKTIEALGFRHGDIVYVHY SQ QVDSSETKGSANDNNGSVAVNIPNNLVPGKSQKADELEVDKELEKLDGLIPRQKTKLCKHGDRGMCEYCSPLPPWDANYA SQ NENNIKHISFHAYLKKLNESTNKRESGSSYIAPLSQPNFKINKHCTNGHEPWPKGICSKCQPSAITLQQQEFRMVDHVEF SQ QSSELINQFIEFWRASGTQRFAYLYGKYEKYDATPLGIKACVHAIYEPPQHDEQDGITMDMEQVTQELNTIDLLAKEMGL SQ LRVGMIFSDLTDAGNGDGTVLCKRHKDSFFLSSLETIMAAQHQTRHPNVSKFSEQGIFSSKFVTCVVSGNLKEEIDIASY SQ QVSIDAEALVSADMIGGSTHPSMAYINDTTEDRYVPEIFYMKKNEYGLTVKENAKPAFPVDYLIVSLTHGFPKDEDTTTQ SQ LFNSVTGFPWSNRQAMGYSQDYHELKRYLHSTAASGNFNDLHDKLANFHLLLYIHSLQILSQEEWELLVKGALSQDYQEP SQ LYKLSASPGWQTLLMIIESA // ID Q6FKN8; PN ATP-dependent RNA helicase DBP5; GN DBP5; OS 284593; 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: Q6FKN8; 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:0005934; GO GO:0010494; GO GO:0031965; GO GO:0044614; GO GO:0005844; GO GO:0005524; GO GO:0000822; GO GO:0003723; GO GO:0003724; GO GO:0008186; GO GO:0016973; GO GO:0006415; GO GO:0006409; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250}; SQ MSATEDKKDPASMLAELKLDKDEGNKTPETKTPESNSAETKTTEEVKELKNPFTQKKEDVENDAAEEKTNEVNKDDAKDE SQ RENKDTNLIKSEYEVKVNLADLQADPNSPLYSVKSFDELGLSPELLKGIYAMKFQKPSKIQERALPLLLSNPPRNMIAQS SQ QSGTGKTAAFSLTMLSRVDETQNVPQAICLAPSRELARQTLEVIQEMGKYTKITTQLIVPDSFEKNTKINANVVVGTPGT SQ LLDLIRRKLIQLQNVKIFVLDEADNMLDKQGLGDQCIRVKKFLPKDTQLVLFSATFADAVKAYAQKVIPNANTLELQRNE SQ VNVKAIKQLYMDCNDEAHKYEVLCELYGLLTIGSSIIFVAKKDTANLLYGKLKHEGHQVSILHSDLRTDERDRLIDDFRE SQ GRSKVLITTNVLARGIDIPSVSMVVNYDLPTLPNGMPDYATYVHRIGRTGRFGRTGVAISFVHDKKSFKILSAIQDYFKD SQ IELTRVPTDDWDEVEDIVKKVLKQ // 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 Q6FQU6; PN Protein transport protein SEC13-2; GN SEC132; OS 284593; 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: Q6FQU6; 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:0005789; GO GO:0000139; GO GO:0005643; 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 MVKIENAHEGVIHHAALNYYGTRLATCSSDKTVKIFEINDVNNSSSLLETLVGHEGPVWYADWCHPSLGENLLATCGYDG SQ KVLIWKESGHGGKMQIIGKHAVHSASVNCVKWAPHEYGLILLCGSADGKISVVELKDGQIASTKILDNAHKFGVNSISWA SQ PLMKTDSSDDGDETTAVKQFISGGNDNLVKIWKFDDDQETYVVADTLEGHKDAVTAVDWSPTTLLQSYVASVSNDKQCLV SQ WTQDHSSKKNDWKKISVNEGKFEQKLGSVSWSLSGNLLAVSDDDKNVTIWKESGDGKWEEVVN // 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 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 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 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 Q6GLC9; PN Synaptic functional regulator FMR1; GN fmr1; OS 8364; SL Nucleus Position: SL-0198; SL Comments: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. 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:0000250|UniProtKB:Q06787}. 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:0000250|UniProtKB:Q06787}. DR UNIPROT: Q6GLC9; DR Pfam: PF05641; DR Pfam: PF16098; DR Pfam: PF12235; DR Pfam: PF00013; DR Pfam: PF17904; DR Pfam: PF18336; DR PROSITE: PS51641; DR PROSITE: PS50084; 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. Binds poly(G) and poly(U), and to a lower extent poly(A) and poly(C). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:P51113, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}. DE Reference Proteome: Yes; GO GO:0030424; GO GO:0043679; 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: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: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:0003682; GO GO:0070840; GO GO:0002151; 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:0003723; GO GO:0035613; GO GO:0033592; GO GO:1990825; GO GO:0035197; GO GO:0045182; GO GO:0030371; GO GO:0006974; GO GO:0072711; GO GO:0034644; GO GO:0007215; GO GO:0006397; GO GO:0051028; GO GO:2000766; GO GO:0010629; GO GO:1900453; 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: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; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWW SQ LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVS SQ YDSENYQLVILSVNEVTIKRANMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN SQ IQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA SQ ENDKNISPEEGMVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRPDKEKGYQSEDL SQ SGTGRGSRPYNNRGRSRRGTGYASDIRYGDPDYRKTTYPEYPRSQAFWIKGTNSEASNASETESDHRDELSDWSLAPAED SQ DRDNYHRRGDGRRRGGPRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEG SQ SRLRTGKDRVQKKEKSEVVDGPQVVVNGIP // 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 