A0A024B7W1 RNA-directed RNA polymerase NS5 POLG 2043570 No SL-0382 [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}. UNIPROT A0A024B7W1 PDB 5GOZ PDB 5GP1 PDB 5H30 PDB 5H32 PDB 5H37 PDB 5IRE PDB 5IZ7 PDB 5JMT PDB 5KQR PDB 5KQS PDB 5KVE PDB 5LBS PDB 5LBV PDB 5LCV PDB 5M5B PDB 5MRK PDB 5NJU PDB 5NJV PDB 5U4W PDB 5UHY PDB 5ULP PDB 5Y0A PDB 5Y6M PDB 5Y6N PDB 6CO8 PDB 6I7P PDB 6JFH PDB 6JFI PDB 6NIP PDB 6NIU Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0051539 GO:0005524 GO:0003725 GO:0005525 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0075512 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039574 GO:0039502 GO:0039694 GO:0019062 MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL 3423 A0A096MK47 Muscular LMNA-interacting protein Mlip 10116 Yes SL-0178 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}. UNIPROT A0A096MK47 UNIPROT D4A3C4 UNIPROT Q569A0 Pfam PF15274 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}. GO:0005635 GO:0031981 GO:0005634 GO:0016605 GO:0042383 GO:0005521 GO:0003714 GO:0010614 GO:1903243 GO:0000122 GO:0045944 MEFEKHEQGNALKKNEKLEERVTFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSHGSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKSLSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSLADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRHSDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSLPVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVEHSSDSPSRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDSSGLFSEQ 807 A0A0B4K7J2 E3 SUMO-protein ligase RanBP2 Nup358 7227 Yes SL-0178 SL-0185 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}. UNIPROT A0A0B4K7J2 UNIPROT D3DMF2 UNIPROT Q8SWV7 UNIPROT Q9VBU7 Pfam PF00638 Pfam PF00641 PROSITE PS50196 PROSITE PS50293 PROSITE PS01358 PROSITE PS50199 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}. P34082 EBI-868243,EBI-191234 Q24090 EBI-191234,EBI-151570 Q9XZC2 EBI-191234,EBI-458892 Q9VWE4 EBI-191234,EBI-122539 Q9VU13 EBI-191234,EBI-137049 A1ZAC2 EBI-152117,EBI-191234 GO:0005642 GO:0005737 GO:0005643 GO:0005634 GO:0046872 GO:0008536 GO:0019789 GO:0007281 GO:0035626 GO:0051028 GO:0006607 GO:0051292 GO:0034587 GO:0008284 GO:0010628 GO:0043547 GO:1900182 GO:0046833 GO:0006606 GO:1903827 GO:0010528 GO:0007419 MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREVLANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDRENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHIENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQIQREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKADAIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMFRIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRNSRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVGMEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVPNPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSMFPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVPTVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLPKPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEEAEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCDKATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKASEAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAPASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEYVPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCNQRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPIKGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGFSFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDTVPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAAKEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVMRREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVGSVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSLSRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAAEQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFGIPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLASNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAIVELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMDYMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS 2718 A0A0G2JXT6 Myotubularin-related protein 6 Mtmr6 10116 Yes SL-0198 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}. UNIPROT A0A0G2JXT6 Pfam PF06602 PROSITE PS51339 PROSITE PS00383 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}. GO:0005783 GO:0005793 GO:0005635 GO:0048471 GO:0032587 GO:0015269 GO:0106018 GO:0004438 GO:0004725 GO:0006897 GO:0046856 MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMKGFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQKEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQNKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSEPAVVSLEYGVARMTC 655 A0A125S9M5 Lamin-2 LMN2 232323 No SL-0178 SL-0179 SL-0182 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}. UNIPROT A0A125S9M5 Pfam PF00038 Pfam PF00932 PROSITE PS51842 PROSITE PS51841 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}. GO:0005882 GO:0005637 MSAQVSKKRGGSNPPKTGQHAASSTTSRTESSATSQTIYERQEVETRTQRTPGGLLLAASSAEVSSGTAGLAGSPLSRHQEKEEFKLLNNRFANYIDTIRAQQEEISVLRRKVETVSSKEVVENQKIKERYNLEIANLRRALDEVSRDLAAAIIERDSLRPERDARLLLDNEKKTLQKRSKDAEAALKDAKNQLAALRDQAKDHDNEIHGLTTENSSLKLQIENLKKDLSQETNLRVDAENRLQSEREKNALLEGIHNEEIVSLRNQRRTEITEVETRMGEEYQSKIVEQLNDLRADLEAVAHEMRLDLERSYQNQLEDSQDLANRYRDEARALLADLSAAQDRIKETQTRSEKQLQELRLQLQRLQAELNGKDDEVQRLQKLLADRQAELQNTHHELSRQIASYQELLDEKIHLDAELATYNALLRTEEERLNMKSPPFPSTPDSQRRGTKRRIADSYTRTRFRNEASATGDIHISEIDAEGQFVRLENKSGQDVVIGGWKLLMVSDNGEDNKTDYKIHSNQVIKAHSSTTIWSANTNVVHEPPADIVMEGRWLVGDHTSVTLSTSDGVEVARREMTQSSTRDDSYLGPSGLPKRSRLVVADSSDHQKNCVIM 614 A0A1I9LN01 Protein LONG AFTER FAR-RED 3 LAF3 3702 Yes SL-0198 Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}. UNIPROT A0A1I9LN01 UNIPROT F4IY42 UNIPROT Q7Y048 UNIPROT Q7Y049 UNIPROT Q93ZE1 UNIPROT Q9LY60 Pfam PF07969 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}. GO:0016021 GO:0048471 GO:0016810 GO:0009704 GO:0010218 GO:0009845 MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP 583 A0A2R8Q3S9 Chloride channel CLIC-like protein 1 clcc1 7955 Yes SL-0178 SL-0182 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}. UNIPROT A0A2R8Q3S9 Pfam PF05934 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}. GO:0034707 GO:0005789 GO:0000139 GO:0031965 GO:0005254 MKLSSSSSFGLCILVVFFCFVVIESAKIRIDGYNDEAWIDPYDMLNYDPTTKRMRKSTESESYQNVPTKRREFNSESCDVPKCPDEHECIKKLHILQKEFDEQKSKSTATLSKPVCLPVFKRFLSKLLKETSKLGLPDDGITAMHYDAEVKLSKQSLAEIQKLLNDEDGWTTGAMDEALSQILVQFKLHDYEAWKWRFEDTFHVDVDTVLKVSLIVLIIVAIICTQLWSVVSWFVQFRRMFAVSFFISLIWNWFHLYMLAFAEHKKNIVQVESFNAKCTGLKQLNWQDSLSEWYRRTWTLQDDPCKKYYEVLVVNPILLVPPTKAITITITNFITDPLKHIGEGISEFLRALLKDLPVTLQIPVLIIIILAILIFVYGSAQAAIHQVARFPRLGWRQEQPPPAVGQRQNPQLRAHEEPWEGGDARQPLPMRQDNRGNHVGNRGDQGFRDANAPENREEDRSMDIRQEFSTKRTPVETLQATGNTFPDDETDSQQRTQELDSGANVEEEVKVEEKEKKESFSVDNKEQKETKSPDRSEPITSEPPSSIDVKTVGADQGNEHLMCTKRKWAAQNGFKLQVILCEINSEASADLPEEEECFSFKHPVQETQS 609 A0JM59 Ubiquitin carboxyl-terminal hydrolase 20 usp20 8364 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. UNIPROT A0JM59 Pfam PF06337 Pfam PF00443 Pfam PF02148 PROSITE PS51283 PROSITE PS00972 PROSITE PS00973 PROSITE PS50235 PROSITE PS50271 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}. GO:0005813 GO:0005737 GO:0048471 GO:0004197 GO:0004843 GO:0036459 GO:0008270 GO:0006897 GO:0016579 GO:0071108 GO:0070536 GO:0008277 GO:0006511 MGDAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYVDHSTLHAQAKKHNLTVNLTTFRVWCYACEKEVFLDPRGPPASQTTSPRLSHRDFPTSAHPLKSVPIAVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLMDQLHEELKEPVPLETQEREEEDRDDQREGERGGTVEEDFLSCDSGGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEKLKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYVHCSSRSCSPHPVESISKHSSTPPRSSPLRTSHSYVLKKAQVLSGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQDLSLPIPGKEDLAKLHSTIHQSAVSKAGTCGDSYAAQGWLSFFMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVICHHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISREWLNKFNTFAEPGPISNQSFLCSHGGIPPNKYHYIDDLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRRKTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEAFVKAKDSDPPGPIDNSKVALTKSSGQVQLKQGADYGQISEETWNYLLNVYGGGPEIAIRQTVAQYQEAEHLHGEQKIEAETRAG 884 A0JMU8 Protein CASC3 casc3 8355 No SL-0198 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}. UNIPROT A0JMU8 UNIPROT B7ZRY2 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003723 GO:0000398 GO:0051028 GO:0000184 GO:0006417 MADRRRRRRRASQDSEGEEEEEESGSDSVGSGGESGAPVRQERSEQGNRKAEPPREGKESECESEDGIEGDAVLSDYESADESEIVPTKEVEEAHYNEEEPLKATLKQENNVEEAPAARDQKPKSKGTVTGERQSGDGQESNEPEEDKTIQKSQKQLDDDEDRKNPAYIPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWVHDRFHEDEQAPKSREELISIYGYDIRSSKNPEEIRPRRPRKPRFSSPSRREENNEKASWPLNRYQDSGDAQPLRPYTNRSAPPSNKVVPSRTYSRQGGYKENRASYQSEEEASLHTYERRQVYGGHRARSSEQGPPPPREFSPEADPIVKEEAVIEKQAAEPSPPPPDRPVEKKSYSRARRSRIKVGDTGKSMEDTTAAELPPPPLMPPAVAAEFTPAPLNVKQGNWEPPAEGGMSGIDEELSQMNLTEQSWNQGQPAYISPRGIPNPMHMGNGPPQYSRMEGMAVQGGRVKRYSSQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYTHGDSSSSMPPQGMIVPPEMHLSHPGMHPHPSPATMSTPNLYPAPVSLPPGQQPPQQLLPPPYFPAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGGVTYYNPVQQQVQPKPSPPRRTSQPVTIKPPPPEENRHLKMNEKINS 686 A0PJ23 RING finger protein Z Z 192848 No SL-0382 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}. UNIPROT A0PJ23 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGLRYSREVKQRYGEKELEGRIPITLDMPQTLYGRYNCKSCWFANKGLIKCSNHYLCLKCLTAMLSRSDYCGICGGILPKKLVFETTPSAPPYTP 95 A1A4S6 Rho GTPase-activating protein 10 ARHGAP10 9606 Yes SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to cell membrane is dependent on PH domain. {ECO:0000250}. UNIPROT A1A4S6 UNIPROT A1L0S5 UNIPROT Q2VPC4 UNIPROT Q2VPC5 UNIPROT Q96EV3 UNIPROT Q96S75 PDB 2MIO Pfam PF00169 Pfam PF00620 Pfam PF14604 PROSITE PS50003 PROSITE PS50238 PROSITE PS50002 OMIM 609746 DisGeNET 79658 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}. P03372 EBI-78473,EBI-1390944 Q92625 EBI-1390944,EBI-1048612 P78314 EBI-1390944,EBI-727062 P46013 EBI-876367,EBI-1390944 Q9UNA1 EBI-1390944,EBI-1390913 Q9ULB1 EBI-1390944,EBI-522901 Q02539 EBI-932603,EBI-1390944 Q9Y426-2 EBI-21517991,EBI-1390944 C9J6V4 EBI-21517910,EBI-1390944 GO:0005829 GO:0048471 GO:0005886 GO:0005096 GO:0007010 GO:0043066 GO:0051056 GO:0007165 MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHLQEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFFLKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQNIVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDSLSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATVADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL 786 A1CS06 Nuclear protein localization protein 4 npl4 344612 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT A1CS06 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0005789 GO:0031965 GO:0048471 GO:0051028 GO:0015031 GO:0006511 MAATRPIILRFESRNGQFRLSVSPQELFPTLKQKILENLPKDVEPSSITLSNKPIGTGGEERSLDGLEGVSIEQVGLKHGDKLFVGYQERKGGETTPAKAHAAADSLRRLNGALVPQTETVTFRPPTSSSATVKNPWEVVQQSPLDDKLDKKDGKIQRPRDMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKINAATNKAELKSSFMPPLSEPYYRVRHDCPSGHPPWPEGICTKCQPSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGSQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDEVDGVTLHEWPNEKEVDEVARLCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRLQAQYPKTTKWSRTGRFGSNFVTCVLSGDEEGAITISSYQASVSAVEMVRADIVEPSAEPSVMLVQSEDDDSDNKSRYIPEVFYRKINEYGVSAQQNAKPSFPVEFLLVTLTHGFPTESNPLFTKSTFPIENREVIGESQDLRSVAKKLVSHRDSNEVIPEVSDFHLLCYLHSLSTFSKTNANRLHSKITRTVTTNLMTPQDEEKLLCRVATSHDPTEGLKLINTPGWATLVTILQESGERPPKRPWLNPADPPRPLSQQGKRHLSSRPESPKSESEQLAKRFKGASLE 674 A1L4K1 Fibronectin type III and SPRY domain-containing protein 2 FSD2 9606 Yes SL-0198 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}. UNIPROT A1L4K1 UNIPROT B3KVG1 UNIPROT B7ZM02 Pfam PF00041 Pfam PF00622 PROSITE PS50188 PROSITE PS50853 DE Reference Proteome: Yes; Q7Z3I7 EBI-10172590,EBI-5661036 Q7Z3B3 EBI-740244,EBI-5661036 Q6NYC8 EBI-2557469,EBI-5661036 Q6P1J9 EBI-5661036,EBI-930143 Q6PJG3 EBI-10253976,EBI-5661036 Q86VK4 EBI-720304,EBI-5661036 Q86YD7 EBI-6658203,EBI-5661036 Q9BXY8 EBI-5661036,EBI-745073 Q9H0A9 EBI-372911,EBI-5661036 Q9H0E9-2 EBI-5661036,EBI-10304361 Q9H6F0 EBI-5661036,EBI-10307481 Q9H788-2 EBI-10308083,EBI-5661036 Q9H788 EBI-5661036,EBI-747035 Q9HC52 EBI-712912,EBI-5661036 Q8NEF3 EBI-745040,EBI-5661036 Q8TAU3 EBI-740727,EBI-5661036 Q8TD31-3 EBI-5661036,EBI-10175300 Q96NC0 EBI-5661036,EBI-2682299 Q96SQ5 EBI-6427977,EBI-5661036 Q9P0T4 EBI-5661036,EBI-745520 Q9UGP5-2 EBI-10320765,EBI-5661036 Q96BZ8 EBI-726510,EBI-5661036 Q14738 EBI-396563,EBI-5661036 Q15973 EBI-2555767,EBI-5661036 P28070 EBI-603350,EBI-5661036 P29972 EBI-5661036,EBI-745213 P31146 EBI-5661036,EBI-1046676 O95990-3 EBI-5661036,EBI-10192902 P10768 EBI-1052334,EBI-5661036 P17024 EBI-5661036,EBI-717634 Q16670 EBI-5661036,EBI-3920053 Q3B820 EBI-719941,EBI-5661036 Q53FD0 EBI-5661036,EBI-740767 Q5JS98 EBI-5661036,EBI-10244393 Q9Y3B7 EBI-5661036,EBI-5453723 Q00994 EBI-741753,EBI-5661036 Q06787-8 EBI-10224470,EBI-5661036 Q08117 EBI-717810,EBI-5661036 Q8IXW7 EBI-5661036,EBI-11976595 Q99608 EBI-5661036,EBI-718177 Q9UIE0 EBI-1105361,EBI-5661036 Q8IY31 EBI-5661036,EBI-744203 Q8N381 EBI-749096,EBI-5661036 Q8N8B7 EBI-954696,EBI-5661036 P46013 EBI-876367,EBI-5661036 Q07002 EBI-5661036,EBI-746238 Q96HP4 EBI-2862111,EBI-5661036 O43602-2 EBI-14148644,EBI-5661036 P0CB47 EBI-17208936,EBI-5661036 P56524-2 EBI-11953488,EBI-5661036 Q3SY00 EBI-10241197,EBI-5661036 O60645 EBI-1052278,EBI-5661036 Q5W5X9-3 EBI-9090990,EBI-5661036 Q14324 EBI-5661036,EBI-5653200 O95990 EBI-743396,EBI-5661036 Q8TD31 EBI-949834,EBI-5661036 P40426 EBI-5661036,EBI-6390275 Q9Y394 EBI-1387800,EBI-5661036 Q9BWG6 EBI-5661036,EBI-748391 Q6NX45 EBI-5661036,EBI-10251462 Q9BT49 EBI-5661036,EBI-741350 Q9H9D4 EBI-5661036,EBI-347633 Q5T619 EBI-5661036,EBI-11985915 Q96EG3 EBI-5661036,EBI-11962574 Q96AL5 EBI-5661036,EBI-741171 Q8IVT4 EBI-5661036,EBI-14086479 Q8TBB1 EBI-5661036,EBI-739832 Q9P1Y5-2 EBI-5661036,EBI-18121830 Q9UK33 EBI-5661036,EBI-746277 P78358 EBI-5661036,EBI-1188472 Q96EZ8 EBI-5661036,EBI-348259 Q8WWY3 EBI-5661036,EBI-1567797 O76064 EBI-5661036,EBI-373337 Q8TAB5 EBI-5661036,EBI-747505 O43482 EBI-5661036,EBI-536879 Q14119 EBI-5661036,EBI-11980193 Q86VK4-3 EBI-5661036,EBI-11741890 Q2TBA0 EBI-7851314,EBI-5661036 Q99633 EBI-5661036,EBI-2798416 Q9Y2P0 EBI-5661036,EBI-5667516 O60941-5 EBI-5661036,EBI-11984733 O95363 EBI-5661036,EBI-2513774 O14964 EBI-5661036,EBI-740220 Q2TBE0 EBI-5661036,EBI-5453285 Q9H0I2 EBI-5661036,EBI-744099 Q9P2K3-2 EBI-5661036,EBI-1504830 Q9H0A9-2 EBI-5661036,EBI-11995806 Q9ULM2 EBI-5661036,EBI-1105370 Q96HB5 EBI-5661036,EBI-744556 Q9ULD5 EBI-5661036,EBI-11975599 Q6ZNE5 EBI-5661036,EBI-2690371 Q96PV4 EBI-5661036,EBI-10171633 Q9BQ89 EBI-5661036,EBI-1752811 P36508 EBI-7254550,EBI-5661036 P53365 EBI-5661036,EBI-638194 Q8IYE0 EBI-5661036,EBI-10749669 Q9UJV3-2 EBI-5661036,EBI-10172526 Q9Y247 EBI-5661036,EBI-742802 Q08117-2 EBI-5661036,EBI-11741437 Q969G3 EBI-5661036,EBI-455078 O95295 EBI-5661036,EBI-296723 P13682 EBI-11041653,EBI-5661036 GO:0005634 GO:0048471 GO:0016529 MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGLEDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEVFITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDFIKDAVAMADRLGKFLKTKTDVEISAQPEFEDQTLDFSDVEQLMGSINTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAHNRAGPSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRSEPATVHTIGSYFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHEFVHPCFSLEKPGCLKVHNGISMPKHVTFY 749 A1YER2 Oxidoreductase HTATIP2 HTATIP2 9595 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT A1YER2 Pfam PF13460 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}. GO:0005737 GO:0005829 GO:0005635 GO:0016491 GO:0004674 GO:0001525 GO:0006915 GO:0030154 GO:0051170 GO:0043068 GO:0045944 GO:0046777 GO:0045765 MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSKFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP 242 A1YK02 Nuclear pore complex protein Nup75 Nup75 7227 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. UNIPROT A1YK02 UNIPROT Q8SZH5 Pfam PF07575 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}. P18431-3 EBI-242176,EBI-144629 Q9VZU6 EBI-500389,EBI-144629 Q9VR15 EBI-107845,EBI-144629 Q03017-1 EBI-200614,EBI-144629 Q7JYZ0 EBI-189350,EBI-144629 Q9VLT9 EBI-174393,EBI-144629 Q9VLP3 EBI-144629,EBI-179169 Q7K0E3 EBI-157547,EBI-144629 P39769 EBI-300360,EBI-144629 Q9W087 EBI-140047,EBI-144629 Q9VDI5 EBI-144629,EBI-166488 Q9VXS4 EBI-144629,EBI-138783 Q8T0S6 EBI-144629,EBI-101858 Q9VX05 EBI-144629,EBI-172809 GO:0031965 GO:0031080 GO:0017056 GO:0006406 GO:0045893 GO:0006606 GO:2000331 MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVTHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAEANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQSNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKSMPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPELEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKPFELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLPALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKRSYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSASELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENVDEIMNLLRLACARNLARALIIENTLPVV 668 A1Z6H7 Nuclear pore membrane glycoprotein 210 Gp210 7227 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT A1Z6H7 UNIPROT Q6NP18 UNIPROT Q9GPI0 Component of the nuclear pore complex. {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. P34082 EBI-868243,EBI-82439 Q9VLS7 EBI-190906,EBI-82439 Q9VQA2 EBI-198744,EBI-82439 GO:0005737 GO:0016021 GO:0031965 GO:0005643 GO:0044611 GO:0044615 GO:0070762 GO:0051028 GO:0006999 GO:0006606 MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTVRTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEPGSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPSEVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTVAYPNRLSISLLPHLNWVTVQGEHHAIALDLFAADGQKITMGTKYSINSEVDESFFAIVDRTRNGSRLFGQAKKEGITQVYGSYKDLSVQAELQIFEELQLAPTKVVLPYDPNSLKPLKLQFHASGGDNNYAWFSGNPQVIQIDTQGQATTEIRDVKSAYVNQEVLKDGGKLTAHTTVKVALSKNQKISRVAHIYFLPPERLQITRSNFETALKDFVHVHVGVYARINNSEVPYTSCDNLHFQLDFSQPILQLEGNEGAEAAHEACHVLRLRATAVGTTSLRVSYMYMDKVLYDIIDLYVFEPLVVLNPIENEVVLPVGSSRNIIYANGPQRSFTVAAEIIQSTAFDEKILKVSKLEFDTQNLITAFTVLCRELGETQFTYRVHNSLPTSSFALYQSEVTTKVHCVRPRFLKLYARHNLRDSCPLEKRTSLLFLKDPENKIEIEIEVHDSNNRRLMNISSLGLDWEFSAGEERYQKNIIPHRQISELEFNHGVTLPSRDLLVLTLSEVATNFRIKGTVSQYNDKLLAQHGIHAERPPFGIKNPQTGLIYTPLIENEIRLHAVNSTLLPKDYMSIFLASGYSERIPIAQGSGYLQLELSEAGIVQVEYNENTRILVLTPLRLGHVRLELTDRCLMNEPSHLSISVVGIGAIEVVSMDRLERTTRIEAIVRLFDTNDNLLLVDQSKLSAYDLSEVVADQSILSVRLGEQENVGPGEIRYTITGNQVGETKILFQSGKGIYKVASDPLNIQVFAPIRLFPRDSTLVVGSSIQVYFHGGPHPNTNMIISVEKEQVATISSTVVTAHKLGTTKIVGKCLLKNPVTGKDEVVSQDSVEVHVVALKGVQIRTPLVRIHSGAVMPATLWGLSDLSPMILGTLQNTKISWKVSQPQVVEIFNVFTTAGIEYQSGDLISVRVRALNPGKATITASVTLADGTILPPATVDLQVFKTLELVTPNAIKMDSILAAPRSILQLKSNMDNVVYKLDDRSNGIVSVTPDGLVHTKDSLGRDLIIATTADQSLPIGIEVKNVQYILVTLMPILKLRELEHKIPRGMNFVFKVSLHDNLGNELSHNIEDFNGLRYELGNKDDVDVQIDNNLTFALNLMRETNNVIGISLKDSTGVKHSMDFIKLSVVESDNLFPTKTIFSVGDIICFDSPLTLSSTWRSSNEQIVYINKHTGIAQVLSHRLKPGEKIEITNGDETKRGGFLKYDLEVRESDTILFVKSVDTFSGPEYRGQLVIRNHLQSEKYSNLIAQNVSKCARELGSVPVNFFTCRLAAKDALGRNLLKMYKVDALFEPSIGQYSCRLQLLTGFIELLSIVKTHDVYLELEAVVAKGVSDKMSLKLVPGIKVFPESVRVTDLKPHEIHISGLDKALLKVQVKPSDSKYFAVDFIEHGHGLSKYRLELFDDLPLDENFYILVVSPDTKQSIEVPIIGNTMLAPKCTDRRYGGPLVYRILENLGFVLTTTVIVIISIWVYMSCFQTQGVTQVNFEAFKKGKSRTELMQQSGRSSQDDTFGDSFNVRNFSPDRRRPPSNALSESYIYGHPRLNSSNRSENSTSFS 1876 A1Z8P9 Nucleoprotein TPR Mtor 7227 Yes SL-0178 SL-0180 SL-0182 SL-0185 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}. UNIPROT A1Z8P9 UNIPROT O01385 Pfam PF07926 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}. Q9VG87 EBI-127250,EBI-3406045 Q9VXU3 EBI-127250,EBI-9942564 Q24238-1 EBI-127250,EBI-3405995 Q9VDR4 EBI-127250,EBI-177749 Q9W1X5 EBI-127250,EBI-3406039 Q7JQU5 EBI-127250,EBI-3433299 Q9VBD5 EBI-127250,EBI-99036 C7LA76 EBI-127250,EBI-3406035 Q9BIS2 EBI-127250,EBI-422052 P54623-2 EBI-127250,EBI-1448924 Q8IRG6 EBI-127250,EBI-3405152 Q7KV88 EBI-127250,EBI-868359 Q9VFA8 EBI-127250,EBI-122584 Q9VWF7 EBI-127250,EBI-3406011 Q9W1M6 EBI-84282,EBI-127250 Q9VNZ7 EBI-127250,EBI-141201 GO:0000775 GO:0005737 GO:0070090 GO:0030496 GO:0072686 GO:0005635 GO:0005719 GO:0042405 GO:0005652 GO:0016363 GO:0031965 GO:0034399 GO:0005643 GO:0005730 GO:0005654 GO:0005634 GO:0005819 GO:1990047 GO:0051233 GO:0031490 GO:0043021 GO:0017056 GO:0006325 GO:0006338 GO:0007549 GO:0060250 GO:0048133 GO:0007094 GO:0000022 GO:0006406 GO:0051781 GO:0090316 GO:0090267 GO:0045840 GO:0045944 GO:0006606 GO:0090235 GO:0007346 GO:0010965 GO:1901673 GO:0060236 GO:0006355 GO:0034976 GO:0009408 GO:0051225 MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNELRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIARVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAVKTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQLTEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSEELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENKKLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASEKNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSEQPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQKEQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEKETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDEEKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREHGEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLKSLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELLRSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRNNEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAITDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEEFKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKNRLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDEHEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKDINQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASIRPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTSSHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTATAPSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKRLRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDNEGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWKQAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSGSDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVSSEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNRFAQRTRNRRPIRRPPPNNFNNGGRFP 2346 A2A6M5 Calcium-binding and coiled-coil domain-containing protein 2 Calcoco2 10090 Yes SL-0198 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}. UNIPROT A2A6M5 UNIPROT Q3TK36 UNIPROT Q3TKZ6 UNIPROT Q3TL30 UNIPROT Q9CWE3 Pfam PF17751 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}. GO:0005776 GO:0000421 GO:0005737 GO:0031410 GO:0005856 GO:0048471 GO:0016605 GO:1901098 GO:0098792 MDQCPIPTLLEHGNFSQVLFNNVEKFYAPRGDIMCYYTLTEKFIPRRKDWIGIFKVGWKTTQEYYTFMWAPLPKDQNKDSATQQEIQFKAYYLPKDVERYQFCYVDEDGLVRGTSVPFQFCPDPDEDIMVVINKEKVEEMEQLSEELYQQNQELKDKYADLHEQLQRKQVALEATQRVNKTLEHKVEEKASWEKEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEKEKASWEEEKASWEKEKAPWEVEKAPWKEVKAYWWNDLHR 331 A2AI05 NADPH-dependent diflavin oxidoreductase 1 Ndor1 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. UNIPROT A2AI05 UNIPROT Q3TQZ6 UNIPROT Q80WC5 Pfam PF00667 Pfam PF00258 Pfam PF00175 PROSITE PS51384 PROSITE PS50902 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}. GO:0005737 GO:0005829 GO:0045111 GO:0005654 GO:0048471 GO:0050660 GO:0010181 GO:0050661 GO:0003958 GO:0016491 GO:0016709 GO:0008219 GO:0036245 GO:0016226 GO:0055114 MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRKSLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVPLDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDVSEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA 598 A2IDD5 Coiled-coil domain-containing protein 78 CCDC78 9606 Yes SL-0198 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. UNIPROT A2IDD5 UNIPROT B4DNY4 UNIPROT B4E1U6 UNIPROT Q05BY7 UNIPROT Q05CA0 UNIPROT Q6T2V5 UNIPROT Q6ZR33 UNIPROT Q8IUR3 UNIPROT Q8NAY7 UNIPROT Q96S12 Pfam PF14739 OMIM 614666 OMIM 614807 DisGeNET 124093 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}.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. Q9NQ75-2 EBI-2874003,EBI-12270182 Q8D194 EBI-2874003,EBI-2847851 GO:0005814 GO:0098536 GO:0048471 GO:0042383 GO:0016529 GO:0030030 GO:0098535 GO:0003009 MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAPGNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQSWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS 438 A3GFS1 Nuclear protein localization protein 4 NPL4 322104 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT A3GFS1 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0036266 GO:0000837 GO:0000839 GO:0031965 GO:0048471 GO:0030894 GO:1990112 GO:0034098 GO:0071629 GO:0006274 GO:0071712 GO:0072671 GO:0051228 GO:0051028 GO:0051974 GO:0070651 GO:1900182 GO:0072665 GO:0030970 GO:1990116 GO:0030433 MSVTLRFRSREGTFRVAANPDADFLLVLEQLLSKISIEDVQNLYLSDKPNSKGELANGLCGKTVTELGLKNGDMLYASYEAATGSNPDSTTNITTSTNNHNSGSISIGHISIPTTTSGPRKVTQLPVDDVLEKDEGLIKRPLTKFCRHGAKGMCEFCSPLPPWDANYRKENAIKHMSYHAYLKELNELKNSKHNSSSYIAPLEEPNYSILLNCNEGHQPYPKGICSKCQPPPITLQLQKFRMVDHVEFATSSIMNNFIDVWRHTGVQRFGVMYGRYEPFDKVPLGIKAVVEAIYEPPQSGELDGITMLPWENEAEVDAIASELGIYKVGVVFTDLTDSGQKNGTVLCKRHKDSYFLSNLEILMAARNQIQHANITKFSSSGQFSSKFVTCVISGGLNGEIEPRSYQVSTSAEALVRADIITGSTQPSRLYVNSSNDRRYVPDVAYSELNEYGLEVKSNAKPTFPVDFLLVSLTDSFPVNPTPMFDTDSNFVIENRDFFNELQNLHAVSKYLNADTSGKGTSLCNFHFLVYLKRTNILGAQEFDLLLRFVRERQYEDYLHLVESPGWMTLITILEQST 577 A3KNS9 All-trans retinoic acid-induced differentiation factor atraid 7955 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}. UNIPROT A3KNS9 UNIPROT Q502E7 UNIPROT Q5RID6 PROSITE PS00022 Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). {ECO:0000250}. GO:0016021 GO:0005635 GO:0048471 GO:0005886 GO:0030154 GO:1903363 GO:0033689 GO:0030501 GO:0045669 GO:0010468 MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSNCSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTVQMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT 230 A3KPL7 Transmembrane protein 170A tmem170a 7955 Yes SL-0178 Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}. UNIPROT A3KPL7 UNIPROT Q6PCR5 Pfam PF10190 May regulate membrane morphogenesis in the endoplasmic reticulum (ER) by promoting ER sheet formation at the expense of ER tubules. {ECO:0000250|UniProtKB:Q8WVE7}. GO:0005789 GO:0016021 GO:0005635 GO:0071786 MIEALIVGEMQDVQIGFVKQILSLNLVPRSNNTTCGNNTSLCDFSEMWYGVFLWAVVSSLIFHLPAALLALATLRRHKVARFFPLGILLMGIIGPLFGGVLTSAAIAGVYKAAGKSMFSLEALVFGVGQSLFIFIISFLRILATL 145 A3KPP3 Ran guanine nucleotide release factor rangrf 7955 Yes SL-0198 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}. UNIPROT A3KPP3 UNIPROT A7E2J7 Pfam PF04603 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}. GO:0005634 GO:0048471 GO:0005886 GO:0005085 GO:0060047 GO:0001947 GO:0015031 MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWEVRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAIPWTLQDFQGVLQSLRLLDSGVFG 183 A3LNW3 Protein transport protein SEC13 SEC13 322104 Yes SL-0178 SL-0185 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}. UNIPROT A3LNW3 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0030127 GO:0005789 GO:0000139 GO:0031080 GO:0035859 GO:0005198 GO:0090114 GO:0051028 GO:0031081 GO:0043547 GO:1904263 GO:0045893 GO:0015031 GO:0030433 MVTIGNAHNDLIHDAVLDYYGKRLATCSSDKSINIFDIDGTESYKLVSTLTGHDGPVWQVSWAHPKFGSILASCSFDGKALIWKEQPETQQWSIIAEHSVHQASVNSVSWAPHELGAVLLCASSDGKVSVVDFNDDGTTSHVVFDAHAIGANSASWAPLSSTPSPNQKDAASLKQQRRFVTCGSDNLAKIWKYDAANNTYVEEARLEGHTDWVRDVAWSPSMLVRTYIATASQDRTVLIWTQDKAGKWQKQLLTEDKFPDVCWRCSWSLSGNILAVSGGDNKVSLWKENLQGKWESAGEVVQ 302 A4FUC9 Rhophilin-2 RHPN2 9913 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT A4FUC9 Pfam PF03097 Pfam PF02185 PROSITE PS51180 PROSITE PS50106 PROSITE PS51860 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}. GO:0048471 GO:0007165 MTDTLLPAAPQPLEKEGNCYFRKGCNPLAQTGRSKLQNQRAALNQQILKAMRMRTGAENLLKAATNQKVREQVRLELSFLNSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFSVALKDFILEHYSEDSYLYEDEIADLMDLRQACRTPSRNEAGVELLMSYFMQLGFVESRFFPPTRQMGILFTWYDSLTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTEAGLESTVDAFQRAAGVLNYLKETFTHTPSYDMSPAMLSVLVKMMLAQAQESTFEKVCLPGLQNEFFLLVKVAQEAAKVGEVYRQLHTAMNQEPVKENIPYSWASLACVKAHHYEALAHYFTATLLIDHQLKPGEDEDHQEKCLSQLYSHMPEGLTPLATLKNVHQRQLLGKSHLCQAVTHHEESMREASLCKKLRNIDVLQEVLSAAHDRSQLKYTQLREDDDLLNLTDAPDIVSKTEREVEIIVPQFSKVTVTDFFQKLGPLSVFSANKRWTAPRSIHFTAEEGDLGFTLRGNSPVQVHFLDPYCSAAAAGTKEGDYIVSIQDVDCKWLTLSEVMKMLKSFGQDDIEMKVVSLLDATSTMHSKCATYSVGMQKTYSMICLGIDVDDKTDKTKKVSKKLSFLSWGTNKNRQKSASTLCLPSVGVTMPPVKKKLSSPFSLLNTDSSLY 686 A4FV75 Trimeric intracellular cation channel type A TMEM38A 9913 Yes SL-0178 SL-0182 Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}. UNIPROT A4FV75 Pfam PF05197 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}. GO:0005623 GO:0016021 GO:0031965 GO:0033017 GO:0042802 GO:0005267 GO:0071313 GO:0007029 GO:0010881 GO:0014808 MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRHHPMASWLCAMLHCFGSYILADLLLGEPVIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVTLMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYICPVLFGSASGGDHHHNNHGGSQGGSGPGSPHSPLPSKSKEELSEGSRKKKTKKAD 299 A4GSN8 Nuclear-pore anchor NUA 3702 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT A4GSN8 UNIPROT F4IDK8 UNIPROT F4IDK9 UNIPROT O64521 UNIPROT O64522 UNIPROT O64524 UNIPROT O64525 UNIPROT Q8H7F1 Pfam PF07926 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}. Self EBI-1545660,EBI-1545660 Q94F30 EBI-1545660,EBI-1545674 GO:0005829 GO:0005739 GO:0005635 GO:0031965 GO:0005643 GO:0005730 GO:0009506 GO:0017056 GO:0006406 GO:0009910 GO:0033234 GO:0016973 GO:0006606 GO:0060968 GO:0048443 MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQSDFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSSEKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSLNWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESSYKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGTALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSVSEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKIISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVAMYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLAMEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAEKRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNNAVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGEVESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALLSASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELRKLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSGLQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRESNMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYNRLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNKKIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKTEDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLSGSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASDNKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQADSLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVEAQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPETLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSSTLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGRAPRGGRGQSPSPP 2093 A4IF89 Exocyst complex component 8 EXOC8 9913 Yes SL-0198 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}. UNIPROT A4IF89 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0005829 GO:0000145 GO:0030426 GO:0005770 GO:0048471 GO:0035091 GO:0017160 GO:0007032 GO:0006887 GO:0022617 GO:0006893 GO:0008104 GO:0015031 MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGGGGAGGRDQLRGQTGFFPSPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSEKRRREQEEAAAPRGPPQVTPKASNPFEDEDDDEPTVPEIEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRARVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVRVAKEHCQQLGDIGLDLTFIVHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV 725 A4IG66 Transmembrane protein 201 tmem201 7955 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000305}. UNIPROT A4IG66 Pfam PF10476 Pfam PF09779 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}. GO:0005639 GO:0031965 GO:0051015 GO:0005521 GO:0030473 MEALNQILIEYPPLVVGGVGATAVAAGGALIYRIATRKKPTHLQVNCWFCNQDTVVPYGNRNCWDCPYCEQYNGFQENGDYNKPIPAQYMEHLNHGVSAGVPETPKTLQWVNCQMLLCKKCNNNQTLKIKQLASFIPREDENYDEEIEVYKHHLEQTYKLCRPCQTAVEYYIKHQNRQLRALLFNHQLRRTRDADKAFIKNTYSLSTPAWLILLRILTFLACAFLVAVALSGYVDESPSVTQTLSGGVVPPKRVLQNENESKTDEGSLMWDDLMGLLPEKAVENARLFWQSGSDHQMAVASVGLLTCITGVLMAGPVRLRRIDAVASVLWLLVICFYLAECYLKTDVPSWLEMVKFGITSVCCLVGFAAAVATRKSTSQRRARGRRYLSGGSPGEFFCNHGPLLSAPVSESSTFIPTPPPNLSQLLIRQQSQRTRKASPSSLPGRLNRALSLGTIPSLARADSGFLFSGSRPSSQCKDSPPSDYYSLKSGSRPSSPGPSPTPSVAGSVTSTSSSARQRRPLISPARLNISGQKLRLFSSPLEPFSLASPPPFLSEHNPMHSRGFLPDVPHFHLQNHGSVIDEGSVFEHLEKPMGSSSSSSNCHVDTTTGNNIESKPGWKGFLGMTLWPGLLFASLTINLSFICIYVYYNWR 651 A4IHT0 Fidgetin-like protein 1 fignl1 8364 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. UNIPROT A4IHT0 Pfam PF00004 Pfam PF17862 Pfam PF09336 PROSITE PS00674 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}. GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0046034 GO:0031122 GO:0010569 MQVPESSLAHLSEWQRDAFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAIIDSDKLEIGLNNYADSILTLAKCQRNESDKWQSSLTTNNVLKLKSVQDMAVAGRRTQLSKSSADASVRVGNGINTSGYSAGLGNNVLRNSGYTVPHAALSDCQMPGGSANFLQKPKISAFTIANTTSVANTSSNTLINNSISMTSSLMQSNEDKDPASFSGHMFLPTTSVHSGKRKAYSALGNESSDIKPNPLVQRQLTNKEATCESGFKTAKEQLWVDQQKKYSNQPQRNPSPLYGGAKKSLGAARSRGLHGKFVPPVPRQEDVQDSNRKVYGQGNSEMNAPSDERLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSDDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVSLMAKEHCSLAEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITPEQVRPIAYIDFQSAFLVVRPSVSQKDLELYENWNKTFGCGR 656 A4RN19 Nuclear protein localization protein 4 NPL4 242507 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT A4RN19 UNIPROT G4MZE9 UNIPROT G4MZF0 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0005829 GO:0005783 GO:0005789 GO:0031965 GO:0042175 GO:0005634 GO:0048471 GO:0051028 GO:0015031 GO:0030433 GO:0006511 MLLRLRGPDGMLRIELDPKDTFNKLGQELMGKLPPTVDPATITVSNAPGSQGDKKLLKDIAKYKVEAIGLKHGDLIFVDYKHQGAEADGTANSDGASQPLTSTTNRLNGQPVLPTEDLPIDPLPTPAPGATIKNPWEVVRQSPLDDRLDKKDGKIPRKRDAMCRHGPKGMCDYCQPLDPFDAKFLAEKKIKYLSMHAHLRKINSATNKPELGSSFIPPLSEPYFRVKHDCPSGHPQWPEGICSKCQPSAITLQPQPFRMVDHVEFASPSIVDSFINTWRRTGGQRYGIMYGKYSEYEEVPLGIKAVVQAIYEPPQVDEVDGVSLNSWDNEKDVNQVARLCGLEPVGAIWTDLLDAGAGDGSVVCKRHADSYFLSSLEVCFAARLQAQHPKPSKWSDTGRFGSNFVTCIISGNEQGEIAISSYQVSNEAVEMVRADIMEPSADPTVMLVREEEEDDGSTSRTRYIPDVFYRRINEYGANVQENAKPSFPVEYLFVTLTHGFPDVAKPMFSDEGAFPIENREYMGESQEHSAAAKALKVHEKASSGSSKDGMKVSNFHLLCFLHQMSVLSKDEESLLCRVATQHDLADAFQLRSTTGWQTLMAILQSTGERIPKRSRQTDVLAADPAASSYPGRRGIDDSDERLAKRFASVRLNARGDGRNGRDRPSAHET 669 A5D7H5 Protein CASC3 CASC3 9913 Yes SL-0198 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}. UNIPROT A5D7H5 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003723 GO:0000398 GO:0051028 GO:0000184 GO:0006417 MADRRRQRASQDTEDEESGASGSDSGGSPARGGGSCSGSVGGGGSGSLPSQRGGRAGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGDDGEYSEEENSKVELKSEANDAANSSAKDEKGEEKPDTKGTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRFGSPPQRDPSWIGERPNKSHRHQGPGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRTGFRPAEAGGQHAGRSGETVKHETSYRSRHLEQTPVRDPSPEADAQVLGSPEKEEVAPEIPNPAPDTAPPVPDRPVEKKSYSRARRTRIKAGDAGKVAEEVPPPPEGLTPAPPVPEATPPTPAKTGNWEAPVDSTTGGLEQDVAQLNITEQNWSPGQPAFLQSRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMIVQPEMHLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS 703 A5D8S5 E3 ubiquitin-protein ligase SH3RF1 sh3rf1 7955 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. UNIPROT A5D8S5 Pfam PF14604 Pfam PF13445 PROSITE PS50002 PROSITE PS00518 PROSITE PS50089 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}. GO:0005794 GO:0030027 GO:0048471 GO:0005078 GO:0046872 GO:0061630 GO:0006915 GO:0001764 GO:0046330 GO:0051865 GO:0043370 GO:2000564 MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRPRRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIIILRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPPPQRHSMEISGPVLISSSNPTAAARIGELSGGLSSSAPSQVHICTTGLIVTPPPSSPVTTATVFTFPPETSYASIPVDALPPPPPPPPQSQSSVVGAAALNAGQRPSPAAGDQSGRQRPTVYVAMFPYSPRKEDELELRKGEMFLVLERCQDGWFKGTSMHTGKIGVFPGNYMSPVSRTVSGSSQPKVPLTLCSQAGRGVTIVSPSSALGSMDLSKPLPVCPNATPSCSLPAAVVTAAHLPTGQHPKVLMHVTSQMTVNQARNAVRTAVSHSQDRPTAAVTPIQSHNPVAYLPSTAVVLQASPVLNSSSGCSSARVGVALGCAAASLTPPNVSAASLDTDAMRPVPMVALPVNAGSTKPLGAASNHGVACRLDKDCKREKKGLLKLLSNKKKLRPSPPSSPTLEAEQSVSMELPQGAVGPEMALSGSAGHNGRIGACPMDSELSMSSSSSNTDAVTHRSSPQDNTAPIAPPPRQPCSSLLSMQHDGRPIVCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGRTGLFPGSFVDSI 867 A5DJU3 Nuclear fusion protein KAR5 KAR5 294746 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT A5DJU3 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MKKILRLVFILVYTNISTFVSAHELEDAASFTADELDRLLEDPPGCIQLAMRPIFEKCVLNGIHAVDPKDRRSSAIEMSVCEFESAGVEYPAECSTTDYDTCIWKLGLVPQYWTTFSGNYRDIGLFCEGVSRNNEKEQLVLLYSNITKVFAGFRHAFYESYSKSQEMKDEMEEGFSRWSADFDIAKDQHKEFYEFVAKQQEHIKIELMKNQKVIFDFHDEQEVRFNSYSNHIVDVIDSMAVDLDIILAKLADDGIIEDMENQKSKSLDIMKSYSEDAELTLSRIVSELERVGIIQKNDVSIVENLNSGLADTSNKVSKLNKDFEDLDSHFQHTKDLIESEVSFLFANLIGEMETKLSQALENVDDRIELHFVSQLEFLDKSLNETWEAILTFKQDWQIFTSIFENFENIPKSISHFVTSGLYKTNEILTQTSYFWSTILNIPVSLLSNILRYTMAASWIAILFILISLRYGSTKSFLLVIMVLLVVFLNTHRW 493 A5DX93 Nuclear protein localization protein 4 NPL4 379508 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT A5DX93 Pfam PF05021 Pfam PF11543 Pfam PF05020 PROSITE PS50249 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}. GO:0036266 GO:0000837 GO:0000839 GO:0031965 GO:0048471 GO:0030894 GO:1990112 GO:0034098 GO:0071629 GO:0006274 GO:0071712 GO:0072671 GO:0051228 GO:0051028 GO:0051974 GO:0070651 GO:1900182 GO:0072665 GO:0030970 GO:1990116 GO:0030433 MSLILRFRSKDGMFRVNTDSSSTFQTVVDQLSLKLPTTDYDQITVSDKPNNKNDLGSQAKTLLSILHQTISELQLKNGDLLFLNYSNAIPQGTLASTSSTKLQSGSIAINSSGGSSGPATASGANASTIRVSPTTHGPVKVSQLPIDDELDSQDGILSRPISSMCRHGAKGMCEYCSPLPPWDENYRKEHAIKHISYHAYLKQQMAKFNKKELSSSYIAPLENPNYAINLNCNEGHQSYPRGICSKCQPLPITLQLQKFRMVDHLEYASHTILNDFINVWRSTGVQRFGYLYGRYEKFDKVPMGIKAVVEAIYEPPQHDELDGLTLLDWEDEPIVDAIAAKLGLQKVGIVFTDLTDSGNRDGTVLCKRHKDSYFLTNLEIIMAAKFQIKNPNITKYANLGEFSSKFVTCVISGGLQGEIEPRSYQVSSSAEGLVKADIITGSTQPSQIYVNGNNDTRYVPDIQYSKINEYGLEVKSNAKPTFPGEFLLVSLTDSFPIDPKPLFTSKISYVIENREFLGHGDIDGLDHLQNLSSVAKFIKLNDSELFDFHWLVHVAKMGILSEEELSLLCKYVKEKKYDDYLQLMESGGWMTFLTILEQST 600 A5E4Z8 Nuclear fusion protein KAR5 KAR5 379508 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT A5E4Z8 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MVGASAISGVVIIANVVAAIAAAAGDGDGGIASTTDTILTLDGIKILNNALLQWKDDCNQRALAEVMPQCIHGVENITPSQQKHTAMELSICEFENNGLDYPLECHASVRNLNTNTCIQALEKSPQYWTTFSGNYRAVKDICHQISLPYEKDQIIEVYENMTLLYRSVMEDLKSSHHKYTVELEMKIQNKFNKLFSVVDDLMRSRAEENNKVNQTFNKFYENFQVSISNALVVMQNSYDGANTNFELMQRHVSYFATELQRILLLVQEQGEKLQVQQEQLVTGNVKLSIQQERLFDNMQLFGNELDKLHNAEVSRVSSVNKQLKLTEFSIRHANSILRENTDELHLQRMLIAEYTPIILGNITTLLMHFLNQSASEIVENFEHSLNLSLEKLSLKIDETANSLAVVNATIARCSIFASSVVETLDSLKNSTIRMMMLFMSMITPSVTFDGLISGAKAIIAFFTLVTRLAAVIAICLLIILIWPIVKSLFFQPLCYLMRRCSYIVVSILVGVAAANFSVWLLQK 523 A5WW21 Ras and EF-hand domain-containing protein rasef 7955 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT A5WW21 UNIPROT A4QP53 Pfam PF13499 Pfam PF00071 PROSITE PS00018 PROSITE PS50222 PROSITE PS51419 Binds predominantly GDP, and also GTP. {ECO:0000250}. GO:0012505 GO:0048471 GO:0005509 GO:0005525 GO:0003924 GO:0006886 GO:0032482 MNHAELRRLFAACDGNQSGRVEYEDFTTVCRELNVPADDIRTLFNKFDLDGDGYINFNDFSSSFQEVSEALNLASLGNCLHSQRRAWDEFENTLDGDVAFYLGRQWDALSELYEGIHSTSDELLLQQFEDLIRALVTEIREHRMESEQLETSLRRTEEVSSSQLAEMEEDLQQQLIHTERRVREEEQKKLDESIAMLQIKHENELADLQTTIERLTKQYQEESKLNTPREDSVKLRAQIKDLMEENEELRASLMKAQMNVSILQVELDKLKNAFTDQKRQHERESDDLKKMVMEFQSYSSHIEMLQEMNKSLYDSNDGLRSALSQENASTKRQLSPRNEVLPRKMKPIRQSTMNQSSFTNEEDTLALVKCWAEKYLDSGVSVQSEMDAMSGIDYDSDDSHHSVETVHHSYSCVPSELEVSEVKPEALRSVARSTVGSISSSLRRRLSAFPVKQNEEDLLDTQDLAPVYRLVLAGDAGSGKSSFLLRLSLNEFRGDIQTTLGVDFQIKKMLVDGEKTNLQIWDTAGQERFRSIARSYFRKAHGVLLLYDVTSESSFLNVREWVEQIRESTDEDIPMCIIGNKVDLRAARPEGSCVSSIHGEKLAMNYNALFCEASAKEGTNVIEAVLHLAREVKKHVKLGRRSESQVKLSLHKRRKTLSNCCGV 663 A5YVF1 Protein SUPPRESSOR OF GENE SILENCING 3 SGS3 4081 Yes SL-0198 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}. UNIPROT A5YVF1 Pfam PF03468 Pfam PF03470 Required for post-transcriptional gene silencing and natural virus resistance. GO:0048471 GO:0031047 GO:0050688 MSFSKWGGKPSNSSEKQKASSTPTVEEINRGVGDIGLNSEQNEGWEVYARKPKNKGGSSAGKQWAPQNPSPKAWGNQNTKAWGHPDVGKKSGTRNNAGSGRGSGNNWSTPSDPQKLARPHLYDGGFPSSAPVPPALKNGWDWSSRVASAHPKDNSQVAAAADDDKASEHDAEDNELDFLDESDDDLHSDDFDSDVGEMSYETRKKNPWFNQLFHSLDSLTVTEINEPERQWHCPACKGGPGAIEWFTGLQSLMTHAKTKGLRVKIHRELAELLEEDLRQRGTSVVPPGEVYGRWGGMEFKDKEIVWPPMVIIMNTRLDKDENDKWIGMGNQELLEYFSSYAAVKARHSYGPQGHRGMSLLIFEASAVGYIEADRLSEHFSENGRNRDAWERRSARFYPGGKRLLYGYMADKKDIDNFNQHSAGKSKLKFEMRSYKEAVWNPAKQMREDNQQLIWFKNKAAKHQMQAKALEESLSLVSEKHRQTLEENKIVRLKTKMHHEQIKEEMEFQEQFFKDQIKIIHDARTAREDNFEKTQQEQREMVKQSNANTASVEDHRVRAEKVAKFIKLQDKEMEEFVEERENLMRTHDDRIAALRRKYWEEEVELERKFDLELSKLMEKYSPKQSDEVNSSGTM 633 A6QLT2 Myotubularin-related protein 2 MTMR2 9913 Yes SL-0198 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}. UNIPROT A6QLT2 Pfam PF02893 Pfam PF06602 PROSITE PS51339 PROSITE PS00383 PROSITE PS50056 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}. GO:0030424 GO:0005829 GO:0031901 GO:0005634 GO:0048471 GO:0005774 GO:0042802 GO:0052629 GO:0004438 GO:0004725 GO:0046855 GO:0032288 GO:0031642 GO:0048666 GO:0046856 GO:0060304 MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADRVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPRRTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYVRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERAGSPAQCVTPVQTVV 643 A6RC50 ATP-dependent RNA helicase DBP5 DBP5 339724 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT A6RC50 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0000822 GO:0003723 GO:0003724 GO:0008186 GO:0016973 GO:0006415 GO:0006409 MATETPAGGPLEARISRAEPKTDASATSEPATGDTTETPAATKPSAADGQTDGASEGFGGSQLQEPEYSVNVKLSDLQADPNNPLYSIKSFEELGLHPSILQGLHSMSFRRPSKIQEKALPLLLNNPPANMIGQSQSGTGKTAAFVLNILSRLDLSPQMELAPQALVLAPSRELARQIVGVIQVMGSYVDKLKVATAVPMESNRNQKVEAPVVVGTPGTVMDLIRKRLFNPQHLKVIVLDEADNMLDQQGLGDQCIRVKGLLPKNIQVVLFSATFPDHVVRYANKFAPNANQITLKHEELTVEGIKQLYLDCDSDEHKFDILVKFYGLLTIGSSIIFVKTRASAVEIERRMVAEGHTVVSLTGGVEGQKRDEIIDKFRQGDAKVLITTNVLARGIDVQTVSMVINYDIPELHAPKATKRIADAQTYLHRIGRTGRFGRVGVAVSFVASKEEWQMLQDIKTYFNTEIQRVNTQDWDEVEEVVKTIIRSSRAGSNFQRS 497 A6XA80 Leukotriene C4 synthase LTC4S 10141 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT A6XA80 Pfam PF01124 PROSITE PS01297 Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4. GO:0005789 GO:0016021 GO:0005640 GO:0008047 GO:0004464 GO:0019370 MKDEVALLATVTLLGVLLQAYFSLQVIRARRAHRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGVYFHEGAAALCGLVYLFTRLRYFWGYARSAQLRLAPLYASARALWLLLALATLGLLAHFLPAAARAALLRLLRALLRTA 150 A6ZMC4 Nuclear fusion protein KAR5 KAR5 307796 No SL-0178 SL-0182 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. UNIPROT A6ZMC4 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MFAMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAETRVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNITELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQIIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKKQLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDISEKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIKRYYQWAALLLSIYLGAKTGSLIDF 504 A6ZTA1 Nucleus-vacuole junction protein 1 NVJ1 307796 No SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT A6ZTA1 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}. GO:0016021 GO:0005640 GO:0006914 MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVFNFISRQSSELDARIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPIILSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALSQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEVESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFRY 321 A6ZUA4 Monopolar spindle protein 2 MPS2 307796 No SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT A6ZUA4 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQKAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALLAGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI 387 A6ZXN8 Nuclear rim protein 1 NUR1 307796 No SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT A6ZXN8 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQDNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCKFMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEVEIFFQLRKWIPTNFMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDTLSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMSPYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKNYHKR 484 A6ZZB9 Spindle pole body component KRE28 KRE28 307796 No SL-0178 SL-0182 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}. UNIPROT A6ZZB9 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE 385 A7MB43 Myotubularin-related protein 9 MTMR9 9913 Yes SL-0198 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}. UNIPROT A7MB43 Pfam PF06602 PROSITE PS51339 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}. GO:0005783 GO:0048471 GO:0032991 GO:0032587 GO:0030234 GO:0019903 GO:0010507 GO:0010922 GO:0050821 GO:0060304 MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGPLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSTISEWRLSYVNKEFSVCPSYPPAVIVPKAIDDDALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRPLNIAQQARAKGGGFEQEAHYPQWRRIHKSIDRYHILQESLIKLVESCNDQTQNMDRWLSKLEASNWLTHIKEILTTACLAAQCLDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNSKQKWESPVFLLFLDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPSELSKFTNPLFEANNLVIWPSVAPQSLQLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNLLRRQLAELETEDGVQESP 549 A7MB64 Inositol 1,4,5-trisphosphate receptor-interacting protein ITPRIP 9913 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT A7MB64 Pfam PF03281 Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}. GO:0016021 GO:0005640 GO:0005886 GO:0004860 GO:1902042 MALGLFRVCLVVVTAIINHPLLFPRENTTVPENEEEIIRQMQAHQEKLQLEQLRLEEEMARLAADKEAEKEALERVAEEGQQQNESRTAWDLWSTLCMILFLVIEVWRQDHQDAPSPECLGSDEDELPDLEGAPLRGLTLPNRATLDHFYERCIRGATADAARTREFVEGFVDDLLEALRSLCSRDSDMEVEDFIGVDSMYENWQVNKPLLCDLFVPFMPPEPYHFHPELWCSSRSVPLDRQGYGQIKVVRADEDTLGCICGKTKLGEDMLCLLHGRNNVVHHGSKAADPLCAPNSPYLDTMRVMKWFQTALTRAWHRIEHKYEFDLAFGQLDTPGSLKIRFRSGKFMPFNLIPVIQCDDSDLYFVSHLAREPGGGTRASSTDWLLSFAVYERHFLRVTSKALPEGACHLSCLQIASFLLSKQSRLTGPSGLGSYHLKTALLHLLLARRPADWKAEQLDARLHELLCFLEKSLLEKKLQHFFIGNRKVPQAMGLPEAVRRAEPLNLFRPFVLQRSLYRKTVDSFYEMLKNAPALISEYSLHIPSDHASLPPKTVIL 556 A7MBC7 Nuclear envelope integral membrane protein 1 NEMP1 9913 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT A7MBC7 Pfam PF10225 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 MAGGMKVAVLPAVGAGPWSWGAGGCGAVRLLLVLFGCFVCGSAGIDLNVVTLRESEILFMNTSRQSCYKNVLIPKWHDIWTRIQIRVNSSKLVRVTQVENEDKLKELEQFSIWNFFSSFLKEKLNDTYINVGLYSTKTCLKVEILEEDTKYSVIVTRRFDPKLFLIFLLGLTLFFCGDLLSRSQIFYYSTGMSVGIVASLLIIIFIVSKFMPKKSPIYIILVGGWSFSLYLIQLVFKNLQEIWRCYWQYLLSYVLAVGFMSFAVCYKYGPLENERSINLLTWTLQLLGLCFMYSSIQIPHIALAIVVIALCTKNLDYPIHWLYITYRKMCKATEKTVPPRLLTEEEYRLQGEVETRKALEQLREYCNSPDCSAWKTVSRIQSPKRFADFVEGSFHLTPNEVSVHEQEYGLGSIIAQDELSEETSSEEEDSDSRYPLVVQQNSFLT 445 A7RVK7 Probable trafficking protein particle complex subunit 2 v1g94938 45351 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. UNIPROT A7RVK7 Pfam PF04628 May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. GO:0005783 GO:0005794 GO:0048471 GO:0006888 MLGNYYFAIVGHYDNPVYEKEFNQQMKMDSNDHRHLNQFIVHAALDLVDESMWGTTGMYLKSVDKFNEWFVSAFDPPLSWIIDPQFFLDLTSWMRFMMLHDVKNDDGIKNFFSDVYETFIKVLMNPFYEINSKIKSANFDKKVLLAAKKHILP 153 A7TFD7 Spindle pole body component KRE28 KRE28 436907 Yes SL-0178 SL-0182 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}. UNIPROT A7TFD7 Pfam PF17097 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}. GO:0000778 GO:0005737 GO:0031965 GO:0005816 METQAVKTIRDELRELENTVAQASDMVLSEQDHRNASAIREMTQSVIAMSKENSLISVSNEIDYNEEIGNLAIDPSLIDEKIKQSNNFVELLKLTHLEQEALDYFLRYTISSTNTLELESTSDPKFVSLENEVTELENKTLTEHRDKIQEAKKDISDKSKDLANKQDQINELCLGAANSVDECWKMLNELEDIHSQRDNDVKETLSQDTTTTSDLIEETYKEWSSLQTSLTELNNSKDELDQLIAFKNEKHKDNDSTKIRNANIKNKTITENVKMLKLLINFWESNFIVPGSKKSKLSNLEVYPQTKKFQFKCAEQYTVIIQLNQNGGSIKSIEIFENDGKSVQENKNLSSLILNKYKNPLSSYPIFQVINDIVEELK 378 A7TH24 Nuclear rim protein 1 NUR1 436907 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT A7TH24 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 GO:0043007 GO:0007096 MNGLDDENQIDERDHYTDDGDYEIDIDSMNMFKSLYYEMMAYFSDLQMHLGEHLMAIDWDMKCKSIAEPVGNCLTALFYIIRLLQDTLLSNYKDVYVSTEAFDLSKSTTLQEFPFLIRFVEVSKTKNLQNAKYIKKKTFMFYFDKLLLFLMILILSTNAYISWTFIWRNFKTYSLLYVVDRPNSKNVTKCSRTDLDQSYMENVSYGSYWTMLSYYIRNFRKKDDLEDEITTVKQKTPNVNEKDYYYQLKKWSPSKFLTSLFCSFSPTCLVFLILSDVSFTTSIAVILHQFIFKYVVFEGYESRINDESIIHSAMISEINQKFVEPRLSKKVQDAKIDATPEGKVYRTEFFPSLTNCKSNLFNRHDLKGRSITESYNDRIKEFEIVTNTNNETHNVIKVVKK 401 A7TTC4 Nuclear protein localization protein 4 NPL4 436907 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT A7TTC4 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0036266 GO:0000837 GO:0000839 GO:0031965 GO:0048471 GO:0030894 GO:1990112 GO:0034098 GO:0071629 GO:0006274 GO:0071712 GO:0072671 GO:0051228 GO:0051028 GO:0051974 GO:0070651 GO:1900182 GO:0072665 GO:0030970 GO:1990116 GO:0030433 MLLRFRSKIGMNRVSCEATDLFGDVVENWVKEVGLNVDPGTVVVGNDPGSAKEPVSNIAGRSVEEMGLKHGDIVYIEYSDSSGSNEGQSVPVNAVGAGSAVISELPVDVLLEKEDGLIKRTRSSLCKHGDKGMCEYCSPLPPWDKEYHAENKLKHISFHSYLKKLNEATNKKSSGSSYIPPLSQPDYKINKRCNNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEIQQSDLINQFIESWRATGMQRFGYLYGSYEKYDSTPLGVKAVVHAIYEPPQHDEQDGLTMDLEQVEEEMQKVDQIAMSMGLLRVGLIFSDLTDTGNGNGTVFCKRHKDSFFLSSLEIIMAAKHQLAFPNASRFSEQGKFSSKFVTCVVSGNLDSEIDITSYQVSIEAEALVDAKMISGSTHPSMAYINETNEEVYVPEIFYMKTNEYGLTVKENAKPAFPVDYLLVSLTHGFITEDSKNQIKFHSTGGFPWANRQAMGLSQDYQELKNYLYSAATGGDYNLLHEKISNFHLLLYIKSLEIFNEKDWSLLITSAISENWEQPLIQLTTTESFNSLVLIMEMI 568 A7WLH8 Small ubiquitin-related modifier 1 SUMO1 9823 Yes SL-0178 SL-0182 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}. UNIPROT A7WLH8 Pfam PF11976 PROSITE PS50053 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}. GO:0005737 GO:0031965 GO:0016607 GO:0097165 GO:0005634 GO:0005886 GO:0016605 GO:0015459 GO:0031386 GO:0008134 GO:0031625 GO:0044389 GO:0071276 GO:0034605 GO:0045759 GO:1902260 GO:0016925 GO:0060021 MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV 101 A7WNB1 Matrix protein M 666363 Yes SL-0415 SL-0418 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}. UNIPROT A7WNB1 Pfam PF06326 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}. GO:0044200 GO:0019031 GO:0055036 GO:0039660 GO:0039702 MNKMNQLVRFVKDTVAVRKPQSEDKSYLPIPSTIGGHEVNSPFAEPTAPSLGIIQPKCKRADWLIKSHLTITTNYEIKEWETWDRAISDILDLYDGNPVFKPILLFVYYVLAYNARKIPGPSNGVRYGAYFDELTTVWHAIPELMNQEIDYSYNHRVLHRKIQYVISFKIQMSSTKRRTSPIESFIEVTSEGLKHTPQFTTILDRARFVYSLTGGRYVIHPF 222 A7Z035 Clathrin interactor 1 CLINT1 9913 Yes SL-0198 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}. UNIPROT A7Z035 Pfam PF01417 PROSITE PS50942 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}. GO:0030136 GO:0005798 GO:0016020 GO:0005654 GO:0048471 GO:0005802 GO:0030276 GO:0008289 GO:0006897 MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSLKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGNFPSQVTATSGNGDFGDWSAFNQAPSVPVAASGELFGSASQPAVELVSSSQPALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQPLQNVSTVLQKPNPLYNQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNMMTQSFGAVNLSSPSNMLPVRPQTNPLMGGPMPMSMPNVMTGTMGMAPLGNSPMMNQSMMGMNMNIGMSTTGMGLTGTMGMGMPNLAMTSGTMQPKQDAFANFANFSK 643 A8E5V9 Stimulator of interferon genes protein sting1 8364 Yes SL-0198 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}. UNIPROT A8E5V9 Pfam PF15009 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}. GO:0005776 GO:0000421 GO:0005737 GO:0031410 GO:0005789 GO:0033116 GO:0016021 GO:0048471 GO:0035438 GO:0061507 GO:0042803 GO:0002218 GO:0000045 GO:0051607 GO:0045087 GO:0032608 GO:0016239 GO:0032481 GO:0061709 MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQQHSEEYSML 329 A8QFF6 Probable spastin homolog Bm1_53365 Bm1_53365 6279 Yes SL-0198 Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT A8QFF6 Pfam PF00004 Pfam PF17862 PROSITE PS00674 Severs microtubules, probably in an ATP-dependent fashion. {ECO:0000250}. GO:0005737 GO:0005874 GO:0048471 GO:0005524 GO:0016853 GO:0008568 MLHPQKLEQQNYETFNKAYLKSKQLVTEGVSIDEISSNNDEQRKRIAMEKYRMGIEYFEKALKISPDKVYPEKRSEVITHREAMKRNLEATKGRLSDLEKMFPSKGNRNLQHRPVQFVSPSISKPQTAQLSSRPISSEKKNINYSNARTRSNLLKGVDDKFGGPLLNEILNQDDVKMSDIIGAETAKRALEETVILPTVNPSLFSGLRQPAQGILLFGPPGNGKTLLARAVAGECGSTMFLNVSAASLTSKWVGDAEKIVRALFQIARNGQPTIIFIDEIDSILCERNEKETEVSRRMKTEFLIQMDGMLSSKDDRLLVIGATNRPEELDSAILRRFPKRILIDVPNAAARLKLIMSLLEKTKTSFDLGLTQRQILAEWTHGYSNSDLVALCREAAMVPIRDLSRKDIKNLVSTELRPITLRDFEIAMKAIKPSTNERMLQKLRKYAATAGQSD 454 A8T6P4 Rab effector MyRIP myrip 7955 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. UNIPROT A8T6P4 Pfam PF02318 Pfam PF04698 PROSITE PS50916 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}. GO:0030864 GO:0048471 GO:0030133 GO:0003779 GO:0046872 GO:0017022 GO:0017137 GO:0006886 MGRKLDLSGLSNNEAEHVLRVVQRDMQLRKKEEERLSEMKQELEEEGSRCLLLSKQQKFNEHCCIRCCSPFTFLLNPKRQCLDCHYNICKSCCSYSQSERGYICAACQKSRHLRTQSLEWFYNNVKSRFKRFGSAKVLKTLYRKHIIERGALSELPEVSAHEGSNDNGSICDGSDSTLYKQSEGHSMADTLTVALRVAEEAIEEAIAKAENYKDSLEKQNEARYLHEHKEELIEELATTIVQKIIQRGKRPEIQEEYEFVWPQNQKSELPSPTSTQNPLATQNSHSTSQPGAVAQSDISKRSRSAYSSDDSPEKGPEVGMAPGVPKSTEVETDIQNYSSLRRESRALSLPGWKSVDRLENSSASSVLQSPDGNWIALQSSQHSRPSLLTKRKSLVFSVLEKESGVVSAYDEMGSDSDPEDQGGWGAALLQFRRRLSDETYYTDSQHDPEWTFTQHPPITSPSSGQYTNTETLNSDSETSPSPSTRARRAPVMKKGPPETHLYPYYRHPADIVALPQLKPDVLDVNFNPHLGGDSSDGEERSEQVKRSRRRRKSKRETSEHSRAHNALYSAATAENSTVLLNAMMMRRQQSQENTVPLNHQTPDSVTSPDILTFNNMSPEPEYQNTLAHNSSAASLPLLSQLGSNNPGFAPQDPLLRAFPVNETLEEELKYKLSELIGQVSERDVKSSDFEPISEVGNKQEDRVSEKDSGKLRPKERRESKRESKLREMEKQSERQTVKLMDTSDAVRQINIERQMKKERERQRDIERQVERERERQRELEKQIEKDRERRREIEMQVEKKQERQKEMEKQLKQEQERQSEIERDLEKKRKSIRMEKRN 838 A8WVD2 Nucleoporin SEH1 npp 6238 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}. UNIPROT A8WVD2 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0005765 GO:0031080 GO:0035859 GO:0005198 GO:0034629 GO:0051028 GO:1904263 GO:0015031 MSADKSPYQIEPYKTVGAHRDLIHCVSFDPHGRRMATCASDMTMAIWDRQPDGNWRRSAHWKCHGGAVWRVIWAHPEFGQIVASCSYDRTIVIWEEQIVRTEKDLKCKESQWIRRTIISDNRSDVTDICFSPRHLGLSLASCNVLGAVRIYEAPDVVDASRWNLIHELQAFHTRCGCVTWSLSRMHRPLIAVGSDEKKAGGKERVVIYENIDGLRKWQRIHSLVFDMPCPITDLKFSPISMVDSHQLAIASGDVHVFNIKVPRTAILEEDGVDNPIHLADYSFQRVALLGDQRKAWRIRYNLIGSVITSTSLDGTLRSWKSLFVNQWVKLSEMNVDDYVPTADEVHKIVEAKTTERLPSQLDKVYF 366 A8XA40 Calnexin cnx 6238 Yes SL-0198 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}. UNIPROT A8XA40 Pfam PF00262 PROSITE PS00803 PROSITE PS00804 PROSITE PS00805 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}. GO:0031410 GO:0005789 GO:0016021 GO:0048471 GO:0005509 GO:0051082 GO:0030968 GO:0007275 GO:0006457 GO:0009408 MLNRKWSFVFLTFLLVISVNANDDVFEDEDEASESGVEKDEFVPSNFVAPKLADTSKPNFFDYFPVGSKIGQTWIKSLAKKDDVDSEIAKYNGEWSIGAPTKVSIEGDYGLIVKTKARHHAIAAKLETPFVFGSNKFIAQYDVKFEEGQECGGGYLKLLSEGAEKDLASFQDKTPYTIMFGPDKCGASGQVHLIFRYKNPVNGTVSEYHAKQPASIGTAYWDDHNTHLFTLVVKPTGEYSVSVDGKSLYYGNMLSDISPSLTPPKEIFDETDLKPEDWDEREQIEDETASKPDDWDENEPQNVVDESATKPYDWNEEENELIPDPEAQKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKPPTIKNPKYRGKWVRPKIANPAYKGKWSPRLIDNPNYFEPKPFDGLAPISAVGIELWTMSENILFDNILITSSEQDASEIAKQTFYIKQQEEYRLAAATGSSNGIFQQIVDATNEKPWLWAVYILCILLPLIAIGVFCFGKGSKPAPNFAKKSDTYSPDDDRVPNLVDDQEEEIIAEDEEDNQPGPSGTQNQPPIDEDEQDEVEQQPSSSKTASSESSSAAEEEDNDHVVHENEPVQPTEEVAKKSPRVTGGAKRRTARRGD 623 A8XV40 Probable spastin homolog spas-1 spas 6238 Yes SL-0198 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}. UNIPROT A8XV40 Pfam PF00004 Pfam PF17862 PROSITE PS00674 Severs microtubules, probably in an ATP-dependent fashion. {ECO:0000250}. GO:0005737 GO:0005874 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016853 GO:0008568 GO:0031122 MFAFSKAPAGCSTYERVTQKFQDGSNKLRAAIEMDELTKQNGTINEKLQTAELYKQARQMLKEANEFNIMDIPESKRSEVREKREKTLNLEKSAQDRLIKICNEVDPNMKRASTAADPCRAARITPRNTRATVPGDKKVSKVKQTEKAPHVCSRGDRCGAHQPPPEKKSTPLKPVNQIRTRVKENKNPIGVQQQVFSFILSCCMRRNCRRPHYLFPCMISLKMNYFKFQATLPNQLNTVNRSNLLKGVDKAIGERLLDEILDSTGVRMDDVAGCHSAKATLEEAVILPALNPNLFSGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNGQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSPDDRILVIGATNRPYELDDAVLRRFPKRIMLNLPDTEARKELITNTLKKHDMMDGLSSSDIRYIASNTSGFSNSDLVALCKEAAMVPVREIHRSKLSVTDGDKIRKIRASDFDTALRTIRPSTSDRILSKLSDFSRNFGC 542 A9C3N6 Protein CUSTOS custos 7955 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:P0DPK0}. UNIPROT A9C3N6 UNIPROT A3KNH5 UNIPROT A8WGJ3 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}. GO:0005635 GO:0097065 GO:0007275 GO:0030178 GO:0060061 GO:0016055 MSESSSEDENTARLKEAVWSFKPEDVKINGKENNGRQSHRADVSKHEHDGNELGTTPEFRSHVAKKLGTYLDGCISEVCSDTVEPAQSENREDEEGFRLFSSSTPGKWMEQSPPPPPKRRPVPSSSDSDSEMEMRFREAAVSLSDILGPVAQNLSEKTEEKSTKEETEDTVTKMKKKKKRKTSSEESQDKVNHQTEKQSNVEGNQEQTTAGERLKKKKKKKKKKRKKLEKDIKKDE 236 A9CB27 Zinc finger protein ZPR1 ZNF259 9555 Yes SL-0198 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}. UNIPROT A9CB27 Pfam PF03367 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}. GO:0030424 GO:0015030 GO:0005737 GO:0097504 GO:0030426 GO:0043025 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0030971 GO:0031369 GO:0008270 GO:1902742 GO:0061564 GO:0030576 GO:0071364 GO:0042023 GO:0001833 GO:0000226 GO:0006397 GO:2000672 GO:0010628 GO:0045927 GO:0042307 GO:0033120 GO:0071931 GO:1990261 GO:0031641 GO:0008380 GO:0021510 GO:0001834 MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPAEKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLASQR 459 A9ULB4 TP53-regulated inhibitor of apoptosis 1 triap1 8364 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43715}. Mitochondrion {ECO:0000250|UniProtKB:O43715}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}. UNIPROT A9ULB4 Pfam PF05254 PROSITE PS51808 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}. GO:0005758 GO:0005739 GO:0048471 GO:0006915 GO:1902166 GO:0015914 GO:0048793 MNSVGEECTDMKREYDQCFNRWFAEKFLKGECSGDPCTELFRRYRDCVQKAIKDKDIPVDGVDFMGPSKSKTESDGSS 78 B0BLK7 RING finger protein Z Z 42764 No SL-0382 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}. UNIPROT B0BLK7 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGSKSSKSSGFENVPSLGLSHTNQPRVSLIREARPSLYGRYNCKCCWFQNKNLVECSDHYLCLKCISSMLRRGQNCEICGKPIPTHIAVTTAPTAPPEP 99 B0BLK9 RING finger protein Z Z 208899 No SL-0382 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}. UNIPROT B0BLK9 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGNCRSKQESHPICPNTQTPEPTEAEFRRAAVNSLYGRYNCKCCWFADRNLINCSDHYLCLRCLNVMLRTSNLCNICWKPLPTRISVPTEPTAPSE 96 B0LSW3 Platelet-activating factor acetylhydrolase IB subunit alpha PAFAH1B1 9685 Yes SL-0178 SL-0182 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}. UNIPROT B0LSW3 Pfam PF08513 Pfam PF00400 PROSITE PS50896 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. GO:0000235 GO:1904115 GO:0005623 GO:0005938 GO:0031252 GO:0005813 GO:0005881 GO:0000776 GO:0005875 GO:0031514 GO:0043005 GO:0043025 GO:0005635 GO:0031965 GO:0048471 GO:0032420 GO:0045202 GO:0070840 GO:0042802 GO:0051010 GO:0051219 GO:0001675 GO:0030036 GO:0008344 GO:0001667 GO:0060117 GO:0048854 GO:0051301 GO:0007268 GO:0090102 GO:0021540 GO:0043622 GO:0000132 GO:0042249 GO:0007281 GO:0021766 GO:0021819 GO:0007611 GO:0016042 GO:0051661 GO:0090176 GO:0031023 GO:0051012 GO:0046329 GO:0007405 GO:0050885 GO:0001764 GO:0051081 GO:0007097 GO:0036035 GO:0001961 GO:0061003 GO:0040019 GO:0009306 GO:0043087 GO:0070507 GO:2000574 GO:0008090 GO:0019226 GO:0047496 MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR 410 B0V3F8 Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog prkra 7955 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT B0V3F8 UNIPROT A4IGC9 Pfam PF00035 Pfam PF16482 PROSITE PS50137 PROSITE PS50835 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}. GO:0005737 GO:0048471 GO:0003725 GO:0008047 GO:0030422 MAPQRSQDKTPIQLLHEYGIKISSAPKYELIHADGDAHQPSFMFSVTIGEVTCKGRGSTKKAAKHEAAEAALKLLKRDSQIIDQRDNNGLSPEAGEASNPVGILQELAMQRVWCLPEYVVFMETGPGHMKEFTIACRLEGLEETGSGSSKKLARRAAAENMIAKLQSLSGSSEITWSPPSRVYVESLRNSTGEKVSLLKRTPLSLPNTDYIQMLLEISLELGFQVTYIDIDELTVNGQYQCLVELSTRPVTVCHGSGVTSSNAHNAAAHNALQYIKMVASKH 282 B1A8Z2 Calcium and integrin-binding protein 1 CIB1 9940 Yes SL-0198 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}. UNIPROT B1A8Z2 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016324 GO:0032433 GO:0030426 GO:0030027 GO:0005815 GO:0005634 GO:0043204 GO:0048471 GO:0032587 GO:0042383 GO:0005509 GO:0001525 GO:0006915 GO:0007155 GO:0007049 GO:0030154 GO:0051301 GO:0007229 GO:0007283 MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 B2MVY4 Cyclin-dependent kinase 4 CDK4 9940 Yes SL-0178 SL-0182 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}. UNIPROT B2MVY4 UNIPROT B2CL06 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005737 GO:0031965 GO:0005634 GO:0005524 GO:0004693 GO:0007049 GO:0051301 MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE 303 B2RUJ5 Amyloid-beta A4 precursor protein-binding family A member 1 Apba1 10090 Yes SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. [Isoform 3]: Golgi apparatus. UNIPROT B2RUJ5 UNIPROT Q3UH49 UNIPROT Q8BMF2 Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 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}. P61294 EBI-8840254,EBI-529766 P20340-1 EBI-8851226,EBI-8840254 GO:0005737 GO:0043197 GO:0098978 GO:0005794 GO:0016020 GO:0005634 GO:0048471 GO:0005886 GO:0048787 GO:0032991 GO:0098685 GO:0045202 GO:0008021 GO:0001540 GO:0030165 GO:0005546 GO:0044877 GO:0007268 GO:0014051 GO:0014047 GO:0001701 GO:0006886 GO:0007626 GO:0035264 GO:0065003 GO:0010468 GO:2000300 MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI 842 B2RZ50 Cyclin-dependent kinase inhibitor 3 Cdkn3 10116 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}. UNIPROT B2RZ50 Pfam PF05706 PROSITE PS50056 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}. GO:0005737 GO:0005829 GO:0048471 GO:0004722 GO:0004725 GO:0007050 GO:0060271 MKPPISIQASEFDSSDEEPADDEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSSGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR 212 B3H5K9 Protein NEDD1 NEDD1 3702 Yes SL-0178 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}. UNIPROT B3H5K9 UNIPROT B6EUA6 UNIPROT Q9FI89 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. GO:0000777 GO:0005828 GO:0005635 GO:0009524 GO:0000919 GO:0009553 GO:0009555 GO:0032467 GO:0060236 GO:2000694 MMSNLVEPSWRLLAASGGDTVKLFDVSADSGDPCVLSYTPSPGCAVNSVKWNHTNLVVASTGEDKKISLWRKNGQSLGTVPVTGKDGGDSAEECLSAISFSKKGSRYICSGGTGQIVKIWDLQRKLCIKKLKGHTSTITGVMYNCKDEHLASVSVGGDLIVHNLASGARATELKDPNGQVLRLLDYSRSSRHLLVTAGDDGTVHLWDTTGRSPKMSWLKQHSAPTAGVCFSPSNEKIIASVGMDKKLYTYDSGSRRSSSCIAYEAPFSSLAFGDNGYILVAGTSNGRVVFYDIRGKPQPVTVLHAFSNSEDVTSLSWQTSKPVIVNEKNYTSEMALLGSTVEDSVVIPDPLPSTTPSASQSAMAPGSRGVSASTVNASSVEQTPNRNHLWPSGPLGRLHALRANDSYNDDMGVFSPIIDVSSVEKWADSEGYNNKDHLVVDNKPSSLLFPSSSKGYSFGDNGSKEHPIFDWKPSSTSKQDDPRAAFSSFGSITPTASSKSEDSALTPPEAWGGDKFSEKFNQLANEKFSDKFSHLHAPSRLAVSSTGASTSGSMFSSSRDFPLSHGQTNFANASLEFPRIRDFSSTFETSSTQTDNNLPSSPLFTKGITAPGNIDSLRLSPNFTRRFSTYAERISTTSSFSDGASLSLGGSPKIKKTGSETREEVLNHLLARPETVVATEAGAMPLMNQGGLKQSQTDQQQVMGSSNFTLQLFQRTLEGTLDSFQNSIHDDVRNLHIEILRQFHMHEMEMSKVLSSILENQAEQMKELKLLRKENQELRQRL 782 B3P100 Protein asunder asun 7220 No SL-0198 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}. UNIPROT B3P100 Pfam PF10221 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}. GO:0005737 GO:0032039 GO:0005634 GO:0048471 GO:0051301 GO:0051642 GO:0046843 GO:0030317 GO:0051321 GO:0051663 GO:0060814 GO:0080154 GO:0007346 GO:0034472 GO:0007283 MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGGGGSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIVSDTAAHIVNTWSHSTQNMSHVMNAMVMVGVPSRNVATSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTDELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNALAAPPAKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISPLLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGATYETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSLCITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMVPLKVKDPSAPPLARRLPRYFPLTTSSSILFHLQRHINWLPHFLHILVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLESLQSLRAAYGDAPLKSEPGASLLRSYTESPLSPERLEPITSGSASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQSNKRLDFSGRLCTPLGQVAKLYPDFGNKDKDSVVTAASITPNVKEESVRS 689 B8PYG1 NMDA receptor synaptonuclear signaling and neuronal migration factor nsmf 7955 Yes SL-0178 SL-0182 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}. UNIPROT B8PYG1 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}. GO:0005938 GO:0030054 GO:0005856 GO:0030425 GO:0016363 GO:0031965 GO:0005886 GO:0014069 GO:0045773 GO:2001224 GO:0048168 MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLIVKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSEPSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQRSLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVDRKAKSFSRSWSDPTPVKPDSLHDSRDSGDLQASSGNLDEEDCDDVDWEEERELERVACEGDDFIPPKLMLISSKVPKAEYVPNIIRRDDPSIIPILYDHEHATFDDILEEIEKKLTAYRKGCKIWNMLIFCQGGPGHLYLLKNKVATFAKVEKEEGMMQFWKKLGRFMSLLNPEPNLIHIMGCYVLGNANGEKLFQNLKRLMKPHGIEFKSPLELSAQGKEMIEMYFDFRLYRLWKTRQHSKLHDYDDLL 570 B9EJ86 Oxysterol-binding protein-related protein 8 Osbpl8 10090 Yes SL-0178 SL-0182 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}. UNIPROT B9EJ86 UNIPROT G3X9N6 UNIPROT Q69ZJ4 Pfam PF01237 Pfam PF00169 PROSITE PS01013 PROSITE PS50003 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}. GO:0032541 GO:0005829 GO:0005783 GO:0005789 GO:0016021 GO:0043231 GO:0016020 GO:0031965 GO:0015485 GO:0008289 GO:0070273 GO:0001786 GO:0140343 GO:0032934 GO:0015248 GO:0032148 GO:0045444 GO:0030336 GO:0010891 GO:0015914 GO:0046326 GO:0046628 GO:0051897 GO:0090204 MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKEDISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQHFKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVSEENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGLKKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFLNRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWDSEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDRKTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSPEPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILLQVIINFIFK 889 C0HAC0 F-box/LRR-repeat protein 5 fbxl5 8030 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT C0HAC0 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 MAPFPDEVDVFTGPHWRMKQLVGLYCEKLSQTNFSNNNDFRSFLQSLCATFKEFKMHEQIENEYIIGLLQQRSCNVYNVHSDNKLSEMLSLFEKGLRSVKSENEQLNYAQQLKERLEAFTQDFLPHMKEEEEVFQPMLMQYFTYEELKDIKKQVIAQHSSQQRWDCAAEVLKGLSLWSQAEELHKAFKYADHEKTDDELEKELCSTHISQLPTEILLCLFRYLGPEDLCHCGQVCSAWSDLAKTGSLWRHLYPVRWARGDYYRGPPDDVNQEPDEEWVKSLQDEGKAYQEWDEDADVDESDASCEDSLAISAAQREKKLLNGMIQNLLPAVGSSVRSIVLAYSSTVSSKMVRQILSLCPNLTHLDLTQTDVTDSAFDSWSSLWACLSLEHLDLSGCEKLTDRTLKKLSLGLGDLASPTCSEKRSDRRAKLLKSPPSPISLLDKRSLRPTGHSRQVLIFKQWPGKLGSAPCSPTRVWVLDASELADIEDAAEWNRRRGVSTPEVRGFVETQPGGLSCCCRRRRGGFRTGFSTSYWQQQYGLGEAGCGHSTCCTGETALRTLGGLQYESYTTRGSAGAEFRTKCSSGGQLCLECDNRTDPSDGRRSLRFLSLSGCYQVTDLGLRALSQRGGLPLLEHLNLSGCLLITEVGLQELVSACPALNDEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE 696 C1BK83 Nucleoporin SEH1 seh1l 8014 No SL-0178 SL-0185 Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}. UNIPROT C1BK83 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0005623 GO:0000777 GO:0005765 GO:0031080 GO:0005198 GO:0051315 GO:0051301 GO:0007080 GO:0051028 GO:0006999 GO:1904263 GO:0015031 MFVARSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKSDNGEWNCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKQRGLSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSNTAYSGKVQIYEYVENTRKYAKVETLMTVTDPVHDIAFAPNLGRSFHVLAIATKDVRIFKLIPMRKESSSSGPTKLEVQLQAQFDGHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILRGDGSPVNGAAGQAGTPGAAGTPGGPASQNALQAVAGRKKAQLMPG 364 C5DK07 Spindle pole body component KRE28 KRE28 559295 Yes SL-0178 SL-0182 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}. UNIPROT C5DK07 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MADDPTINGLELQLNAAEEHATALTEEALQNQDLHYKEVVEQLKRSVEQLVEDNESLFTAVDLPPEVDPTCISGRILDLAQLTQQLKSTHLQQETLDNFLRYTISSTDILQLESESDERYASVSRAVSQLQDNDIIQLDSEVDQIKQDIRKAGQTIADQREALNELCLETGNLADECHTLLSELEEATRTREMVEKQAAVEVTNDHPVEEMYASWQSLKEELQQESHLRRHLNQLKQSKASLEAILGTKNGNEHKDTNVMQEYASYDAFIRFWISKFTNKEMENLEVFPRSNKFQFTHRGTDVVISLGPRGISRVELYGKGIPLEKIAAARKDVNEEASRGEELYMSINRIIDKIKEHTTVS 362 C5DQ18 Nuclear rim protein 1 NUR1 559307 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT C5DQ18 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 MSLRISKDVSVSVNTADLLPEDDGFDRVDGDNRGWFSVFLGLFNTHPSDWNIALNEAIETIDWDSKSITLAQPLGNFFTFAFYVVRLLQLSLIKPNLSRINEKTDHFDLSKSEMLKKYEYLYHFTNDKNQSVGNVYYRFLGRLGKFFDICIVLLTFTNGFITYKFFWGNFKMYCLFYLKKGPHLRNVTKASLQKLGQDDDDGSLWSSLRYFWNGTKDKEGSTDDRDDDDGDIHYKLFKWTPSQFITMLFVSFAPTAVVFLLFTEVSFLTLIAVIVHQWVLHRLVIDCYGNRLVHESVIASANLAEVEAKFVKPRMSKKVQDVAIDCTPHGDGMVKFYPALTTNRSHIFQTHSLTGELITETFNPSTKEFEDLQTEGTTHNVIRTAPYAAGDLLHRDPYWYQRNMIMRDVAHRPYFHSREVSPTRYHPSRISPRPGQYSPLVSSTSGMSTPLMRPDRSPFLNTRPSLGEREELFHRGNSRSPLRQPIENFKSLDRSSDSQSPIRRHNGDSDA 511 C5DZ48 Spindle pole body component KRE28 KRE28 559307 Yes SL-0178 SL-0182 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}. UNIPROT C5DZ48 UNIPROT B2G406 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MKSDLDGYEVRIKSLENQTAHYSEQALLEQEQRVLASLREITQNVIAMGQENSLVEIKGELESKEESELVIDPSGFQEKIDTFVELVELLKVTHLEQETLDNFLRYTISSSNLLQINSVQDAKYVELESQVKELEQGTLESHKREIEATKGQIKNLCQELSMAQDSINETFLDTSNALEECDALLNELTQLRMEKQTSEEADTIEDDPVSQTYEDWESLQKSKLELRLLEEETSRLQSRVESYEDYQKRSRQLSNNDPRMLQNHKALELLVELWMTKFLPQPGISHLELFPQSRKFQFDVEPTFTVVITLADQTTFQNVQVYRKDAKSLVMDHGLNDEIKNSYLGTNNIYNGLNDIIHTLQRRVQAKGSN 370 C5E006 Monopolar spindle protein 2 MPS2 559307 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT C5E006 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MDFDKSSSSLVLDLAWNQVDKKNQDFIYAKDFPALIMSIEEILSRGQQTPLAFLSNTGKSVIDTFAREKEFFKIYRDEFKEIFHGLVGKTFKDTIEGTNVSRSVLDEQGQEPDVSTTPTRQQRSSPRKVNRLLKNLETRVASMKDELKFKDEILAEKDRELIQLTRKLSDYKDKYEFVQRQFSFYKDHGESPRRNSSESEQLNLEQNASTKHEFIISELKRKLQEQTLAISNLKEQLQRGEGAGVLYTNYSKRYNPLHNDGPMVLVLATLVFLTIILLIGSMIWVTGGKDDSNSFSQYSWWENNSLLSRIGWFFRDWSDTGVDYVNFEPSSDAYERIMGIRRI 343 C5E2E7 Monopolar spindle protein 2 MPS2 559295 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT C5E2E7 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MDTERHATLLLDLVWPEVDEKAQGFIYAKDFPLVVSRMEEILNRGKLERDRAQLVSETGREILRKFGSDQEFFKVYKEDFRELFDGLVGTSFKSAVKSCAGDGVLDRLQDSQAVDGIQDEKTSSHALQEEVMRLREQVRVLSSKNDEKDREITARDEIIADLQGKDASPAGSPRSLQRMRTLQARVTSLEDELSFRDEVIREKDRELLNLTKRVGEFKDKYQFLEREFQFYKGHREQKSPDSIKEATRHEFIISELRRKITEQSEIIGQMRMQVEAKPGALHPQGIGSTAGLPLNLPLRLVLRLIIGAILAYLAFDIGIRSLKAVGGLFGSSSPATLTPKSELSWWEQNTLLSKLLWFFKDLFDTYNLDAGRDEVVSANYDKLFGV 386 C5E3S7 Nuclear rim protein 1 NUR1 559295 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT C5E3S7 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 MTFRLSRFESPLIEDDGESRASLLGYSPENELYTDVDENRESRFRRFMSFISSSPYDMFLAINEHVESIDWDSKASTIAGPLGNFFTCSLYTARLLQDSLIRPNQQKLDKKRDSFDLSRSEILRKFEYLSQVPKSGVVVTHLNWYWKFLTFLNVALQITVGFLILINLFVAYKFLIGHFQVYSLFYTKTSPRSKNVTKRSLSDLSFKSLEEVTNSSLWTMIRYMFVRKRLIIKDAPKGKYYYQLRKWTPGKFYTALFSAFSPISVIFLLVTEVSFKTALAVIGHQYILFLVLFKRYESRLDDEACLAKAHFEEINEKVIKPKTTIKTQDAMVDATTYGGGAAFFPSFTTTRSHIFQTHAVTGDIITERYNPETRNFEDVENTGRAKNYISQIQGVSHGQQVVSRSKAMNGATARPQFFSRQPSPSKIGTPSIILNYRTSPFSAPTTPTLKPVNGVQNGQSIFRNSPDPSKANSLNCDTSHLSRNNTLSRLRRNSVSPTKSGNYCSASGMRAIHKSNFGADSSVSYSMEAPSNELPFEEVARRGRHPFEITASRDLPAGRSSAVSSRHSSISPFKGNTSFAGRESLDSRPPFR 592 C8XPB2 RNA-directed RNA polymerase NS5 POLG 64296 No SL-0382 [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}. UNIPROT C8XPB2 Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0005525 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLKGIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSDSMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIERWMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKPSVDIWLDSIFISSPVLVRRVSHTATISDTKVQTACPTNGEAKLEEEASAEYECKKTYSDRGWGNGCGLFGKGSIVACAKYTSTGHMDVYEIDSTKIEYVTKAQVHAGMKHDDTTMVKEVKFEPTTGSMDVEFTGYGTLGLECHVQTMVDMANYYLVVMGQEAWLVHKQWVEDITLPWKIGEGGFWRDKHYMVEFTEPHATTMTVMVLGAQEGALRTALAGAMVVTYTDSSGTKKFSLKGGHVSCKARMNGLVLKGSTYTMCKGGFSFVKTPTDTGHGTAVMQVKVSKGTPCRIPVQAVDSSNGGTNRATLITANPIAATTEDEVMIELSPPYGESYIMIGTGDDKLTYHWHKSGSTIGSLFTETYKGAQRMAIIGDDAWDFSSSSNFFNSIGKALHTVFGNVFHSIFGGLSWITKIILGGMFLWLGVNSRNQTMCMVLMAVGGILLFMTLGVSGEVGCSLDIKRRELKCGDGLFLFNDVNDWTHKYKFHPEDPKLLASLIKKSHQEGRCGLSSVNEVEHRMWNSIKTEINAMFEENGVDLSVVVKDSKLHYKMGSHAFPKVEEGLSLGWKNWGKSLVFEPKQSNVSFIIDGTSEDCPFTNRIWNAFVVEEFGIGMFTTNVFLTHKVDFTKQCDASLLGAGVKGDVAVHGDPTLWMESRKENGTWQLHTIQMNGLRECFWPQTHTIHGSSVMESAMFLPKQYGGPVSHHNHYTGYAVQTAGPWNVQPLIVKRETCPGTQVRVDEQCRDRGNSVRSTTSEGKIIPEWCCRSCTLPPVSFWGPDSCWYAMEIRPQNVHEEHLVRSWASAGTGMAESSLGLVALFLFTDIFARKRMTRKFMVIGCLGVLSVMIVGGFTALDLIRYIIVVGQHFASMNHGGDVAYLAIIAVGKLRPGLLMMYSFKAAWSPKERVMVALGLLVFQAVLGDFVHTGLWEWADAAGMCILIIQGMATRKEKTYIMPILALLTPLSMEIIRKTGIFACVGLLGLSLWRGGDTTMRKGMPLLAGAATAASGLTRASLSVVFILCATAASRRSWPIGEIMAIVGIVGTGFGMAVNDQASLAGPMLVFGLIMIVYATLGRADGLTLKRVGDITWEEEAVHSGSSTRYDVTLNEAGEFKLVHEEPVVWSHVVFLVVALIAASVHPIALVVVTIIWTYGKKHLRGGVLWDIPIAPPVEEAEPLEDGVYAILQSGLMGKAQAGVGVAQEGVFHTMWHVTRGGFLMVGGKRLTPHWASVKRDLICYGGNWKLDGKWDGVEEVQLIAVAPGKAPTNVQTKPGVFRMADGTEIGAVALDYPSGTSGSPIVNEKGQVIGLYGNGIVIGGSGYVSSIAQIAGGEGVTEEPLLDTATMLRKGKLTVLDYHPGAGKTRIFLPYILKECVRRKLRTLVLAPTRVVLSEMREALRDVAVKYHTQAFQAAGTGRELVDAMCHATLSHRMLESSRSVNWEVIIMDEAHYMDPTSIAARGWAAHKANNHESAVIFMTATPPGSANEFPESNGEIEDLRRDIPTEPWNKGHEWILEDRRPTVWFLPSIRAANNIAACLRRSERSVVVLNRQTFETVYPTIKTKKPDFILATDIAEMGANLGVERVIDCRTSYKPVLTTDGRVVIKGPLRIPASAAAQRRGRVGRCKDRDTDSYVYSEETSEDNGHYVCWTEASMLLDNMEVKGGMVAPLYDVEAQKTEMVPGEARLRDDQRKVFRTLIKRYDLPVWVSWQVAKSGLMLEDRKWCFDGDDENTILNDNGEKILARSPGGQRKFLCPRWNDSRLYYDNASLMSFLAFAEGRRSYLGVWHAVQMAPLKLGEKLTESLDTMVMLMRSEEGTRAYKLASTNAPEAVTILLMTGIVVACTLGVGLAFMWPKGVDKMSMGMITMSIAGYLMLQGGLTPVQVASVLLIFFIFMVVLIPEAGTQRSINDNKTLYVLLGVALLIGAITANEMGYLEKTKRDLLGERVQNEWKLELPMFDLRPGAAWSIYVGLATLVMPVLDHWIRTEYGSLSLTGIAQQASILQAMDKGVPFFKLNMSVIVLLVSVWNNFSMLSVLCGVGLLGVHCAFVLPGLRAQAAKQAQRRVYHGVAKNPVVDGQTTAEIETAPEMPPLYEKKLALVLLGVVAIANGVMVRSAFSMAETVVLLSAAVGPLLEGNTSAIWNGPMAVAMAGIMRGNYYAGIGLAYNLWILQSPKRGRSTTMTLGELWKRQLNLMGKREFELYKITDIHEVDRSQAQAVMKAGIDNVGISVSRGTSKLKWMVDRNYVEPLGRVVDLGCGRGGWSYLCAASKRVSSVKAYTLGITGHEKPVNVQSLGWNIIKFKDKTDVFKMEPHACETLLCDIGESSSNPLVEMERTLKVIDNVERWMSPTTESYCFKVLAPYRPEVIERLERFQLKYGGGIVRVPFSRNSTHEMYYVSGVKNNLTHMVSCVSRLLLRRMTHPDGRCKVEADVVFPTGTRNVASDLGPMDLSKVKDRVNRLRSEQGTWFQDDSHPYRTWHYLGSYVAKQSGSAATMVNGVVKMLSMPWDRIENVTQLAMTDTTPYGQQRVFKEKVDTRAPPPPPGTRAIMEVVNKWMFDFLAREKAPRICTKEEFINKVRSNAALGNMLEEQDGWKDAATAVQDPRFWALVDRERQVHLEGRCETCIYNMMGKREKKPAEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSLAGVEGVGLQYLGYVVKNVWEKSNGIMYADDTAGWDTRVTEADLDDEQYLLSKMEGYHKKLASAVMNMTYKYKVVKVPRPGPGGKVFMDVIARQDQRGSGQVVTYPLNTGTNMKVQLIRMAEGEGVISRHDIERVTIKTLNALRVWLAENGAERLSRMAVSGDDCVVAPLDERFGLALHHLNAMSKIRKDIDDWTESIPWRSWESVPFCSHHFHQLFLKDGRSIVVPCRDQDELVGRARVSPGNGWKLKETACLSKAYAQMWLLMYFHKRDLRLMGNAICSSVPAHWVPTGRTTWSIHAHNEWISSERMLDVWNKVWIVDNPHMPDKTCIDDWRDVPYLPKSQDRLCGSLIGITARASWAENIRAVVNKIRGMIGNEVYSDHLSVMGRYTYSVQEVGTVL 3401 D3Z5T1 Coiled-coil domain-containing protein 78 Ccdc78 10090 Yes SL-0198 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}. UNIPROT D3Z5T1 Pfam PF14739 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}. GO:0005814 GO:0005737 GO:0098536 GO:0048471 GO:0042383 GO:0016529 GO:0030030 GO:0098535 GO:0003009 MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIATHHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQQALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASSTNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPRENEYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQHLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL 437 D3ZZ07 Cathepsin 7 Cts7 10116 Yes SL-0198 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}. UNIPROT D3ZZ07 Pfam PF08246 Pfam PF00112 PROSITE PS00139 PROSITE PS00639 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}. GO:0005768 GO:0005615 GO:0005794 GO:0005764 GO:0005634 GO:0048471 GO:0004197 GO:0007049 GO:0051301 GO:0045930 GO:0051603 GO:0060707 MTVAVFLAILCLRAALAAPRPDYSLDAEWEEWKRNNAKTYSPEEEKQRRAVWEENVKMIKWHTMQNGLWMNNFTIEMNEFGDMTGEEMRMMTDSSALTLRNGKHIQKRNVKIPKTLDWRDTGCVAPVRSQGGCGACWAFSVAASIESQLFKKTGKLIPLSVQNLIDCTVTYGNNDCSGGKPYTAFQYVKNNGGLEAEATYPYEAKLRHCRYRPERSVVKIARFFVVPRNEEALMQALVTYGPIAVAIDGSHASFKRYRGGIYHEPKCRRDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGEQWGERGYMKLPRDQNNYCGIASYAMYPLL 331 D7RF80 RNA-directed RNA polymerase NS5 POLG 33743 No SL-0382 [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}. UNIPROT D7RF80 UNIPROT B1PMU9 UNIPROT H8Y6L3 UNIPROT H8Y6L4 UNIPROT H8Y6L5 UNIPROT Q14F58 Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRKTVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCDDSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEGWVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKPSVDVWLDDIHQENPAKTREYCLHAKLANSKVAARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKFSCEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVVLELDKTAEHLPKAWQVHRDWFEDLSLPWRHGGAQEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGSKYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLITPNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGMLSSVGKALHTAFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWREVTDWYDGYAFHPESPSVLAASLKEAYEEGICGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDKRDPSDYRGGKVGTLRRSGKEMKTSWKGWSQSFVWSVPEAPRRFMVGVEGAGECPLDKRRTGVFTVAEFGMGMRTKVFLDLRETASSDCDTGVMGAAVKSGHAVHTDQSLWMRSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPAGLAGPRSHYNHIPGYAEQVKGPWSQTPLRVVREPCPGTAVKIDQSCDKRGASLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQGGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGSSVVWCGMVVLGLVVTGLVTIEGLCRYVVAVGILMSMELGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVATYFLLLVLELGFPEASLSNIWKWADSLAMGALILQACGQEGRTRVGYLLAAMMTQKDMVIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLAGLLGGEGVGLRLLAFRKLAERRNRRSFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLTAEWCGEVEWNPDLVNEGGEVNLKVRQDAMGNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAVWTLFEMLGSGRRSELVFSGQETRTERNRPFEIKDGAYRIYSPGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVDEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQETHQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPEIPLSVQGTGWMSKGQITVLDMHPGSGKTHRVLPELVRQCADRGMRTLVLAPTRVVLKEMERALAGKKVRFHSPAVEGQTTAGAIVDVMCHATYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGEWREGFDWITEYEGRTAWFVPSISKGGAVARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVIDGRTNIKPEEVDGKVELTGTRKVTTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVATFYGPEQVKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEENAIDGADGDLVRFKTPGGSERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAPEAFLTIVEVAVLGVATLGILWCFVARASVSRMFLGTVVLFAALFLLWIGGVDYGHMAGIALIFYTLLTVLQPEPGKQRSSDDNRLAYFLLGLFSLAGLVTANEMGMLDKTKADLAGLVWRGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQLQTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPMSLGLGVALAAFHLAIVASGLEAELTQRAHRVFFSAMVKNPMVDGDVINPFPDGETKPALYERRMSLILAIALCMGSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTMPMACGMAGLVRGSFWGLLPMGHRLWLRTTGTRRGGAEGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDKARELLKRGETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFRTGMDVYSLEAHRADTILCDIGESSPDPLAEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGLVRVPFSRNSTHEMYFSTAISGNIINSVNTQSRKLLARFGDQRGPTKVPEVDLGTGTRCVVLAEDKVREADVAERIAALKTQYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQVGTKIIMRAVNDWIFERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWPNAREAVEDPEFWRLVDEERERHLGGRCAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGTSLNYLGWHLKKLSELEGGLFYADDTAGWDTRITNADLEDEEQILRYLEGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVVTYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEHGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAKVRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMGDKGKVREWRDIPYLPKSQDGLCSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII 3416 D8V072 Matrix protein M 1559361 Yes SL-0415 SL-0418 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}. UNIPROT D8V072 Pfam PF06326 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}. GO:0044200 GO:0019031 GO:0055036 GO:0039660 GO:0039702 MLSRIKQGIKTKRSSSSSSSRSKTGDEDSSLMLRWVYDNDPPLKQTDTFQYLMAPTAPTDKASSSYIATTYKVDCKVEIISRASIRNFDELINIASCLIDSYDGQLLIKPWIITVYLTIITHLVKEPDTHGVRSSVNRYHNGFNEILTLYINKNFAPENKKYSFKKNLSTTHKGNQCNIIISIDLLPTDRKGKSIKDVYEVKMPDNREIPNFQQMLKPYNLKVKEKNGKYLISHKMSSSDDSIDVSDSDENEF 253 E1BPK6 Unconventional myosin-VI MYO6 9913 Yes SL-0198 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}. UNIPROT E1BPK6 Pfam PF16521 Pfam PF00063 PROSITE PS51456 PROSITE PS51844 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}. GO:0005905 GO:0030136 GO:0005829 GO:0030175 GO:0005794 GO:0005902 GO:0016459 GO:0005634 GO:0048471 GO:0032587 GO:0051015 GO:0005524 GO:0005516 GO:0003774 GO:0006897 GO:0015031 GO:0007605 MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLMGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLAVHRNIRDDEGFIVRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHDFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAQLVKRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKAEMNKQVKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIARSEAELIIDEAQADPAALRSLDFHPVTSKINGTRRTMTPEQMAKEMSEILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK 1295 E1C7U0 Stimulator of interferon genes protein STING1 9031 Yes SL-0198 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}. UNIPROT E1C7U0 UNIPROT A0A1D5P7Q9 PDB 6NT6 PDB 6NT7 PDB 6NT8 PDB 6NT9 Pfam PF15009 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}. GO:0005776 GO:0000421 GO:0005737 GO:0005829 GO:0005789 GO:0005768 GO:0005794 GO:0030176 GO:1990701 GO:0005741 GO:0005654 GO:0048471 GO:0005777 GO:0035438 GO:0061507 GO:0042803 GO:0019901 GO:0008134 GO:0031625 GO:0002218 GO:0000045 GO:0071360 GO:0035458 GO:0051607 GO:0045087 GO:0032608 GO:0002230 GO:0051091 GO:0016239 GO:0032092 GO:0045944 GO:0032481 GO:0051259 GO:0050727 GO:0061709 MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP 379 E7F4N7 Stimulator of interferon genes protein sting1 7955 Yes SL-0198 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}. UNIPROT E7F4N7 UNIPROT K4Q6R6 PDB 6MYD Pfam PF15009 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005783 GO:0005789 GO:0033116 GO:0016021 GO:0048471 GO:0035438 GO:0061507 GO:0002218 GO:0000045 GO:0039528 GO:0051607 GO:0045087 GO:0038061 GO:0002230 GO:0016239 GO:0032481 GO:0010506 GO:0009615 GO:0061709 GO:0032606 MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRMSEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSFYIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKITHNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSRELFQNLKQQDGEIFMDPTNEVHPVPEEGPVGNCNGALQATFHEEPMSDEPTLMFSRPQSLRSEPVETTDYFNPSSAMKQN 398 E7FDB3 Nanos homolog 1 nanos1 7955 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:11691838}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11691838}. UNIPROT E7FDB3 Pfam PF05741 PROSITE PS51522 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}. GO:0005737 GO:0060293 GO:0048471 GO:0003723 GO:0030371 GO:0008270 GO:0007281 GO:0008354 MDFLNHNYLSARASYDYTFNFWNDYLGLSTLVTKNSKHSVPQNPNSITESLKATLGLDDSPPCPCVMGEGDSGGHLDSCCCPPPASISILDLKERFSILSPFQNQNQGSLLSSSQEREIGIGGGFAGFDLFGVERKMRKPAARNKQEPKICVFCRNNGAPEEVYGSHVLKTPDGRVVCPILRAYTCPLCSANGDNAHTIKYCPLSKDQPAQRVLKGGRAVGGKRVKIF 228 E9P860 NFX1-type zinc finger-containing protein 1 homolog znfx 6239 Yes SL-0198 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}. UNIPROT E9P860 UNIPROT Q23388 Pfam PF13086 Pfam PF13087 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}. GO:0000775 GO:0031380 GO:0005634 GO:0048471 GO:0005524 GO:0003700 GO:0003723 GO:0003724 GO:0008270 GO:0030702 GO:0031048 MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFLQYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYEELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPGLPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENSSSSRRRFRDEEVQEEEGDHILSSEDVHAARNVCETKILVRGVPQKNDSELSKLINGSKLYVRFERPFVKLAHNLELLYVVNYAISSRKSIVRDHSKAIIRGLFEKDFLLKLKSKFLESSFDNDTWTPEGTELLFEIFHLFFTTARYKGGFMLTLPRFAPSWHDFSMAFDIADMDGLEEAGVGDDELRNLRRLIGYIETWIKRAERERNPSPLALRSYSVYEKAGSSDSGRQVLSESRGAGSSNVYGHDEVDFVDHRRRDEFGHRDNYRTENRRHKSPDNFGEVHRRLDEQQQQRHEDESSRYRDDSRQSRRADDRRDQYQYNESTSMENHLGFHNGGGTVSEHSRDDKFVSPQNCEEKRKYCEEDTDAKPQQPYRFEEIKFEPIWVKCEKSEPPEDFKTLPSVPVLSEYVNPVEPYLRRIQDDGKYKSVHHYLDVQFRLLKEDLVSPLRDGIDLYKKNGTCKGRRIEGAPCSDISIFNVEKVDGKQVTERDGYEMRIIWPAQYDILKLLDNDREMKELGLVMLSCDRFKEDFHLGHIQSSYLMRNGSLHFAVHEETSPFKPNTTYQMAQGTSYLPCYKHVLENLKRISSFKPLPFERYLVHGSKIIFRPNFQQAEKSEYQISEEKKLMKTYNELRSLAACARYTKGKPIPRGVDDDDEDYEFSKSRELSKEDIDLEYRQLQEPIFRPLVGVDIKDSNLIQINKKWYNVSRLLDEFHPDYMDESQRLAFCNTFKYELSLIQGPPGTGKTHIGVQIVKTILQNRSYWKITEPILVVCFTNSGLDNLLERIYQMIENDEELSKDNGRPKIIRFGSKCDSNYLKRQNVMRQDVYEQYKSKVSDGAQKKMSKAGAARRHKADNLAISSYTLFCSRNKLLSYEMLSRVMDPNHQMEIQQFTYDHVDTKGIPLSPDEAIGCWLLERDFGKATKSQTKKAKKPKFQGAQLDSEDENKDYFTVEDSDDEEDELDDEKLLDKLFEKMNLECSGADILSAVHASHADEYYTKGPWEIVQDKRPSVVVLMEKKTKPCNAKFTVDEQINNLVSEIKDMILSSQPVPKKDLNDIKYIFSLARLKRWSLYITWCDALRSIVTENLPRQIREYREACENFKNAQNRVDAEIMRMTMIIGATTTGCSRLRPTLEKVGPRILIVEEAAEVLEAHIISAMISTVEHVVMIGDHKQLRPNPAVHELGVAYGLRISMFERLVERGLPFSQLRQQHRMNLTISDKIVKLSFYDNVTDAENVGLYPDVQGMATNLFFWSHTSMEESPDEVSWLNKHEISMTVALVKHLLKQNYTTNDIVVLATYSAQKNLMYREYANVFGSTPDSNVIPVETVDSFQGKERKIVIVSLVRSHRGGRENTGIGFLAVANRICVALTRAQHGMYIIGNGAYIMNNSELWNKIVNNLRRSNLIEYNLPLKCVAHGNIVTVKDPQDFATKSPEGGCMQKCDTKKFCGHVCERLCHPNMEEEHLQRCLYNCDKKCSNPQFQHRCKKACYEECGSCLYLVEVTLDCGHRITTPCSRINSSKCDQSCTKKLLCGHACAAKCGEECTLVSECSQLVGMPLSCGHIKQLTCSKISANEIDLTCDQRCEKTMLACPHKCAEICGQPCTVECMEVVNVTLGCSHSQDVVCSSFMPGMTDHIECLTKVPKTLSPCKHTELVLCKQAPSTKLCTRRCTSYLEKCGHTCENDCGICFTTKTHICQNMCQKVLNCGHTCSAKCGESCPPCKAFCTNKCEHQSCGAGERGFGRDCSKLCALCVNNCSNKCAHRSCTLKCFEECNVKPCTEPCTDKLKCGHACLGICGEQCPKICGTCERNKYIECVSGTSSTSRVHRLIMIPKCYHVFPVEVLDDHVKKQKEANEKLKCPKCSAFIVGVLRYARYTKKYYLNENMRKLESNIRNIHQSTLEGRVFQAVQDSIGEIRNVTTNLTNASEDILRNFHQKILDIRTSAETFKGKPEHKFKFASLLQVANCCLAITRLLSVSSKFRVSRRKDIPPTFDLMSVRVLGDMPFPKLIDELNRVNIHLSNTYETFMPGAIIPKLKWLISRMTVLQQLTSMCHQLVLEKKDIADSDAHAINDACLNMFRYNEQHNYALNIENFEAIVVKVAPKLLEPTPKFWSWRRLQVPEL 2443 E9PXF8 Myotubularin-related protein 13 Sbf2 10090 Yes SL-0198 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}. UNIPROT E9PXF8 UNIPROT E9Q305 UNIPROT Q8BJ67 UNIPROT Q8BJD2 UNIPROT Q8BJP4 UNIPROT Q91VH0 Pfam PF02141 Pfam PF02893 Pfam PF06602 Pfam PF00169 Pfam PF12335 Pfam PF03456 PROSITE PS50211 PROSITE PS50003 PROSITE PS51339 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}. P0DP23 EBI-397435,EBI-911785 GO:0030424 GO:0010008 GO:0016020 GO:0048471 GO:0005774 GO:0019902 GO:0019208 GO:0035091 GO:0017112 GO:0006914 GO:0043087 MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHYCSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQSALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLNGMAFAGFVSERGPPYRACDLFDELVAFEVERIKVEEKNPLKMIKHIRELAEQLFKNENPNPHMAFQKVPRPTEGSHLRVHILPFPKINEARVQELIQENLAKNQNAPPATRIEKKCVVPAGPPVVSIMEKVITVFNSAQRLEVVRNCISFIFENKTLETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKDDNHIPHLKQKLPDGQHQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRASAPGDWESGSNSIVTNSIAGSVAESYDTESGFEDSENSDVANSVVRFIARFIDKVCTESGVTQDHIRSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLPGEEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQLQQSVQEGLQITSASFQLIKVAFDEEVSPEVVDIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFSKTIVKGAKKAGKMTIGRQYLLKKRTGTIVEERVNRPGWNEEDDISVSDDSELPTSTTLKASEKSTMEQLVEKACFRDYQRLGLGTISGNSSRSKPEYFRVTASNRLYSLCRSYPGLLVIPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGFHGKGVVGLFKSQNSPQAVSTSSLESSSSIEQEKYLQALLTAVIVHQKLRGSSTLTVRPALALSPVHGYRDKSFTQSNPKSSAKEPVHNQGVWASLRSSTRLISSPTSFIDVGARLAGKDHSASFSNSTYLQNQLLKRQAALYIFGEKSQLRSSKVEFAFNCEFVPVEFHEIRQVKASFKKLMRACIPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVWVCLEEGWDITTQVTSLAQLLSDPFYRTIAGFRTLVEKEWLSFGHKFSQRSSLALNSQGGGFAPIFLQFLDCVHQVHNQYPTEFEFNLYYLKFLAFHYVSNRFKTFLLDSDYERLEHGTLFDDKGDKHAKKGVCIWECIDKMHTRSPIFFNYLYSPVEVEALKPNVNVSSLKKWDYYTEETLSAGPSYDWMMLTPKHFPYEESDVAGGAGPQSQRKTVWPCYDDVTCSQPDALTRLFSEIEKLEHKLNQTPERWHQLWEKVTTDLKEEPRTAHSLRHSAGSPGIASTNVPSYQKRPALHPLHRGLGEDQSTTTAPSNGVEHRAATLYSQYTSKNDENRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKYTSDKAFFDLKTSKRVYNFCAQDGQSAQQWMDRIQSCISDA 1872 E9Q9A9 2'-5'-oligoadenylate synthase 2 Oas2 10090 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. UNIPROT E9Q9A9 UNIPROT Q8K4E5 UNIPROT Q8VI92 Pfam PF01909 Pfam PF10421 PROSITE PS00832 PROSITE PS00833 PROSITE PS50152 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}. GO:0005737 GO:0005829 GO:0016020 GO:0005654 GO:0005634 GO:0048471 GO:0001730 GO:0005524 GO:0003725 GO:0046872 GO:0051607 GO:0045071 GO:1903487 GO:0060700 GO:0009617 GO:0009615 GO:0006401 GO:0060337 MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK 742 E9QAT4 Protein transport protein Sec16A Sec16a 10090 Yes SL-0198 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}. UNIPROT E9QAT4 UNIPROT A2AIX1 UNIPROT Q80U43 UNIPROT Q811L5 Pfam PF12932 Pfam PF12931 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}. Q61584 EBI-8350418,EBI-647676 Q5S006 EBI-647676,EBI-2693710 Q5S007 EBI-5323863,EBI-647676 P39428 EBI-647676,EBI-520123 GO:0005829 GO:0005783 GO:0070971 GO:0005789 GO:0012507 GO:0005794 GO:0000139 GO:0031090 GO:0048471 GO:0048208 GO:0007029 GO:0006888 GO:0007030 GO:0043000 GO:0070863 GO:0032527 GO:0070973 GO:0072659 GO:0050821 GO:0034976 MQPPPQAVPSGVAGPPPAGNPRSMFWANSPYRKPANNAPVAPITRPLQPVTDPFAFNRQTLQNTPVGSSSKSSLPNLPGPALSVFSQWPGLPVTPTNAGDSSTGLHEPLSGTLSQPRADASLFPPASTPSSLPGLEVSRNAEADPSSGHEVQMLPHSAHYIPGVGPEQPLGGQMNDSGSGPDQPMNRHAPHDGAVTHAASPFLPQPQMPGQWGPAQGGPQPSYQHHSPYLEGPVQNMGLQAASLPHFPPPSSLHQGPGHESHAPQTFTPASLASGEGNEIVHQQSKNHPLSSFPPKHTFEQNSRIGNMWASPELKQNPGVNKEHLLDPAHVNPFTQGNSPENQAHHPPVAATNHALQEAASGALSMFFQGEETENEENLSSEKAGLDKRLNLDSFSSTSRLGHPPPPGASGVYQAFPRGPSSEAAQEGDAQPYFSQSVGVRLDKQSTVPPANDAWGDVPGTGTRCASGPQCENVENLEFVQNQEVLPRETLSVDPFPLSDQIRYGPLPGPAASRPATVGLTRGGGLNLEAPDTPLHPTRPDSVSSSYSSHSHRSPPGSARPQELVGTFIQQEVGKLEDDTSGSFFKQIDSSPVGGETDEVTGSQNCCSSLSQPSTPSPPKPTGVFQTSANSSFEPVKSHLVGVKPVEADRANMVVEVRGTQYCPKKRRAAVAPPDATSGNLEQPPDNMETPCAPQACPLPLSTTGEAGQLVSNTAGTPLDTVRPVPDKRPSARAQGPVKCESPATTLWAQNELPDFGGNVLLAPAAPALYVPVKPKPSEVVHHPEKGMSGQKAWKQGSVPPLQNQDPPGASENLENPPKVGEEEALPVQASSGYASLLSSPPTESLHNQPVLIAQPDQSYNLAQPINFSVSLLNPNEKNQSWGDAVVGERSIVSNNWALGGDPEERAALSGVPASAVTGASLPSSIPQNCAPQGSGSSEMIASQSASWLVQQLSPQTPQSPHPNAEKGPSEFVSSPAGNTSVMLVPPASSTLVPNSNKAKHSSNQEEAVGALDFTLNRTLENPVRMYSPSPSDGPASQQPLPNHPRQSGPGLHNQDHFYQQVTKDAQDQHRLERAQPELVPPRPQNSPQVPQASCPEPSNPESPPTQGQSESLAQPPASPASVNTGQLLPQPPQASSASVTSTNSSQAAVRSEQLWLHPPPPNTFGPAPQDLASYYYYRPLYDAYQSQYPSPYPSDPGTASLYYQDMYGLYEPRYRPYDSSASAYAENHRYSEPERPSSRASHYSDQLAPRQGYPEGYYNSKSGWSSHSDYYANYYSGQYDYGDPSRWDRYYGSRLRDPRTWDRRYWYDSEHDPYRKDHYAYSDRPEKCDDHWRYDPRFTGSFDDDAEIHRDPYGEEADRRSIHSEHSARSLRSTHSLPSRRSSLSSHSHQSQIYRSHHVTGGSFEAPHAPGSFHGDYAYGTYASNFSGAHGFPEYSYPADTSWPAVEQVPSRPTSPEKFTVPHVCARFGPGGQLLKVIPNLPSEGQPALVEIHSLETLLQHTPEQEEMRSFPGPLGKDDTHKVDVINFAQNKATKCLQNESLIDKESASLLWKFIILLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNEAVEQVEEEESGEAQLSFLTDSQTVTTSVLEKETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRFANSLPINDPLQTVYQLMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASKGLLDAAHFCYLMAQVGFGVYTKKTTKLVLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAHTCSLPNFQVFKFIYLCRLAEMGLATQAFHYCEVIAKSVLTQPGAYSPVLISQLTQMASQLRLFDPQLKEKPEEESFVEPAWLVQLQHVERQIQEGTVLWSQDGTEPQQCRITSGSEVEQSDGPGLNQQAGPQADNPLLMPSTEPLMHGVQLLPTAPQTLPDGQPAHLSRVPMFPVPMSRGPLELSPAYGPPGSALGFPESSRSDPAVLHPGQALPPTTLSLQESGLPPQEAKSPDPEMVPRGSPVRHSPPELSQEEFGESFADPGSSRTAQDLETSPVWDLGSSSLTRAPSLTSDSEGKKPAQAVKKEPKEPKKTESWFSRWLPGKKRTEAYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSFPRVPQVAPTGPAGPPTASVNVFSRKAGGSRARYVDVLNPSGTQRSEPALAPADFFAPLAPLPIPSNLFVPNPDAEEPQPADGTGCRGQAPAGTQSKAESTLEPKVGSSTVSAPGPELLPSKPDGSQGGEAPGDHCPTGAPHGGSVPFYNPAQLVQASVTSGNSRPGRIGQRKYAALN 2357 F0JAI6 Kinetochore and Eb1-associated basic protein Kebab 7227 Yes SL-0198 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}. UNIPROT F0JAI6 UNIPROT Q961C7 UNIPROT Q9VQ69 DE Reference Proteome: Yes; Q7JN06 EBI-134484,EBI-126566 GO:0000777 GO:0048471 GO:0005876 GO:0043515 GO:0008017 MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERSLYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKENQELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKGIKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQLQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKIEKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCIEAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP 548 F1M391 Stimulator of interferon genes protein Sting1 10116 Yes SL-0198 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}. UNIPROT F1M391 PDB 5GRM PDB 5GS5 Pfam PF15009 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}. GO:0005776 GO:0000421 GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0005768 GO:0005794 GO:0030176 GO:1990701 GO:0005741 GO:0005654 GO:0048471 GO:0005777 GO:0005886 GO:0035438 GO:0061507 GO:0042802 GO:0042803 GO:0019901 GO:0008134 GO:0031625 GO:0002218 GO:0000045 GO:0071360 GO:0035458 GO:0071407 GO:0051607 GO:0045087 GO:0032608 GO:0002230 GO:0051091 GO:0016239 GO:0032092 GO:0045944 GO:0032481 GO:0051259 GO:0031323 GO:0010468 GO:0050727 GO:0061709 MPYSNLHPSIPRPRSYRFKLAAFVLLVGSLMSLWMTGEPPSHTLHYLALHVASQQLGLLLKKLCCLAEELCHVQSRYQGSYWKAVRACVGSPICFMALILLSFYFYCSLENTSDLRLAWHLGILVLSKSLSMTLDLQSLAPAEVSAVCEEKNFNVAHGLAWSYYIGYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLEEILADVPESRNHCRLIVYQESEEGNSFSLSQEVLRHIRQEEKEEVTMSGPPTSVAPRPSLLSQEPRLLISGMEQPLPLRTDLI 379 F1MAD2 InaD-like protein Patj 10116 Yes SL-0198 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}. UNIPROT F1MAD2 PDB 3UIT Pfam PF09045 Pfam PF00595 PROSITE PS51022 PROSITE PS50106 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}. GO:0045177 GO:0016324 GO:0005923 GO:0048471 GO:0032991 MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRKGLLVFTDGSITNGNAHRPCSSITASESLPWTQRSGNEDFTSVIQQMAQGRHIEYIDIERPSTGGLGFSVVALRSQSLGLIDIFVKEVHPGSVADRDQRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQSRTSTSSADTTLPETVRWGHTEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGSTNVQGMTSEQVAQVLRNCGNSVRMLVARDPVGEIAVTPPTPASLPVALPVVATRTLGSDSSPFETYNVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSIIPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEQPSSREAVAEPPEVPELTGSLKPETNSRMEAEEIGERLDNLRKDTVQALEKPDVYPEDIPGCPENELKSRWENLLGPDYEVMVATLDTQIADDEELQKYSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRTVEPSLLEAEVDRSVDVSTEDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPMRSVIVIRSLVADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEEEKEEKEEHFIFHSNNNGDNSESPETVHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDMDSSSEAWEMHEFLSPRLERRGEEREMLVDEEYEIYQDRLRDMEAHPPPPHIREPTSASPRLDLQAGPQWLHADLSGGEILECHDTESMMTAYPQEMQDYSFSTTDMMKETFGLDSRPPMPSSEGNGQHGRFDDLEHLHSLVSHGLDLGMMTPSDLQGPGVLVDLPAVTQRREQEELPLYRLPSARVVTKPSSHVGMVSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTKALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPSVNNKGKTPPQNQDQNTQEKKAKRHGTAPPPMKLPPPYRAPSADTEESEEDSALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPDGPAAADGRMRVGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVNQMAVAPFPVPSHSPSPVEDLGGTEPVSSEEDSSVDAKPLPERESSKPEDLTQAVDDSMVAEQEKASESPDSAARQMKQPGYSAQVSSSSQEIPSAPAPLCQSTHADVTGSGNFQAPLSVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGVDLRSSSHEEAITALRQTPQKVRLVIYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIVKGGAADLDGRLIRGDQILSVNGEDVRQASQETVATILKCVQGLVQLEIGRLRAGSWASSRKTSQNSQGDQHSAHSSCRPSFAPVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGVSIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGDRIVSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEMMSAGSQLGSPTADRHPQDPEELLQRTAD 1836 F1N3B8 2'-5'-oligoadenylate synthase 2 OAS2 9913 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. UNIPROT F1N3B8 UNIPROT Q53AV7 Pfam PF01909 Pfam PF10421 PROSITE PS00833 PROSITE PS50152 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}. GO:0005829 GO:0016020 GO:0005654 GO:0005634 GO:0048471 GO:0001730 GO:0005524 GO:0003725 GO:0046872 GO:0051607 GO:0045071 GO:1903487 GO:0060700 GO:0009617 GO:0009615 GO:0006401 GO:0060337 MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVFFGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLWSYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCGAEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNWLRSLRQNESPGPSWNVLPASLYITPGHLLDKFVKDFLQPNQTFQDQIKKALKIICSFLEENCFRHSTTKIQVIQGGSTVKGTALKTGSDASLVVFANSLKSYTSPKNERYNIIKEIHEQLEACRQEKDFEVKFEISKWKPPWVLSFTLKSKVLNESVDFDVLPAFNALGELKSGSTPSPRTYTELIHLYKPSDVFLEGEFSACFTKLQRNFVRSLPLKLKDLIRLLKHWYCGCEKKLKQKGSLPPKYALELLSIYAWEKGSGAQDFDMAEGFRTVLELVIQYQHLCVFWTVNYSFDDEILRNFLLGQIRRTRPVILDPADPTGDVGGGHRWCWHLLAKEATEWLSSLCFKDKSGCPIQPWNVPKKRVQTPGSCGAGIYSMVNEMHLLRSHRFLD 714 F1N4E5 Torsin-1A-interacting protein 1 TOR1AIP1 9913 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT F1N4E5 Pfam PF05609 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}. GO:0016021 GO:0005637 GO:0005634 GO:0001671 GO:0032781 GO:0034504 MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSEEDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVRSGDSVESGDQTTRSSSQYKESFWQSSQSGDFTAFDEQPLKLSSGYQKTPQEWAEKTVRIRTRMLTSSPGMRSIYGSFSDDDSVQKSELGNQSPSTSNQQMTGQPKSVSSVKTKRYWPFAVIAALLIGGFLYTRPPEAETTAVQEFQNQMKQLMNKYQGQDEKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNSDTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL 600 F1P963 7,8-dihydro-8-oxoguanine triphosphatase NUDT1 9615 Yes SL-0178 SL-0182 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}. UNIPROT F1P963 PDB 5MZF Pfam PF00293 PROSITE PS51462 PROSITE PS00893 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}. GO:0001669 GO:0005829 GO:0005759 GO:0031965 GO:0035539 GO:0008413 GO:0047693 GO:0036219 GO:0003924 GO:0046872 GO:0030515 GO:0046061 GO:0006203 GO:0042262 GO:0006281 MGTSRLYTLVLVLQPERVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELREESGLTVDTLHKVGQIMFEFVGEPELMDVHIFCTDSVQGTPVESDEMRPQWFQLDQIPFTDMWPDDSYWFPLLLQKKKFHGYFRFQGPNTILDYTLREVDKL 156 F1QNV4 Nuclear pore complex protein Nup133 nup133 7955 Yes SL-0178 SL-0185 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}. UNIPROT F1QNV4 UNIPROT Q7SZE9 Pfam PF03177 Pfam PF08801 Involved in poly(A)+ RNA transport (By similarity). Involved in nephrogenesis (PubMed:30427554). {ECO:0000250|UniProtKB:Q8WUM0, ECO:0000269|PubMed:30427554}. GO:0000777 GO:0016020 GO:0031080 GO:0017056 GO:0051028 GO:0031081 GO:0006606 GO:0006355 GO:0006405 GO:0000972 MFSPRGTPGSGRRQAPRTGGRRSVSAVQPGLLFSPRRSAVTARSTPTRVQSHAVVESYNFDVQTFGSSLPVKVMEALTMADVDDQISVKVEASGWAWMVCGERLIVWKVSQTSVAKLSVCKDLQLPSSEFAYSADLVSISSSGPLDLAPIQSISVLAVSPDGLVRFWPSLAHEGSYTEISLDLSGHLSNYVAAVKGGSFIVSSYRGHLLRLSADSSGKLHHRPVQQGQGMLSGIGRRVSSLFGIRGQPADLSVFSVLWVKASSCLYSLSSCGLSKWEVDENSETQVLSWSTNQIITDSITDAIWDSESNYSEIKKGVNVLYLDMQPSNAGLVVLAAAWYPGDTPCVAYFCLVTLAESIVPSPDLLTVEVTKYNPPFQSEEELLKTRLVLPDPSSPAAYLYNEELVFACSTGAGRGGLAEEKILFSSPGDRVRGGGVCADLPVFFSQNSGLVAVLARETASLLPETMEDSLCTSVAGPGPEGTPLETPPKIDMVAQEDKTKLLKQAFLQFCRHDLVGAQSMVDELFPSDGEGSADLDTVVTQIDLDLVDDYPACDPRWAESVPDEGAGFTLTSLILLHQLEDKMKAHRCLMDFLLQTGLLDRLTSTKVRSCPMATRLLLCEHAEKLSAAIVLKNHHAKHPELVNTAIQTALKKNSTDTPTNLTPADVFFREVSQISSIFECLLDEEEKALKEHPDAARWGEVVLSVNDIIKDMLQAAAQYRETKASLYRAPENCSPEPEYIPWTASGGVGGVRSVISRQHELILRAAYPHADAELRSVLCEQLVALLDSLLSGYVAQLTSLRRGGQQERYDTLENEYTQKRSELLKPLLELGQHQWVAALAEKYCDFDILVQLCERTDNQSRLQQYMVKFADQNFADFLFRWYMEKGKRGKLLSQPMATHQQLASFLQAHDHLSWLHDIHVQDYQRAHRTLYNQANMETRYFSKKKTLLALSKLTALASDMPEPVHRRQLNDIVEQERFLLHQETLPKQLLEEKQLNPDSMPLLSPQNLISLYICDENRGANEYDFKKALDLLEYFEEENGIDVDALKREIFSKALKKDWKESWSSSDDNDDPLEAARDSTFVKILQKLIQERVSLQTYLPDIKDLLQEDELESLKSKPYFEFLLRANYEHYLKVQI 1136 F1R0H0 Solute carrier family 2, facilitated glucose transporter member 10 slc2a10 7955 Yes SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT F1R0H0 UNIPROT A8KB28 UNIPROT I1SV80 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:22116938}. GO:0012505 GO:0005887 GO:0048471 GO:0005351 GO:0072358 GO:0046323 GO:0030903 MGCSVLLLTITVSTLGGLVFGYELGIISGALPQLQTHFSLGCVQQEAVVSALLIGSLFASIIGGWLIDRHGRRTSILLSNLLILAGSVILTTGTSFFALVIGRAVIGFAMTVSSMSCCIFVSEMVTPERRGLMVTLYEVGITVGILIAYAVNYIFNNVPLTGWRYMFGFAIIPSLIQLASIVLLPKQAEVFVIHDDDSRQADRLTEETETSNQHQQSEKYGVSDLFKSKDNMRRRTVIGVGLVLSQQFTGQPNVLFYASTILFSVGFQSNASAILASVGFGIVKVIATLLAMLCSDRAGRRSLLIGGCSMLAVGLILTGFLCRQSVIDTTKRCTSVGPHSNLTLSAEHDEGVGFSSQTLDVHEHLRSFSQSEDIYKWIIFTCLMAVVSAFSVSFGPMTWVVLSEIFPKDIRGRAFSFINCFNVGANLIVSFSFLSIIDVIGLSGVFLMYGVVGIAGVVFIYLVLPETKGKSLQDIDRELSQTRMIHRQELCSIFQRRRFSPGYQRVQLTSTAT 513 F4HRT5 Protein CROWDED NUCLEI 1 CRWN1 3702 Yes SL-0178 SL-0180 SL-0182 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}. UNIPROT F4HRT5 UNIPROT Q0WKV7 UNIPROT Q8GZ88 UNIPROT Q9FYH0 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}. GO:0000789 GO:0005829 GO:0005739 GO:0005635 GO:0005652 GO:0031965 GO:0034399 GO:0005654 GO:0005634 GO:0006997 GO:0097298 MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEWSSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANALVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQEGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKARELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALDRKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTEEERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERLKKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLFEEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSRFLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKMLKLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVAADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRKRGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEEGIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKVSIGKKLWTFLTT 1132 F4HXV6 Nuclear pore complex protein NUP155 NUP155 3702 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4HXV6 UNIPROT Q9LQU6 Pfam PF08801 Major component of the nuclear pore complex (NPC). {ECO:0000305|PubMed:12034489}. GO:0005643 GO:0044611 GO:0005730 GO:0005886 GO:0009506 GO:0017056 GO:0051028 GO:0006913 GO:0006606 GO:0036228 GO:0006405 GO:0000972 MSQDDEIVMRDVTSAGICIGDRIGREAASQLDLEEALEASRYASHPYSTHPREWPPLIEVGETWELPSVLIERYNTAGGEGTALCGIFPEIRRAWASVDNSLFLWRFDKRDGQCPEYSGEEQAICAVGLAKCRPGVFVEAIQYLLVLATPVELVLVGVCCTEGPDGRDPYAEISVQPLPDYTISSDGVTMTCVTCTNKGRIFMAGRDGHIYELLYTTGSGWNKRCRKVCLTAGVGSMISRWVVPNVFKFGAVDPVVEMVVDNERQILYARTEEMKLQAYVSGPNGEGPLKKVAEERNLLNQKDLSQGNRQSAVAGRSNKPSIVSISPLSMLESKWLHLVAALSDGRRMYLSTSSSGSGSTISFSGFNNHRQTPNCLKVVSTRPSPPLGVGVGLGFGAASVAGRTQNDDLSMKIETAYYSVGTLVLSDSSPPAMSSLLVVSRDSSVHSQAGSSSGPSSRSSRALREVVSSLPIEGRMLFVADVLPSPDTAATIQSLYSELEYCGVEVSGESYEKACGKLWARSDLSTQHILPRRKIVVFTTMGMMELVFNRPVDILRRLLESNSPRSLLEDFFTRFGVGEAAAMCLMLAARIINFEDLISNIVADKAAEAFEDPRIVGMPQFDGSSGLSNTRTATGGFSMGQVVQEAEPIFSGAHEGLCLCTSRLLFPLWELPVMSKKTSSDTMSEDGVVICRLSTSAMHVLESKIRSLEKFLRSRRNQRRGLYGCVAGLGDVTGSILYGTGSELGATERNMVRNLFGAYSNGGESANKRQRLPYSPAELAATEVRAMECIRQLLLRSAEALFLLQLLSQHHVARLVQELDANLKQALVQLTFHQLVCSEEGDQIATRLISAVMEYYTGSDGRGTVDDISPRLREGCPSYFKESDYKFYLAVERLERAALTSDAEEKENVAREAFSFLSKVPGSADLQTVCKRFEDLRFYEAVVCLPLQKAQALDPAGDAFNDQLDASIREHALAQRKQCYEIIANALRSLASPLASPTLDEASRSQYICQIVHLGVQSTDRAFREYLYKAMIELHLENELLEYGGPDLVPFLQNAGSHSESQVGAVSTGSSPLGHSGTQISSDQAKYFDLLAKYYVSKRQHVLAAHVFLRLAERRAISLGDSPTLERRRDDLSQAVLQAKNASNSDGLVGSAQGVSDSGLLDLLEGKLAVLQFQIKIRDKLEAIASNFESSVAMQDSDQNGQVLDGDSSDDTNLANAANEMAMEVSSELKSVTQLYNEYAVPFELWEICLEMLYFANYSGDADSSIIRETWARLIDQALSQGGIREACAVLKRVGSHIYPGDGVVLPLDVLCLHLERAALERSERIENVRDEDIAKALLAACKGAAEPVLNAYDRLLSNAAVVPSPNLRIRLLRSVLVVLREWAMSVLSDRMGSSPTRSSLILGGSFALENKAALNQGARDKIANAANRYMTEVRRLALPPNKTDGVYAGFKELDESLLSPFSF 1464 F4HXY7 CDP-diacylglycerol--serine O-phosphatidyltransferase 1 PSS1 3702 Yes SL-0178 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. UNIPROT F4HXY7 UNIPROT Q9XI59 Pfam PF03034 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}. GO:0005789 GO:0016021 GO:0031965 GO:0003882 GO:0009556 GO:0006646 GO:0006659 MEPNGYRKERRKEQHLGRMNGGGGDVETDLDPWTAWAYKPRTISLLLIGACFLIWASGALDPDSTTSDDLVTSVKRGVWAMIAVFLAYSLLQAPSTVLIRPHPAIWRLVHGMAVIYLVALTFLLFQRRDDARQFMKFLHPDLGIELPEKSYGADCRIYVPDHPTNRFKNLYDTVFDEFFLAHIFGWWGKAILIRNQPLLWVLSIGFELLEVTFRHMLPNFNECWWDSIVLDILICNWFGIWAGMYTVRYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAHWDKDEWHPLQGPWRFIQVLTLCIIFLTVELNTFFLKFSLWIPPRNPVILYRLILWWLIAIPTTREYNSYLQDRKPVKKVGAFCWLSLGICIVELLICIKFGSGLYPTEMPLWVVTLWGSVGLGLVAFLLSWTWKIQKILAQKRR 425 F4HYD7 Ran-binding protein M homolog RANBPM 3702 Yes SL-0198 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}. UNIPROT F4HYD7 UNIPROT Q8VYQ8 UNIPROT Q9C8P9 Pfam PF10607 Pfam PF00622 PROSITE PS50188 PROSITE PS50897 PROSITE PS50896 DE Reference Proteome: Yes; GO:0005737 GO:0005634 GO:0048471 MNSSPPPANSANGDTTNNGENGQDLNLNFLDKIRLSAKRDAKEDEGEELPTELNTINSAGGFLVVSPDKLSVKYTNTNLHGHDVGVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKFTKDDAVGGGINYASQEFFFTKNGTIVGKIPKDIRGHLFPTVAVHSQNEEVLVNFGKKKFAFDIKGYEASERNKQQLAIEKISIPPNIGYGLVKTYLLHYGYEETLDAFNLATKNTVPPIHIDQENAIDEDDSSYALKQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVVCFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGLTGFQDIVEDCFALLAYEKPEESSVWYFLEDSQRELVADAVNAAILSTNPNKKDVQRSCHLQSHLEKLLRQLTVCCLERRSLNGDQGETFRLRHVLNNNR 467 F4I1T7 Nuclear pore complex protein NUP214 NUP214 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4I1T7 UNIPROT F4I1T6 UNIPROT Q94C88 UNIPROT Q9ZVV0 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}. GO:0005739 GO:0044613 GO:0044615 GO:0008139 GO:0017056 GO:0009793 GO:0051028 GO:0006606 GO:0006405 GO:0010070 MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNSNGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKHSYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVDSIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLAVTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPYFVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQRLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKLQKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTGYVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGPLRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDKTIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARRGVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNASSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSERLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSNTTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFESSKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIPISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSLFPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQSTVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASSPTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSGELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGGSNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGFGGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK 1819 F4I316 SUN domain-containing protein 3 SUN3 3702 Yes SL-0178 SL-0182 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}. UNIPROT F4I316 UNIPROT O23133 UNIPROT Q8GX04 UNIPROT Q8H7G6 Pfam PF07738 PROSITE PS51469 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]. GO:0005737 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0005635 GO:0031965 GO:0005886 GO:0043621 GO:0042742 GO:0009409 GO:0009651 GO:0009414 MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPLSLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINNTGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNSRNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTIKIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGVDAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSEPVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQEGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTGSGAWLLLLISSTFIMFVLSL 660 F4I3V6 Protein SHORT HYPOCOTYL IN WHITE LIGHT 1 SHW1 3702 Yes SL-0178 SL-0182 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}. UNIPROT F4I3V6 UNIPROT Q0WTQ6 UNIPROT Q8LGA9 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}. GO:0016021 GO:0031965 GO:0005634 GO:0009738 GO:0009908 GO:0010100 GO:0009958 GO:1901333 GO:0048578 GO:0009787 GO:0031540 GO:0010380 GO:0090227 GO:0009642 GO:0009416 MAAATTTLSSSSSSPSLTLINASHRFVSVTPFSSNSIFLRRRFRRLNRSLASSSSHSRRRYESDDRFFGGGDNYDVVPDDDGFSDDDDEEDERESSVDLLIRFLRSMFKKVSKRTKKASRRILPAAMSPRLVSFAVDGILLLGSLSITRAFLEVICNLGGTVFTVILLIRLFWAAASFFQTYGNSFGPNPVN 192 F4ICX9 TSK-associating protein 1 TSA1 3702 Yes SL-0178 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}. UNIPROT F4ICX9 UNIPROT F4ICY0 UNIPROT Q94AE1 UNIPROT Q9C831 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}. GO:0009535 GO:0005788 GO:0005635 GO:0005777 GO:0099503 GO:0005773 GO:0005509 GO:0050832 GO:0009640 MEIYTMKTNFLVLALSLCILLSSFHEVSCQDDGSGLSNLDLIERDYQDSVNALQGKDDEDQSAKIQSENQNNTTVTDKNTISLSLSDESEVGSVSDESVGRSSLLDQIKLEFEAHHNSINQAGSDGVKAESKDDDEELSAHRQKMLEEIEHEFEAASDSLKQLKTDDVNEGNDEEHSAKRQSLLEEIEREFEAATKELEQLKVNDFTGDKDDEEHSAKRKSMLEAIEREFEAAMEGIEALKVSDSTGSGDDEEQSAKRLSMLEEIEREFEAASKGLEQLRASDSTADNNEEEHAAKGQSLLEEIEREFEAATESLKQLQVDDSTEDKEHFTAAKRQSLLEEIEREFEAATKDLKQLNDFTEGSADDEQSAKRNKMLEDIEREFEAATIGLEQLKANDFSEGNNNEEQSAKRKSMLEEIEREFEAAIGGLKQIKVDDSRNLEEESAKRKIILEEMEREFEEAHSGINAKADKEESAKKQSGSAIPEVLGLGQSGGCSCSKQDEDSSIVIPTKYSIEDILSEESAVQGTETSSLTASLTQLVENHRKEKESLLGHRVLTSPSIASSTSESSATSETVETLRAKLNELRGLTARELVTRKDFGQILITAASFEELSSAPISYISRLAKYRNVIKEGLEASERVHIAQVRAKMLKEVATEKQTAVDTHFATAKKLAQEGDALFVKIFAIKKLLAKLEAEKESVDGKFKETVKELSHLLADASEAYEEYHGAVRKAKDEQAAEEFAKEATQSAEIIWVKFLSSL 759 F4ID16 Nuclear pore complex protein NUP98B NUP98B 3702 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4ID16 UNIPROT Q9LQ50 Pfam PF04096 PROSITE PS51434 DE Reference Proteome: Yes; GO:0005635 GO:0044614 GO:0008139 GO:0003723 GO:0017056 GO:0071456 GO:0051028 GO:0000973 GO:0006606 GO:0006405 GO:0034398 MFGSSNNNPFGQSSISSPFGTQTHSLFGQTNNNASNNPFATKPFGTSTPFGAQTGSSMFGGTSTGVFGAPQTSSPFGASPQAFGSSTQAFGASSTPSFGSSNSPFGGTSTFGQKSFGLSTPQSSPFGSTTQQSQPAFGNSTFGSSTPFGASTTPAFGASSTPAFGVSNTSGFGATNTPGFGATNTTGFGGSSTPGFGASSTPAFGSTNTPAFGASSTPLFGSSSSPAFGASPAPAFGSSGNAFGNNTFSSGGAFGSSSTPTFGASNTSAFGASSSPSFNFGSSPAFGQSTSAFGSSSFGSTQSSLGSTPSPFGAQGAQASTSTFGGQSTIGGQQGGSRVIPYAPTTDTASGTESKSERLQSISAMPAHKGKNMEELRWEDYQRGDKGGQRSTGQSPEGAGFGVTNSQPSIFSTSPAFSQTPVNPTNPFSQTTPTSNTNFSPSFSQPTTPSFGQPTTPSFRSTVSNTTSVFGSSSSLTTNTSQPLGSSIFGSTPAHGSTPGFSIGGFNNSQSSPLFGSNPSFAQNTTPAFSQTSPLFGQNTTPALGQSSSVFGQNTNPALVQSNTFSTPSTGFGNTFSSSSSLTTSISPFGQITPAVTPFQSAQPTQPLGAFGFNNFGQTQIANTTDIAGAMGTFSQGNFKQQPALGNSAVMQPTPVTNPFGTLPALPQISIAQGGNSPSIQYGISSMPVVDKPAPVRVSPLLTSRHLLQRRVRLPTRKYRPSDDGPKVPFFSDEEENSSTPKADAFFIPRENPRALFIRPVERVKSEHPKDSPTPLQENGKRSNGVTNGANHETKDNGAIREAPPVKVNQKQNGTHENHGGDKNGSHSSPSGADIESLMPKLHHSEYFTEPRIQELAAKERVEQGYCKRVKDFVVGRHGYGSIKFLGETDVCRLDLEMVVQFKNREVNVYMDESKKPPVGQGLNKPAVVTLLNIKCMDKKTGTQVMEGERLDKYKEMLKRKAGEQGAQFVSYDPVNGEWTFKVEHFSSYKLGDEYDV 997 F4IGA5 Nuclear pore complex protein NUP133 NUP133 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000305|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4IGA5 UNIPROT F4IGA4 UNIPROT Q9SJ43 Pfam PF03177 Pfam PF08801 DE Reference Proteome: Yes; GO:0016020 GO:0031080 GO:0017056 GO:0051028 GO:0031081 GO:0006606 GO:0006355 GO:0006405 GO:0000972 MFSPLTKRAKQSSRNEKTPRNRVPPPDSPVTPATQNRNNFISDRPATGTPAPWAPRLSVLARVSPGNNGDKGVDSDQLKPVFVGEFPQLLRDEQSYPGDACVSGGMDKETCLSWFITGSKVFVWSHLTTLPSRKCVVLELPVVVLVNEESGSGLQDGKSWLVNVVSWDTSAGAATRASRSRSPVGVVMCNRKTRAVVYWSDIFSGQEAAPAEKARHLIKRQSNGIRSSRAENSDLNSLITTAVAAAERLCIAIACSSNGELWQFTCSPTGVKSNQVQLNISSSSVSEGYPRSLIWRFSQGLARESCWEFLMLTDCDIHCFTIEPYPDLTVSEVWQHEIVGTDGDSGIKKDIASQKQIWPLDLQVDDQGKVITVLVATICMDRASSSSYTQYSLLTLQHKSEMRFADGREEKVLEKQGPIQVIIPKARVEDKDFLFSMRLRVGGRPPGSAIILSGDGTATVCYCHGSSTRLYKFDLPYDAGKVLDASVLSSTDEHEYGAWTVLTEKAGVWAIPEKAVVLGGVEPPERSLSRKNSSNERSTRDETRVTPYGVDRTAGRENSDIQNIEDKGNPKMGFTRQTARDEESEALLGQLFEGFLLSGKVDGSLEKLSQSGAFDRDGEANVFARKSKSIVDTLAKHWTTTRGAEIVAMTVISSQLVEKQQKHENFLHFLALSKCHEELCSKQRHSLQIILENGEKLAAMIQLRELQNMINQNRSARFGSPQAGSEDQVSCALWDLIQFVGERARRNTVLLMDRDNAEVFYSKVSELEEVFYCLNRQLEYIIRADQPLGTQLQRACELSNACVTILQTALDYKNEHQMWYPPLEGLIPWHSQTVVCNGLWCIASFMLHLLTEASRIDISAKSDIYTHLEVLTEVLLEACAGSTFAKLEREEENKGLLNEYWTRRDTIFDSLYRQAKEFMEAEIQGIRERTEATDEDIFRNRCSNLISIAKRHAGYKIMWKICYDLNDTGLLRNLMHEGVGPQGGFSYFVFQQLYDMKQFSKLLRLGEEFQDELLIFLKRHSDLVWLHQVFLHQFSSASDTLHTLALSQDEESMTTVEERTGPEPEDVQPTFADRKRFLNLSKIAYVADKDADSESKVKRIEADLNLLKLQEEITKALPNGEARNRLFRPEELIETCLNIQGRWTAIKAFEVFAWTSSSFRENHRSLLEECWRNAADQDDWDRHHQASTNEGWSEEETLQNLRNTALFQASKRCYGPTRVNTFDGDFAQVLPLRRENPEDSTSSVEDVLMSHKDFAEAGKLMLTAIMLGCVEEEGIVAEEFSSPME 1285 F4IMH3 Protein NUCLEOLAR COMPLEX ASSOCIATED 4 NOC4 3702 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000269|PubMed:23382868}. UNIPROT F4IMH3 UNIPROT O22737 UNIPROT Q8VZE1 Pfam PF03914 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}. GO:0016021 GO:0030692 GO:0031965 GO:0005730 GO:0005654 GO:0032040 GO:0009793 GO:0006364 MASILSKKQKKNEKYTLKELKSLGHDLLTSRSHINNLPLLLTFVSPESPPQFVVESLLSLQSFFTPLLSQLPPTSSSPSSTKTEDPEVVFKAWLRSKFDEFVKLLLDVLVSQQSEDSLRGIVLGTLMEFVKLLNAGRFHSSIYHRLLDAIIHSEVDIEIFLDILTSKYFKYIDVRYFTYISMEKFVKTLEASVSADRTVIENNEAESDSKESLELSVRKIYQVLSQIPPPEKQAEKSQHEMWSGSDESISEKPTDKKKKTEKGDSTLLSPATISKRMKLKFTKAWISFLRLPLPIDVYKEVLASIHLTVIPHLSNPTMLCDFLTKSYDIGGVVSVMALSSLFILMTQHGLEYPFFYEKLYALLVPSVFVAKHRAKFLQLLDACLKSSMLPAYLAASFTKKLSRLSLSIPPAGSLVITALIYNLLRRNPTINHLVQEIVENADEANTEAGEHNESQPKTIKKRKLGIDYFNNQESDPKKSGALKSSLWEIDTLRHHYCPPVSRFISSLETNLTIRSKTTEMKIEDFCSGSYATIFGDEIRRRVKQVPLAFYKTVPTSLFADSDFPGWTFTIPQEEGTC 577 F4IUX6 Regulator of nonsense transcripts UPF2 UPF2 3702 Yes SL-0198 Nucleus, nucleolus {ECO:0000269|PubMed:19602621}. Cytoplasm {ECO:0000269|PubMed:19602621}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT F4IUX6 UNIPROT O80955 Pfam PF02854 Pfam PF04050 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}. GO:0005737 GO:0035145 GO:0005730 GO:0048471 GO:0005844 GO:0003729 GO:0042742 GO:0009867 GO:0048571 GO:0000184 GO:0009611 GO:0009863 MDHPEDESHSEKQDDEEALARLEEIKKSIEAKLTLRQNNLNPERPDSAYLRTLDSSIKRNTAVIKKLKQINEEQREGLMDDLRGVNLSKFVSEAVTAICEAKLKSSDIQAAVQICSLLHQRYKEFSASLTQGLLKVFFPGKSAEDLEADKNSKAMKKRSTLKLLLELYYVGVIEDSNIFINIIKDLTSVEQLKDRDTTQTNLTLLTSFARQGRIFLGLPISGQDEDFFKGLDVTADQKKSFKKAFNTYYDALADLLQSEHKLLLQMEKENAKLVNAKGELSEDSASSYEKLRKSYDHLYRNISSLAEALDMQPPVMPEDGTTRLTAGDEASPSGTVKDTSVPEPIWDDEDTKTFYECLPDLRAFVPAVLLGEAEPKSNEQSAKAKEKLSESSSEVVENQQTTEDTTEVSADSASMDDRSNAEQPKEKEEVEKEKAKDTKKEKGKEKDSEKKMEHEKEKGKSLDVANFERLLQRLPGCVSRDLIDQLTVEYCYLNSKTNRKKLVKALFNVPRTSLELLAYYSRMVATLASCMKDIPSMLVQMLEDEFNSLVHKKDQMNIETKIRNIRFIGELCKFKIVPAGLVFSCLKACLDEFTHHNIDVACNLLETCGRFLYRSPETTLRMTNMLDILMRLKNVKNLDPRQSTLVENAYYLCKPPERSARISKVRPPLHQYVRKLLFSDLDKDSIANVLKQLRKLPWSECEQYILKCFMKVHKGKYGQIHLIASLTSGLSRHHDEFVVAVVDEVLEEIRVGLELNEYGAQQKRLAHMRFLGELYNYEHVDSSVIFETLYLTLLYGHDTSEQEVLDPPEDFFRVRMVIILLETCGHYFDRGSSKKRLDQFLIHFQRYILSKGHLPLDIEFDLQDLFANLRPNMTRYSTIDEVNAAILQLEEREHASSGDKVSIERHSDTKPSNKSSSDVISSNGKSTAKDIRENGEAHGEESDSDSGSGSVVRDGQNEELDDGNHERGSESGDGDDYDDGDGPGSDDDKFRVRQKVVTVDLEEQADFDQELKALLQESMEQRKLELRGRPALNMTIPMSVFEGSGKDHHHFGRVVGENGEEVLDEENGEQREVQVKVLVKRGNKQQTRQMLIPSDCALVQSTKQKEAAELEEKQDIKRLVLEYNERDEEEANGLGTQILNWTSGGSRGSTRTGEGSGKSGGSRHRFYYHQGGGGSYHARRK 1181 F4IZR5 Protein EXPORTIN 1B XPO1B 3702 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT F4IZR5 UNIPROT Q0WV73 UNIPROT Q94IV0 UNIPROT Q94KD5 UNIPROT Q9M9N0 Pfam PF08767 Pfam PF18777 Pfam PF18784 Pfam PF18787 Pfam PF03810 Pfam PF08389 PROSITE PS50166 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005634 GO:0009506 GO:0005049 GO:0008536 GO:0009553 GO:0051028 GO:0009555 GO:0009846 GO:0009860 GO:0046825 GO:0000055 GO:0000056 MAAEKLRDLSQPIDVVLLDATVEAFYSTGSKEERASADNILRDLKANPDTWLQVVHILQNTSSTHTKFFALQVLEGVIKYRWNALPVEQRDGMKNYISDVIVQLSRDEASFRTERLYVNKLNIILVQIVKQEWPAKWKSFIPDLVIAAKTSETICENCMAILKLLSEEVFDFSKGEMTQQKIKELKQSLNSEFQLIHELCLYVLSASQRQELIRATLSALHAYLSWIPLGYIFESPLLEILLKFFPVPAYRNLTLQCLSEVASLNFGDFYDMQYVKMYSIFMNQLQAILPLNLNIPEAYSTGSSEEQAFIQNLALFFTSFFKLHIKILESAPENISLLLAGLGYLISISYVDDTEVFKVCLDYWNSLVLELFGTRHHACHPALTPSLFGLQMAFLPSTVDGVKSEVTERQKLYSDPMSKLRGLMISRTAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHEDTEKQMLSKLSKQLSGEEWAWNNLNTLCWAIGSISGSMVVEQENRFLVMVIRDLLSLCEVVKGKDNKAVIASNIMYVVGQYSRFLRAHWKFLKTVVHKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGESEPFVSELLSGLATIVGDLQPHQIHTFYESVGSMIQAESDPQKRGEYLQRLMALPNQKWAEIIGQARQSADILKEPDVIRTVLNILQTNTRVATSLGTFFLSQISLIFLDMLNVYRMYSELVSSSIANGGPYASRTSLVKLLRSVKREILKLIETFLDKAENQPHIGKQFVPPMMDQVLGDYARNVPDARESEVLSLFATIINKYKVVMRDEVPLIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFRALIQLSSEQLKLVMDSVIWAFRHTERNIAETGLNLLLEMLKNFQKSDFCNKFYQTYFLQIEQEVFAVLTDTFHKPGFKLHVLVLQHLFSLVESGSLAEPLWDAATVPHPYSNNVAFVLEYTTKLLSSSFPNMTTTEVTQFVNGLYESRNDVGRFKDNIRDFLIQSKEFSAQDNKDLYAEEAAAQMERERQRMLSIPGLIAPSEIQDDMADS 