Q6INS1; PN F-box/LRR-repeat protein 5; GN fbxl5; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250}. DR UNIPROT: Q6INS1; 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: No; 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 MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSNNNDLLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSHTVYNVH SQ SDNKLSEMLVLFEKGMKNVKNEYKQLNYVQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDEMKDIKKKVIAQHCS SQ QKDTTELLRGLSLWNKAEELQKVLKYSVDEKAERNSKTQKSSSSISSLPPEVMLNIFTYLNPQDLCRCSQVNTEWAQLAK SQ TGSLWRHLYPVLWARGDWYSGSHAYLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEEEDSSISMAQREKELLNS SQ LVHYILPYVGHSVKTLVLAYSSATSSKVIRQMLEYCPNLEHLDLTQTDISDSAFNGWHFGACQTLHHIDLSGCDKITDLT SQ LEKLSVALGIPSAHKKRLLKCYRNNRTLKDIRNQMRCSSLAQITGESTIYSDAFWANSDRSQDYTSPPIWILDSGNPGDI SQ EDAADWKFRTTDGLCVLEMAPSVTCFSNGCCSRARPGRWTNVGWQEHCKAATVSYCGHTLCGNTLRTIHTLPEASALCNI SQ GTRTLHSDITDCFPGSAKSDQQAARALQFLSLSGCHQITDHGLRALTIGGGLPKLEHLNLSGCLNVTGSGLQDLVATCPS SQ LNDEHFYYCDNISGPHGATASGCQNLQCGFRMCCRSGE // ID Q6NRD3; PN E3 ubiquitin-protein ligase SH3RF1; GN sh3rf1; OS 8355; SL Nucleus Position: SL-0198; SL Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. DR UNIPROT: Q6NRD3; DR UNIPROT: Q3L1I1; 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. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway (By similarity). Plays an essential role in the anterior neural development. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:16125690}. DE Reference Proteome: No; GO GO:0005794; GO GO:0030027; GO GO:0048471; GO GO:0005078; GO GO:0046872; GO GO:0061630; GO GO:0006915; GO GO:0001764; GO GO:0046330; GO GO:0051865; GO GO:0043370; GO GO:2000564; TP Membrane Topology: Unknown; Source: UniProt - Sequence Analysis; SQ MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRKELRCPECRTLVECGVDELPSNILLVRLLDGIRQRP SQ RKAGDGGSAGNSTNALRAQGSVTTNGGLNDAQNTQSGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIV SQ LRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGML SQ GDKIGIFPISYVEFNSAAKQLIELDKPSGADTGEGSSGTSHSGNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSM SQ EISPPVLISSSNPTAAARISELTGLSCSAPSQDMNPPLLPPPPMATPVITSASSGAAAVAQRNIIGPVEQVPHLRTSARP SQ SVFIAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRALTTATPAKVAMATATTSNVV SQ NLVTPTPPGAPCQKLPVSGVEFAKTSSTNGVSPAGVPGCHIQTSPQSKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAA SQ VTPIQAQTPAASALPQQAAASQQVPPPLSAPAAYINAAMNISRPSVPAASAASSALPTAAFEAESSWKSSSGLSGCSFSE SQ NVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPHSPTQEVEQTNSEAAAALEGAVGPDIVPVIVNGRAAPC SQ TVDCDSVSASTPAQDNRKPASLDNNIPIAPPPRQPCSSLGSVLNDSRPCERYRVMVSYPPQSEAELELKEGDIVFVHKKR SQ EDGWFKGTLQRNGKTGLFPGSFVENI // 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 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 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 Q6NW58; PN Spastin; GN spast; OS 7955; SL Nucleus Position: SL-0198; SL Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {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}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}. DR UNIPROT: Q6NW58; DR UNIPROT: Q6JUU0; 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. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also 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: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:0048675; GO GO:0019896; GO GO:0007409; GO GO:0021955; GO GO:0032506; GO GO:0031122; GO GO:0006888; GO GO:0007032; GO GO:0010458; GO GO:0090148; GO GO:0001578; GO GO:0000226; GO GO:0051013; GO GO:0000281; GO GO:0051228; GO GO:0043066; GO GO:0031468; GO GO:0045773; GO GO:0031117; GO GO:0034214; GO GO:0051260; GO GO:0072593; TP Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021}; SQ MNSGHKARLRGGRACGPVSDGSARGNRLLFYTRSLSRVPEWLLRVLLLLLRWLFQPIRRAMAARAKECGPDGSEETGERI SQ RNYHKQAFEFISVALQIDEDEKGDKQKAVQWYRKGIAELEKGIQIQVTGAGEKADRARKLQDKMITNLSMAEDRLKLLGN SQ LLSQSPAESSSDDSFYSFSNGNLRPAPASGAVSKKKDTLTITNQTSLRPKNPPKSTPNASGLNCTPSAAQSSRTGPQNNQ SQ KGPTVKGKNNVKASTTATASPQRKRDMKNFKNVDSKLASLILNEIVDSGSVVRFDDIAGQDLAKQALQEIVILPALRPEL SQ FTGLRAPARGLLLFGPPGNGKTMLAKAVAMESNATFFNISAATLTSKYVGEGEKLVRALFAVARELQPSIIFIDEIDSLL SQ CERREGEHDASRRLKTEFLIEFDGVQSGGDERVLVMGATNRPQELDEAVLRRFAKRIYVALPTEETRLKLLKNLLSKHRN SQ PLSQKELSQLARLTDGYSGSDLTSLAKDAALGPIRELKPEQVRNMSAHEMRDIRISDFLESLKRIKRSVSPQTLDQYVRW SQ NREYGDTTGV //