1076 F4JS25 Suppressor of RPS4-RLD 1 SRFR1 3702 Yes SL-0198 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}. UNIPROT F4JS25 UNIPROT Q8GYX1 UNIPROT Q9SZU6 Pfam PF13181 PROSITE PS50005 PROSITE PS50293 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}. Q9SUR9 EBI-1778186,EBI-4436454 Q9SUT5 EBI-1581364,EBI-4436454 Q9FPR2 EBI-4481446,EBI-4436454 GO:0005737 GO:0005783 GO:0016021 GO:0043231 GO:0005634 GO:0048471 GO:0042742 GO:0009816 GO:0031348 GO:0045892 MATATATSERFELAKHCSSRNWSKAIRVLDSLLAKESSILDICNRAFCYNQLELHKHVIKDCDKALLLEPFAIQAFILKGRALLALGRKQEAVLVLEQGYKSALQQTADVKQLLELEELLKDARREIDGILKSHATESPQETPAYHSEKSDEKSDKLDNHESGASSNGNSHESSSELGEQSKIVSFSKVASKASKQSDGNSDLCNGSVYKEKENGKCGSQINGYYESCKPCNGSDLHDNLAESSDRFGELSINGNKISIKSSKMSHKAEARCGISDESRKNKKYTIARISGTHSISVDFRLSRGIAQVNEGNYTKAISIFDKVLKEEPTYPEALIGRGTAYAFQRELESAIADFTKAIQSNPAASEAWKRRGQARAALGEYVEAVEDLTKALVFEPNSPDVLHERGIVNFKSKDFTAAVKDLSICLKQEKDNKSAYTYLGLAFASLGEYKKAEEAHLKSIQLDSNYLEAWLHLAQFYQELADHCKALECIEQVLQVDNRVWKAYHLRGLVFHGLGEHRKAIQELSIGLSIENTIECLYLRGSCYHAVGEYRDAVKDYDATVDVELDAVEKFVLQCLAFYQKELALYTASKVSSEFLCFDIDGDIDPMFKEYWCKRLHPKNVCEKVYRQPPLRESLKKGKLKKQDLAITKQKANILRFADLIGKRIQYDCPGFLPNKRQHRMAGLAVIEIAQKVSKAWRIEWRNSTKGTTKNGKKNRRRERTNILSQNRGGAGCSSSSFSETSTGYASLEDRSSGRSILSWQDVYSPAVRWRQISEPCDPVVWVNKLSEEFNSGFGSHTPMVLGQAKVVRYFPNYERTLTLAKSIIKDKLSVRSKKDKVIDLSKDEKIEKIMRAETCDELHNIVGEDFWVATWCDSTGSEGKRLEGTRITCIQKPGRLGYDFSIRTPCTPARWSDFDEEMTSAWEALCTAYCGENYGSTELDALETVRDAILRMTYYWYNFMPLARGTAVTGFVVLLGLLLAANMEFTETIPKGLQIDWEAILNVEPGSFVDSVKSWLYPSLKINTSWRDHTEISSAFSTTGAVVAALSTYND 1052 F4KBW6 Nuclear pore complex protein NUP205 NUP205 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4KBW6 UNIPROT Q9LU53 Pfam PF11894 DE Reference Proteome: Yes; GO:0005635 GO:0044611 GO:0017056 GO:0051028 GO:0006999 GO:0015031 MVSPKDLVAIVHSSLLGTSRPTPTQRIELTHAIRNSFPSLQNLLSFPPPKPSDRAQVQSKEIRLPDSLPISLDDQDIAISLKLSDELHLNEIDSVRLLVSSNQEWGLMGRDPLEIQRLATGLWYTGRRDLTSTLYTLLRAVVLDEGLEPDLIADIQGLLEELIEAGLRQRLITLIKELNREDPTGLGGPLCERYLIDSRGALVERRAVVQRERLILGHCLVLSILVDRPGSKDVKDIYYILKDNAAQLTEGNDTISSQITFSLLFSLIITFVSDAISRLSDKSSMISQDASFRTDFQDIVMASGSDPTADGFIGGIRLAWAVHLMLIHDGISGMDTISTASTTDMGHICSCLESIFSKNVFQFLLDNVLRTAAYQNDEEDIIYIYNAYLHKLASCFLSHPIARDKVKESKDMAMSVLNSYRTSDPLDGSMQTEESDRPLPFISLMEFKEPELLSGNDVLWTFVNFAGEDHTNFKTLVAFLEMLCTLASTQEGASKVYELLRGTSFRSIGWPTLFDCIRIYDEKFKQSLQTAGAMMPEFLEGDAKALVAYLNVLQKVVENGNPTERKNWFPDIEPFFKLLGYENIPPYLKGALRKTIAAFVNVFPEMRDSIWAFLEQYDLPVVVGSQVGKSDQSSQVYDMQFELNEVEARREQYPSTISFLNLINALIAGEKDVNDRGRRAYSDPCEKWQLVVACLQHFHMILSMYDIQEEDLDGFTEHPHFLVSLETSSLQTQLPIIELLKDFMSGKALYRNLMGILQVGVNSIISERLSKTYGKILEKAVQLSLEILLLVFEKDLLVSDVWRPLYQPLDIILSQDHNQIIALLEYVRYDSLPQIQRSSIKIMNILRCSRLVGLVPMLIKIDAANSLIEDYAACLEGRLEEGEVVENSCDDLGVLIMQLLVDNINRPAPSITHLLLKFDLDAPVEGTVLQPKFHYSCLKVILEMLEKLPNPDINFLLFEFGFQLLCELNLDPLTSGPTMDLLSSKKYQFFLQHLDTIGVATLPKRSGSQALRISSLHQRAWLLKLLAIALHTGSGSSSAHLEACQSILSHLFGREVTEAANEPFSSSTYPQDGLDYAGTSSISKSKALALLEILQFRSPDASMQLPQIVSSLKYDSLVEDILGNRDTSVSGSIYYYSERGDRLIDLSSFSNKLWQKLHSGFPLVDSFPNVAELSEVRETIQQLLKWGWKYNRNLEEQAAQLHMLAGWSQIVEVSACRRISSLDNRSEILYRILDASLSASASPDCSLKMAFVLTQVALTCIAKLRDDRFSFQGALSSDTVTCLDVMMVKHLSTGACHSVLFKLVMAILRHESSESLRRRQYALLLSYFQYCQHMIALDVPTSVVQFLLLNEQDGEDLDIQKIDKEQADLARANFFIIKKEAQGILDLVIKDASQGSEFGKTISLYVLEALVCIDHERYFLSQLQSRGFIRSCLGSISNISYQDGTHLLESQQRACTLEAELALLLRISHKYGKSGGQVLFSMGALEHIASCRAISFKGNMRRVDMKLQSDVGYNVQKQRTIITAVLRLVFALTSLVETSEFFEGRNKIVRDVVEFIKGHQSLFDQLLREDFTQADDLLMEQIILAVGILSKVWPFEENDGYGFVQGLFDMMSKLFIASPIKSILSQGSELKLSQLRFSLTSYLYFLVTKNSLRLQVSDDSLDSSTKLRQPTLLLLASLLSHVTDSLERAAEKKSLLLHKIRDINELSRQDVDAIIKICDSQEYVTPSDNIHKRRYIAMVEMCQIVGNRDQLITLLLQLAEHVLNIILIHLQDRSVSSNERGSYGSKSHIQQEVTDLCGKLSPTIDRLALLNEGKVGHNLKVFQRLATTVKEMAIQKCV 1838 F4KHD8 Nuclear pore complex protein GP210 GB210 3702 Yes SL-0178 SL-0182 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4KHD8 UNIPROT Q9FI62 DE Reference Proteome: Yes; GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MVPVSFCFFFLLLLLSAGESSSQLVSGPHITDVNILLPPKMKNPVEYRLQGSDGCFKWSWDHHDILSVTPEFNSSSHCSTSARLRSISPYSGRKETAVYATDIQTGMVIRCKVFIDNFSRIQIFHNSIKLDLDGLSMLRVRAFDNEDNEFSSLVGLQFIWKLMPESGGSTHHLAHVPLKESPLTDCGGLCGYLDIQKKLEDSGVFADLFVVKGTKIGHEKVSVHLLEAPLTHIADEIVLTVAEAMSLEPRSPVYVLMGASFGYTLKVMRGNVPQAVDLPSPHHRWSVLNSSVAQVDSLIGLTKALSLGVTTVVVEDTRVAGHIQGSSINVVTPDTLILYISPWSMSGDLITESKPFPSSMHWYVVSGRQYLIQMKIFSGRPDAHEIYITETDDIKLYGKDSDYWKIVSLPDELSSEYGQRNSRILNAISPGLGELTSTLTYFSGHQESKEVLKVVQEIRVCEKVQFTLNSEDDTPKVLLPWTPAVYQEMELIVTGGCAKASSDYKWFTSDISILSVSAYGIIQAKRPGIATVKVVSTFDSQNFDEVIVEVSIPSSMVMLQNFPVETVVGSHLKAAVTMKALNGATFSRCDAFNSLIKWKTGSESFVIVNATSEMMMLDELRSMDSSPPCSRASIYTASTGRTVLQATLAKEFHYFDKSLSESIDLKATLTIGAYLPLSVRQDSDGNHHGGYWFDKAQEETDFGVSKLYLVPGTYVDVMLLGGPERWDDNVEFTETVKTLYEDEEDLTSRVNVHHEVDRRANMYRISCQKLGSYKLVFLRGNLLGIDHPVPAVAEALLSVHCSLPSSVVLIVDEPVNKLDVIRAASQADRAPGRLRVTPVTVANGQIIRVAAVGISEFGEAFSNSSTLSLRWELTSCNNLAYWDDDYNSKMTKSGWERFLALRNESGLCTVRATVSGIDYSFKSQYSTLLPQGSESTLTDAVRLQLVSTLRVTPEFNLVFFNPNAKVNLSMTGGSCLWEAVVNNSRVAEVIRPPSGLQCSQMMLSPKGLGTTIVTVYDIGVSPPLSALALIKVADVDWIKIASGDEISIMEGSTHSIDLLTGIDDGMTFDSSQYSLMDIMVHIEDDLVEHVTVDEDSLSVGEHVATSSFKIAARRLGITTLYVSARQQSGGKVLSQTIKVEVYSPPRLHPQGIFLVPGASYVLTIEGGPTMNVSVDYTTVDNEVAKIEKSGRLYATSPGNTTIYATIYGSEGAVICQAIGNAEVGLPATAMLVAQSDTVAVGHEMPVSPSFPEGDLLSFYELCSAYKWTIEDEKVLIFIASSINVEENAGFVNVVQGRSAGKTRVTIAFSCDFVSPGLYSESRTYEASMILSVVPDLPLSLGAPMTWVLPPFYTSSGLLPSSSEPQKHRDGQSHRGNIVYSILKDCSSRADFERDTISINGGSVKTTDSNNVACIQAKDRTSGRIEIAACVRVAEVAQIRMKSEGIPFHVIDLAVGGELELPINYYDTLGIPFLEAHGVTTYNVETNHRDVVFIKTVNDQPSAYIKGIKHGKALIRVSIGDNLRKSDYVLVSVGAHIFPQNPVIHTGNLLNFSITGADNEVTGQWFTSNRSVISVNVASGQAKAISQGSTHVTFKGHGLKLQTKVTVLFGNTIYVDSPGETLTNVHVPAEGYKFPVKFRENKFAVTEHGNKATFNCQVDPPFIGYTKPWMDLDTGNTYCLFFPYSPEHLVHSMSITKDMKPHVSFSVDASLKEARRVSGSASALLIGGFSVTGPDKLNINPDSNTTIISLVGNTDVQIHCRNKGRLSISLIKRDDFGIAGHAQYKVNVLRSEQFTDRIIITLPATGQIVEIDVCYDTGESLVASSKDGYSVLLKILWGVLVLVVSVIILMKVIDRQVPTGATGTATYSGNAAQGTPERRSGTVIYHEESPRTPSPFMEYVKRTVDETPYYRREGRRRFNPQNTM 1923 F5H982 Nuclear egress protein 1 NEC1 868565 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT F5H982 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MPKSVSSHISLATSTGRSGPRDIRRCLSSRLRSVPPGARSASVSSKHRNGLRKFISDKVFFSILSHRHELGVDFLREMETPICTSKTVMLPLDLSTVAPGRCVSLSPFGHSSNMGFQCALCPSTENPTVAQGSRPQTMVGDALKKNNELCSVALAFYHHADKVIQHKTFYLSLLSHSMDVVRQSFLQPGLLYANLVLKTFGHDPLPIFTTNNGMLTMCILFKTRALHLGETALRLLMDNLPNYKISADCCRQSYVVKFVPTHPDTASIAVQVHTICEAVAALDCTDEMRDDIQKGTALVNAL 302 F5HA27 Nuclear egress protein 2 NEC2 868565 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT F5HA27 Pfam PF04541 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}. GO:0044201 GO:0016021 MSVVGKRVVDELCRVVSSYLGQSGQSLDLERCIDGAPVYAKGGATAICTVRMQHGCVYHLEFVYKFWAHLLEEMHYPFSPCFVISNNGLSTTLKCFLCRPSDAVSQFGHVLPVESDVYLAKNTSVVLGQDDFTKFKASLVFSKNLGVYNSMVICRTYFTDYRQVLQFLVVTPKSHKRLKSLLETVYCLAAPVADSAAQGGAGFPTNGRDARACTSDVTAVYWAGQGGRTVRILGAFQWSLGRAVALVRRSWPWISAGIAFLCLGLVWMRPS 271 F5HDD0 Envelope glycoprotein M gM 868565 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT F5HDD0 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0019012 GO:0055036 MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVYIFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCIHFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDAIFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIVIRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI 400 F5HFZ4 Nuclear egress protein 1 NEC1 295027 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT F5HFZ4 PDB 5D5N Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MSSVSGVRTPRERRSALRSLLRKRRQRELASKVASTVNGATSANNHGEPPSPADARPRLTLHDLHDIFREHPELELKYLNMMKMAITGKESICLPFNFHSHRQHTCLDISPYGNEQVSRIACTSCEDNRILPTASDAMVAFINQTSNIMKNRNFYYGFCKSSELLKLSTNQPPIFQIYYLLHAANHDIVPFMHAENGRLHMHVIFENSDVHIPCDCITQMLTAAREDYSVTLNIVRDHVVISVLCHAVSASSVKIDVTILQRKIDEMDIPNDVSESFERYKELIQELCQSSGNNLYEEATSSYAIRSPLTASPLHVVSTNGCGPSSSSQSTPPHLHPPSQATQPHHYSHHQSQSQQHHHRPQSPPPPLFLNSIRAP 376 F6S3G9 Aquaporin-11 AQP11 9796 Yes SL-0198 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}. UNIPROT F6S3G9 Pfam PF00230 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}. GO:0005623 GO:0009986 GO:0005737 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0005886 GO:0015267 GO:0015254 GO:0015250 GO:0009992 GO:0048388 GO:0080170 GO:0050680 GO:1904293 GO:0032364 GO:0008284 GO:0033577 GO:0051260 GO:0006612 GO:0072014 MTALRALWSEMQDTCTSLGLMLSVVLLAGLARVVARQQQLHRPMAHAFVLEFLATLQLCCCTHELLLLSEQEPAHPTWPLTLIYFFTLVHGLTLVGTSSNPCGVMMQMMLGGMSPEMGAVRLLAQLIGALGSRYCIGALWSLGLTKYHVSERSFACKNPIQVDLPKAVIVEALCSFIFHSALLNFQEVRPKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFKCFDEAFLQFFIVYWLAPSLGILLMILMFSFFLPWLYNNHTINKKE 272 F6ZDS4 Nucleoprotein TPR Tpr 10090 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT F6ZDS4 UNIPROT Q8R4A0 UNIPROT Q921B9 Pfam PF07926 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}. Q7TPH6 EBI-1811542,EBI-8317182 P83510 EBI-7280013,EBI-8317182 GO:0005737 GO:0005868 GO:0019898 GO:0000776 GO:0072686 GO:0005635 GO:0042405 GO:0031965 GO:0034399 GO:0005643 GO:0044615 GO:0005634 GO:0003682 GO:0070840 GO:0031072 GO:0051019 GO:0003729 GO:0042803 GO:0017056 GO:0015631 GO:0051301 GO:0034605 GO:0035457 GO:0007094 GO:0006406 GO:0031990 GO:0046832 GO:0000122 GO:0045947 GO:0006999 GO:0031453 GO:0090316 GO:0090267 GO:0046827 GO:0042307 GO:0006611 GO:0006606 GO:0010965 GO:1901673 GO:0032880 GO:0070849 GO:0006405 GO:0006404 MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSSTSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELSRLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDTVEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN 2431 F7EQ49 G-protein coupled estrogen receptor 1 GPER1 9544 Yes SL-0198 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}. UNIPROT F7EQ49 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0030424 GO:0043679 GO:0016323 GO:0005623 GO:0030054 GO:0005737 GO:0030659 GO:0030425 GO:0043198 GO:0044327 GO:0032591 GO:0005769 GO:0005783 GO:0005789 GO:0098978 GO:0005794 GO:0000139 GO:0098686 GO:0099055 GO:0099056 GO:0045095 GO:0031966 GO:0005635 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0048786 GO:0042734 GO:0055037 GO:0005802 GO:0003682 GO:0030284 GO:0004930 GO:0005496 GO:1990239 GO:0003707 GO:0007189 GO:0030263 GO:0007049 GO:0071392 GO:0071333 GO:0071389 GO:0071375 GO:0071356 GO:0006954 GO:0045087 GO:0030518 GO:0071157 GO:0008285 GO:0051053 GO:0070373 GO:0045599 GO:0010629 GO:0050728 GO:0002695 GO:0051055 GO:0051898 GO:1904706 GO:0019228 GO:0030264 GO:0043065 GO:0097755 GO:2000724 GO:0030335 GO:0008284 GO:0043280 GO:0007204 GO:2000353 GO:0045742 GO:0070374 GO:2001238 GO:0045745 GO:0010628 GO:0032962 GO:0032024 GO:0043410 GO:0050769 GO:0001956 GO:0014068 GO:1903078 GO:0001934 GO:0090200 GO:0051281 GO:0045944 GO:0070474 GO:0051480 GO:0043401 MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV 375 G0S024 Nucleoporin NIC96 NIC96 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S024 UNIPROT G0ZGU3 PDB 5CWS PDB 5HB2 PDB 5HB3 Pfam PF04097 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}. G0S4T0 EBI-4325187, G0SFH5 EBI-4325173,EBI-4325194 G0S156 EBI-4325171,EBI-4325173 GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MSLIGNGPSVPPSSTKASLFSSPTTSANPTGGLFGSTTGGSSLFAPKTAGSTTTSTTQPTSTTGLGTSLFGTSTTANTQNTANAARPSLFTAGNSIFGTSTTQPGLGASSLTTAATSNQQAQQQQQQRQQHQQAAPTGALFDSLLARNKKQAEGETALGELPSLQLGLADLRQRLRKLGPSSDRPIEPGKAHYFLAASGVDPGAAVRDLGALGLQAKTERTAASVGPAAGPSGVSTTGFGTGLGEVDVDTYLSNLQTKTTLSMIADGLERSARDFDAFLEENVTLEWEAQRKRIYQHFGIKPRDSSVAGTTTAQPTATPSKDGQGTFGRSRRKASQPPPGERPAQRMSILGRSTMMRSVIGTPTRIGAHAPEFSDVEARKDSSGAAVASVDDRFLREKQAKLAEKIREFNDARQRGTPFYICRDLADLESKSGDRHGPHIVEAYRAVMEMVGEHPDAGEAPRERQFAKMYLDPNTQSANALAMRKQILKGATTFLEKQFWNEVNSLIAKYPQDANLGGLPDVVSKIKAYIRLRIARKTLVPDNVELQQINGEYVWAIVFYLLRAGFVTEAAQYVNSNQAHFRAIDRTFSGYINSYASSEERRLKRQMQDRCMSEYNQRIRNAPEGSIDPFRMACYKIIGRCDLSNRSLDGLQTDVNDWIWLQFNLARETDRSLELAGESYGLAELQASIREIGLKHFPKTAAEDTNGSFGMFFYLQILAGMFEQAIAYLYPFSYVDAVHFAIALTYYGLLRPVDAASAGNELLSHNTRSMPQINFGRMLGYYTRDFRAANPAAAVDYLVLICLNADEAAGGQQAQAALCHEALRELVLESREFSRLIGDIRPDGRRIRGVIEERGPLIALGQEDDFIRTITLQAASFADDNGRTTDAVLLYHLAEDYDTVVSIVSRALSEAISLEIGEDPMRLIPVKPRVTNAEGQVEEAAPGSSLSLAAIDDPVELAKAMMGMYERDHMFWQKIREPNRVACSVLLQMADIKSLVEQGRWAECLDKIRALDILPLTARGDPGTIRSYAARFPSLAQPVAINVPNLLMWTVLCCMRQRERLAGGQFAGNESTARLMMDELKQMTVDLMAYTSQLRYRLPPHLHEALARASAD 1112 G0S0E7 Nucleoporin NUP120 NUP120 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S0E7 PROSITE PS00678 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}. GO:0031965 GO:0005643 GO:0051028 GO:0015031 MAFDNFEILYKETRLNLEPASPSSVVQLRVAPTNAYGRSSLSSSSSSRPASATADDEKGYRTKNLATASSIYYRKHHSSPRGFLWRVLDNNTVLSIRVADVCRQEKVADAPLILNLRFASPLRPACVGFADHEDHDALFVYAIDQSNQLWSIILRPDHFRKRSATEGGLGDASRVYSPPGFGFKHPHRLAVVSPDQLIVTMHDGGILKFDRNKNHESHGSPWRESIYNVAGWGQSLRGLVPFQRNPTVRYEKINMELTAAASTAVTTMGHAETAFLFTICLDHRMRVWDVRTGQILYTGDILNNTKRDPQEVGKWTVDPSQNNLIRILDNGRGQCLVVTYSPVGAGEFKFWKVKANDQGSIHVTDCFPDARLMSPNPTSLDVWTLADFAIAQQPDGPELWALWKNNTSYRVNRLQIIPRNATAPFADGWKAVCVESPGPTPRASGSWNPTDSTEKWLDLIFSPGRFSKSTLETALAMYEKGLGTYKETVSRSGKGIAESICSVIGSTTTLDRSSQGGADYDQFRNTSETQWMRFWRLLLELDKQRGEALSLVFDQYDGMVWVTCADLLAAVRQCSDLERLYHNLQSPEKKNEDVAALISAGLTFVETFSDSMHQLCKAALRAELYENSALSDRERMQLFLDRAGFWVTDEDWAQVLDIVGQNYQMVTSRLYEDLFDLITATSEANSQELREPFTIFGKKVVVRAVQETVELHWQILFSQLILLVNMVDSESEEARPLHTRFDVGSVYRRLIDALRRLEHLRWMTKTELSVSPSKSRSGSSSPTLSKRGQDESYTRTALEELAGHLFGLPESNNMPLLSSITDLVLDLCAPTSTTVLNTWLIQCWLLKEGRPDLALELMPFAEQDPFSTYVQGRVFLALRDYDTAAQHFRKAAIGLSIPLKHVDRHSAGLLDDTEWNLLNSGLPNYYAHIVNLYDKQKAYSYVMEFSRLALQFAQTSNQDSASIKTEMLSRLFTASTATSHFEEAHSALLAMDDEALQKSYLRKLLERMCESGQSSELISLPFSGLQNKVDEILAEKCRATRDVLNGVPYHQILYAWRISHNDYRGAAAILLDRLEKLRRSGEGDKLGAEDGENGAGNDALDTQVTRQYLIVINALSCVAPQEAYILEDVPPPVPGKGTNDEEYSQTGSKRKLGKLNATSGEEDLDSRIEELARLLDSESAGDKKARPSSSSEEDQQLLERMQKFSTAVRQEQGQQTPRRLLRLEDLRKQYQQELDRIVAIQNNQFALTADGEDEDEDMMDIA 1262 G0S0R2 Nucleoporin NUP57 NUP57 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S0R2 UNIPROT G0ZGU2 PDB 5CWS PDB 5CWT Pfam PF13874 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}. GO:0031965 GO:0005643 GO:0051028 GO:0015031 MFSSLNTRPAGQSLFGANTGGGLFGQSLANQPQQQQQPLQQQQQQAAPALGQSQINQNQQLGGSLWQPGSLTAYQKPIPEQIKLIVDKWNPNHPNCAFKTYLYNKVDEHTVPLYGPGPNEDPKEWEEALQRKPAPNFIPVLCSGFPSIVARLMLQRRVITEFNNKLHQINASLDAILSRHDLDHTVRAFNARRRHAELSRRCLHLAARVQVLRNRGYALSGDEDELKQKLQQIDKTLNDPAQGSRLEELWSRLIVLRGYAEDLKDQINQAGITESDGLGEEIEAKAKKILEDYDKQLQHLKKQVEEAKKDFEEWEKQHNPAPAPAR 326 G0S156 Nucleoporin NUP53 NUP53 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S156 UNIPROT G3EQ73 PDB 5HAX PDB 5HB3 PDB 5HB7 PDB 5HB8 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}. G0S024 EBI-4325171,EBI-4325173 G0S4T0 EBI-4325187, G0SFH5 EBI-4325194,EBI-4325171 G0S7B6 EBI-4325479,EBI-4325171 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MPPLILHNVPDDELYVGDDGIQRPFAMVFPQQDGSLRSRKANLETGAFGKSTRRTRSKAATPAKREDPTIAAADKIFSNWLASQNQSAPQTSVPAPAQRKPNLIPSSSSQNLAQGHDESSAPSQTRFFRKQEPTEVILRGYRNAQHQYAAINHYEQIAGRICEDYPREPPVESRRYKSELRDPAFTHRRALTPEERAKVNRAMSGEHWVKVTFESAEAADKAVYSSPQLIQGHLVYAEYYKGVPPAQDEAIPDPSVAAFGAALSRTQTLRQRNRGSFSLSGTQEAGGPDASPTSSLTADTGTLASGVEISTSTSNTLNGGAAAGGAEKSQDDEFCRVIPTVRKAKLLPMEEALLPAPTFTQRIANHIPFLRWFNGAMIGSEVPRTETGEFDWVRASLFWKLMWWLDFLLGLFGGDIRDAEKDDKED 426 G0S235 Nucleoporin NDC1 NDC1 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S235 UNIPROT G0ZGV7 Pfam PF09531 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}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MAAAVRRSPYKDFLQPALQRRFATATLVVLATAYFEALLLARWSSWLWSWFPLGPTGFRAALFFLCGIFVIILRISQYHPGIRTSDSPIATLVRYAPRWTTFETLFTYALSAWIFSLVYLGTVPDDAGFERITYFTYDRARLNEKPIFLTTHLVLLGIYQGVRHLYSDIDRLSLGTAQPSNGDSSKATGEDGHVSTQMRRFRDQLPKIVVHSLHQSVMGLLLSASLYPLLLRDLLWRVNMTMLRPLYSLPRTNVPPANLPYSPSTLLRCLAASVMVMFAWTAANTAFSLLLVKSPLKNGKPLTADAKDPNGSLLNGLKNKKLSIKCFAMWELAYIARDFPDRRKAIFEDMDRKDGPMWSQVYKICLDTLHTLSSNIDAYTAPPAPATTPQQAETALGDKPRTSAPPKEDHIFAPLPSNKSAFRTSVSSAFQNAALAGPGGPPASLSPVAKRTLHAARSRLLEAAAPNAEIEVTPSSFFRELALKYVLSSPLAGYPFRQTRRRRLASAVLGSPYGEPSLYVNAASAVSGLAVSSLREDRYGHVQRDVASLIRELTSLGEKLNAFVNEGGMGKHWTDVVELEGEDKCEEVEEVVNAVKHALKRVIVAFEPYARDLRLTRGEVKKAREVAGLEQEVEVREVMPEMVQIR 646 G0S2G1 Protein ELYS ELYS 759272 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WYP5}. UNIPROT G0S2G1 UNIPROT G0ZGV2 Pfam PF13934 Required for the assembly of a functional nuclear pore complex (NPC). {ECO:0000250|UniProtKB:Q8WYP5}. GO:0005643 GO:0051028 GO:0015031 MLDFTHFPEVFPTDGPRPYDQHFVRQTETFRKSLDGVLFIDRVLGALGLPDAAKAYPPRGDAGLRALHQQVCSAKVSAHAKLSVLYYLLLDHDEHRGSRSQLADALAEEVGLPANYQILMRGLWHMDRKEFKFALEHLAHPSLPAEFADEIITVLVRDGHTTGDYSLPLAYYHAVRPVLQTSSALENLFAALARTSVTDALAFSRTYPDHGARQLLFERLVASVLEEHGSGQVAGRSASRAKELVSLPLTGVEEKWLNDYLSTGEGRKSRSAKAVVQMRQVVTGRQKELGAVVGVRAGR 299 G0S2X1 Nucleoporin NUP37 NUP37 759272 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH4}. UNIPROT G0S2X1 UNIPROT G0ZGV1 PROSITE PS00678 DE Reference Proteome: Yes; GO:0005643 GO:0051028 GO:0015031 MALQPVPRMRRTLQNTQHTYSLGRRIYDVKTYPVQSPQGATILIYGHENGATVVWRGGRRLKPPKPQTNEKRNGTKPEDAVMIIDSDDETGPTFVDKPEFEDSPSVADGSVAEIIQTLDLALGTAVNHIAVLPMPPCAAEDASWNGANILKTKIVFAVTCATNDVYVITLPLTPPSHEAKARPELRKSLLAGNAGKGVWGETLTLLTGPSRSCNGVAISLVKHRSSSRSRSSERSAAQAAPITRVVVAAHSREASGTLRLWDVPLEAKPGTINRVEPFQTEYLPSPLTSISFNPVNLTQLLTVASPHAVRIYDYATASLPSDDTSEGPFPSQGSWLISLYPPFARGPAMSTSRKPIVAAEWIARGRAILTLLADGQWGIWDLDGASPTAAGGGSNLFSKTSAGLRGTAITAFSVTGHLEGTSPLRNPTTQKASSSSSGEFVPMTPHTRRDAIATAFGGSPEKLAAVRGGITVAQLPSTLTSGAGDESAVLFLGGADPIVCVIPVLSKFWDSQLRRAAGGGVNLWSGAQPTRMIRLTDLSAGLLGERCTGAVAITKAVRANASTNGILKEDDNSGSQGLPIEVLLQGESRLVIVHENGDAPTSSLTSRLLGARKKQRDEFKSVNAIVAYPPLEKPSVSFNLNLTQRPEKPGTLFAPRSRHSKSLFEQSIDTIPSTDAGDEETIPATSAPSSQQGFMFATDLELAADLPDDEADAEGRDVEQELLDIMEIDRELEQLEQARERGRKRVFFEEG 751 G0S381 Nucleoporin AMO1 AMO1 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S381 UNIPROT G0ZGU0 PDB 6B4G PDB 6B4H Pfam PF00642 PROSITE PS50103 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}. GO:0031965 GO:0005643 GO:0046872 GO:0051028 GO:0015031 MTVCRFWQQGYCRNGNACKFEHPPKGGQNYNRFGALSGSGQGMGGRVSEPPHYPGLSEDAIQKDLTSELPTWILSCYGPGRDAPEQLFGGYPREQSFEEIRLHFYNGLMAGNPQGALNEIQAAYQAAQQQIQNTLQNIPAAVQFILDAANKHPNRIDICRESSKGSSTGGSVFGRNVNPFQQSSAAPLNPFGAPSTPSTSAFGQPSPLGQKSSAFGTPAFGQPSQPVSAFGKPSALGGGSAFGSPQTGSTFGQPSVLGAKPSAFGQPAFGQPAFGQPAFGQSAFGQPSALGPKPGAFGTSAGSAFGASTTTAPSPFGAAAQATQPANPFGQPSQQAANSFGKPAAPASAFGQPSTTTAQNPFGQPSTQSSAFGQQQPQQAGTFGSPSLFGQQQQQPSNVFGQPSTTSAFGSQAATSGFSQLGNATSTIGASPAGAQAPASKSPYHPGSTRQHPDLLSYATKNPAGGLDTFKGKPVVYETPKGAAKPVPHIRQFDGTLVRIWMPDGAPAYTADTEAEDPKVYEDEGVKRQWQSFLEKGRFEGGMPEVPPRREWCVWDF 557 G0S450 Nucleoporin SEH1 SEH1 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S450 UNIPROT G0ZGV0 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0031965 GO:0005643 GO:0005198 GO:0051028 GO:1904263 GO:0015031 MSKAAAFLTDPPLVDDRPSFETILKHGHQDLVQAVAFNGHGDRCATGSVDGKIRVFNRLKEGIWRLCDNWTAHAGEILELQWLPTTVYPNLLASLGIEGRFKLWAEDPSAAPGRRFAESTRNGPLITIPSPRLSSHPSHLTHSQHPQQQPHHHHAPESILPSNPPPTSNPPQATGSTTAGSGAKPAFETRNPRSPYRSFSIKHIDDTRTTYLALLSADGGLTVYENDRVENLAAFSLMDEFNVLDPTAATGPGQASTAPRGQETSFRVRFDPNPDVCYTALRDGVLSDALGLVVAVQDTVKVYRTRDAVRASLGLAAATKEFYLAAEVVAGVHRGLVRDVAWAPGNIRGYDIIATACQDGFVRVFRLDTLSPSTSDTTKFAREPSSIDLTQGGELDDEKRAQESAPESRWSSSRVRRHATRRQGPSQDALTITTSGLRASLDSHNHQQTPSRELDAADRRSRRAWTNQPGQVRHTLTEISRLDNHRTPVWRVAFDDDGQILGSVGDEGKLLCYRQKPDGTWAKSSEMSVVKVKMAAPQ 538 G0S4F3 Nucleoporin NUP82 NUP82 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S4F3 UNIPROT G0ZGT7 PDB 5CWW PROSITE PS00678 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}. GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0000055 GO:0000056 MPKIKSFAPAWLNEPAPGHKLFAPAADDGTATVPLAYGKKIKPGPRRTIARRGTEIFVACGKQIRWGDLAQLKESWESRPSRSSVGPTSTKKDSSDFDDGAATAGYRIIKTPVADDIRQLVMSPNQDFLAVLTSHTVHICILPDSSHLHIQDTTPFKPKFWTLGPTTHVTSRSAVVSAVWHPLGVNGHALVTVTEDAIVRVWELSTADRWTFDAPTLAIDLKKLADATYLDQDFGVSTSATNKGFSPDAFDMEVAAACFPTRDSGGWAPMTLWLAMTSGDVYALCPLLPQRWTPPPTLIPSLSASIVAKVAAAEDNPESTPEERLVAQQQLEWMSEIDNQEPKLVEEATGEATIEVYTRPSRPGLVPKLQGPFDFDLNPEDEQDDEVELKDIYVIGEKPRVADLMRGEEEELEMMKEDQHNGLSLNIICLLSTSGQVKICLDIDGVEAQWLPPRSKNKRLFAPPPEPPSLLTFQTFDTLKPAEVTPDGWPMFSEDATSPYSFYVTHPAGITYISLTPWVFRLESELQSDSEAGTEFRIDLLAKGQGSERDRIFTQTRTQSPLAAATSIDDPDLGYFILSATQTDPIALFFETPERPVVPKETSVVIPEHVEERPPSPYWEPRPLFHPAEALDKPSAVPAWIDNLRTGRRRPLLTQELRLSMATLEVFHDGHKVVSTEVSDINDAVAELFRKCEALQGELRDQIKKVNEVKNRIHTITGDDLSDDPPVSEDQLIKQRIRVARERQEELANRMERLRKKFGRTTTRELSDKEKAWIEEVQNMATSILGPEAGQGALATTPNLAKQPWKRLEEIKTLRNALMAEAEQLQKVGDDTEESTPASQMPSLKIPSEIRKAKMAQVMSLLERESALVDAVKARIERLSIG 882 G0S4T0 Nucleoporin NUP192 NUP192 759272 Yes SL-0178 SL-0185 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}. UNIPROT G0S4T0 UNIPROT G0ZGU6 PDB 4KNH PDB 5CWV PDB 5HB4 Pfam PF11894 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}. G0S024 EBI-4325187, G0S156 EBI-4325187, G0SFH5 EBI-4325194,EBI-4325187 G0S7B6 EBI-4325187, GO:0005643 GO:0051028 GO:0015031 MTDLRKLEALQALHAELVAVRQHRFEGLQVLETLLEEQTDAFKALIAKPARDTKDREALGKEPKKLKIGEEEYSLNEDFVNDCLKLADELDLNEKESARILIDCDAEGDVETQSRPLWECGVIRFHQERKYLLDCMRLILEIAADEDIDAGLQESFGVAAEDKIFGIPPPWERNKENQPTQVKKFIPRCMEAMKGVRSMLQCMADKANARNMLQQASLVRPLDNQETLDFSRLSLVEQHECLASILHAAVQRHHATIADFQDFIKILRKWDKYDHFLIHLIPVLAAYITEFGSPEGMGDLQQARRLNDFICKGGDEDSWALPVLGAAVRAWWIAEHNGFYLDDTVQDLRGINLDEEDEQRTKQFLDALKEGAFDFILSVAADCKAQEWQDPSQLGARQWLQRKIPSLPSEPFPFSHFLQHSLMVHLEGFVDATISNLPDVLRKLRTEEDEQRQLRPNHEQDMDLERFLIIISYAYEGRPDAAMSFWEDPDSNLAGFLQWASRRASTPLVSAFCEMLRCLADNEECATAAHNFLLDEGHQASGKMKRSQSLTWSQIFKELEYFTTKVCSERPNPPQASMHRPGRPGADPAEIEPESALMLECYLRLIAKLATESEIARKRLIMDEDFNLVDTILKLSVGVIPHRLRACIFYVLKALMIRKTHEELDAMWRWVEAWMTNPFSSLPGSQGAPQRISFLGQTPGPQECMEMMFREFGTGFEQSNAFIQLLTTLLVPPEGLNSLNDSVPFPEWLGSSIRTLGIEPYVDFVFDVFANRTKDISDPSQLRILRLSCLDFVMVCLVTFNEDLIVLGHESNISIDDAMAATNLATYVRLHPFSRVMEWLFNEKVITSLINTIHQDPISLGSASPDSPLVVSILRAIQVMIKALELQETYLHLVRPEVLRYQGEAGVRRKPVANAAYSAFEDGILSHLSLVVDLGKYCNLGHAELTLACLKLLEKISTSSRILSAWSPDSGRLGHRNKAIVQLERNGEGETISASLSASIMATLDPALAASGENYRVKLAILDFLYACLRATPDQPTIAHQLLGFHCELSKLGIEPKGPFDMQKSLFHSLLNVLITLTVSEEEQGMRGYLVTLKYRVLRILQLLWKSPLSASLVMDELRATNFLFHMLLREVQIQPQLPWDGQLVTGCEFLLSDASLAYIDYLASRAAIFEYIGKELCSVSQNRIPSIKRQIFDALNGQIFVDEEAPLTIPSIFDFFDFINTDYKWEEIPSPHFTYLKDLDLGPCILEHKYAGVHYDIRKAQEILALKRKEYEHSQLATPEFLETVELEEKVLIEWLTVRNRANLLLTARLNLLQAWANLLLVMIESNDFKSTPKMAFLLQALQAILPTLEAFSSLKSDEAFELARVAKVLLWKLDFSQDSDAGLDREQFTVGNLIGDKLFQLFQLCLSAISQCSGTPELRSLYYSICYRYLTAVVDNDATVAATPASSTIGPTRSVTNARARTLKAITLYGDRLLNVICDDAYGSDTTCQTAAMILLNALVHTSRASSAAGVSPADVDCPIIDALNRLNFIGVLVDSLKEILNEWLAPSSTFDPSLSTNASPSLPIPASPSQQYTSAKLALLLQLCQTRQGAKYVLQANLFRALEQSGVFAADPELVEVDSESGVPRVVALERHYALLVALARVVGAAVTARGAHNIVQGRKFLTQHRGLVVHVLKKNAGIGGGVVGNSLASSINGGSTATMTRRDEILAQQALEERIEELAEAFMLLITATGFLEYESEQVPSEQPRAHTTFFH 1756 G0S4X2 Nucleoporin NUP49 NUP49 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S4X2 UNIPROT G3EQ72 PDB 5CWS Pfam PF13634 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}. GO:0031965 GO:0005643 GO:0008139 GO:0017056 GO:0051028 GO:0015031 MSLFGTNTTSQTPAGGGLFGTTTSQSAQTGSLFGTATSQPQQTGGLFGSTATQTPSSQLQSTGLFGSTTATSQPQQTGGLFGSTTTTTSQPQQTGGLFGATATSQPQSTGGLFGNTTTTSQPAQTVGLFGTTTQPQPAQSGGLFGSATQQKPATGGLFGSTTTNTGAGLFGNTSNTIGGGGLFGQTAKPATGGLFGQSTTQPQQQQNATPGLTMGQSTNTQQQVVPGVRIDLSNIKSTTRFNDLTEALQQEIAKIDEEIQKCIRDKEAVDAFLPAHGEQLAAIPTDVNFVTRKSEGAHNALSSDILAIDQLRELVKQDADNARLSFKAIDNLKLPMQYHQAGLWSKQMGGAGTAGASGASADADGQSNADLISYFSKTADEMEEMMKKFEKTITEIEAHLTGVEAHAMAMQNVAAQSRNAAQGGVDERVYELAAVLREFEESILKVAGVVGGVKEGVTELQLRDFMGHGS 470 G0S6T0 Nucleoporin POM33 POM33 759272 Yes SL-0178 SL-0182 SL-0185 Nucleus membrane {ECO:0000250|UniProtKB:Q12164}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12164}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12164}. UNIPROT G0S6T0 UNIPROT G0ZGV8 Pfam PF03661 Contributes to proper distribution and/or efficient assembly of nuclear pores. {ECO:0000250|UniProtKB:Q12164}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MAPPPPSADVPLAERLQRLASTLQFAWFSGHALLLLCVFRYAFSWIRFNYYSGMARFCYRFAFIAAAATYGIVVYKTWRARQKTGVKTSGIKDYLRDENIQYLVLALVWLFMPQYPLALLPYGIYSVFHVATYVRANLIPTLVPPQRINAPAGASPNAKPQYTQHPASEAIGVFVKKYYDSSMSMVARLEIMLWLRLILSVILFQRRSWILFAIYTTFLRTRFSQSIHVQNAFALLEARIDNLIGAQGTPPQARQVWDNVKTAARQFYAVTDLNKYESGVAAPKKSS 287 G0S7B6 Nucleoporin NUP170 NUP170 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S7B6 UNIPROT G0ZGU4 PDB 5HAX PDB 5HAY PDB 5HAZ PDB 5HB0 PDB 5HB1 Pfam PF03177 Pfam PF08801 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}. G0S156 EBI-4325479,EBI-4325171 G0S4T0 EBI-4325187, G0SFH5 EBI-4325194,EBI-4325479 GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MEPMTPMRPIPGAYVNTPAPPTANPARRRLFTEASSSGAAATTQLGAAPAPLASTMAPGPEINSGLMTPQAREDLPPVAKAAQVVNQTLQLDDSYPDLDSYCRPGASSDYEMQSSDSSWAPFHVVRHHNIPDKVFEHLNAGEVFTKLGLFAEIGYAWASIDSSLFLWDYTHPNPELIGYEEATHTITAVALVPPKPGVFVKTITHVLVVATTSEIILLGVSATPTPSGSKSLTLYSTRMSVHRGGSDVSFIVGTKDGRIFLGGESDTDIHEIFYQQEERWFSSRCGKINHSHPGWSAVVPSLAGLPFGSRQQEWLRGLYVDDTRNLLYSLSNRSTIRTYHMEGPEKLTKVIEKDKTSCLRDFAHMADSSPLFTDKTNIVALSPIPATEASKLHLMALTDTGCRLFLSATSSASYTMGGATSLAPQSMQLQFVKFPPRESPTRIRTLNGQIIDSQLDKTSRALDPSALGFRFSPGYFFDVVRKHPNQDMLFVSAPDTGRIKVTQPASALKYFEQGTWIELENGNRTIEIGLTTAPFAAAKQPLGFGNELAVQFDQVPGEFAVLTNTGVHIVRRRRLVDIFAKALGNCVSASDDALEREVRKFINQYGRVETIAAALAVACGQGSDLRTGTGRGMDRNTENLARAAFIEYGGQPRLAESDGKQSVSESVRLSSRHDALALYLTRLVRTLWKAKVVQVGSGSDISSTIPTSKLVTIQENVERLRNFLEANKSTIQGLAPPSERLFGRQEDIANQKEHQALHALQKLMESISEGISFVLMLFDERVSDIYARLDAVSQQQLKDLTYEQLFSQTPGKELAKVLVKAIVNRNIASGANVETVADALRRRCGSFCSPDDVVTFKAQEQLQRASEQAHNSPVLRALLAESLRLFEQVAGSLTPANLTTAVEQYISLKYYAGAIQLCLTVAQQKDRGNTALSWVNDGKPANDSRKKAFDERKICYNLIHQVLDKLESDFAGEPELVDGRPTLAATKRMEAYNVVNDSSDEVFHFDLYEWYIEKGWTDRILSIDSPHVITYLQRLAETDFRHAELLCRFYTTRSRFFEAAQVQTNLAKSDLNISLKDRIILLSRAKGNASVNTIGISRQQQQQLNHEASELLEIAHIQDDLLERLVADPRIPEERKAEIEEFLDGPIRTLTDLFNDYADQANYYDLCLLIFHAADFHNPRTILDTWNNLINQSHFEAEQRREYWEIVQAGGDLPAGVIAPIAEPPLPYVYVSQQIQLIAHRTSLDSLIFPVNSLLPVVCAYAINNGQDASIGADPCWPIQLFLNLGVPHALVVQVLENVLDTQEAPFTGRRRKLVVQWIAMAVDMWVREVERRGAMAAAAASGASGSEAVMGSWVSELLGRADQVLTQIAGTGATLRGGAASDAEEIASLRRTVKGLKRSVDMLLGGEMARMSFFR 1416 G0S7F3 Nucleoporin GLE1 GLE1 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S7F3 UNIPROT G0ZGT9 PDB 6B4G PDB 6B4H Pfam PF07817 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}. GO:0031965 GO:0005643 GO:0016973 MAGSSPLNHHLWSSPSRTVEEILAEDRNSEARHRYLLELARKEHERVREEAARIYREQLAREERERLLAERRKEEERIRLEQQIAAENARLNALKATRIEIPPLLPDPVPAPSTVNGKPTLPAAVATEAKRCPSEPSLVNGIASNGVVEAPAAASIKTLEPAKPAASAFKAAGSATTAAPVAPIASVQPSTNGVVSAVASTPKTAPPAPTETPPDRYVEIHRNLKGLRKYMAEQAKTNLKLKQRMGDMRREIRKSVGQLTTGGMAANKDKQQKIKSILTEALSNQVESALVDPNNFVVEPRKPVEGATNNDPLLPSIFVYLINIFAKAAISQFINEAGARPETADPVGICVAAILSEPDFLWRGASLIDILIAKFRIVCPVLFGYRGSEKTEQGRQRLGWWKESGQWISEQQHMDRMTGLGAGFAAISLRKFALSKKQNPYPPRFYWMAMAKIVNTPPAEISNTQCVVLKAMVQNYEAKFIEFYGSAAIAALRTALIDFPARAPHKSAAVNSLEVLAQMLKRDTGLDLG 529 G0S7R3 Nucleoporin POM34 POM34 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S7R3 UNIPROT G0ZGV6 Pfam PF08058 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}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MSSTLSVAKAASTPVKQITSAVGPVKESPGNWKHPRLAEITRRQSRNIFGEKNVRQIVYNVAAIVLLEIFRVFASPSIPSQLILPSLRPYSLWIHAVFLVIPLTNIVIALLPLFRPVDDLSDIPLTPAQRKLLGLPPSSKPATPNSVYSTPPRYSRTPSLAGSPASIKSYTSSTLPTASSPTPGAAGIGAGSPAAPIYLSPSKFTTSTSSQQFSPSPSGASPLLHRAISNTSTASGVSPYGSPNSPSKFGASTNSTLAASTISTSTFSVSTTSSIAHVLNNSRLRESVIEGVPATPTPVGKGASVKANSKWLYQRGRRTSSNNWVY 326 G0S8I1 Nucleoporin NUP56 NUP56 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S8I1 UNIPROT G0ZGV9 Pfam PF00638 PROSITE PS50196 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}. GO:0031965 GO:0005643 GO:0046907 GO:0051028 GO:0015031 MADDPHNTSTSDVSELVPDNTEPSAANVKEDAETTAARRELKQTTISDKAKRDSAQLSQEDDKSASEEDDNKSDAGEPEKKKPRTSRGLTPEVQLAAPKQEVPKETVASPKKRTHDELEQDGKEEEEKKEGEKPSSQNRAERDEPEKKRPRDRQASLSVERDGQKEVEPLSAQESRPSSAEKPKIEEKKDESKDTKVDKPQTSSSAFANSSMAKFASSTTSPFGAFGAAAAGKTNLFGLPATSSNIFGSKSADASAAPAGPPKLSFGSASAASPFASLNGQAGGMSSLFKSPFASAFSGGSSALKTAGATGFGKPGEPLKTGKSAKPFGAPESDEEDEGEGEEGEENKSENGEGEEKEEEEKEEKASGEEKKKFKLQKVHIDDGEGNETTLLSVRAKMYVMEKGVGWKERGAGMLKVNVPKQAVEVEEGNQPDADSFDPAALDDAARKLVRLIMRQDSTLRVILNTPILPAMKFQVNHKLKAATVLFTAFEGGEARQVQMKMSQANATQFSNMVEKIKEKLAAA 524 G0S9A7 Nucleoporin NUP133 NUP133 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S9A7 UNIPROT G3EQ74 Pfam PF03177 Pfam PF08801 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}. GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MFSSTLHEDGPATRTRSSRRRQRPVASDSSLQTQPKAKRQRVPLTESNTAPTPTPADADAPPEMFEVKPDPVLAKRERDGIGIENIENLGPRRELSLRSKKPKSGERTSKGDGSIILTTNNAFTVSKLPALPDRLRAEPTSRQHGAIFSSGYALALTHTHAFVWPYTATTASPETFTFALPYPSKHASDPLPLGALVPPSASSDDPGLVVVMPVSGRVVYWESISSAATLDFIRQQRTGIEDAISGMYSSEHITQLVSAESAGFVLVFSSGRIAYMSVRDPHGRPGITVQYLRSPFGGASLGFLSTLRHALSGSSRGDIAAAHANHGPRVGERVVIAASSKGRLQAWKIHRGGHHEPVAEADVRERLVEAVNEADAKTQAFPSESFEVLDFAFVPRGLEPKYVNASRLSEALTHEEDSLQHMLLLVGFSRGHQARYSLVETVLAPEGARIGTVRPITSYTSPVRPGALEKPRLYLPRPALVAFVVFDRAVVVASMVAPPDSPDSQLQEDSHILPPTFEDVVDFRDDDTLQVVGSGSEEPGAGTSSEDVRPHRHKTKNPTAVLLLPGVGIVRVAITDIERFASDAPPRVTAKSKLEQAVFFGIKSDNPLVFQGRRALPFSDREVCDAAVELSHEIVNSKTPFIPSVPASLEGNMKSRSAYLDALITFLNACKVNMDERTRWMLLYDAEKMAVATWIWQKHEQFLAERPRADKKTLISEAAVFINENQKTELNVAAGQVDPVRHWFIHDIFRLDIFVAWAYQIIKYHYTQKLSDEPGLNRLVWEAVTINNGALLEARQFRLDKAAQYGVDPAVVPTGNGLPEPWTSTYFITNNLKRLTEFCHQWLAKHDAQPSADPRFDARLLDTVRERLPSLTSQYFTSLSEYITWAASSTDPETQDRCRAYQAAYAEDVYKKIVKLKEFDLWEEAVELAREFEAFDALADVVVGQILMLEAAAADPTTTESKAQENAALAQVKKQRLGRLMEEFGEGFASRAYEVLLDAAGVQAVLEFAFDRKGFITKWLRGKPELARISWVNEVLREGDVGGAAETLLGLGMSREVQVWNKKVELSLGKLALLAEGGGSDDEAGKGEVGGTIKKIDAELEVVKVQDLLYQWILASVHEAVDSSAEVELAVKQFGGLIPRRQKALLQIFEDGIARLLKHEVLDPLTLIDLLTLSSLGPGHYEGMGDQFFLALKVAHYAALENAEEVRRLIWRRCLVRDDWRQVNETNLKGDEEALEAVGETAAYRTLFACFDEESSTPTFRPHHTLKPSDCLGVYTEPEQLDSRFAAMDDSFRGKLVEAMRAEDRLLRGFVEKAQLDEWWRATRETAERMVGVAAQKGHRRVNSGSVGNGGVNGLSLNGRVKMY 1364 G0SAK3 Nucleoporin NUP145C NUP145 759272 Yes SL-0178 SL-0182 SL-0185 [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}. UNIPROT G0SAK3 UNIPROT G3EQ75 UNIPROT G3EQ76 PDB 5CWW PDB 5HB0 PDB 5HB5 PDB 5HB6 Pfam PF04096 Pfam PF13634 Pfam PF12110 PROSITE PS51434 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}. GO:0031965 GO:0005643 GO:0016787 GO:0003723 GO:0017056 GO:0051028 GO:0015031 MSFGFGSGGFGQNNNSSTFGGFGSTPTTNTGFGSTGTTAFGSTSNTTGGGLFGGGGGGFGSGNTFGSGFGSKPAFGTPATTSSTSLFGSTTTTAGGTGFGSGGFGSTNTSSPFGGGGTSLFGNKTTTGFGSGTSTFGSNTGGGLFGGGSTTTGFGATNNPGIGTNVGDPPGTAVVPFSPTVEKEVNNPSQSNSYQNILFMDAYKKWSAEELRLADYNQGRKTAAPGGTGAFGSSGFGGFGTTSNTGGFGSNTGGGLFGNTQQNTGGFGTTNTTGSAFGSGGGLFGNKPATGGLFGTSSSQPAQSGGLFGSGTASTFGSSNTGTTSTFGSNNNTGGGLFGSNNTSSKPAFSFGTSNTSTPGFGTATTGSGFGTGTTTNTGGGLFGNTAQNTNTGGGLFGNQQQSGSAFGSGTGFGQQNQSTGTSLFGNTQQKPGGLFGSTTTNTSGGLFGSTNTGTSTFGQTPATQNTGGGLFGSKPAGTGGLFGSTATNQPASTGGLFGNLNTNAQTQQPATGGLFGNLGQNNQAKPSLFGTSTTTGGGLFGNTNAQQQTGSLFGTSTAQQQPQTGLGASLFGSSQQQQQQPQTFSTSITDISAYGATTLFSGLPDDKIQNPGPLATPLSGKAKVKSRSILPMYKLSPANASRLVTTPQKRAYGFSFSAYGSPTSPSSSASSTPGAFGQSILSSSINRGLNKSISASNLRRSLNVEDSILQPGAFSANSSMRLLGGPGSHKKLVINKDMRTDLFSPPNKDKQPQEDGTAARKTVTKRVSFDTSNVETPEKTIESSIPATDDSGYLKPDARSTANGTNGANGAKSSPVAAASPPEMEQVKGKELAVVHEEESPAPAQTDKPRGSQIEPGAYWMSPTADDIRAMNRMQRQRVVGFTVGRENVGSVQFKVPVDLSNINLDDLFGTIVILEPRSATVYPNAAKKPPMGKGLNVPALISLEHSWPRGGPTIKGRRLERHIERLKSIPDTTFESYDPETGVWAFSVEHFTTYGLGDDDDYDDDDYETEPESAVKSTPRPVTSPSISKSSTSPIDPDDTFEFRRSRRALPGAFDDAALSDTDEVANHAQRQGTLSPEPQDADTPLPSREWPEDESMADGLDEYQLEAYEEASQQGSVDEQEDFLPSRFAADNDAPQVPAGIMRARMRAVKKLNAPTKIEVAGGDDWTQILQASVKAPRTMDRATLRALNESGAVWEMKDRGSPPPQATATVSDGMGFATSIDLMKSLFEQAKAPTQPALTTSGKGFVKWPYEQRSKTDTEENLAVPRTNWGPNELLISTQHNEPNLLPVDAADDSATSPSTLARLQQYINLVSSKKQLQRVAGPEFRELAQGDSVWELAALLFDDNGEGVSQFWQQLVSEATDRALSFTAGLEEKAIICLAGNRVDEACRHLLAAGNFRLATLVSTIGKVDNKDIRAQLKDWRESNVLAEFSEPIRAIYELLAGNASVCAGVKNVPIENRVNSFTISQRFGLDWMRSFGLRLWYTSGVIPDVAAAVRSFQEDIEQDREPEPDSALWTLLKAFASREYDWSDTRLGWLLTKAIYTTGKVSFGEDALQKLDKASVTFASALTAASHWVPATFVLLQLSDPASREAAVRDHLGRHAHRIGSPRNLMSPFFTLQKFGVPEAWIWEAKALDYRSRQDSQQEFLALIWAQNYAEANRTFVTRVGPDLVIERNLPRLFAFAQLLFKVKKHLPNWERSAAVYLLYPMAVMQNQGSGKLDRFDNQLIDGLVALHSQTHGDIRQEAAIADMAEELIKCKGAAAASDPRLLQLLPQDVRGKYLRAQVLEAF 1793 G0SB44 Nucleoporin POM152 POM152 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SB44 UNIPROT G0ZGV5 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}. GO:0016021 GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MSDAPAVGAFPQTPVAARRGPARPSDSTTSTTIKRTSPLPLAPQAGRQATNISPVIPLHILDAPTQRFYAFAFYLALTAWKLYDWTQVLEEDTESFLLFLKWIAIDCVFLFGLPELRIPWLELSQPFVMVAFAIHAMFDWILMFNIGFPWQSWVIGLLKVFYDREIAISEHNVKLSSILQNSSLIMGRQIINILPEGSAILNPELQPFCLGGDRKTANIPIFFNSTIPVEVELIRTDFETGQQESIKLSKSQLRDIERRAKRESQDGDTVQSIVQFDFPVKKTGAYRLGRVLDEYKLEVQRRNPLTFVVSCPKAWVGPALSAHRCVGDLSDLSMMVEGTPPLKIKYSRMINGKDHSFHFQSLQPEGFVSPLSGLRSNNWGYDEDDISWARAQKVPVGLNESMHSSGDWQYSIDEVQDGFGNIIKYDSLADDPDGKPKPKHLTQSFVVKKRPVIRLEGCDLRHPLKVAKGKSKNLPVSYGLSGGSREDSTYQIAWQFSPIDTLTESGDHGDVVTIGTYTAKNNRDRPTISAPGLYTLKSVSASQCEGEIQEPSSCLLLNPLEPRLSLRHEEIPDTCAGNSIGLRVDLDLIGTPPFIVRYDVISNGERRSERVSIPGLRYQLDLVPRIAGHHKYIFTHVGDSIYDGQKLSGPEYVLEQDVKPAAAALIQHSTGKMSSCLGDQVTVDILLLGDPPFTLEWELIHDGKRKQFKVPNIQENSYQIKTAPLTTGGEYTLGLTSVQDKRGCRNFLQEELKISVRRQSPRAAFGQVDGKRKILAVEGSSVKLPLRLTGEGPWKVYYANLHDGSPDKPKVQEKIIKSDNGFLEVRGRGAFAITDVWDSQCHGVVDPKASRFDVDWFPRPELSVALTHGVSKTETGFQLQDVCEGDVSGFEVALKGTPPFTVEYEVRHHPLQGSSSLSKKKIEGVVGKEAIQADTSKAGTYTYKFTALEDDLYSSNRGFQPIIVKQNVNRKPTASFVKPGQTFKYCKSEQDNEDGIPITLTGVPPFFLEVEIKHQSAAVPEIYRTPAIDSHSYELKIPRHHLRLGTQHIRIRDIRDGSGCHSTSGILSGPSVQVQLFEAPTIYPLETRTDYCVGERISYTLSGQAPFEVWYTFNGVELKAKSPNTNFRRIAESPGEFTITSVSDKASECRAPVSITKTIHPLPAVRISKGKSVRVDIHEGGEVDILFEFFGTPPFEFTYTRSTNARKGQKSQVLETRHDISHEHSKVIKASQEGTYEVVAIKDKYCSFSTQAVVGLEGGKKDKTKKLKVY 1270 G0SBQ3 Nucleoporin NSP1 NSP1 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SBQ3 UNIPROT G0ZGU1 PDB 5CWS Pfam PF05064 Pfam PF13634 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}. GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MSFTFGQPSTSGASGQSNTSTAPASGGLFGSTTGSSTPAFSFGNTSGTQSGSLFGGATTGQKTSLFGNTSSTTPAGTPATSLFGQSTSSSSGPSLFGNASKPSGNLFGNTSTSAAGSSTPAGTPSLFGSKTATTSAGASSTTPAATAGSGSLFGSTTATTQGSSTPTSTGLFGGSSTASKSLFGSTTTPATGTSGSQTTPAKPLFGSFGSTTPAGAPPTDATKTAGLFGNLSKPATTGTSTPTLFGSTSATTQGQSSTPLFGAKPAETSTTTAASGAATPATSAPASTTPTLFGGATLTSSAPAASTSTSTATASTPAATKPLFGATATTSAPGSSTTTATPGLFSTTPATTAAAGSSTATSTLFGTKPATTTAAAASSTPAATSTPSLFGSKPASTTAPASGTPTTTTAPASTSAPATTTAAPTSGASATASTTTAGQDAKTTTAGLGASTVGPQSQLPRLKNKTMDEIITRWATDLAKYQKEFKEQAAKVMEWDRLLVENGEKIQKLYTSTYEAERASNEIERQLSNVESQQEELTAWLDRYERELDELYAKQMGSAAGEQAAGPDQERERTYKLAEKLTDQLDEMGKDLAKMIKEINDMSNTLSKGSKPDDPLTQIVRVLNGHLAQLQWIDTNAAALQAKVAAAQKAAGSMGANVPGTETDAAESFYRSYRGGLK 678 G0SBS8 Nucleoporin NUP159 NUP159 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SBS8 UNIPROT G0ZGT8 PDB 5CWW 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}. GO:0031965 GO:0005643 GO:0051028 GO:0015031 MAFSFGNAGGGGGGVTQGKDLEVIQTEGLGFLALAGDAKVQLTSKWSPPPAPTASLLSIASRKGLVAAAGPDAVHVATTESVRKAFLAEKNGDSEVRPFNPEAKLPLPLRISQLAFTADEQYLVLSAETGGGLRAYDVNSLTQGNTQSAFELATNGETLRQLAPNPMPESAAFCAIVTTNGNLYMANLAERTLVSGPNGPTLRSQVSCAAWSTKGKQLVAGMADGSIYQMTPDGTEKAHIPKPPNLGDYHVSSVVWLENNVFLTIHNPTNSTNPDDKTVYHVITRQQSSGSPPNFTFQKLNDPVEPFVADKTPHHTVLRLKDFPPNLQDLLLVSSTAVETIGLLTRSKTPLATDKPADAITNVFTTTELADDSRRAQLPMSEDMMETYPIGVALDLSSKEKVYKPIPTDEEIEYSPGPLPGLWVLNNEGVLASWWVVYNESIRAGTTYSGIGGSSEVIPASPAPALASSTAPVPAFASPVSKPTFGSPSPATPAFGGPSALGTKASPWATAGGAASSTPTFGQPSFGKPAAPAFGQASFPGLGQKVSPWATGSTTSAAPAFGQSGFASAGTAPGKVFGSSFTAPSSGGFASFATKSGFASLSAPSGGSSIFSSKPGAPLTSAAPEVSMDTDTAFPPPSTKTDKPAFGSSPFVLGSTFKADPTAAHDIEKPKEGESKSLFDTGFGLSLEDAAKQPASAAESKDEEMRSTTPPLPPPTETKPKSIFESTTPTTTPAPQKFEFKTTTPSGFSTLLGSTKPVASSMPNIFATPKPTSAEKPKSIFDTLKPKEESKENLLKASEPPLPPDTTSKAVFQPGSSSSESAESSPGAAAKAAFKVGNDETPKPQKELAPKPEAVPLPPDFVKAKPKTEAKETKAEEPAVSPNLPVKPLAKKAEPIPAVPESASEEEQGQAEEEEAESGEEEEEEEEEGEGEEEEEEEEEEEEEEEEGEEGEEQSEAGSEGSGVDVAKDLSPTAKFGSMTPGYTPHTSLGGMAESTFSTISRSEVAEQSRPLFGEITKNAPPLFPAAGPLPVSPRSPSPVRGVVRSSILRPTETPRPVDTTPVPSRKGLLQKTASFGMSTGQKPAVDPNVKAQRKLAEKLKAEEQVLVDPEDEGIQQILQSKVEPTLRMNEFLAVDTKLAPMKPGRDDVPNACETLWRDINRMIDRLGLNSRSLQSFILGHTSHGKPGGRQKDDLEKPDDWVLIEAYDLGDMIDNKLARELEAGRIKDVEGTMAAIHNLGRDLAKLRAKEEDLRKLFNAQVDPDQIALTKALPLSAEQLAQQNELRRSYASFSKLLTEAEEALTVLKAKLASANAARGRRGAGAAQVPTVDAIIRTINKMTSMAEKRSGDIDVLESQMRKLRIGSLGPAGTPNGNGVGAGTVVPATPGGGGRSRESSPFVTPQSSRRAMFMSPGSVGTATPRGLLAATGTPSPTKKKLSMYTAEEKRELRAREAKRKATLRMLRESLARVGPNVVRLRDDD 1481 G0SDP9 Nucleoporin NUP152 NUP152 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SDP9 UNIPROT G3EQ77 Pfam PF13634 Pfam PF00638 PROSITE PS50196 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}. GO:0031965 GO:0005643 GO:0046907 GO:0051028 GO:0015031 MDPPSKKRSIFGGITSLFRSSTAPPEDRKGKSTNSNSVTANAPSLPPPQPESNGASSPFSPAKRASEAQLSVRKIIPKPQGPSSKLSQSVSASEIAHRPAPSTPAPAAATPVPKRRPGDNPHKLAASTSTPALQNLPNPPAPATSSKATSFSGAPSTPRPSIFRNSLYARPAPATTYTQRVSSHPLTQSFPPVTPGRPGRAANVDINNRILSNTASTELFPMKIPEPPRHLTGEMLAKEVPEDPNRAGSIYADEYLAHLCPPEFDDLQRRQFFCILDLRRLKYAADEVFLKKDWKINILNFAKEYEKSRSLIMLRYGLYEFKTVRASEAVKREWKLKHGIPDSDDESGAPAKTNGGGKRKAEEDLEPSSSTFTHTASPNKRARATEAPATNKRKANDELEEESQPSKLQKPGSPSPAKTPSATKSVFESIANKTASPQTAPKSSLFSSSTAAKPNGSIFDNAQKTPATSSNIFGHLSDASKDEDNESDTGSEAEAEDETPAKKKKKTTVNGASSSAPSEGGESTQSRSIFDRITRDANGQPVRQLPEGGLFSGESRKRSLSPVKELPANNTWNASAGIKFATPGTSSIFGSSNPKPPATTDTIDFAASTTKKPEEAAAPAEAPKEATPTTNLFGAQTKATEEAPKPAATNIFGSTTNPTETSIPAGSLFSAKPATSTTNSLFGATTSAAGQKKDEESKPTEAAPAPAPATSTLFGAKPATTESPKTNLFQFGTPNKTETAPATQPQFGGLFGKPPSTETPTEKPATTSLFGTDASKPATTSSLFGSATTAADKPAATNLFGSTTTPADKPTTTNLFGSTSTQATSGSDEPTAKKFAFGGTTESKPTTSLFGSTTPAPATSTENKGGLFGATTTSATPATNTKPLFGSTPAPAQENKPLFGSSTTTAAPVFQFGSTPASTSTEQKPLFGATAATDSKPLFGSTSATSTEQKPLFGSSTTMTEQKPLFGSISTTATEQKPLFGSTSTTEAKPLFGAAPASTEQKSLFGITPSTTENNPASIFGNSSTSTEQKPLFGSAPASTEQKPLFGSTPSTTENKPAGLFGNTSTTSTSTPLFNFGSQNTTASQPSTTGSIFGSASASFTFTAGGSDGTIKNPFASDGSYSAPTSFNFGSGDSQSSSAPFTFGAGGGTPSFTFGASSDSSNASNNASSAPIFSFGASQPSSTPLFGQNNPPAASNIFASSLAPVGGTSTGTSKHVPSFLESENKASAYSSLDSPFTFGGASSLATTPAASTPEPSAANAAAAGEDQGASADADEQPQEQISLTDGGPGEEDESVVHEVRAKAVKLVTAADSSADSSNGSGEKPAEKKSNSPWKVMGVGPLRLLKHKQTGAVRMLLRAEPRGNIALNKLVLPQFTYKPDAATPKFIKFAAARDDGKGLETWMIQVKTPQLAQELAAALEEHKKANEKKDGEKNEESEKKDEKQEEKKNEEKKDEKEEKKDEKK 1463 G0SDQ4 Nucleoporin NUP85 NUP85 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SDQ4 UNIPROT G0ZGU8 Pfam PF07575 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}. GO:0031965 GO:0005643 GO:0051028 GO:0015031 MFRVPDDSILSSSPAPSTPDKSRRAGSSNLFRDSTASSAASTTPAGTPPVKFLGSSIMRPSDKNASSSVDDDQPAVGLFTGIGGGVGVGMGAGTGATAAAKAAKKNLFAAVSGERRRNVPLGRSGRGHDSRQPSRLRKSIGVDDLEDEEEEEEKKKKPQLLKPKGKVQEKKKDEPVRGLFTGTSLAPPPLSKAAAAATTTTTTGPTKSFGLTYEEFGESEEEDSGLTGGQDAEGELDDSMWLERSPERPAIGDESDLLLMATPAATERVRREAEDIFRATAMGAGATTRRHEYRYASLAKDVYTQLGTAPLVEPPQLILSTEALLEQLYDEGVGTHDDDARLDETLAAVAVQLINLWQDHVDAIAQPEEDGHVADIGPGPRASPFEKAYWLATLALQLHHTRALDGGVEPLPATLFQWLNDRHDMYAGQVEEILRYRPSPACHSLFWQAVFMSLLRGRVKDATQLLRRAGWEHVRRGGQQRGEYAYSDRALENVLRVVDETVSVLESCPGYDGNWEIWSSEWTLFRVRAQGALEHLRRFAEGKDTSFGDSLFGSSTGSNRGYTGYRDHTLAGLARRAESQVPWDVYESLNVVFDIVLGQQASILEAAQDWLEATIGLFGWWDERNNNNNNNNNNNNNNNGYQKPGRTQALVLHSSPAHHINNDSESYLDRLARAFHAAVASDFHFNSQNPVEIGMACIFEDNIKGVIGLLRSWSLPIAAAVAQVASLGRWLPPHRPKGMYALEDLDMDDLEVLGVDPGAPDEVDGVKDSTLVQYAQALVEYEGLETVRDRAGVYREGWELAISVLGRMDSPERSEEMVRDIVEHLVQGLTVDSTETVDRLWTMLNELSMITYAEEMTETFGDILARESHRYGEAMWYYALAHRPNKVREVMNLLISYSLIQSTAFPPAADLDDYLHRLLSDRKHTLEQYAKQDMEAAELLGKMLSGYAALRQFYDIRDNVDATSISPVSRRQQAAAALISVIASSDDNIRGGLVDQTRDGIVSEDFLLALLGEALVFVSNPDNTFVHHGHAAVPILSQDQIDVLLKAVEDLTAVSERVYNVCDEFLQLVLASAPGGALKGSKPADLLKKGQDGQQMVLAGSSLIASQLQKSLLGGSGSALGKVPVKRGWDWREGMPAKMKGEDVIRRLRLGLAKDLARLWLAEADALVW 1169 G0SEA3 Nucleoporin GLE2 GLE2 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SEA3 UNIPROT G0ZGV3 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0005829 GO:0031965 GO:0034399 GO:0005643 GO:0016973 MAGLFGTTTSTTTSTLGDLKNDVELGSPPEDSITDLSFNPNPNDPKDFLAVSSWDKKVRVYEIAANGQNQGKVQMEHEGPVFAVDFFKDGTKVISAGADKQAKVLDLASGQAMQVAAHDAPIRCVKYFEAGGTPMAVTGSWDKTIKYWDFRSATPAGTVQCQERVYTMDVKENLLVIGTADRYIDVINLKEPVKFYKTLQSPLKWQTRVVSCFTDSQGFAIGSIEGRCAIQYVEDKDQSMNFSFKCHRDTPQNNVTNVHAVNAISFHPQHGTFSTAGSDGTFHFWDKDAKHRLKGYPNVGGSITATKFNRNGTIFAYAISYDWSKGYQGNTANYPTKVMLHPVLGDECKPRPSVKKR 357 G0SER9 Nucleoporin NUP84 NUP84 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SER9 UNIPROT G0ZGU7 Pfam PF04121 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}. GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MSPAFNIPDSIESSRGSSQSPHHGLNPEEMADIEATSQDNAVRVGEEIDYFAAQLDRYDADQTGSPPERRSRAFQLVDSYYTFTRKRLDRLRERQARQRSAQRGSWQRAGSIEMDLDDADEENDDILDEELQQLEDEVQIWDLLRRILPLRYHDATQNQKKEHDGSTKSRRQWWNEFMVSDSVARERKVVLEWLQNSASYGPPIDEVVSDLQHNAERGDILAHGWLHTRHKIKLQKSVNAYQGVLDPRDAAAAQSHLSSNSLITQLDPDAVTRQARKLEPQDESFERAIWLGCFEMLRRGCSMSEIREWLAVRTELWRAFSIAPLPLSNPDDEEQPDFDPVSLILWRRMCYAIATDGGTSDYDRAVYGLLAGDIPSVEKVCKTWDDVLFAHYNALLRTQFDLFLIKHGGDAAAKAAQQFPSFNAVAYHGDPATATKRLIDSLETGMKTSAEAFRPAKALQAAIVADDLDKFLFHQGLLLSIRANKKEKSKLIPEYPFPHESFSDKKYYDLGDHQGLRILAHVLIIILTLDRLSGVAKDKGPLQARHQAAENSIAAYISYLRLVRLEEMIPLYCSKLHGPRVYSTLSRNLIHIVDIDARLHQLTIMRNLGIDVSEFVKSQPLIYLDDVQDELVSCDAKDQFKILEDGPATLKYGRLVKPDFFGDDADYVDPEDDALIRSMEWLLLVPGLFVETCAYAVRIYKYFLKRTRLRAARAFSRRVRGHEIIRTKFPNLLKDVDENDPAAWFEEFAAAQLPSDLLESCPASQEKLITITRHLWELESLVRALDSIETLTSLAALTREESVPMTREMWQEVSQTVRIAKACMRPVLKEWLLTTYDGRSVEQDFLDIRQAYIPETILAYISCLHFAGTSLSRDNLLECMDLAAIIAEKDSDVAKEFMRCGRMKELVEAFASASKALAIWSGEKKGSQTNSKKLRELGWSRELWSIKS 948 G0SFH5 Nucleoporin NUP188 NUP188 759272 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SFH5 UNIPROT G0ZGU5 PDB 5CWU Pfam PF10487 Pfam PF18378 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}. G0S024 EBI-4325173,EBI-4325194 G0S156 EBI-4325194,EBI-4325171 G0S4T0 EBI-4325194,EBI-4325187 G0S7B6 EBI-4325194,EBI-4325479 GO:0031965 GO:0005643 GO:0017056 GO:0051028 GO:0015031 MATLTDRTYLPPLEDCLTGRTVILSWRLVASALEDADLARLTSPALSTFLRDGFVHELLKHPARVFEPKDLKQEFETKTSSIQTVAPGVDTIKKDALWLADAVAINQVAALRIVLIEYQTRAHSHLVLPLSTQDVANIQEAAGVGDAHASSILSLLNPASAVDAETMWCDFETEARRRERILATYLSERRSFTAAVDALVTFLLHSAPGQHKDLDSLRRALLKDAFAFDEDLDVPDRSKLLTMAPTYMNLVEDCIARAQALPAKLGESFKTEAFELDWLRTAITEAVHSLSIAFQALDLDTPYFAPHELLSEWFELMNSSLFLESILGFEVVADLAMPARSLVSAICLKMLNIDRTIQFLHDFDYPDGEEPYLLSSQTLNKIHTAVTNAVNSGVAASLPVAFAWSLIVHQMHLGYQERAERRDLLVNQRAQAGFELEFQPSASTPNRRRRNSAGSIVSLEASPYDDFLREQRLDNDIAPVEQIAMLATSRGQVYQVMSEMALCLGTTHEAAFRPAVGARARLVFQDLLKRSAYLIPYQDEPVFSLLAILATGRQYWDVTDALSASSLNQVYTDMLDDETLFTQFTMQAINRFPYEFNPFSVLCRVLAAALITNKDKADVVTGWLWRTPTLTVDWNPAWDRSYELCFEDENTNSFRLTRDVDLFGSASPARPRHLAAEERFIIPEGTLGRFVTDVGRTARLEFEHSALALLGKRLEVKAAEEICDSGMAPLDVDEQAEAVAMLATVLRAESLKSTAKGGDPEAPLKFLKEASRLLPHNKDILTVISDTIDGLVEKELLELDGPQIAVLASCLQFLHAALAVCPGRVWAYMSRCALIAGDARPGRLSRITGSLDMYAERFDLLSSAVKLFAALIDSAACSAVQRRAGSTALVSVRSAVENPWLGTSEKILSRVALAIAQAALDVYESTTTWRFRSELDRSILVRDVVGLMHKLVVHAHTLSSHLTSTLSPAAAHIISSFLTPPPSASSLRFQPLLGTLLVALITPRATLYPGQSRILAERVTSVLAFCTSLLRAADFLGQTHIPLQTHLFQSACLLARLPAANAVYRAPVLELLRALVEVAGRAANGSGEPPSLLGYLGSHAARSFISLVEGIDKPFGRVEHAVVTWRFFAAVIRNRQQWMAGCLLTGRTPREALKGGGEQKIERKVGEGSVLAAAMERLREVKSLDVQEAVAVMDFVVSAQNYWPWTIFAVRKEKEVVDALRGYVRGLKAPGMVMKTDGAAAAAFQARIAAYVAETFAMQLYHMRQMRQAEKFAGELVADLDYFLREGVMVWGYNASLHGNFARNFAKRFPGVEVDDFKRTMWLPRELGKGYYYALEVAEQMLGFDAGWGGVKQSGFRKEMETANLNLSLVEAQVSLFHAWEYLLLELTLSLLPKKENAAFARQVLQVVEQCLEANQRSQPPENIFVVLGHARAGLALTLLQRLADANQLPRDVTHLLALVSSAIHAVENPFGANDLPYFRTLLKILFVVLRAAKQGTAKPGESNVAITQQVLTILDRVVARCFRALAALVHEQQQNATDGTTTAPEDLALITAILQACLSVPGIEQCQVQVLNIMAAHDVFQVAVALFSWADRLLPANPSPASSSTSTSATNPASGDPVYGELALLFLLELSALPALAEHLACDGLLGHLAAARLAGYMRRTNVGPFAENAGAARCYAIWAKCLLPLLLNILAALGSTVAPEVAWVLNQFPNLLQSSVERIEPPGFSRPTLSLASTPPRQKFISLLEISEIHSLALLTRVLAACRAQNARDVPEVTWDGAKVLECVEYWLRGRKVLRERLVPLGPREVEWRGMVATGGVVGVAGDGGEGCENRLEEKAVGLLVGVREVLEGGLEGEGE 1858 G4SLH0 Titin homolog ttn 6239 Yes SL-0178 SL-0182 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}. UNIPROT G4SLH0 UNIPROT A7DT28 UNIPROT G4SLD6 UNIPROT G5EDP1 UNIPROT G5EDT5 UNIPROT G5EF69 UNIPROT G5EFF0 UNIPROT Q65XY2 UNIPROT Q8ISF3 UNIPROT Q8ISF4 Pfam PF00041 Pfam PF07679 Pfam PF00069 PROSITE PS50853 PROSITE PS50835 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. G5ECY0 EBI-312458,EBI-2914644 GO:0031672 GO:0031674 GO:0031965 GO:0051015 GO:0005524 GO:0046872 GO:0017022 GO:0004674 MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSEITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKCVTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFVNGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRALGNNGRNSRQAVNMFELNYTQRSSSVPRGVRHLESHIEVSNMTGEEKKTQQQTRTDAASIVESRFHPQPPKPPRAGTSRRFLPEPPKFVTTLPSVITVNAEEKLVLSVDVQAIPAAEFAWHVNGFEVKKSQSVVLLDEHNKSTLVLHPPVKQGKYKVTARNDVGSDSVTTQVTRIGEVKDGAGSEPPDIVESAVTVTCSHEEDVGSHSSLQTVRRIQEMQEEDEVDPIKPFIEATSPKVKESVEHPFANILNPKKREERLSPSGKGKHLLFAPRITAHPSESVFKILDGSPLKLRVMASSLPPATFLWMLNNFELRSNQNVTIRNDEENSSEIEFQKAPNGNVTVSAKNHLGEDRWTGKVILQYESPPPGQKITTIEKVTESWTLEEAVITQVVPTAADPGDRIVIIVRFDENKTSNCQFNWTINGVNIEKLEENLVAVESTEFESSLIVEKLEEQLCGEVVCVVKNQHGEVFSSSAHLRIRDDDSSFEIVPPNLPEECAPKIVEPLHSASFLDGQAMSLRCKITANPSAAVVWSKDDVNVEDWVLNKDVTTTVLDGGVCELLNPECFAEDAGLYKCTATNPHGTAETAAFINVEGAEYIKDHEEAEISESVLTDDVHIILPPKFIETLTAETDNFQQLGYVRMVATVRSVAPITVSWQKDGMDIYENEKYEVMQFADGAQILTIRAPTNLDSGVYTCTAESEHGVSNSSCQVELTISAESSPESFEKVEITPPEEVKETGIDDDIEVILKEEVSGTAQIEKREEEFKLLVKVADQVASTLVANVFLEAVHEAVKKIVETEDEEEDNQIEATQEPRFETSTDEYHVKENGTIKMAATISGHPTPFLEWYFGEEKLQVSQNVSMYYEAGTSAIILKNVQKRQGGNYFLRAHNCHGESILPMKLTVDPIEAVTHVLETSIPKVVVEQDAKEEEVRRAAEIISEQFAQLWVQDAQTEAVSAQAHQTPVVAEQASEEPTLPEVVAALQEQKPSVEKAPQPQFEVLETEDQDVVEQMQKQLPPVQKSMSVQEEKASSQRTPSPMNYEDKVKTIQSNLLRVNSHEAMEPIEATNLLLNTALQLKNEHVCDETTTVIVTQQPQKYDQLVTVVESNIEYHALRLSTSSSSPLKFIDLETIIQKPSTSCESIDRMFVEKSKRTANAQHRIVVLQGMSNTFHNAITWSLKKVKKLVGDAEAKAYADVEVVKQDETNEQVMTIIDNDTIVPQLLQVAAAANKLKLENVSVALIKEGDRAHQELVIEYESSIDEPMFEPVHNTSHLTFHQQQPTGPDQHVWSRRSKFEEDEAHVVAVFVEVDANCPDQSVEIVATVNAAYEGDNRQGIEDEPFTEVSQSLATESSAAPQAPKFLRKLVNCFGRIGEPVQLKCLIAGMPQPEIEWTVDGDPIVPNDEYSIVYEDGVCILRIESTLIEDEGEYCCTASNVAGTTFSKCYLKLSEADDDAVDLLRQLSEIKIIDPTLSTGYPMSMISDEENTSHQLLSNVLLTDKEVPITATYNEDLSRAESFRRFFESAETTVKVTELYQGESVEAQFQQPEKREQVSTSNTDVMFVNQKVDVMESTVSTVGNAVRQSVSSSTNSWDYMFNDPFPESQEINVIENELYEPRVPLLPQKLSYKGQEIFANTNTVERNSKAGAKAKGEVENLKKCVETLLLFDAEMDMKDIKESSPKKEIISKKDQQSLDDQIKVTQQILKDVERDLNKMERTSPGKSLSPNKRTFAPKDVEDIEAAIFSISDQLADRQSSEEALREALQEMILSNSSPMKELSRNNETSKPEVLKSEIQKIPEVETKISEVYPIVKLKQAISAIENSLLEDTEVTEIMKRKGSDKDKRKATRIKRVPSAHSARITPITSNLRDRLNQLHQLTVSEDSGSLKQNEEAKEIQELFVKIEKEINTIAELCKEKMTKKGADTVTHVLNSVLQHVASIINVILVAQDHQPIEVHAETTKTAEVSVWYSFDVHPESEDIIGIVDEEPTNRRPSSTPRGSTRSSNLTTSQDSQATTKMTVSSEDTIEAPIAPPRKGRSLSRDAERLLEIQPRAPPRRSRQSGDTLSPEPTPVLTLVKSDETPAPVRPPRSRSRHSGDELAETSPEAQPIRPPRSHSRHSGDELEEVQPVRPPRSKSKTADANCLQIESMDESQYSLSCIHIQKTNFAFTNSTHETSNASVVVDLRNMAQLECTVQSLDDLASIQMLCEESDYPSDTDRSLLLAGTVRYFNRASPSLHEVSPSLNMESVSMDLKPETEPEEIVQDVYVNVELHSVPSLSSLVEVNPNTLMQTLASEKSSLKAAEEDEKEGEEEGEEEVTADVSFIGRSVLSTETLDVVLEEKDMSQMNSTLPLDYERAFSSNTIRETDILSDESITVDSSYHKSPEPTVDFARSQVKSEEVTENFSLIHKPARRRVTGIVVNSLIYTIAANIAEDNTFDVDVVQEPQRYNISIKVIEDIVDFTSLTIMSDCEDDPPADVLVLKQDTSKLQALSYDDISVATTRTGITVSIVARSLNDGIYASLEEIAWGEVEMTVPDIMQMSTEEKSSLQFNVTVSESNLEEAKSLKSQVSFRSSQNSVSEMDNTISSTATISIPSYVVKLESTATITCELNNYLPKNCTIDWYCGKTKIIIDHEQFDRISHDLLEVLIIRSVEAINGNLYSLKINEDLFPVAYLIVENTNLTTSANILTRPETQFVMEGQPTVITVELDDPNVIVNWLKDRRPLHENERIRLETDGQGNHRVIIPNTCVGDQGTYLALTSSESVAITLVVEERIEEKEVMVIASGTESEEDDVQEYLVPPGSTATIACELEECELKRSIRWLRDGKDIRFEQGKTEHVQNGLKHYLVVHDATSLDSGLYKTERSEEQCEETIIPRGVVATIQCQTSEPQESIQWSKDGNIIPSDISRFEFRSLDNNQSHEMVISNISWSDAGVYSVLINGKSSFVSKIVVVESELITQSVEEEPEAEPEIDVSLHIVESEQIIELNVPQSPKLGASHETLVPIGQDDIEVIDKQEAAPVVESIEETSSIGSEEFEIIEKFTEEEVPKVAEPSEPTQADVPKIAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPTQADVPKVAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPIQEEVPKEAAPSEPTQEDVPKGAAPLEPTQEDVPKEAAPSGPTQEDVPKEEAPSEPTQEDVPKEAAPSEPTQENVPKEAAPSEPTKDVPKEAAPSEPIQEEVPKEATLSEPTQEQSEVSKRSEPVEPTQIQQAASEEETPLEETNETVVQTNEDVKEAEVPENAEAQKVVDSSDLQVAASEIAHLAIDEAVLETSNQPSQFDSLQEQKPSVVHENEHVRSVCVDLTFSRDSEQIVSDVIVAEVGYDEDECSTIADTITSLSSSPLYTAPVFTERLPSSACFANSKLTLEVMFSGVPQPTISWLIDDHELVSDGERISIKCENGVSAIRFFNVDRNAGGFLKCRATNCAGQVETSCEIVAADEISVISDSSITSSTRPHFVVPLPERVTHTVNDHITIKCKFSGQPLPAAMWEKDGVLLDLQKYQVTTEDGTSILKIESASLDDKAVYTCTIANEAGCESTSCTIDVVDDHLGLQQTGLHVMCERDQNDVELDILVQSPNHLGVTFNFPPVNRTLARQPPYFLLPLSDKVVIDEKCTLKCVVMGIPLVIVKWIVDGVVVTEDDNHEIHFEDGIALLRMKNIKKDKSVVQCEAINCKGKVTTSCVLTKCGVEESEAGDLQKPSFVLSLKDTCTTTDHATLKCIVVGTPLPDVSCSFNGVTDNSKIRSEDGIVLIQVNDVTEEGIVVECTISNETGSSTSNCVVKIIKQEEKNYQRPIIVFNQAGSVNNERELSVKVGVIASPEPTLFWKHNGKSIEEGGDYYLIFEDGIGILKVFNIQDGSHEFTCIAKNEYGQTTVEIPVEIGLKTENKLTLVKTLNDIAVVDDIVQLKIVAEGDLPIEFKWFEDGQILEDDSSHKITVDKCISTLQLKLEETGTRIITCEVSNSSSKVNASCNVERVHNTVSDFVMTNDNSTRFLAVGRKCTRERNNTILKAVVVARENIGDICEIDGEKIPDAYIEGNSLSIKVDTLSKKLSNVSFKVSASEGKVFETRKIEIAQEDTDEENFEINYSLRIDEQSGNTTYTFENSELYQGNQSRELDNTERNFTVNKEKDESKKPSEVQPAEIVEQKDVPVQETSAPTVEKLAPVESKETPEVQAAEIVEQKDVPVPETRAPTVEPTVEKHTPVDSKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKHTPVESKEKSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPSVEPTVEKLAPVESKETSEVQQAEIVEQKDVPVPETSAPSVEPTVEKLAPAESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETPEVQPAEILEQKDVTCEEEIKELLTEVEVELFFSKAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLAPVDSKETSEVEPAEIVEQKDVTCEEEIKELLTEVEVELLFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAHEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDLPVPETSAPTVEPTVEKLAPVESKKTSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETTATTFEPTKEKLAPVDSKETSEVQTAEIVEQKDVPVPETSATTVEPTKEKLAPGESKETSEVQQAAIVEQKDVAVPETSATTVEPTKEKLAPVESKETSEIQTAEIVEQKDVPVPETSTSYVEPTKEKLAPGESKETSEVQQAAIVEQKDVPVPETSATTVEPTKEKLAPVESKETSEIQQAAVVEQKDVPVPETSATTVEPTKEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTFEPTVEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTVEPTVEKLAPVESKETSVESKETQADAKLKKEKDDKHKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEAAAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKEKHDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDRLKKDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLKKEKDDKLKHEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEKNDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEANAKLQKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKGDKLKLEDQTNQSRIFEETSIEVTSLLKCKQQAIIVSKSFALCERVVLNAEEPFTLEVFCNAVFVKQRTDKIGIGIIFERSGASKKDESRPDRLDDNCVLTDVTDGLSILSPPPKAKKHLKKKKKHHKKEKIAVKETEQDEKTVSHLKPEISGMERKRSNSGSSDIFVDVDIEAGEESIHTDALVDLNFYDYDQMELSIFEDYDSDDDSASIDCDVSLSNVAADDGIDVFPSDGDTQEVEQKVTLPKKHQSDEDVISKEEENLETSVSYGSIEETVSFTIGTGQSIIEHPKSHAVGQMNSEVIIKCKTSQPISDAKWFCNGMVLLPDEQVNMTVTGCEAVLRLVKFLPQNKGNYHVLIDGSIGSQPAILSGPVPPVILNKLTKPITHQAGKSFTYKFNFMGAPAPRLRVLSNGEPVSFDVKYEIYDNIASLYIPKMSKRDGGEYTVVLENKYGKDESDLHITMVDTPLKPRKAQLVALTDTSATFKWLPPHTGESDILHYIVMRRSTESRRWRNIGHVQEKTFTAIELVPNEFYAFRIVAVNGFGEGAPSEIIEVNTLDYDQEESFDFAGEEELKLDDVQVNNEVVTEITIEESEVTIEEHRKLKKKSKKSKKTTDEPELDSEIALEVSSDITSSLEITTESTIPDTAPESQETLNVEIAVTETTVQKITNPSDESAKKDVNEDTAVSSIVKKDDKDVNKKSLPESGLTTKKEIQGKPEKKIMKKKTEKADSSISETSETLTKDLTQTKQSEPEPAKRTTETSVQDEVKRKTETTSKSKQTTEEHPQPGGKSDSSISSTSDASEVKQVQQSESEAQKVTEKPETAKLESKSKMTEDTTKESDNKETVDEKPKKKVLKKKTEKSDSTISETSETSAVESAGPSESETQNVAAVDKEKKQKETDEKQKLEAEIAGKKSTEQKSKLEAEAKLKRAAEEDAAKKQKEKTEAASKKAAAEKLELEKQAQINKAAEADAVKKQNELDEQNKLEATKKLAAEKLKLEEQSAAKSKQAAEEQAKLDAQTKAKAAEKQTGLEKDEKSNKDSGSNETVEEKPKKKVLKKKTEKSDSSISQKSDTSKTVAESAGSSESETQKVADATSKQKETDKKQKLEAEITAKKSADEKSKLETESKLIKAAEDAAKKQKEKEDKLKLEADVASKKAAAEKLELEKQAQIKKAAEADAVKKQKELAEKQKLESEAATKKAAAEKLKLEEQAQINKAAEADAVKKQKELDEKNKLEANKKSAAEKLKLEEESAAKSKQTVEEQAKLDAQTKEKTAEKQTGLEKDDKSTKDSESKETVDEKPKKKVLKKKTEKSDSSISQKSVTSKTVVESGGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAEADAVKKEKELAEKQKLESEAATKKAAAEKLKLEEQKKKDAETASIEKQKEQEKLAQEQSKLEVDAKKSAEKQKLESETKSKKTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSDTAKTVAESAGQSDSETQKVSEADKAHKQKESDEKQKLESEIAAKKSAEQKSKLETEAKTKKVIEDESAKKQKEQEDKKKGDDSAKKQKDQKEKQKLESEATSKKPTSEKQKDEKTPQEKAKSENETVMTTEPQQLEVKSEPKKSDKTETVEKEVASSTEKSDDSKTKEPKEKKKIIKKKKDTTKPQEASKELSSDESRIDLESDISLSLDTVTESDDLSTASTIKLQKESDESGIDSRMGQTSEAEDSPFISQPVSATVTEMAGEAKFTVKFSRKPIYVKWMRDDREIRVAYGKASVETTDDSSVLVIKNIDGKDVGNIYAVFDSEYRSAMARLDLRVPCKITLESSSNAPEIVAGKNLDLSFKISGYPLPTNIELLHNNENLRTRSDVTDFDDSISIRMKRLKLEDSGEIKIIGKNDSSEDQLRIPINVIEVTSKPTSLQVTSTERETVTLTWSLPTELNGSNVNEYLVERKTVDGGRWRHACTVTDSRAVVDGLFSGTEYVFRVVAVNGAGQSAPSDTIEATTQAEEEIDETVPTSPVEKVKEPVSKKPENTKESEGHKKRDRKESEDHDENNLGKSGKDEFATSGESGTSNQNEESAQLNTSFTSTEQHGQTEKQVRKGTRKSLTRSLNIRESDIDADVVEVEYDEQGDDIPSDPTTSGTYAFDKIEEEPARTSGEMAMAEKDSDAMEVRGLNKKLSKKGGKEGTSTEKSSSKTKKQEKSALSVQEMNKSLKKKGEKGEAETAASDFIENADQTGMSIQDLNKSMKKKVESGEATGQINDASNNKDADELSIQDSQQSLKKKSENESVTGEQLDKSQEVEDDKMTIQSLKKSIKKKPESREVSGGKSEKSKEKESDEMSIQQLNKSVKKKPENEAVTQGKSGKSQEQESDKMSIQALNKSMKKKDGVDGVEGNINIGRSDGDQLSVNDIDAELSTSEQVENASQNLGATADSDGDSLSLQTLKKRISKKGIHGEAESKLGEKQSGSDSFTLQDLYEELKAKEDAVEAGAETSNADQSAEKTSLEVRDMKKKMKKKQVSGTAENLIGESNRDETSMEIRDLNTQHSNQTGEDESSTFNFGQKDQEQYSMVMKDVSKKLARQNAEEIQSGKLIPTTNEEKTGLALTGKNKNLKKGEENEKTKFEAKHLGSSSASDSLAESTLRSKKTKKGEVEKSELSIDMKNQDKTTLATTLLEDDLAKTTSAEESEAEHLVALQNKEKTSLAMRRKRVSFDSSTKSESIEDVIPDKNRDSDKMSITGIKKKMSQKSESAEAQKNESPEVKEISSFEEKTLKSKKKSKADRNQGTEANLGDKTIDKDYLSVTDKNQSLEKSEASGQAEKSIKAPNKSKVTTSFADESLTSELDRLMADEEMAEMMFAEEEKAADLLNVMNKNKGLNKSEQEESQEISLKSQSKVKDSDSLSSTDKKIGLKKSDKDQKLGTSKIFGSKDQESVGYEEKTSNFSKQRRGVSDLGSDAMTDQKNVQESQYAEISADDHMSKTGADGEISATRTIVDGSDAAQGSEYAEISKKRKFKRAEQIGEAETSLCDSRENTHDSLSISDVNPELRRSNVEISAFGQIDLTAEEVTSLTDINKDAQLTKKQDENDAKKSVSKNLKAGAKKDSDTLSITSKKDKFGKRQDSREASATVEQQGEEKVTKNLKGSRGKKEKLGDAGIDVNFENQEEFASTTGDIESIVSEKGHDTYSEKTVKSSKKKSPQTAGAEYGGSESLNASSALSTTDVDAQLKNQEKDGVAESSIGKSNQKDSYSEQELNVNKKKKQAVGAAMNQGSGSTKESDNLAVASVESNLAKDSANQEASLHGLVDNDATSLSQLDSEHRLKKRDDELSAHTKLGKHTQSENIALTETDDSLVKGDSEESAELNIKQQGETAEDKYVESRKKTTLKKKPEQKQVTDTLSAVDGRHDTTSLSVADSGISFDKSMENELAGSGDGTASASVSAKVRGADGNAKTNLISSFEKPGQESKTSKTLSGKQKKQEKSSFAEKNAGFDLSMGEGKNDESVESSLQKNRDADSLALQGTDLAFSKPSDSSANAHLDMPQRELTLRICQAETVDWSDDSEVEEGTRTSAPGEVKKKKKFIISAISQDGEFSDAESITFDENGVRVEKRRRKKRDPKEYMGAGELAMRIPAFAKKMQYIGCIEGDVVVFTIKVVSDDVPLIRMYRNDFPVANFDKMAFEGFTKGSEHSFNVTINDIRKLDGGKLVFEAKNDYGVDKCTILLDVRDSGSFIEDYSEIHRSAEIQNSVGDVQVKEGETAKLTGRVDGFPLPELIWIKNGKEIDMMVPSTKYQLDYHSDGEFEARIANCTFEDDDDYSLLVENLAGVDSCNFQVFVDCNEYPDDEHFNRRRRLQRGRRVMEASSDSELDDAKKRKKRRIKRVVERRNPNAPRLTQLIPPRFDKILSDHDAIEGENVVMMVETLGEPEPQVRFYRDGKLIDDGSGDRMEVRHEDEMRKHWLILKDICKDEEAEYACQAINVAGEAWCFSDVVVHMSEESRDDDKSVDEVDDSTVLEEKKDDGDDKSKPKTKKKIIKKKETPESEQVTAAEPEQQKISEVDVQSVAETEVGAKKKPDAEKPTDLSKAKKDSKSKKSDEPEASTEEKSTTEKPTNDKTSKKSAEKKTVKPKKEVTGKPLEAKKPVEDKKDASQPSSSKESSPPTDGKKKKQIPKALFIPDEISSRFGDPSTMHSETNITTTIRGREGSADAKTPLVEPLSASVSMKVESAKEKAEFSFKRRSETPDDKSRKKEGLPPAKKSEKKDEVTAEKQSTEALIESKKKEVDESKISEQQPSDKNKSEVVGVPEKAAGPETKKDVSEIEEVPKKKTIKKKTEKSDSSISQKSNVLKPADDDKSKSDDVTDKSKKTTEDQTKVATDSKLEKAADTTKQIETETVVDDKSKKKVLKKKTEKSDSFISQKSETPPVVEPTKPAESEAQKIAEVNKAKKQKEVDDNLKREAEVAAKKIADEKLKIEAEANIKKTAEVEAAKKQKEKDEQLKLETEVVSKKSAAEKLELEKQAQIKKAAEADAVKKQKELNEKNKLEAAKKSAADKLKLEEESAAKSKKVSEESVKFGEEKKTKAGEKTVQVESEPTSKKTIDTKDVGATEPADETPKKKIIKKKTEKSDSSISQKSATDSEKVSKQKEQDEPTKPAVSETQMVTEADKSKKQKETDEKLKLDAEIAAKTKQEADEKSKLDAQEKIKKVSEDDAARKEKELNDKLKLESEIATKKASADKLKLEEQAQAKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAGADAVKKQKELDEKNKLEANKKSAAGKLKIEEESAAKSKQTVEEQAKLDAQTKAKTAEKQTKLEKDEKSTKESESKETVDEKPKKKVLKKKTEKSDSSISQKSETSKTVVESAGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQSHIKKAAEVDAVKKQKELEEKQRLESEAATKKADAEKLKLEEQKKKAAEIALIEIQKEQEKLAQEQSRLEDEAKKSAEKQKLESETKSKQTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSKSAKSTVDAAETLESDFNLVEKKTVQKVEQSPDESTSATIKRDPAQKTEEISKQDDGDEKKTTTDGKPPKPEDSEATPKKRVVKKKTQKSDSVASDASLADVSKLSDDVEEKPKKKVLKKKTEKSDSVISETSSVDTIKPESVEIPTEKAEQMILHNRFSTDSAVESEPKNAHKDDTEKTTDDMMTRRKSSAIFSDDEQSISSKTSSEGRRRRRRTGFASKFASDTLALRGDNVEIEAELLAEDDTVTWKVNGKDADLNSRCHEMSHTFFRTLIIDEVEPTDSGMEITATCGTESHTTILKVEELPVDFVKYLPRKTSGKEGQEVTISVTLNHPIDISKVVWLKDGKPLEINKDYSIDTVGCSVSLTLRRAKYEDSGKYKVVCDGVDCSTHLSIQGKPVLKNVSETKPVITVDKDDQFSLLVAYDSNPEASFSMTVDGKDLEFDGRSRIDVVDDGLKLTKRGVSKTDAGEYEVKLKNEFGEVAQKFDVKVNDTPSAPGDVSVVKAESDCLHIEWTAPTEDNGAEVTSYVIEKKESGRRKFHKVATVNGKKTSYVVDDLEIETPYIVRIAAVNKFGTGEFIETKPVQTGSPFQVPTVEFPPTIDNVTSTSCSLSWPKPIEDGGSPVYGYDVYKRENEGEWQKMNGEELVFTESFNVRALSSGKEYEFKIEACNEAGLRSNSNVVSKKLTVEGLVPEIILDMPMVKVLDNDKVEVTWKSDGEKEFVVQYKSDGSSIWASVDIGGPRSESAATSKCIIDGLREGIPYVFRVAARNQHGTGEFSEPTIPVVVLADDAPRVLKAIKPVKIPKKGELRLECHAAGHPAPEYIWYKDGKEIIPTDENTEIVNEGSMSALIIHELAGEDVGLYKVLVENIHGTAESEAEVGISDVRAHFNSSFSELTEIEEGHDIELTCEVSDEEAVVNWYKDGKKLVASDRVQFYAMARKRTLRIKGSTDADSGVYKCETTDGRSRTEGEVIVNEQEPHILVGPQDAIVKDFGETMVLFCETSKPVRKVKWFKNGVEIWPQMNKAIMENDGKRATLEIKNFDKHDIGAYTASVSEKETSAPAKLVFEVAPNLIIPTEIRDGVTVHAGNEFDFAVEFSGFPIPTIHLTNNGTPLKAIAVVTEYDDSVSVRMKDVTLDNSGTVRVIAESPLGQCIKEIPLKIIDKPSAPCDLQFKEVTEDSVFLSWQPPLETNGAPLTGYVIERKAVDNNRWRPCGQVKPTKLTFVAEDLFCNQVYGFRILAVNEVGESEPCDTVDVLTLESSEPVSESSELFVPKIAILRTPQVTVAVDETKVTLRWEECPETSLYKVERKKVGDSDWLEIANTDRNKFKDRSLTESGEYVYQVTATGIHAVSSPSEETNPVKILVPGSEMPASKTEKKTDAAKSESEQKSAEEIVAEKQVDQSQASESTTEAVEEKKTKKVVKKKVAENKGEETLQEVKEKLKKGKAVEKVQDESRRGSLQASSDNESVTTTSEKRSEAELEKNSEKSAEKKSTSADLEAADKAETEKSETGKETTEKKKKVVKKVAKKGLVKADKSKIELTAGKEGEISAQVAETGVSVEWKKDGKALDASYTVTSTGGVSTVKIPIVDVNTSGVFTCKVKSSEGDEEEVSIAVTVKLPEVPKVEAEQSIVEVKVGDVAKLSAKISEPASSVNWTKDDKPIKEDGNVKAQLSPDGTAQLTISKTDSAHSGIYKLNVENDAGKGKVEIALRIKGAAKGAPGIPTGPIVFDDVTESSAEFSWKAPENNGGCEITGYNVERKESKNKGWKQCGKTKELKFKADGLEEGTDYDVKVSAVNTMGTGSALEGKITTLKKKEETGKQKSEKSESDEKKSESDKVSELKQIGKPEYVSSTATSIALKWTSDNDEVTYTVQMKEANSKRPWAVVAKEISECSATIAQLKEGTSYLFRVIAQNKTGQTVTSEQSESIECKDTTESKKPAFTNAPTDLTAVKNGKTKITAEFTGHPAPEIHWFKNKKEIFSGKRQWIENIAGATSLTIGEMREDDEGEYKIVVKNTAGSVEHSCKLTMDQLPEINRVDRYASTLVFDKGETVKLRLSFSGRPQPEVIWIDNNGKVIEESRKMKIEKTVLNTVLTINSIDSQDQGEFALKIKNRCGEDKYAIGIQVTDRPAAPGKPAVEDQNVDSVRLRWAAPTNDGGSPVRNYTVEMCTEKGKTWTKAEVTKQAFITLFNLVPGESYRFRVRADNTFGQSEPSDESELVVVKNVSRVVEEPKKKEVKVKEQESVDYERVAKDSEPSEYKTIDIHRLPNDLQAKYIIHEELGKGAYGTVYRATEKATGKTWAAKMVQVRPGVKKENVIHEISMMNQLHHEKLLNLHEAFDMGNEMWLIEEFVSGGELFEKILEDDSLMSEEEVRDYMHQILLGVSHMHKNQIVHLDLKPENILLKAKNSNELKIIDFGLARKLDPKKSVKLLFGTPEFCAPEVVNYQPVGLSTDMWTVGVISYVLLSGLSPFLGDSDEDTLANVSASDWDFDDPSWDDVSDLAKDFICRLMIKDKRKRMSVQDALRHPWITGPLLSAFNDLSEYVKKMQPKLDKSGVPARQKRNFLSLKRWSDDLLPIGRLAKRGAIFRRLTMDGVFERNIAFDTDAAPSVKKQLEDIVANVGDLIATLSCDVDGVPSPKVQWYKDDKELTVPSMKYDSFYNEGLAELTVKNIVESDAGKYTCRATNDLGSIMTHAKLSVKADEKKKKKSKTSPAVIEKKKDRKTSKVVVIEEMIDMPPNFHHLLQDDEAKIGEPKILVVTNTTLPEPTVDWYHNGEHISINDSNYLRKHDKGRYELHILSVDSTDEGKWKAVGKNAFGECESEAKLTVVIPDGQYAPSFGKQLSDVKCSESDILKLEVNIQANPAPEINWFRNESEIEHSQHHRLQFDDGSGNYSLTIIDAYAEDSGEYKCVAKNKIGKAHTVCCVRIEELLSKRSKKIDGSKAPRFRMQLPTPREVPQGADLTLVCSVSGTPHPNIKWTKDDKPIDMSNKQVRHENGVCTLHIIGARDDDQGRYVCEAENIHGVAQSFSVVEIKEAVDKDHVRPKFLEPLVNCSTCEGNEMVLECCVTGKPIPTITWYKDGLKLIIENRMLQYTDRKGVSRLNIMNVVMNDDGEYTCEAVNSLGKDFTHCTVKVVDMGLSKTRLTPVRSRSRSRSRSPSVVGGEIQRPPVVTRPLADATVTEGNRELLEVEVDGFPTPTIEWYHDGKLVAESRTLRTYFDGRVAFLKIYEAHEEHNGQYVCKVSNKLGAVETRAIVVVEAPDAAEHVTQMPTFVKKLQDVVLKTAGETATFTCQSYANPAAQVVWLHNGKALQQTKSNYKTRLFDDNTATLVIENVTDELCGTYTAVANNQFGDVHTSAQLTISGSEAKKIAASLPYFIIELKPKINVVEGATLSIQADLNGSPIPEVVWLKDNSELVESDRIQMKCDGVNYQLLVRDVGLEDEGTYTITAENEKGKIRQNTEVSVTKSKEVKEKKEKKKVEKKDEGKKKPGRPGLPRPSGASKTEQVTMAFDAPSEGPADSYEVERRCPDQREWVSCGSTKSLELEIKGLTPNTEYIFRVAGKNKQGLGEWSEMTSTLKTASVGQAPQFTISPQSKIIANRDDEFEIAVEFSGTPTPSVKWYKENLQIVPDEKIDVATTSTSSILNLKSQEENGTFNCLIENELGQASASCQVTIFNKPASLQSTPDHSLERNLVPTLQKALNNESAQAGQQIMLTCRISSRSESTVAWFKDDERIESAGRYELSSDKKSNHKLVCHAVQSQDTGKYRCVVTNKYGYAESECNVAVEDVTKFIAPSFSATLSDSTAILGHNITLECKVEGSPAPEVSWTKDGERISTTRRIRQTQDENGNCKLSISKAESDDMGVYVCSATSVAGVDSTSSMVMIAKTTGTDSHLVIAQTADEKHEKPRFTRAPPSLIEVNESGQFTLIAKAVGEPKPTVTWLKDGREILRTNRIYHHFVTGDGESHLIAECVVSKTSGIFSCKAENPNGTVIAETQVIVQRMKPANQLANVAPKFTIPLTDMGIVNGHPTTLSCNVTGSPEPTLEWIYIDDSGHKINLTSSTTDWTECRFGKVAELKSERVLREQRGTYQCIATNSSGQATTQCYLLVGELSDEPAGPPRFVKCLQDTWTPLKESIEFSVELAGFPTPDLTWYHNEKKINEGKDVKITFPSDTTSVLSIKNVSLASLGMYFVEASNIHGVLRTAGRLNVSDERRKAEPPQFKHVLEPVLAVQPKVAFSEEHPRASSSAATARVKKGAAPMFLQGLEDMDLKAGASAAVAGKLGRKLRPHRSTTNDADKLAKALAQSLRLDEPRASIDSRPESAANAALDEVRAAINSRNKRVCRPKFMVKPKPRKVLEEYKSLRLKTAISGNPMPQVHWDKEGIILETGNKYSIYNDGDFYYLEVHHVSTFDKGFYNCTAANNEGIITCTSEIDVLPNKEDSAAQVAKRKSRKEAKAPNFIEVLPGRSQANLNESLCVECSVSAYPCASIIWTRNSVRLLPQADRYTMSYDGECASLKFISVTPGDEGTYACEAVNELGSAVTNMNLQVSGVDPNAAEGIPPLFRFEKIKSVRKVVDGSRVELAAELVQASEPLQIRWLRNKVTIVDSPSFSYSRSENMVFLTIADVFPEDGGEYTVEAKNQSGIARCTMQLDVRNNERSVADEAPRVFDFEPTTRSDPGVSVELRAKVIGHPDPVISWTKAGQKLNNEEKYMMRNEGDKFILRIANVTRADAGKYELTAINPSGQANAELELTVVQSTKTVGAKPKFNESPISVQTCEKNRAELRASFSGTPAPACRWFYNGNELIDGLDGYTITSSDTNSSLLINSVDKKHFGEYLCTIRNQNGEELANAMILSEVLSMFYSSLFLVVFVDIVAQCHVARLLHFLNEERFVGRNIFA 18562 G5EEH9 Nuclear pore complex protein Nup96 npp 6239 Yes SL-0178 SL-0182 SL-0185 [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}. UNIPROT G5EEH9 UNIPROT D1MN48 UNIPROT H2L014 Pfam PF04096 Pfam PF13634 Pfam PF12110 PROSITE PS51434 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}. O02333 EBI-6455549,EBI-328275 G5ECG0 EBI-6455549,EBI-320612 Q21443 EBI-6455549,EBI-314110 P91457 EBI-6455549,EBI-2004585 Q8TA83 EBI-331999,EBI-6455549 P91400 EBI-6455549,EBI-325226 P34402 EBI-1570073,EBI-6455549 P90900 EBI-6455549,EBI-322249 GO:0005737 GO:0000776 GO:0005635 GO:0031965 GO:0005643 GO:0044614 GO:0043186 GO:0008139 GO:0003723 GO:0008236 GO:0017056 GO:0051301 GO:0009792 GO:1990893 GO:0051028 GO:0031081 GO:0006997 GO:0030719 GO:0000973 GO:0006606 GO:0034501 GO:0090435 GO:0015031 GO:0006405 GO:0034398 MFGQNKSFGSSSFGGGSSGSGLFGQNNQNNQNKGLFGQPANNSGTTGLFGAAQNKPAGSIFGAASNTSSIFGSPQQPQNNQSSLFGGGQNNANRSIFGSTSSAAPASSSLFGNNANNTGTSSIFGSNNNAPSGGGLFGASTVSGTTVKFEPPISSDTMMRNGTTQTISTKHMCISAMSKYDGKSIEELRVEDYIANRKAPGTGTTSTGGGLFGASNTTNQAGSSGLFGSSNAQQKTSLFGGASTSSPFGGNTSTANTGSSLFGNNNANTSAASGSLFGAKPAGSSLFGSTATTGASTFGQTTGSSLFGNQQPQTNTGGSLFGNTQNQNQSGSLFGNTGTTGTGLFGQAQQQPQQQSSGFSFGGAPAATNAFGQPAAANTGGSLFGNTSTANTGSSLFGAKPATSTGFTFGATQPTTTNAFGSTNTGGGLFGNNAAKPGGLFGNTTNTGTGGGLFGSQPQASSGGLFGSNTQATQPLNTGFGNLAQPQIVMQQQVAPVPVIGVTADVLQMQANMKSLKSQLTNAPYGDSPLLKYNANPEIDGKSSPASTQRQLRFLAAKKGALSSSSDAQDSSFIIPPISKVMSDLSPAVTRSADVTKDLNYTSKEAPPSLARGLRNSTFNPNMSLTNRSVHESSALDKTIDSALDASMNGTSNRLGVRGSVRRSNLKQLDMSLLADSSRVGRESRVADPDALPRISESERRQDVVTSTPAVDPVQAVIQRHNDRNRDPPSLNLDTTCDEHTGLEPVSAATSSAASVVSTPSEETVNVNSAAGVKLTKPDYFSLPTINEMKNMIKNGRVVLEDGLTVGRSSYGSVYWPGRVELKDVALDEIVVFRHREVTVYPNEEEKAPEGQELNRPAEVTLERVWYTDKKTKKEVRDVVKLSEIGWREHLERQTIRMGAAFKDFRAETGSWVFRVDHFSKYGLADDDEPMDGSPPQQALQASSPLQVIDMNTSARDVNNQVQRKKVHKATDAHHQEIILERVPAPAALGDVVPIIRRVNRKGLGGGTLDDSREESCIGNMTTEFNESGHDSIIEEGQQPEKKPKLELLADLEYESSRFIRNLQELKVMPKANDPAHRFHGGGHSAKMIGYGKSKLIDIGIVKGRSSHVGWSETGCLVWSAQPRHNQVLFGTIDRTSDVNENTLISMLDVNVHVSETSRKGPSSQSNSVKSSLTSNFVTYSDSYSSMFAKYIDVAQAGGYDGHVSVWKLISALFPYERREGWSFERGEEIGEWLRTEAVKSVPDDRSADTSSNGVWNQLCLGDIDKAFQIAIDNNQPQLATMLQTSAVCPEATVHCFKAQLDNWKKCETLHLIPKETLKCYVLMSGLSHYEWDQDGKNHSINCLDGLNWIQALGLHVWYLRAWTGLEESYDAYQKDVNAGRAASNRGDLPGELIKLACESQHSVEVVLDCAAGENPNDYFLQWHVWSLLYSVGYRTMSKTSETRLHRNYSSQLEASSLSKYALFVLQHIDDDEERSTAVRSLLDRIARFTDNDMFDSISEQFDIPSEWIADAQFSIAKSVDDSTQLFELAVAAKNYLEICRLFVDDIAPTAVVAGDHDALKAACAMVRPFENQIPEWGATGMVYTDYCRLINLIENDAEEELLQDVLESLETRLHAPTISKNSLQKLSLQTIGRVLFEYRADKNTLPEWTKLLGHRQMFKIFRDRSSWGIERFTIEFD 1678 G5EEU2 Histone-lysine N-methyltransferase set-25 set 6239 Yes SL-0178 SL-0180 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}. UNIPROT G5EEU2 Pfam PF00856 PROSITE PS50280 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}. GO:0005720 GO:0005652 GO:0046872 GO:0008168 GO:0032259 MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPNNERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGWTCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFWIYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACENGTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGFGVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRFINHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF 714 G5EFL0 Poly(A) RNA polymerase gld-4 gld 6239 Yes SL-0198 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}. UNIPROT G5EFL0 Pfam PF01909 Pfam PF03828 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}. GO:0005737 GO:0005730 GO:0043186 GO:0048471 GO:0005844 GO:0031499 GO:0005524 GO:0046872 GO:0004652 GO:0071044 GO:0051321 GO:0006378 GO:0007275 GO:0071050 MNEDSRLSSSQQPSTSTPRSSIPSTMNSDEPNTCRRLSQSQEQPSTSRTCKSETPEFGYSDSLPFAPWRRKRYGLNIQGLHEEIVDMYHWIKPNEIESRLRTKVFEKVRDSVLRRWKQKTIKISMFGSLRTNLFLPTSDIDVLVECDDWVGTPGDWLAETARGLEADNIAESVMVYGGAFVPIVKMVDRDTRLSIDISFNTVQGVRAASYIAKVKEEFPLIEPLVLLLKQFLHYRNLNQTFTGGLSSYGLVLLLVNFFQLYALNMRSRTIYDRGVNLGHLLLRFLELYSLEFNFEEMGISPGQCCYIPKSASGARYGHKQAQPGNLALEDPLLTANDVGRSTYNFSSIANAFGQAFQILLVAVTLRERKGKNHVAMRAYKGSLLHLIMPFTSKELTYRNWLMSGVLSMPGQEAPASYDLNQLHNTLVSPMVDLSRYAWLRKAPAKAEKRDSRPLTIVNPADDRQTLAQQLKKQILEQTEAKKSLEKMPACDDNKKEEELVATRETDVELEAEDTESEGHHNGENDLILTGPPLPTSTQSVNTSATVSTAASISEREDTDSPGLSSSMGNQSSEEDEDNGINNRNNSAVPVQFKKPFNEVVAQPARESKRTQTTSEDKMQDQFHFNGYSYPPPSRYAAGTAAPSHKHRNAHPQRQRPSIRNLSQGSDGSDEYNVESWNNNIRQGRRASSNSPSPSRQQTNTRNCGPTNNIPYDSFRSQNKNSTLDGSNNSSEEPITMYADVVKKKSSITTSTNTSTADVNVTNGNPIPANGIIPQSMAVVNVGRGSYRNALTTSPMTPPSAHTSMQKQHHLRKDNECGFDNNSATSSTDLSHHQPQLVPPVNRLQR 845 G5EFV8 Vacuolar protein sorting-associated protein 52 homolog vps 6239 Yes SL-0198 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}. UNIPROT G5EFV8 UNIPROT G5EFV9 Pfam PF04129 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}. O01839 EBI-313277,EBI-318981 Q09501 EBI-318986,EBI-318981 P32743 EBI-318996,EBI-318981 O61975 EBI-318991,EBI-318981 Q20742 EBI-312606,EBI-318981 Q22227 EBI-316403,EBI-318981 Q22544 EBI-313477,EBI-318981 P91820 EBI-313618,EBI-318981 P34574 EBI-319001,EBI-318981 Q9N575 EBI-319010,EBI-318981 GO:0005829 GO:0000938 GO:0005797 GO:0000138 GO:0043204 GO:0048471 GO:0017137 GO:0019905 GO:0032456 GO:0006896 GO:0007041 GO:1904810 GO:1904811 GO:0090326 GO:0015031 GO:0042147 MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQLHNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDANDRGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEFLLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFSIGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVLKSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDARPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESKHTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECIQLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY 702 G7IBJ4 Protein CNGC15a CNGC15A 3880 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}. UNIPROT G7IBJ4 Pfam PF00027 Pfam PF00520 PROSITE PS50042 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}. GO:0016021 GO:0031965 GO:0005262 GO:0044325 GO:0005249 GO:0036377 GO:0009877 MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRINLWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELIIDSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEKAWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHFFQFGIFDDAVTLEITSSNFLTKYYYCLWWGLRNLSSSGENLLTSTHVAEINFAVIVAILGLVLFALLIGNMQTYLQSTTIRLEEWRIRRTDTERWMHHRQLPHYLKENVRRHDQFRWVATRGVDEEAILRDLPVDLRRDIKRHLCLNLVRQVPLFDQMDDRMLDAICERLKPTLCTPGTCIVREGDPVDEMLFIVRGRLDSCTTNGGRTGFFNTCRIGSGDFCGEELLPWALDPRPTAVLPSSTRTVRAITEVEAFALIAEDLKFVAAQFRRLHSKQLRQTFRFYSHQWRTWAACFIQAAWFRYKRMKETNEVKEKENLMMMSNVKYYGNDDSQYFSAPLQVPKGSSYSMYSGKLVGSLRRGRSMRYGSELDMLGTLRKPIEPDFNDDGD 710 H2KZB2 Ankyrin repeat and LEM domain-containing protein 2 homolog lem 6239 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:22770216}; Single-pass membrane protein {ECO:0000269|PubMed:22770216}. UNIPROT H2KZB2 UNIPROT Q5W7E5 PROSITE PS50297 PROSITE PS50088 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}. Q03565 EBI-6258914,EBI-2535603 Q19848 EBI-6258914,EBI-2414048 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0051721 GO:0051301 GO:0007084 GO:0042326 GO:0035307 MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGTPREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEGFRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRVLTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATVTVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAFLREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEKSINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQISSELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI 603 H2L056 UBX domain-containing protein 3 ubxn 6239 Yes SL-0198 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}. UNIPROT H2L056 UNIPROT A0A0K3ARL0 UNIPROT A0A0K3ATZ0 UNIPROT A0A0K3AWX1 UNIPROT Q6A589 PROSITE PS50033 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}. GO:0000785 GO:0005737 GO:0005634 GO:0048471 GO:0036435 GO:0044877 GO:0030154 GO:0042006 GO:1903364 GO:0045977 GO:1905634 GO:0007283 MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSSSRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSSGSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSMAIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKEAFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQRLAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASLAADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQTLINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI 613 H2QII6 E3 SUMO-protein ligase RanBP2 RANBP2 9598 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT H2QII6 PDB 4GA1 PDB 4GA2 Pfam PF12185 Pfam PF00160 Pfam PF00638 Pfam PF00641 PROSITE PS00170 PROSITE PS50072 PROSITE PS50196 PROSITE PS50005 PROSITE PS50293 PROSITE PS01358 PROSITE PS50199 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}. GO:0005642 GO:0005737 GO:0005635 GO:0031965 GO:0005643 GO:0005634 GO:0046872 GO:0003755 GO:0008536 GO:0003723 GO:0016740 GO:0051028 GO:0006607 GO:0043547 GO:0006457 GO:0016925 MRRSKADVERYIASVQGSTPSPRQKSIKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAVYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLESFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLREIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLARYDVGAIRAHDGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNAAKLRLLVQHEINTLRAQEKHGLQPALLVHWAKCLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDVVNGNIEDAMTAFESIQSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIKIIDDSDSNLSVVKKLPVPLESVKEMLKSVMQELEAYSEGGPLYTNGSLRNADSEIKHSTPSHTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVATASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQFAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQNTKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCVACQNPGKQNQTTSAVSTPASSETSRAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQSPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSPGSQVGTGFKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENDTGFQAQDISGQKNGSGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWTAYDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERTDVTQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNTSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPNKCELSKNSDIEQSSDSKVKNLSASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLEGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFFITLKKAELLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI 3224 H2QL32 High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A PDE9A 9598 Yes SL-0198 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}. UNIPROT H2QL32 UNIPROT K7AGW3 PDB 4QGE Pfam PF00233 PROSITE PS00126 PROSITE PS51845 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}. GO:0005783 GO:0005794 GO:0048471 GO:0032587 GO:0042383 GO:0047555 GO:0046872 GO:0046069 GO:0046068 GO:0019934 GO:0010613 MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCCQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQENFSQMDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA 593 I6V1W0 Protein brambleberry bmb 7955 Yes SL-0178 SL-0182 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. UNIPROT I6V1W0 Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:22863006}. GO:0016021 GO:0031965 GO:0061472 GO:0007344 MALWFVLLWVSSLQYAEVEAFFDWLKKADPAPTPPPAESIVPILLHGEAPAFEMSVVDEKFLAEAKQMELSPLDSCHFRVVAQLKATCSGLSEEQLAKLGVALFNCQSEVEGRRTYPCTEEMSIKECTADMDSDTWNAYHIVSNRARSVCYATRQQHFRKRAELTVNALISTATSQLDAMKDLKEGQKELRDMTAASLDKLLEGHGALQIQQGALKEGQEQLDASISENLQRLAQEKALISTGQQLVAQLIQGITQRMENVSGQLKDQTAEVQEGHQAILEDLAVVRGSAQDIYEKMELNLNGFLQQQNTTAHFYTELMRKLELMNGTLGYMLTYLDNMQTRLEDRLHMIQGYLGWAGLSLRALWTCVMHAGYFLLCAVLLSFLQCTTFSRVTLLLSVPINAIAEINQQAALDLISLTLLLFTLSLGRWFVLQLLWALSKIKGRTCSRPPHLSIYPPKEKTPEKQHEFGEKCPASSSTPVQSDPVCDLEVESFMMGDPCVLGVSPSRCPPKFSHHHLGGTPNHSTPRLKSRHSIAATELDNIPQRNLGVFLETVNRSRSSSPNQSLASSSSFSGRSLCSGITRLGQPCKKRAVVGQDYCRVHEGGHTSYSRL 612 K7NAJ3 Interferon alpha/beta receptor 1b ifnar1b 8022 No SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:24244163}. Note=Mainly detected in perinuclear regions, when overexpressed in RTG-2 cell line. {ECO:0000269|PubMed:24244163}. UNIPROT K7NAJ3 Pfam PF09294 Pfam PF01108 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}. GO:0005829 GO:0005634 GO:0048471 GO:0004905 GO:0001934 MLAELPQPQNLTLLTLNTQYVLTWDWDQTTTGNSVSFTVEYMAKYKMKMKKKNWSRVCERTTRTRCDLTGSDLHYLGMYVLRVRASADGVDSDWVNKDFCPDIDASLGPPSRAELAPVGNLLDVTISDPLTSTQHSMKEHVLFLYYRILYWSRSDDPQGLKPKVLDSSNNLVTPPELEAWAWYCVMIQSRYDYYNKTSSYTEPQCMQTEGDTPYGQIFLYFLVSMMVCFLLVLLSSYAFFRFYRGLKNTFYPSIQLPAHIQEYLCDSSPGSDMPRLITADSEAELCCDKLTICPEVVLLEIHVPPPLTAPPSELEQDSGRHIRQDSGDSGIYSTEGGSAQQGRSGGEPIRRDQEVDSWQTLEQVKMEEMGRELADERDLDEGVVDVCV 388 K9N638 Non-structural protein 11 1a 1263720 No SL-0382 [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}. UNIPROT K9N638 PDB 4R3D PDB 5DUS PDB 5HIH PDB 5WKJ PDB 5WKK PDB 5WKL PDB 5WKM Pfam PF16348 Pfam PF01661 Pfam PF16251 Pfam PF09401 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF11633 Pfam PF08715 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 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}. GO:0033644 GO:0044220 GO:0016021 GO:0004197 GO:0008242 GO:0003723 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0039648 GO:0039548 GO:0039579 GO:0039502 GO:0019079 GO:0019082 MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLNESGVLL 4391 M9PBE2 E3 ubiquitin-protein ligase Hakai Hakai 7227 Yes SL-0198 Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}. UNIPROT M9PBE2 UNIPROT Q86NQ9 UNIPROT Q8INV9 UNIPROT Q8INW0 UNIPROT Q95RE3 UNIPROT Q9VIT1 Pfam PF18408 PROSITE PS00518 PROSITE PS50089 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}. Q9VU72 EBI-100923,EBI-166182 A1Z9X0 EBI-100923,EBI-160861 Q9VI24 EBI-100923,EBI-106037 Q24558 EBI-100923,EBI-102508 Q9VI16 EBI-100923,EBI-175006 P25171 EBI-100923,EBI-181948 Q7KTX7 EBI-100923,EBI-131530 Q9W2M4 EBI-100923,EBI-138493 Q9VU89 EBI-100923,EBI-157217 Q9VI55 EBI-100923,EBI-172922 Q9VU18 EBI-100923,EBI-172681 Q8T0I9 EBI-100923,EBI-103726 Q9V472 EBI-100923,EBI-497141 Q4Z8K6 EBI-100923,EBI-183849 Q9VGB9 EBI-100923,EBI-123122 Q9V9R6 EBI-100923,EBI-160643 Q9VN36 EBI-100923,EBI-134459 Q9VRC3 EBI-100923,EBI-169095 Q9XZU1 EBI-100923,EBI-126291 Q9VSQ3 EBI-100923,EBI-145474 Q9VC48 EBI-100923,EBI-146422 Q9VMS5 EBI-100923,EBI-140737 Q8MYW5 EBI-100923,EBI-186621 Q9VGU7 EBI-100923,EBI-142527 Q9W550 EBI-100923,EBI-118257 Q9VZT6 EBI-100923,EBI-89759 P54356 EBI-122038,EBI-100923 Q9VJE3 EBI-100923,EBI-186054 Q9VJ53 EBI-100923,EBI-122209 Q9VXD4 EBI-100923,EBI-149308 Q9VMD4 EBI-100923,EBI-86395 Q9VFU6 EBI-100923,EBI-159819 Q9VCM3 EBI-100923,EBI-99802 Q8T3Y1 EBI-100923,EBI-166306 B7YZT2 EBI-100923,EBI-182799 Q9V9V8 EBI-100923,EBI-124864 Q9VVV6 EBI-100923,EBI-135353 Q9VF73 EBI-100923,EBI-164368 P42282 EBI-100923,EBI-77008 Q9W3J9 EBI-100923,EBI-98170 Q9V9V0 EBI-100923,EBI-135868 O46070 EBI-100923,EBI-122171 Q9W5B6 EBI-100923,EBI-127398 Q9VEA5 EBI-100923,EBI-83826 M9MRI4 EBI-100923,EBI-156486 Q9VKQ0 EBI-100923,EBI-111864 Q9V4B8 EBI-100923,EBI-145217 Q9VZM9 EBI-100923,EBI-158602 Q9VSB2 EBI-100923,EBI-111803 Q9VPE1 EBI-100923,EBI-147129 A1ZAC8 EBI-100923,EBI-88363 Q9VQF9 EBI-100923,EBI-88022 Q9VDC1 EBI-100923,EBI-107959 Q9W1R5 EBI-100923,EBI-122690 Q9VSY2 EBI-100923,EBI-172334 P11455 EBI-100923,EBI-85264 Q9Y156 EBI-100923,EBI-181059 Q8IQB8 EBI-100923,EBI-129121 Q9VAZ1 EBI-100923,EBI-161824 Q9VD25 EBI-100923,EBI-119510 Q7K4Z4 EBI-100923,EBI-159623 Q94981 EBI-100923,EBI-98607 O76924 EBI-100923,EBI-150281 O97365 EBI-100923,EBI-120898 Q7JXC4 EBI-151216,EBI-100923 P23696 EBI-100923,EBI-101960 Q9V460 EBI-100923,EBI-134850 A1Z8L7 EBI-100923,EBI-163776 Q9VLP3 EBI-100923,EBI-179169 Q9VHR4 EBI-100923,EBI-117032 Q7K127 EBI-100923,EBI-169919 Q9VHG0 EBI-100923,EBI-195376 Q9VHA9 EBI-100923,EBI-150802 Q8T3X9 EBI-100923,EBI-133004 Q9V428 EBI-100923,EBI-96007 Q9W379 EBI-100923,EBI-158956 Q9W5X1 EBI-100923,EBI-195166 Q9VXE7 EBI-100923,EBI-165741 GO:0031410 GO:0005634 GO:0048471 GO:0005886 GO:0036396 GO:0045296 GO:0061630 GO:0004842 GO:0008270 GO:0007015 GO:0040003 GO:0007391 GO:0007427 GO:0060429 GO:0008258 GO:0007494 GO:0016567 GO:0030155 GO:0035282 MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIASRPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESVADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR 473 O00159 Unconventional myosin-Ic MYO1C 9606 Yes SL-0178 SL-0185 [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}. UNIPROT O00159 UNIPROT Q4LE56 UNIPROT Q6NVJ7 UNIPROT Q86Y95 PDB 4BYF Pfam PF00612 Pfam PF00063 Pfam PF06017 PROSITE PS50096 PROSITE PS51456 PROSITE PS51757 OMIM 606538 DisGeNET 4641 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}. P32121 EBI-714559,EBI-350423 P49407 EBI-743313,EBI-350423 Q5S007 EBI-5323863,EBI-350423 Q7KZN9 EBI-3248549,EBI-350423 P36957 EBI-351007,EBI-350423 P25786 EBI-359352,EBI-350423 P13569 EBI-349854,EBI-350423 O75807 EBI-714746,EBI-350423 P29353 EBI-78835,EBI-350423 Q9Y2K6 EBI-2511991,EBI-350423 Q8IY92 EBI-2370740,EBI-350423 Q92731 EBI-78505,EBI-350423 P03372 EBI-78473,EBI-350423 Q9UH99 EBI-1044964,EBI-350423 Q92614 EBI-949059,EBI-350423 Q8IXM2 EBI-350423,EBI-4280811 Q8N726 EBI-350423,EBI-625922 Q7Z7F7 EBI-350423,EBI-7825445 Q96BQ5 EBI-350423,EBI-7219131 Q9UPN6 EBI-350423,EBI-7954236 Q6P4F7 EBI-350423,EBI-7543265 P21333-2 EBI-350423,EBI-9641086 O95425-2 EBI-350423,EBI-10965323 P23528 EBI-350423,EBI-352733 Q8N9B5-2 EBI-350423,EBI-10268138 Q14151 EBI-350423,EBI-352869 P52756 EBI-350423,EBI-714003 Q6PJ61 EBI-350423,EBI-2322982 O95425 EBI-350423,EBI-487145 Q9NX63 EBI-350423,EBI-743375 Q8N302 EBI-350423,EBI-747899 Q9BWT7 EBI-350423,EBI-3866279 Q9Y2T2 EBI-350423,EBI-2371151 P55884 EBI-350423,EBI-366696 Q9UHB6 EBI-350423,EBI-351479 O75528 EBI-350423,EBI-473249 O60292 EBI-350423,EBI-2559690 Q9P0K7-3 EBI-350423,EBI-10977843 P11233 EBI-350423,EBI-1036803 G3V1L9 EBI-350423,EBI-10969999 Q9Y5J9 EBI-350423,EBI-1049085 Q6IBS0 EBI-350423,EBI-722204 P52943 EBI-350423,EBI-947590 Q92828 EBI-350423,EBI-2835660 Q9NYL9 EBI-350423,EBI-352614 Q27J81-2 EBI-350423,EBI-11025144 O75128 EBI-350423,EBI-3446582 Q0ZGT2-4 EBI-350423,EBI-10977819 Q9Y4F1 EBI-350423,EBI-5235630 Q96I25 EBI-350423,EBI-740272 O15042-2 EBI-350423,EBI-10973137 Q9NR12 EBI-350423,EBI-350517 Q5TB80 EBI-350423,EBI-1059012 Q8TB52 EBI-350423,EBI-2556210 Q8WYL5 EBI-350423,EBI-1222387 O14974 EBI-350423,EBI-351726 Q9Y281 EBI-350423,EBI-351218 O75533 EBI-350423,EBI-876542 Q16643 EBI-350423,EBI-351394 P12268 EBI-350423,EBI-353389 P26583 EBI-350423,EBI-1057009 O43795-2 EBI-350423,EBI-10965344 Q0ZGT2-2 EBI-350423,EBI-11030061 Q96FS4 EBI-350423,EBI-1054981 B4E1Q4 EBI-350423,EBI-11030799 Q96RN5-2 EBI-350423,EBI-11030807 Q9H2D6-5 EBI-350423,EBI-1023227 Q9Y6N5 EBI-350423,EBI-1170418 O94875 EBI-350423,EBI-311323 O15143 EBI-350423,EBI-1044647 Q86SQ0 EBI-350423,EBI-2798483 P28289 EBI-350423,EBI-2659631 Q71RC2 EBI-350423,EBI-2878091 Q9H0L4 EBI-350423,EBI-747012 P0DP23 EBI-350423,EBI-397435 Q13813 EBI-350423,EBI-351450 Q13435 EBI-350423,EBI-749111 O14639-3 EBI-350423,EBI-11030070 Q0ZGT2 EBI-350423,EBI-351705 Q96N67-4 EBI-350423,EBI-11017737 Q12792 EBI-350423,EBI-1056675 Q53F19 EBI-350423,EBI-6657994 Q9ULV4 EBI-350423,EBI-351384 Q9Y5L4 EBI-350423,EBI-1057344 P80723 EBI-350423,EBI-358583 E9PR71 EBI-350423,EBI-11030795 P62136 EBI-350423,EBI-357253 Q93074-3 EBI-350423,EBI-11030781 Q5M775 EBI-350423,EBI-350473 Q155Q3 EBI-350423,EBI-1104700 Q01082-3 EBI-350423,EBI-4400743 Q9UHB6-4 EBI-350423,EBI-10977805 Q9H0G5 EBI-350423,EBI-5464397 Q8WX93 EBI-350423,EBI-2803991 Q7Z460 EBI-350423,EBI-913476 A1L390 EBI-350423,EBI-4401429 Q8IVT2 EBI-350423,EBI-2555085 Q6WCQ1-2 EBI-350423,EBI-10965272 P35611-2 EBI-350423,EBI-11030777 Q13347 EBI-350423,EBI-354047 Q9BSF4 EBI-350423,EBI-10974729 Q9NVS9 EBI-350423,EBI-11030787 O75083 EBI-350423,EBI-351917 P60981 EBI-350423,EBI-745191 Q9H3U1-2 EBI-350423,EBI-10977801 Q7Z4V5 EBI-350423,EBI-1049136 Q6IN84 EBI-350423,EBI-5454865 Q8IWX8 EBI-350423,EBI-2555370 J3KP15 EBI-350423,EBI-11030773 P28290 EBI-350423,EBI-722905 O15145 EBI-350423,EBI-351829 Q01082 EBI-350423,EBI-351561 Q9UDY2 EBI-350423,EBI-1042602 Q96EV2 EBI-350423,EBI-1210748 Q5T5U3 EBI-350423,EBI-1642518 P20839 EBI-350423,EBI-2866691 P35269 EBI-350423,EBI-457886 O15020 EBI-350423,EBI-308449 Q13045 EBI-350423,EBI-351549 Q9H3F6 EBI-350423,EBI-2505886 Q8IX12-2 EBI-350423,EBI-10972011 Q8VDD5 EBI-400906,EBI-350423 P24941 EBI-375096,EBI-350423 P98175-2 EBI-350423,EBI-10974418 Q9Y4I1-2 EBI-350423,EBI-10965332 P47755 EBI-350423,EBI-762451 Q13838 EBI-350423,EBI-348622 Q8WW12 EBI-350423,EBI-10972020 Q8N573-2 EBI-350423,EBI-11030811 P63261 EBI-350423,EBI-351292 Q4KMQ1 EBI-350423,EBI-3942777 Q9Y2X0-2 EBI-350423,EBI-10970047 O43707 EBI-350423,EBI-351526 Q8N556 EBI-350423,EBI-3893163 Q9BQ61 EBI-350423,EBI-744881 Q8N3V7-2 EBI-350423,EBI-10965260 Q96H55 EBI-10983249,EBI-350423 Q08379 EBI-618309,EBI-350423 Q14684 EBI-372051,EBI-350423 Q15051 EBI-2805823,EBI-350423 P03496 EBI-2547442,EBI-350423 O76071 EBI-350423,EBI-725145 Q14240 EBI-73473,EBI-350423 O14908 EBI-350423,EBI-373132 Q9Y5J5 EBI-350423,EBI-1055859 Q9HC98 EBI-350423,EBI-740364 O75365 EBI-350423,EBI-1043866 Q9P2S5 EBI-350423,EBI-1054904 O75368 EBI-2854777,EBI-350423 P20936 EBI-1026476,EBI-350423 O60496 EBI-1046024,EBI-350423 P17252 EBI-1383528,EBI-350423 P28324 EBI-11277718,EBI-350423 Q8IZP0 EBI-375446,EBI-350423 Q15139 EBI-1181072,EBI-350423 Q13115 EBI-6591081,EBI-350423 P33993 EBI-355924,EBI-350423 Q13509 EBI-350989,EBI-350423 Q71U36 EBI-302552,EBI-350423 P17706-3 EBI-14013987,EBI-350423 P30307 EBI-974439,EBI-350423 Q14761 EBI-722217,EBI-350423 Q16829 EBI-1265847,EBI-350423 Q8NI37 EBI-9089276,EBI-350423 Q9H0C8 EBI-2620298,EBI-350423 Q9H596 EBI-7357329,EBI-350423 Q9UQK1 EBI-2506727,EBI-350423 Q9NYA1-1 EBI-12512636,EBI-350423 Q8IVT5 EBI-486984,EBI-350423 Q9Y572 EBI-350423,EBI-298250 Q9Y6K9 EBI-350423,EBI-81279 Q99759 EBI-350423,EBI-307281 P62993 EBI-401755,EBI-350423 GO:0009925 GO:0005903 GO:0005623 GO:0005737 GO:0030659 GO:0005829 GO:0070062 GO:0031941 GO:0016328 GO:0016020 GO:0045121 GO:0005902 GO:0016604 GO:0005643 GO:0005730 GO:0005654 GO:0045335 GO:0005886 GO:0032587 GO:0060171 GO:0016461 GO:0051015 GO:0030898 GO:0005524 GO:0005516 GO:0000146 GO:0008022 GO:0017160 GO:0005102 GO:0071346 GO:0038096 GO:0051028 GO:0030838 GO:0030335 GO:0038089 GO:1900078 GO:0045815 GO:0090314 GO:1900748 GO:0006605 GO:0006612 GO:2000810 GO:0030050 MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFVLRHAPRCPENAFFLDHVRTSFLLNLRRQLPQNVLDTSWPTPPPALREASELLRELCIKNMVWKYCRSISPEWKQQLQQKAVASEIFKGKKDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPGSELLITKAKNGHLAVVAPRLNSR 1063 O00299 Chloride intracellular channel protein 1 CLIC1 9606 Yes SL-0178 SL-0182 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}. UNIPROT O00299 UNIPROT Q15089 UNIPROT Q502X1 PDB 1K0M PDB 1K0N PDB 1K0O PDB 1RK4 PDB 3O3T PDB 3P8W PDB 3P90 PDB 3QR6 PDB 3SWL PDB 3TGZ PDB 3UVH PDB 4IQA PDB 4JZQ PDB 4K0G PDB 4K0N Pfam PF13409 PROSITE PS50405 OMIM 602872 DisGeNET 1192 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}. P32121 EBI-714559,EBI-347404 Q5S007 EBI-5323863,EBI-347404 O75832 EBI-752185,EBI-347404 Q9Y2H1 EBI-991501,EBI-347404 P03372 EBI-78473,EBI-347404 P13569 EBI-349854,EBI-347404 Q9Y251 EBI-5453868,EBI-347404 P40692 EBI-744248,EBI-347404 Q9H0R8 EBI-746969,EBI-347404 Q5NID2 EBI-2796292,EBI-347404 A0A384KST0 EBI-2845592,EBI-347404 P20292 EBI-3904621,EBI-347404 P24539 EBI-1044810,EBI-347404 P27449 EBI-347404,EBI-721179 Q93050 EBI-347404,EBI-2891238 P34130 EBI-347404,EBI-3907456 P50416 EBI-347404,EBI-2817330 Q99676 EBI-347404,EBI-3907489 P05386 EBI-354582,EBI-347404 P10827 EBI-286285,EBI-347404 Q9Y6K9 EBI-81279,EBI-347404 P37198 EBI-347978,EBI-347404 Q9NR11 EBI-3916142,EBI-347404 P60710 EBI-353957,EBI-347404 Q61879 EBI-400918,EBI-347404 Q9NQW6 EBI-2553589,EBI-347404 Q9NQX4 EBI-1237297,EBI-347404 Q8N3V7 EBI-352936,EBI-347404 P47755 EBI-762451,EBI-347404 Q96FW1 EBI-1058491,EBI-347404 Q9WUM4 EBI-8316222,EBI-347404 Q9D6P8 EBI-11062253,EBI-347404 P36873 EBI-356283,EBI-347404 P46940 EBI-297509,EBI-347404 O00400 EBI-11135403,EBI-347404 Q86WR7 EBI-347404,EBI-2880603 Q4KMQ1-2 EBI-347404,EBI-11978969 Q6FHY5 EBI-16439278,EBI-347404 P15336 EBI-1170906,EBI-347404 P19320 EBI-6189824,EBI-347404 Q13162 EBI-2211957,EBI-347404 Q81Z98 EBI-2809746,EBI-347404 A0A0F7REA8 EBI-347404,EBI-2830099 Q8CZM8 EBI-347404,EBI-2848309 Q81XG9 EBI-347404,EBI-2811950 P01889 EBI-1046513,EBI-347404 P11171 EBI-347404,EBI-1050906 Q14164 EBI-347404,EBI-307369 P62330 EBI-347404,EBI-638181 P23508 EBI-347404,EBI-307531 Q8N5H7 EBI-745980,EBI-347404 Q15139 EBI-1181072,EBI-347404 O15116 EBI-347619,EBI-347404 Q5HYW2 EBI-347404,EBI-2859639 Q81U22 EBI-2814904,EBI-347404 Q9HCN8 EBI-2339921,EBI-347404 GO:0072562 GO:0005903 GO:0034707 GO:0005737 GO:0070062 GO:0005615 GO:0016020 GO:0005739 GO:0005635 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0031982 GO:0045296 GO:0005254 GO:0005244 GO:0006821 GO:0070527 GO:0045669 GO:0051726 GO:0034765 GO:0051881 GO:0007165 MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK 241 O00423 Echinoderm microtubule-associated protein-like 1 EML1 9606 Yes SL-0198 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}. UNIPROT O00423 UNIPROT Q86U15 UNIPROT Q8N536 UNIPROT Q8N5C4 UNIPROT Q8WWL6 PDB 4CI8 Pfam PF03451 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 OMIM 600348 OMIM 602033 DisGeNET 2009 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}.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. Q9H9L3 EBI-751335,EBI-751327 Q9Y266 EBI-751327,EBI-357298 Q14203 EBI-724352,EBI-751327 Q96GG9 EBI-740086,EBI-751327 GO:0005829 GO:0005874 GO:0005875 GO:1990023 GO:0097431 GO:0048471 GO:0005509 GO:0008017 GO:0015631 GO:0007420 GO:0002244 GO:0000226 GO:0007052 GO:0007405 MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI 815 O01971 Emerin homolog 1 emr 6239 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O01971 Pfam PF03020 PROSITE PS50954 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}. Q9XTB5 EBI-2535391,EBI-6260308 GO:0005639 GO:0005635 GO:0005521 GO:0007059 GO:0000281 GO:0010165 MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVSAATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAETNPEDTI 166 O02173 Probable trafficking protein particle complex subunit 2 sedl 6239 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. UNIPROT O02173 Pfam PF04628 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}. Q9NA81 EBI-367817,EBI-367809 P34605 EBI-312149,EBI-367809 GO:0005783 GO:0005794 GO:0048471 GO:0006888 MATKEFYFAIIGHCDQPIFEMDFPVGEKKTKESEGTRHLNHYIGHAALDIVDEHALTTSQMYLKMVDKFNEWYVSAFVTASRIRFIMLHTHRADEGIKQFFQEMYETYIKHAMNPFYEIDDVIESPAFEQKATLYGRKYLS 141 O02768 Prostaglandin G/H synthase 2 PTGS2 9986 Yes SL-0178 SL-0179 SL-0182 SL-0183 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}. UNIPROT O02768 Pfam PF03098 Pfam PF00008 PROSITE PS50026 PROSITE PS50292 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}. GO:0005737 GO:0005789 GO:0043005 GO:0051213 GO:0019899 GO:0020037 GO:0046872 GO:0004601 GO:0004666 GO:0042803 GO:0050873 GO:0071498 GO:0071456 GO:0071471 GO:0019371 GO:0046697 GO:0007566 GO:0006954 GO:0043154 GO:1902219 GO:0090336 GO:0031622 GO:0033138 GO:0031394 GO:0001516 GO:0008217 GO:0042127 GO:0150077 GO:0006979 MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTHFKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQQYNYQQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPPAVQKVAKASIDQSRQMKYQSLNEYRKRFLLKPYESFEELTGEKEMAAELEALYGDIDAVELYPALLVERPRPDAIFGESMVEMGAPFSLKGLMGNPICSPNYWKPSTFGGEVGFKIVNTASIQSLICNNVKGCPFTSFNVPDPQLTKTVTINASASHSRLEDINPTVLLKGRSTEL 604 O02824 Alpha-1A adrenergic receptor ADRA1A 9986 Yes SL-0178 SL-0182 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}. UNIPROT O02824 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0016021 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0046982 GO:0007512 GO:0061049 GO:0010507 GO:0001985 GO:0150099 GO:0001994 GO:0007200 GO:0097195 GO:0010613 GO:0001996 GO:0043410 GO:1903997 GO:0045987 GO:0001997 GO:0055117 GO:0019229 MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVGPLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV 466 O04326 Nuclear pore complex protein NUP35 NUP35 3702 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT O04326 UNIPROT Q8VYL9 Pfam PF05172 PROSITE PS51472 DE Reference Proteome: Yes; Q9C933 EBI-4452551,EBI-4424446 Q8GYN0 EBI-4424446,EBI-4450073 Q8L586 EBI-4424446,EBI-4455687 Q8LB17 EBI-4434215,EBI-4424446 Q8LF05 EBI-4424446,EBI-4439718 Q8RXL7 EBI-4424446,EBI-4427323 Q8RY62 EBI-4458877,EBI-4424446 Q93VN2 EBI-4424446,EBI-4452986 Q93XX0 EBI-4424446,EBI-4435989 Q93Z42 EBI-4466134,EBI-4424446 Q93ZQ3 EBI-4450641,EBI-4424446 Q93ZW4 EBI-4455720,EBI-4424446 Q946Y7 EBI-4438441,EBI-4424446 Q94A32 EBI-4438745,EBI-4424446 Q94A99 EBI-4451043,EBI-4424446 Q94CH8 EBI-4424550,EBI-4424446 Q94JU2 EBI-4459794,EBI-4424446 Q9CAN1 EBI-4424446,EBI-4424904 Q9FI47 EBI-4424446,EBI-4435326 Q9FZ98 EBI-4424446,EBI-4425682 Q9LJU6 EBI-4424446,EBI-4429742 Q9LQ32 EBI-4436710,EBI-4424446 Q9LSW5 EBI-4424446,EBI-4425852 Q9LVD9 EBI-4431584,EBI-4424446 Q9LXV1 EBI-4424446,EBI-4430604 Q9LYP1 EBI-4436922,EBI-4424446 Q9M1J1 EBI-4424446,EBI-4436721 Q9M1J7 EBI-4438348,EBI-4424446 Q9M2J9 EBI-4434027,EBI-4424446 Q9M9S6 EBI-4424446,EBI-4434173 Q9SA23 EBI-4436558,EBI-4424446 Q9SD04 EBI-4459803,EBI-4424446 Q9SHG7 EBI-4424446,EBI-4436589 Q9SIH4 EBI-4451446,EBI-4424446 Q9SIQ8 EBI-532034,EBI-4424446 O48741 EBI-4436108,EBI-4424446 O65397 EBI-4457543,EBI-4424446 O80594 EBI-4428472,EBI-4424446 O80895 EBI-4424446,EBI-4456509 O81062 EBI-4440921,EBI-4424446 O82174 EBI-4424446,EBI-4453441 O82219 EBI-4424446,EBI-4433315 P26587 EBI-4460900,EBI-4424446 P27202 EBI-4461393,EBI-4424446 P30302 EBI-4431139,EBI-4424446 P42813 EBI-4424446,EBI-4432112 P47192 EBI-4424446,EBI-4433747 P53799 EBI-4424446,EBI-4476955 P82874 EBI-2352074,EBI-4424446 P92941 EBI-4438503,EBI-4424446 Q147J7 EBI-4432597,EBI-4424446 Q38935 EBI-4444120,EBI-4424446 Q41975 EBI-4449798,EBI-4424446 Q42328 EBI-4436355,EBI-4424446 Q42342 EBI-4424446,EBI-2295493 Q5XF13 EBI-4424446,EBI-4431954 Q5XF36 EBI-4431742,EBI-4424446 Q6IDC5 EBI-4431568,EBI-4424446 Q6NLF5 EBI-4424446,EBI-4431243 Q7XA86 EBI-4429137,EBI-4424446 Q84WI4 EBI-4429346,EBI-4424446 Q8GWH4 EBI-4426287,EBI-4424446 Q8GWM8 EBI-4424446,EBI-4425706 Q8GWT5 EBI-4424446,EBI-4439395 Q8GX78 EBI-4425789,EBI-4424446 Q9SRE4 EBI-4434931,EBI-4424446 Q9SRT3 EBI-4455819,EBI-4424446 Q9STW3 EBI-4429423,EBI-4424446 Q9XI60 EBI-4424446,EBI-4424450 Q9ZSD4 EBI-4476863,EBI-4424446 Q9ZV66 EBI-4424446,EBI-4429327 O22690 EBI-4424446,EBI-4436104 GO:0031965 GO:0044613 GO:0044615 GO:0005543 GO:0003697 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0006355 MSAAAHRTPKSGRQSLLFQDLASPVSARRGKFSSPGQAAAVSALWRENFGGSDLPPPPMYTLDDRSDFSPESGIADYSASPDAKSDRRTPFQSSGKNIVTPGKGKLEASPSFSLLNAQQSQQVSGSPSWWSQSKAGSSTEQDDKGKGSPVEGVVQPGALVTLPPPREVARPEVQRQIIPTGNLDEEEWVTVYGFSPGDTNLVLREFEKCGMVLKHVPGPRNANWMHILYQNRSDAHKALNKAGMMINGVVIVGVKPVDPIQKQALNERLNNQGFMPLPPPSSTRNTARPLSRPQYLQNGSAFSPQPSGGAMASPSKSMVSKFFDLMFGV 329 O08684 Phospholipase D1 PLD1 10029 No SL-0198 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}. UNIPROT O08684 Pfam PF00169 Pfam PF00614 Pfam PF13091 Pfam PF00787 PROSITE PS50035 PROSITE PS50195 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}. GO:0005789 GO:0000139 GO:0031902 GO:0048471 GO:0070290 GO:0035091 GO:0004630 GO:0048017 GO:0016042 GO:0006654 MSLKSEHRVNTSALQKIAADMSNLIDNLDTRELHFEGEEVEFDTSPGDPKAQEKYIPFSSIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREMPSLPRSSENTIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGSDFLKDHRFGSYAAVHENMLAKWYVNAKGYFEDIANAMEEAAEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGLSMGSLAAATMESMESLSLKDNHRSHKNEPILKSVDDVDPKLKGVGKPRKFSKFSLYRQLHRRHLHNSDSVSSIDSASNTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRIPWHDIGSVLHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQSTAHELRYQVPGAVPAKVQLLRSAADWSAGIKHHEESIHSAYINVIENSKHYIYIENQFFISCADDKVVFNKVGDAIAQRILKAHREGQRYRVYIVIPRLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKPELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSIMDGKEYQAGCFAQGLRLQCFRLVLGYLSDPSEDLQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLMQLRDFISKPILAKDDPIRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT 1036 O08788 Dynactin subunit 1 Dctn1 10090 Yes SL-0178 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}. UNIPROT O08788 UNIPROT E9QLJ1 UNIPROT Q3TZG7 Pfam PF01302 Pfam PF12455 PROSITE PS00845 PROSITE PS50245 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}. Q4ACU6 EBI-771450,EBI-776180 Q7TPH6 EBI-1811542,EBI-776180 P06493 EBI-776180,EBI-444308 Q9UJW0 EBI-776180,EBI-2134033 P61163 EBI-776180,EBI-774234 Q9NZ32 EBI-776180,EBI-2559426 Q9BTE1 EBI-776180,EBI-747324 Q14203 EBI-776180,EBI-724352 O00399 EBI-776180,EBI-2559415 P47755 EBI-776180,EBI-762451 A8K8J9 EBI-776180,EBI-2559432 O75935 EBI-776180,EBI-347442 P42025 EBI-776180,EBI-367493 P48651 EBI-776180,EBI-8652106 Q9Y592 EBI-776180,EBI-8600408 Q9NP97 EBI-776180,EBI-372128 P47756-2 EBI-776180,EBI-353608 P52907 EBI-776180,EBI-355586 O14949 EBI-776180,EBI-720294 Q86XL3 EBI-776180,EBI-1773621 O15235 EBI-776180,EBI-712205 Q9BV73 EBI-776180,EBI-1053100 Q15643 EBI-776180,EBI-1047183 O75935-3 EBI-776180,EBI-10962292 B4E1G1 EBI-776180,EBI-10984153 Q9Y6G9 EBI-776180,EBI-2556107 Q96L93-6 EBI-776180,EBI-10988217 Q13561 EBI-776180,EBI-715074 Q8CG73 EBI-4281130,EBI-776180 Q7TMB8 EBI-772928,EBI-776180 Q9CQV8 EBI-771608,EBI-776180 GO:0005623 GO:0005938 GO:0099738 GO:0031252 GO:0120103 GO:0005814 GO:0005813 GO:0005737 GO:0005868 GO:0005829 GO:0045171 GO:0000776 GO:0005874 GO:0005875 GO:0015630 GO:0035371 GO:0072686 GO:0043005 GO:0043025 GO:0005635 GO:0032991 GO:0005819 GO:0000922 GO:0042802 GO:0008017 GO:0003774 GO:0019901 GO:0015631 GO:0051301 GO:0010457 GO:0031122 GO:0000132 GO:0032402 GO:0034454 GO:0061744 GO:0007528 GO:0050905 GO:0070050 GO:1990535 GO:1905515 GO:0051081 GO:0090316 GO:0090063 GO:0031116 GO:1904398 GO:0060236 GO:0042147 GO:0010970 GO:0021517 MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS 1281 O13671 Importin-alpha re-exporter kap109 284812 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. UNIPROT O13671 UNIPROT Q9USC9 Pfam PF03378 Pfam PF08506 Pfam PF03810 PROSITE PS50166 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}. GO:0005829 GO:0005635 GO:0031965 GO:0034399 GO:0005525 GO:0005049 GO:0008536 GO:0006611 GO:0006606 MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDEVAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSDALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFTYTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRKHAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHINANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVFTFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKLAENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLPVFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFVEPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGPDNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQAQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVLQSYGYVI 967 O13681 Integral inner nuclear membrane protein ima1 IMA1 284812 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:18692466}. UNIPROT O13681 Pfam PF09779 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}. GO:0034506 GO:0016021 GO:0034992 GO:0044732 GO:0005635 GO:0005637 GO:0031965 GO:0071765 MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPFYAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDANDYEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLLDGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFLLRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISILNNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSKFSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNRRNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA 615 O13712 Meiotically up-regulated gene 61 protein mug61 284812 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. UNIPROT O13712 UNIPROT Q9USD6 Pfam PF12949 Pfam PF09402 Required for correct meiotic chromosome segregation. {ECO:0000269|PubMed:16303567}. Q9P7F8 EBI-1542405,EBI-15798909 O42841 EBI-1542405,EBI-21242362 Q9UUJ1 EBI-1542405,EBI-443389 Q10436 EBI-1542405,EBI-21242299 Q10169 EBI-1542405,EBI-7989032 O13787 EBI-1542405,EBI-21242328 Q9P6P8 EBI-1542405,EBI-21242420 Q9P6M1 EBI-1542405,EBI-1542559 Q09835 EBI-1542405,EBI-21242393 O14223 EBI-1542405,EBI-21242449 Q9UT35 EBI-1542405,EBI-21242469 O42901 EBI-1542405,EBI-21242494 Q09825 EBI-1542405,EBI-929731 Q9Y806 EBI-1542405,EBI-21242528 Q9Y7X6 EBI-1542405,EBI-1559673 P36596 EBI-1542405,EBI-1794119 P10815 EBI-1542405,EBI-1187843 O94361 EBI-1542405,EBI-21242566 GO:0005623 GO:0034506 GO:0005789 GO:0005639 GO:0005635 GO:0005720 GO:0031965 GO:1990707 GO:1990421 GO:0005524 GO:0070197 GO:0006998 MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGVTNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPFETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNTTSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLVGLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKFDSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWHQEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFGLKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVYLKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAAITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSIQLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL 844 O13746 Uncharacterized protein C16E8.18 SPAC16E8 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O13746 DE Reference Proteome: Yes; GO:0005829 GO:0016021 GO:0031965 GO:0005634 MEVTSFILNATFKEFACFGNNYLIILPGIMLERNVFRHLNYSTNSICSHYQFFGGHYESFELLVVIVYYFSHVGSFSLAEIYRITWDKRIVLYGTTTTLVYCSEGSD 107 O13760 Uncharacterized membrane protein C17A2.10c SPAC17A2 284812 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O13760 DE Reference Proteome: Yes; GO:0005829 GO:0016021 GO:0031965 GO:0005634 MTCVNVCFFLFPPCHRNKITEADKSLVDLLIPSLCCSLAVFPSIPLINTHSNLCLFSNFSHSCFLFCTHPDTLPTSLSINPKKLSLSFSFPLSQKRPFPNFLHPFTGSELSLFRCLLLFFFFLLFFLSFSFSFSFLFFLSQIFIVYFSSFPILHFLFFFFLCVCVFLSFLFSLSHLLSLAILFLPLLLRVFSTLSRLPRLFCLCLQKKRRVLIPFAFTSFRKIASLPCVC 230 O13818 Uncharacterized PH domain-containing protein C19A8.02 SPAC19A8 284812 Yes SL-0178 SL-0182 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}. UNIPROT O13818 UNIPROT Q9USA8 Pfam PF00169 Pfam PF16016 PROSITE PS50003 PROSITE PS51778 DE Reference Proteome: Yes; GO:0032541 GO:0005737 GO:0016021 GO:0031965 GO:0005886 GO:0005816 GO:0016538 GO:0061817 GO:0045737 MAAPANASSKKDHVIPVLLNECSIDSPSFRASMYYLGNQIKAFNEWSHDFLCCCNKFIESIMAIEPIVASMSLNAMPSNVASGFFDPDYATTALLHGQDLFRSSYMVQLQQAKNLRKFIVAPLDLFRDSKVKPLLQLNDRFKAEQAKYDAEVLRYSSLGHSKDLSQMRDEAKSLYEARKSYFTVALQYVVRVTSFRSSIDFIVIESICKFSIETFRLTDRLHESNRHINDQLIRLLSYETKLKESYPSLKRIVSNVFDRIEKEILKRVQPPTNLDAYRFDPQQICQTNATKRQGWLLRNISSSKADNKAIWRKYWFFVDNGYVGYLINDANGGVFESEKIGVLLCKFSVLPSNHRKFCFQIKTKSVSYILQAETHMEMLEWGSVINNAREHCINSGISANRILSPTLPSFSAKATSIINPQVNGRSNSTGKIGKNYRPRRTYSGRLLCGPNNYEVSTIMRSPTISTVPPPKYLSNSINGAKFLNPLAPWTLVNAPLITNLTHETITSLLDQEAFFHGNSPCALLANFWGSVNYGHVLERQNVYIEDLSNPSYKRLAREIHIEKLPSELKLRNAEFRGIFGESEASTVLFVCRVCSKREDQIRMPGRMYCTMKGIYIYYNINGLVLIEHFPISSILNVKQFASTKCDYFYMNIQNIGTVRFRLYLDSSKALTDRLNVLLCNYIADKPNSSIQLLSCIKRLNDDVKRFERGGDDNALKSYGVQPSQEDLLIRRGRSSRALTNLINKNESNDSFMEDLRDFKIAMLPKETVQVVRSHHLDDIVFDRVYNVSTKALFHIVFGDRSTVLSGAYNLHGVDDVEFLPWGKDPKTNLSRRYINYKVYNYDQEGQCQSYHYEDCQIMDVRNDYHLYIMTWLHHSWTLPYRDYFKIVTKTSISHLRREKSRLLISVGLEWIVKPFAISKVIEAECRKLAIKYIKTEVNFLEKATRRARNQPLIAIINQYGRVGDYNESMVYRRKIPFNCELKNLSIIDIIRNNWWLFLQGLAIDLLKLPWAVFHIFLRYLFSHSFLVIIFACSVILNLSLMFCFGAKYWDERQNNKFVGQVFDEFKNIETSARYVYMKDVDDLLVGLPTYLHPNVTYPSECLQSFALKSSPQKSHWLRKRNYIAEKRKKILENLASLNYYEYIIHEDAVYQYIQQELLGCDKAREFDLYPPSMQRYCDSCTQDWRNRTLFFGKDTLATRLLTLETVENADYAA 1213 O13838 Nucleoporin nup40 nup40 284812 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side. UNIPROT O13838 Pfam PF05172 PROSITE PS51472 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}. GO:0005635 GO:0031965 GO:0034399 GO:0005643 GO:0044613 GO:0044615 GO:0005543 GO:0003697 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0006355 GO:0006407 MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQPRNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF 371 O13864 Importin subunit beta-1 kap95 284812 Yes SL-0178 SL-0185 Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}. UNIPROT O13864 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. GO:0005737 GO:1990023 GO:0005635 GO:0034399 GO:0005643 GO:0005634 GO:0005525 GO:0061608 GO:0008139 GO:0008536 GO:0051028 GO:0006606 MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLWQSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICESVSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGCLVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAADILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVAMLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCHFAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQILDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPSFVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQTYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSESLTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA 863 O13898 Dolichyl-phosphate-mannose--protein mannosyltransferase 1 ogm1 284812 Yes SL-0178 SL-0182 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}. UNIPROT O13898 Pfam PF02815 Pfam PF02366 Pfam PF16192 PROSITE PS50919 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}. GO:0097582 GO:0012505 GO:0005789 GO:0016021 GO:0031965 GO:0004169 GO:0000032 GO:0044845 GO:0031505 GO:0035269 MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMDVYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIFDNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLWNLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVTIRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHKPIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQREVTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFYEQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHYLPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDNLSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASEAAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQEENVAESAQARVE 893 O13918 Zinc homeostasis factor 1 zhf1 284812 Yes SL-0178 SL-0182 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}. UNIPROT O13918 UNIPROT P78885 Pfam PF01545 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}. GO:0005623 GO:0005789 GO:0000324 GO:0000329 GO:0005794 GO:0016021 GO:0031965 GO:0005385 GO:0006877 GO:0098849 GO:0006882 GO:0140209 GO:0062111 MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILGALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESVLPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGDALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHELHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS 387 O13961 Nuclear envelope protein ndc1 cut11 284812 Yes SL-0178 SL-0182 SL-0185 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. UNIPROT O13961 UNIPROT Q9UTH4 Pfam PF09531 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}. GO:0005623 GO:0005737 GO:0016021 GO:0044732 GO:0005635 GO:0031965 GO:0005643 GO:0070762 GO:0005816 GO:0106166 GO:0017056 GO:0071790 GO:0051028 GO:0006999 GO:0015031 MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIATEELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHEEINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQNEALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAANALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS 601 O13965 Meiotically up-regulated gene 70 protein mug70 284812 Yes SL-0178 SL-0182 Cytoplasm. Nucleus membrane; Multi-pass membrane protein. UNIPROT O13965 UNIPROT Q9USF6 Pfam PF00571 Pfam PF00564 PROSITE PS51371 PROSITE PS51745 Has a role in meiosis. {ECO:0000269|PubMed:16303567}. GO:0005737 GO:0005829 GO:0016021 GO:0031965 GO:0005634 GO:0051321 MTVGTLSVVSSTASDTASHVSDTRKRQYQRDEALRKKIISELGKKSGNFESPVRKIRRNGEPGTVDSAALDPALTVHMQSLVTETAQLMAAKRQNCVLVVDDDEQLAGIVTATDIATRCVGAGLNARQTLIADIMSTSPLCITSDTRFDDALLLMIEHKFRHLPVVSDGGPDGSAGDEGDVIGIINMRACLREPLNRIARQQEAAQKLVEALEGAQEEIENKSVSGNTNSSSVSGNHAAEFLEYVESLKKKASGLEIMSLIDSSEEPFLVGTRTTVAEATESMARSGVSAVLVMDNGAVSGVFTAHDVVLRVLAAGLDPYRSSVIRVMTPHPDCALASLRVSTALERMIEGKFSNLPVVDESDAIIGMLSLFHLATAIEQTPEEEEEVFDQAENDAGIEPSNGFEDQQQQLLGNSNEVVENYDVNPPLPLNPLPSNTQQSESTYEYSARQLPKPPVQAWQNENLSSNNKPQEYVGVENDYNFSNNPPTAMSEQSFHPSVSQKPMDTPENGSNSFAASPYLQPYNSASQLAPSYVGSLPQYHGNPSFVEQALQDLVQPTDSASQIFPLNPQSPSQFTIKYRSIAGRVHRLRLDGINSVSDLRTAVEEREKEQLVTLTYIDDEGDVVELVSDSDLREAILLARRRGLPRLEVRGVAAFTNHLESSHPPISTVDSSIGSASVVEKGVANSIVDIHQPTAKADKGNSKKPIYIGIVSSSIVILAVSMWYLRRKR 730 O13999 Meiotically up-regulated gene 155 protein mug155 284812 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O13999 Has a role in meiosis. {ECO:0000269|PubMed:16303567}. GO:0005737 GO:0016021 GO:0031965 GO:0051321 MRPTSGCSKDDTIQKQNRRHNTVDNKQEKLPLSIEIFLNKQINKISFDTIRSKQNCRLKEIYCRLKIRCRLKKKFIKSLSKKIISYHFISFHTIVVLLLLPPFSHLLVLVYPSVFTTAFYHQKWALRLNPCLPTYFFHRQRQCVTLLIRNANENMRARRVNSVMLTKPKQFLFLLEFITLFIFTYCL 187 O14089 Importin subunit beta-2 kap104 284812 Yes SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. UNIPROT O14089 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}. GO:0005737 GO:0005829 GO:1990023 GO:0005635 GO:0034399 GO:0005643 GO:0005634 GO:0005525 GO:0061608 GO:0008139 GO:0051028 GO:0006606 MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV 910 O14188 Ras GTPase-activating-like protein rng2 rng2 284812 Yes SL-0178 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. UNIPROT O14188 UNIPROT Q9USG0 PDB 1P2X PDB 1P5S Pfam PF00307 Pfam PF00612 Pfam PF00616 Pfam PF03836 PROSITE PS50021 PROSITE PS50096 PROSITE PS50018 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}. GO:0005826 GO:0120104 GO:0005737 GO:0071341 GO:0110085 GO:0044732 GO:0005635 GO:0005816 GO:0051015 GO:0005516 GO:0005096 GO:0051017 GO:1903478 GO:0000917 GO:1903475 GO:1903479 GO:1902405 GO:1903477 GO:0030835 GO:0030838 GO:1903476 GO:0071574 GO:0007165 MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEFSKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTSGLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSISRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIPLFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLEKLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAILLRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVKNFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKINTLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCTIENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETLQSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTVKVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS 1489 O14199 UDP-N-acetylglucosamine transferase subunit alg14 alg14 284812 Yes SL-0178 SL-0182 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}. UNIPROT O14199 Pfam PF08660 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}. GO:0005783 GO:0030176 GO:0031965 GO:0043541 GO:0006488 MNTYVLTAIAVLASLIILLVGRNAIKSSKKKPFQKHLLVFFGSGGHTGEMLNLLNALDDKLYSVRSYVAGSDDTMSVSKASLLSNSLPSVKSKIFKVPRARYVKQSWLTTPFTAFWSLLGSISVIFWNPFGIPDVILCNGPGTCVFICLLGYLAKFLGKNVKIVYVESFARVKSLSLSGKILMPFVDRFLVQWPDLATKYKRAEYIGIVA 210 O14253 Nuclear cap-binding protein subunit 1 cbc1 284812 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P34160}. Nucleus {ECO:0000269|PubMed:16823372}. UNIPROT O14253 Pfam PF02854 Pfam PF09088 Pfam PF09090 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}. GO:0005829 GO:0072686 GO:0005845 GO:0005846 GO:0005634 GO:0048471 GO:0003729 GO:0000340 GO:0000339 GO:0045292 GO:0000398 GO:0051028 GO:0000184 MSSYRGSTRPRKRTREGENYGFRPHRGNSQELLAARIKKDITFLADPRGNSVAADDINYVAMSLSREANDPETISTILDCIQTTAFIIPVKIPHLATLIIRASLRVPLILEKAAAYFCLQYFTNLNSFLYYEAKVDLRMLICMSFALQPGTLKPLFSLLADAISKETKPSVWGDNFLRIILINLPYFIAANNDLGKKDFANEILDQCEIYVRHRKSSITLSNPLSIHDNLSEEELDLLYKQLILSRENDFTFPYISQPWKFFESDFVHIVPVSPSIPEWTFQPTPQQNELPSFKRFFELFNNFEIRTTPDASDVAASIFRDISVDVINHLEFNRVEAAQVLTDLDVYFTYKTFALRGTPVNELPNLDPSESRWKAEDIIVEAVLGELLGSQNTTYKPVYYHSLLIECCRIAPKILAPTFGRVIRLMYTMSSDLPLQTLDRFIDWFSHHLSNFNFHWKWNEWIPDVELDDLHPKKVFMRETITRELILSYYTRISDSLPEELRCLLGEQPSGPNFVYENETHPLYQQSSQIIEALRLHKPLEELDIILQSEEIQNSETSAVRLVMSCAYSLGSRSFSHALNVFEKHLNTLKHFSRKSLDSEIEVVDELFSFWKLQPFNAVMWLDKMLNYSIISITSIIEWLIKQDVTIWSRSYTWSLVNTTFNKLAARLRRSVSNKEDSSLINEANEEKEIVTNLLLSALRALISENAENIWVSHWLNLMLKYVESNFLSVKKDTIEEANEPVQENTSEEQEDTKMQPVDAVDEQPSENNQTAADATNEEK 780 O14310 Nucleoporin npp106 npp106 284812 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:9372936}. UNIPROT O14310 Pfam PF04097 Has a role in promoting mRNA export from the nucleus. {ECO:0000269|PubMed:9372936}. GO:0005829 GO:0005635 GO:0034399 GO:0005643 GO:0005634 GO:0017056 GO:0006406 GO:0016973 GO:0006606 MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLAESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEFMEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTTNIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSSSAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLMRSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHRVSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFERAISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPAYQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGDYDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVVKVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYRTISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL 933 O14329 Probable zinc transporter zrg17 zrg17 284812 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O14329 Pfam PF01545 Probable transporter involved in the regulation of zinc homeostasis. {ECO:0000269|PubMed:18199682}. Q9HGQ3 EBI-21242769,EBI-21242755 GO:0005623 GO:0005829 GO:0000139 GO:0016021 GO:0031965 GO:0005385 GO:0006882 GO:1904257 GO:0062111 MTQNHNIPTAIQIQNPINNNVSVTISDQLPKPSANNPNLLSVDTRPTHRKGHHHKHSLSHQYFLPPKNRQPLEIPASYPIPTFKETFAILTFPQKLKLTSSILFFLVAVGVLLSGDATILLTLSCSLIVEGVLIIINVWRETLDSFLVWRHTCLRYPFGMQQMELLVDFSFSILLIFLGMNLLKEPAEHAIEDWGNLHHAGDHEEETVHIHLTISLFASAIISGFALLLDHPSAHIRELNSRFFHGLTLVPSLILVLLLSLGYQVGSFLSHLLSLTIAVTALVNGFSIAKSLALMLLLTYSNKEKVFECVSLIKEDTRIDQLNYAAIWQPHYNTCIANIGLTVSGGEREQAAVREDIIRIIQKTVGSIFGAGVQPKWEISVDIQRA 386 O14657 Torsin-1B TOR1B 9606 Yes SL-0178 SL-0182 Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}. UNIPROT O14657 Pfam PF06309 OMIM 608050 DisGeNET 27348 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}. P16104 EBI-494830,EBI-2564400 A2APR8 EBI-10973834,EBI-2564400 P32971 EBI-13076860,EBI-2564400 Q9H3K2 EBI-2564400,EBI-2868909 Q9H0V9-2 EBI-2564400,EBI-21511115 Q8IWL3 EBI-1805738,EBI-2564400 A4D1S0 EBI-21511322,EBI-2564400 P20036 EBI-2802853,EBI-2564400 Q9UBM8 EBI-21494458,EBI-2564400 Q9NRD1 EBI-3938499,EBI-2564400 Q9UG22 EBI-15891037,EBI-2564400 P29016 EBI-1033762,EBI-2564400 Q9BRR6-2 EBI-21524597,EBI-2564400 GO:0005783 GO:0005788 GO:0070062 GO:0005635 GO:0031965 GO:0005524 GO:0016887 GO:0042802 GO:0019894 GO:0051085 GO:0007029 GO:0071763 GO:0034504 GO:0006986 MLRAGWLRGAAALALLLAARVVAAFEPITVGLAIGAASAITGYLSYNDIYCRFAECCREERPLNASALKLDLEEKLFGQHLATEVIFKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLHPKGLKSNFVHLFVSTLHFPHEQKIKLYQDQLQKWIRGNVSACANSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGVSYRKAIFIFLSNAGGDLITKTALDFWRAGRKREDIQLKDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYRHVKMCVRAEMRARGSAIDEDIVTRVAEEMTFFPRDEKIYSDKGCKTVQSRLDFH 336 O14681 Etoposide-induced protein 2.4 homolog EI24 9606 Yes SL-0178 SL-0182 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}. UNIPROT O14681 UNIPROT A8K7D6 UNIPROT B4DKL6 UNIPROT Q9BUQ1 OMIM 605170 DisGeNET 9538 Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.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. A0A142I5B9 EBI-20625235,EBI-2339413 P51668 EBI-2339413,EBI-743540 P62837 EBI-2339413,EBI-347677 F5H1C8 EBI-21259559,EBI-2339413 Q9H1C4 EBI-4401271,EBI-2339413 Q6NUS6 EBI-11278332,EBI-2339413 Q8N4P2 EBI-6958994,EBI-2339413 P11234 EBI-2339413,EBI-752162 P27105 EBI-1211440,EBI-2339413 Q9NUH8 EBI-8638294,EBI-2339413 O15173 EBI-1050125,EBI-2339413 Q6PL24 EBI-2339413,EBI-11603430 Q12982 EBI-2339413,EBI-752094 Q9UI14 EBI-2339413,EBI-712367 Q8IWL3 EBI-1805738,EBI-2339413 GO:0005829 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0031965 GO:0006915 GO:0016236 GO:0030308 MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTSAEKFPSPHPSPAKLKATAGH 340 O14770 Homeobox protein Meis2 MEIS2 9606 Yes SL-0198 Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}. UNIPROT O14770 UNIPROT A6NJI5 UNIPROT A8MWD5 UNIPROT B3KP98 UNIPROT B3KPQ6 UNIPROT Q96DI2 UNIPROT Q96KI4 UNIPROT Q96KI5 UNIPROT Q9NRS1 UNIPROT Q9NRS2 UNIPROT Q9NRS3 PDB 3K2A PDB 4XRM PDB 5BNG PDB 5EG0 Pfam PF05920 Pfam PF16493 PROSITE PS50071 OMIM 600987 OMIM 601740 DisGeNET 4212 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}.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. Self EBI-2804934,EBI-2804934 A0A1B0GWI1 EBI-2804934,EBI-10181422 Q5TZZ9 EBI-2804934,EBI-10181435 Q6P1W5 EBI-2804934,EBI-946029 Q9UJX0 EBI-9057006,EBI-2804934 Q5NG24 EBI-2804934,EBI-2803358 GO:0000790 GO:0048471 GO:0003677 GO:0001228 GO:0003700 GO:0000981 GO:0000978 GO:0043565 GO:0003712 GO:0003714 GO:0008134 GO:0001654 GO:0045638 GO:0000122 GO:0031016 GO:0110024 GO:0045931 GO:0045944 GO:0070848 GO:0009612 GO:0006366 GO:0008542 MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGMSMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMMMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ 477 O14976 Cyclin-G-associated kinase GAK 9606 Yes SL-0198 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. UNIPROT O14976 UNIPROT Q5U4P5 UNIPROT Q9BVY6 PDB 4C57 PDB 4C58 PDB 4C59 PDB 4O38 PDB 4Y8D PDB 5Y7Z PDB 5Y80 Pfam PF00069 Pfam PF10409 PROSITE PS51182 PROSITE PS50076 PROSITE PS51181 PROSITE PS50011 PROSITE PS00108 OMIM 602052 DisGeNET 2580 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}. O14966 EBI-372165,EBI-714707 P10275 EBI-714707,EBI-608057 Q9Y6W8 EBI-3922712,EBI-714707 Q9Y586 EBI-6659161,EBI-714707 Q5S007 EBI-714707,EBI-5323863 P11142 EBI-714707,EBI-351896 Q9UL15 EBI-714707,EBI-356517 Q38SD2 EBI-1050422,EBI-714707 Q76MZ3 EBI-400413,EBI-714707 A2AUM9 EBI-2554268,EBI-714707 P63005 EBI-917499,EBI-714707 Q9Z1Z0 EBI-7597484,EBI-714707 P10126 EBI-773865,EBI-714707 G3X972 EBI-11079353,EBI-714707 P09497 EBI-726598,EBI-714707 Q9NYZ3 EBI-2511327,EBI-714707 Q13492 EBI-2803688,EBI-714707 Q00610 EBI-354967,EBI-714707 O15027 EBI-357515,EBI-714707 P51805 EBI-714707,EBI-7135904 Q9Y496 EBI-714707,EBI-1104844 Q14789 EBI-714707,EBI-709973 Q2M2I8-2 EBI-714707,EBI-10965264 Q8N556 EBI-714707,EBI-3893163 O43175 EBI-714707,EBI-350495 O75146 EBI-714707,EBI-4402639 P47756-2 EBI-714707,EBI-353608 P27482 EBI-714707,EBI-747537 P53992 EBI-714707,EBI-81134 Q14677 EBI-714707,EBI-1171113 Q9UHB6 EBI-714707,EBI-351479 P49757-4 EBI-714707,EBI-10983190 Q9ULH0-4 EBI-714707,EBI-10982220 P42566 EBI-714707,EBI-396684 P55735 EBI-714707,EBI-1046596 Q13813 EBI-714707,EBI-351450 Q96PK6 EBI-714707,EBI-954272 E9PK67 EBI-714707,EBI-11017432 Q00610-2 EBI-714707,EBI-10963396 Q96FJ0 EBI-714707,EBI-745021 Q8IVT2 EBI-714707,EBI-2555085 P53675 EBI-714707,EBI-358826 P09496-2 EBI-714707,EBI-4401010 P08047 EBI-714707,EBI-298336 Q9H0K6 EBI-714707,EBI-5464419 Q8WXE9 EBI-714707,EBI-539742 Q27J81 EBI-714707,EBI-2557882 P14384 EBI-714707,EBI-2561541 Q14677-3 EBI-714707,EBI-10983245 P28066 EBI-714707,EBI-355475 Q3B7T1 EBI-714707,EBI-2870947 Q6ZRV2 EBI-714707,EBI-2556538 Q9UBH6 EBI-714707,EBI-8799896 O00159-3 EBI-714707,EBI-10965365 Q16643 EBI-714707,EBI-351394 Q5T0W9 EBI-714707,EBI-2556565 O00443 EBI-714707,EBI-641094 H0YEF7 EBI-714707,EBI-10983177 Q9NSY1 EBI-714707,EBI-1383367 F5GWT4 EBI-714707,EBI-11081194 P09497-2 EBI-714707,EBI-10965328 Q9UM54-6 EBI-714707,EBI-10983181 Q8N3V7-2 EBI-714707,EBI-10965260 P0DP23 EBI-714707,EBI-397435 Q9UK73 EBI-714707,EBI-310482 Q13492-2 EBI-714707,EBI-10983186 P63010 EBI-714707,EBI-432924 O94973-2 EBI-714707,EBI-10981066 Q13470-2 EBI-714707,EBI-11018037 Q8TDG2 EBI-714707,EBI-11062242 O00291 EBI-714707,EBI-473886 O95782-2 EBI-714707,EBI-10965313 Q9BY43 EBI-714707,EBI-747981 P98082 EBI-714707,EBI-1171238 Q07912 EBI-714707,EBI-603457 Q96CW1-2 EBI-714707,EBI-10965256 Q9H2Y7 EBI-714707,EBI-1211501 Q5TB80 EBI-714707,EBI-1059012 O15027-5 EBI-714707,EBI-10990372 Q8TEH3 EBI-714707,EBI-8796791 Q8N684-2 EBI-714707,EBI-5280595 P15735 EBI-1383819,EBI-714707 Q9Y4C4 EBI-2864441,EBI-714707 O43493 EBI-1752146,EBI-714707 Q8N3R9-2 EBI-16399750,EBI-714707 Q9UJ41-2 EBI-6448458,EBI-714707 Q9Q2G4 EBI-6248094,EBI-714707 Q9NQ11 EBI-714707,EBI-6308763 O60763 EBI-356164,EBI-714707 P49023 EBI-702209,EBI-714707 Q8IWL3 EBI-1805738,EBI-714707 Q6IQ23 EBI-2125301,EBI-714707 Q9P296 EBI-2874691,EBI-714707 Q8TBP5 EBI-18636064,EBI-714707 Q09019 EBI-724564,EBI-714707 Q9ULV8 EBI-2341018,EBI-714707 Q8N2M8-3 EBI-21570860,EBI-714707 Q96SL4 EBI-749411,EBI-714707 Q9NSE4 EBI-1054770,EBI-714707 Q9NZL4 EBI-356763,EBI-714707 O95630 EBI-396676,EBI-714707 O15169 EBI-714707,EBI-710484 GO:0005737 GO:0005829 GO:0005925 GO:0005794 GO:0043231 GO:0016020 GO:0048471 GO:0098793 GO:0031982 GO:0005524 GO:0051087 GO:0030276 GO:0030332 GO:0004674 GO:0007049 GO:0051085 GO:0072318 GO:1905224 GO:0072583 GO:0007029 GO:0007030 GO:0090160 GO:0061024 GO:0010977 GO:0034067 GO:0072659 GO:0006898 GO:0016191 MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF 1311 O15173 Membrane-associated progesterone receptor component 2 PGRMC2 9606 Yes SL-0178 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}. UNIPROT O15173 UNIPROT Q569H1 Pfam PF00173 OMIM 607735 DisGeNET 10424 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}. A0A142I5B9 EBI-20625235,EBI-1050125 O14681 EBI-1050125,EBI-2339413 Q9HBL7 EBI-714824,EBI-1050125 Q96I36 EBI-6570698,EBI-1050125 Q15077 EBI-10235794,EBI-1050125 P04233 EBI-2622890,EBI-1050125 Q96GC9 EBI-2800296,EBI-1050125 Q5HYA8 EBI-11334880,EBI-1050125 Q6NUS6 EBI-11278332,EBI-1050125 Q96GX1 EBI-11349465,EBI-1050125 Q9P0N5 EBI-721260,EBI-1050125 Q86UK5 EBI-7260649,EBI-1050125 Q86X19 EBI-11343485,EBI-1050125 Q9Y4C4 EBI-2864441,EBI-1050125 P11279 EBI-2805407,EBI-1050125 P02545 EBI-351935,EBI-1050125 O43493 EBI-1752146,EBI-1050125 P27824 EBI-355947,EBI-1050125 Q9NWU2 EBI-1050125,EBI-1051077 Q96G75 EBI-1050125,EBI-745055 Q9NZ01 EBI-1050125,EBI-2877718 Q8TDV0 EBI-11955647,EBI-1050125 P0DOE9 EBI-6138585,EBI-1050125 Q77M19 EBI-6149376,EBI-1050125 Q14164 EBI-1050125,EBI-307369 P05154 EBI-1050125,EBI-722597 Q9BVC6 EBI-1050125,EBI-1057733 M0R671 EBI-1050125,EBI-22236610 F1LML3 EBI-1050125,EBI-22250907 F1LM93 EBI-1050125,EBI-22238190 A0A0G2K261 EBI-1050125,EBI-22242041 Q5U2U8 EBI-1050125,EBI-12593069 Q5RKH1 EBI-1050125,EBI-22255293 D4A1H9 EBI-1050125,EBI-22247753 D4A7J8 EBI-1050125,EBI-22255230 P42346 EBI-1050125,EBI-1571489 A0A0G2K781 EBI-1050125,EBI-22253355 P00176 EBI-1050125,EBI-22254579 O08662 EBI-1050125,EBI-22259134 Q5PQL2 EBI-1050125,EBI-920599 D3ZYG0 EBI-1050125,EBI-22084151 Q925D4 EBI-1050125,EBI-21235177 D3ZGM1 EBI-1050125,EBI-22255730 M0RBS9 EBI-1050125,EBI-22254001 Q5RKH0 EBI-1050125,EBI-22247688 D4A104 EBI-1050125,EBI-22258567 O95429 EBI-2949658,EBI-1050125 O76064 EBI-1050125,EBI-373337 O60906 EBI-1050125,EBI-12828299 Q14656 EBI-1050125,EBI-13046724 Q96H72 EBI-1050125,EBI-10287091 Q96JF0-2 EBI-1050125,EBI-12908338 Q9Y5Y5 EBI-1050125,EBI-981985 Q9H2H9 EBI-1050125,EBI-9978441 Q9H2L4 EBI-1050125,EBI-2852148 P11215 EBI-1050125,EBI-2568251 Q9UBY5 EBI-1050125,EBI-12033434 O95159 EBI-1050125,EBI-718439 O60636 EBI-1050125,EBI-3914288 Q9P0L0 EBI-1050125,EBI-1059156 P01031 EBI-8558308,EBI-1050125 Q13021 EBI-1050125,EBI-750078 Q9BWQ6 EBI-1050125,EBI-751204 P02787 EBI-1050125,EBI-714319 Q9H3K2 EBI-1050125,EBI-2868909 P78329 EBI-1050125,EBI-1752413 P59542 EBI-1050125,EBI-12847034 Q7RTY0 EBI-1050125,EBI-12243266 O43681 EBI-1050125,EBI-2515857 Q86UD5 EBI-1050125,EBI-9916342 Q8IWU4 EBI-1050125,EBI-10262251 Q8IWB1 EBI-1050125,EBI-2556412 Q8IVQ6 EBI-1050125,EBI-2849773 O14569 EBI-1050125,EBI-717654 Q5RI15 EBI-1050125,EBI-2834035 O00264 EBI-1050125,EBI-1045534 Q9Y342 EBI-1050125,EBI-3919291 Q9BTX3 EBI-1050125,EBI-12876824 Q9P0S3 EBI-1050125,EBI-1054848 Q6ZPD8 EBI-1050125,EBI-12831978 Q8N661 EBI-1050125,EBI-2548832 Q96IV6 EBI-1050125,EBI-12142299 O00124 EBI-1050125,EBI-1993850 A0A024RCD1 EBI-1050125,EBI-18958976 Q6N075 EBI-1050125,EBI-3920969 Q7L5A8 EBI-1050125,EBI-11337888 Q9H9B4 EBI-1050125,EBI-355861 Q13277 EBI-1050125,EBI-1394295 I3L0A0 EBI-1050125,EBI-12213001 Q9H0Q3 EBI-1050125,EBI-713304 Q96HH6 EBI-1050125,EBI-741829 Q96GQ5 EBI-8636004,EBI-1050125 Q8N2M4 EBI-1050125,EBI-12015604 Q96PS8 EBI-1050125,EBI-12820279 Q6UX40 EBI-1050125,EBI-12845616 Q01453 EBI-1050125,EBI-2845982 Q8N5I4 EBI-1050125,EBI-3923585 Q8IWL3 EBI-1805738,EBI-1050125 P22315 EBI-1050125,EBI-7174007 Q78IK4 EBI-1050125,EBI-12523754 Q8CI59 EBI-1050125,EBI-10767480 Q62351 EBI-1050125,EBI-3869520 Q9CR62 EBI-1050125,EBI-299894 Q60930 EBI-1050125,EBI-444578 P51881 EBI-1050125,EBI-445370 P48962 EBI-1050125,EBI-299469 Q61102 EBI-1050125,EBI-6907927 Q9JI39 EBI-1050125,EBI-10767359 Q9Z2I9 EBI-1050125,EBI-773730 P08680 EBI-1050125,EBI-10767448 P58281 EBI-1050125,EBI-776163 Q8CAQ8 EBI-1050125,EBI-776087 Q80UU9 EBI-1050125,EBI-1634859 O55022 EBI-1050125,EBI-770756 GO:0012505 GO:0005783 GO:0016021 GO:0016020 GO:0005635 GO:0020037 GO:0015232 GO:0005496 GO:0003707 GO:0060612 MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGLGAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD 223 O15182 Centrin-3 CETN3 9606 Yes SL-0178 SL-0185 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}. UNIPROT O15182 UNIPROT Q53YD2 UNIPROT Q9BS23 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 602907 DisGeNET 1070 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}. Q92844 EBI-356349,EBI-712959 Q2NKQ1-4 EBI-10182463,EBI-712959 Q8NA72 EBI-712959,EBI-2561090 P04792 EBI-352682,EBI-712959 Q9H0K1 EBI-712959,EBI-1181664 Q70CQ1 EBI-2511022,EBI-712959 Q9R1K9 EBI-2553037,EBI-712959 Q9Y4C4 EBI-2864441,EBI-712959 Q5S007 EBI-5323863,EBI-712959 O14874 EBI-1046765,EBI-712959 O95976 EBI-2802079,EBI-712959 Q01831 EBI-372610,EBI-712959 Q8NA72-3 EBI-11751537,EBI-712959 P18509 EBI-8588930,EBI-712959 Q5VW00 EBI-3951747,EBI-712959 O15273 EBI-954089,EBI-712959 Q15293 EBI-948278,EBI-712959 Q9Y6K9 EBI-712959,EBI-81279 Q9UQ80 EBI-924893,EBI-712959 O43679 EBI-2865580,EBI-712959 O00141 EBI-1042854,EBI-712959 O95994 EBI-712648,EBI-712959 P19237 EBI-746692,EBI-712959 P17540 EBI-712973,EBI-712959 Q96EV8-2 EBI-16749183,EBI-712959 Q8N490-2 EBI-10769878,EBI-712959 Q12798 EBI-2512818,EBI-712959 O00212 EBI-3918631,EBI-712959 O43924 EBI-712685,EBI-712959 Q5UIP0 EBI-711331,EBI-712959 Q13432 EBI-711260,EBI-712959 GO:0005814 GO:0005813 GO:0005737 GO:0005815 GO:0044615 GO:0005730 GO:0070390 GO:0005509 GO:0008017 GO:0051301 GO:0007098 GO:0051028 GO:0015031 MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI 167 O15504 Nucleoporin NUP42 NUP42 9606 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT O15504 UNIPROT A4D143 UNIPROT B4DP42 UNIPROT Q49AE7 UNIPROT Q9BS49 PDB 6B4F PDB 6B4I PDB 6B4J PROSITE PS50103 DisGeNET 11097 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}. Q13158 EBI-494804,EBI-2515057 Q9H0R8 EBI-746969,EBI-2515057 P25054 EBI-727707,EBI-2515057 P24386 EBI-2515129,EBI-2515057 Q7KZI7 EBI-516560,EBI-2515057 Q8BH74 EBI-2554056,EBI-2515057 Q9ERU9 EBI-643756,EBI-2515057 Q6PFD9 EBI-646104,EBI-2515057 P57740 EBI-295687,EBI-2515057 P63280 EBI-80180,EBI-2515057 Q14974 EBI-286758,EBI-2515057 P49790 EBI-286779,EBI-2515057 Q9BVL2 EBI-2811583,EBI-2515057 Q09161 EBI-464743,EBI-2515057 Q8N4J0 EBI-11963218,EBI-2515057 Q92905 EBI-594661,EBI-2515057 A0A0F7RN56 EBI-2821677,EBI-2515057 Q81KT8 EBI-2515057,EBI-2809955 Q8IW93-1 EBI-25410216,EBI-2515057 P55735 EBI-2515057,EBI-1046596 A5YKK6 EBI-1222758,EBI-2515057 Q9GZY0 EBI-444173,EBI-2515057 GO:0005829 GO:0043657 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0046872 GO:0005049 GO:0003723 GO:0075733 GO:0006406 GO:0006611 GO:0016925 GO:1900034 GO:0060964 GO:0006110 GO:0006409 GO:0016032 GO:0019083 MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYFSSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAPAFGGGSSVAGFGSPGSHSHTAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQFQSKKFTLGKIPLKPPPLELLNV 423 O17213 Protein rogdi homolog H14A12 6239 Yes SL-0178 Nucleus envelope {ECO:0000250}. UNIPROT O17213 Pfam PF10259 DE Reference Proteome: Yes; GO:0005623 GO:0005635 GO:0005634 GO:0043291 GO:0032502 GO:0007035 MEVQSLTITTNYPPKPASPNPQDIRDTIRSNKTNENLWIQRKDVDTTLRSALEHLKACCIVLNLSAKCDERLNVAVSHGTTEKYQLMSRTGSSDNLKAAVTLLDDNVIQAEVTVKYPKAGGGYYRAVAQPDVQWKLQQLQDLGNHISRVTITLCDLQHEVNLLKGDGERDAFTLATGARILEELKLTMNEISLARNSIMLPRKRSLLELCYFPPTRKFVPPLPQDQLISFYISCCRLVCASYQMVPKTVHPQGLSVFMAESQLPHLDDVIKHLNTVMAILQKLINYLSATMS 292 O17482 Protein timeless tim 7244 No SL-0198 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}. UNIPROT O17482 UNIPROT O44430 UNIPROT O44785 Pfam PF04821 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}. GO:0005634 GO:0048471 GO:0048511 MDWLLATPQLQSVFSSLGSLVGGTYVVSPNALAILEEINHKLTYEDQTLRTFRRAIGFGQNVRVDLIPLLENAKDDAVLESVIRILVNLTVPVECLFSVDLMYRTEVGRHTIFELNKLLYNSKEAFTDPKSTKSVVEYMKHILESDPKLSPHKCDQINNCLLLLRNILHIPETHAHFLMPRLQPGSGHQVSMQNTILWNLFIQSIDKLLLYLMTCPQRSLWGVTMVQLIALIYKDQHVSTLQKLLNLWFEASLSESSDDNESNTTPPKQASGDSSPMLTSDPTSDSSDNGSGGKKESCEERRQALREGTDATLHEVSRKGHEYQNAMASSNAANYILEGPCSAQQPWSDCEMQEYKQMTAVISEPLNLSQPADNVNYTTNANYARTTSTDILTKTTSLKHEGFKPPAPRRNTLSAILSDNYAPLSFISAVKLGQKSPHAGQLQLIKGKCCPQKRECPSSQSEHSDCGYGTQMENPESISTSSNDDDGPQGKPQHQKPPCSSKHRSKQRIFAVPQDTKDLRRKKLVKRSKSSLINMKGLVLHTPNDDDISNLLKEFTVDFLLKGYNYLVEELHSQLLSNAKMPIDTSHFFWLVTFFLKFAAQLELDMEHIDTILTFDVLSFLTYEGVSLCEQLELNARQEGADLRPYLRRMHLVVTAIREFLQAIEAYNKVTHLSEDDRYRLRQLQLQISATTDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDNAAKLEGGQTIGLSEHISQFATLEVMHYYGILLEDFSNNGEYVNDCIFTMMHHIGGDLDQVGVLYQPIILKAYSRIWEADYDICDDWSDLIEYVIHKFLNTPPKSPMAIPTASLTELTKEQNQEHTACPWSQEDMDSLCWYFVQSKRQNDVIGNIAKLFSNNGNKIKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLATPTSLTTDSGIELKESAYGKPSDDVQVLLDLIRKENKSQHLVWLQKLLLECCYVKMMIKCGSCQTDVEPIMEPVVYHCMFKQKPIPVVQWNNEQSSTMLYQPFMLLLHKLGIQLPADAGLIFARIPDFWTPETMYGLAKKLGPLDKLTLKFDPRDLEDAPPSRHHTGARNSLSSISSLEADFGDSEGLALIPEVDPAVEKAAAAASAIPNNEIFALPRVKHCNSIIRYTPDPTPPVPSWLQLVMRTKCSKRRSPATDASDCTSTSTMIADDEIKSYASMAQASHTKLNSGYPTSTLVCMNKLSNCSFAAPPNENSSSSGCGGTASSMSMPNMPDGNSDALMKTSFERLAVTGARYLRPSNTDQDYSALVASVYENEFANSDNVSVASDLTRMYVSDEDEKHELQLQQVE 1343 O18158 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase ogt 6239 Yes SL-0198 Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9083068}. UNIPROT O18158 UNIPROT Q21232 Pfam PF13844 Pfam PF00515 Pfam PF13181 PROSITE PS50005 PROSITE PS50293 Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. {ECO:0000250|UniProtKB:O15294}. Q17446 EBI-313084,EBI-312987 GO:0005634 GO:0048471 GO:0016262 GO:0097363 GO:0004722 GO:0040024 GO:0006112 GO:0005977 GO:0009100 GO:0019915 GO:0006470 GO:0006493 GO:0000003 GO:0009266 MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAVNQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLPTLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSGGDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVSAYLRALNLSGNHAVVHGNLACVYYEQGLIDLAIDTYKKAIDLQPHFPDAYCNLANALKEKGSVVEAEQMYMKALELCPTHADSQNNLANIKREQGKIEDATRLYLKALEIYPEFAAAHSNLASILQQQGKLNDAILHYKEAIRIAPTFADAYSNMGNTLKEMGDSSAAIACYNRAIQINPAFADAHSNLASIHKDAGNMAEAIQSYSTALKLKPDFPDAYCNLAHCHQIICDWNDYDKRVRKLVQIVEDQLCKKRLPSVHPHHSMLYPLSHAARIAIAAKHASLCFDKVHVQMLGKTPLIHADRFSVQNGQRLRIGYVSSDFGNHPTSHLMQSIPGMHDRSRVEVFCYALSVNDGTNFRSKLMNESEHFVDLSQIPCNGKAAEKIAQDGIHILINMNGYTKGARNEIFALRPAPIQVMWLGYPSTSGATFMDYIITDAVTSPLRLANAFTEKLAYMPHTFFIGDHAQMLRHLTDKVVVKDKETTERDSCLIMNTANMDPILAKSEIKEQVLDTEVVSGPNKELVRAEMVLPVLEVPTEPIKQMIMTGQMTMNVMEDMNVQNGLGQSQMHHKAATGEEIPNSVLLTSRAQYQLPDDAIVFCNFNQLYKIDPSTLDMWIKILENVPKSILWLLRFPYQGEEHIRKYCVERGLDPSRIVFSNVAAKEEHVRRGQLADVCLDTPLCNGHTTGMDILWTGTPMVTMPLESLASRVATSQLYALGVPELVAKTRQEYVSIAVRLGTDADHLANMRAKVWMARTSSTLFDVKQYCHDMEDLLGQMWKRYESGMPIDHITNNTETPHGL 1151 O18735 Receptor tyrosine-protein kinase erbB-2 ERBB2 9615 Yes SL-0198 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}. UNIPROT O18735 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. GO:0009925 GO:0005769 GO:0005887 GO:0005634 GO:0048471 GO:0005886 GO:0043235 GO:0005524 GO:0001042 GO:0004714 GO:0071364 GO:0071363 GO:0035556 GO:0007275 GO:0030182 GO:0030307 GO:0008284 GO:0033674 GO:0043410 GO:0090314 GO:0045943 GO:0045727 GO:0070372 GO:0032886 GO:0007169 MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQLCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVFEALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTVPWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCLPCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKGCPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGGTAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLPPETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEYLAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV 1259 O18737 Calcium-binding and coiled-coil domain-containing protein 2 CALCOCO2 9913 Yes SL-0198 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}. UNIPROT O18737 Pfam PF17751 Pfam PF18112 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:1901098 GO:0098792 MEETVDDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDITCYYTLTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPVDLNSESAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLLSYMGLDCDSLSYQVPTSNQGGTRQDPGLVFGNPYSGIQESSAPSLLSIKKCPTCKSDFAADVFDHNLALEQHLQTLSLNCPICDKTFPAKEKQIFEDHVFCHTL 450 O22224 Nuclear pore complex protein NUP93A NUP93A 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT O22224 UNIPROT Q94CF2 Pfam PF04097 DE Reference Proteome: Yes; Q01525 EBI-637502,EBI-2356241 GO:0005635 GO:0005643 GO:0005730 GO:0009506 GO:0017056 GO:0016973 GO:0006606 MANDQEMSGWTDLLHSSSKLLEQAAPSSQFPPLQRNLDQLEALSKKLKAKTLRNEAPSQSIAATRLLAREGINAEQLARDLKSFELKTTFEDVFPAEATSVEEYLQQVHEMAMVSAIQEAQKDNVRSFNDYMMKVLEEDWRKEKRDFLQSLSRISMLPKTNMIDTSREAHAGQLVPVGSSPRVSSTPGKELVALANIPIHEKKAYVYGEVVKKLNTSRERGMPFRPAMCFKDAYDTLGAEVTRGKSVNMQKIWQLVQAITGEDSAVRQGVSKRMALAIGARHHLQHGHEKFIMDTIQTHPTQAALGGSVGNLQRIRAFLRIRLRDYGVLDFDSTDARRQPPVDTTWQQIYFCLRTGYYEEAREIARSTRSSQQFAPLLTEWITTDGMVAAESAAIASEECEKMLRMGDRLGRTAYDKKKLLLYTIISGSRRQIERILRDLSTLFNTIEDFLWFKLSCIRDVTGGSSSVVLNDGLAPYSLDDLQAYLNKFEPSYYTKNGKDPLVYPYVLLLSVQLLPAIMHLSKEAGDGGYNIDAVHIAISLVDHSVLSEGSGTGHKLSVMDSNAEASSMIRQYGSMFLHHGDLQMTVEYYAQAAATVGGGQLAWSGRSNVDQQRQRNLMLKQLLTEILLRERGIYFLLGARGSGEEGQLGRFFPDSRLRQQFLVEAAHQCQEAGLYDKSIELQKRVGAFSAALETINKCLSEAICSLARGRLDGESRTSGLILAGNDILETYKYYPEVSLQERERVMEQETILRELEAILSIHKLGRLGNHLDALREIAKLPFLHLDPRMPDATADVFQSASPYFQTCVPDLLKVALTCLDNVPDTDGSIRAMRSKIAGFLASNTHRNWPRDLYEKVARSF 861 O22873 bZIP transcription factor 18 BZIP18 3702 Yes SL-0198 Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm {ECO:0000269|PubMed:27896439}. UNIPROT O22873 UNIPROT O23726 Pfam PF00170 PROSITE PS50217 Transcription factor that may participate with bZIP34 in the gametophytic control of pollen development. {ECO:0000269|PubMed:27896439}. Q9LZW4 EBI-4438646,EBI-307576 Q94AY3 EBI-1787347,EBI-4438646 GO:0005737 GO:0005654 GO:0005634 GO:0048471 GO:0003700 GO:0043621 GO:0044212 MEDPSNPQPNQSNLSQCPPLATAPTPAPVRGPYHRRAHSEVQFRLPEDLDLSEPFGGFDELGSEDDLFCSYMDIEKLGSGSGSASDSAGPSAPRSDNPFSAENGGAEAGNSRPRHRHSLSVDGSSTLESIEAKKAMAPDKLAELWVVDPKRAKRIIANRQSAARSKERKARYILELERKVQTLQTEATTLSAQLSLFQRDTTGLSSENTELKLRLQVMEQQAKLRDALNEQLKKEVERLKFATGEVSPADAYNLGMAHMQYQQQPQQSFFQHHHQQQTDAQNLQQMTHQFHLFQPNNNQNQSSRTNPPTAHQLMHHATSNAPAQSHSYSEAMHEDHLGRLQGLDISSCGRGSNFGRSDTVSESSSTM 367 O23523 RGG repeats nuclear RNA binding protein A RGGA 3702 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:25783413}. Nucleus {ECO:0000250|UniProtKB:Q9SQ56, ECO:0000255|PROSITE-ProRule:PRU00768}. UNIPROT O23523 UNIPROT A8MQG3 UNIPROT A8MQJ5 Pfam PF04774 Pfam PF09598 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}. GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0003729 GO:0009738 GO:0071470 GO:0071472 GO:0009787 GO:0009737 GO:0006970 GO:0009651 MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLPPAQAVREARSDAPRGGGGRGGFNRGRGGYNRDDGNNGYSGGYTKPSGEGDVSKSSYERRGGGGAPRGSFRGEGGGPGGGRRGGFSNEGGDGERPRRAFERRSGTGRGSDFKRDGSGRGNWGTPGEEIAAETEAVAGVETEKDVGEKPAVDDVAADANKEDTVVEEKEPEDKEMTLDEYEKILEEKKKALQSLTTSERKVDTKVFESMQQLSNKKSNDEIFIKLGSDKDKRKDDKEEKAKKAVSINEFLKPAEGGNYYRGGRGGRGRGGRGRGGVSSGESGGYRNEAAPAIGDAAQFPSLGGK 355 O23593 RGG repeats nuclear RNA binding protein B RGGB 3702 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q9SQ56}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}. UNIPROT O23593 UNIPROT Q8LB56 Pfam PF04774 Pfam PF09598 Binds RNA. {ECO:0000250|UniProtKB:Q9SQ56}. GO:0005829 GO:0005634 GO:0048471 GO:0005777 GO:0003729 MASVNPFDLLDDDAEDPSQIVASKPLKVVAPVQTAKSGKMPTKPPPPSQAVREARNAPGGGRGAGRGGSYGRGGRGGNNRDSRNNDGPANENGYGGGYRRSEEGDGARRGGPVGGYRGDRRGSYSNGGDSGDSERPRKNYDRHSRTAYGNEDKRDGAGRANWGTTQDDITPVTEESTAVVDKNLTVEKQDGEGEATDAKNETPAEKAEEKPEDKEMTLEEYEKVLEEKKKALQATKVEERKVDTKAFEAMQQLSSKKSNNDEVFIKLGTEKDKRITEREEKTRKSLSINEFLKPADGKSYYRPRGGYQGGREGRGPREGNQRDGGRNLREGGRNQRDGGAAAQAPTPAIGDSAQFPTLGK 360 O35346 Focal adhesion kinase 1 Ptk2 10116 Yes SL-0198 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}. UNIPROT O35346 UNIPROT Q62900 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS00661 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. Q5XI86 EBI-6252926,EBI-6252940 GO:0005912 GO:0016324 GO:0016323 GO:0005623 GO:0005737 GO:0005829 GO:0043197 GO:0005925 GO:0098978 GO:0014704 GO:0030027 GO:0005815 GO:0016604 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0098794 GO:0042383 GO:0001725 GO:0003779 GO:0005524 GO:0042802 GO:0005178 GO:0008432 GO:0004715 GO:0019902 GO:0043548 GO:0019901 GO:0019903 GO:0004713 GO:0044877 GO:0042169 GO:0031625 GO:0001525 GO:0001568 GO:0030644 GO:0071560 GO:0021955 GO:0043542 GO:0048013 GO:0007173 GO:0030198 GO:0045444 GO:0060396 GO:0007229 GO:0007254 GO:0000165 GO:0000226 GO:2000811 GO:0043066 GO:0010507 GO:0050771 GO:0030336 GO:0022408 GO:0046621 GO:0051964 GO:0001764 GO:0007097 GO:0038083 GO:0018108 GO:0097755 GO:0010613 GO:0045785 GO:0030307 GO:0030335 GO:0008284 GO:0060252 GO:0050766 GO:0014068 GO:0045860 GO:0051897 GO:0001934 GO:0014911 GO:0048661 GO:0050806 GO:2000060 GO:0046777 GO:0030155 GO:0033628 GO:0042127 GO:0008360 GO:0010632 GO:0051893 GO:0045667 GO:0001932 GO:1900024 GO:0046685 GO:0042493 GO:0032355 GO:0009749 GO:0009612 GO:0014070 GO:0010033 GO:0010243 GO:0007172 GO:0007179 GO:0001570 MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH 1055 O35387 HCLS1-associated protein X-1 Hax1 10090 Yes SL-0178 SL-0182 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}. UNIPROT O35387 UNIPROT Q542F8 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}. O14925 EBI-642449,EBI-1047996 Q9H477 EBI-642449,EBI-10982959 H3BS42 EBI-642449,EBI-10984149 P56199 EBI-642449,EBI-2554465 P10809 EBI-642449,EBI-352528 P37198 EBI-642449,EBI-347978 Q92604 EBI-642449,EBI-6116942 P12236 EBI-642449,EBI-356254 Q9H061 EBI-642449,EBI-10963884 Q7KZ85 EBI-642449,EBI-2515547 O15066 EBI-642449,EBI-3931791 Q9H078-2 EBI-642449,EBI-10984145 O75165 EBI-642449,EBI-4324603 G3XAN4 EBI-642449,EBI-10982949 B4E1G1 EBI-642449,EBI-10984153 P42227 EBI-642449,EBI-602878 Q8BWG8 EBI-642449,EBI-641778 Q8CIH5 EBI-642449,EBI-617954 GO:0015629 GO:0016324 GO:0005938 GO:0030136 GO:0005737 GO:0005783 GO:0043231 GO:0030027 GO:0005758 GO:0005741 GO:0005739 GO:0031965 GO:0000932 GO:0016529 GO:0005667 GO:0019966 GO:0019904 GO:0047485 GO:0007166 GO:0071345 GO:0043066 GO:2000251 GO:0030854 GO:0033138 GO:0050731 GO:0014068 GO:0051897 GO:0045944 GO:0030833 MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR 280 O35413 Sorbin and SH3 domain-containing protein 2 Sorbs2 10116 Yes SL-0198 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}. UNIPROT O35413 UNIPROT Q923T8 Pfam PF00018 Pfam PF14604 Pfam PF02208 PROSITE PS50002 PROSITE PS50831 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}. P49286 EBI-7458031,EBI-1188341 GO:0016324 GO:0030425 GO:0005925 GO:0030027 GO:0043025 GO:0048471 GO:0005886 GO:0014069 GO:0045202 GO:0003676 GO:0019904 GO:0095500 GO:0007015 GO:0061049 GO:0007219 GO:1904393 MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDKKSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSRAQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCDDLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCPKRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPFRRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQPFHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEVKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAIAKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSLSSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL 1196 O35425 Bcl-2-related ovarian killer protein Bok 10090 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT O35425 Pfam PF00452 PROSITE PS50062 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}. GO:0005623 GO:0033106 GO:0005737 GO:0031901 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0005743 GO:0031966 GO:0005741 GO:0005739 GO:0005640 GO:0005634 GO:0055038 GO:0032588 GO:0051400 GO:0046983 GO:0046982 GO:0042803 GO:0044877 GO:0005102 GO:0031625 GO:0006919 GO:0008635 GO:0006915 GO:0007420 GO:0006921 GO:0097192 GO:0072332 GO:0008630 GO:0008584 GO:0051902 GO:1901029 GO:0060546 GO:0043524 GO:0051402 GO:0048709 GO:0043065 GO:1902237 GO:1900119 GO:2001244 GO:1901030 GO:1903899 GO:0051259 GO:0010506 GO:1901382 GO:0051480 GO:1904708 GO:0001836 MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER 213 O35646 Calpain-6 Capn6 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}. UNIPROT O35646 UNIPROT Q3UM55 Pfam PF00168 Pfam PF01067 Pfam PF00648 PROSITE PS50004 PROSITE PS50203 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}. GO:0005737 GO:0005874 GO:0048471 GO:0005876 GO:0008017 GO:0001578 GO:0006508 GO:0051493 MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGNKAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQEVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDDGEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL 641 O35744 Chitinase-like protein 3 Chil3 10090 Yes SL-0178 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. UNIPROT O35744 UNIPROT P70201 UNIPROT Q3U462 UNIPROT Q3UV87 UNIPROT Q61201 PDB 1E9L PDB 1VF8 Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0031410 GO:0005576 GO:0005635 GO:0048237 GO:0004563 GO:0030246 GO:0008061 GO:0102148 GO:0006032 GO:0006954 GO:0000272 MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY 398 O35864 COP9 signalosome complex subunit 5 Cops5 10090 Yes SL-0198 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}. UNIPROT O35864 UNIPROT Q3UA70 UNIPROT Q8C1S1 Pfam PF18323 Pfam PF01398 PROSITE PS50249 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}. GO:0030054 GO:0000785 GO:0008180 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0008021 GO:0005667 GO:0019899 GO:0035718 GO:0046872 GO:0004222 GO:0008237 GO:0019784 GO:0004843 GO:0003713 GO:1990182 GO:0043066 GO:0051091 GO:0045944 GO:0000338 GO:0016579 GO:0051726 GO:1903894 GO:0046328 GO:0006355 MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA 334 O36388 Envelope glycoprotein M gM 654901 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT O36388 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MKSSKKDIFILHIWLKLMGCYVFMFITSVVLPIAAMFPNLGFPCYYNTLVDYSKLNLREKNQAQHLTPTLFLEAPEMFFYVTYSFIVDCCSLVYYALAAVAVVKAKKHAPGLMALSQWIMAVGSPTLLYMAVLKLWTIQLYIHTLSYKHIYLAAFVYCLHWLLSMVYTECYITNVSSQWTSSELKKTIPENILLYRVVHVLKPIMMNVHLSVVALETLIFCLSFMMAIGNSFYVMVSDIVFGAINLYLILPIIWYFVTEFWLSKYLPRQFGFYFGVLVASIILILPVVRYDKIFVAAQIHRAVSINIAMIPLCALVALLVRACRVYTDRKKIAYTALPSKPQTIKYTKPIEPSTKQAPDSSIFLEEESDTDFEQ 374 O36417 Nuclear egress protein 2 NEC2 654901 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT O36417 Pfam PF04541 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}. GO:0044201 GO:0016021 MASGKKLIDQLCSVVSSFLCPSISSLDIDRCAVGPHIFSRGSSQAICTVKLLHGEVYNLEFVYRYWAHILEKYNFPFSPTFIICNNGLAVTLKCYVSEPRDLSSRYGQATSMALDVNLQRNSFVVLSQDDFIKFKTPLVFAKDLDITNSMVVCRTYLTSSRNSLQFLVVKSKNPRRLENVLDMIKRAVEATGSNLPATREKPLPLEQTEQLESTLPSSGHLRVLQSTSLTGRCPSWGAACALLLLSLAVGLMAILAAKLMQWP 263 O36420 Nuclear egress protein 1 NEC1 654901 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT O36420 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MHKIQKMSCTPSVRSRYTLKRKRLNSAKSATLKKKKVFLSNSEFFAGVSTNYELGKDFLREMDTPICTSNTVFLPVKFSDVAPGRCLTLSPYGHSSVLGFHCQECKPDSSSGFTQAQQSAESNELLSVNLCFLNNVEKVVQHKAFYLSLLGHSMNTVKQSLGQPSLLYCYTVLKKFYPQIFPIFTANGPMLTMYIIFTSLTLHVSEAVLRILTDNVENHNLSADCYKGHYILSIEPQALEESNLNVCVTKICDLVAQLDFSDELKQEYVNGSTLIANFLN 280 O40955 RNA-directed RNA polymerase p90 POLN 11044 No SL-0382 [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}. UNIPROT O40955 Pfam PF01661 Pfam PF05407 Pfam PF00978 Pfam PF12601 Pfam PF01443 PROSITE PS51743 PROSITE PS51154 PROSITE PS51657 PROSITE PS50507 PROSITE PS51889 [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}. GO:0033644 GO:0044220 GO:0016020 GO:0005524 GO:0004197 GO:0046872 GO:0008174 GO:0003723 GO:0003724 GO:0003968 GO:0006396 GO:0006351 GO:0039694 MERLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRPCTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAEVGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNARLAGIMKSAKRCAADSLSVAGWLDTIWGAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEIAATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAEHRALRCREWDFEVLRARADTAAAPAPLAPRPARYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARAWAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQSAATSSPPGDPPPPRCARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPVPPTSAGPADRARDAELEVAYEPSGPPTSTKADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVATPGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWARVACPLLGAGVYGWSAAESLRAALAATRTEPAERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELCRYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGVPQVRCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPRCAYGRALSEARTHKDFAALSQRWSASHADASSDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGGGPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTTRILAAFTREDLYVCPTNALLHEIQAKLRARDIEIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVICVGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVRRLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAELKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKNHTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAARELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKIIMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLRELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKHVSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVRELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD 2116 O42446 Deoxyribonuclease-1 dnase1 8127 No SL-0178 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}. UNIPROT O42446 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0004530 GO:0000737 GO:0002283 GO:0002673 GO:0070948 MQTYRSRMHLVCSLGLFLTLLHLSNSLLLGAFNIKSFGDTKASNATLMNIITKIVKRYDVILIQEVRDSDLSATQTLMNYVNKDSPQYKYIVSEPLGASTYKERYLFLYREALVSVVKSYTYDDGPEETGQDTFSREPFVVMFSSKNTAVRDFTLIPQHTSPDLAVRELNALYDVVLDVRARWNTNDIVLLGDFNAGCSYVSGSAWQQIRIFTDKTFHWLITDAADTTVSQTVCPYDRIVVTTDMMRGVVQNSAKVYNYMTDLNLKQDLALAVSDHFPVEVKLS 284 O43463 Histone-lysine N-methyltransferase SUV39H1 SUV39H1 9606 Yes SL-0178 SL-0180 Nucleus. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin. UNIPROT O43463 UNIPROT B2R6E8 UNIPROT B4DST0 UNIPROT Q53G60 UNIPROT Q6FHK6 PDB 3MTS Pfam PF00385 Pfam PF05033 Pfam PF00856 PROSITE PS00598 PROSITE PS50013 PROSITE PS50868 PROSITE PS50867 PROSITE PS51579 PROSITE PS50280 OMIM 300254 DisGeNET 6839 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}. O43159 EBI-2008793,EBI-349968 P17987 EBI-349968,EBI-356553 Q99832 EBI-349968,EBI-357046 P48643 EBI-349968,EBI-355710 P45973 EBI-349968,EBI-78219 P78371 EBI-349968,EBI-357407 P50991 EBI-349968,EBI-356876 P40227 EBI-349968,EBI-356687 P83916 EBI-349968,EBI-78129 P01106 EBI-349968,EBI-447544 P49368 EBI-349968,EBI-356673 O75556 EBI-349968,EBI-8830751 Q8IWI9 EBI-349968,EBI-2815196 Q14839 EBI-349968,EBI-372916 P50990 EBI-349968,EBI-356507 O60281 EBI-349968,EBI-1224010 Q13185 EBI-349968,EBI-78176 P60409 EBI-10172290,EBI-349968 Q8NHQ1 EBI-739624,EBI-349968 Q96ED9 EBI-349968,EBI-743290 Q9BRK4 EBI-741037,EBI-349968 V9HWG0 EBI-349968,EBI-10183977 Q63HR2 EBI-949753,EBI-349968 Q8TB24 EBI-1570523,EBI-349968 P52732 EBI-355697,EBI-349968 P26447 EBI-717058,EBI-349968 P24588 EBI-703640,EBI-349968 P83917 EBI-78119,EBI-349968 Q9UER7 EBI-77321,EBI-349968 Q13371 EBI-349968,EBI-5772890 Q9UPU5 EBI-349968,EBI-1642365 Q9NPA3 EBI-349968,EBI-750096 Q9H582-2 EBI-349968,EBI-21512288 Q9H0I2-2 EBI-349968,EBI-20831259 Q9BTE3-2 EBI-349968,EBI-9384556 Q96KQ7-2 EBI-349968,EBI-744391 Q93008-1 EBI-349968,EBI-10964523 Q70CQ2-2 EBI-349968,EBI-21521617 Q6VMQ6-2 EBI-349968,EBI-12070560 Q5TDH0-3 EBI-349968,EBI-21659653 Q15047-3 EBI-349968,EBI-11149962 Q15018 EBI-349968,EBI-1056583 O60732 EBI-349968,EBI-1188463 O00257 EBI-349968,EBI-722425 Q92997 EBI-739789,EBI-349968 P60410 EBI-10171774,EBI-349968 Q8WV44 EBI-725997,EBI-349968 Q96I34 EBI-710402,EBI-349968 Q9UGI0 EBI-527853,EBI-349968 Q7Z4V0 EBI-11962468,EBI-349968 Q8TAU3 EBI-740727,EBI-349968 Q8WW24 EBI-349968,EBI-750487 Q8N680 EBI-2515601,EBI-349968 A6NEM1 EBI-5916454,EBI-349968 Q96ED9-2 EBI-10961706,EBI-349968 Q6TGC4 EBI-10892722,EBI-349968 Q15156 EBI-349968,EBI-867256 P29590 EBI-295890,EBI-349968 P68432 EBI-349968,EBI-79764 GO:0005677 GO:0000775 GO:0000794 GO:0000792 GO:0005652 GO:0005654 GO:0005634 GO:0033553 GO:0003682 GO:0042054 GO:0046974 GO:0018024 GO:0047485 GO:0008757 GO:0000976 GO:0008270 GO:0007049 GO:0030154 GO:0006974 GO:0071456 GO:0006325 GO:0000183 GO:0036123 GO:0036124 GO:0034968 GO:0042754 GO:0000122 GO:0045892 GO:0048511 GO:0006364 GO:0016032 MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF 412 O43502 DNA repair protein RAD51 homolog 3 RAD51C 9606 Yes SL-0198 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. UNIPROT O43502 UNIPROT O43503 UNIPROT Q3B783 Pfam PF08423 PROSITE PS50162 OMIM 602774 OMIM 613390 OMIM 613399 DisGeNET 5889 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}.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. O43542 EBI-2849976,EBI-2267048 O75173 EBI-3934482,EBI-2267048 Q6JEL2 EBI-2267048,EBI-6426253 Q96MF4 EBI-2267048,EBI-21802615 P43378 EBI-2267048,EBI-742898 O43543 EBI-3918457,EBI-2267048 Q86YZ3 EBI-2267048,EBI-1047017 Q8IZS8 EBI-2267048,EBI-2267087 O00571 EBI-2267048,EBI-353779 O15315 EBI-2267048,EBI-2824089 Q8TBP5 EBI-18636064,EBI-2267048 Q9UK85 EBI-1753048,EBI-2267048 Q15768 EBI-3908475,EBI-2267048 Q5T8I9 EBI-9675710,EBI-2267048 Q9HBV2 EBI-17498703,EBI-2267048 GO:0030054 GO:0005737 GO:0005829 GO:0043231 GO:0005739 GO:0005654 GO:0005634 GO:0048471 GO:0033063 GO:0033065 GO:0005657 GO:0005524 GO:0008821 GO:0003677 GO:0008094 GO:0007596 GO:0006310 GO:0006281 GO:0000724 GO:0007066 GO:0007141 GO:0010971 GO:0007131 GO:0007062 GO:0007283 GO:0000722 MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSESHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVIVDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRKQRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL 376 O43567 E3 ubiquitin-protein ligase RNF13 RNF13 9606 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O43567 UNIPROT A6NC87 UNIPROT B3KR12 UNIPROT Q05D66 UNIPROT Q6IBJ9 PDB 5ZBU PDB 5ZC4 Pfam PF02225 Pfam PF13639 PROSITE PS50089 OMIM 609247 OMIM 618379 DisGeNET 11342 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}.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. P51668 EBI-743540,EBI-2129183 P62837 EBI-347677,EBI-2129183 P61077 EBI-348268,EBI-2129183 Q9Y2X8 EBI-745527,EBI-2129183 P51965 EBI-2129183,EBI-348546 Q969T4 EBI-2129183,EBI-348496 P61088 EBI-2129183,EBI-1052908 Q13404 EBI-2129183,EBI-1050671 P22314 EBI-2129183,EBI-709688 P42229 EBI-749537,EBI-2129183 P48681 EBI-10966836,EBI-2129183 P32241 EBI-3917984,EBI-2129183 O00214 EBI-740058,EBI-2129183 O00182-2 EBI-12130578,EBI-2129183 Q86Y82 EBI-2691717,EBI-2129183 Q9UEU0 EBI-723716,EBI-2129183 O43291 EBI-7810230,EBI-2129183 Q9Y240 EBI-3957044,EBI-2129183 Q9H8J5 EBI-2830042,EBI-2129183 Q9Y3E1 EBI-2129183,EBI-2847459 Q9H6Y7 EBI-2129183,EBI-1055214 Q92572 EBI-2129183,EBI-4289921 P59780 EBI-2129183,EBI-3914571 P56377 EBI-2129183,EBI-1054374 P51798 EBI-2129183,EBI-4402346 P29597 EBI-2129183,EBI-1383454 P24468 EBI-2129183,EBI-2795198 O60637 EBI-2129183,EBI-750541 O43602-2 EBI-2129183,EBI-14148644 O14617-2 EBI-2129183,EBI-21566092 GO:0005829 GO:0005783 GO:0005789 GO:0000139 GO:0016021 GO:0043231 GO:0031902 GO:0005765 GO:0005637 GO:0005654 GO:0008432 GO:0046872 GO:0061630 GO:0004842 GO:0070304 GO:0051865 GO:0006511 MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSAQSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV 381 O43586 Proline-serine-threonine phosphatase-interacting protein 1 PSTPIP1 9606 Yes SL-0198 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}. UNIPROT O43586 UNIPROT B5BU74 UNIPROT B5BUK4 UNIPROT O43585 UNIPROT O95657 PDB 2DIL Pfam PF00611 Pfam PF14604 PROSITE PS51741 PROSITE PS50002 OMIM 604416 OMIM 606347 DisGeNET 9051 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}.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. Self EBI-1050964,EBI-1050964 Q8WWY3 EBI-1567797,EBI-1050964 O00560 EBI-1050964,EBI-727004 O43684 EBI-1050987,EBI-1050964 Q86YD7 EBI-1050964,EBI-6658203 Q9H788 EBI-747035,EBI-1050964 Q96B02 EBI-716589,EBI-1050964 Q96D16 EBI-1050964,EBI-744419 Q14D33 EBI-10217913,EBI-1050964 O75386 EBI-5357290,EBI-1050964 Q9UQ90 EBI-1050964,EBI-717201 Q9Y228 EBI-765817,EBI-1050964 Q9Y473 EBI-3438881,EBI-1050964 Q9Y4Z0 EBI-1050964,EBI-372521 Q9Y5E9 EBI-1050964,EBI-10329013 P48023 EBI-495538,EBI-1050964 X5D7R7 EBI-1050964,EBI-21250265 X5DP17 EBI-1050964,EBI-21250593 Q96T60 EBI-1050964,EBI-1045072 Q09161 EBI-464743,EBI-1050964 P62910 EBI-438408,EBI-1050964 P31939 EBI-1048599,EBI-1050964 Q9UMN6 EBI-765774,EBI-1050964 Q9UBS9 EBI-1056837,EBI-1050964 Q9BVP2 EBI-641642,EBI-1050964 Q9UKX3 EBI-1050964,EBI-373433 Q96LW2 EBI-1054572,EBI-1050964 P49207 EBI-1051893,EBI-1050964 P05408 EBI-722635,EBI-1050964 P42766 EBI-1050964,EBI-356819 P61513 EBI-356793,EBI-1050964 Q15058 EBI-1045252,EBI-1050964 Q9Y3U8 EBI-1057689,EBI-1050964 Q75MH1 EBI-1058398,EBI-1050964 Q7L1Q6 EBI-1046727,EBI-1050964 Q8IZX4 EBI-475871,EBI-1050964 P62750 EBI-353254,EBI-1050964 P61254 EBI-352405,EBI-1050964 Q9Y265 EBI-353675,EBI-1050964 Q9UJX6 EBI-396211,EBI-1050964 Q02543 EBI-350523,EBI-1050964 P83881 EBI-1054835,EBI-1050964 Q9Y6E2 EBI-1051021,EBI-1050964 P18077 EBI-353383,EBI-1050964 P37268 EBI-714550,EBI-1050964 P62899 EBI-1053664,EBI-1050964 P39023 EBI-1056348,EBI-1050964 Q76P68 EBI-1059174,EBI-1050964 Q99996 EBI-1048311,EBI-1050964 P15924 EBI-355041,EBI-1050964 P47914 EBI-714039,EBI-1050964 P46779 EBI-366357,EBI-1050964 Q9NR30 EBI-357942,EBI-1050964 P16403 EBI-358372,EBI-1050964 O43390 EBI-713419,EBI-1050964 Q53FD0-2 EBI-1050964,EBI-14104088 Q8IX18 EBI-1050964,EBI-2514301 Q05209 EBI-1050964,EBI-2266035 Q15287 EBI-1050964,EBI-395959 Q2TBE0 EBI-1050964,EBI-5453285 P00540 EBI-1050964,EBI-1757866 Q9BWG6 EBI-1050964,EBI-748391 Q03014 EBI-1050964,EBI-747421 P17752 EBI-1050964,EBI-3956833 O75031 EBI-7116203,EBI-1050964 Q96GM5 EBI-1050964,EBI-358489 A0A0S2Z5X4 EBI-1050964,EBI-16429014 P28702-3 EBI-1050964,EBI-16429492 O15169 EBI-1050964,EBI-710484 P32969 EBI-1050964,EBI-358122 Q96GY3 EBI-1050964,EBI-748884 Q08426 EBI-1050964,EBI-2339219 Q9UK33 EBI-1050964,EBI-746277 Q3SY00 EBI-1050964,EBI-10241197 Q96EZ8 EBI-1050964,EBI-348259 Q9H9D4 EBI-1050964,EBI-347633 Q63ZY3 EBI-1050964,EBI-2556193 Q14005-2 EBI-1050964,EBI-17178971 P0CG20 EBI-1050964,EBI-11986293 Q9GZV7 EBI-1050964,EBI-11956675 Q06630 EBI-1050964,EBI-36794 Q12446 EBI-1050964,EBI-10022 O15553 EBI-7644532,EBI-1050964 GO:0032154 GO:0005737 GO:0005856 GO:0005829 GO:0030027 GO:0016020 GO:0048471 GO:0005886 GO:0001931 GO:0008092 GO:0042802 GO:0007155 GO:0006897 GO:0006954 GO:0045087 GO:0007165 MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL 416 O43709 Probable 18S rRNA (guanine-N(7))-methyltransferase BUD23 9606 Yes SL-0198 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}. UNIPROT O43709 UNIPROT A8K501 UNIPROT C9K060 UNIPROT Q96P12 UNIPROT Q9BQ58 UNIPROT Q9HBP9 PDB 6G4W Pfam PF08241 Pfam PF12589 OMIM 194050 OMIM 615733 DisGeNET 114049 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}.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}. P01100 EBI-852851,EBI-1044726 Q6ZWV7 EBI-2554199,EBI-1044726 P06748 EBI-78579,EBI-1044726 Q9UI30 EBI-1044726,EBI-373326 Q9C0C9 EBI-1044726,EBI-2339946 Q8IUE6 EBI-1044726,EBI-1642157 Q13618 EBI-456129,EBI-1044726 P00973 EBI-3932815,EBI-1044726 Q16512 EBI-602382,EBI-1044726 P55072 EBI-1044726,EBI-355164 Q5NHY6 EBI-1044726,EBI-2796153 Q9Y478 EBI-1044726,EBI-719769 GO:0005730 GO:0005654 GO:0048471 GO:0008168 GO:0046982 GO:0003723 GO:0016435 GO:0006325 GO:2000234 GO:0070476 GO:0031167 MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVGLDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAVLQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF 281 O45717 Protein nud-2 nud 6239 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:20005871}. Note=Recruited to the nuclear envelope by unc-83. {ECO:0000269|PubMed:20005871}. UNIPROT O45717 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}. Q23064-3 EBI-326083,EBI-2902257 O01738 EBI-326083,EBI-2416420 Q20398 EBI-326083,EBI-322716 Q94420 EBI-320790,EBI-326083 O44139 EBI-2414979,EBI-326083 O76447 EBI-314341,EBI-326083 GO:0005623 GO:0005813 GO:0005871 GO:0000776 GO:0005635 GO:0045202 GO:0008017 GO:0016477 GO:0051642 GO:0007059 GO:0051303 GO:0000132 GO:0007020 GO:0007100 GO:0007097 GO:2000574 GO:0051932 GO:0048489 GO:0047496 MDLSEDQIRGLPHHELLGHFLQMREEFNEFQTSSAEIEKMMDSELDDLKTQLKKAETRVQQMTTEQIRNKDRQDDSRVQFAQVEEQLRRENSHLHEQCESQRERIRKLEQRNDVLETSERNKEYLASDLGSKLDHAIEKIAMLESELYERQVAAEEMHRLREEQLRTTERPRLIVEPLRNDPEILPDEPSPGPSKEEFKMSSEDVFMEDVQHHEDVRMEETIAKIDEVRIDDNKNIQEKSQRVSTGTGAGACINRIVKDLMTKVERLDSILSTIRVSNNSSNNNSSHLTTTRA 293 O46382 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 ARFGEF1 9913 Yes SL-0198 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}. UNIPROT O46382 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. GO:0005829 GO:0000139 GO:0016363 GO:0005730 GO:0048471 GO:0030532 GO:0005802 GO:0005086 GO:0034237 GO:0010256 GO:0007030 GO:0030837 GO:0034260 GO:0090284 GO:0090303 GO:0015031 GO:0032012 GO:2000114 MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHIPQEHEGDLDPQTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGENHDCEEKPQDIVQSIVEEMVNIVVGDTGERTTINVSADGNNGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFGTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQETSEMKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFTKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPAKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGAKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGYTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPISGETAPPTPSPVSENQLDTISQKSVDIHDSIQPRSADNRQQAPLASVSTVNEEISKIKPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSRKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRASAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ 1849 O54923 Exocyst complex component 6 Exoc6 10116 Yes SL-0198 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}. UNIPROT O54923 Pfam PF04091 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}. GO:0000145 GO:0090543 GO:0030426 GO:0016020 GO:0048471 GO:0030218 GO:0006887 GO:0006893 GO:0015031 GO:0006904 MAESGEALGTVPEHERILQEIESTDTACVGPTLRSVYDGQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRADAEKLKVQVTDTNRRFQDAGKEVIEQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMQRYYSALKTMEQLENVYFPRVSQYRFCQLMMDTLPKLREDIKDISMSDLKDFLESIRKHSDKIGETAMKQAQQQKSFSIAVQKQTNMRFGKNMHVNNDRTLEEKSDIILKHTLEEEAENDEEVLTVQDLVDFSPVYRCSHIYSALGDEETFENYYRKQRKKQARLVLQPQSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFSVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKMVISKFPFQDPDLEKQSFPKKFPMSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVKQLRGLVTGMSQHM 804 O54940 BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 Bnip2 10090 Yes SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}. UNIPROT O54940 UNIPROT Q8K4H0 Pfam PF12496 Pfam PF13716 PROSITE PS50191 Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}. GO:0005814 GO:0005737 GO:0005829 GO:0043231 GO:0005635 GO:0048471 GO:0031616 GO:0004309 GO:0006915 GO:0001824 GO:0007098 GO:0006798 GO:0043410 GO:0045666 GO:0051057 GO:0090649 GO:0051146 MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ 326 O54943 Period circadian protein homolog 2 Per2 10090 Yes SL-0198 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. UNIPROT O54943 UNIPROT O54954 PDB 3GDI PDB 4CT0 PDB 4U8H Pfam PF08447 Pfam PF12114 PROSITE PS50112 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}. Q923E4 EBI-1802585,EBI-1266779 O08785 EBI-79859,EBI-1266779 Q96EB6 EBI-1802965,EBI-1266779 Q9WTL8-2 EBI-644559,EBI-1266779 Q9WTL8 EBI-1266779,EBI-644534 Q3ULA2 EBI-896325,EBI-1266779 P97784 EBI-1266779,EBI-1266607 Q9JMK2 EBI-771709,EBI-1266779 Q9R194 EBI-1266619,EBI-1266779 P67870 EBI-1266779,EBI-348169 O14503 EBI-1266779,EBI-711810 Q06486 EBI-2910316,EBI-1266779 P51449 EBI-1266779,EBI-3908771 Q99PV5 EBI-6143801,EBI-1266779 Q16526 EBI-741297,EBI-1266779 Q60953 EBI-1266779,EBI-3895605 P29590 EBI-295890,EBI-1266779 Q8C4V4 EBI-1266779,EBI-1266589 Q8BFZ4 EBI-6898235,EBI-1266779 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0042826 GO:1990226 GO:0042802 GO:0019900 GO:0035257 GO:0036002 GO:0070063 GO:0000978 GO:0003713 GO:0001222 GO:0008134 GO:0000976 GO:0032922 GO:0097167 GO:0007623 GO:0043153 GO:0006631 GO:0006094 GO:0005978 GO:0070932 GO:0019249 GO:0042754 GO:0060567 GO:0070345 GO:0031397 GO:0000122 GO:2000678 GO:0045892 GO:0120162 GO:0051726 GO:0042752 GO:0051946 GO:0050796 GO:0050767 GO:0019229 GO:0002931 GO:0009416 GO:0050872 MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFRLMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSESQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSYTTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRTRNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGYGSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVAEMQSSPPAQVKAVTTIERDSSGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESCSEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTSHTEVSAHLSSLTLPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKEVLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKTGKNRKLKSKRVKTRDSSESTGSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVPAYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQPEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTPPAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGTSRDRQPKAPPTCNEPSDTQNSDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMIPDTEESEQFIKYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGGLPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT 1257 O54946 DnaJ homolog subfamily B member 6 Dnajb6 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT O54946 UNIPROT Q3TE94 UNIPROT Q3U6L0 UNIPROT Q3UNJ5 UNIPROT Q3UYT7 UNIPROT Q99LA5 UNIPROT Q9QYI9 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. Q8CG73 EBI-4281130,EBI-642500 Q9CQV8 EBI-771608,EBI-642500 Q8BWG8 EBI-642500,EBI-641778 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0030018 GO:0001671 GO:0051087 GO:0003677 GO:0031072 GO:0042802 GO:0044183 GO:0051082 GO:0030036 GO:0061077 GO:0060710 GO:0060717 GO:0030198 GO:0045109 GO:0043154 GO:0090084 GO:0045892 GO:0006457 GO:0034504 GO:0032880 GO:0060715 MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH 365 O55034 Sperm-associated antigen 4 protein Spag4 10116 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O55034 Pfam PF07738 PROSITE PS51469 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}. GO:0005623 GO:0005737 GO:0016021 GO:0034993 GO:0005874 GO:0031514 GO:0005635 GO:0005637 GO:0042802 GO:0043495 GO:0030154 GO:0090286 GO:0006998 GO:0007283 MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRPKLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVYREICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQGQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFPKVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH 444 O55227 Protein unc-50 homolog Unc50 10116 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O55227 Pfam PF05216 May be involved in cell surface expression of neuronal nicotinic receptors. Binds RNA. {ECO:0000269|PubMed:10980252}. GO:0005794 GO:0000139 GO:0030173 GO:0005637 GO:0003723 GO:0007166 GO:0015031 MLPSTSLNSSMYGNGALNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARDDPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFISNKYLVKRQSRDYDVEWGYAFDVHLNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVVLLYPFAPLIVLYGLSLALGWNFTHTLCSFYKYRVK 259 O55242 Sigma non-opioid intracellular receptor 1 Sigmar1 10090 Yes SL-0178 SL-0179 SL-0182 SL-0183 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}. UNIPROT O55242 UNIPROT Q9JKU9 Pfam PF04622 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}. G3I8R9 EBI-988311,EBI-1557700 P61168 EBI-8019871,EBI-1557700 P63141 EBI-644033,EBI-1557700 GO:0030054 GO:0031410 GO:0005783 GO:0005789 GO:0030426 GO:0016021 GO:0005811 GO:0005635 GO:0005637 GO:0005640 GO:0014069 GO:0098839 GO:0042802 GO:0004985 GO:0038023 GO:0036474 GO:0006869 GO:0007399 GO:0070207 GO:0043523 MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS 223 O55653 Early E3A 11.6 kDa glycoprotein E311 10534 No SL-0415 SL-0418 Host nucleus membrane; Single-pass membrane protein. UNIPROT O55653 Pfam PF05393 DE Reference Proteome: No; GO:0044200 GO:0016021 MTGSTIAPTTDYRNTTATGLKSALNLPQVHAFVNDWASLGMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNPHNEKIHRLDGLKPCSLLLQYD 101 O56860 p3 gag 53182 Yes SL-0382 [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}. UNIPROT O56860 Pfam PF03276 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}. GO:0042025 GO:0044220 GO:0044163 GO:0019013 GO:0003677 GO:0003723 GO:0075521 GO:0046718 GO:0019076 MARELNPLQLQQLYINNGLQPNPGHGDIIAVRFTGGPWGPGDRWARVTIRLQDNTGQPLQVPGYDLEPGIINLREDILIAGPYNLIRTAFLDLEPARGPERHGPFGDGRLQPGDGLSEGFQPITDEEIQAEVGTIGAARNEIRLLREALQRLQAGGVGRPIPGAVLQPQPVIGPVIPINHLRSVIGNTPPNPRDVALWLGRSTAAIEGVFPIVDQVTRMRVVNALVASHPGLTLTENEAGSWNAAISALWRKAHGAAAQHELAGVLSDINKKEGIQTAFNLGMQFTDGNWSLVWGIIRTLLPGQALVTNAQSQFDLMGDDIQRAENFPRVINNLYTMLGLNIHGQSIRPRVQTQPLQTRPRNPGRSQQGQLNQPRPQNRANQSYRPPRQQQQHSDVPEQRDQRGPSQPPRGSGGGYNFRRNPQQPQRYGQGPPGPNPYRRFGDGGNPQQQGPPPNRGPDQGPRPGGNPRGGGRGQGPRNGGGSAAAVHTVKASENETKNGSAEAVDGGKKGGKD 514 O59718 Nuclear envelope morphology protein 1 nem1 284812 Yes SL-0178 SL-0182 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}. UNIPROT O59718 Pfam PF03031 PROSITE PS50969 Catalytic component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology. {ECO:0000250}. GO:0005783 GO:0005789 GO:0016021 GO:0071595 GO:0031965 GO:0005634 GO:0004721 GO:0030437 GO:0071072 GO:0071763 GO:0023052 MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHANIMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSYSYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSGHSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSRGSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALVDSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK 476 O59744 Uncharacterized transcriptional regulatory protein C530.08 SPBC530 284812 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O59744 Pfam PF04082 Pfam PF00172 PROSITE PS00463 PROSITE PS50048 DE Reference Proteome: Yes; GO:0005829 GO:0016021 GO:0031965 GO:0005634 GO:0000981 GO:0000978 GO:0008270 GO:0006357 GO:0006351 MDNESHSQETESKILEGAKVATRRRRVTRACDMCRRKKIKCDGLRPCKNCKAGKLECTYHMPSSRKSSFSPEYVENLESRVRYLETLLKKNTNFDLSSNSPSFLFFLREQKFQATNELENMSPERKVIFTSMINYGNLFVDAKHGTRYFRGGSSIHVLIQHLIRRLPGDFEICEPYSAYPLGNKNIQFDDNDPEYQFFTPTPRFSIDFMVSSVDPREIQLPGIEEALCITKAAVSYVSGIVFYTTYADFPKKIRLLYSGNYQGNFFPLFLSILCVGYYHHLLNNPSNTELQSLIKKYSFYSERLVKSADNFTIESIQCLLILSIYRYCRTEISAAWYYMKLGLNCCLRLGLHRNITEGFTEEQIDSRRRIFWAIYCYDRQLCTLFGFPLGVRDEDIDQCLPVTPKFPSVTEIEANARLFFFHGVKLYKISSRILTKLYSPNSRNVTKKHISYAVIQDLEQLLDGFYNSLPRVFRAEQPGEFQANHFFYNLQLVYYSFRMLIYRPLLHYLEADSPAMQALKVPDRQTAFTLACKCVDSAIVCVQNLSHLSKGLKRTLDRYYWTTVYCGFSTIVTLIFAALLTKNTNLLIHISVARESIEALAHECVTRRLLPLIDKMRESLMKILESNADGYKQMSPTKAPQVFESESNVPINNGPQQSIDKESNSNTQLPQVETEGQQQSVFDGNIGTIPYQAYNMNEDSFIDINTLSSMLNYHTQAVSIHHPSFYISRSDVPLEEEFQIPNELLAVDPVAESMQENSDIINEAFGLVDPDVSDGKSRESSSLNNSTPFNPTVNIDPASILEHFSQNVMKDSQNS 815 O59809 Probable importin c550.11 SPCC550 284812 Yes SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O59809 Pfam PF08506 Pfam PF03810 PROSITE PS50166 Active in protein import into the nucleus. {ECO:0000250}. GO:0005829 GO:0005635 GO:0005643 GO:0005634 GO:0005525 GO:0005049 GO:0061608 GO:0008536 GO:0006406 GO:0006606 MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIPEEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLDDRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESLMSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSPRVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVKLASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGYLRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEVDIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENTVDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITYGGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVFLLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMITLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNYLLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT 1029 O60100 Probable importin subunit beta-4 kap123 284812 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus. Nucleus envelope. UNIPROT O60100 UNIPROT Q9US72 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. GO:0005737 GO:0005829 GO:0005635 GO:0034399 GO:0005634 GO:0061608 GO:0008139 GO:0008536 GO:0006606 MDAQFTLELTQLLFQSIAPDTTQITEATRALETKYLKEPGSLLSLFHIMGTCENPQVRQLAAIEARKLCHKYWSSVDADVQNQIRSNLLDITLKEPESIVRHAFGRVIAALAKLDLPEGKWNELSAFLVQATMDQNDSIREMAVYVLYSIAETVDLDNKLLLDFVNLFSQTITDSSRTVRVTSVQGLGAIAEVLESDDKKLLHAYRATLPGMLLVLQDVVQVGDVDASKQVFDVFNTFLIASGAIISKALGNIIEIITGIANSKQVDDEIRCMALSFIISCIRFKSRKLQALKLGKPLVLTLMEVATEETTDDIDEDCPARLALRSIDLLSTHLSPSQVFYPMFEAACAFSQSPQASYRKAALLSIGVAVEGSSESVAGNLPNIFPIIINGLCDNDMDVRQAALLALSQIAVEIPTEVSKHHAQLLPLVFELMSTQGVKVGKSACNCIDALLEGLDKSEISGYLPMLMERLVGLLEFSDTPDIKSCVAAAIGSAAFAAQDDFIPYFERTMASLSQCLHTTDDDEGYELRGTVMDTLGAIANAVGKQAFLPYTEQLIQLAYEGIQIDHSRLRECSFCFYAVLARVYKEEFAPFLEHIVPALFKSIDQDESDILSERIGAPTAEEISQLLDSVETNEEENDEELEKAMGVNSAIAMEKEIAADALGEICMYVGAPFTPYLEPTVEKLVACTTHFYEGVRKSALSSLWRCATTYYKVCNVPQWQPGLPLKVPVPDTVKNIFEAVRKCTFDTLEEEYEKTVATDILRNFAESIKTCGPVVLGDDYEKLCEVVMEVLQKQHIVQAGDVFDDDFEEEDIVSNEEVDDTEQDALLIDSACDVVIALAVALGGSFADSFKVFYPQIVKYYMSKNGNERAMAVACVGEVAGGIESAITPFTRDVFSLFMAALEDSEGEVRSNAAYSMGLLCQFSTEDLSSEYLNILQKLQPFFTQEVFRTALDNAIGCISRLILHNQNAIPVDQVLPIVFSKLPLKEDYLENAPLYHMILALYRQQNPCLVQHLGELIPVFASVLTGSPEQLNDELRSELLSMVKEIAPQYESVVSNYPQLVALLQ 1067 O60131 Uncharacterized transcriptional regulatory protein C16G5.17 SPBC16G5 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O60131 Pfam PF00172 PROSITE PS00463 PROSITE PS50048 DE Reference Proteome: Yes; GO:0016021 GO:0031965 GO:0005634 GO:0000981 GO:0000978 GO:0008270 GO:0006357 MVGKSKNRAHKNIRARSCLRCRRRKVKCDRQYPCSRCKESEESCTYGVNEQAVQLLEEPLSRPITRETDSSAHQETRTRLEENNLPKTQKFGFVDWKTILKSSAEFQGIVQRDPESRLREALETDPKLKKRLECILETIPPWDVCESLLKVYANTFNVTNYILDFEQADKLLSDLKNSNHVFATSIILIVTAIAVALSLESFPSNIERYFSAVNHSAIELSDALNSKIDDFLNEEVIFRLWRNIDRIRLHAIRAQLCMRNQFRSMNTDLCYAIHYACFVNPIFQNTDTEYEANMEVWLSICEIDALECVLRSCQPWVQHDIYGKLLSQRKMGSDVISYEFHSLLGQLLTCGLEIYKAIHTSTVNEFVNSIQFYESQLSLVLMEIESKFSNIDGSDIHFRYLFLKTVFWTVRKNLYQGFITVSRTLVPNYPDIVQKLGQTSIQLSRLISNSMDCFEKYGWLKAMLILVTHTFLIIHVCSERGYDVPKDFWNVTASVQATLEEKKYPGIVWERIHYVLNIYTTINSVEPELSEDHGDLDDQNLFQVFTDIFDFNFNFPLPNL 560 O60158 Bouquet formation protein 4 bqt4 284812 Yes SL-0178 SL-0179 SL-0182 Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane protein {ECO:0000305}. UNIPROT O60158 UNIPROT Q9USF5 PDB 5YBX PDB 5YC2 PDB 5YCA PDB 6A6W PROSITE PS51299 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}. GO:0005623 GO:0005737 GO:0005639 GO:1990862 GO:0005634 GO:0003677 GO:0051301 GO:0070197 GO:0044820 MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF 432 O60175 Protein OPI10 homolog SPBC21H7 284812 Yes SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O60175 Pfam PF05603 DE Reference Proteome: Yes; GO:0005829 GO:0005635 GO:0005634 GO:0061608 GO:0006606 MFGAICAGRLVQTNLQQVADNQFVFQLDSAESLNHIVVFLLPNSPFPVGMGAKVYFQWPGKPFQFLGYLTNEKPSAIFRLKNTIQTLSENENCVGITAMLGISVEPLTNFTETPAVSTSASNVIAKPLPPVTSVAQKILTNLYNFLASFATSQLPPNSIGLGDLRPNDTFIPLRVFQDWHAKFLNKLSNNPNFLDSEDQI 200 O60238 BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like BNIP3L 9606 Yes SL-0178 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. UNIPROT O60238 UNIPROT B0AZS9 UNIPROT Q5JW63 UNIPROT Q8NF87 Pfam PF06553 OMIM 605368 DisGeNET 665 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}. A0PK00 EBI-849893,EBI-10171534 Self EBI-849893,EBI-849893 Q12983 EBI-749464,EBI-849893 Q5T700 EBI-10173166,EBI-849893 Q969F0 EBI-849893,EBI-743099 Q9BXN2 EBI-3939278,EBI-849893 Q9NRQ5 EBI-8640191,EBI-849893 P17152 EBI-723946,EBI-849893 Q7CIP6 EBI-849893,EBI-2852197 A0A384LD58 EBI-2856011,EBI-849893 P51452 EBI-849893,EBI-1049755 Q16610 EBI-947964,EBI-849893 O14936 EBI-849893,EBI-1215506 Q8IU85 EBI-849893,EBI-3911453 Q8NI37 EBI-9089276,EBI-849893 Q13021 EBI-750078,EBI-849893 Q9NQ11 EBI-849893,EBI-6308763 Q81X61 EBI-2817767,EBI-849893 Q81TT4 EBI-849893,EBI-2810319 A0A384L1C8 EBI-2846642,EBI-849893 Q01844 EBI-739737,EBI-849893 Q6NUQ1 EBI-849893,EBI-726876 Q9H2S6-2 EBI-849893,EBI-12003398 P60520 EBI-849893,EBI-720116 Q9H0R8 EBI-849893,EBI-746969 O43169 EBI-849893,EBI-1058710 Q9NRS4 EBI-849893,EBI-10313040 Q9BXN2-6 EBI-11989440,EBI-849893 P38182 EBI-849893,EBI-2684 Q15848 EBI-849893,EBI-10827839 Q9Y4P8 EBI-719396,EBI-849893 Q92934 EBI-849893,EBI-700771 P10415 EBI-77694,EBI-849893 P03247 EBI-849856,EBI-849893 Q9P104 EBI-739600,EBI-849893 GO:0005829 GO:0005783 GO:0016021 GO:0031224 GO:0005741 GO:0005739 GO:0005635 GO:0016607 GO:0042802 GO:0005521 GO:0042803 GO:0071456 GO:0051607 GO:0097345 GO:0035694 GO:0043066 GO:0060548 GO:0010917 GO:0043065 GO:0016239 GO:0042981 GO:1903146 GO:0043067 GO:1903214 GO:0016032 MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY 219 O60271 C-Jun-amino-terminal kinase-interacting protein 4 SPAG9 9606 Yes SL-0198 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}. UNIPROT O60271 UNIPROT A6H8U5 UNIPROT A8MSX0 UNIPROT B4DHH2 UNIPROT O60905 UNIPROT Q3KQU8 UNIPROT Q3MKM7 UNIPROT Q86WC7 UNIPROT Q86WC8 UNIPROT Q8IZX7 UNIPROT Q96II0 UNIPROT Q9H811 PDB 2W83 Pfam PF16471 Pfam PF09744 PROSITE PS51776 PROSITE PS51777 OMIM 605430 DisGeNET 9043 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}. P53350 EBI-476768,EBI-1023301 Q07832 EBI-2552999,EBI-1023301 P23771 EBI-6664760,EBI-1023301 A3KN83 EBI-2855422,EBI-1023301 Q9UQ88 EBI-1023301,EBI-373024 Q9UKN8 EBI-1023301,EBI-1237240 Q9UBC2 EBI-1023301,EBI-2556746 Q8WUA4 EBI-1023301,EBI-1237062 P11274 EBI-1023301,EBI-712838 Q00613 EBI-719620,EBI-1023301 Q06945 EBI-6672525,EBI-1023301 Q12955 EBI-2691178,EBI-1023301 Q14566 EBI-374900,EBI-1023301 Q14C86 EBI-1049788,EBI-1023301 Q14683 EBI-80690,EBI-1023301 P30291 EBI-914695,EBI-1023301 P33991 EBI-374938,EBI-1023301 P33993 EBI-355924,EBI-1023301 P49736 EBI-374819,EBI-1023301 Q8ZED8 EBI-2840186,EBI-1023301 Q14240 EBI-73473,EBI-1023301 P61026 EBI-1023301,EBI-726075 P61006 EBI-1023301,EBI-722293 Q96BY7 EBI-2963262,EBI-1023301 Q9NY27 EBI-1048740,EBI-1023301 Q9P260 EBI-2831057,EBI-1023301 Q6IN85 EBI-1055598,EBI-1023301 Q9UQE7 EBI-80718,EBI-1023301 Q9Y4E8 EBI-1043104,EBI-1023301 Q9Y6Y0 EBI-715774,EBI-1023301 P19838 EBI-1023301,EBI-300010 GO:0001669 GO:0034451 GO:0005737 GO:0005829 GO:0070062 GO:0005765 GO:0048471 GO:0042802 GO:0008432 GO:0019894 GO:0005078 GO:0030159 GO:0007257 GO:0032418 GO:0030335 GO:0051149 GO:0045666 GO:0042147 GO:0051146 GO:0016192 MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLGMGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVTNGQGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLDTEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGNILDSFTVCNSHVLCIASVPGARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLGGITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSEVDENVPTAEEATEATEGNAGSAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDKVTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEPGSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGNE 1321 O60318 Germinal-center associated nuclear protein MCM3AP 9606 Yes SL-0178 SL-0185 [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}. UNIPROT O60318 UNIPROT C9JL56 UNIPROT Q2M3C1 UNIPROT Q6PJP6 UNIPROT Q9BSY5 UNIPROT Q9UMT4 PDB 4DHX Pfam PF16766 Pfam PF16769 Pfam PF16768 Pfam PF03399 PROSITE PS50250 OMIM 603294 OMIM 618124 DisGeNET 8888 [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}.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. Q9NRI5 EBI-308480,EBI-529989 P25054 EBI-308480,EBI-727707 P60953 EBI-81752,EBI-308480 P63000 EBI-308480,EBI-413628 Q5NGE6 EBI-2796264,EBI-308480 P30304 EBI-747671,EBI-308480 P62487 EBI-308480,EBI-347928 Q8BUH2 EBI-10962405,EBI-308480 Q9BVG8 EBI-2125614,EBI-308480 Q9NSK0 EBI-949319,EBI-308480 P13533 EBI-1048066,EBI-308480 Q9CYN2 EBI-9986662,EBI-308480 Q9R1K9 EBI-2553037,EBI-308480 P54132 EBI-621372,EBI-308480 Q09472 EBI-447295,EBI-308480 Q7CIS2 EBI-308480,EBI-2864684 A0A0H2W148 EBI-2847163,EBI-308480 Q81KK8 EBI-2822258,EBI-308480 Q81YE8 EBI-2811064,EBI-308480 Q5NIJ3 EBI-308480,EBI-2798422 A0A384KUI4 EBI-2846272,EBI-308480 Q9NPA8 EBI-308480,EBI-719226 Q9P0N5 EBI-308480,EBI-721260 Q9UKK9 EBI-308480,EBI-721623 Q14194 EBI-473101,EBI-308480 Q15149 EBI-308480,EBI-297903 Q6P5F9 EBI-2550236,EBI-308480 C5E524 EBI-12561527,EBI-308480 Q194T2 EBI-11515076,EBI-308480 Q9H0B3-2 EBI-21526503,EBI-308480 Q12798 EBI-2512818,EBI-308480 Q9BTL4 EBI-2806011,EBI-308480 Q9NYQ7 EBI-308480,EBI-308417 O94985 EBI-308480,EBI-522075 GO:0005694 GO:0005737 GO:0005829 GO:0031965 GO:0044615 GO:0005654 GO:0005634 GO:0070390 GO:0003682 GO:0010484 GO:0004402 GO:0042393 GO:0003676 GO:0006406 GO:0034728 GO:0016973 GO:0016446 MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSSVGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGAESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKSIFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDHPPDKRPVRLNRPRGGTLFGRTIQDVFKSNKEVGRLGNKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETESREKKEDSLRGTPARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKKLAVVHFFDHASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTEDAPFQHSPLGKAAGRTGASSLLNKSSPVKKPSLLKAHQFEGDSFDSASEGSEGLGPCVLSLSTLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDMCPEKERYMRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQKEGSLRDWYDFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQGYNVLLSLNKGDILREVQQFHPAVRNSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKDALRALNFAYTVSTQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSVFITRKLTVSVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPVSTQRPGSDTVGGGRGEECGVEPDAPLSSLPQSLPAPAPSPVPLPPVLALTPSVAPSLFQLSVQPEPPPPEPVPMYSDEDLAQVVDELIQEALQRDCEEVGSAGAAYAAAALGVSNAAMEDLLTAATTGILRHIAAEEVSKERERREQERQRAEEERLKQERELVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETDQRVRVARCCEDVCAHLVDLFLVEEIFQTAKETLQELQCFCKYLQRWREAVTARKKLRRQMRAFPAAPCCVDVSDRLRALAPSAECPIAEENLARGLLDLGHAGRLGISCTRLRRLRNKTAHQMKVQHFYQQLLSDVAWASLDLPSLVAEHLPGRQEHVFWKLVLVLPDVEEQSPESCGRILANWLKVKFMGDEGSVDDTSSDAGGIQTLSLFNSLSSKGDQMISVNVCIKVAHGALSDGAIDAVETQKDLLGASGLMLLLPPKMKSEDMAEEDVYWLSALLQLKQLLQAKPFQPALPLVVLVPSPGGDAVEKEVEDGLMLQDLVSAKLISDYTVTEIPDTINDLQGSTKVLQAVQWLVSHCPHSLDLCCQTLIQYVEDGIGHEFSGRFFHDRRERRLGGLASQEPGAIIELFNSVLQFLASVVSSEQLCDLSWPVTEFAEAGGSRLLPHLHWNAPEHLAWLKQAVLGFQLPQMDLPPLGAPWLPVCSMVVQYASQIPSSRQTQPVLQSQVENLLHRTYCRWKSKSPSPVHGAGPSVMEIPWDDLIALCINHKLRDWTPPRLPVTSEALSEDGQICVYFFKNDLKKYDVPLSWEQARLQTQKELQLREGRLAIKPFHPSANNFPIPLLHMHRNWKRSTECAQEGRIPSTEDLMRGASAEELLAQCLSSSLLLEKEENKRFEDQLQQWLSEDSGAFTDLTSLPLYLPQTLVSLSHTIEPVMKTSVTTSPQSDMMREQLQLSEATGTCLGERLKHLERLIRSSREEEVASELHLSALLDMVDI 1980 O60356 Nuclear protein 1 NUPR1 9606 Yes SL-0198 Nucleus {ECO:0000269|PubMed:10092851, ECO:0000269|PubMed:16300740}. Cytoplasm {ECO:0000269|PubMed:16300740}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16300740}. UNIPROT O60356 UNIPROT B2R5C4 UNIPROT O60357 UNIPROT Q6FGG3 Pfam PF10195 OMIM 614812 DisGeNET 26471 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}. P00352 EBI-752170,EBI-3908808 Q15761 EBI-3918088,EBI-3908808 Q01105 EBI-3908808,EBI-1053182 Q02383 EBI-3908808,EBI-2609565 P04279 EBI-3908808,EBI-953955 Q9H221 EBI-3908808,EBI-3908684 GO:0005737 GO:0005654 GO:0005634 GO:0048471 GO:0032993 GO:0010698 GO:0003682 GO:0003677 GO:0003713 GO:0002526 GO:0042771 GO:0008584 GO:0043066 GO:1902902 GO:0010507 GO:0010667 GO:0045786 GO:0008285 GO:0043433 GO:1904036 GO:0050680 GO:0048147 GO:0045820 GO:0062099 GO:1904691 GO:0045787 GO:2001244 GO:0150078 GO:0043525 GO:1903862 GO:1901800 GO:0031401 GO:0006473 GO:0065003 GO:0010506 GO:2000194 GO:1905897 GO:0009636 GO:0035914 MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR 82 O60583 Cyclin-T2 CCNT2 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}. Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}. UNIPROT O60583 UNIPROT A8KA48 UNIPROT D3DP73 UNIPROT D3DP74 UNIPROT O60582 UNIPROT Q29R66 UNIPROT Q53SR4 UNIPROT Q5I1Y0 PDB 2IVX Pfam PF00134 OMIM 603862 DisGeNET 905 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}. Q16659 EBI-1384105,EBI-2836757 A3KMF4 EBI-11085928,EBI-2836757 Q9ERL0 EBI-11086057,EBI-2836757 O95402 EBI-394392,EBI-2836757 Q9UHB7 EBI-395282,EBI-2836757 O00472 EBI-395274,EBI-2836757 P42568 EBI-716132,EBI-2836757 P50750 EBI-1383449,EBI-2836757 A0A3Q0PRD7 EBI-2810412,EBI-2836757 Q12802-1 EBI-25409719,EBI-2836757 Q07139-1 EBI-25410958,EBI-2836757 GO:0008024 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0097322 GO:0003682 GO:0061575 GO:0016538 GO:0019901 GO:0070063 GO:0001223 GO:0007049 GO:0051301 GO:0019085 GO:0019086 GO:0032786 GO:0045944 GO:0000079 GO:0051147 GO:0006357 GO:0007519 GO:0042795 GO:0006366 GO:0006368 MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM 730 O60711 Leupaxin LPXN 9606 Yes SL-0198 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. UNIPROT O60711 UNIPROT B2R8B4 UNIPROT B4DV71 UNIPROT Q53FW6 UNIPROT Q6FI07 PDB 1X3H PDB 4XEF PDB 4XEK PDB 4XEV Pfam PF00412 PROSITE PS00478 PROSITE PS50023 OMIM 605390 DisGeNET 9404 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}. Q14289 EBI-744222,EBI-298640 Q8IVE3 EBI-744222,EBI-2815745 P25800 EBI-8639312,EBI-744222 P31274 EBI-1779423,EBI-744222 Q494U1 EBI-10241513,EBI-744222 Q8N3L3 EBI-744222,EBI-6116822 Q06455-4 EBI-10224192,EBI-744222 O14733 EBI-744222,EBI-492605 Q9Y473 EBI-3438881,EBI-744222 Q99608 EBI-744222,EBI-718177 Q7Z3B4-2 EBI-21504088,EBI-744222 Q9Y6K9 EBI-744222,EBI-81279 P09022 EBI-3957603,EBI-744222 Q8D0I3 EBI-744222,EBI-2860455 Q8ZBT8 EBI-744222,EBI-2865235 Q8CLR7 EBI-744222,EBI-2844920 Q8CZX0 EBI-2843256,EBI-744222 A0A384LCM3 EBI-744222,EBI-2860622 A0A0J1I0J1 EBI-744222,EBI-2820004 Q5NGW8 EBI-744222,EBI-2803320 Q9BUY5 EBI-743265,EBI-744222 Q96BD5 EBI-745085,EBI-744222 P49639 EBI-744222,EBI-740785 Q96HA1 EBI-739990,EBI-744222 Q9NV31 EBI-747481,EBI-744222 P48059 EBI-744222,EBI-306928 Q63HR2 EBI-744222,EBI-949753 Q8TAP4-4 EBI-744222,EBI-11742507 P18206-2 EBI-744222,EBI-11027067 P01137 EBI-744222,EBI-779636 P21549 EBI-744222,EBI-727098 Q96HA1-2 EBI-744222,EBI-11956563 Q06455-2 EBI-744222,EBI-11984663 Q494U1-3 EBI-744222,EBI-12014286 P29972 EBI-744222,EBI-745213 Q9Y2X9 EBI-744222,EBI-396200 Q9Y2X7-3 EBI-744222,EBI-11070376 Q9ULM0 EBI-744222,EBI-2803624 Q9UGP4 EBI-744222,EBI-2652871 Q9NXC5 EBI-744222,EBI-2515122 Q9NVD7 EBI-744222,EBI-747655 Q9NR12 EBI-744222,EBI-350517 Q9H939 EBI-744222,EBI-2609610 Q99700-2 EBI-744222,EBI-16813710 Q96SN8-2 EBI-744222,EBI-21545131 Q96F86 EBI-744222,EBI-997311 Q93052 EBI-744222,EBI-718388 Q8IZD4 EBI-744222,EBI-521595 Q86YT6 EBI-744222,EBI-2129148 Q76N32 EBI-744222,EBI-9051024 Q69YQ0 EBI-744222,EBI-351113 Q2TAL8 EBI-744222,EBI-2798044 Q16204 EBI-744222,EBI-1045350 Q15654 EBI-744222,EBI-742327 Q15154-2 EBI-744222,EBI-16811645 Q15052-2 EBI-744222,EBI-21521235 Q14161 EBI-744222,EBI-1046878 Q14155-1 EBI-744222,EBI-717540 Q13177 EBI-744222,EBI-1045887 Q13153-2 EBI-744222,EBI-1019502 Q05397 EBI-744222,EBI-702142 Q05209 EBI-744222,EBI-2266035 P29558-2 EBI-744222,EBI-21554551 O95613 EBI-744222,EBI-530012 GO:0042995 GO:0005737 GO:0005829 GO:0005925 GO:0016020 GO:0016607 GO:0005634 GO:0048471 GO:0005886 GO:0002102 GO:0046872 GO:0003712 GO:0007155 GO:0050859 GO:0007162 GO:0065003 GO:0033628 GO:0007165 MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL 386 O62275 Argonaute protein wago-4 wago 6239 Yes SL-0198 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}. UNIPROT O62275 Pfam PF02170 Pfam PF02171 PROSITE PS50821 PROSITE PS50822 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}. Q9XVJ3 EBI-2418617,EBI-326728 GO:0048471 GO:0003723 GO:0031048 GO:0060966 MPALPPVYTPSGAPSSVHAPPAVPPVPVPTQPLRSEYQTSNDACIKRLEELNIAPAAKLYPTPTEPGKCGVEAEIQTNVFGIEMHQDSLFYQYSVNITTELKNGKEVTFTKKGKDDFVVTERHDKCCAILFRALGDYEEFFKTSDSCLIYDGQSILFSNVDLFQGFREGAVKTKYMQLDGGEMDHKDLKSLPCIKLEVFPTKNPAVKFTREAVARRATDSNLDSVSLAYQQILELALTQPCLRNTARYVVFDHGKMFFIDPLGEGFEKCDVVDVGDGKQVVPGLKKTINFIEGPYGRGRSNPSVVIDGMKVAFHKNQPILDKLKEITTQPVEHGLKGLEKDRCAAVIKGLDCYSTYGGRERHHKIEGIHHEGARNARFELNDGGSCTVAQYFEDVYNITLRYPDTNLIVSKERGNINFYPMELLKISSHQRVQIPQLTSAQSQKTTKESAVLPDVRQRLILTGKNAAQISSDNEVLGKMGVSVCEDPLMVKGRSIPAVKLANAEIGANPINVKDNKWRANRFTRPATAPNVWAMYVVGTASTRITLDTLKKFADEFAAMCKSKGVNMPAPADISLIHMDAIESRLYDATKANCTFVFIITDDSITTLHQRYKMIEKDTKMIVQDMKLSKALSVINAGKRLTLENVINKTNVKLGGSNYVFVDAKKQLDSHLIIGVGISAPPAGTKYAMENKGVLNPNVIGYAYNAQHNQEFSGDFVLNSASQDTLAPIEDIVMHSLNEYQKFHDGGLPRRVIVYRTGTSEGNHGSIMAYEIPLARAAMRDFSPDIQLVYIVVSKDHSFRFFKPDLASLASRPQATSSTASRHSAMPAAPKAWDLNIAPGILVDSIVTNPACKQFFLNSHITLQGTAKTPLYTVLADDAKVSMTALEDITYKLCHLHQIVGLPTSLPTPLYVANEYAKRGRNLWNEAVALNNVPTVSGPEADRLKELTKSICYKASGDLTGRRVNA 965 O64629 Serine/threonine-protein kinase Aurora-3 AUR3 3702 Yes SL-0198 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}. UNIPROT O64629 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0032133 GO:0000775 GO:0000780 GO:0005634 GO:0048471 GO:0005819 GO:0005876 GO:0051233 GO:0005524 GO:0035175 GO:0044022 GO:0035174 GO:0007059 GO:0043987 GO:0043988 GO:0016572 GO:0007052 GO:0016310 GO:0032465 MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI 288 O64740 Protein transport protein SEC13 homolog B SEC13B 3702 Yes SL-0178 SL-0185 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}. UNIPROT O64740 UNIPROT Q8LAX1 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 Required for protein transport from the endoplasmic reticulum to the Golgi apparatus. {ECO:0000305|PubMed:24280388}. Q9C9L2 EBI-4426144,EBI-4454838 Q8LAZ7 EBI-4454838,EBI-531132 O48847 EBI-3387563,EBI-4454838 Q9LT89 EBI-4426178,EBI-4454838 GO:0030127 GO:0005829 GO:0005783 GO:0000139 GO:0005635 GO:0005643 GO:0031080 GO:0005730 GO:0005198 GO:0090114 GO:0051028 GO:0015031 MPGQKIETGHEDIVHDVQMDYYGKRIATASSDCTIKITGVSNNGGSQQLATLTGHRGPVWEVAWAHPKYGSILASCSYDGQVILWKEGNQNQWTQDHVFTDHKSSVNSIAWAPHDIGLSLACGSSDGNISVFTARADGGWDTSRIDQAHPVGVTSVSWAPATAPGALVSSGLLDPVYKLASGGCDNTVKVWKLANGSWKMDCFPALQKHTDWVRDVAWAPNLGLPKSTIASGSQDGKVIIWTVGKEGEQWEGKVLKDFMTPVWRVSWSLTGNLLAVSDGNNNVTVWKEAVDGEWEQVTAVEP 302 O70582 Arachidonate 12-lipoxygenase, 12R-type Alox12b 10090 Yes SL-0198 Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}. UNIPROT O70582 Pfam PF00305 Pfam PF01477 PROSITE PS00711 PROSITE PS00081 PROSITE PS51393 PROSITE PS50095 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}. GO:0048471 GO:0004052 GO:0047677 GO:0003824 GO:0005506 GO:1990136 GO:0016702 GO:0019369 GO:0046513 GO:0061436 GO:0051122 GO:0043651 GO:0019372 GO:0055114 GO:0010628 GO:0043410 GO:0070257 GO:0006497 GO:0006665 MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKDPWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIPSYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIKNIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRILDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLLESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLCIPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTIPELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPDDRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI 701 O74446 Sad1-interacting factor 2 sif2 284812 Yes SL-0178 SL-0182 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}. UNIPROT O74446 UNIPROT Q1MTQ4 Pfam PF02582 Required for sporulation where it is believed to have a role in meiotic nuclear division. {ECO:0000250}. GO:0016021 GO:0005759 GO:0031965 GO:0051321 GO:0140053 GO:0030435 MSNRIGPQRSTKTAAKLRLLPSTEEFDDFRRQDTGREVYSQIPQIEGSTAKRDAEHLGKRHREFLPRVTAYCTCDTFRVDLLFKFFQSRRSSHKTRPKQFDECIYSPYSYNNEETTDLLPDTLESSRGTLNRESSQESLQSIFEESGLDRNQPLFREVFCFTYGVVVLWGYTIDEEHRFLRELGRFEIEKLKIEDMEVEEFNYYITTLYQPRIFNDFIALRDASNYMIRLSISHAIAQSVKISLFEELVNETIDATKDTPQMIAETGRVNLKREEIMMAVGQLFILRININLQGSVLDSPELMWTEPQLEPIYTAARSYLEINQRVALLNQRVEVIGDLLSMLKEQITHTHDESLEWIVVILMGLLVLIALFSIVVDWKLFQ 382 O74476 Importin subunit beta-3 sal3 284812 Yes SL-0178 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}. UNIPROT O74476 UNIPROT Q9US74 Pfam PF18808 Pfam PF18816 Pfam PF18829 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}. GO:0005737 GO:0005829 GO:0005635 GO:0031965 GO:0034399 GO:0005643 GO:0005634 GO:0005525 GO:0061608 GO:0008139 GO:0006606 GO:0010389 MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDVAGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAEGAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVNFSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGKTMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKPDFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHDGVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVAAVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGNDTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLELPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTIITILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF 1095 O74500 Nucleoporin nup60 nup60 284812 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. UNIPROT O74500 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}. GO:0031965 GO:0005643 GO:0044615 GO:0017056 GO:0008298 GO:0031990 GO:0006607 GO:0016973 GO:0006611 GO:0034398 MSSGPIRTLHKGKAARNRTPYDRIAASKDGNHSNGPQTPSKSIFQRAKEWLTPSSWKKAISIFSSPVVNKHEDSFDSKTDEEYLQNVSTTTEDVSMLINTPVTEKYEQEHRDTSAQATPSIVEQSPNQMLANFFSKKGKTPLNEIEKEGIISILNKSASPSSSVISPAASLNRFQTPRAAAISKRESGVSSEPRARTSSLTPGNTPNSAKQWSAFRSTFSPLREQDQLSTISPNSLLPAQRLSYYGPTLSTPYNRRLRHKRHSTTPISLSNSIAPSLSFQPKKARYESANVSFNDTSFTNVPTSSPLHQSTTANHPEKTPSRAAASLLSILDSKEKNTPSITAKAGSPQSAPSKASYISPYARPGITTSRRRHDQIRPSSEKSEPEKKEPSAFETLEKSSNVQTYKPSLMPEFLEKASTHGSFAKQKEGEQTSLSEKTALSEPENKTPVFSFKAPSATTDKPSPPVSSIFSFNAPSAASTKPSPAVSSTFSFNAPTTTPSATSFSIINKEKPARSPNETIDVDLEEEGSGISAEVEVANEGEDLQKNATEVKASTSEKPVFRFEAVTDEKNSEVSSSNQASSSTMISQPNTGFSFGSFNKPAGQEEKPQQRSLFSASFTTQKPELPAAKIEPEVQMTNVAIDQRSFEQAEKSPISVSESTSLVEVEKPSAEGTNEHKQDATMTLEKTDKQGSLEEEPFPKFSFTVLPKENGENLSTMESTQELPKFSFSVLKEEKN 736 O74510 Bouquet formation protein 3 bqt3 284812 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O74510 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}. GO:0005623 GO:0005789 GO:0005635 GO:1990862 GO:0051301 GO:0044821 GO:0044820 MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL 255 O74525 Uncharacterized membrane protein C70.04c SPCC70 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. UNIPROT O74525 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0031965 MKQNNKKPLPSKTKEISLETDWIDVIETMRETNESPKSQNPSEEATTVNELSCEAKPKLLFTPTKSSLSIGNFPYKEFDPVLKFPGIHYTYSRERLWGTCVILSTLFWSYYVLSNSELLEFEASEYSLLFILIIALDALLTVSLFGLFHHLMFLTTNYSYTINSTLDISKGFFINVLSTMVQALVTVTIAFTKFVTIDFPIYVFSSLFLYHPLSRSRQLPTKMQLDGSGERKTDSSLVHQNPPN 244 O74889 SAC3 family protein 1 SPCC576 284812 Yes SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O74889 Pfam PF03399 PROSITE PS50250 DE Reference Proteome: Yes; GO:0005737 GO:0005829 GO:0005635 GO:0005643 GO:0005634 GO:0070390 GO:0006406 GO:0042274 MEKRNETGNNRLKRSNNRGKSKKDWKDASVETTPRETSVDEDNTSVFEDVEAQDSRQKRFSSTLEGNRFEELRSLREKEREVAIQNGLIDDPTKPRQLDEAVTFVGTCPDMCPEYEREQREYQNNLERWEINPETGRVDKNLAVKAFHRPAAGNEQALPSDVRPPPVLKKSLDYLVDKIVCGPDPLENTHFFVRDRTRSIRQDFTLQNCRDLDAVACHERIARYHILCIHQLCEKKQFSAQQEVEQLRKGILQSLCEFYDDLRKVKIRCPNEPEFRSYAIITHLRDPDVVRQSQILPIEIFDDQRVQLALRLSALAQKNNERVGHILPRNTEACPNLYTRFFKLVQSPAVTYLMACLLESHFMSIRKGALKAMRKAFMSAHANFPCGDLKRILHFDTVEQAASFSRYYGLEVSDDNGELSINLNKTAFFNDSKPDFRQLFSQTLVESKLQNRSFADIINGSRYNIDRVSPNTAFSTNIPLSLPFANKEPQPIAGFKKNTPETSVVSKNLSTFNGKFNVNAPVFTPRSFPTKPFSATDISSVQPTNLPNGSTNGTETFIPPVQNSITSNKEAVKPIKNKPKPISFESLSAVGNLIISDSLSRIVRQILQNLYTEWVHEKTNLVFATMFRTIFREVLLDGIASEVYLKSLKKHAISQISVRAHHSWVKKQEKMMLEMREKNRQEKYFSVLNSVVKAESSNITRLPIKRTFYGDTRNLDKASEKLRAEHDRTRRLWKPVLMDSLFSNLQKFPVYEDWHLLIFNASTSSMMKTWLCAKFSLKETNKTSFWHSSYNLFNRQYHVDMPDNVSDLPQTRLCYGACVYNVGLLDEEKRKDLANSDLNSSPKLIQGNDSRSAHESSANKLFSFVHDISRLTITKLPLLLIFWSDSNLDMQGITQKYRFLELITSTWSAISSIHVLTITNDRDMDLEHSLKVLLDNVTVEKSPFAQLEELEVVRKKREAEIEASSKTVKRLASNNKFLTDSNVEGLLEAPTSLENSLVEDDKWASLRQKIKAARDLLKKVETFY 1024 O74907 Protein bcp1 bcp1 284812 Yes SL-0178 Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O74907 Pfam PF13862 Involved in nuclear export, actin cytoskeleton organization and vesicular transport. {ECO:0000250}. GO:0005623 GO:0005737 GO:0005783 GO:0097431 GO:0005635 GO:0005634 GO:0019207 GO:0015631 GO:0006974 GO:0000132 GO:0034453 GO:0090307 GO:0007052 GO:0000079 GO:0000055 MAKRHAEENEDTVMSESLKVVDTDFINVDFEFFDPQPIDFHAFKNLLKQLLGYDHTNVNLSALADLILSQPLLGSTVKVDGNNSDPYAMLSVINLNTRRDEPVIKQLTSYIISRLAKSNSRLENELQKLLEPNSGSQVGLIVNERLINMPVQVIPPMYNMLLEEMQWAINENEPYNFTHYLLLSRTYTEIESKLMDDERPSKKGKKSKKTSGEEVMFFHPEDEQFREVAIDIADYPFANQDFNPDANRVFQDAGIKPQGELLLMTNEDFKNLVPKLMEIYSA 282 O75112 LIM domain-binding protein 3 LDB3 9606 Yes SL-0198 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. UNIPROT O75112 UNIPROT A2TDB7 UNIPROT A6NIV4 UNIPROT B4E3K3 UNIPROT Q5K6N9 UNIPROT Q5K6P0 UNIPROT Q5K6P1 UNIPROT Q96FH2 UNIPROT Q9Y4Z3 UNIPROT Q9Y4Z4 UNIPROT Q9Y4Z5 PDB 1RGW PDB 4YDP Pfam PF15936 Pfam PF00412 Pfam PF00595 PROSITE PS00478 PROSITE PS50023 PROSITE PS50106 OMIM 601493 OMIM 605906 OMIM 609452 DisGeNET 11155 May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.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. P02768 EBI-714423,EBI-1222667 GO:0005912 GO:0005856 GO:0031941 GO:0048471 GO:0031143 GO:0001725 GO:0030018 GO:0003779 GO:0008092 GO:0046872 GO:0051371 GO:0005080 GO:0030036 GO:0007507 GO:0061061 GO:0045214 MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASDPGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPASAQPPAAASPSAASPPLATAAAHTAIASASTTAPASSPADSPRPQASSYSPAVAASSAPATHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASTYSPSPGANYSPTPYTPSPAPAYTPSPAPAYTPSPVPTYTPSPAPAYTPSPAPNYNPAPSVAYSGGPAEPASRPPWVTDDSFSQKFAPGKSTTSISKQTLPRGGPAYTPAGPQVPPLARGTVQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFTCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPLCAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDRPLCKKHAHTINL 727 O75140 GATOR complex protein DEPDC5 DEPDC5 9606 Yes SL-0198 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}. UNIPROT O75140 UNIPROT A6H8V6 UNIPROT A8MPX9 UNIPROT B4DH93 UNIPROT B9EGN9 UNIPROT Q5K3V5 UNIPROT Q5THY9 UNIPROT Q5THZ0 UNIPROT Q5THZ1 UNIPROT Q5THZ3 UNIPROT Q68DR1 UNIPROT Q6MZX3 UNIPROT Q6PEZ1 UNIPROT Q9UGV8 UNIPROT Q9UH13 PDB 6CES PDB 6CET Pfam PF00610 Pfam PF12257 PROSITE PS50186 OMIM 604364 OMIM 614191 DisGeNET 9681 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}.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}. Q5T011 EBI-10749411,EBI-11102814 Q12980 EBI-2650314,EBI-11102814 Q8WTW4 EBI-11102814,EBI-1043552 Q99459 EBI-11102814,EBI-374880 P58043 EBI-9638431,EBI-11102814 Q9Y664 EBI-11102814,EBI-1048252 Q96MD2 EBI-11102814,EBI-20840475 Q969R8 EBI-11102814,EBI-723695 Q5T011-5 EBI-11102814,EBI-10245139 Q93079 EBI-352469,EBI-11102814 Q1RMZ1 EBI-21285976,EBI-11102814 GO:0005829 GO:1990130 GO:0005765 GO:0005764 GO:0048471 GO:0005096 GO:0044877 GO:0034198 GO:0035556 GO:0032007 GO:1904262 GO:0010506 MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEINRASIRQDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSAPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKPASEKAKNGRDTSLGSPKESENALPIQVDYDAYDAQVFRLPGPSRAQCLTTCRSVRERESHSRKSASSCDVSSSPSLPSRTLPTEEVRSQASDDSSLGKSANILMIPHPHLHQYEVSSSLGYTSTRDVLENMMEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSGQRDPTHSSAELLELAYHEAAGRHSNSRQPGDGMSFLNFSGTEELSVGLLSNSGAGMNPRTQNKDSLEDSVSTSPDPILTLSAPPVVPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADIDRRDEDGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNPAVPPPLSSSPLYSRGLVSRNRPEEEDQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVEFSHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEAHCDIYGDRPRADEDEWQLLDGFVRFVEGLNRIRRRHRSDRMMRKGTAMKGLQMTGPISTHSLESTAPPVGKKGTSALSALLEMEASQKCLGEQQAAVHGGKSSAQSAESSSVAMTPTYMDSPRKDGAFFMEFVRSPRTASSAFYPQVSVDQTATPMLDGTSLGICTGQSMDRGNSQTFGNSQNIGEQGYSSTNSSDSSSQQLVASSLTSSSTLTEILEAMKHPSTGVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVAMQQPATTWHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTSCLEKMHASAP 1603 O75146 Huntingtin-interacting protein 1-related protein HIP1R 9606 Yes SL-0198 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. UNIPROT O75146 UNIPROT A6NHQ6 UNIPROT Q6NXG8 UNIPROT Q9UED9 PDB 1R0D Pfam PF07651 Pfam PF16515 Pfam PF01608 PROSITE PS50942 PROSITE PS50945 OMIM 605613 DisGeNET 9026 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}. O14976 EBI-714707,EBI-4402639 P03372 EBI-78473,EBI-4402639 Q62925 EBI-4402639,EBI-636664 Q13404 EBI-4402639,EBI-1050671 P22314 EBI-4402639,EBI-709688 P61088 EBI-4402639,EBI-1052908 P60033 EBI-712921,EBI-4402639 P60710 EBI-353957,EBI-4402639 Q9WTI7 EBI-777558,EBI-4402639 P35579 EBI-350338,EBI-4402639 P47755 EBI-762451,EBI-4402639 Q9UHB6 EBI-351479,EBI-4402639 G3X972 EBI-11079353,EBI-4402639 P09497 EBI-726598,EBI-4402639 Q9NYZ3 EBI-2511327,EBI-4402639 Q13492 EBI-2803688,EBI-4402639 Q00610 EBI-354967,EBI-4402639 Q9ERG0 EBI-2693855,EBI-4402639 Q96H55 EBI-10983249,EBI-4402639 Q8N6K0 EBI-19027521,EBI-4402639 O95274 EBI-2561547,EBI-4402639 Q8N468 EBI-20809966,EBI-4402639 P19320 EBI-6189824,EBI-4402639 Q9NZQ7 EBI-4314282,EBI-4402639 Q9NUM3 EBI-2823239,EBI-4402639 C5E519 EBI-12562139,EBI-4402639 P32970 EBI-18539709,EBI-4402639 P35414 EBI-2875891,EBI-4402639 P46059 EBI-21560873,EBI-4402639 Q14627 EBI-4320063,EBI-4402639 P21709 EBI-968453,EBI-4402639 Q86VU5 EBI-2836030,EBI-4402639 Q6PJG9 EBI-7910762,EBI-4402639 Q96FJ0 EBI-745021,EBI-4402639 P35813 EBI-4402639,EBI-989143 Q96D71-2 EBI-4402639,EBI-10284498 Q15311 EBI-4402639,EBI-749285 Q10567-2 EBI-4402639,EBI-11037749 P23246 EBI-4402639,EBI-355453 O75688-2 EBI-4402639,EBI-21645158 O00291 EBI-4402639,EBI-473886 O60939 EBI-21671881,EBI-4402639 A2RU67 EBI-6911574,EBI-4402639 GO:0016324 GO:0005938 GO:0005905 GO:0030136 GO:0030665 GO:0005856 GO:0005829 GO:0032839 GO:0043197 GO:0043231 GO:0005739 GO:0043025 GO:0048471 GO:0005886 GO:0014069 GO:0032587 GO:0097060 GO:0051015 GO:0035615 GO:0030276 GO:0032051 GO:0042802 GO:0035091 GO:0005547 GO:0043325 GO:0080025 GO:0005546 GO:0046982 GO:0042803 GO:0017124 GO:0007015 GO:0006919 GO:0006915 GO:0048268 GO:0055123 GO:0061024 GO:0030837 GO:0043066 GO:0034316 GO:0043065 GO:1905445 GO:0045742 GO:1901030 GO:2000588 GO:0032092 GO:0048260 GO:0050821 GO:0006898 GO:0032956 GO:2000369 GO:0030100 GO:0060453 MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIEISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVSKLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADRLIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRRIEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPLAQKPSVAPRQDHQLDKKDGIYPAQLVNY 1068 O75147 Obscurin-like protein 1 OBSL1 9606 Yes SL-0198 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). UNIPROT O75147 UNIPROT A4KVA4 UNIPROT A4KVA5 UNIPROT Q96IW3 UNIPROT S4R3M6 PDB 2CPC PDB 2E6P PDB 2E6Q PDB 2LU7 PDB 2LVC PDB 2WP3 PDB 2WWK PDB 2WWM PDB 3KNB PDB 5FM5 Pfam PF07679 PROSITE PS50853 PROSITE PS50835 OMIM 610991 OMIM 612921 DisGeNET 23363 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}.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. Q92844 EBI-356349,EBI-1223896 P04792 EBI-1223896,EBI-352682 Q8IYT8 EBI-714340,EBI-1223896 Q8WVZ9 EBI-473695,EBI-1223896 Q96RR4 EBI-1104575,EBI-1223896 Q8IYM1 EBI-2585067,EBI-1223896 A7MCY6 EBI-359969,EBI-1223896 Q16539 EBI-73946,EBI-1223896 Q15759 EBI-298304,EBI-1223896 P02768 EBI-714423,EBI-1223896 Q8NEP3 EBI-11906667,EBI-1223896 C5E524 EBI-12561527,EBI-1223896 B4URF7 EBI-6050648,EBI-1223896 Q8IVT5 EBI-486984,EBI-1223896 GO:1990393 GO:0005813 GO:0005737 GO:0005829 GO:0005794 GO:0014704 GO:0031430 GO:0048471 GO:0030018 GO:0008093 GO:0055003 GO:0007010 GO:0007030 GO:0000226 GO:0050775 GO:0043687 GO:0034067 GO:0007088 MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPVVVWEKGGQQLAASERLSFPADGAEHGLLLTAALPTDAGVYVCRARNAAGEAYAAAAVTVLEPPASDPELQPAERPLPSPGSGEGAPVFLTGPRSQWVLRGAEVVLTCRAGGLPEPTLYWEKDGMALDEVWDSSHFALQPGRAEDGPGASLALRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPPESPPADPDEAPAPVVEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHWEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCAARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIAVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLIIHRLKADDDGIYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETLEAGVEGRWSRDGEELPVICQSSSGHMHALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPILAEMFKGHKNTVLLTWKPPEPAPETPFIYRLERQEVGSEDWIQCFSIEKAGAVEVPGDCVPSEGDYRFRICTVSGHGRSPHVVFHGSAHLVPTARLVAGLEDVQVYDGEDAVFSLDLSTIIQGTWFLNGEELKSNEPEGQVEPGALRYRIEQKGLQHRLILHAVKHQDSGALVGFSCPGVQDSAALTIQESPVHILSPQDRVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESELLVVKMDGRKHRLILPEAKVQDSGEFECRTEGVSAFFGVTVQDPPVHIVDPREHVFVHAITSECVMLACEVDREDAPVRWYKDGQEVEESDFVVLENEGPHRRLVLPATQPSDGGEFQCVAGDECAYFTVTITDVSSWIVYPSGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLQKEDTVRRLVLPAVQLEDSGEYLCEIDDESASFTVTVTEPPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKDGLEVEESEALVLERDGPRCRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLHFGAPGRVELRCEVAPAGSQVRWYKDGLEVEASDALQLGAEGPTRTLTLPHAQPEDAGEYVCETRHEAITFNVILAEPPVQFLALETTPSPLCVAPGEPVVLSCELSRAGAPVVWSHNGRPVQEGEGLELHAEGPRRVLCIQAAGPAHAGLYTCQSGAAPGAPSLSFTVQVAEPPVRVVAPEAAQTRVRSTPGGDLELVVHLSGPGGPVRWYKDGERLASQGRVQLEQAGARQVLRVQGARSGDAGEYLCDAPQDSRIFLVSVEEPLLVKLVSELTPLTVHEGDDATFRCEVSPPDADVTWLRNGAVVTPGPQVEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSARLHVRETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHDSRLSMAQDGHIHRLFIHGVILADQGTYGCESHHDRTLARLSVRPRQLRVLRPLEDVTISEGGSATFQLELSQEGVTGEWARGGVQLYPGPKCHIHSDGHRHRLVLNGLGLADSGCVSFTADSLRCAARLIVREVPVTIVRGPHDLEVTEGDTATFECELSQALADVTWEKDGNALTPSPRLRLQALGTRRLLQLRRCGPSDAGTYSCAVGTARAGPVRLTVRERTVAVLSELRSVSAREGDGATFECTVSEVETTGRWELGGRPLRPGARVRIRQEGKKHILVLSELRAEDAGEVRFQAGPAQSLALLEVEALPLQMCRHPPREKTVLVGRRAVLEVTVSRSGGHVCWLREGAELCPGDKYEMRSHGPTHSLVIHDVRPEDQGTYCCQAGQDSTHTRLLVEGN 1896 O75569 Interferon-inducible double-stranded RNA-dependent protein kinase activator A PRKRA 9606 Yes SL-0198 Cytoplasm, perinuclear region. Cytoplasm. UNIPROT O75569 UNIPROT A8K3I6 UNIPROT Q53G24 UNIPROT Q6X7T5 UNIPROT Q8NDK4 PDB 2DIX Pfam PF00035 Pfam PF16482 PROSITE PS50137 OMIM 603424 OMIM 612067 DisGeNET 8575 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}.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. Self EBI-713955,EBI-713955 Q5S007 EBI-5323863,EBI-713955 P60953-1 EBI-3625591,EBI-713955 Q9UPY3 EBI-395506,EBI-713955 Q9HA38 EBI-2548480,EBI-713955 Q9NX58 EBI-713955,EBI-713507 Q15633 EBI-713955,EBI-978581 Q92731 EBI-78505,EBI-713955 P03496 EBI-2547442,EBI-713955 P03485 EBI-713955,EBI-2547543 P03495 EBI-713955,EBI-2548993 P62487 EBI-347928,EBI-713955 Q8TES7 EBI-2350063,EBI-713955 P61965 EBI-1247084,EBI-713955 P62753 EBI-356625,EBI-713955 Q9H898-2 EBI-11529334,EBI-713955 P19525 EBI-640775,EBI-713955 O56264 EBI-6150240,EBI-713955 Q0HD54 EBI-6147978,EBI-713955 Q86VP6 EBI-456077,EBI-713955 Q9UPE1 EBI-6381269,EBI-713955 Q81YN3 EBI-2819062,EBI-713955 O60506 EBI-713955,EBI-1024357 Q14558 EBI-724449,EBI-713955 Q9NZI8 EBI-1053892,EBI-713955 Q9Y3U8 EBI-1057689,EBI-713955 P0DTD1 EBI-25475891,EBI-713955 Q96SI9 EBI-713955,EBI-740355 O95793 EBI-358174,EBI-713955 Q08426 EBI-713955,EBI-2339219 Q8TBB1 EBI-713955,EBI-739832 P78563-4 EBI-12002366,EBI-713955 O15226 EBI-713955,EBI-766011 O75928-2 EBI-348567,EBI-713955 P38732 EBI-713955,EBI-24379 Q7L5N1 EBI-486838,EBI-713955 O60383 EBI-473825,EBI-713955 Q15047 EBI-79691,EBI-713955 GO:0005737 GO:0005829 GO:0016020 GO:0005654 GO:0048471 GO:0070578 GO:0003725 GO:0008047 GO:0019899 GO:0042802 GO:0070883 GO:0042803 GO:0003723 GO:0034599 GO:0006955 GO:0042474 GO:0010586 GO:0008285 GO:0042473 GO:2001244 GO:0031054 GO:0035196 GO:0030422 GO:0006468 GO:0050821 GO:0009615 GO:0048705 GO:0016032 MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTDYIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK 313 O75608 Acyl-protein thioesterase 1 LYPLA1 9606 Yes SL-0178 SL-0182 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}. UNIPROT O75608 UNIPROT O43202 UNIPROT Q9UQF9 PDB 1FJ2 PDB 5SYM Pfam PF02230 OMIM 605599 DisGeNET 10434 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}. P03496 EBI-1052185,EBI-2547442 Q8N3Z0 EBI-20628340,EBI-1052185 P19320 EBI-6189824,EBI-1052185 Q14164 EBI-1052185,EBI-307369 P40337 EBI-1052185,EBI-301246 Q08379 EBI-618309,EBI-1052185 Q5VUG0 EBI-12025260,EBI-1052185 Q8IWL3 EBI-1805738,EBI-1052185 GO:0005737 GO:0005829 GO:0005783 GO:0070062 GO:0031965 GO:0005886 GO:0052689 GO:0016298 GO:0004622 GO:0008474 GO:0004620 GO:0006631 GO:0042997 GO:0002084 GO:0050999 MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID 230 O75694 Nuclear pore complex protein Nup155 NUP155 9606 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT O75694 UNIPROT Q9UBE9 UNIPROT Q9UFL5 PDB 5A9Q PDB 5IJN PDB 5IJO Pfam PF03177 Pfam PF08801 OMIM 606694 OMIM 615770 DisGeNET 9631 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}.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. Q5S007 EBI-5323863,EBI-1050769 Q9HBL7 EBI-714824,EBI-1050769 Q96I36 EBI-6570698,EBI-1050769 Q99459 EBI-1050769,EBI-374880 Q9Y275 EBI-519169,EBI-1050769 Q15077 EBI-10235794,EBI-1050769 P51159 EBI-716881,EBI-1050769 Q8IY21 EBI-2807346,EBI-1050769 Q9Y586 EBI-6659161,EBI-1050769 Q8WYP5 EBI-396018,EBI-1050769 Q53GS7 EBI-1955541,EBI-1050769 O43281 EBI-1050769,EBI-718488 Q8WVZ9 EBI-473695,EBI-1050769 Q8IY92 EBI-2370740,EBI-1050769 Q99P88 EBI-2551981,EBI-1050769 Q09019 EBI-724564,EBI-1050769 Q6GQQ9 EBI-527784,EBI-1050769 Q9ERU9 EBI-643756,EBI-1050769 Q68CZ1 EBI-5235485,EBI-1050769 Q86VQ0 EBI-6658186,EBI-1050769 Q66GS9 EBI-1046993,EBI-1050769 Q9P0N5 EBI-721260,EBI-1050769 Q86X19 EBI-11343485,EBI-1050769 Q15637 EBI-1050769,EBI-744603 P02545 EBI-351935,EBI-1050769 Q15388 EBI-711636,EBI-1050769 O15155 EBI-749204,EBI-1050769 P27824 EBI-355947,EBI-1050769 P19320 EBI-6189824,EBI-1050769 Q15843 EBI-716247,EBI-1050769 Q92905 EBI-594661,EBI-1050769 Q13618 EBI-456129,EBI-1050769 P02751 EBI-1220319,EBI-1050769 A0A384KHV9 EBI-2862405,EBI-1050769 P01889 EBI-1050769,EBI-1046513 Q9Y4K3 EBI-1050769,EBI-359276 P11171 EBI-1050769,EBI-1050906 P11802 EBI-1050769,EBI-295644 P19532 EBI-1050769,EBI-1048957 P23508 EBI-1050769,EBI-307531 P40337 EBI-1050769,EBI-301246 Q86UK5 EBI-7260649,EBI-1050769 Q8IVT5 EBI-486984,EBI-1050769 GO:0043657 GO:0016020 GO:0005635 GO:0031965 GO:0044611 GO:0017056 GO:0086014 GO:0075733 GO:0006406 GO:0006998 GO:0006606 GO:0036228 GO:0016925 GO:1900034 GO:0060964 GO:0006110 GO:0006405 GO:0000972 GO:0006409 GO:0016032 GO:0019083 MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANELLQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIVGLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALYNWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH 1391 O75716 Serine/threonine-protein kinase 16 STK16 9606 Yes SL-0198 Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}. UNIPROT O75716 UNIPROT A8K9H9 UNIPROT Q5U0F8 UNIPROT Q96KI2 UNIPROT Q9BUH4 UNIPROT Q9UEN3 UNIPROT Q9UP78 PDB 2BUJ Pfam PF00069 PROSITE PS50011 PROSITE PS00108 OMIM 604719 DisGeNET 8576 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}. O15162 EBI-740019,EBI-749295 Q6UY14 EBI-742002,EBI-749295 Q8IWZ5 EBI-749295,EBI-5235829 P50222 EBI-748397,EBI-749295 Q8IYX7 EBI-749295,EBI-3957636 O43186 EBI-748171,EBI-749295 O43597 EBI-742487,EBI-749295 O43734 EBI-749295,EBI-744798 O95967 EBI-749295,EBI-743414 P12757 EBI-2902468,EBI-749295 P14373 EBI-719493,EBI-749295 P15884 EBI-749295,EBI-533224 P49247 EBI-749295,EBI-744831 P60370 EBI-749295,EBI-10172150 P60409 EBI-10172290,EBI-749295 P60410 EBI-749295,EBI-10171774 P60411 EBI-749295,EBI-10172052 Q04864 EBI-307352,EBI-749295 Q08117 EBI-717810,EBI-749295 Q0VD86 EBI-749295,EBI-6509505 Q13137 EBI-739580,EBI-749295 Q13829 EBI-2505861,EBI-749295 Q15654 EBI-742327,EBI-749295 Q5JR59 EBI-742948,EBI-749295 Q5JST6 EBI-749295,EBI-2349927 Q5JXC2 EBI-749295,EBI-2801965 Q6PEX3 EBI-749295,EBI-3957672 Q7Z3S9 EBI-749295,EBI-945833 Q8HWS3 EBI-749295,EBI-746118 Q8N5Z5-2 EBI-749295,EBI-10189368 Q8N5Z5 EBI-743960,EBI-749295 Q92824 EBI-751290,EBI-749295 Q96EY1-2 EBI-749295,EBI-3952284 Q96Q35 EBI-749295,EBI-750451 Q99081 EBI-749295,EBI-722877 Q9BQ13 EBI-749295,EBI-10189448 Q9GZT8 EBI-749295,EBI-740897 Q9NRY6 EBI-750734,EBI-749295 Q9UKT9 EBI-749295,EBI-747204 Q9Y295 EBI-749295,EBI-719554 Q8XC86 EBI-749295,EBI-10038594 Q7DB77 EBI-749295,EBI-6480811 B7UM99 EBI-2504426,EBI-749295 Q9Y4P1-2 EBI-749295,EBI-21856470 Q96GV9 EBI-749295,EBI-2350695 Q8WVV4-1 EBI-749295,EBI-11986735 Q6ZVX7 EBI-749295,EBI-2877737 Q6BDS2 EBI-749295,EBI-11028496 Q5QP82-2 EBI-749295,EBI-10983996 Q3ZCM7 EBI-749295,EBI-302558 Q13509 EBI-749295,EBI-350989 P20930 EBI-749295,EBI-1058782 Q96KN3 EBI-2692890,EBI-749295 Q6NX45 EBI-10251462,EBI-749295 Q9HB66 EBI-1054754,EBI-749295 Q6P2I7 EBI-1047027,EBI-749295 Q14680 EBI-749295,EBI-1046702 Q14164 EBI-749295,EBI-307369 P40337 EBI-749295,EBI-301246 O75116 EBI-749295,EBI-366288 P26441 EBI-749295,EBI-1050897 Q96RG2 EBI-749295,EBI-1042651 P63162 EBI-749295,EBI-712493 Q93063 EBI-749295,EBI-1047761 P41235 EBI-749295,EBI-1049011 Q15583 EBI-749295,EBI-714215 Q05084 EBI-749295,EBI-1046751 Q9NRH2 EBI-1053132,EBI-749295 Q13185 EBI-78176,EBI-749295 A8MQ03 EBI-3867333,EBI-749295 P0DPK4 EBI-22310682,EBI-749295 Q7Z3K6-2 EBI-12224671,EBI-749295 Q70EL1-9 EBI-11975223,EBI-749295 Q9BQ13-2 EBI-12278688,EBI-749295 Q04864-2 EBI-10829018,EBI-749295 Q07627 EBI-11959885,EBI-749295 Q52LG2 EBI-11953846,EBI-749295 O14508 EBI-617737,EBI-749295 Q9Y3S2 EBI-749295,EBI-373456 Q93015-2 EBI-749295,EBI-12126220 Q06546 EBI-749295,EBI-638925 Q9NQX0 EBI-11320284,EBI-749295 Q7RTU4 EBI-17508719,EBI-749295 Q6P1L6 EBI-10252492,EBI-749295 Q9BS75 EBI-10693436,EBI-749295 P27918 EBI-9038570,EBI-749295 Q9Y6H3 EBI-12811889,EBI-749295 Q15323 EBI-948001,EBI-749295 Q5T749 EBI-10981970,EBI-749295 O95994 EBI-712648,EBI-749295 Q6UY14-3 EBI-10173507,EBI-749295 P51114-2 EBI-11022345,EBI-749295 Q2I0M5 EBI-12821217,EBI-749295 P31321 EBI-2805516,EBI-749295 A8MUP2 EBI-749295,EBI-12842046 O15496 EBI-726466,EBI-749295 Q96D03 EBI-742054,EBI-749295 A0A087WVE9 EBI-12808086,EBI-749295 Q8IUC1 EBI-1052037,EBI-749295 Q03431 EBI-2860297,EBI-749295 O43559 EBI-725515,EBI-749295 GO:0005737 GO:0005829 GO:0005798 GO:0016020 GO:0048471 GO:0005524 GO:0004715 GO:0004674 GO:0000978 GO:0071560 GO:0045944 GO:0046777 MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI 305 O75821 Eukaryotic translation initiation factor 3 subunit G EIF3G 9606 Yes SL-0198 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. UNIPROT O75821 UNIPROT O14801 UNIPROT Q969U5 PDB 2CQ0 PDB 2MJC PDB 5K0Y Pfam PF12353 Pfam PF00076 PROSITE PS50102 OMIM 603913 DisGeNET 8666 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}. Q5S007 EBI-5323863,EBI-366632 P09622 EBI-353366,EBI-366632 O95714 EBI-1058922,EBI-366632 P03372 EBI-78473,EBI-366632 Q08379 EBI-618309,EBI-366632 Q8IZU0 EBI-10175124,EBI-366632 Q9P2Y5 EBI-2952704,EBI-366632 Q9Y6I4 EBI-2512643,EBI-366632 Q9Z0R6 EBI-2551755,EBI-366632 P23116 EBI-2552342,EBI-366632 O15372 EBI-709735,EBI-366632 Q6ZWV7 EBI-2554199,EBI-366632 E9QNG1 EBI-11017012,EBI-366632 P27635 EBI-352398,EBI-366632 P60229 EBI-2678912,EBI-366632 Q9QZD9 EBI-7466616,EBI-366632 Q49MI3-2 EBI-21731382,EBI-366632 A9UHW6-2 EBI-366632,EBI-9118295 P03366 EBI-6164084,EBI-366632 Q13618 EBI-456129,EBI-366632 A0A384L807 EBI-366632,EBI-2844797 Q5NEC0 EBI-366632,EBI-2796355 P62330 EBI-366632,EBI-638181 O60739 EBI-366632,EBI-1043343 P20339 EBI-399437,EBI-366632 P55884 EBI-366632,EBI-366696 Q9UMQ6 EBI-366632,EBI-3915726 Q8K337-1 EBI-25409743,EBI-366632 Q6ZR37 EBI-20845503,EBI-366632 Q6FHY5 EBI-16439278,EBI-366632 P40217 EBI-366632,EBI-8951 Q6IQ23 EBI-2125301,EBI-366632 Q9Y262 EBI-366632,EBI-373519 Q99613 EBI-366632,EBI-353741 Q7L2H7 EBI-366632,EBI-353901 Q14152 EBI-366632,EBI-366617 Q13347 EBI-366632,EBI-354047 P60228 EBI-366632,EBI-347740 P55884-2 EBI-366632,EBI-16399439 O15371 EBI-366632,EBI-353818 O00303 EBI-366632,EBI-711990 O75822 EBI-366647,EBI-366632 Q99547 EBI-366632,EBI-373187 GO:0005737 GO:0005829 GO:0016282 GO:0033290 GO:0005852 GO:0048471 GO:0003723 GO:0003743 GO:0001732 GO:0006413 GO:0075525 MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN 320 O75844 CAAX prenyl protease 1 homolog ZMPSTE24 9606 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O75844 UNIPROT B3KQI7 UNIPROT D3DPU7 UNIPROT Q8NDZ8 UNIPROT Q9UBQ2 PDB 2YPT PDB 4AW6 PDB 5SYT PDB 6BH8 Pfam PF01435 Pfam PF16491 OMIM 275210 OMIM 606480 OMIM 608612 DisGeNET 10269 Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C.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. P08473 EBI-353759,EBI-1056377 Q5S007 EBI-5323863,EBI-1056377 Q6NUS6 EBI-11278332,EBI-1056377 Q96GX1 EBI-11349465,EBI-1056377 Q16666-2 EBI-6273540,EBI-1056377 Q08AM6 EBI-2107455,EBI-1056377 P54219 EBI-21493000,EBI-1056377 O15263 EBI-1056377,EBI-21800352 P14324 EBI-948245,EBI-1056377 P04798 EBI-10194262,EBI-1056377 Q77M19 EBI-6149376,EBI-1056377 Q9UET6 EBI-1056377,EBI-1055987 P16401 EBI-1056377,EBI-5327611 A4D263 EBI-1056377,EBI-20831539 P47902 EBI-8514176,EBI-1056377 P06821 EBI-2547404,EBI-1056377 O00624-2 EBI-21654602,EBI-1056377 Q20MH8 EBI-12576433,EBI-1056377 C5E519 EBI-12562139,EBI-1056377 Q6DPW5 EBI-1056377,EBI-12562156 Q99679 EBI-6309069,EBI-1056377 P29084 EBI-2853321,EBI-1056377 Q13503 EBI-394678,EBI-1056377 Q6PEY0 EBI-21551278,EBI-1056377 P22732 EBI-2825135,EBI-1056377 Q8WTR4 EBI-2833203,EBI-1056377 Q86WS5 EBI-21771370,EBI-1056377 Q9BY78 EBI-2129375,EBI-1056377 Q02223 EBI-519945,EBI-1056377 Q9BVJ7 EBI-724940,EBI-1056377 GO:0070062 GO:0030176 GO:0016020 GO:0005637 GO:0032991 GO:0003690 GO:0046872 GO:0004222 GO:0008235 GO:0007628 GO:0030282 GO:0071586 GO:1990036 GO:0061762 GO:0061337 GO:0048739 GO:0003231 GO:0044255 GO:0071480 GO:0008340 GO:0006281 GO:0003417 GO:0001942 GO:0003007 GO:1990164 GO:0043979 GO:0044029 GO:0006925 GO:0060993 GO:0001889 GO:0043007 GO:0035264 GO:1903799 GO:0050905 GO:0006998 GO:0030327 GO:0006508 GO:0010506 GO:0030500 GO:0008360 GO:2000772 GO:0050688 GO:0043516 GO:0048145 GO:0010906 GO:2000618 GO:0032350 GO:0019216 GO:1903463 GO:0040014 GO:1903025 GO:0070302 GO:2000730 GO:0032006 GO:0060307 GO:0072423 GO:0048538 GO:0003229 MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH 475 O76050 E3 ubiquitin-protein ligase NEURL1 NEURL1 9606 Yes SL-0198 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}. UNIPROT O76050 UNIPROT Q5TDR2 UNIPROT Q5TDR3 UNIPROT Q8TAN0 UNIPROT Q9H463 Pfam PF07177 PROSITE PS51065 PROSITE PS50089 OMIM 603804 DisGeNET 9148 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}. P62256 EBI-2129909,EBI-2129917 P61088 EBI-2129917,EBI-1052908 Q07065 EBI-702400,EBI-2129917 GO:0097440 GO:0030054 GO:0043197 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0046872 GO:0045183 GO:0061630 GO:0004842 GO:0007420 GO:0071230 GO:0007595 GO:0008285 GO:0045746 GO:0007399 GO:0007219 GO:0043065 GO:0060999 GO:0045741 GO:0051491 GO:0048170 GO:0090129 GO:0006513 GO:0007519 GO:0007288 MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRREADDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGRDERALVFTSRPVRVAETIFVKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFGLHGTITQIRILGSTILAERGIPSLPCSPASTPTSPSALGSRLSDPLLSTCSSGPLGSSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYACGLRLKKALHACCPICRRPIKDIIKTYRSS 574 O76070 Gamma-synuclein SNCG 9606 Yes SL-0198 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. UNIPROT O76070 UNIPROT O15104 UNIPROT Q96P61 Pfam PF01387 OMIM 602998 DisGeNET 6623 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}. P36895 EBI-2551936,EBI-1053810 E9QKK1 EBI-10967445,EBI-1053810 P15090 EBI-1053810,EBI-715333 P16035 EBI-1053810,EBI-1033507 P63167 EBI-349105,EBI-1053810 P63162 EBI-1053810,EBI-712493 Q93063 EBI-1053810,EBI-1047761 P25205 EBI-355153,EBI-1053810 A6NEW6 EBI-1058455,EBI-1053810 P41235 EBI-1053810,EBI-1049011 Q96AE4 EBI-711404,EBI-1053810 P17844 EBI-351962,EBI-1053810 P26038 EBI-528768,EBI-1053810 GO:0030424 GO:0005813 GO:0005737 GO:0070062 GO:0043025 GO:0016604 GO:0048471 GO:0005819 GO:0045202 GO:0008344 GO:0007268 GO:0009306 GO:0014059 GO:0046928 GO:0050808 MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD 127 O76329 Interaptin abpD 44689 Yes SL-0178 SL-0182 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. UNIPROT O76329 UNIPROT Q54KE8 Pfam PF00307 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. {ECO:0000269|PubMed:10704840}. Q54CH1 EBI-922673,EBI-922333 Q55FK4 EBI-922673,EBI-923109 Q55CS9 EBI-922673,EBI-922719 Q23858 EBI-922673,EBI-922479 P34122 EBI-922673,EBI-922223 P25870 EBI-922673,EBI-922873 P34121 EBI-922673,EBI-922516 Q54HL0 EBI-922673,EBI-922776 Q54KG1 EBI-922673,EBI-922528 Q54T81 EBI-922673,EBI-922504 Q54NB6 EBI-922673,EBI-922647 P46800 EBI-922673,EBI-922628 Q552M5 EBI-922673,EBI-922619 Q557E0 EBI-922673,EBI-922634 P54651 EBI-922673,EBI-922325 Q55GF9 EBI-922673,EBI-922339 Q6RZZ9 EBI-922673,EBI-922684 Q54BF6 EBI-922673,EBI-923149 P34118 EBI-922673,EBI-922706 Q86HW7 EBI-922673,EBI-922768 Q869Y7 EBI-922673,EBI-922419 Q23921 EBI-922673,EBI-922745 Q54JM5 EBI-922673,EBI-922759 Q54BH4 EBI-922673,EBI-923145 Q54BP1 EBI-922673,EBI-923138 Q54DL5 EBI-922673,EBI-922272 Q54FU0 EBI-922673,EBI-923247 Q54G01 EBI-922673,EBI-923094 Q54G31 EBI-922673,EBI-923215 Q54GS4 EBI-922673,EBI-923090 Q54GY1 EBI-922673,EBI-922371 Q54H23 EBI-922673,EBI-922580 Q54I73 EBI-922673,EBI-923085 Q54NB4 EBI-922673,EBI-922353 Q54R55 EBI-922673,EBI-922697 Q54RZ4 EBI-922673,EBI-922740 Q54TQ6 EBI-922673,EBI-922268 Q54U97 EBI-922673,EBI-923179 Q54U98 EBI-922673,EBI-923175 Q54VJ7 EBI-922673,EBI-923191 Q54VQ1 EBI-922673,EBI-922276 Q54W02 EBI-922673,EBI-923183 Q54XP9 EBI-922673,EBI-922287 Q556V8 EBI-922673,EBI-922522 Q55CE3 EBI-922673,EBI-923130 Q55CZ0 EBI-922673,EBI-923125 Q55F82 EBI-922673,EBI-923195 Q55F84 EBI-922673,EBI-923117 Q55GC0 EBI-922673,EBI-923102 Q55GC5 EBI-922673,EBI-923098 Q75JY8 EBI-922673,EBI-923167 P33519 EBI-922673,EBI-922261 Q86K01 EBI-922673,EBI-923199 Q559R0 EBI-922673,EBI-922602 P52285 EBI-922673,EBI-922789 Q95ZG4 EBI-922673,EBI-922344 P32255 EBI-922673,EBI-922437 P32256 EBI-922673,EBI-922454 Q55AR3 EBI-922673,EBI-922237 Q54TH8 EBI-922673,EBI-922491 Q54LP7 EBI-922673,EBI-922254 Q54WN5 EBI-922673,EBI-923208 Q55EX9 EBI-922673,EBI-923160 GO:0005789 GO:0032580 GO:0016021 GO:0005815 GO:0005635 GO:0031965 GO:0042175 GO:0003779 GO:0098609 GO:0007275 GO:0009847 MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRLHYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQISDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTYISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSFEGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEVEKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKIGGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTNSSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQETHRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERINQQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSNIDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIENQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEKDENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIEKENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDSQFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKVKQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQLKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQSELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLKEKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPPTASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIAQEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT 1738 O77059 Cryptochrome-1 cry 7227 Yes SL-0198 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}. UNIPROT O77059 UNIPROT Q9TYA0 PDB 4GU5 PDB 4JZY PDB 4K03 Pfam PF00875 Pfam PF03441 PROSITE PS51645 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}. P18431 EBI-242141,EBI-94117 P49021 EBI-266295,EBI-94117 P07663 EBI-496170,EBI-94117 GO:0005737 GO:0005829 GO:0005641 GO:0005654 GO:0005634 GO:0048471 GO:0032991 GO:0009882 GO:0071949 GO:0050660 GO:0008020 GO:0009881 GO:0009785 GO:0071482 GO:0048512 GO:0032922 GO:0007623 GO:0050980 GO:0009649 GO:0043153 GO:0042332 GO:0045475 GO:0050958 GO:0045892 GO:0007602 GO:0018298 GO:0042752 GO:0045187 GO:0009637 GO:0009416 GO:0071000 GO:0009588 MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV 542 O77507 DNA repair protein RAD51 homolog 1 RAD51 9986 Yes SL-0198 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}. UNIPROT O77507 Pfam PF08423 PROSITE PS50162 PROSITE PS50163 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}. GO:0005737 GO:0005815 GO:0005759 GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0003690 GO:0000150 GO:0003697 GO:0017116 GO:0072757 GO:0006974 GO:0071479 GO:0000730 GO:0006268 GO:0000724 GO:0036297 GO:1990426 GO:0010569 MAMQMQLEANADTSVEEESFGPQPVSRLEQCGINANDVKKLEEAGFHTEEAVAYAPKKELINIKGISEAKADKILTEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVTVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD 339 O77691 Protein S100-A6 S100A6 9796 Yes SL-0178 Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. UNIPROT O77691 Pfam PF01023 PROSITE PS00018 PROSITE PS50222 PROSITE PS00303 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}. GO:0005829 GO:0031234 GO:0005635 GO:0048471 GO:0001726 GO:0005509 GO:0048306 GO:0042803 GO:0044548 GO:0005523 GO:0008270 MACPLDQAISLLVAIFHKYSSREGDKNTLSKGELKELIQKELTIGAELEDSEIAKLLDDLDQNKDQVVNFQEYVTFLGALAMIYNEVLKACS 92 O77737 Bcl-2-like protein 1 BCL2L1 9823 Yes SL-0178 SL-0182 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}. UNIPROT O77737 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. GO:0030054 GO:0005813 GO:0005737 GO:0005829 GO:0016021 GO:0005759 GO:0005741 GO:0031965 GO:0030672 GO:0046982 GO:0042803 GO:0006897 GO:0097192 GO:0008630 GO:0007093 GO:0043066 GO:1902236 GO:1900118 GO:2001243 GO:0032465 MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK 233 O77751 Transmembrane protein 109 TMEM109 9986 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT O77751 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}. GO:0005783 GO:0016021 GO:0031965 GO:0005640 GO:0033017 GO:0005244 GO:0071480 GO:0060548 GO:0034765 MAGSGSSAPWGKHLLHAVLMVLVALVLLHSALAQSHRDFAPPGQQRREAPVDLLTQIGRSVRETLDTWIGPETMHLISETLSQVMWAISSAISVAFFALSGIAAQLLTALGLDGDHLTQGLKLSPSQVQTFLLWGAGALVVYWLLSLLLGLVLAVLGRILGGLKLVIFLAGFVALVRSVPDPSTRALLLLALLTLYALLSRLTGSRASGAQLEAKVRGLERQVDELRWRQRRAAKGARSVEEE 243 O80480 Importin subunit alpha-4 IMPA4 3702 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:Q96321}. UNIPROT O80480 UNIPROT F4HZG6 UNIPROT O49602 UNIPROT Q94KD4 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. Q94CL9 EBI-1773344,EBI-2131464 F8RP38 EBI-6368424,EBI-2131464 Q9SZU7 EBI-25519488,EBI-2131464 Q9LUA3 EBI-541107,EBI-2131464 Q9SIC8 EBI-4450726,EBI-2131464 Q058P7 EBI-2131464,EBI-4431752 Q8GUP4 EBI-4476287,EBI-2131464 Q8GX29 EBI-2131464,EBI-604376 GO:0005829 GO:0043657 GO:0005643 GO:0005654 GO:0061608 GO:0008139 GO:0080034 GO:0006607 GO:0030581 MSLRPSTRAELRKKIYKTGVDADEARRRREDNLVEIRKNKREDSLLKKRREGMMLQQQLPLGAGLDGPQTAAAVEKRLEGIPMMVQGVYSDDPQAQLEATTQFRKLLSIERSPPIDEVIKAGVIPRFVEFLGRHDHPQLQFEAAWALTNVASGTSDHTRVVIEQGAVPIFVKLLTSASDDVREQAVWALGNVAGDSPNCRNLVLNYGALEPLLAQLNENSKLSMLRNATWTLSNFCRGKPPTPFEQVKPALPILRQLIYLNDEEVLTDACWALSYLSDGPNDKIQAVIEAGVCPRLVELLGHQSPTVLIPALRTVGNIVTGDDSQTQFIIESGVLPHLYNLLTQNHKKSIKKEACWTISNITAGNKLQIEAVVGAGIILPLVHLLQNAEFDIKKEAAWAISNATSGGSHEQIQYLVTQGCIKPLCDLLICPDPRIVTVCLEGLENILKVGEADKEMGLNSGVNLYAQIIEESDGLDKVENLQSHDNNEIYEKAVKILERYWAEEEEEQILQDGGNDNSQQAFNFGNNPAAPVGGFKFA 538 O80528 Serine/threonine-protein kinase haspin homolog HASPIN 3702 Yes SL-0198 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}. UNIPROT O80528 UNIPROT Q84WE0 PROSITE PS50011 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}. GO:0005694 GO:0005737 GO:0005856 GO:0005634 GO:0048471 GO:0009524 GO:0005524 GO:0035402 GO:0072354 GO:0004674 GO:0035407 GO:0072355 GO:0035556 GO:0000278 MGQRVDLWSEVIKSEEEDGDIPKIEAVFQRRKKPDKSSEAVNFGWLVKGARTSSVNGPKRDSWARSLSTRGRESIAVRAYVNNQPQKKAAGRKKPPIPKGKVVKAPDFQKEKEYFRDIDAFELLEESPSPNKSSTWTMGEQVVPEMPHLSTRLEKWLISKKLNHTCGPSSTLSKILENSAIHQESVCDNDAFDSLSLKTPDKSSAGNTSVFRLIPSCDENLAAEDVPVRKIKMESIDLEDELKRLSLTSDLIPTHQDFDQPILDLLSACGQMRPSNFIEAFSKFCEPESIVKIGEGTYGEAFRAGSSVCKIVPIDGDFRVNGEVQKRADELLEEVILSWTLNQLRECETTAQNLCPTYIKTQDIKLCQGPYDPILIKAWEEWDAKHGSENDHPDFPEKQCYVMFVLEHGGKDLESFVLLNFDEARSLLVQATAGLAVAEAAFEFEHRDLHWGNILLSRNNSDTLPFILEGKQVCIKTFGVQISIIDFTLSRINTGEKILFLDLTSDPYLFKGPKGDKQSETYRKMKAVTEDYWEGSFARTNVLWLIYLVDILLTKKSFERSSKHERELRSLKKRMEKYESAKEAVSDPFFSDMLMDQIS 599 O89019 Inversin Invs 10090 Yes SL-0198 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}. UNIPROT O89019 UNIPROT O88849 Pfam PF00023 Pfam PF12796 Pfam PF00612 PROSITE PS50297 PROSITE PS50088 PROSITE PS50096 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}. Q9QZZ4 EBI-4281382,EBI-4281337 Q8BP00 EBI-4282243,EBI-4281337 Q91ZR4 EBI-4281337,EBI-4282339 Q9QY53 EBI-77230,EBI-4281337 Q8K3E5 EBI-4281337,EBI-4280729 P11499 EBI-4281337,EBI-492813 P63017 EBI-4281337,EBI-433443 P38647 EBI-4281337,EBI-772469 P20029 EBI-4281337,EBI-772325 GO:0097546 GO:0097543 GO:0005576 GO:0016020 GO:0005874 GO:0005634 GO:0048471 GO:0005819 GO:0005516 GO:0048513 GO:0060971 GO:0060287 GO:0001822 GO:0090090 GO:0031016 GO:0009791 GO:1904108 GO:0006468 GO:0016055 MNISEDVLSTGSSLASQVHAAAVNGDKGALQRLIVGNSALRDKEDRFGRTPLMYCVLADRVDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLQHPSVKDDSDLEGRTSFMWAAGKGNDDVLRTMLSLKSDIDINMSDKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGQLDTDPPRSHCSSSAPVLPCPPSPQNEGSKQDATPSKQPPASHTVQSPDPEHSRLPGRCPGRASQGDSSIDLQGTASRKPSETPIEHCRGPSACVHPRSWEGGNSSKNQGTSSVEKRRGETNGKHRRCEEGPSSARQPLCTGSGRPAEKGEDSSPAVASASQQDHPRKPNKRQDRAARPRGASQKRRTHQLRDRCSPAGSSRPGSAKGEVACADQSSLHRHTPRSKVTQDKLIGGVSSGLPLSTEASRSGCKQLYEDICASPETGVAHGPPPGQCMNIHLLPVEQRLLIIQRERSRKELFRRKNKAAAVIQRAWRSYQLRKHLSRLLHLKQLGAREVLRCTQVCTALLLQVWRKELELKFPKSISVSRTSKSPSKGSSATKYARHSVLRQIYGCSQEGKGHHPIKSSKAPAVLHLSSVNSLQSIHLDNSGRSKKFSYNLQPSSQSKNKPKL 1062 O89039 Atypical chemokine receptor 3 Ackr3 10116 Yes SL-0198 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}. UNIPROT O89039 UNIPROT Q9JLZ0 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. P30560 EBI-21299265,EBI-21299313 O08565 EBI-21299265,EBI-11167786 GO:0005623 GO:0009986 GO:0005905 GO:0005737 GO:0005769 GO:0005768 GO:0009897 GO:0016021 GO:0005634 GO:0048471 GO:0005886 GO:0055037 GO:0019957 GO:0016493 GO:0019958 GO:0016494 GO:0019956 GO:0015026 GO:0005044 GO:0001525 GO:0019722 GO:0007155 GO:0060326 GO:0070098 GO:0006935 GO:0006955 GO:1902230 GO:0007204 GO:0070374 GO:1905322 GO:0031623 GO:0001570 MDVHLFDYVEPGNYSDINWPCNSSDCIVVDTVQCPAMPNKNVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLACMSVDRYLSITYFTSTSSYKKKMVRRVVCVLVWLLAFFVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMSASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQNTK 362 O92532 RNA-directed RNA polymerase POLG 356424 No SL-0382 [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. UNIPROT O92532 Pfam PF07652 Pfam PF01543 Pfam PF01542 Pfam PF01539 Pfam PF01560 Pfam PF01538 Pfam PF01006 Pfam PF01001 Pfam PF01506 Pfam PF08300 Pfam PF08301 Pfam PF12941 Pfam PF02907 Pfam PF00998 PROSITE PS51693 PROSITE PS51192 PROSITE PS51194 PROSITE PS51822 PROSITE PS50507 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 are 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}. GO:0005576 GO:0044167 GO:0044186 GO:0044191 GO:0042025 GO:0044220 GO:0020002 GO:0016021 GO:0044385 GO:0019031 GO:0019013 GO:0055036 GO:0005524 GO:0004197 GO:0005216 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0017124 GO:0005198 GO:0008270 GO:0075512 GO:0039654 GO:0039520 GO:0039645 GO:0039707 GO:0051259 GO:0039545 GO:0039563 GO:0039547 GO:0039502 GO:0019087 GO:0039694 GO:0019062 MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPIGRSWGQPGYPWPLYGNEGCGWAGWLLSPRGSRPNWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVLGGPLGGVAAALAHGVRAIEDGVNYATGNLPGCSFSIFLLALLSCLTTPASAIQVRNASGIYHLTNDCSNNSIVFEAETIILHLPGCVPCIKVGNGSRCWLSVSPTLAVPNSSVPIHGFRRHVDLLVGAAAFCSAMYIGDLCGSVFLVGQLFTFRPKHHQVTQDCNCSIYAGHITGHRMAWDMMLNWSPTVSYVVSSALRVPQLLLEVITGAHWGVLGALLYFSMVANWAKVIAVLFLFAGADATTYTGSAVSSTTGAFVSLFSPGPTQNLQLVNSNGSWHINRTALNCNDSLQTGFIAGLFARYKFNSTGCPERMSKCRPLHSFEQGWGPISYVNISGSSEDKPYCWHYAPRPCGIVPARNVCGPVYCFTPSPVVVGTTDQRGIPTYTWGENVSDVFLLHSARPPLGAWFGCTWMNSSGFVKTCGAPPCRIKPTINETDLVCPTDCFRKHPDASFVKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIHKVRVFVGGVEHRFNAACNWTRGDRCELDDRDRFEMSPLLFSTTQLAILPCSFTTMPALSTGLIHLHQNIVDIQYLYGVSTAVVSWAMKWEYVVLAFLVLADARVCACLWLMFLVGQAEAALENVIVLNAASAASCQGLLWGLIFICCAWHVRGRAVPVTTYALLQLWPLLLLILALPRRAYAFDSEQAASAGLLVLGLITIFTLTPAYKQLLISMLWWIQYFIALTEAQLHQWVPSLLVRGGRDAVILLACLFHPQLGFEVTKILLALLGPLYLLQYSLLKTPYFVRAHILLRACMFFRGMARGRYAQAILLRIGAWTGTYIYDHLAPLSDWACDGLRDLAVAVEPVVFSPMEKKVITWGADTAACGDIIAGLPVAARRGNLLFLGPADDVKGKGWRLLAPITAYAQQTRGIVGTIVTSLTGRDKNEVEGEIQVVSTATQSFLATAVNGVLWTVYYGAGSKTLAGPKGPVCQMYTNVDQDLVGWPAPAGARSLTPCSCGSSDLYLVTRNADVIPARRRGDNRAALLSPRPISTLKGSSGGPMLCPSGHVAGIFRAAVCTRGVAKSLDFAPVESMQSSQRSPSFSDNTSPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGSYMSTSHGIDPNIRTGVRTITTGGAITYSTYGKFLADGGCSGGAYDVIICDECHSTDPTTVSGIGTVLDQAETSGVRLTVLATATPPGSVTVPHPNITESALPTTGEIPFYGKAVPLEYIKGGRHLIFCHPKKKCDELAKQLVSLGLNAVAFYRGVDVSVIPTSGDVVVCATDALMTGYTGDFDSVIDCNVTVTQVVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGKHGVYRYVSQGERPSGMFDSVILCEAYDTGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQAEENFAYLVAYQATVCARAKAPPPSWDTMWKCLIRLKPMLTGPTPLLYRLGPVQNEVVTTHPITKYIMTCMSADLEVITSTWVLVGGVVAALAAYCLSVGCVVICGRISTSGKPVLIPDREVLYQQFDEMEECSRHIPYLAEGHLIAEQFKQKVLGLIQSTSKQAEELKPAVHAAWPKLEQFWQKQLWNFVSGIQYLAGLSTLPGNPAIASLMSFSASLTSPLSTHQTLLLNILGGWVASQLANPTASTAFVVSGLAGAAVGSIGLGRVIVDVLAGYGAGVSGALVAFKIMCGETPSAEDMVNLLPALLSPGALVVGVVCAAILRRHAGPSEGATQWMNRLIAFASRGNHVSPTHYVPETDTSRQIMTILSSLTVTSLLRKLHEWINTDWSTPCSSSWLRDIWDWVCEVLSDFKTWLKAKLVPALPGVPFLSCQRGFRGTWRGDGICHTTCPCGSEITGHVKNGTMKISGPRWCSNVSHRTFPINATTTGPSVPIPEPNYTRALWRVSAEEYVEVKRVGDSHFVVGATTDNLKCPCQVPAPEFFTEVDGVRLHRYAPRCKPLLRDEVSFSVGLSSYAVGSQLPCEPEPDVTVVTSMLIDPSHVTAEAAARRLARGSPPSLASSSASQLSAPSLKATCTMHGAHPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVPEFEEREMSVPAECHRPRRPKFPPALPIWATPGYNPPVLETWKSPTYEPPVVHGCALPPSGPPPIPPPRRKKVVQLDSSNVSAALAQLAAKTFETPSSPTTGYGSDQPDHSTESSEHDRDDGVASEAESYSSMPPLEGEPGDPDLSSGSWSTVSEEGDSVVCCSYSYSWTGALVTPCAAEEEKLPINPLSNSLIRHHNLVYSTSSRSAATRQKKVTFDRVQLLDQHYYDTVKEIKLRASHVKAQLLSTEEACDLTPPHSARSKFGYGAKDVRSHASKAINHINSVWADLLEDTQTPIPTTIMAKNEVFCVDASKGGRKSARLIVYPDLGVRVCEKRALFDVTRKLPTAIMGDAYGFQYSPQQRVDRLLKMWRSKKTPMGFSYDTRCFDSTVTERDIRTEQDIYLSCQLDPEARKVIESLTERLYVGGPMYNSKGQLCGQRRCRASGVLPTSMGNTVTCFLKATAACRAAGFTDYDMLVCGDDLVVVTESAGVNEDIANLRAFTEAMTRYSATPGDEPSPTYDLELITSCSSNVSVAHDGDGRRYYYLTRDPVTPLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVLMTHFFQILQAQETLDRALDFDIYGVTYSITPLDLPVIIQRLHGMAAFSLHGYSPDELNRVASCLRKLGAPPLRAWRHRARAVRAKLIAQGGKAAVCGKYLFNWAIKTKLRLTPLRGASALDLSGWFTSGYGGGDVYHSASRARPRFLLLCLLLLSVGVGIFLLPAR 3015 O94319 Protein transport protein sec13 sec13 284812 Yes SL-0178 SL-0185 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}. UNIPROT O94319 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. O13637 EBI-21245957,EBI-21245929 GO:0030127 GO:0005737 GO:0005829 GO:0005789 GO:0000139 GO:0031080 GO:0005634 GO:0035859 GO:0005198 GO:0090114 GO:0006886 GO:0051028 GO:1904263 MTTVDTQHDDMIHDAILDYYGKRLATCSSDQTIKVFSIENNQQTLLETLRGHSGPVWQLGWAHPKFGTILASASYDGHVIVWRETGGVWSELMDHTAHQASVNAVSWAPHEYGALLACASSDGKVSVLEFKDDGSCDTRIFTAHEPGCNAVCWSPPSLSGSVVGQSPAAGPKKLATAGCDNLVKIWAFDAGVNNWILEDTLAGHVDWTRDVAWAPSVGLTKTYLASASQDKNVFIWTKEGDGPWQKTPLTEEKFPDIAWRVSWSLSGNILAVSCGDNKVYLFKESQNKWQLLNELSN 297 O94353 Nuclear membrane organization protein apq12 apq12 284812 Yes SL-0178 SL-0182 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}. UNIPROT O94353 Pfam PF12716 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0042175 GO:0044255 GO:0051028 GO:0006998 MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNKTTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF 115 O94385 Nucleoporin pom152 pom152 284812 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT O94385 UNIPROT Q9USB0 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}. GO:0016021 GO:0005635 GO:0031965 GO:0005643 GO:0070762 GO:0017056 GO:0051028 GO:0006999 GO:0006913 GO:0006606 GO:0030474 MVTRVASSERPRPLVPESIVDAPTQRLYAIGVFVALQAYKIYDLLKLETSSISDVPKSGFLVKWIIIDAIYLRLLPKFRIPWLSFQPAATLLQIAIFAAINLLLSSLSSLKWISIGSILLPYFKKKELSISEHKINPNNVIHNSSRILGQYTLQVLPEGTAKINPLHENYCLNSLRKDQYVDLAIQFNSTIPKYIQYSHVDLETKEETLVEVSGRSLRKLLSSSSKNPKEPRLQTIYLKTNKRGLYTLKHVVDKSKLDVRIFRSEAVVVSCPTATFASRQSGGRLRERCVGDTDNAELKVTGVAPLQVTYRNWDGKHFNTHIIDSTIPDDFHPPAVVLSSNPKDIVFYKGIDIQWARSSEIFVPINTLLKAPGQWIYAVTQVTDALGNSQQFPSNDQFLLRFAHGYTEADGESHSLPENVYSVFVHQRPDIQFRGCSIESPANLFPNKETSLSLYSSFSEYNSLEVGVDRYELGLDPQNITVPPLSHKTYQISPRSSANINVKKPGIYVLSSVSSQYCSGEVLEPNTCLVVTPPEAKVSVSFEEISDQCAGSIGARADLELEGTPPFTIAYRMTKDNEASRIQYVTTDRTRYQLNFTPKKAGKYRYIILGIQDANYGYRELSGSSFYKDQTVFPLADASFEERRNGDLSTVVKTSCIGDTMSLPVLLTGSAPWTLEYEIFRNNKREESHVVESKDPRYILEVPMLVHGSQYTITLVSVKDSNGCKRSLNTADTVIKVRRQRPTATFYSSDNTYTLKSVEGALMKIPLRLAGEKPWYVEYSHTSGLNKVSHHKEVLNDPNSYLTVRKSGTYTLLSVSDSSCPGTIQNVEQKYQVEWLPRPFLSIPSLESSVKGKTRYYEQNAVCAGDSSAFEVQLSGSGPFLLKHDKILVDEKSKTYPKQKSELSTVQNTVLVKADTAVPGVYHYEFTKLSDSLYSDSDAVTIVNNQSYQAVVLQRVNSLPKASFMNVEKLYTFCINTDVTQSNAQLIAIQLQGASPFSLVIGIKNELTGSVSKYTLNDIHESVYKFAFPQEQLTLGKHVVRLLQVRDANGCAASITKTQPAAKVSVVEMASLAPLGSRQYYCVGDRLSFALQGLPPFDVEYEFNGVTQHATSDSHILTRLIELPGVVAMKSISDHGSHCKSYINPPIEQIVHDIPTVRISNGKDVIENIHEGDQAEISFHFTGTPPFSFSYARRALGKKRPGKVLETHTVTGINEYEYKVLSSVEGVYTVLSVQDKYCRYPQDSTSSSNI 1250 O94418 Meiotically up-regulated gene 87 protein mug87 284812 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O94418 Pfam PF04097 Has a role in meiosis. {ECO:0000269|PubMed:16303567}. GO:0005829 GO:0005635 GO:0005643 GO:0017056 GO:0051321 GO:0016973 GO:0006606 GO:0010389 MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTWKKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRVSFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIISKAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEIIQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPYKYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFLLMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQELSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAKQADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNLLLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQKSSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT 851 O94464 Nucleus-vacuole junction protein 2 nvj2 284812 Yes SL-0178 SL-0182 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}. UNIPROT O94464 PROSITE PS51847 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}. GO:0005737 GO:0005783 GO:0005789 GO:0016021 GO:0071561 GO:0008289 GO:0006869 GO:1990854 MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQDQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELFSNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWYYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSPDTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADIWYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNNYLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRHISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASKSFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESNYSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSRNQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL 779 O94473 Uncharacterized membrane protein C1919.04 SPCC1919 284812 Yes SL-0178 SL-0182 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}. UNIPROT O94473 DE Reference Proteome: Yes; GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 MDLSFIEGFETIWTVVRAVVLNYLLRSLKILSTILYVSAVISWNVSLKVFGNVLLPGFLTIRTVVIFILRIVSLFLWILADPAILLVQSVYWYFIRAPARFILMVGITLYPLYVLLSWAVFLGIIVGFSLNSVFTFIDSFATPSSNSTVTEAMTKMKNEKVLEYPYKDRNIMLGDLASRIPSKDSEKLDEERQPIALEKTKSLDSISHSSSSSRKSSTELKIPPVETRIVAEIPVPSSVKRRRHRPNKSMGSIKNS 256 O94490 Uncharacterized transcriptional regulatory protein C417.09c SPCC417 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227}; Multi-pass membrane protein {ECO:0000305}. UNIPROT O94490 Pfam PF04082 Pfam PF00172 PROSITE PS50048 DE Reference Proteome: Yes; GO:0016021 GO:0031965 GO:0005634 GO:0000981 GO:0000978 GO:0008270 GO:0006357 GO:0006351 MHARMQPHEDRSRSGMSRSEAMELEDQLEEEERGGNVVVGSSSANANASTAETGKKSAGGSKPKRRRGERIPPSKRIRKAIAYVNKYASGCFGRVERRLVCTRSISRHSNQKLLDFCVECKKHKIKCVGNFPCGRCLKKGLECVIETPPRLLMNKDEISLNLQRLSHMETILSKLMPSMSLDLPSLEAKIAELSESLQTYPDKVLTDIELGSYQQVTLNETQTYYEDAGSNESFVARVHEIICQGREFQVQHKLTNKGNKTFEDILDPADNTVASLIHALPPKDITFYLLMTFWQFSSDNNHFYYNTKLFAAKVHHLFDDPTSFQSKDGGFVCMLLLSMAMGSLFSYIRHPEFLSDENHDRWTYPGSQFYQNAKLLFPKVISESSLETVQSFFLAGMYLSPTLAHEVVYMYFGIAMRAAVANGMHKKSANAQFSGDVAELRKRLFWSVYCMERKIGISLGRPESLVRSEIDIHFPEYRESLDSQNFIASFRTFTLAIKISLLTNKVYDMWYSSLHGKANLKAATIKEIVNEIEAWRQQLSPDLEIQNIGPDSRSYRGIVHLHLAYHIVRIAMGRPFLLHRLRERTMNSKTDEGARLLTDKLISYCYSSALHIVDLLVLLRMHKFLSVYSFMDYHSCHAASFIILVHLLINPSEQTIEQLNTAIDILNFVTDRFPLLKGSTDVITNLRAFAEQSEVYQSRLNATEPAYSTQVPFFPRDADYHNQINLQNLWNDENINASLEALFNDAKGFGFLLPADNFIFPSDDGDM 767 O94569 Uncharacterized transcriptional regulatory protein C1773.12 SPBC1773 284812 Yes SL-0178 SL-0182 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}. UNIPROT O94569 Pfam PF04082 Pfam PF00172 PROSITE PS00463 PROSITE PS50048 DE Reference Proteome: Yes; GO:0016021 GO:0000228 GO:0031965 GO:0005730 GO:0005634 GO:0000981 GO:0000978 GO:0008270 GO:0006357 GO:0006351 MVPIKKISTACDLCRQRKLRCNGELPKCQNCVVYSETCKYNKRKRVKKPNVDKDDPHIVVGQPPVKKSTAGITREYTEMIELRNHIITLSKRSVNMESRIDDMLNLLNYDLSEKRETSNEIPSLVQQIQNCGFLIDEKMRRYPGIFQIHPKDYTMNDLFPQSFPTWISVYRNVPEKAWANRCVEWYFRYINSCWPLFDLENFMDLFDNFYSDKEKTKGAWVVSFYAIMALAVSRSKRKDKEKISKSLFSTSWFLVQKPGFFLTARLDKIQALTIMIQFCAHLSLYNLCKVLCGQMCLMVKDLDLHKEATNPNVDIEVDELNRRVFWTCYIFETTTSLIFGTPPELGDLEIDCQLPSMDVLPRFTESSQGGIVFCSEIQLTIIKNEIRKKIYKCLASASEEVYKEAVLSIRGKLIVWERNLPDELKQYYDVIKLNGTIPKNVDFENQHIFTACVEIYLSYCITQLYFYDPLTNYETCLEIARKAADAIRSYFMVIEPIFKKICYLWLFLYCPFTPFQILFSNILKMEKGTSDEKIEDLDRMYSLYRFFVEMKEINGEFADKLSRVALDCIDAAEHYLELKSSVGSNIFELESLLV 594 O94573 Uncharacterized transcriptional regulatory protein C1773.16c SPBC1773 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. UNIPROT O94573 Pfam PF04082 Pfam PF00172 PROSITE PS00463 PROSITE PS50048 DE Reference Proteome: Yes; GO:0016021 GO:0000228 GO:0031965 GO:0005634 GO:0000981 GO:0000978 GO:0008270 GO:0006357 GO:0006351 MKRIRNACELCRRKKLRCNGELTCQNCMVYGEECRYVKRVKHDNRAAVQENERYPILYTPLSTSDHDNDEENEINELKNAVKALDKRFDNFELKLEALFSLLRSQQDSERKVKPGGFPSLVSQILSAGALVDSKLQAYTMRTNFFSNGFSSNDLFPHSFPTWKSAFRDVPDKDWAKTCLDWYFRFINCNWPIFYKKQYMESFEKLYIDKNLVKGAWIVSFYAILALAVSRDKRVDNSKLAESFFATSWFLIQRPGFFLTPQLEKIQALVIMIQFASHLSLYNLCKKLCGQVCLMVKDLNLHKESTDKDLDQDMAELHRRIFWVCYIFETTTSLIFGTPPVLGDLEIECKYPDINYAHCFAENVQGDLIFTCEISLTVLKHEIRTKLYNSNNVFLDKGQKGVISNIQTKILNFERAIPSEMKHYFEILKAGNGLPEELDIIKQHFFTACVEIYLSYCNTLIYLYLADDSIEGSKICLSTARAAIDVIKGFLVVLDPISKNICYLWLFLYCPFTPFLTVFSHLLEDDDLDADICVKDVDRLYSIHAFFLKMKDISGEFAERLSVITENFIQSAEQYLALQNTSVFGTFDALSESFSI 595 O94652 Nucleoporin gle1 gle1 284812 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT O94652 Pfam PF07817 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}. Q09847 EBI-21243842,EBI-21243819 GO:0005737 GO:0005829 GO:0005635 GO:0031965 GO:0034399 GO:0005643 GO:0044614 GO:0005634 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0006446 GO:0006449 MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWAKKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKHKENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFARLQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQLMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP 480 O94756 Meiotic expression up-regulated protein 14 meu14 284812 Yes SL-0178 SL-0182 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}. UNIPROT O94756 Pfam PF13805 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}. GO:0036286 GO:0035974 GO:0031965 GO:0005886 GO:0070056 GO:0070057 GO:0008289 GO:0031322 GO:0070941 GO:0006897 GO:0140043 GO:0006469 MPKSSNLKMQRKGSLRENGLVKGLNKNKFSISKLKELSHADDSRKSHRIIRSGKSSGEAYKQAGKGLMNLGNHLSDWGAKSSNLSLNDISDKIGVLVSELGETEIEFVKAFNENRIKFKAIRAMEDSIAPSRAHRQRLISSIEREEERDPLSPKLTDLQNQLVRTEAENLVGEMQLDNTSREVFKSSFQGLMDAFQLRAQKQMTLSYYASQLAELINDEVAYPGDNPAAYSQKYATQIMHQCVESMARLLAPVTSETTEHVGSDCEFTRKSSSSVEFSDHSQDSGDPSQQNILQVKNVQAVLSIPEAESYKAQLLSSIAEEQKKKELQAKSTVFL 335 O94901 SUN domain-containing protein 1 SUN1 9606 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT O94901 UNIPROT A5PL20 UNIPROT B3KMV7 UNIPROT B4DZF7 UNIPROT B7WNY4 UNIPROT B7WP53 UNIPROT E9PDU4 UNIPROT E9PF23 UNIPROT F8WD13 UNIPROT Q96CZ7 UNIPROT Q9HA14 UNIPROT Q9UH98 Pfam PF09387 Pfam PF07738 Pfam PF18580 PROSITE PS51469 OMIM 607723 DisGeNET 23353 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}. Self EBI-2796904,EBI-2796904 Q5NFR9 EBI-2796367,EBI-2796904 Q6NUS6 EBI-11278332,EBI-2796904 Q8N6G5 EBI-10267100,EBI-2796904 P04578 EBI-6163496,EBI-2796904 Q8NF91 EBI-928867,EBI-2796904 Q8WXH0 EBI-2372294,EBI-2796904 Q8WXH0-1 EBI-6170976,EBI-2796904 Q8NF91-1 EBI-6170938,EBI-2796904 P50402 EBI-489887,EBI-2796904 P02545 EBI-2796904,EBI-351935 Q9P0N5 EBI-721260,EBI-2796904 Q401N2 EBI-21749821,EBI-2796904 Q86UE6 EBI-9028422,EBI-2796904 P16444 EBI-749514,EBI-2796904 Q9Y6Q1 EBI-7183095,EBI-2796904 Q8TCN5 EBI-2796904,EBI-9661677 Q15654 EBI-2796904,EBI-742327 A2RUC4 EBI-2796904,EBI-21511702 Q8WWF5 EBI-2129267,EBI-2796904 Q9BQ31 EBI-6426177,EBI-2796904 Q6AZY7-2 EBI-21598366,EBI-2796904 Q9NVF7 EBI-740282,EBI-2796904 Q53F39-2 EBI-21694292,EBI-2796904 GO:0005623 GO:0005737 GO:0005639 GO:0043231 GO:0034993 GO:0005635 GO:0031965 GO:0005521 GO:0043495 GO:0051642 GO:0090286 GO:0070197 GO:0006998 GO:0090292 GO:0021817 GO:0001503 GO:0009612 GO:0007283 GO:0007129 MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCDDCKGKRHLDAHPGRAGTLWHIWACAGYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK 812 O94972 E3 ubiquitin-protein ligase TRIM37 TRIM37 9606 Yes SL-0198 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}. UNIPROT O94972 UNIPROT A8K0V9 UNIPROT A8K8U4 UNIPROT A8MZ79 UNIPROT B4DGZ3 UNIPROT F8WEE6 UNIPROT Q7Z3E6 UNIPROT Q8IYF7 UNIPROT Q8WYF7 PDB 3LRQ Pfam PF00917 Pfam PF00643 PROSITE PS50144 PROSITE PS50119 PROSITE PS50089 OMIM 253250 OMIM 605073 DisGeNET 4591 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}.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. Q7Z2E3 EBI-741602,EBI-847814 Q5VVX9 EBI-2130181,EBI-741602 Q9H5Z6 EBI-741626,EBI-741602 Q7L590 EBI-374912,EBI-741602 O43663 EBI-741602,EBI-741137 Q8N5R6 EBI-740841,EBI-741602 P62256 EBI-2129909,EBI-741602 P54764-2 EBI-741602,EBI-21371515 Q9NRI5 EBI-741602,EBI-529989 A8K932 EBI-741602,EBI-10174671 Q2TBE0 EBI-741602,EBI-5453285 P57075 EBI-2105393,EBI-741602 Q7TSJ6 EBI-6305003,EBI-741602 Q86UD4 EBI-7233259,EBI-741602 Q86Y33 EBI-741602,EBI-10260504 Q8TAU3 EBI-740727,EBI-741602 Q96NC0 EBI-2682299,EBI-741602 Q9BWG6 EBI-741602,EBI-748391 Q92993 EBI-741602,EBI-399080 Q96EZ8 EBI-348259,EBI-741602 Q13895 EBI-741602,EBI-358049 P26196 EBI-351257,EBI-741602 P32969 EBI-741602,EBI-358122 O95990-3 EBI-10192902,EBI-741602 Q3B820 EBI-719941,EBI-741602 Q9Y247 EBI-742802,EBI-741602 Q9Y272 EBI-740818,EBI-741602 Q9Y2D8 EBI-2212028,EBI-741602 Q96SN8 EBI-741602,EBI-308374 X5D778 EBI-741602,EBI-17183751 X5DP31 EBI-741602,EBI-21247516 Q68CZ1 EBI-5235485,EBI-741602 Q6ZU80 EBI-2873150,EBI-741602 Q96T60 EBI-741602,EBI-1045072 P08238 EBI-741602,EBI-352572 P58526 EBI-2851618,EBI-741602 Q96M61 EBI-741835,EBI-741602 Q8IYF1 EBI-741705,EBI-741602 Q9UBZ4 EBI-742588,EBI-741602 P51116 EBI-740459,EBI-741602 O95990 EBI-743396,EBI-741602 Q6ZVK8 EBI-740486,EBI-741602 Q96KB5 EBI-536853,EBI-741602 P53618 EBI-741602,EBI-359063 Q6ZU52 EBI-739493,EBI-741602 Q01844 EBI-741602,EBI-739737 Q9H4K1 EBI-740128,EBI-741602 Q8TCX5 EBI-746325,EBI-741602 Q8N720 EBI-625509,EBI-741602 Q15398 EBI-748280,EBI-741602 P07305 EBI-725224,EBI-741602 Q8IVW4 EBI-741602,EBI-3919850 O43167 EBI-741602,EBI-744471 Q8N8B7-2 EBI-741602,EBI-11955057 P29972 EBI-741602,EBI-745213 P28702-3 EBI-741602,EBI-16429492 A0A0S2Z4G9 EBI-741602,EBI-16428950 A0A0S2Z4M1 EBI-741602,EBI-16429430 Q8IYY4 EBI-741602,EBI-10264440 Q96SQ5 EBI-6427977,EBI-741602 O60941-5 EBI-741602,EBI-11984733 O00311 EBI-741602,EBI-374980 Q96C24 EBI-741602,EBI-747142 Q14241 EBI-741602,EBI-742350 Q86Y33-5 EBI-741602,EBI-11983537 O15169 EBI-741602,EBI-710484 Q6P5F9 EBI-2550236,EBI-741602 Q8N0Z3 EBI-2361917,EBI-741602 Q8N137 EBI-947360,EBI-741602 Q96KN7 EBI-1050213,EBI-741602 Q96MT8 EBI-741977,EBI-741602 Q96ST8 EBI-2799206,EBI-741602 P39009 EBI-741602,EBI-6194 Q12417 EBI-741602,EBI-710 P32571 EBI-741602,EBI-19840 GO:0016235 GO:0005737 GO:0005829 GO:0048471 GO:0005777 GO:0003682 GO:0042803 GO:0005164 GO:0061630 GO:0031625 GO:0004842 GO:0008270 GO:0070842 GO:0035518 GO:0036353 GO:0046600 GO:0032088 GO:0000122 GO:0051091 GO:0051092 GO:0051865 MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR 964 O95248 Myotubularin-related protein 5 SBF1 9606 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12668758}. UNIPROT O95248 UNIPROT A0A024R4Z9 UNIPROT A6PVG9 UNIPROT G5E933 UNIPROT O60228 UNIPROT Q5JXD8 UNIPROT Q5PPM2 UNIPROT Q96GR9 UNIPROT Q9UGB8 Pfam PF02141 Pfam PF02893 Pfam PF06602 Pfam PF00169 Pfam PF12335 Pfam PF03456 PROSITE PS50211 PROSITE PS50003 PROSITE PS51339 OMIM 603560 OMIM 615284 DisGeNET 6305 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}.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. Q9NTG7 EBI-724621,EBI-2322878 P03372 EBI-78473,EBI-2322878 P04792 EBI-352682,EBI-2322878 P11279 EBI-2805407,EBI-2322878 Q7CJU1 EBI-2322878,EBI-2855448 GO:0005737 GO:0005829 GO:0005789 GO:0016021 GO:0016604 GO:0048471 GO:0019208 GO:0008138 GO:0017112 GO:0006661 GO:0006470 GO:0043087 GO:0007283 MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYCACLTFWEPAEPSQQETTRVEDATEREEEGDEGGQTHLSPTAPAPSAQLFAPKTLVLVSRLDHTEVFRNSLGLIYAIHVEGLNVCLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLADSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFLSRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTIPECVHIPPLPEPLQSQTHSVLSMVLDPELELADLAFPPPTTSTSSLKMQDKELRAVFLRLFAQLLQGYRWCLHVVRIHPEPVIRFHKAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRPTDLFDELVAHEVARMRADENHPQRVLRHVQELAEQLYKNENPYPAVAMHKVQRPGESSHLRRVPRPFPRLDEGTVQWIVDQAAAKMQGAPPAVKAERRTTVPSGPPMTAILERCSGLHVNSARRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAQELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLDEHGIAAALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPTEDLAPAQEVGEAPSQEDERSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNSMAGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVQRESRRLPPIQKPKLLRPRLLPGEECVLDGLRVYLLPDGREEGAGGSAGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVAALTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSAHTPGRPPRVTKDKGPSLRTLSRNLVKNAKKTIGRQHVTRKKYNPPSWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMSSLVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSVQDNALQRVSRCYRQNRFPVVCWRSGRSKAVLLRSGGLHGKGVVGLFKAQNAPSPGQSQADSSSLEQEKYLQAVVSSMPRYADASGRNTLSGFSSAHMGSHGKWGSVRTSGRSSGLGTDVGSRLAGRDALAPPQANGGPPDPGFLRPQRAALYILGDKAQLKGVRSDPLQQWELVPIEVFEARQVKASFKKLLKACVPGCPAAEPSPASFLRSLEDSEWLIQIHKLLQVSVLVVELLDSGSSVLVGLEDGWDITTQVVSLVQLLSDPFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHVSRRFRTFLLDSDYERIELGLLYEEKGERRGQVPCRSVWEYVDRLSKRTPVFHNYMYAPEDAEVLRPYSNVSNLKVWDFYTEETLAEGPPYDWELAQGPPEPPEEERSDGGAPQSRRRVVWPCYDSCPRAQPDAISRLLEELQRLETELGQPAERWKDTWDRVKAAQRLEGRPDGRGTPSSLLVSTAPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSGSRQAARRSTSTLYSQFQTAESENRSYEGTLYKKGAFMKPWKARWFVLDKTKHQLRYYDHRVDTECKGVIDLAEVEAVAPGTPTMGAPKTVDEKAFFDVKTTRRVYNFCAQDVPSAQQWVDRIQSCLSDA 1868 O95259 Potassium voltage-gated channel subfamily H member 1 KCNH1 9606 Yes SL-0178 SL-0179 SL-0182 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. UNIPROT O95259 UNIPROT B1AQ26 UNIPROT O76035 UNIPROT Q14CL3 PDB 5J7E Pfam PF00027 Pfam PF00520 Pfam PF13426 PROSITE PS50042 PROSITE PS50113 PROSITE PS50112 OMIM 135500 OMIM 603305 OMIM 611816 DisGeNET 3756 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}.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. O00560 EBI-727004,EBI-2909270 Q7L8L6 EBI-747570,EBI-2909270 Q96HA8 EBI-741158,EBI-2909270 GO:0030673 GO:0030054 GO:0009986 GO:0030425 GO:0031901 GO:0005887 GO:0099056 GO:0043231 GO:0005637 GO:0043204 GO:0048471 GO:0005886 GO:0098839 GO:0008076 GO:0071889 GO:0005516 GO:0005251 GO:0042802 GO:0044325 GO:1902936 GO:0019901 GO:0044877 GO:0005249 GO:0071277 GO:0007520 GO:0048015 GO:0071805 GO:0006813 GO:0042127 GO:0034765 GO:0042391 GO:0001964 MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS 989 O95271 Poly [ADP-ribose] polymerase tankyrase-1 TNKS 9606 Yes SL-0178 SL-0185 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}. UNIPROT O95271 UNIPROT O95272 UNIPROT Q4G0F2 PDB 2RF5 PDB 3UDD PDB 3UH2 PDB 3UH4 PDB 4DVI PDB 4I9I PDB 4K4E PDB 4K4F PDB 4KRS PDB 4LI6 PDB 4LI7 PDB 4LI8 PDB 4MSG PDB 4MSK PDB 4MT9 PDB 4N3R PDB 4N4V PDB 4OA7 PDB 4TOR PDB 4TOS PDB 4U6A PDB 4UUH PDB 4UW1 PDB 4W5S PDB 4W6E PDB 5EBT PDB 5ECE PDB 5ETY PDB 5GP7 PDB 5JHQ PDB 5JTI PDB 5JU5 PDB 5KNI PDB 6QXU Pfam PF00023 Pfam PF12796 Pfam PF13606 Pfam PF00644 Pfam PF07647 PROSITE PS50297 PROSITE PS50088 PROSITE PS51059 PROSITE PS50105 OMIM 603303 DisGeNET 8658 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}. O60239 EBI-1105254,EBI-624860 Q9NRI5 EBI-1105254,EBI-529989 P21709 EBI-1105254,EBI-968453 Q9NWT6 EBI-745632,EBI-1105254 P62826 EBI-1105254,EBI-286642 Q9NWV8 EBI-745725,EBI-1105254 O95235 EBI-2551319,EBI-1105254 Q3UES3 EBI-11025893,EBI-1105254 P80314 EBI-772351,EBI-1105254 P54274 EBI-710997,EBI-1105254 O60232 EBI-741415,EBI-1105254 Q96A37 EBI-2130320,EBI-1105254 Q9H201-2 EBI-21644004,EBI-1105254 Q5SW79 EBI-1104799,EBI-1105254 Q9BS91 EBI-18915901,EBI-1105254 Q8N6W0 EBI-12139335,EBI-1105254 Q7L775 EBI-6255981,EBI-1105254 Q06649 EBI-1105254,EBI-5323518 O15084 EBI-359567,EBI-1105254 A0A384L0P2 EBI-1105254,EBI-2841116 Q8TER5-1 EBI-25399492,EBI-1105254 Q86WJ1-2 EBI-21569730,EBI-1105254 P54274-2 EBI-711018,EBI-1105254 O75298-3 EBI-21508625,EBI-1105254 O60547 EBI-746373,EBI-1105254 P12956 EBI-353208,EBI-1105254 P56279 EBI-1105254,EBI-749995 O00560 EBI-1105254,EBI-727004 Q9Y530 EBI-8502288,EBI-1105254 Q9NX46 EBI-1105254,EBI-718580 Q8TF42 EBI-1105254,EBI-1380492 Q6P5F9 EBI-2550236,EBI-1105254 O75367-2 EBI-1105254,EBI-6249599 O75367 EBI-1105254,EBI-2868511 A4D1S0 EBI-21511322,EBI-1105254 Q96CW1-2 EBI-10965256,EBI-1105254 Q9H2G9 EBI-2548012,EBI-1105254 Q9BSI4-2 EBI-11057768,EBI-1105254 Q7L8J4 EBI-747389,EBI-1105254 Q2T9K0-6 EBI-21768440,EBI-1105254 Q07954 EBI-1046087,EBI-1105254 Q6P1L5 EBI-3893327,EBI-1105254 Q9UPT6 EBI-717887,EBI-1105254 GO:0000781 GO:0005737 GO:0005829 GO:0005794 GO:0000139 GO:0097431 GO:0016604 GO:0000784 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0000242 GO:0042393 GO:0003950 GO:1990404 GO:0008270 GO:0051301 GO:0031670 GO:0007052 GO:0051028 GO:1904908 GO:1904357 GO:1904743 GO:0018105 GO:0018107 GO:0090263 GO:0051973 GO:1904355 GO:0032212 GO:0045944 GO:0006471 GO:0070213 GO:0070198 GO:0070212 GO:0000209 GO:0015031 GO:0032210 GO:0051225 GO:0016055 MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT 1327 O95295 SNARE-associated protein Snapin SNAPIN 9606 Yes SL-0198 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}. UNIPROT O95295 UNIPROT D3DV56 UNIPROT Q5SXU8 Pfam PF14712 OMIM 607007 DisGeNET 23557 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}. A1L4K1 EBI-5661036,EBI-296723 Q16539 EBI-73946,EBI-296723 Q15849-1 EBI-1633392,EBI-296723 Q62668-1 EBI-1635608,EBI-296723 Q08850 EBI-296723,EBI-918243 O70377 EBI-296723,EBI-1573765 Q62668 EBI-296723,EBI-1573598 Q9NV70 EBI-296723,EBI-1045313 Q5S007 EBI-296723,EBI-5323863 P60881 EBI-1027214,EBI-296723 Q9D0F1 EBI-309872,EBI-296723 Q96L14 EBI-743488,EBI-296723 Q6A065 EBI-2554140,EBI-296723 H7BX26 EBI-11022011,EBI-296723 P51151 EBI-4401353,EBI-296723 O43493 EBI-1752146,EBI-296723 Q8TDR4 EBI-3923210,EBI-296723 Q5SW79 EBI-1104799,EBI-296723 A5D8V7 EBI-8466445,EBI-296723 Q8N7C3 EBI-11059915,EBI-296723 O60296 EBI-2851680,EBI-296723 Q99816 EBI-346882,EBI-296723 Q9UPT5-1 EBI-6251402,EBI-296723 P78537 EBI-348630,EBI-296723 Q2M2I5 EBI-2952736,EBI-296723 Q96EV8 EBI-465804,EBI-296723 Q5JTB6 EBI-3923605,EBI-296723 Q6QNY1 EBI-465872,EBI-296723 P35609 EBI-296723,EBI-77797 P05023 EBI-296723,EBI-358778 O00499 EBI-719094,EBI-296723 Q5VT25 EBI-296723,EBI-689171 Q8N3K9 EBI-2323272,EBI-296723 P17661 EBI-1055572,EBI-296723 P50570 EBI-346547,EBI-296723 Q03001 EBI-296723,EBI-310758 Q8IWE2 EBI-296723,EBI-2686288 Q9H6L5 EBI-5664372,EBI-296723 O95163 EBI-296723,EBI-347559 Q14974 EBI-286758,EBI-296723 Q04695 EBI-296723,EBI-297873 P24043 EBI-2529730,EBI-296723 P11047 EBI-296723,EBI-714904 Q9UPN3-5 EBI-6131019,EBI-296723 Q7Z406 EBI-296723,EBI-355595 P11055 EBI-296723,EBI-5654298 P12883 EBI-519141,EBI-296723 Q14511 EBI-2108053,EBI-296723 Q15149 EBI-297903,EBI-296723 Q15276 EBI-447043,EBI-296723 Q9UJ41 EBI-913954,EBI-296723 Q96Q15 EBI-296723,EBI-1049832 P11277 EBI-514908,EBI-296723 Q01082 EBI-296723,EBI-351561 O94826 EBI-2800236,EBI-296723 P09493 EBI-296723,EBI-351158 P07951 EBI-296723,EBI-352633 Q969Q1 EBI-5661333,EBI-296723 P62258 EBI-296723,EBI-356498 P63104 EBI-347088,EBI-296723 O75923 EBI-296723,EBI-2799016 Q9BZ29 EBI-2695893,EBI-296723 P13929 EBI-4287222,EBI-296723 Q9UL45 EBI-465781,EBI-296723 Q7Z465 EBI-3942634,EBI-296723 Q8CZZ7 EBI-296723,EBI-2842831 Q96AW1 EBI-715058,EBI-296723 O60282 EBI-717170,EBI-296723 Q96R06 EBI-413317,EBI-296723 Q9Y561 EBI-296693,EBI-296723 Q5T0J7-2 EBI-12833746,EBI-296723 Q70UQ0-4 EBI-12190633,EBI-296723 Q8TDM0-3 EBI-13025473,EBI-296723 Q9UBB9 EBI-1105213,EBI-296723 P08779 EBI-356410,EBI-296723 Q9NYB9-2 EBI-296723,EBI-11096309 P67936 EBI-296723,EBI-1642100 P35900 EBI-296723,EBI-742094 Q13515 EBI-296723,EBI-10229433 Q68D86 EBI-296723,EBI-10171570 Q7Z6G3-2 EBI-296723,EBI-10172876 P49585 EBI-296723,EBI-2563309 Q8N9N5-2 EBI-296723,EBI-11524452 P20700 EBI-296723,EBI-968218 Q8IV53 EBI-296723,EBI-2871584 P06753 EBI-296723,EBI-355607 Q7Z3Y9 EBI-296723,EBI-12084444 Q9UJ41-4 EBI-296723,EBI-14093916 P51946 EBI-296723,EBI-741406 P08727 EBI-742756,EBI-296723 Q96BD8 EBI-296723,EBI-741854 P07951-2 EBI-296723,EBI-10977815 A1L168 EBI-18396958,EBI-296723 Q9Y5B8 EBI-296723,EBI-744782 Q8IYW4 EBI-296723,EBI-20842218 Q2T9L4 EBI-4311436,EBI-296723 Q7Z3Y8 EBI-3044087,EBI-296723 P19012 EBI-739566,EBI-296723 Q96NL6 EBI-2514016,EBI-296723 P48039 EBI-296723,EBI-1188238 Q12934-2 EBI-296723,EBI-12123320 Q9Y3C0 EBI-296723,EBI-712969 Q63ZY3 EBI-296723,EBI-2556193 Q9H1M0 EBI-296723,EBI-751933 Q96EV8-2 EBI-16749183,EBI-296723 Q86WT6-2 EBI-11525489,EBI-296723 Q9UIL1-2 EBI-21638756,EBI-296723 Q9NX95-3 EBI-21651984,EBI-296723 Q07866-2 EBI-11979975,EBI-296723 Q8WVE6 EBI-10264837,EBI-296723 Q96GS4 EBI-10193358,EBI-296723 Q9NV70-2 EBI-10961687,EBI-296723 Q9Y2V7 EBI-3866319,EBI-296723 Q9UJT2 EBI-852101,EBI-296723 Q08345 EBI-296723,EBI-711879 P26641 EBI-351467,EBI-296723 P54257 EBI-712814,EBI-296723 Q92993 EBI-399080,EBI-296723 Q16891 EBI-473801,EBI-296723 O95251 EBI-473199,EBI-296723 Q9NUP1 EBI-296723,EBI-465852 Q6QNY0 EBI-465930,EBI-296723 GO:1904115 GO:0031083 GO:0099078 GO:0005623 GO:0030054 GO:0000139 GO:0005765 GO:0048471 GO:0030141 GO:0045202 GO:0008021 GO:0030672 GO:0000149 GO:0008089 GO:0048490 GO:0097352 GO:0034629 GO:0008333 GO:0006886 GO:1902774 GO:0007042 GO:0032418 GO:0007040 GO:0032438 GO:0010977 GO:0031175 GO:0007269 GO:1902824 GO:0051604 GO:0043393 GO:2000300 GO:0008090 GO:0016079 GO:0031629 GO:0016188 GO:0048489 GO:0072553 GO:0016032 MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK 136 O95528 Solute carrier family 2, facilitated glucose transporter member 10 SLC2A10 9606 Yes SL-0198 Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}. UNIPROT O95528 UNIPROT A8K4J6 UNIPROT Q3MIX5 UNIPROT Q9H4I6 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 OMIM 208050 OMIM 606145 DisGeNET 81031 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:11592815, ECO:0000269|PubMed:16550171}.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. GO:0012505 GO:0016021 GO:0005887 GO:0048471 GO:0005886 GO:0005351 GO:0046323 GO:1904659 GO:0008645 MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFAVPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPLPARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFLLYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS 541 O95831 Apoptosis-inducing factor 1, mitochondrial AIFM1 9606 Yes SL-0198 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}. UNIPROT O95831 UNIPROT A4QPB4 UNIPROT B1ALN1 UNIPROT B2RB08 UNIPROT D3DTE9 UNIPROT Q1L6K4 UNIPROT Q1L6K6 UNIPROT Q2QKE4 UNIPROT Q5JUZ7 UNIPROT Q6I9X6 UNIPROT Q9Y3I3 UNIPROT Q9Y3I4 PDB 1M6I PDB 4BUR PDB 4BV6 PDB 4FDC PDB 4LII PDB 5FMH PDB 5FS6 PDB 5FS7 PDB 5FS8 PDB 5FS9 PDB 5KVH PDB 5KVI Pfam PF14721 Pfam PF07992 OMIM 300169 OMIM 300614 OMIM 300816 OMIM 310490 DisGeNET 9131 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}.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. A0A142I5B9 EBI-20625235,EBI-356440 O00165 EBI-356440,EBI-357001 O15027 EBI-356440,EBI-357515 O43715 EBI-356440,EBI-2820212 Q9Y3Q8 EBI-739485,EBI-356440 P13569 EBI-349854,EBI-356440 Q5S007 EBI-5323863,EBI-356440 P09622 EBI-353366,EBI-356440 P08559 EBI-715747,EBI-356440 P35610 EBI-6621955,EBI-356440 O43615 EBI-356440,EBI-861737 Q8IXI1 EBI-356440,EBI-1396563 Q7Z434 EBI-356440,EBI-995373 P00403 EBI-356440,EBI-2105756 Q6UXV4 EBI-356440,EBI-9641073 O75431 EBI-356440,EBI-7415268 Q9Y3D9 EBI-356440,EBI-1054270 Q9NVH1 EBI-356440,EBI-1055336 Q9BYN8 EBI-356440,EBI-721378 Q99618 EBI-356440,EBI-739534 Q96EY7 EBI-356440,EBI-721110 Q8N4Q1 EBI-356440,EBI-2562213 Q5JTV8 EBI-356440,EBI-2559665 Q16891 EBI-356440,EBI-473801 Q16775 EBI-356440,EBI-3905342 Q15773 EBI-356440,EBI-1051875 Q13011 EBI-356440,EBI-711968 Q02952 EBI-356440,EBI-2562430 P82650 EBI-356440,EBI-1050752 P50454 EBI-356440,EBI-350723 P36542 EBI-356440,EBI-711768 P31689 EBI-356440,EBI-347834 P18085 EBI-356440,EBI-1237085 P16615 EBI-356440,EBI-358933 P13804 EBI-356440,EBI-1052886 O95721 EBI-356440,EBI-490676 O76031 EBI-356440,EBI-1052667 O75683 EBI-356440,EBI-2691252 A8MXV4 EBI-356440,EBI-11350801 Q9Y5L4 EBI-356440,EBI-1057344 Q9Y5J9 EBI-356440,EBI-1049085 Q9Y512 EBI-356440,EBI-748409 Q9Y4W6 EBI-356440,EBI-358755 Q9Y2W6 EBI-356440,EBI-12842466 Q9Y2S7 EBI-356440,EBI-713000 Q9Y2Q9 EBI-356440,EBI-5325249 Q9ULX6 EBI-356440,EBI-357530 Q9UJS0 EBI-356440,EBI-1222503 Q9P0J0 EBI-356440,EBI-372742 Q9P032 EBI-356440,EBI-2606839 Q9NX63 EBI-356440,EBI-743375 Q9NX40 EBI-356440,EBI-2683029 Q9NX14 EBI-356440,EBI-1246182 Q9NVI7 EBI-356440,EBI-352007 Q9NSE4 EBI-356440,EBI-1054770 Q9NS69 EBI-356440,EBI-1047508 Q9NPL8 EBI-356440,EBI-6268651 Q9H845 EBI-356440,EBI-2510719 Q9H078 EBI-356440,EBI-2107221 Q9BW72 EBI-356440,EBI-2867844 Q9BSH4 EBI-356440,EBI-747797 Q9BPX6 EBI-356440,EBI-2371996 Q99714 EBI-356440,EBI-79964 Q96TA2 EBI-356440,EBI-2818916 Q96EX1 EBI-356440,EBI-2874543 Q96EL2 EBI-356440,EBI-1055789 Q96E52 EBI-356440,EBI-6570817 Q96C36 EBI-356440,EBI-358366 Q96C01 EBI-356440,EBI-373319 Q96BR5 EBI-356440,EBI-6269632 Q96A73 EBI-356440,EBI-725897 Q92667 EBI-356440,EBI-2119593 Q92665 EBI-356440,EBI-720602 Q8IYU8 EBI-356440,EBI-3197790 Q8IUX1 EBI-356440,EBI-2800657 Q86TX2 EBI-356440,EBI-11109648 Q7L0Y3 EBI-356440,EBI-2107046 Q7KZN9 EBI-356440,EBI-3248549 Q70CQ3 EBI-356440,EBI-2512374 Q6UB35 EBI-356440,EBI-1046835 Q6KCM7 EBI-356440,EBI-11289059 Q6DKK2 EBI-356440,EBI-948354 Q5TC12 EBI-356440,EBI-1166891 Q5T9A4 EBI-356440,EBI-1384144 Q5JTJ3 EBI-356440,EBI-2874677 Q4VC31 EBI-356440,EBI-1051617 Q49B96 EBI-356440,EBI-16768453 Q3ZCQ8 EBI-356440,EBI-355175 Q16795 EBI-356440,EBI-1045087 Q16740 EBI-356440,EBI-1056029 Q16718 EBI-356440,EBI-746417 Q14249 EBI-356440,EBI-9369928 Q14061 EBI-356440,EBI-711311 Q12849 EBI-356440,EBI-1054150 Q04837 EBI-356440,EBI-353460 P99999 EBI-356440,EBI-446479 P83111 EBI-356440,EBI-2878119 P62072 EBI-356440,EBI-1200391 P61088 EBI-356440,EBI-1052908 P56381 EBI-356440,EBI-3904845 P56277 EBI-356440,EBI-746397 P55789 EBI-356440,EBI-718281 P54819 EBI-356440,EBI-1056291 P53701 EBI-356440,EBI-10763431 P51970 EBI-356440,EBI-1237250 P49821 EBI-356440,EBI-748312 P49753 EBI-356440,EBI-1052865 P48047 EBI-356440,EBI-355815 P46199 EBI-356440,EBI-359432 P38117 EBI-356440,EBI-1056543 P36957 EBI-356440,EBI-351007 P36551 EBI-356440,EBI-3907775 P35232 EBI-356440,EBI-354213 P34897 EBI-356440,EBI-352908 P32322 EBI-356440,EBI-848624 P31930 EBI-356440,EBI-1052596 P31040 EBI-356440,EBI-1057265 P30405 EBI-356440,EBI-5544229 P28331 EBI-356440,EBI-1043922 P25705 EBI-356440,EBI-351437 P24539 EBI-356440,EBI-1044810 P22695 EBI-356440,EBI-1051424 P20674 EBI-356440,EBI-715032 P19404 EBI-356440,EBI-713665 P19367 EBI-356440,EBI-713162 P18859 EBI-356440,EBI-2606700 P14854 EBI-356440,EBI-1047480 P13073 EBI-356440,EBI-1056574 P10606 EBI-356440,EBI-1053725 P10599 EBI-356440,EBI-594644 P09669 EBI-356440,EBI-715040 P08574 EBI-356440,EBI-1224514 P07919 EBI-356440,EBI-1224427 P06576 EBI-356440,EBI-356231 P05023 EBI-356440,EBI-358778 P00367 EBI-356440,EBI-356544 O96008 EBI-356440,EBI-1057581 O96000 EBI-356440,EBI-1246371 O95202 EBI-356440,EBI-1052895 O94925 EBI-356440,EBI-1043737 O94826 EBI-356440,EBI-2800236 O75964 EBI-356440,EBI-1044001 O75947 EBI-356440,EBI-724024 O75746 EBI-356440,EBI-1047585 O75616 EBI-356440,EBI-6393536 O75489 EBI-356440,EBI-1224896 O75380 EBI-356440,EBI-719854 O75306 EBI-356440,EBI-1224806 O60313 EBI-356440,EBI-1054131 O60220 EBI-356440,EBI-1049822 O43920 EBI-356440,EBI-1246091 O43819 EBI-356440,EBI-357012 O43464 EBI-356440,EBI-517086 O00429 EBI-356440,EBI-724571 O00217 EBI-356440,EBI-1246309 Q69YU5 EBI-356440,EBI-16768469 F5H1C8 EBI-21259559,EBI-356440 Q9H1C4 EBI-4401271,EBI-356440 Q9BZR8 EBI-1385773,EBI-356440 Q8IY21 EBI-2807346,EBI-356440 Q96KQ7 EBI-744366,EBI-356440 P21860 EBI-720706,EBI-356440 O75807 EBI-714746,EBI-356440 Q96JM2 EBI-1210359,EBI-356440 P57078 EBI-4422308,EBI-356440 Q96DB2 EBI-301713,EBI-356440 Q9H492 EBI-720768,EBI-356440 P40692 EBI-744248,EBI-356440 O95166 EBI-712001,EBI-356440 Q9H0R8 EBI-746969,EBI-356440 Q8N0X7 EBI-2643803,EBI-356440 P03372 EBI-78473,EBI-356440 P16104 EBI-494830,EBI-356440 P83887 EBI-2553410,EBI-356440 Q9GZQ8 EBI-373144,EBI-356440 Q96NL6 EBI-2514016,EBI-356440 P10398 EBI-365961,EBI-356440 Q13418 EBI-747644,EBI-356440 P51617 EBI-358664,EBI-356440 Q96FW1 EBI-1058491,EBI-356440 Q02539 EBI-356440,EBI-932603 P53004 EBI-356440,EBI-7410441 Q9HAV7 EBI-356440,EBI-1043499 Q9H0I3 EBI-356440,EBI-715690 Q92522 EBI-356440,EBI-876335 P83881 EBI-356440,EBI-1054835 P61604 EBI-356440,EBI-711483 P27694 EBI-356440,EBI-621389 P35244 EBI-356440,EBI-621428 P15927 EBI-356440,EBI-621404 Q9UHB6 EBI-356440,EBI-351479 Q9BSD7 EBI-356440,EBI-2689235 Q96HS1 EBI-356440,EBI-713608 Q6PI48 EBI-356440,EBI-3917045 Q10713 EBI-356440,EBI-2514696 P49411 EBI-356440,EBI-359097 P18887 EBI-356440,EBI-947466 P0DMV8 EBI-356440,EBI-11052499 P00374 EBI-356440,EBI-10039315 O43813 EBI-356440,EBI-3046631 P45880 EBI-356440,EBI-354022 O95831-1 EBI-5456281,EBI-356440 O95831-3 EBI-5651213,EBI-356440 P0DOE9 EBI-6138585,EBI-356440 Q8JPQ9 EBI-6152703,EBI-356440 Q13617 EBI-456179,EBI-356440 Q13616 EBI-359390,EBI-356440 Q93034 EBI-1057139,EBI-356440 Q92905 EBI-594661,EBI-356440 Q86VP6 EBI-456077,EBI-356440 Q13618 EBI-456129,EBI-356440 O95747 EBI-620853,EBI-356440 Q77M19 EBI-6149376,EBI-356440 Q15047 EBI-79691,EBI-356440 O76061 EBI-713858,EBI-356440 Q92956 EBI-356440,EBI-1056653 Q9BUV8 EBI-356440,EBI-1050079 P01889 EBI-356440,EBI-1046513 Q9HAW0 EBI-356440,EBI-1055224 Q9BRX2 EBI-356440,EBI-1043580 O75365 EBI-356440,EBI-1043866 Q8NC60 EBI-717871,EBI-356440 Q8IX03 EBI-715828,EBI-356440 Q13547 EBI-301834,EBI-356440 Q05513 EBI-295351,EBI-356440 Q13322 EBI-80275,EBI-356440 Q13153 EBI-1307,EBI-356440 P05129 EBI-949799,EBI-356440 P04049 EBI-365996,EBI-356440 Q9Y6X8 EBI-356440,EBI-948566 Q8IYE1 EBI-356440,EBI-10961312 Q9H2G2 EBI-356440,EBI-1022272 Q13061 EBI-356440,EBI-10757323 Q9HCD5 EBI-356440,EBI-2863498 O75311 EBI-356440,EBI-16357053 P08621 EBI-1049228,EBI-356440 Q86X27 EBI-356440,EBI-1050841 P0DTD1 EBI-25475880,EBI-356440 P62937 EBI-356440,EBI-437708 Q13509 EBI-350989,EBI-356440 Q71U36 EBI-302552,EBI-356440 O14829 EBI-2931238,EBI-356440 Q9NX70 EBI-394656,EBI-356440 Q04206-2 EBI-356440,EBI-289947 Q9Y572 EBI-356440,EBI-298250 P20333 EBI-356440,EBI-358983 Q13233 EBI-356440,EBI-49776 Q99759 EBI-356440,EBI-307281 Q00653 EBI-356440,EBI-307326 Q15628 EBI-356440,EBI-359215 GO:0005829 GO:0005743 GO:0005758 GO:0005739 GO:0005634 GO:0048471 GO:0003677 GO:0071949 GO:0016174 GO:0016651 GO:0046983 GO:0006919 GO:0006915 GO:1904045 GO:0071392 GO:0070301 GO:0071732 GO:0090650 GO:0030261 GO:0070059 GO:0033108 GO:0032981 GO:0051402 GO:0030182 GO:0055114 GO:0043065 GO:0043525 GO:0045041 GO:1902510 GO:0002931 GO:1902065 MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED 613 O95996 Adenomatous polyposis coli protein 2 APC2 9606 Yes SL-0198 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}. UNIPROT O95996 UNIPROT Q05BW4 UNIPROT Q9UBZ1 UNIPROT Q9UEM8 UNIPROT Q9UQJ8 UNIPROT Q9UQJ9 UNIPROT Q9Y632 Pfam PF05956 Pfam PF16689 Pfam PF05923 Pfam PF18797 Pfam PF00514 Pfam PF05924 OMIM 612034 OMIM 617169 DisGeNET 10297 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}.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. Q9NRI5 EBI-1053045,EBI-529989 P16035 EBI-1053045,EBI-1033507 GO:0005884 GO:0030877 GO:0016342 GO:0005737 GO:0005829 GO:0005794 GO:0045171 GO:0031258 GO:0005874 GO:0015630 GO:0030496 GO:0048471 GO:0098794 GO:0008013 GO:0045295 GO:0008017 GO:0090630 GO:0001708 GO:0016477 GO:0000226 GO:0090090 GO:0007026 GO:0007389 GO:0045732 GO:0045595 GO:0016055 MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYVRKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPAALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCGQPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVPEKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGATSLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPDSPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSALALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVASALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMGHRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPAAAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPRGREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASDLDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVKTSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRSRSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQHKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKESPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSESPSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRSTLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPISAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE 2303 O95999 B-cell lymphoma/leukemia 10 BCL10 9606 Yes SL-0198 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. UNIPROT O95999 UNIPROT Q5VUF1 PDB 2MB9 PDB 6BZE PDB 6GK2 Pfam PF00619 PROSITE PS50209 OMIM 137245 OMIM 603517 OMIM 616098 DisGeNET 8915 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}.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. Self EBI-958922,EBI-958922 Q12933 EBI-958922,EBI-355744 P50750 EBI-1383449,EBI-958922 Q13261 EBI-958922,EBI-980354 Q07955 EBI-398920,EBI-958922 Q8WUM9 EBI-958922,EBI-3909857 O14745 EBI-349787,EBI-958922 Q05513 EBI-958922,EBI-295351 P33215 EBI-2366213,EBI-958922 O95684 EBI-1266334,EBI-958922 Q8N6Y0 EBI-958922,EBI-739895 Q9BZD6 EBI-958922,EBI-3918643 P62807 EBI-354552,EBI-958922 Q14525 EBI-1049638,EBI-958922 P31749 EBI-296087,EBI-958922 P20749 EBI-958922,EBI-958997 Q9H257 EBI-958922,EBI-751319 Q9Y2V7 EBI-3866319,EBI-958922 Q9BXL7 EBI-7006141,EBI-958922 Q9UDY8 EBI-1047372,EBI-958922 Q9Y6K9 EBI-81279,EBI-958922 Q9H0F6 EBI-3942966,EBI-958922 Q6P5F9 EBI-2550236,EBI-958922 GO:0032449 GO:0005737 GO:0005881 GO:0005829 GO:0001772 GO:0005764 GO:0045121 GO:0005634 GO:0048471 GO:0002096 GO:0032991 GO:0050700 GO:0019899 GO:0042802 GO:0019900 GO:0051059 GO:0002020 GO:0008022 GO:0043422 GO:0019901 GO:0043621 GO:0044877 GO:0003713 GO:0008134 GO:0031625 GO:0002250 GO:0001783 GO:0008219 GO:0006968 GO:0071222 GO:0071260 GO:0038095 GO:0007249 GO:0016064 GO:0045087 GO:0042226 GO:0031663 GO:0042109 GO:0002906 GO:0001843 GO:0043065 GO:0043280 GO:2001238 GO:0043123 GO:0045416 GO:0033674 GO:0032765 GO:0051092 GO:0042327 GO:0031398 GO:0050870 GO:0045893 GO:0016567 GO:0050856 GO:0032094 GO:0009620 GO:0002223 GO:0070231 GO:0050852 GO:0002224 MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ 233 O96018 Amyloid-beta A4 precursor protein-binding family A member 3 APBA3 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}. UNIPROT O96018 UNIPROT O60483 UNIPROT Q9UPZ2 PDB 2YT7 PDB 2YT8 PDB 5UWS Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 OMIM 604262 DisGeNET 9546 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}. Q9NWT6 EBI-745632,EBI-6115839 Q9H6Z9 EBI-1175354,EBI-6115839 P16152 EBI-351348,EBI-6115839 P78552 EBI-6115839,EBI-1391535 Q9UHD2 EBI-6115839,EBI-356402 Q9NSD9 EBI-6115839,EBI-353803 Q9H6S1 EBI-6115839,EBI-359973 Q9BY42 EBI-6115839,EBI-1045669 Q9BSJ5-2 EBI-6115839,EBI-21508079 Q99590 EBI-6115839,EBI-3934011 Q99569-2 EBI-6115839,EBI-4324902 Q96P71-2 EBI-6115839,EBI-15098952 Q8TEU7-3 EBI-6115839,EBI-21543860 Q8TBX8 EBI-6115839,EBI-1383637 Q8N9R8-2 EBI-6115839,EBI-21554215 Q6PD62 EBI-6115839,EBI-1019583 Q6P5Z2 EBI-6115839,EBI-1384335 Q5JTD0-2 EBI-6115839,EBI-10980237 Q12986-2 EBI-6115839,EBI-21604769 Q08AH1 EBI-6115839,EBI-2818055 Q06481-2 EBI-6115839,EBI-21531175 P55789 EBI-6115839,EBI-718281 P29803 EBI-6115839,EBI-2957428 P17029 EBI-6115839,EBI-10199654 P05067-10 EBI-6115839,EBI-21535835 O94985-2 EBI-6115839,EBI-16041593 O75319 EBI-6115839,EBI-719569 Q96BW9 EBI-6115839,EBI-13943422 P32320 EBI-9250559,EBI-6115839 Q9QYP6 EBI-6115874,EBI-6115839 A7MCY6 EBI-359969,EBI-6115839 Q92844 EBI-356349,EBI-6115839 Q6P5F9 EBI-2550236,EBI-6115839 Q86VW1 EBI-21721937,EBI-6115839 Q9BZB8-3 EBI-21821945,EBI-6115839 GO:0005737 GO:0043197 GO:0048471 GO:0005886 GO:0045202 GO:0001540 GO:0019899 GO:0004857 GO:0007268 GO:0001701 GO:0043086 GO:0015031 GO:0010468 MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL 575 O97921 Prostaglandin-H2 D-isomerase PTGDS 9796 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT O97921 Pfam PF00061 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}. GO:0005576 GO:0005615 GO:0005794 GO:0031965 GO:0048471 GO:0005791 GO:0004667 GO:0005501 GO:0036094 GO:0001516 GO:0045187 MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLTSTFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRPEVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN 194 P00519 Tyrosine-protein kinase ABL1 ABL1 9606 Yes SL-0178 SL-0182 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. UNIPROT P00519 UNIPROT A3KFJ3 UNIPROT Q13869 UNIPROT Q13870 UNIPROT Q16133 UNIPROT Q17R61 UNIPROT Q45F09 PDB 1AB2 PDB 1ABL PDB 1AWO PDB 1BBZ PDB 1JU5 PDB 1OPL PDB 1ZZP PDB 2ABL PDB 2E2B PDB 2F4J PDB 2FO0 PDB 2G1T PDB 2G2F PDB 2G2H PDB 2G2I PDB 2GQG PDB 2HIW PDB 2HYY PDB 2HZ0 PDB 2HZ4 PDB 2HZI PDB 2O88 PDB 2V7A PDB 3CS9 PDB 3EG0 PDB 3EG1 PDB 3EG2 PDB 3EG3 PDB 3EGU PDB 3K2M PDB 3PYY PDB 3QRI PDB 3QRJ PDB 3QRK PDB 3T04 PDB 3UE4 PDB 3UYO PDB 4J9B PDB 4J9C PDB 4J9D PDB 4J9E PDB 4J9F PDB 4J9G PDB 4J9H PDB 4J9I PDB 4JJB PDB 4JJC PDB 4JJD PDB 4TWP PDB 4WA9 PDB 4XEY PDB 4YC8 PDB 4ZOG PDB 5DC0 PDB 5DC4 PDB 5DC9 PDB 5HU9 PDB 5MO4 PDB 5NP2 PDB 5OAZ PDB 6AMV PDB 6AMW PDB 6BL8 PDB 6NPE PDB 6NPU PDB 6NPV Pfam PF08919 Pfam PF07714 Pfam PF00017 Pfam PF00018 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50001 PROSITE PS50002 OMIM 189980 OMIM 608232 OMIM 617602 DisGeNET 25 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}.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. P06241 EBI-375543,EBI-515315 P62993 EBI-375543,EBI-401755 P16333 EBI-375543,EBI-389883 P27986 EBI-375543,EBI-79464 P19174 EBI-375543,EBI-79387 O43900 EBI-375543,EBI-1751761 Q9HCM9 EBI-375543,EBI-739510 Q9Y697 EBI-375543,EBI-1751791 Q92918 EBI-375543,EBI-881 P78345 EBI-375543,EBI-366493 Q8NFP9 EBI-375543,EBI-723014 O43390 EBI-375543,EBI-713419 O00254 EBI-375543,EBI-1751853 Q9Y5Y3 EBI-375543,EBI-1751869 Q9UL51 EBI-375543,EBI-1751885 P78357 EBI-375543,EBI-1751903 Q96NS5 EBI-375543,EBI-1751918 Q07890 EBI-375543,EBI-298181 O94856 EBI-375543,EBI-1751948 Q9NZV5 EBI-375543,EBI-1751965 P49450 EBI-375543,EBI-1751979 Q92874 EBI-375543,EBI-1751995 Q7Z408 EBI-375543,EBI-1957312 P98161 EBI-375543,EBI-1752013 P43699 EBI-1391923,EBI-375543 P50570 EBI-375543,EBI-346547 Q96GP6 EBI-375543,EBI-1752088 Q14315 EBI-375543,EBI-489954 P31273 EBI-375543,EBI-1752118 Q92664 EBI-375543,EBI-1752104 Q9UJV9 EBI-375543,EBI-1046350 O43493 EBI-375543,EBI-1752146 Q15427 EBI-375543,EBI-348469 Q12979 EBI-375543,EBI-489922 Q13023 EBI-375543,EBI-1056102 P15586 EBI-375543,EBI-1752200 P23760 EBI-375543,EBI-1167564 Q9UIF9 EBI-375543,EBI-934890 Q9UM47 EBI-375543,EBI-1236377 Q13415 EBI-375543,EBI-374847 P06865 EBI-375543,EBI-723519 Q9H2X0 EBI-375543,EBI-947551 P51587 EBI-375543,EBI-79792 Q9UMN6 EBI-375543,EBI-765774 Q12947 EBI-375543,EBI-1752316 Q9BYB0 EBI-375543,EBI-1752330 Q9UBS5 EBI-375543,EBI-724156 Q8IZD9 EBI-375543,EBI-1752361 P28340 EBI-375543,EBI-716569 Q9NYQ7 EBI-375543,EBI-308417 P78329 EBI-375543,EBI-1752413 O43708 EBI-375543,EBI-748043 Q9H5I1 EBI-375543,EBI-723127 P46013 EBI-375543,EBI-876367 O76039 EBI-375543,EBI-1752465 Q14008 EBI-375543,EBI-310585 Q13087 EBI-375543,EBI-1752525 O14513 EBI-375543,EBI-1752508 O95886 EBI-375543,EBI-1752541 Q9Y5X2 EBI-375543,EBI-1752557 P42566 EBI-375543,EBI-396684 Q96RL7 EBI-375543,EBI-1752583 Q9UMY4 EBI-375543,EBI-1752602 Q9C0E4 EBI-375543,EBI-949557 Q15036 EBI-375543,EBI-1752620 P34820 EBI-375543,EBI-1752660 P30260 EBI-375543,EBI-994813 O75751 EBI-375543,EBI-1752674 Q86UR5 EBI-375543,EBI-1043236 Q9NZQ3 EBI-375543,EBI-745080 P26992 EBI-375543,EBI-743758 P50851 EBI-375543,EBI-1052167 O76081 EBI-375543,EBI-1052678 Q92988 EBI-375543,EBI-1752755 Q96PC5 EBI-375543,EBI-1050253 Q9BQ89 EBI-375543,EBI-1752811 P20810 EBI-375543,EBI-1268770 Q9H1R2 EBI-375543,EBI-1752795 P02765 EBI-375543,EBI-1223374 Q9Y3S1 EBI-375543,EBI-948521 Q13905 EBI-375543,EBI-976876 Q9UQ16 EBI-375543,EBI-1111783 Q9Y5K6 EBI-375543,EBI-298152 O15255 EBI-375543,EBI-954396 Q8TB24 EBI-375543,EBI-1570523 O95157 EBI-375543,EBI-1752913 O43281 EBI-375543,EBI-718488 O15085 EBI-375543,EBI-311099 P08047 EBI-375543,EBI-298336 P98164 EBI-375543,EBI-947916 Q86SG6 EBI-375543,EBI-1752987 Q9H0X9 EBI-375543,EBI-1753005 Q9NQC3 EBI-375543,EBI-715945 O60244 EBI-375543,EBI-394489 Q9UK85 EBI-375543,EBI-1753048 Q9BXM0 EBI-375543,EBI-1753064 O43918 EBI-375543,EBI-1753081 Q96AC6 EBI-375543,EBI-724040 Q9HCQ7 EBI-375543,EBI-1753111 O15056 EBI-375543,EBI-310513 P32239 EBI-375543,EBI-1753137 Q15027 EBI-375543,EBI-751746 O14490 EBI-375543,EBI-1753207 Q8WX92 EBI-375543,EBI-347721 Q9NUR3 EBI-375543,EBI-1753189 P13671 EBI-375543,EBI-1753221 P42167 EBI-375543,EBI-455283 Q99572 EBI-375543,EBI-1753251 O15117 EBI-375543,EBI-1753267 Q14767 EBI-375543,EBI-1546118 Q9NQ76 EBI-375543,EBI-1753293 Q9Y2J2 EBI-375543,EBI-310986 O60493 EBI-375543,EBI-727209 Q9UHL9 EBI-375543,EBI-372530 Q05193 EBI-375543,EBI-713135 Q9ULH1 EBI-375543,EBI-346622 Q9UN86 EBI-375543,EBI-1044298 P49916 EBI-375543,EBI-1753381 Q9P1A6 EBI-375543,EBI-1753397 Q9Y2H0 EBI-375543,EBI-722139 Q9BZM3 EBI-375543,EBI-1753426 Q9UJT2 EBI-375543,EBI-852101 P12018 EBI-375543,EBI-1753454 Q9ULD4 EBI-375543,EBI-1753470 Q9Y3Q4 EBI-375543,EBI-1753521 Q9NRJ4 EBI-375543,EBI-1753487 O60721 EBI-375543,EBI-1753504 O75326 EBI-375543,EBI-1753538 Q08209 EBI-375543,EBI-352922 Q14999 EBI-375543,EBI-308606 Q9BWW9 EBI-375543,EBI-1753592 Q8TAS1 EBI-375543,EBI-1753608 P21333 EBI-375543,EBI-350432 P29074 EBI-375543,EBI-710431 Q9UN72 EBI-375543,EBI-1753660 P52803 EBI-375543,EBI-1753674 P20774 EBI-375543,EBI-1753690 Q99259 EBI-375543,EBI-743184 P46108 EBI-375543,EBI-886 P12931 EBI-375543,EBI-621482 P31946-2 EBI-10770173,EBI-375543 P61981 EBI-359832,EBI-375543 Q04917 EBI-306940,EBI-375543 Q9BY11 EBI-375543,EBI-721769 Q03468 EBI-375543,EBI-295284 P10275 EBI-375543,EBI-608057 P10721 EBI-375543,EBI-1379503 P14618-1 EBI-375543,EBI-4304679 Q38SD2 EBI-375543,EBI-1050422 Q5S007 EBI-375543,EBI-5323863 P00533 EBI-375543,EBI-297353 Q64010-2 EBI-2642543,EBI-375543 P97465 EBI-914917,EBI-375543 Q8BTZ4 EBI-10976824,EBI-375543 Q8BL66 EBI-647872,EBI-375543 Q1H9T6 EBI-11104272,EBI-375543 Q15637 EBI-375543,EBI-744603 P53999 EBI-375543,EBI-998260 P61604 EBI-375543,EBI-711483 P26641 EBI-375543,EBI-351467 P62258 EBI-375543,EBI-356498 Q9Y295 EBI-375543,EBI-719554 Q01844 EBI-375543,EBI-739737 P63220 EBI-375543,EBI-714051 Q12906 EBI-375543,EBI-78756 P31946 EBI-375543,EBI-359815 P52272 EBI-375543,EBI-486809 P35637 EBI-375543,EBI-400434 Q9BY44 EBI-375543,EBI-1776615 P27348 EBI-375543,EBI-359854 P05386 EBI-375543,EBI-354582 P17844 EBI-375543,EBI-351962 P12956 EBI-375543,EBI-353208 Q96AG4 EBI-375543,EBI-358888 Q07065 EBI-375543,EBI-702400 P63104 EBI-375543,EBI-347088 P53355 EBI-375543,EBI-358616 P08238 EBI-375543,EBI-352572 P78362 EBI-375543,EBI-593303 Q63767 EBI-375543,EBI-1176801 Q13671 EBI-375543,EBI-366017 Q13315 EBI-495465,EBI-375543 P54274-2 EBI-375543,EBI-711018 Q9BX66 EBI-375543,EBI-433642 P31947 EBI-375543,EBI-476295 Q8CBW3 EBI-375543,EBI-375511 Q8IZP0 EBI-375543,EBI-375446 GO:0015629 GO:0005623 GO:0031252 GO:0005737 GO:0005829 GO:0030425 GO:0005739 GO:0043025 GO:0016604 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0098794 GO:0032991 GO:0051015 GO:0003785 GO:0005524 GO:0000405 GO:0003677 GO:0046875 GO:0000400 GO:0016301 GO:0000287 GO:0030145 GO:0051019 GO:0038191 GO:0004515 GO:0004715 GO:0001784 GO:0070064 GO:0008022 GO:0004672 GO:0005080 GO:0004713 GO:1990837 GO:0042169 GO:0017124 GO:0019905 GO:0003713 GO:0030036 GO:0090135 GO:0050798 GO:1990051 GO:0046632 GO:0006914 GO:0002322 GO:0050853 GO:0001922 GO:0060020 GO:0072358 GO:0007050 GO:0006464 GO:0006974 GO:1903351 GO:0070301 GO:0071222 GO:0034599 GO:0021587 GO:0048668 GO:0071103 GO:0006975 GO:0006897 GO:0043542 GO:0007173 GO:0045184 GO:0038096 GO:0007229 GO:0008630 GO:0030035 GO:0006298 GO:0051882 GO:0000278 GO:0030514 GO:0022408 GO:2000773 GO:2000352 GO:0070373 GO:0043124 GO:1900272 GO:0045930 GO:1900275 GO:0071901 GO:0051444 GO:0001843 GO:0060563 GO:0050885 GO:0038189 GO:0038083 GO:0018108 GO:0035791 GO:1905555 GO:2000251 GO:1904531 GO:0043065 GO:0090050 GO:0007204 GO:0010595 GO:0070374 GO:0051894 GO:0043123 GO:1902715 GO:1900042 GO:1904528 GO:0045931 GO:0051149 GO:1901216 GO:0033690 GO:0051353 GO:0050731 GO:0001934 GO:0051281 GO:0051496 GO:1900026 GO:0045944 GO:2000096 GO:0009791 GO:0046777 GO:0006468 GO:0032956 GO:2000249 GO:0042981 GO:0010506 GO:0030516 GO:0032489 GO:0030155 GO:2000145 GO:0030100 GO:1903053 GO:1902036 GO:0031113 GO:1905244 GO:2001020 GO:0045580 GO:0006355 GO:0006979 GO:0042770 GO:0048536 GO:0034446 GO:0050852 GO:0048538 GO:0002333 MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR 1130 P00533 Epidermal growth factor receptor EGFR 9606 Yes SL-0178 SL-0182 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. UNIPROT P00533 UNIPROT O00688 UNIPROT O00732 UNIPROT P06268 UNIPROT Q14225 UNIPROT Q68GS5 UNIPROT Q92795 UNIPROT Q9BZS2 UNIPROT Q9GZX1 UNIPROT Q9H2C9 UNIPROT Q9H3C9 UNIPROT Q9UMD7 UNIPROT Q9UMD8 UNIPROT Q9UMG5 PDB 1DNQ PDB 1DNR PDB 1IVO PDB 1M14 PDB 1M17 PDB 1MOX PDB 1NQL PDB 1XKK PDB 1YY9 PDB 1Z9I PDB 2EB2 PDB 2EB3 PDB 2EXP PDB 2EXQ PDB 2GS2 PDB 2GS6 PDB 2GS7 PDB 2ITN PDB 2ITO PDB 2ITP PDB 2ITQ PDB 2ITT PDB 2ITU PDB 2ITV PDB 2ITW PDB 2ITX PDB 2ITY PDB 2ITZ PDB 2J5E PDB 2J5F PDB 2J6M PDB 2JIT PDB 2JIU PDB 2JIV PDB 2KS1 PDB 2M0B PDB 2M20 PDB 2N5S PDB 2RF9 PDB 2RFD PDB 2RFE PDB 2RGP PDB 3B2U PDB 3B2V PDB 3BEL PDB 3BUO PDB 3C09 PDB 3G5V PDB 3G5Y PDB 3GOP PDB 3GT8 PDB 3IKA PDB 3LZB PDB 3NJP PDB 3OB2 PDB 3OP0 PDB 3P0Y PDB 3PFV PDB 3POZ PDB 3QWQ PDB 3UG1 PDB 3UG2 PDB 3VJN PDB 3VJO PDB 3VRP PDB 3VRR PDB 3W2O PDB 3W2P PDB 3W2Q PDB 3W2R PDB 3W2S PDB 3W32 PDB 3W33 PDB 4G5J PDB 4G5P PDB 4HJO PDB 4I1Z PDB 4I20 PDB 4I21 PDB 4I22 PDB 4I23 PDB 4I24 PDB 4JQ7 PDB 4JQ8 PDB 4JR3 PDB 4JRV PDB 4KRL PDB 4KRM PDB 4KRO PDB 4KRP PDB 4LI5 PDB 4LL0 PDB 4LQM PDB 4LRM PDB 4R3P PDB 4R3R PDB 4R5S PDB 4RIW PDB 4RIX PDB 4RIY PDB 4RJ4 PDB 4RJ5 PDB 4RJ6 PDB 4RJ7 PDB 4RJ8 PDB 4TKS PDB 4UIP PDB 4UV7 PDB 4WD5 PDB 4WKQ PDB 4WRG PDB 4ZAU PDB 4ZJV PDB 4ZSE PDB 5C8K PDB 5C8M PDB 5C8N PDB 5CAL PDB 5CAN PDB 5CAO PDB 5CAP PDB 5CAQ PDB 5CAS PDB 5CAU PDB 5CAV PDB 5CNN PDB 5CNO PDB 5CZH PDB 5CZI PDB 5D41 PDB 5EDP PDB 5EDQ PDB 5EDR PDB 5EM5 PDB 5EM6 PDB 5EM7 PDB 5EM8 PDB 5FED PDB 5FEE PDB 5FEQ PDB 5GMP PDB 5GNK PDB 5GTY PDB 5GTZ PDB 5HCX PDB 5HCY PDB 5HCZ PDB 5HG5 PDB 5HG7 PDB 5HG8 PDB 5HG9 PDB 5HIB PDB 5HIC PDB 5J9Y PDB 5J9Z PDB 5JEB PDB 5LV6 PDB 5SX4 PDB 5SX5 PDB 5U8L PDB 5UG8 PDB 5UG9 PDB 5UGA PDB 5UGB PDB 5UGC PDB 5UWD PDB 5WB7 PDB 5WB8 PDB 5X26 PDB 5X27 PDB 5X28 PDB 5X2A PDB 5X2C PDB 5X2F PDB 5X2K PDB 5XDK PDB 5XDL PDB 5XGM PDB 5XGN PDB 5XWD PDB 5Y25 PDB 5Y9T PDB 5YU9 PDB 5ZTO PDB 5ZWJ PDB 6ARU PDB 6B3S PDB 6D8E PDB 6DUK PDB 6JZ0 PDB 6P1D PDB 6P1L PDB 6P8Q PDB 6S89 PDB 6S8A PDB 6S9B PDB 6S9C PDB 6S9D Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 131550 OMIM 211980 OMIM 616069 DisGeNET 1956 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}.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. D4A631 EBI-297353,EBI-6251168 O60645 EBI-1052278,EBI-297353 O94875 EBI-311323,EBI-297353 P00519 EBI-375543,EBI-297353 Self EBI-297353,EBI-297353 P42566 EBI-297353,EBI-396684 Q9UJ41 EBI-297353,EBI-913954 P23467 EBI-297353,EBI-1265766 Q12913 EBI-297353,EBI-2264500 P08575 EBI-1341,EBI-297353 P62157 EBI-397403,EBI-297353 Q29376 EBI-297353,EBI-1256881 P0DP23 EBI-297353,EBI-397435 P0DP28 EBI-397460,EBI-297353 P13866 EBI-297353,EBI-1772443 P23470 EBI-297353,EBI-2258115 Q9BZP6 EBI-297353,EBI-14357960 Q92731 EBI-78505,EBI-297353 Q6PK50 EBI-297353,EBI-9356629 Q16543 EBI-297353,EBI-295634 Q96BE0 EBI-9356686,EBI-297353 Q8K2C9 EBI-8329978,EBI-297353 Q53FC7 EBI-297353,EBI-9356749 Q9BPW0 EBI-297353,EBI-9356778 Q13451 EBI-297353,EBI-306914 Q8IVD9 EBI-297353,EBI-744342 P04626 EBI-641062,EBI-297353 P21860 EBI-720706,EBI-297353 O14965 EBI-448680,EBI-297353 P14618-1 EBI-297353,EBI-4304679 P97313 EBI-2272005,EBI-297353 P78527 EBI-297353,EBI-352053 P17936 EBI-297353,EBI-715709 P50281 EBI-297353,EBI-992788 P63010 EBI-297353,EBI-432924 Q8TF42 EBI-297353,EBI-1380492 Q9UBS4 EBI-297353,EBI-713113 O75223 EBI-297353,EBI-6912130 P62701 EBI-297353,EBI-354303 P11142 EBI-297353,EBI-351896 O95782 EBI-297353,EBI-353552 P62269 EBI-297353,EBI-352451 P34931 EBI-297353,EBI-354912 P54652 EBI-297353,EBI-356991 P01040 EBI-297353,EBI-724303 P62805 EBI-297353,EBI-302023 P29353 EBI-297353,EBI-78835 P11021 EBI-297353,EBI-354921 P08195 EBI-297353,EBI-702356 Q75V66 EBI-297353,EBI-8769971 P38646 EBI-297353,EBI-354932 O95155 EBI-297353,EBI-1641720 Q01469 EBI-297353,EBI-1054073 Q92832 EBI-297353,EBI-947754 Q6UWL2 EBI-297353,EBI-2821581 P25705 EBI-297353,EBI-351437 Q8N163 EBI-297353,EBI-355410 Q09666 EBI-297353,EBI-2555881 Q13098 EBI-297353,EBI-725197 P62993 EBI-297353,EBI-401755 Q9UJM3 EBI-297353,EBI-2941912 Q71U36 EBI-297353,EBI-302552 P49411 EBI-297353,EBI-359097 Q8WV24 EBI-297353,EBI-738731 P10586 EBI-297353,EBI-7188069 Q9BYJ9 EBI-297353,EBI-1051237 Q92522 EBI-297353,EBI-876335 P53680 EBI-297353,EBI-297662 P62841 EBI-297353,EBI-372635 Q96JX3 EBI-297353,EBI-8770074 O60716 EBI-297353,EBI-701927 P30711 EBI-297353,EBI-8770084 P48594 EBI-297353,EBI-1055490 Q96QV6 EBI-297353,EBI-6286100 P12830 EBI-297353,EBI-727477 P23634 EBI-297353,EBI-1174388 Q01650 EBI-297353,EBI-6138761 P35321 EBI-297353,EBI-6149907 P18621 EBI-297353,EBI-726937 P31943 EBI-297353,EBI-351590 P23246 EBI-297353,EBI-355453 P08581 EBI-297353,EBI-1039152 Q5JNZ5 EBI-297353,EBI-8770070 Q10567 EBI-297353,EBI-1171303 P26232 EBI-297353,EBI-3953920 O94973 EBI-297353,EBI-1642835 Q9H0D6 EBI-297353,EBI-372110 P23468 EBI-297353,EBI-2682990 Q9UMD9 EBI-297353,EBI-2528742 P16615 EBI-297353,EBI-358933 Q8IUR7 EBI-297353,EBI-1049469 P31947 EBI-297353,EBI-476295 P27824 EBI-297353,EBI-355947 P04114 EBI-297353,EBI-3926040 O95470 EBI-297353,EBI-1046170 Q9UQB8 EBI-297353,EBI-525456 P04792 EBI-297353,EBI-352682 P04083 EBI-297353,EBI-354007 Q96RL7 EBI-297353,EBI-1752583 P49756 EBI-297353,EBI-2211856 Q9UK59 EBI-297353,EBI-2871803 Q96CW1 EBI-297353,EBI-297683 P16144 EBI-297353,EBI-948678 P35221 EBI-297353,EBI-701918 P35222 EBI-297353,EBI-491549 P08238 EBI-297353,EBI-352572 P07900 EBI-297353,EBI-296047 P43307 EBI-297353,EBI-714168 P40763 EBI-297353,EBI-518675 Q00325 EBI-297353,EBI-358549 O95573 EBI-297353,EBI-1190822 O60884 EBI-297353,EBI-352957 P27348 EBI-297353,EBI-359854 P68366 EBI-297353,EBI-351772 Q8NFI3 EBI-297353,EBI-2857825 O00483 EBI-297353,EBI-1049381 A1L0T0 EBI-297353,EBI-720553 P16083 EBI-297353,EBI-358466 Q14457 EBI-949378,EBI-297353 Q92622 EBI-297353,EBI-2952709 Q13480 EBI-517684,EBI-297353 P16333 EBI-297353,EBI-389883 P29353-7 EBI-297353,EBI-9691288 P46108-1 EBI-287556,EBI-297353 P04406 EBI-354056,EBI-297353 Q68CZ2 EBI-1220488,EBI-297353 P15941 EBI-2804728,EBI-297353 P42224 EBI-1057697,EBI-297353 Q9Y2R2 EBI-297353,EBI-1211241 P17252 EBI-297353,EBI-1383528 P16885 EBI-617403,EBI-297353 Q8WUI4 EBI-297353,EBI-1048378 O75791 EBI-297353,EBI-740418 P09769 EBI-297353,EBI-1383732 Q92870 EBI-79277,EBI-297353 Q9NSE2 EBI-617866,EBI-297353 Q9BRG2 EBI-2339271,EBI-297353 P49069 EBI-1748958,EBI-297353 O00750 EBI-641107,EBI-297353 P04150 EBI-493507,EBI-297353 P16234 EBI-2861522,EBI-297353 Q13094 EBI-346946,EBI-297353 O43561 EBI-297353,EBI-1222766 Q6S5L8 EBI-9453524,EBI-297353 P10599 EBI-297353,EBI-594644 P18031 EBI-297353,EBI-968788 Q12933 EBI-355744,EBI-297353 Q12929 EBI-375576,EBI-297353 Q92625 EBI-1048612,EBI-297353 Q9UBN7 EBI-297353,EBI-301697 P42229 EBI-749537,EBI-297353 Q14247 EBI-351886,EBI-297353 Q9UNE7 EBI-357085,EBI-297353 Q38SD2 EBI-1050422,EBI-297353 P30307 EBI-297353,EBI-974439 P42685 EBI-1383583,EBI-297353 Q8WUM4 EBI-310624,EBI-297353 P45984 EBI-713568,EBI-297353 Q07954 EBI-1046087,EBI-297353 P32121 EBI-297353,EBI-714559 P34932 EBI-356933,EBI-297353 O60603 EBI-297353,EBI-973722 O00459 EBI-346930,EBI-297353 P52630 EBI-1546963,EBI-297353 O14543 EBI-297353,EBI-714146 O14544 EBI-3929549,EBI-297353 Q07890 EBI-298181,EBI-297353 P10636 EBI-366182,EBI-297353 Q9NRF2 EBI-310491,EBI-297353 Q8N5H7 EBI-297353,EBI-745980 P46109 EBI-297353,EBI-910 Q05397 EBI-702142,EBI-297353 O00401 EBI-957615,EBI-297353 P07948 EBI-79452,EBI-297353 Q9H6Q3 EBI-297353,EBI-1222854 P31946 EBI-297353,EBI-359815 Q99952 EBI-297353,EBI-1384210 Q14155 EBI-717515,EBI-297353 P46108 EBI-886,EBI-297353 P05067 EBI-297353,EBI-77613 P49798 EBI-297353,EBI-9688865 P49407 EBI-743313,EBI-297353 Q99704 EBI-1384360,EBI-297353 P51636 EBI-297353,EBI-603607 P14923 EBI-702484,EBI-297353 P26447 EBI-717058,EBI-297353 Q92569 EBI-79893,EBI-297353 P45983 EBI-297353,EBI-286483 Q9UPY6 EBI-297353,EBI-3907133 Q99962 EBI-297353,EBI-77938 Q99759 EBI-297353,EBI-307281 P51451 EBI-2105445,EBI-297353 Q13153 EBI-297353,EBI-1307 P15498 EBI-297353,EBI-625518 P63104 EBI-297353,EBI-347088 Q15750 EBI-358643,EBI-297353 Q02156 EBI-706254,EBI-297353 P08631 EBI-297353,EBI-346340 Q02297 EBI-2460704,EBI-297353 Q13387 EBI-722813,EBI-297353 Q13905 EBI-297353,EBI-976876 P42684 EBI-1102694,EBI-297353 Q13322 EBI-297353,EBI-80275 P12931 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EBI-297353,EBI-22241807 O15357 EBI-297353,EBI-1384248 Q9UKW4 EBI-297353,EBI-297568 Q63768 EBI-297353,EBI-8423843 P54100 EBI-297353,EBI-22084104 F1LWB1 EBI-297353,EBI-22084199 Q64725 EBI-297353,EBI-2615512 Q9WVR3 EBI-297353,EBI-920167 Q5RJK6 EBI-297353,EBI-22084302 F1LNG5 EBI-297353,EBI-22085642 G3V7X3 EBI-297353,EBI-22085594 Q9QZC5 EBI-297353,EBI-22085551 P50904 EBI-297353,EBI-5747849 P41499 EBI-297353,EBI-7180604 Q9WUD9-2 EBI-297353,EBI-22179963 Q9WUD9 EBI-297353,EBI-7784541 Q8CFN2 EBI-297353,EBI-7023929 A0A0G2K3B0 EBI-297353,EBI-22180056 A0A0G2JSR4 EBI-297353,EBI-22156317 Q5XI26 EBI-297353,EBI-22150963 F1M9D6 EBI-297353,EBI-15667209 Q8K4S7 EBI-297353,EBI-8536678 D3ZY64 EBI-297353,EBI-22236644 B2GV15 EBI-297353,EBI-16219426 D3ZV15 EBI-297353,EBI-21998185 P24135 EBI-297353,EBI-22236548 P10686 EBI-297353,EBI-520788 E9PT59 EBI-297353,EBI-22237732 D4A3T0 EBI-297353,EBI-11702585 P59622 EBI-297353,EBI-22237808 Q8R424 EBI-297353,EBI-22237695 F1M3E4 EBI-297353,EBI-22237648 Q920L0 EBI-297353,EBI-22237619 Q4KM68 EBI-297353,EBI-22237548 Q9EQH1 EBI-297353,EBI-7620518 P97573 EBI-297353,EBI-8008869 P85968 EBI-297353,EBI-22237670 D4A5Q1 EBI-297353,EBI-22236396 P52631 EBI-297353,EBI-10764775 Q63788 EBI-297353,EBI-22237563 P08461 EBI-297353,EBI-916164 A0A0R4J8U1 EBI-297353,EBI-22236360 Q63065 EBI-297353,EBI-7383638 Q5M824 EBI-297353,EBI-7152521 Q32PX8 EBI-297353,EBI-22237992 B5DFI9 EBI-297353,EBI-22237955 F1M9C0 EBI-297353,EBI-22237909 D3Z8I4 EBI-297353,EBI-22237883 P52632 EBI-297353,EBI-15667283 Q5BK11 EBI-297353,EBI-22237117 F1MAF2 EBI-297353,EBI-22251970 Q58FF7 EBI-297353,EBI-9996483 P09651 EBI-297353,EBI-352662 Q32P51 EBI-297353,EBI-2556580 P17844 EBI-297353,EBI-351962 P61221 EBI-297353,EBI-2510446 Q8IXB1 EBI-297353,EBI-2949763 P60709 EBI-297353,EBI-353944 Q15208 EBI-297353,EBI-458376 Q16875 EBI-297353,EBI-764464 Q9UHB6 EBI-297353,EBI-351479 Q9ULV4 EBI-297353,EBI-351384 Q9Y383 EBI-297353,EBI-352851 P23469 EBI-2258070,EBI-297353 Q6ZWB6 EBI-6426198,EBI-297353 Q14515 EBI-2682673,EBI-297353 P18433 EBI-2609645,EBI-297353 P0DMV8 EBI-11052499,EBI-297353 Q96JA1 EBI-297353,EBI-2865191 O14944 EBI-17272224,EBI-297353 Q6UW88 EBI-15482510,EBI-297353 Q99075 EBI-7211558,EBI-297353 P35070 EBI-297353,EBI-25434897 P15514 EBI-297353,EBI-953674 O94898 EBI-297353,EBI-2830372 P60033 EBI-712921,EBI-297353 P33992 EBI-297353,EBI-359410 P33993 EBI-297353,EBI-355924 P07948-1 EBI-297353,EBI-6895930 P07948-2 EBI-297353,EBI-3951572 Q8NBJ4 EBI-712073,EBI-297353 P62491 EBI-745098,EBI-297353 P46098-2 EBI-21749217,EBI-297353 Q13635-2 EBI-21717270,EBI-297353 Q6XE38 EBI-21823017,EBI-297353 Q9Y5F2 EBI-21658546,EBI-297353 Q15303 EBI-80371,EBI-297353 P02533 EBI-297353,EBI-702178 P10809 EBI-297353,EBI-352528 P31689 EBI-297353,EBI-347834 P68104 EBI-297353,EBI-352162 Q99959 EBI-297353,EBI-702235 Q04695 EBI-297353,EBI-297873 P13647 EBI-297353,EBI-702187 P05141 EBI-297353,EBI-355133 P22681 EBI-297353,EBI-518228 P10412 EBI-297353,EBI-358163 Q14289 EBI-297353,EBI-298640 P29317 EBI-297353,EBI-702104 Q9NR50 EBI-297353,EBI-702257 Q96EY1 EBI-297353,EBI-356767 P40855 EBI-297353,EBI-594747 P61978 EBI-297353,EBI-304185 P02538 EBI-297353,EBI-702198 P49023 EBI-297353,EBI-702209 P62807 EBI-297353,EBI-354552 P52597 EBI-297353,EBI-352986 P04264 EBI-297353,EBI-298429 Q14974 EBI-297353,EBI-286758 P98172 EBI-297353,EBI-538287 Q13191 EBI-297353,EBI-744027 P62258 EBI-297353,EBI-356498 Q14192 EBI-297353,EBI-701903 P31949 EBI-297353,EBI-701862 P07947 EBI-297353,EBI-515331 Q07065 EBI-297353,EBI-702400 Q9UBB4 EBI-297353,EBI-702390 Q14134 EBI-297353,EBI-702370 Q96AG4 EBI-297353,EBI-358888 Q9H5V8 EBI-297353,EBI-1019736 Q07912 EBI-297353,EBI-603457 O75815 EBI-297353,EBI-702336 Q969Z0 EBI-297353,EBI-702328 P06576 EBI-297353,EBI-356231 O43592 EBI-297353,EBI-286683 P54760 EBI-297353,EBI-702121 P0CG47 EBI-297353,EBI-413034 P55060 EBI-297353,EBI-286709 P56945 EBI-297353,EBI-702093 P07437 EBI-297353,EBI-350864 P22682 EBI-640919,EBI-297353 O00443 EBI-297353,EBI-641094 P68431 EBI-297353,EBI-79722 P13987 EBI-297353,EBI-297972 P98083 EBI-297353,EBI-300201 Q17R13 EBI-457220,EBI-297353 GO:0016324 GO:0009925 GO:0016323 GO:0030054 GO:0009986 GO:0030665 GO:0005737 GO:0031901 GO:0030139 GO:0005789 GO:0005768 GO:0010008 GO:0005615 GO:0005925 GO:0000139 GO:0005887 GO:0016020 GO:0045121 GO:0097489 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0043235 GO:0070435 GO:0045202 GO:0051015 GO:0005524 GO:0051117 GO:0045296 GO:0005516 GO:0003682 GO:0003690 GO:0019899 GO:0048408 GO:0005006 GO:0042802 GO:0005178 GO:0004709 GO:0019901 GO:0019903 GO:0004713 GO:0004714 GO:0004888 GO:0031625 GO:0001618 GO:0043006 GO:0007202 GO:0048143 GO:0030154 GO:0007166 GO:0098609 GO:0071230 GO:0071276 GO:0071549 GO:0071364 GO:0071392 GO:0071260 GO:0034614 GO:0021795 GO:0007623 GO:0048546 GO:0016101 GO:0001892 GO:0007173 GO:0038128 GO:0061029 GO:0001942 GO:0042743 GO:0007611 GO:0097421 GO:0030324 GO:0010960 GO:0000165 GO:0061024 GO:0007494 GO:0060571 GO:0007275 GO:0043066 GO:1905208 GO:0042059 GO:1901185 GO:0045930 GO:0045746 GO:0042177 GO:0048812 GO:0001503 GO:0042698 GO:0038083 GO:0018108 GO:0097755 GO:0045780 GO:0090263 GO:0030307 GO:0030335 GO:0008284 GO:0045737 GO:0045739 GO:0045740 GO:0050679 GO:0070374 GO:0048146 GO:1900087 GO:0050729 GO:0033674 GO:0043406 GO:1901224 GO:0010750 GO:0033138 GO:0042327 GO:1903800 GO:1902722 GO:0051897 GO:1900020 GO:1903078 GO:0001934 GO:0048661 GO:0032930 GO:0051968 GO:0045944 GO:0045893 GO:0045907 GO:0046777 GO:0051205 GO:2000145 GO:0070372 GO:0046328 GO:0050999 GO:0050730 GO:0014066 GO:0006357 GO:0051592 GO:0033590 GO:0033594 GO:0006970 GO:0070141 GO:0007435 GO:0007165 GO:0043586 GO:0006412 GO:0007169 GO:0042060 MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA 1210 P01112 GTPase HRas, N-terminally processed HRAS 9606 Yes SL-0198 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. UNIPROT P01112 UNIPROT B5BUA0 UNIPROT Q14080 UNIPROT Q6FHV9 UNIPROT Q9BR65 UNIPROT Q9UCE2 PDB 121P PDB 1AA9 PDB 1AGP PDB 1BKD PDB 1CLU PDB 1CRP PDB 1CRQ PDB 1CRR PDB 1CTQ PDB 1GNP PDB 1GNQ PDB 1GNR PDB 1HE8 PDB 1IAQ PDB 1IOZ PDB 1JAH PDB 1JAI PDB 1K8R PDB 1LF0 PDB 1LF5 PDB 1LFD PDB 1NVU PDB 1NVV PDB 1NVW PDB 1NVX PDB 1P2S PDB 1P2T PDB 1P2U PDB 1P2V PDB 1PLJ PDB 1PLK PDB 1PLL PDB 1Q21 PDB 1QRA PDB 1RVD PDB 1WQ1 PDB 1XCM PDB 1XD2 PDB 1XJ0 PDB 1ZVQ PDB 1ZW6 PDB 221P PDB 2C5L PDB 2CE2 PDB 2CL0 PDB 2CL6 PDB 2CL7 PDB 2CLC PDB 2CLD PDB 2EVW PDB 2GDP PDB 2LCF PDB 2LWI PDB 2N42 PDB 2N46 PDB 2Q21 PDB 2QUZ PDB 2RGA PDB 2RGB PDB 2RGC PDB 2RGD PDB 2RGE PDB 2RGG PDB 2UZI PDB 2VH5 PDB 2X1V PDB 3DDC PDB 3I3S PDB 3K8Y PDB 3K9L PDB 3K9N PDB 3KKM PDB 3KKN PDB 3KUD PDB 3L8Y PDB 3L8Z PDB 3LBH PDB 3LBI PDB 3LBN PDB 3LO5 PDB 3OIU PDB 3OIV PDB 3OIW PDB 3RRY PDB 3RRZ PDB 3RS0 PDB 3RS2 PDB 3RS3 PDB 3RS4 PDB 3RS5 PDB 3RS7 PDB 3RSL PDB 3RSO PDB 3TGP PDB 421P PDB 4DLR PDB 4DLS PDB 4DLT PDB 4DLU PDB 4DLV PDB 4DLW PDB 4DLX PDB 4DLY PDB 4DLZ PDB 4DST PDB 4DSU PDB 4EFL PDB 4EFM PDB 4EFN PDB 4G0N PDB 4G3X PDB 4K81 PDB 4L9S PDB 4L9W PDB 4NYI PDB 4NYJ PDB 4NYM PDB 4Q21 PDB 4RSG PDB 4URU PDB 4URV PDB 4URW PDB 4URX PDB 4URY PDB 4URZ PDB 4US0 PDB 4US1 PDB 4US2 PDB 4XVQ PDB 4XVR PDB 521P PDB 5B2Z PDB 5B30 PDB 5E95 PDB 5P21 PDB 5VBE PDB 5VBZ PDB 5WDO PDB 5WDP PDB 5WDQ PDB 5WFO PDB 5WFP PDB 5WFQ PDB 5WFR PDB 5WPL PDB 5X9S PDB 5ZC6 PDB 621P PDB 6AMB PDB 6AXG PDB 6BVI PDB 6BVJ PDB 6BVK PDB 6BVL PDB 6BVM PDB 6CUO PDB 6CUP PDB 6CUR PDB 6D55 PDB 6D56 PDB 6D59 PDB 6D5E PDB 6D5G PDB 6D5H PDB 6D5J PDB 6D5L PDB 6D5M PDB 6D5V PDB 6D5W PDB 6DZH PDB 6E6C PDB 6E6P PDB 6Q21 PDB 721P PDB 821P Pfam PF00071 PROSITE PS51421 OMIM 109800 OMIM 163200 OMIM 188470 OMIM 190020 OMIM 218040 DisGeNET 3265 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}.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. P42337 EBI-641748,EBI-350145 P27986 EBI-79464,EBI-350145 Q12967 EBI-350145,EBI-365861 O15211 EBI-350145,EBI-712355 Q9NZL6 EBI-350145,EBI-365926 Q8WWW0-2 EBI-960502,EBI-350145 Q9NT62-2 EBI-21549195,EBI-350145 Q96SQ9-2 EBI-21537560,EBI-350145 P18827 EBI-2855248,EBI-350145 P04049 EBI-365996,EBI-350145 P05783 EBI-297888,EBI-350145 P42684 EBI-1102694,EBI-350145 Q13671 EBI-350145,EBI-366017 Q03385 EBI-923705,EBI-350145 Q13671-1 EBI-366030,EBI-350145 Q9EQZ6 EBI-772212,EBI-350145 Q9UQ13 EBI-993879,EBI-350145 P20936 EBI-1026476,EBI-350145 Q03386 EBI-1026899,EBI-350145 Q07889 EBI-297487,EBI-350145 P21359 EBI-1172917,EBI-350145 Q86Z23 EBI-12062109,EBI-350145 P09067 EBI-3893317,EBI-350145 P08678 EBI-5364,EBI-350145 Q13503 EBI-394678,EBI-350145 P53611 EBI-536715,EBI-350145 Q53EQ6 EBI-10748977,EBI-350145 Q8N5S1 EBI-21587304,EBI-350145 Q16288-2 EBI-21583219,EBI-350145 Q6PEY0 EBI-21551278,EBI-350145 P26842 EBI-520729,EBI-350145 P21453 EBI-2681920,EBI-350145 Q9NRW4-2 EBI-21542510,EBI-350145 Q8TBF2 EBI-7280826,EBI-350145 O00141 EBI-1042854,EBI-350145 O95620-2 EBI-21824577,EBI-350145 P13995 EBI-1058895,EBI-350145 P15056 EBI-365980,EBI-350145 P54277 EBI-2893308,EBI-350145 Q0VAA5 EBI-350145,EBI-21824821 Q15392 EBI-5457558,EBI-350145 Q16850 EBI-2680495,EBI-350145 Q9H0R4-2 EBI-21692182,EBI-350145 Q9Y277-2 EBI-21506455,EBI-350145 Q8WTQ1 EBI-21825134,EBI-350145 Q9UN70 EBI-2681692,EBI-350145 Q8NFB2 EBI-21757569,EBI-350145 O14880 EBI-724754,EBI-350145 Q04631 EBI-602447,EBI-350145 Q7Z569 EBI-350145,EBI-349900 Q9Z0S9 EBI-476965,EBI-350145 P10398 EBI-350145,EBI-365961 GO:0005737 GO:0005829 GO:0098978 GO:0005794 GO:0000139 GO:0005654 GO:0048471 GO:0005886 GO:0019003 GO:0005525 GO:0003924 GO:0008022 GO:0044877 GO:0009887 GO:0007050 GO:0007166 GO:0071480 GO:0090398 GO:0006935 GO:0042832 GO:0006897 GO:0048013 GO:0097193 GO:0001889 GO:0000165 GO:0007093 GO:0008285 GO:0010629 GO:0034260 GO:0043524 GO:2000251 GO:0030335 GO:0008284 GO:0045740 GO:0050679 GO:0070374 GO:0043547 GO:0032729 GO:0046330 GO:0043406 GO:0043410 GO:2000630 GO:0010863 GO:0001934 GO:0090314 GO:0046579 GO:1900029 GO:0045944 GO:0090303 GO:0007265 GO:0048169 GO:0098696 GO:0035900 GO:0007165 GO:0002223 GO:0050852 GO:0042088 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS 189 P03185 Nuclear egress protein 2 NEC2 10377 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P03185 UNIPROT Q777G7 Pfam PF04541 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}. P0CK47 EBI-2620196,EBI-2620189 P04275 EBI-981819,EBI-2620196 P28799 EBI-2620196,EBI-747754 Q9NSC5 EBI-2620196,EBI-748420 O75094 EBI-2620196,EBI-2622593 Q99873 EBI-2620196,EBI-78738 GO:0044201 GO:0016021 GO:0046765 MASPEERLLDELNNVIVSFLCDSGSLEVERCSGAHVFSRGSSQPLCTVKLRHGQIYHLEFVYKFLAFKLKNCNYPSSPVFVISNNGLATTLRCFLHEPSGLRSGQSGPCLGLSTDVDLPKNSIIMLGQDDFIKFKSPLVFPAELDLLKSMVVCRAYITEHRTTMQFLVFQAANAQKASRVMDMISDMSQQLSRSGQVEDTGARVTGGGGPRPGVTHSGCLGDSHVRGRGGWDLDNFSEAETEDEASYAPWRDKDSWSESEAAPWKKELVRHPIRRHRTRETRRMRGSHSRVEHVPPETRETVVGGAWRYSWRATPYLARVLAVTAVALLLMFLRWT 336 P03215 Envelope glycoprotein M gM 10377 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P03215 UNIPROT Q777D4 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVYITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLHFLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMVLGAVNLFLILPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLIRICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSEEEIFP 405 P03246 E1B protein, small T-antigen E1BS 28285 No SL-0415 SL-0416 Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. UNIPROT P03246 Pfam PF01691 PROSITE PS50062 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. GO:0044203 GO:0020002 GO:0016020 GO:0019050 MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRRQEQSPWNPRAGLDPRE 176 P03248 E1B protein, small T-antigen E1BS 10519 No SL-0415 SL-0416 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}. UNIPROT P03248 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 MEVWAILEDLRQTRLLLENASDGVSGLWRFWFGGDLARLVFRIKQDYREEFEKLLDDIPGLFEALNLGHQAHFKEKVLSVLDFSTPGRTAAAVAFLTFILDKWIRQTHFSKGYVLDFIAAALWRTWKARRMRTILDYWPVQPLGVAGILRHPPTMPAVLQEEQQEDNPRAGLDPPVEE 178 P03263 I-leader protein LEAD 10515 Yes SL-0382 Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:3005631}. Note=Might be loosely associated with the nuclear membrane. UNIPROT P03263 Pfam PF03052 DE Reference Proteome: Yes; GO:0044220 MRADREELDLPPPVGGVAVDVVKVEVPATGRTLVLAFVKTCAVLAAVHGLYILHEVDLTTAHKEAEWEFEPLAWRVWLVVFYFGCLSLTVWLLEGSYGGSDHHAARAQSPDVRARRSELDDNIAQMGAVHGLELPRRQVLRHRGT 145 P03600 RNA-directed RNA polymerase POL1 928299 Yes SL-0382 [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}. UNIPROT P03600 Pfam PF00548 Pfam PF00680 Pfam PF00910 PROSITE PS51874 PROSITE PS50507 PROSITE PS51218 [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}. GO:0044165 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0008234 GO:0003723 GO:0003724 GO:0003968 GO:0039690 GO:0070613 GO:0018144 GO:0018259 GO:0006351 GO:0019082 GO:0039694 MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAYAFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQLLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMTWGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPGEKDNAQSSPVILLEGLAGQMQNFCETTLVSVGKTCTAVNAISTCCGNLKALAGRILGMLRDFIWKTLGFETRFLADASLLFGEDVDGWLKAISDLRDQFIAKSYCSQDEMMQILVLLEKGRQMRKSGLSKGGISPAIINLILKGINDLEQLNRSCSVQGVRGVRKMPFTIFFQGKSRTGKSLLMSQVTKDFQDHYGLGGETVYSRNPCDQYWSGYRRQPFVLMDDFAAVVTEPSAEAQMINLISSAPYPLNMAGLEEKGICFDSQFVFVSTNFLEVSPEAKVRDDEAFKNRRHVIVQVSNDPAKAYDAANFASNQIYTILAWKDGRYNTVCVIEDYDELVAYLLTRSQQHAEEQEKNLANMMKSATFESHFKSLVEVLELGSMISAGFDIIRPEKLPSEAKEKRVLYSIPYNGEYCNALIDDNYNVTCWFGECVGNPEQLSKYSEKMLLGAYEFLLCSESLNVVIQAHLKEMVCPHHYDKELNFIGKIGETYYHNQMVSNIGSMQKWHRAILFGIGVLLGKEKEKTWYQVQVANVKQALYDMYTKEIRDWPMPIKVTCGIVLAAIGGSAFWKVFQQLVGSGNGPVLMGVAAGAFSAEPQSRKPNRFDMQQYRYNNVPLKRRVWADAQMSLDQSSVAIMSKCRANLVFGGTNLQIVMVPGRRFLACKHFFTHIKTKLRVEIVMDGRRYYHQFDPANIYDIPDSELVLYSHPSLEDVSHSCWDLFCWDPDKELPSVFGADFLSCKYNKFGGFYEAQYADIKVRTKKECLTIQSGNYVNKVSRYLEYEAPTIPEDCGSLVIAHIGGKHKIVGVHVAGIQGKIGCASLLPPLEPIAQAQGAEEYFDFLPAEENVSSGVAMVAGLKQGVYIPLPTKTALVETPSEWHLDTPCDKVPSILVPTDPRIPAQHEGYDPAKSGVSKYSQPMSALDPELLGEVANDVLELWHDCAVDWDDFGEVSLEEALNGCEGVEYMERIPLATSEGFPHILSRNGKEKGKRRFVQGDDCVVSLIPGTTVAKAYEELEASAHRFVPALVGIECPKDEKLPMRKVFDKPKTRCFTILPMEYNLVVRRKFLNFVRFIMANRHRLSCQVGINPYSMEWSRLAARMKEKGNDVLCCDYSSFDGLLSKQVMDVIASMINELCGGEDQLKNARRNLLMACCSRLAICKNTVWRVECGIPSGFPMTVIVNSIFNEILIRYHYKKLMREQQAPELMVQSFDKLIGLVTYGDDNLISVNAVVTPYFDGKKLKQSLAQGGVTITDGKDKTSLELPFRRLEECDFLKRTFVQRSSTIWDAPEDKASLWSQLHYVNCNNCEKEVAYLTNVVNVLRELYMHSPREATEFRRKVLKKVSWITSGDLPTLAQLQEFYEYQRQQGGADNNDTCDLLTSVDLLGPPLSFEKEAMHGCKVSEEIVTKNLAYYDFKRKGEDEVVFLFNTLYPQSSLPDGCHSVTWSQGSGRGGLPTQSWMSYNISRKDSNINKIIRTAVSSKKRVIFCARDNMVPVNIVALLCAVRNKLMPTAVSNATLVKVMENAKAFKFLPEEFNFAFSDV 1866 P04288 Envelope glycoprotein M gM 10299 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P04288 UNIPROT B9VQD7 UNIPROT Q09IC3 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0044220 GO:0016021 GO:0019031 GO:0055036 MGRPAPRGSPDSAPPTKGMTGARTAWWVWCVQVATFVVSAVCVTGLLVLASVFRARFPCFYATASSYAGVNSTAEVRGGVAVPLRLDTQSLVGTYVITAVLLLAVAVYAVVGAVTSRYDRALDAGRRLAAARMAMPHATLIAGNVCSWLLQITVLLLAHRISQLAHLVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLMELAPTHHRVVGPARAVLTNALLLGVFLCTADAAVSLNTIAAFNFNFSAPGMLICLTVLFAILVVSLLLVVEGVLCHYVRVLVGPHLGAVAATGIVGLACEHYYTNGYYVVETQWPGAQTGVRVALALVAAFALGMAVLRCTRAYLYHRRHHTKFFMRMRDTRHRAHSALKRVRSSMRGSRDGRHRPAPGSPPGIPEYAEDPYAISYGGQLDRYGDSDGEPIYDEVADDQTDVLYAKIQHPRHLPDDDPIYDTVGGYDPEPAEDPVYSTVRRW 473 P04406 Glyceraldehyde-3-phosphate dehydrogenase GAPDH 9606 Yes SL-0198 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}. UNIPROT P04406 UNIPROT E7EUT4 UNIPROT P00354 UNIPROT Q53X65 PDB 1U8F PDB 1ZNQ PDB 2FEH PDB 3GPD PDB 4WNC PDB 4WNI PDB 6ADE PDB 6IQ6 Pfam PF02800 Pfam PF00044 PROSITE PS00071 OMIM 138400 DisGeNET 2597 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}. P00533 EBI-354056,EBI-297353 Self EBI-354056,EBI-354056 P28482 EBI-959949,EBI-354056 P32121 EBI-714559,EBI-354056 P42771 EBI-375053,EBI-354056 O15264 EBI-2116951,EBI-354056 Q5S007 EBI-5323863,EBI-354056 P00441 EBI-354056,EBI-990792 P04075 EBI-709613,EBI-354056 P02730 EBI-7576138,EBI-354056 P04920 EBI-1390787,EBI-354056 P02730-2 EBI-20795597,EBI-354056 P13569 EBI-349854,EBI-354056 P48147 EBI-1049962,EBI-354056 Q13043 EBI-367376,EBI-354056 P42858 EBI-354056,EBI-466029 Q15303 EBI-80371,EBI-354056 P04626 EBI-641062,EBI-354056 Q60823 EBI-400263,EBI-354056 Q9H492 EBI-720768,EBI-354056 P49768 EBI-354056,EBI-297277 Q9H0R8 EBI-746969,EBI-354056 O95166 EBI-712001,EBI-354056 P60520 EBI-720116,EBI-354056 Q3KSU8 EBI-354056,EBI-2621128 Q06187 EBI-624835,EBI-354056 P43351 EBI-706448,EBI-354056 P03372 EBI-78473,EBI-354056 Q9GZQ8 EBI-373144,EBI-354056 P35228 EBI-6662224,EBI-354056 P05109 EBI-354056,EBI-355281 P06702 EBI-354056,EBI-1055001 Q00325 EBI-354056,EBI-358549 P62805 EBI-354056,EBI-302023 P36895 EBI-2551936,EBI-354056 O35071 EBI-2366194,EBI-354056 P51451 EBI-2105445,EBI-354056 Q96FW1 EBI-1058491,EBI-354056 Q8N2N9-3 EBI-354056,EBI-11053866 Q96G25 EBI-354056,EBI-394405 Q8NG31-2 EBI-354056,EBI-10973816 Q96FC7 EBI-748888,EBI-354056 Q9H6K4 EBI-8477908,EBI-354056 Q9Y2Z9 EBI-718148,EBI-354056 Q99807 EBI-11017131,EBI-354056 O75489 EBI-1224896,EBI-354056 Q8TB22 EBI-372221,EBI-354056 Q9NQH7 EBI-1171467,EBI-354056 P25705 EBI-351437,EBI-354056 Q9C002 EBI-3905285,EBI-354056 Q9HAC7 EBI-21929540,EBI-354056 Q96HJ9 EBI-16769656,EBI-354056 O00483 EBI-1049381,EBI-354056 O00746 EBI-744871,EBI-354056 Q8N3Z0 EBI-20628340,EBI-354056 Q3MIX3 EBI-3923548,EBI-354056 P0C7P0 EBI-11150788,EBI-354056 Q15051 EBI-2805823,EBI-354056 P15336 EBI-1170906,EBI-354056 P18084 EBI-354056,EBI-1223434 P04487 EBI-6150681,EBI-354056 P0C1C6 EBI-6151657,EBI-354056 P03496 EBI-2547442,EBI-354056 P19320 EBI-6189824,EBI-354056 Q13617 EBI-456179,EBI-354056 Q13620 EBI-456067,EBI-354056 Q15843 EBI-716247,EBI-354056 Q7L5N1 EBI-486838,EBI-354056 Q13616 EBI-359390,EBI-354056 Q92905 EBI-594661,EBI-354056 Q13618 EBI-456129,EBI-354056 Q86VP6 EBI-456077,EBI-354056 O00141 EBI-354056,EBI-1042854 Q9H0J4 EBI-1053637,EBI-354056 P10599 EBI-354056,EBI-594644 O60739 EBI-354056,EBI-1043343 O95292 EBI-1188298,EBI-354056 Q16526 EBI-741297,EBI-354056 O75602 EBI-354056,EBI-20850469 O95425 EBI-354056,EBI-487145 Q5VST9-6 EBI-354056,EBI-10989451 Q502W7 EBI-354056,EBI-20845787 P48751 EBI-354056,EBI-20805570 Q00535 EBI-354056,EBI-1041567 A1A4G5 EBI-354056,EBI-12104738 Q5TZA2 EBI-354056,EBI-3923672 P57740 EBI-354056,EBI-295687 Q99442 EBI-354056,EBI-949221 Q8NFJ5 EBI-354056,EBI-2561555 Q6A163 EBI-354056,EBI-11958242 O76041 EBI-354056,EBI-2880203 Q69YH5 EBI-354056,EBI-6911908 Q13283 EBI-1047359,EBI-354056 Q63HK5 EBI-354056,EBI-9053916 Q5T6S3 EBI-354056,EBI-2339674 Q6P1J9 EBI-354056,EBI-930143 O95139 EBI-354056,EBI-1053340 O15015 EBI-354056,EBI-745608 A8MT65 EBI-354056,EBI-20869384 Q03936 EBI-354056,EBI-12176441 P04908 EBI-354056,EBI-358971 P0DTD1 EBI-25475880,EBI-354056 P0DTC3 EBI-25475894,EBI-354056 P0DTD3 EBI-25475917,EBI-354056 Q9UBX2 EBI-11600078,EBI-354056 P48039 EBI-1188238,EBI-354056 Q00537 EBI-624648,EBI-354056 Q13164 EBI-1213983,EBI-354056 Q6IQ23 EBI-2125301,EBI-354056 Q92696 EBI-9104196,EBI-354056 Q9BZE9-2 EBI-354056,EBI-21554613 O14556 EBI-354056,EBI-1057431 Q15915 EBI-11963196,EBI-354056 P15927 EBI-621404,EBI-354056 Q9NXU5 EBI-354056,EBI-711759 Q9BX70 EBI-354056,EBI-710091 Q16363 EBI-354056,EBI-711505 Q15102 EBI-354056,EBI-711522 Q9UN74 EBI-354056,EBI-712273 O00231 EBI-354056,EBI-357816 P50453 EBI-354056,EBI-711626 P04183 EBI-354056,EBI-712550 O43504 EBI-354056,EBI-713382 Q06830 EBI-354056,EBI-353193 Q99558 EBI-354056,EBI-358011 O43353 EBI-354056,EBI-358522 Q9UHD2 EBI-354056,EBI-356402 P20333 EBI-354056,EBI-358983 Q99759 EBI-354056,EBI-307281 Q13077 EBI-354056,EBI-359224 P60709 EBI-353944,EBI-354056 Q13268 EBI-354324,EBI-354056 Q04864 EBI-354056,EBI-307352 Q92993 EBI-399080,EBI-354056 GO:0005737 GO:0005829 GO:0070062 GO:0097452 GO:0043231 GO:0005811 GO:0016020 GO:0015630 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:1990904 GO:0031982 GO:0019828 GO:0097718 GO:0004365 GO:0042802 GO:0008017 GO:0051287 GO:0050661 GO:0035605 GO:0061844 GO:0061621 GO:0071346 GO:0050832 GO:0006094 GO:0006096 GO:0051873 GO:0031640 GO:0000226 GO:0010951 GO:0017148 GO:0051402 GO:0035606 GO:0052501 GO:0050715 GO:0050821 GO:0016241 MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE 335 P04492 E1B protein, small T-antigen E1BS 28282 Yes SL-0415 SL-0416 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}. UNIPROT P04492 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 MELETVLQSFQSVRQLLQYTSKNTSGFWRYLFGSTLSKVVNRVKEDYREEFENILADCPGLLASLDLCYHLVFQEKVVRSLDFSSVGRTVASIAFLATILDKWSEKSHLSWDYMLDYMSMQLWRAWLKRRVCIYSLARPLTMPPLPTLQEEKEEERNPAVVEK 163 P04876 Matrix protein M 11278 No SL-0415 SL-0418 Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. UNIPROT P04876 Pfam PF06326 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}. GO:0044200 GO:0019031 GO:0055036 GO:0039660 GO:0039657 GO:0039522 GO:0039702 MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKSFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEEEASGAWVLDSVRHSKWASLASSF 237 P04888 Matrix protein M 696863 Yes SL-0415 SL-0418 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}. UNIPROT P04888 UNIPROT Q91DS1 Pfam PF06326 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}. GO:0044200 GO:0019031 GO:0055036 GO:0039660 GO:0039702 MSTLRKLFGIKKSKGTPPTYEETLATAPVLMDTHDTHSHSLQWMRYHVELDVKLDTPLKTMSDLLGLLKNWDVDYKGSRNKRRFYRLIMFRCALELKHVSGTYSVDGSALYSNKVQGSCYVPHRFGQMPPFKREIEVFRYPVHQHGYNGMVDLRMSICDLNGEKIGLNLLKECQVAHPNHFQKYLEEVGLEAACSATGEWILDWTFPMPVDVVPRVPSLFMGD 223 P05129 Protein kinase C gamma type PRKCG 9606 Yes SL-0198 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}. UNIPROT P05129 UNIPROT B7Z8Q0 PDB 2E73 PDB 2UZP Pfam PF00130 Pfam PF00168 Pfam PF00069 Pfam PF00433 PROSITE PS51285 PROSITE PS50004 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 PROSITE PS00479 PROSITE PS50081 OMIM 176980 OMIM 605361 DisGeNET 5582 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}.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. O95831 EBI-949799,EBI-356440 Q9NRD5 EBI-949799,EBI-79165 Q86UR1 EBI-949814,EBI-949799 O00471 EBI-949799,EBI-949824 Q8TD31 EBI-949834,EBI-949799 P17252 EBI-1383528,EBI-949799 P08238 EBI-352572,EBI-949799 O60256 EBI-949799,EBI-724960 O95816 EBI-949799,EBI-355275 P05141 EBI-949799,EBI-355133 P07900 EBI-949799,EBI-296047 P10809 EBI-949799,EBI-352528 P11142 EBI-949799,EBI-351896 P11908 EBI-949799,EBI-4290895 P17066 EBI-949799,EBI-355106 P48741 EBI-949799,EBI-877656 P31689 EBI-949799,EBI-347834 P31948 EBI-949799,EBI-1054052 P36776 EBI-949799,EBI-357448 P60891 EBI-949799,EBI-749195 P68371 EBI-949799,EBI-351356 Q00325 EBI-949799,EBI-358549 Q14257 EBI-949799,EBI-356710 Q14558 EBI-949799,EBI-724449 Q16543 EBI-949799,EBI-295634 Q16822 EBI-949799,EBI-2825219 Q58FF8 EBI-949799,EBI-2961708 Q9BQ70 EBI-949799,EBI-745182 Q9Y6Y0 EBI-949799,EBI-715774 P04792 EBI-949799,EBI-352682 P11413 EBI-949799,EBI-4289891 Q14766 EBI-949799,EBI-947693 GO:0044305 GO:0005911 GO:0005829 GO:0030425 GO:0005634 GO:0048471 GO:0005886 GO:0099524 GO:0014069 GO:0099523 GO:0097060 GO:0005524 GO:0004698 GO:0004672 GO:0004697 GO:0004674 GO:0004712 GO:0008270 GO:0007268 GO:0007635 GO:0060384 GO:0035556 GO:0007611 GO:0043524 GO:1901799 GO:0042177 GO:0031397 GO:0018105 GO:0016310 GO:0030168 GO:0032425 GO:0099171 GO:0046777 GO:0006468 GO:0042752 GO:0050764 GO:0032095 GO:2000300 GO:0043278 GO:0048265 GO:1990911 GO:0048511 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 697 P05480 Neuronal proto-oncogene tyrosine-protein kinase Src Src 10090 Yes SL-0198 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}. UNIPROT P05480 UNIPROT Q2M4I4 PDB 6F3F Pfam PF07714 Pfam PF00017 Pfam PF00018 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50001 PROSITE PS50002 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}. Q8T4F7 EBI-298680,EBI-466810 Q4ACU6 EBI-771450,EBI-298680 Q3UHD9 EBI-771911,EBI-298680 Q8C180 EBI-298680,EBI-6880000 Q9QWI6 EBI-775592,EBI-298680 Q01973 EBI-298680,EBI-6082337 P54763 EBI-298680,EBI-537711 P19367 EBI-713162,EBI-298680 P52789 EBI-741469,EBI-298680 P35438 EBI-400084,EBI-298680 Q01097 EBI-400125,EBI-298680 Q9CQV8 EBI-771608,EBI-298680 P16054 EBI-298451,EBI-298680 P07141 EBI-777188,EBI-298680 GO:0005884 GO:0005901 GO:0030054 GO:0005737 GO:0005856 GO:0005829 GO:0031234 GO:0005925 GO:0098978 GO:0005770 GO:0005764 GO:0016020 GO:0005743 GO:0005739 GO:0043005 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0002102 GO:0014069 GO:0099091 GO:0032587 GO:0005524 GO:0070700 GO:0050839 GO:0071253 GO:0019899 GO:0046875 GO:0030331 GO:0070851 GO:0020037 GO:0005158 GO:0005178 GO:0044325 GO:0016301 GO:0019900 GO:0004715 GO:0051219 GO:0008022 GO:0019904 GO:0004672 GO:0019901 GO:0005080 GO:0004713 GO:0044877 GO:0097110 GO:0042169 GO:0005102 GO:0031625 GO:0032148 GO:0034332 GO:0086098 GO:0045453 GO:0060444 GO:0007155 GO:0007049 GO:0030154 GO:0016477 GO:0008283 GO:0098609 GO:0071398 GO:0071498 GO:0070301 GO:0071456 GO:0032869 GO:0071222 GO:0071375 GO:0036120 GO:0071393 GO:0034614 GO:0071560 GO:0007173 GO:0030900 GO:0007229 GO:0035556 GO:2000811 GO:0043066 GO:0043154 GO:2001237 GO:0051895 GO:2001243 GO:0051902 GO:0031333 GO:0051974 GO:0032211 GO:0045892 GO:0048011 GO:0042476 GO:0048477 GO:0036035 GO:0018105 GO:0038083 GO:0018108 GO:0016310 GO:0043065 GO:0090263 GO:0045785 GO:0045737 GO:0050715 GO:0035306 GO:2000573 GO:0010634 GO:0070374 GO:0010628 GO:0010907 GO:0046628 GO:1902533 GO:2000394 GO:0043406 GO:2000386 GO:0050731 GO:0043552 GO:2000588 GO:0071803 GO:0031954 GO:0051897 GO:1900182 GO:0010954 GO:0071902 GO:0051222 GO:0051057 GO:0014911 GO:0045893 GO:0001545 GO:0050847 GO:0046777 GO:0031648 GO:0006468 GO:2001286 GO:0042127 GO:0060491 GO:0022407 GO:2000641 GO:0010632 GO:0033146 GO:0098962 GO:0043393 GO:0010447 GO:0051602 GO:0070555 GO:0009612 GO:0051385 GO:0031667 GO:0009615 GO:0043149 GO:0034446 GO:0045056 GO:0007179 GO:0007169 GO:0060065 MGSNKSKPKDASQRRRSLEPSENVHGAGGAFPASQTPSKPASADGHRGPSAAFVPPAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTRKVDVREGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 541 P05769 RNA-directed RNA polymerase NS5 POLG 301478 No SL-0382 [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}. UNIPROT P05769 UNIPROT Q9Q9F7 PDB 2PX2 PDB 2PX4 PDB 2PX5 PDB 2PX8 PDB 2PXA PDB 2PXC PDB 2V8O PDB 2WV9 Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0075512 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKHLTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCWIRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDSTKATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGDSCITIMAADKPTLDIRMMNIEATNLALVRNYCYAATVSDVSTVSNCPTTGESHNTKRADHNYLCKRGVTDRGWGNGCGLFGKGSIDTCAKFTCSNSAAGRLILPEDIKYEVGVFVHGSTDSTSHGNYSTQIGANQAVRFTISPNAPAITAKMGDYGEVTVECEPRSGLNTEAYYVMTIGTKHFLVHREWFNDLLLPWTSPASTEWRNREILVEFEEPHATKQSVVALGSQEGALHQALAGAIPVEFSSSTLKLTSGHLKCRVKMEKLKLKGTTYGMCTEKFTFSKNPADTGHGTVVLELQYTGSDGPCKIPISSVASLNDMTPVGRMVTANPYVASSTANAKVLVEIEPPFGDSYIVVGRGDKQINHHWHKEGSSIGKAFSTTLKGAQRLAALGDTAWDFGSVGGVFNSIGKAVHQVFGGAFRTLFGGMSWISPGLLGALLLWMGVNARDKSIALAFLATGGVLLFLATNVHADTGCAIDITRRELKCGSGIFIHNDVEAWIDRYKYLPETPKQLAKVVENAHKSGICGIRSVNRFEHQMWESVRDELNALLKENAIDLSVVVEKQKGMYRAAPNRLRLTVEELDIGWKAWGKSLLFAAELANSTFVVDGPETAECPNSKRAWNSFEIEDFGFGITSTRGWLKLREENTSECDSTIIGTAVKGNHAVHSDLSYWIESGLNGTWKLERAIFGEVKSCTWPETHTLWGDAVEETELIIPVTLAGPRSKHNRREGYKVQVQGPWDEEDIKLDFDYCPGTTVTVSEHCGKRGPSVRTTTDSGKLVTDWCCRSCTLPPLRFTTASGCWYGMEIRPMKHDESTLVKSRVQAFNGDMIDPFQLGLLVMFLATQEVLRKRWTARLTLPAAVGALLVLLLGGITYTDLVRYLILVGSAFAESNNGGDVIHLALIAVFKVQPAFLVASLTRSRWTNQENLVLVLGAAFFQMAASDLELTIPGLLNSAATAWMVLRAMAFPSTSAIAMPMLAMLAPGMRMLHLDTYRIVLLLIGICSLLNERRRSVEKKKGAVLIGLALTSTGYFSPTIMAAGLMICNPNKKRGWPATEVLTAVGLMFAIVGGLAELDIDSMSVPFTIAGLMLVSYVISGKATDMWLERAADVSWEAGAAITGTSERLDVQLDDDGDFHLLNDPGVPWKIWVLRMTCLSVAAITPRAILPSAFGYWLTLKYTKRGGVFWDTPSPKVYPKGDTTPGVYRIMARGILGRYQAGVGVMHEGVFHTLWHTTRGAAIMSGEGRLTPYWGNVKEDRVTYGGPWKLDQKWNGVDDVQMIVVEPGKPAINVQTKPGIFKTAHGEIGAVSLDYPIGTSGSPIVNSNGEIIGLYGNGVILGNGAYVSAIVQGERVEEPVPEAYNPEMLKKRQLTVLDLHPGAGKTRRILPQIIKDAIQKRLRTAVLAPTRVVAAEMAEALRGLPVRYLTPAVQREHSGNEIVDVMCHATLTHRLMSPLRVPNYNLFVMDEAHFTDPASIAARGYIATRVEAGEAAAIFMTATPPGTSDPFPDTNSPVHDVSSEIPDRAWSSGFEWITDYAGKTVWFVASVKMSNEIAQCLQRAGKRVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILDEGEGRVILSVPSAITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTMLAHWTEAKILLDNIHLPNGLVAQLYGPERDKTYTMDGEYRLRGEERKTFLELIKTADLPVWLAYKVASNGIQYNDRKWCFDGPRSNIILEDNNEVEIITRIGERKVLKPRWLDARVYSDHQSLKWFKDFAAGKRSAIGFFEVLGRMPEHFAGKTREALDTMYLVATSEKGGKAHRMALEELPDALETITLIAALGVMTAGFFLLMMQRKGIGKLGLGALVLVVATFFLWMSDVSGTKIAGVLLLALLMMVVLIPEPEKQRSQTDNQLAVFLICVLLVVGLVAANEYGMLERTKTDIRNLFGKSLIEENEVHIPPFDFFTLDLKPATAWALYGGSTVVLTPLIKHLVTSQYVTTSLASINAQAGSLFTLPKGIPFTDFDLSVALVFLGCWGQVTLTTLIMATILVTLHYGYLLPGWQAEALRAAQKRTAAGIMKNAVVDGIVATDVPELERTTPQMQKRLGQILLVLASVAAVCVNPRITTIREAGILCTAAALTLWDNNASAAWNSTTATGLCHVMRGSWIAGASIAWTLIKNAEKPAFKRGRAGGRTLGEQWKEKLNAMGKEEFFSYRKEAILEVDRTEARRARREGNKVGGHPVSRGTAKLRWLVERRFVQPIGKVVDLGCGRGGWSYYAATMKNVQEVRGYTKGGPGHEEPMLMQSYGWNIVTMKSGVDVFYKPSEISDTLLCDIGESSPSAEIEEQRTLRILEMVSDWLSRGPKEFCIKILCPYMPKVIEKLESLQRRFGGGLVRVPLSRNSNHEMYWVSGASGNIVHAVNMTSQVLIGRMDKKIWKGPKYEEDVNLGSGTRAVGKGVQHTDYKRIKSRIEKLKEEYAATWHTDDNHPYRTWTYHGSYEVKPSGSASTLVNGVVRLLSKPWDAITGVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPQGVKTVMDETTNWLWAYLARNKKARLCTREEFVKKVNSHAALGAMFEEQNQWKNAREAVEDPKFWEMVDEERECHLRGECRTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWMSRENSGGGVEGAGIQKLGYILRDVAQKPGGKIYADDTAGWDTRITQADLENEAKVLELMEGEQRTLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEAVIGPDDIESIERKKKFAVRTWLFENAEERVQRMAVSGDDCVVKPLDDRFSTALHFLNAMSKVRKDIQEWKPSQGWYDWQQVPFCSNHFQEVIMKDGRTLVVPCRGQDELIGRARISPGSGWNVRDTACLAKAYAQMWLVLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWILENEWMEDKTTVSDWTEVPYVGKREDIWCGSLIGTRTRATWAENIYAAINQVRSVIGKEKYVDYVQSLRRYEETHVSEDRVL 3434 P05783 Keratin, type I cytoskeletal 18 KRT18 9606 Yes SL-0198 Cytoplasm, perinuclear region. Nucleus, nucleolus. UNIPROT P05783 UNIPROT Q53G38 UNIPROT Q5U0N8 UNIPROT Q9BW26 Pfam PF00038 PROSITE PS00226 PROSITE PS51842 OMIM 148070 OMIM 215600 DisGeNET 3875 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}.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. O15027 EBI-357515,EBI-297888 O75190 EBI-297888,EBI-1053164 P01112 EBI-297888,EBI-350145 Self EBI-297888,EBI-297888 Q8NFJ9 EBI-297888,EBI-1805484 Q96RK4 EBI-297888,EBI-1805814 Q9BXC9 EBI-297888,EBI-748297 Q8IWZ6 EBI-1806001,EBI-297888 Q15628 EBI-359215,EBI-297888 P05787 EBI-297888,EBI-297852 Q99816 EBI-297888,EBI-346882 Q9BQ69 EBI-297888,EBI-5324932 P13569 EBI-349854,EBI-297888 Q14108 EBI-1564650,EBI-297888 P04792 EBI-297888,EBI-352682 Q96CS2 EBI-297888,EBI-2514791 Q08379 EBI-618309,EBI-297888 P61981 EBI-297888,EBI-359832 Q8NFA0 EBI-2511075,EBI-297888 P28799 EBI-297888,EBI-747754 Q9Y6K9 EBI-297888,EBI-81279 Q14094 EBI-297888,EBI-1104653 Q9NUX5 EBI-297888,EBI-752420 Q9D7I8 EBI-11048238,EBI-297888 P63167 EBI-349105,EBI-297888 Q8IYE0-2 EBI-10247802,EBI-297888 P15336 EBI-1170906,EBI-297888 P19320 EBI-6189824,EBI-297888 P02751 EBI-1220319,EBI-297888 Q14161 EBI-1046878,EBI-297888 Q5VU43 EBI-297888,EBI-1105124 P52292 EBI-349938,EBI-297888 O43913 EBI-374928,EBI-297888 Q96GM5 EBI-297888,EBI-358489 Q92837 EBI-3934879,EBI-297888 Q99757 EBI-2932492,EBI-297888 Q6PKC3 EBI-749812,EBI-297888 Q8N2W9 EBI-297888,EBI-473160 Q96MU7 EBI-2849854,EBI-297888 Q09472 EBI-297888,EBI-447295 Q99459 EBI-297888,EBI-374880 P02671 EBI-348571,EBI-297888 P27348 EBI-359854,EBI-297888 P05452 EBI-297888,EBI-1047626 P23508 EBI-297888,EBI-307531 O75688 EBI-297888,EBI-1047039 Q9BVR6 EBI-741889,EBI-297888 P19012 EBI-297888,EBI-739566 O14964 EBI-740220,EBI-297888 Q9Y5B8 EBI-744782,EBI-297888 O95751 EBI-740738,EBI-297888 Q8IYI6 EBI-742102,EBI-297888 Q15834 EBI-739674,EBI-297888 A0A087WXM9 EBI-297888,EBI-20740139 P08670 EBI-297888,EBI-353844 Q5HYC2 EBI-297888,EBI-948754 Q15149 EBI-297888,EBI-297903 Q96M95 EBI-297888,EBI-747041 Q12860 EBI-297888,EBI-5564336 Q8WWL7 EBI-297888,EBI-767764 P48668 EBI-2564105,EBI-297888 Q9NY99 EBI-8556870,EBI-297888 Q66PJ3 EBI-297888,EBI-2683099 Q8WYP5 EBI-297888,EBI-396018 Q8IYB4 EBI-297888,EBI-15749355 P01730 EBI-297888,EBI-353826 Q9Y616 EBI-297888,EBI-447690 Q5JVL4 EBI-297888,EBI-743105 A0A0S2Z505 EBI-297888,EBI-16437709 P07196 EBI-297888,EBI-475646 A0A0S2Z4Q4 EBI-297888,EBI-16429135 Q9NX04 EBI-8643161,EBI-297888 P02538 EBI-297888,EBI-702198 Q3SY84 EBI-297888,EBI-2952676 Q14533 EBI-297888,EBI-739648 Q8TD31-3 EBI-297888,EBI-10175300 Q9P2K3-2 EBI-297888,EBI-1504830 Q9BVG8-5 EBI-297888,EBI-14069005 Q8WW24 EBI-297888,EBI-750487 Q5XKE5 EBI-297888,EBI-2514135 O75022 EBI-2830524,EBI-297888 Q8N0S2 EBI-6872807,EBI-297888 P62993 EBI-401755,EBI-297888 P29353 EBI-297888,EBI-78835 GO:0005912 GO:0071944 GO:0034451 GO:0005737 GO:0005829 GO:0070062 GO:0005882 GO:0045095 GO:0005815 GO:0005730 GO:0048471 GO:0098641 GO:0003723 GO:0097110 GO:0005198 GO:0009653 GO:0007049 GO:0070268 GO:0097191 GO:0043000 GO:0097284 GO:0045104 GO:0031424 GO:0043066 GO:0033209 GO:0016032 MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSNSMQTIQKTTTRRIVDGKVVSETNDTKVLRH 430 P06105 Protein SCP160 SCP160 559292 Yes SL-0178 SL-0182 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. UNIPROT P06105 UNIPROT D6VWA3 Pfam PF00013 PROSITE PS50084 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. P10591 EBI-8591,EBI-16374 P53863 EBI-29183,EBI-16374 P11484 EBI-8627,EBI-16374 P10592 EBI-8603,EBI-16374 P02829 EBI-16374,EBI-8659 P38788 EBI-16374,EBI-24570 P40150 EBI-8632,EBI-16374 P32589 EBI-8648,EBI-16374 P15108 EBI-16374,EBI-8666 P31539 EBI-16374,EBI-8050 P25491 EBI-10420,EBI-16374 P32527 EBI-16374,EBI-29684 P46997 EBI-26138,EBI-16374 P25294 EBI-16374,EBI-17244 P38934 EBI-3593,EBI-16374 P16140 EBI-16374,EBI-20254 P36008 EBI-16374,EBI-6329 P02994 EBI-16374,EBI-6314 P26783 EBI-16374,EBI-16150 P32905 EBI-16374,EBI-16032 P05317 EBI-16374,EBI-15447 P26321 EBI-16374,EBI-15398 P49626 EBI-16374,EBI-15394 P14120 EBI-16374,EBI-15333 P41805 EBI-16374,EBI-15270 P16861 EBI-16374,EBI-9428 P32501 EBI-16374,EBI-6270 P15790 EBI-16374,EBI-9533 P38011 EBI-16374,EBI-7405 P34160 EBI-745,EBI-16374 P38285 EBI-20853,EBI-16374 Q12476 EBI-31475,EBI-16374 P32357 EBI-340,EBI-16374 P15646 EBI-6838,EBI-16374 P39960 EBI-3517,EBI-16374 P06101 EBI-4266,EBI-16374 P23293 EBI-17078,EBI-16374 P36041 EBI-16374,EBI-26995 GO:0005623 GO:0000781 GO:0005737 GO:0005783 GO:0005789 GO:0000329 GO:0031965 GO:0042175 GO:0005844 GO:0001965 GO:0003729 GO:0003723 GO:0043577 GO:0030466 GO:0006348 GO:0007059 GO:0045141 GO:0000750 MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKPAVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVAANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYLKKLASNLDEEKVKIPSKFQFLIDAEELKEKYNVIVTFPSTPDDELVSFVGLRDKVGEAITYARSSSKSYVVESLDISKAHSKNLTHAKNLIMYFTKYSVLKGLEESHPNVKISLPSIQSLPTAETVTIHISAKSDEANDIKAVRKELISFVNNIPPSETLVITDLDYELFGGSIKHCLLASESSVAFVQFGDYYPNDNSILLVALTEDEDFKPSIEEIQASLNKANESLNSLRTKQNNMETKTYEFSEEVQDSLFKPSSATWKLIMEDISEQEGHLQIKLHTPEENQLTVRGDEKAAKAANKIFESILNSPSSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVTLTGLEYNLTHAKKYLAAEAKKWADIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLDFEMENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAAKRVESIVAEASDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGGEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKDAENSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRENFDREVDVPASIYEYVSERGAFIQKLRMDLSVNVRFGNTSKKANKLARAPIEIPLEKVCGSTEGENAEKTKFTIEEVGAPTSSEEGDITMRLTYEPIDLSSILSDGEEKEVTKDTSNDSAKKEEALDTAVKLIKERIAKAPSATYAGYVWGADTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMVLKSLRR 1222 P06704 Cell division control protein 31 CDC31 559292 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Spindle pole body, SPB half- bridge. UNIPROT P06704 UNIPROT D6W2V8 PDB 2DOQ PDB 2GV5 PDB 3FWB PDB 3FWC PDB 4MBE Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. Q00684 EBI-4192,EBI-4259 P14832 EBI-5463,EBI-4259 P32472 EBI-2883297,EBI-4259 Q02959 EBI-8484,EBI-4259 P02293 EBI-8088,EBI-4259 Q02796 EBI-30514,EBI-4259 Q02206 EBI-16204,EBI-4259 P38890 EBI-24263,EBI-4259 P25302 EBI-18626,EBI-4259 P11484 EBI-4259,EBI-8627 P10591 EBI-4259,EBI-8591 Q06677 EBI-4259,EBI-30084 P32447 EBI-3003,EBI-4259 Q07457 EBI-31563,EBI-4259 P26448 EBI-3824,EBI-4259 P38915 EBI-17964,EBI-4259 Q12060 EBI-8287,EBI-4259 P39723 EBI-20675,EBI-4259 Q04477 EBI-27228,EBI-4259 P46675 EBI-18471,EBI-4259 P50102 EBI-19863,EBI-4259 Q6WNK7 EBI-1251050,EBI-4259 Q99181 EBI-4259,EBI-8579 P38305 EBI-20939,EBI-4259 GO:0005737 GO:0005825 GO:0005815 GO:0044732 GO:0005643 GO:0070390 GO:0005509 GO:0042802 GO:0008017 GO:0051301 GO:0051028 GO:0043161 GO:0015031 GO:0043549 GO:0030474 MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS 161 P06782 Carbon catabolite-derepressing protein kinase SNF1 559292 Yes SL-0178 SL-0182 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}. UNIPROT P06782 UNIPROT D6VTA0 PDB 2FH9 PDB 2QLV PDB 3DAE PDB 3HYH PDB 3MN3 PDB 3T4N PDB 3TDH PDB 3TE5 Pfam PF16579 Pfam PF00069 Pfam PF08587 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. Q84VQ1 EBI-2042415,EBI-17516 Q9SCY5 EBI-2042436,EBI-17516 Q42384 EBI-17516,EBI-1382964 P12904 EBI-17537,EBI-17516 P32562 EBI-4440,EBI-17516 P34164 EBI-17516,EBI-17187 P10591 EBI-8591,EBI-17516 P11484 EBI-17516,EBI-8627 P25491 EBI-10420,EBI-17516 P39987 EBI-22339,EBI-17516 P09435 EBI-17516,EBI-8611 P02829 EBI-17516,EBI-8659 P32589 EBI-17516,EBI-8648 P31539 EBI-17516,EBI-8050 P11792 EBI-16703,EBI-17516 P30822 EBI-20589,EBI-17516 Q99750 EBI-724076,EBI-17516 Q9BQ66 EBI-17516,EBI-739863 Q9UKT9 EBI-747204,EBI-17516 P50222 EBI-748397,EBI-17516 P14373 EBI-17516,EBI-719493 O43597 EBI-742487,EBI-17516 P54619 EBI-1181439,EBI-17516 P32578 EBI-17516,EBI-17179 Q00816 EBI-17516,EBI-8270 P38990 EBI-17516,EBI-12863 Q04739 EBI-17516,EBI-7244 P22204 EBI-5569,EBI-17516 P32598 EBI-13715,EBI-17516 P07270 EBI-13378,EBI-17516 P36047 EBI-16783,EBI-17516 P14693 EBI-17516,EBI-24602 GO:0005623 GO:0000144 GO:0005737 GO:0005739 GO:0005641 GO:0031965 GO:0031588 GO:0005634 GO:0005774 GO:0004679 GO:0005086 GO:0005524 GO:0042802 GO:0004672 GO:0004674 GO:0005975 GO:0007155 GO:0006995 GO:0000132 GO:0071940 GO:0035556 GO:0001403 GO:0017148 GO:1900436 GO:0045722 GO:0016239 GO:2000222 GO:0006468 GO:0001302 GO:0006986 GO:0090606 MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLKPHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANKSVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRANMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNEKIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN 633 P07663 Period circadian protein per 7227 Yes SL-0198 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. UNIPROT P07663 UNIPROT O17483 UNIPROT O76882 UNIPROT O76883 UNIPROT O76884 UNIPROT O76885 UNIPROT Q24446 UNIPROT Q24447 UNIPROT Q24448 UNIPROT Q24449 UNIPROT Q6PVA3 UNIPROT Q8MLY0 UNIPROT Q9GN20 UNIPROT Q9GN51 UNIPROT Q9GQH9 UNIPROT Q9GV48 UNIPROT Q9GV53 UNIPROT Q9GV54 UNIPROT Q9GV55 UNIPROT Q9W4X0 PDB 1WA9 PDB 3GEC PDB 3RTY Pfam PF00989 PROSITE PS50112 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}. O77059 EBI-496170,EBI-94117 Self EBI-496170,EBI-496170 Q7JWQ7 EBI-89424,EBI-496170 Q26416 EBI-176027,EBI-496170 P49021 EBI-266295,EBI-496170 P49021-3 EBI-266326,EBI-496170 P33438 EBI-496159,EBI-496170 Q9VB55 EBI-184355,EBI-496170 Q9VXJ0 EBI-85627,EBI-496170 P11996 EBI-124104,EBI-496170 Q9VTW8 EBI-131131,EBI-496170 Q9VLX9 EBI-179831,EBI-496170 O61735 EBI-496170,EBI-143834 Q24533 EBI-147892,EBI-496170 O76324 EBI-496170,EBI-189923 GO:0044297 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0042802 GO:0046982 GO:0042803 GO:0003712 GO:0003714 GO:0001222 GO:0008134 GO:0000976 GO:0001306 GO:0048148 GO:0048512 GO:0032922 GO:0007623 GO:0042745 GO:0060086 GO:0007620 GO:0007619 GO:0008340 GO:0008062 GO:0009649 GO:0043153 GO:0045475 GO:0007616 GO:0045433 GO:0007617 GO:0000122 GO:2000678 GO:0045892 GO:0042752 GO:0045187 GO:1904059 GO:0001932 GO:0009416 GO:0006979 GO:0009266 GO:0007622 MEGGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKGAGQGAGQAQTLISASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQAIEQLQQEEEEDQSGSESEADRVEGVAKSEAAQSFPIPSPLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSFCCVISMHDGIVLYTTPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRGLKSGGFGVIGRPVSYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAAVSALGYLPQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVNPWSRKLEFVVGHHRVFQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPAELDPPKTEPPEPRGTCVSGASGPMSPVHEGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGNGTNSGTGTGTASSSKGGTAAIPPVTLTESLLNKHNDEMEKFMLKKHRESRGRTGEKSKKSANDTLKMLEYSGPGHGIKRGGSHSWEGEANKPKQQLTLGTDAIKGAAGSAGGAVGTGGVGSGGAGVAGGGGSGTGVAGTPEGRATTTSGTGTPGGAGGGGGAGAAAAAGASSSVGSSTPGPSSYPTCTQNINLWPPFSVGITPPVHSTHTAMAQSSFSSAGLFPTFYYIPASLTPTSPTRSPRMHKHPHKGGTDMPTTSQQAAAAAAQAMPLQYMAGVMYPHPSLFYTHPAAAAATAMMYQPMPFPGMANALQIPERPLGSQSAYNKSVYTTTPASMTKKVPGAFHSVTTPAQVQRPSSQSASVKTEPGSSAAVSDPCKKEVPDSSPIPSVMGDYNSDPPCSSSNPANNKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDPKHRKLKSMSTSESKIMEHPEEDQTQHGDG 1224 P07948 Tyrosine-protein kinase Lyn LYN 9606 Yes SL-0198 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. UNIPROT P07948 UNIPROT A0AVQ5 PDB 1W1F PDB 1WA7 PDB 3A4O PDB 5XY1 PDB 6NMW Pfam PF07714 Pfam PF00017 Pfam PF00018 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50001 PROSITE PS50002 OMIM 165120 DisGeNET 4067 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}.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. O92972 EBI-79452,EBI-710506 P00533 EBI-79452,EBI-297353 Self EBI-79452,EBI-79452 P10275 EBI-79452,EBI-608057 Q13480 EBI-79452,EBI-517684 P10721 EBI-79452,EBI-1379503 P08581 EBI-79452,EBI-1039152 Q05397 EBI-79452,EBI-702142 P05556 EBI-703066,EBI-79452 P13612 EBI-79452,EBI-703044 P48023 EBI-495538,EBI-79452 Q80X56 EBI-2553252,EBI-79452 O95684 EBI-1266334,EBI-79452 P35579 EBI-350338,EBI-79452 Q86X19 EBI-11343485,EBI-79452 Q61879 EBI-400918,EBI-79452 Q9D620 EBI-8399105,EBI-79452 Q9NQW6 EBI-2553589,EBI-79452 Q9WUM4 EBI-8316222,EBI-79452 Q9UHB6 EBI-351479,EBI-79452 Q80X90 EBI-688023,EBI-79452 Q9D6P8 EBI-11062253,EBI-79452 Q9H0B6 EBI-726994,EBI-79452 P11049 EBI-6139068,EBI-79452 P29350 EBI-78260,EBI-79452 P08238 EBI-352572,EBI-79452 A0A2S9PK33 EBI-2865067,EBI-79452 Q7CJG3 EBI-79452,EBI-2844548 P46527 EBI-79452,EBI-519280 Q8R5G7 EBI-79452,EBI-621463 Q9NRA0 EBI-79452,EBI-985324 Q8CI15 EBI-79452,EBI-985291 Q9JIA7 EBI-985434,EBI-79452 P11802 EBI-79452,EBI-295644 Q5U3Y8 EBI-7618036,EBI-79452 Q969Q1 EBI-79452,EBI-5661333 Q9BYV6 EBI-79452,EBI-2341179 O43172 EBI-79452,EBI-718395 P06493 EBI-79452,EBI-444308 P07900 EBI-79452,EBI-296047 P08631 EBI-79452,EBI-346340 P09769 EBI-79452,EBI-1383732 P15924 EBI-79452,EBI-355041 Q16543 EBI-79452,EBI-295634 Q8IX12 EBI-79452,EBI-356265 Q9NWB6 EBI-79452,EBI-2808785 Q9UQ35 EBI-79452,EBI-1050142 Q6P2Q9 EBI-79452,EBI-538479 Q9BUQ8 EBI-79452,EBI-540096 Q58FF7 EBI-79452,EBI-9996483 P29144 EBI-79452,EBI-1044672 P68400 EBI-79452,EBI-347804 Q8NEV1 EBI-79452,EBI-21265922 P84090 EBI-79452,EBI-711389 Q02413 EBI-79452,EBI-1045757 Q12874 EBI-79452,EBI-1051880 Q15029 EBI-79452,EBI-357897 Q15428 EBI-79452,EBI-2462271 Q15459 EBI-79452,EBI-1054743 Q8IWX8 EBI-79452,EBI-2555370 Q99873 EBI-79452,EBI-78738 Q9Y2W1 EBI-79452,EBI-352039 Q13115 EBI-6591081,EBI-79452 P33993 EBI-355924,EBI-79452 Q71U36 EBI-302552,EBI-79452 Q08857 EBI-8346984,EBI-79452 P16671 EBI-2808214,EBI-79452 Q9QWY8-1 EBI-698517,EBI-79452 Q9QWY8-2 EBI-698524,EBI-79452 P26660 EBI-79452,EBI-706322 P27958 EBI-706378,EBI-79452 Q913V3 EBI-79452,EBI-10052968 Q9WMX2 EBI-710918,EBI-79452 Q99759 EBI-79452,EBI-307281 P67870 EBI-348169,EBI-79452 P20273 EBI-78277,EBI-79452 Q9HCN6 EBI-79452,EBI-515278 Q07666 EBI-1364,EBI-79452 GO:0005737 GO:0005829 GO:0070062 GO:0031234 GO:0098978 GO:0005794 GO:0034666 GO:0043231 GO:0042629 GO:0045121 GO:0030061 GO:0005758 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0099091 GO:0005524 GO:0019899 GO:0046875 GO:0043015 GO:0043208 GO:0005178 GO:0044325 GO:0016301 GO:0004715 GO:0051219 GO:0140031 GO:0005161 GO:0004713 GO:0017124 GO:0005102 GO:0031625 GO:0002250 GO:0001782 GO:0050853 GO:0007596 GO:0030154 GO:0006974 GO:0031668 GO:0034605 GO:0071300 GO:0050663 GO:0097028 GO:0048013 GO:0030218 GO:0002774 GO:0002431 GO:0038095 GO:0038096 GO:0060397 GO:0002553 GO:0002768 GO:0045087 GO:0035556 GO:0050900 GO:0031663 GO:0030889 GO:0008285 GO:0070373 GO:0050777 GO:1902532 GO:0043407 GO:0070667 GO:0002762 GO:0001933 GO:0034136 GO:0034144 GO:0031175 GO:0014003 GO:0038083 GO:0018108 GO:0030168 GO:0002576 GO:1902961 GO:0030335 GO:0008284 GO:0051272 GO:2000670 GO:0060369 GO:0060252 GO:0070668 GO:0010976 GO:0070447 GO:0043552 GO:0014068 GO:0001934 GO:0046579 GO:0070304 GO:0042531 GO:0046777 GO:0006468 GO:0002902 GO:0050855 GO:0033628 GO:0042127 GO:0001817 GO:0050707 GO:0070372 GO:0045646 GO:0050727 GO:0033003 GO:0043304 GO:0090025 GO:0090330 GO:0001932 GO:0051279 GO:0043200 GO:0048678 GO:0009743 GO:0042493 GO:0009725 GO:0032868 GO:0014070 GO:0006991 GO:0009636 GO:0007165 GO:0002223 GO:0031295 GO:0002513 GO:0034142 GO:0007169 GO:0016032 MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP 512 P08325 Matrix protein M 11283 Yes SL-0415 SL-0418 Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. UNIPROT P08325 PDB 2W2R Pfam PF06326 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}. GO:0044200 GO:0019031 GO:0055036 GO:0039660 GO:0039657 GO:0039522 GO:0039702 MSSFKKILGLSSKSHKKSKKMGLPPPYDESCPMETQPSAPLSNDFFGMEDMDLYDKDSLRYEKFRFMLKMTVRSNKPFRSYDDVTAAVSQWDNSYIGMVGKRPFYKIIAVIGSSHLQATPAVLADLNQPEYYATLTGRCFLPHRLGLIPPMFNVQETFRKPFNIGLYKGTLDFTFTVSDDESNEKVPHVWDYMNPKYQSQIQQEGLKFGLILSKKATGTWVLDQLSPFK 229 P08928 Lamin Dm0 Lam 7227 Yes SL-0178 SL-0179 SL-0180 SL-0182 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}. UNIPROT P08928 UNIPROT Q9VMQ0 Pfam PF00038 Pfam PF00932 PROSITE PS51842 PROSITE PS51841 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}. Self EBI-188444,EBI-188444 Q9GQN4 EBI-149669,EBI-188444 Q9VPX2 EBI-3433683,EBI-188444 M9NFI9 EBI-9933576,EBI-188444 Q8IPM8 EBI-129885,EBI-188444 Q24247 EBI-187829,EBI-188444 Q9V9S0 EBI-117239,EBI-188444 Q9VMV9 EBI-182234,EBI-188444 Q9VMT1 EBI-3430567,EBI-188444 P23226 EBI-239813,EBI-188444 Q8IQX8 EBI-3432029,EBI-188444 Q9VT04 EBI-125572,EBI-188444 Q8SXF0 EBI-195791,EBI-188444 P34082 EBI-868243,EBI-188444 P16568 EBI-188444,EBI-112159 P25028 EBI-188444,EBI-106103 O01382 EBI-188444,EBI-91422 P20240 EBI-115143,EBI-188444 Q9XTM1 EBI-188444,EBI-96207 Q9VD23 EBI-188444,EBI-187890 Q8T3J9 EBI-188444,EBI-139759 Q9VAU6 EBI-188444,EBI-184493 P52295 EBI-145898,EBI-188444 Q9VR64 EBI-146474,EBI-188444 GO:0005737 GO:0005638 GO:0005635 GO:0005641 GO:0005637 GO:0005652 GO:0005634 GO:0000922 GO:0003682 GO:0005102 GO:0005200 GO:0008344 GO:0007569 GO:0007417 GO:0040003 GO:0006342 GO:0001745 GO:0048546 GO:0035262 GO:0070870 GO:0007112 GO:0007110 GO:0007084 GO:0008285 GO:0050777 GO:0006998 GO:0071763 GO:0007097 GO:0031081 GO:0006997 GO:0030838 GO:2000433 GO:1900182 GO:1905832 GO:0090435 GO:0048137 GO:0007283 GO:0007430 MSSKSRRAGTATPQPGNTSTPRPPSAGPQPPPPSTHSQTASSPLSPTRHSRVAEKVELQNLNDRLATYIDRVRNLETENSRLTIEVQTTRDTVTRETTNIKNIFEAELLETRRLLDDTARDRARAEIDIKRLWEENEELKNKLDKKTKECTTAEGNVRMYESRANELNNKYNQANADRKKLNEDLNEALKELERLRKQFEETRKNLEQETLSRVDLENTIQSLREELSFKDQIHSQEINESRRIKQTEYSEIDGRLSSEYDAKLKQSLQELRAQYEEQMQINRDEIQSLYEDKIQRLQEAAARTSNSTHKSIEELRSTRVRIDALNANINELEQANADLNARIRDLERQLDNDRERHGQEIDLLEKELIRLREEMTQQLKEYQDLMDIKVSLDLEIAAYDKLLVGEEARLNITPATNTATVQSFSQSLRNSTRATPSRRTPSAAVKRKRAVVDESEDHSVADYYVSASAKGNVEIKEIDPEGKFVRLFNKGSEEVAIGGWQLQRLINEKGPSTTYKFHRSVRIEPNGVITVWSADTKASHEPPSSLVMKSQKWVSADNTRTILLNSEGEAVANLDRIKRIVSQHTSSSRLSRRRSVTAVDGNEQLYHQQGDPQQSNEKCAIM 622 P09216 Protein kinase C epsilon type Prkce 10116 Yes SL-0198 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}. UNIPROT P09216 PDB 1GMI Pfam PF00130 Pfam PF00168 Pfam PF00069 Pfam PF00433 PROSITE PS51285 PROSITE PS50004 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 PROSITE PS00479 PROSITE PS50081 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}. P15336 EBI-1170906,EBI-6049581 P48442 EBI-6140357,EBI-6049581 GO:0071944 GO:0005737 GO:0005856 GO:0005829 GO:0005783 GO:0098978 GO:0000139 GO:0016020 GO:0005739 GO:0031594 GO:0005634 GO:0048471 GO:0005886 GO:0099523 GO:0030315 GO:0071889 GO:0003785 GO:0005524 GO:0004698 GO:0004699 GO:0008047 GO:0019899 GO:0035276 GO:0046872 GO:0019901 GO:0004697 GO:0004674 GO:0017124 GO:0030546 GO:0005102 GO:0007155 GO:0007049 GO:0051301 GO:0071361 GO:0071456 GO:0036120 GO:0071380 GO:0035556 GO:0031663 GO:0035641 GO:0002281 GO:0043066 GO:0051562 GO:0010917 GO:0031397 GO:0051280 GO:0018105 GO:0030838 GO:0010811 GO:2001031 GO:0032467 GO:0010634 GO:0010763 GO:0043123 GO:0032024 GO:0050996 GO:0043410 GO:0070257 GO:0032230 GO:0090303 GO:0006468 GO:0061178 GO:0019216 GO:0050730 GO:0051279 GO:2000300 GO:0043278 GO:0035669 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLAAGAESPQPASGNSPSEDDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRASSSTDGQLASPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSGFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHSKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKMKPPFKPRIKTKRDVNNFDQDFTREEPILTLVDEAIVKQINQEEFKGFSYFGEDLMP 737 P09280 Nuclear egress protein 2 NEC2 10338 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P09280 Pfam PF04541 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}. GO:0044201 GO:0016021 MSRRTYVRSERRRGCGDNLLQRIRLVVPSALQCCDGDLPIFDPQRPPARCVFQFNGEDNVSEAFPVEYIMRLMANWAQVDCDPYIKIQNTGVSVLFQGFFFRPTNAPVAEVSIDSNNVILSSTLSTGINLSALESIKRGGGIDRRPLQALMWVNCFVRMPYVQLSFRFMGPEDPSRTIKLMARATDAYMYKETGNNLDEYIRWRPSFRSPPENGSPNTSVQMQSDIKPALPDTQTTRVWKLALPVANVTYALFIVIVLVVVLGAVLFWK 269 P09283 Nuclear egress protein 1 NEC1 10338 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P09283 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MHLKPTRFFHANQPPMPHSYEMEDLCFDDMQYRWSPSNTPYRSMSRRYKSVSRSGPSMRVRSRTPCRRQTIRGKLMSKERSVYRHYFNYIARSPPEELATVRGLIVPIIKTTPVTLPFNLGQTVADNCLSLSGMGYHLGLGGYCPTCTASGEPRLCRTDRAALILAYVQQLNNIYEYRVFLASILALSDRANMQAASAEPLLSSVLAQPELFFMYHIMREGGMRDIRVLFYRDGDAGGFMMYVIFPGKSVHLHYRLIDHIQAACRGYKIVAHVWQTTFLLSVCRNPEQQTETVVPSIGTSDVYCKMCDLNFDGELLLEYKRLYALFDDFVPPR 333 P09290 Protein UL20 homolog 39 10338 Yes SL-0415 SL-0418 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}. UNIPROT P09290 Pfam PF04544 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}. GO:0044175 GO:0044178 GO:0044200 GO:0020002 GO:0016021 GO:0019012 GO:0019058 MNPPQARVSEQTKDLLSVMVNQHPEEDAKVCKSSDNSPLYNTMVMLSYGGDTDLLLSSACTRTSTVNRSAFTQHSVFYIISTVLIQPICCIFFFFYYKATRCMLLFTAGLLLTILHHFRLIIMLLCVYRNIRSDLLPLSTSQQLLLGIIVVTRTMLFCITAYYTLFIDTRVFFLITGHLQSEVIFPDSVSKILPVSWGPSPAVLLVMAAVIYAMDCLVDTVSFIGPRVWVRVMLKTSISF 240 P09298 Envelope glycoprotein M gM 10338 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P09298 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFNATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWGLLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMAALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSYMDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRTNYPSQGYGYVYENDSTYETDREDELLYERSNSGWE 435 P09917 Arachidonate 5-lipoxygenase ALOX5 9606 Yes SL-0178 SL-0182 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. UNIPROT P09917 UNIPROT B7ZLS0 UNIPROT E5FPY5 UNIPROT E5FPY7 UNIPROT E5FPY8 UNIPROT Q5JQ14 PDB 2ABV PDB 3O8Y PDB 3V92 PDB 3V98 PDB 3V99 Pfam PF00305 Pfam PF01477 PROSITE PS00711 PROSITE PS00081 PROSITE PS51393 PROSITE PS50095 OMIM 152390 DisGeNET 240 Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. {ECO:0000269|PubMed:21233389}. P50221 EBI-2864512,EBI-79934 Q04864 EBI-307352,EBI-79934 Q6UWX4 EBI-79934,EBI-10196655 Q86Y26 EBI-10178410,EBI-79934 Q8IYX8-2 EBI-79934,EBI-10181988 Q8N0S2 EBI-79934,EBI-6872807 Q96MT8 EBI-741977,EBI-79934 Q9Y6D9 EBI-79934,EBI-742610 Q92542-2 EBI-21836984,EBI-79934 Q9Y252 EBI-2341483,EBI-79934 Q15811-2 EBI-79934,EBI-8052395 O94830 EBI-79934,EBI-8444979 Q9UQ49 EBI-79934,EBI-21699246 Q9UPU7 EBI-79934,EBI-2947180 Q9NYA4 EBI-79934,EBI-1052346 Q9BXB4 EBI-79934,EBI-2514786 Q9BWT6 EBI-79934,EBI-11137441 Q96RR4-2 EBI-79934,EBI-21545123 Q96L93-2 EBI-79934,EBI-21618523 Q96C34-2 EBI-79934,EBI-21601272 Q96AD5 EBI-79934,EBI-716499 Q92530 EBI-79934,EBI-945916 Q8WXG6-2 EBI-79934,EBI-21599664 Q8ND83 EBI-79934,EBI-10269374 Q8N3R9-2 EBI-79934,EBI-16399750 Q8IY63-2 EBI-79934,EBI-11041933 Q86SX3-2 EBI-79934,EBI-10989467 Q7Z2K6 EBI-79934,EBI-10976398 Q7LBC6 EBI-79934,EBI-2511832 Q6PJ69 EBI-79934,EBI-2130441 Q6P474 EBI-79934,EBI-1048095 Q6P1M9 EBI-79934,EBI-10252512 Q6P1K2 EBI-79934,EBI-713832 Q4VCS5-2 EBI-79934,EBI-3891843 Q2NKX8 EBI-79934,EBI-1042535 Q15349-2 EBI-79934,EBI-21578316 Q15042 EBI-79934,EBI-1053078 Q14746 EBI-79934,EBI-389449 Q14008-2 EBI-79934,EBI-21500522 Q13615-2 EBI-79934,EBI-21502132 Q13042-2 EBI-79934,EBI-10974085 Q09019 EBI-79934,EBI-724564 Q00653 EBI-79934,EBI-307326 P48449 EBI-79934,EBI-3930711 P30566 EBI-79934,EBI-2511688 P29144 EBI-79934,EBI-1044672 P31025 EBI-1052433,EBI-79934 Q9P0N9 EBI-3258000,EBI-79934 Q8CLD8 EBI-2851532,EBI-79934 Q8D078 EBI-79934,EBI-2840175 Q96MT8-3 EBI-11522539,EBI-79934 A6NGQ2 EBI-18583589,EBI-79934 O43716 EBI-6929453,EBI-79934 Q6PII3 EBI-747830,EBI-79934 Q8IYJ2-2 EBI-13381098,EBI-79934 Q6FHY5 EBI-16439278,EBI-79934 P14061 EBI-12867244,EBI-79934 Q6P2R3 EBI-12696312,EBI-79934 GO:0005829 GO:0005576 GO:0005615 GO:1904813 GO:0005635 GO:0005641 GO:0016363 GO:0031965 GO:0005654 GO:0048471 GO:0034774 GO:0004051 GO:0005506 GO:0019221 GO:0036336 GO:0042593 GO:0006959 GO:0035655 GO:0002232 GO:0002523 GO:1901753 GO:0019370 GO:0006691 GO:0002540 GO:2001301 GO:0019372 GO:0042759 GO:0016525 GO:0001937 GO:0050728 GO:1903573 GO:1903671 GO:0061044 GO:0061045 GO:0043312 GO:0030501 GO:1904999 GO:1900407 GO:1900015 GO:0045598 GO:0050727 GO:0106014 GO:0050796 GO:1903426 MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI 674 P0C044 F protein F 11104 No SL-0382 Host cytoplasm {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. UNIPROT P0C044 Pfam PF01543 DE Reference Proteome: No; GO:0044220 GO:0019028 GO:0005198 MSTNPKPQKKKTNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRERLPSGRNLEVDVSLSPRLVGPRAGPGLSPGTLGPSMAMRAAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA 162 P0C6T8 Non-structural protein 11 1a 233262 No SL-0382 [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}. UNIPROT P0C6T8 UNIPROT Q91A29 Pfam PF16348 Pfam PF11963 Pfam PF01661 Pfam PF16251 Pfam PF09401 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF01831 Pfam PF05409 Pfam PF08715 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}. GO:0033644 GO:0044220 GO:0016021 GO:0004197 GO:0008242 GO:0003723 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0039648 GO:0039548 GO:0039579 GO:0039502 GO:0019079 GO:0019082 MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREIVMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGVCFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYALIRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVAYVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFKGWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWIPILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYFNMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKICHAVVSKSKELLDVSLDSLSAAIHYLNSKIVDLAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRVTFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSLTPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRRVTFKEQPTVNEIASTPKTIKVFYELDKDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLASKLYCAFTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVEMSDFADLESVIQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPANIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKDKLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRVTSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFVKGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPDARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAEKQVVLVSNNQEDFDLISKCQITAVEGTKKLAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGVRTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVNVTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLMLQSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTGVDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQLYDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYNPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVYTNFKLIGHTICDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYFNRPLLVDENKFDVLKVDDVDDGGDISESDAKESKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLTGCRYVVRTANALSMAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISADNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQWIKSTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALYTAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFILFRHVAYGCSKPGCLFCYKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVTDVKQVGCYMRLFYERDGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDKNLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLADSVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKACCKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFLLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGVIRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDLGSTVFNVPTKVLRYGYHVLHFITHALSADGVQCYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTEGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVRIVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILAVIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGTIMPLWFCLLYISVVVSNHAFWVFAYCRRLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDDKVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTVLAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLPVQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQGRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCVISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSINHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCYLFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKDNTVLQALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVWQIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKIVYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYASNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTNQDSYGGASVCIYCRARVEHPDVDGLCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV 4383 P0C6U6 Non-structural protein 11 1a 277944 No SL-0382 [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}. UNIPROT P0C6U6 UNIPROT Q6Q1S3 PDB 2VRI PDB 3TLO PDB 5GWY Pfam PF16348 Pfam PF01661 Pfam PF09401 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF08715 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 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. {ECO:0000269|PubMed:20181693}. [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}. GO:0033644 GO:0044220 GO:0016021 GO:0004197 GO:0008242 GO:0003723 GO:0003968 GO:0036459 GO:0008270 GO:0039520 GO:0039648 GO:0039548 GO:0019079 GO:0019082 MFYNQVTLAVASDSEISGFGFAIPSVAVRTYSEAAAQGFQACRFVAFGLQDCVTGINDDDYVIALTGTNQLCAKILPFSDRPLNLRGWLIFSNSNYVLQDFDVVFGHGAGSVVFVDKYMCGFDGKPVLPKNMWEFRDYFNNNTDSIVIGGVTYQLAWDVIRKDLSYEQQNVLAIESIHYLGTTGHTLKSGCKLTNAKPPKYSSKVVLSGEWNAVYRAFGSPFITNGMSLLDIIVKPVFFNAFVKCNCGSESWSVGAWDGYLSSCCGTPAKKLCVVPGNVVPGDVIITSTSAGCGVKYYAGLVVKHITNITGVSLWRVTAVHSDGMFVASSSYDALLHRNSLDPFCFDVNTLLSNQLRLAFLGASVTEDVKFAASTGVIDISAGMFGLYDDILTNNKPWFVRKASGLFDAIWDAFVAAIKLVPTTTGVLVRFVKSIASTVLTVSNGVIIMCADVPDAFQSVYRTFTQAICAAFDFSLDVFKIGDVKFKRLGDYVLTENALVRLTTEVVRGVRDARIKKAMFTKVVVGPTTEVKFSVIELATVNLRLVDCAPVVCPKGKIVVIAGQAFFYSGGFYRFMVDPTTVLNDPVFTGDLFYTIKFSGFKLDGFNHQFVTASSATDAIIAVELLLLDFKTAVFVYTCVVDGCSVIVRRDATFATHVCFKDCYNVWEQFCIDNCGEPWFLTDYNAILQSNNPQCAIVQASESKVLLERFLPKCPEILLSIDDGHLWNLFVEKFNFVTDWLKTLKLTLTSNGLLGNCAKRFRRVLVKLLDVYNGFLETVCSVAYTAGVCIKYYAVNVPYVVISGFVSRVIRRERCDMTFPCVSCVTFFYEFLDTCFGVSKPNAIDVEHLELKETVFVEPKDGGQFFVSGDYLWYVVDDIYYPASCNGVLPVAFTKLAGGKISFSDDVIVHDVEPTHKVKLIFEFEDDVVTSLCKKSFGKSIIYTGDWEGLHEVLTSAMNVIGQHIKLPQFYIYDEEGGYDVSKPVMISQWPISNDSNGCVVEASTDFHQLECIVDDSVREEVDIIEQPFEEVEHVLSIKQPFSFSFRDELGVRVLDQSDNNCWISTTLVQLQLTKLLDDSIEMQLFKVGKVDSIVQKCYELSHLISGSLGDSGKLLSELLKEKYTCSITFEMSCDCGKKFDDQVGCLFWIMPYTKLFQKGECCICHKMQTYKLVSMKGTGVFVQDPAPIDIDAFPVKPICSSVYLGVKGSGHYQTNLYSFNKAIDGFGVFDIKNSSVNTVCFVDVDFHSVEIEAGEVKPFAVYKNVKFYLGDISHLVNCVSFDFVVNAANENLLHGGGVARAIDILTEGQLQSLSKDYISSNGPLKVGAGVMLECEKFNVFNVVGPRTGKHEHSLLVEAYNSILFENGIPLMPLLSCGIFGVRIENSLKALFSCDINKPLQVFVYSSNEEQAVLKFLDGLDLTPVIDDVDVVKPFRVEGNFSFFDCGVNALDGDIYLLFTNSILMLDKQGQLLDTKLNGILQQAALDYLATVKTVPAGNLVKLFVESCTIYMCVVPSINDLSFDKNLGRCVRKLNRLKTCVIANVPAIDVLKKLLSSLTLTVKFVVESNVMDVNDCFKNDNVVLKITEDGINVKDVVVESSKSLGKQLGVVSDGVDSFEGVLPINTDTVLSVAPEVDWVAFYGFEKAALFASLDVKPYGYPNDFVGGFRVLGTTDNNCWVNATCIILQYLKPTFKSKGLNVLWNKFVTGDVGPFVSFIYFITMSSKGQKGDAEEALSKLSEYLISDSIVTLEQYSTCDICKSTVVEVKSAIVCASVLKDGCDVGFCPHRHKLRSRVKFVNGRVVITNVGEPIISQPSKLLNGIAYTTFSGSFDNGHYVVYDAANNAVYDGARLFSSDLSTLAVTAIVVVGGCVTSNVPTIVSEKISVMDKLDTGAQKFFQFGDFVMNNIVLFLTWLLSMFSLLRTSIMKHDIKVIAKAPKRTGVILTRSFKYNIRSALFVIKQKWCVIVTLFKFLLLLYAIYALVFMIVQFSPFNSLLCGDIVSGYEKSTFNKDIYCGNSMVCKMCLFSYQEFNDLDHTSLVWKHIRDPILISLQPFVILVILLIFGNMYLRFGLLYFVAQFISTFGSFLGFHQKQWFLHFVPFDVLCNEFLATFIVCKIVLFVRHIIVGCNNADCVACSKSARLKRVPLQTIINGMHKSFYVNANGGTCFCNKHNFFCVNCDSFGPGNTFINGDIARELGNVVKTAVQPTAPAYVIIDKVDFVNGFYRLYSGDTFWRYDFDITESKYSCKEVLKNCNVLENFIVYNNSGSNITQIKNACVYFSQLLCEPIKLVNSELLSTLSVDFNGVLHKAYVDVLCNSFFKELTANMSMAECKATLGLTVSDDDFVSAVANAHRYDVLLSDLSFNNFFISYAKPEDKLSVYDIACCMRAGSKVVNHNVLIKESIPIVWGVKDFNTLSQEGKKYLVKTTKAKGLTFLLTFNDNQAITQVPATSIVAKQGAGFKRTYNFLWYVCLFVVALFIGVSFIDYTTTVTSFHGYDFKYIENGQLKVFEAPLHCVRNVFDNFNQWHEAKFGVVTTNSDKCPIVVGVSERINVVPGVPTNVYLVGKTLVFTLQAAFGNTGVCYDFDGVTTSDKCIFNSACTRLEGLGGDNVYCYNTDLIEGSKPYSTLQPNAYYKYDAKNYVRFPEILARGFGLRTIRTLATRYCRVGECRDSHKGVCFGFDKWYVNDGRVDDGYICGDGLIDLLVNVLSIFSSSFSVVAMSGHMLFNFLFAAFITFLCFLVTKFKRVFGDLSYGVFTVVCATLINNISYVVTQNLFFMLLYAILYFVFTRTVRYAWIWHIAYIVAYFLLIPWWLLTWFSFAAFLELLPNVFKLKISTQLFEGDKFIGTFESAAAGTFVLDMRSYERLINTISPEKLKNYAASYNKYKYYSGSASEADYRCACYAHLAKAMLDYAKDHNDMLYSPPTISYNSTLQSGLKKMAQPSGCVERCVVRVCYGSTVLNGVWLGDTVTCPRHVIAPSTTVLIDYDHAYSTMRLHNFSVSHNGVFLGVVGVTMHGSVLRIKVSQSNVHTPKHVFKTLKPGDSFNILACYEGIASGVFGVNLRTNFTIKGSFINGACGSPGYNVRNDGTVEFCYLHQIELGSGAHVGSDFTGSVYGNFDDQPSLQVESANLMLSDNVVAFLYAALLNGCRWWLCSTRVNVDGFNEWAMANGYTSVSSVECYSILAAKTGVSVEQLLASIQHLHEGFGGKNILGYSSLCDEFTLAEVVKQMYGVNLQSGKVIFGLKTMFLFSVFFTMFWAELFIYTNTIWINPVILTPIFCLLLFLSLVLTMFLKHKFLFLQVFLLPTVIATALYNCVLDYYIVKFLADHFNYNVSVLQMDVQGLVNVLVCLFVVFLHTWRFSKERFTHWFTYVCSLIAVAYTYFYSGDFLSLLVMFLCAISSDWYIGAIVFRLSRLIVFFSPESVFSVFGDVKLTLVVYLICGYLVCTYWGILYWFNRFFKCTMGVYDFKVSAAEFKYMVANGLHAPHGPFDALWLSFKLLGIGGDRCIKISTVQSKLTDLKCTNVVLLGCLSSMNIAANSSEWAYCVDLHNKINLCDDPEKAQSMLLALLAFFLSKHSDFGLDGLIDSYFDNSSTLQSVASSFVSMPSYIAYENARQAYEDAIANGSSSQLIKQLKRAMNIAKSEFDHEISVQKKINRMAEQAATQMYKEARSVNRKSKVISAMHSLLFGMLRRLDMSSVETVLNLARDGVVPLSVIPATSASKLTIVSPDLESYSKIVCDGSVHYAGVVWTLNDVKDNDGRPVHVKEITKENVETLTWPLILNCERVVKLQNNEIMPGKLKQKPMKAEGDGGVLGDGNALYNTEGGKTFMYAYISNKADLKFVKWEYEGGCNTIELDSPCRFMVETPNGPQVKYLYFVKNLNTLRRGAVLGFIGATIRLQAGKQTELAVNSGLLTACAFSVDPATTYLEAVKHGAKPVSNCIKMLSNGAGNGQAITTSVDANTNQDSYGGASICLYCRAHVPHPSMDGYCKFKGKCVQVPIGCLDPIRFCLENNVCNVCGCWLGHGCACDRTTIQSVDISYLNEQGVLVQLD 4060 P0C6V1 Non-structural protein 11 1a 11144 Yes SL-0382 [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}. UNIPROT P0C6V1 UNIPROT P19751 Pfam PF16348 Pfam PF11963 Pfam PF01661 Pfam PF16251 Pfam PF09401 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF01831 Pfam PF05409 Pfam PF08715 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}. GO:0033644 GO:0044220 GO:0016021 GO:0004197 GO:0008242 GO:0003723 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0039648 GO:0097264 GO:0039548 GO:0039579 GO:0039502 GO:0019079 GO:0019082 MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVDCSRLPALECCVQSAIIRDIFVDEDPQKVEASTMMALQFGSAVLVKPSKRLSVQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGVCLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPRGKYSCKAYALLRGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELSPVWRDSLDNEVVVAWHVDRDPRAVMRLQTLATVRSIEYVGQPIEDMVDGDVVMREPAHLLAPNAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDTCGFRGWVPGNMMDGFPCPGCCKSYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGGAAYWSPYPGMWLPVIWSSVKSYSYLTYTGVVGCKAIVQETDAICRFLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAEFACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSLMVNFSREVVDMCMDMALLFMHDVKVATKYVKKVTGKVAVRFKALGIAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGVITFIQEVPELVKNFVDKFKTFFKVLIDSMSVSILSGLTVVKTASNRVCLAGSKVYEVVQKSLPAYIMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPSSFEKICIVDKLYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVVFNDKPKVKEVPSTRKIKIIFALDATFDSVLSKACSEFEVDKDVTLDELLDVVLDAVESTLSPCKEHGVIGTKVCALLERLVDDYVYLFDEGGEEVIASRMYCSFSAPDEDCVATDVVYADENQDDDADDPVVLVADTQEEDGVAREQVDSADSEICVAHTGGQEMTEPDVVGSQTPIASAEETEVGEACDREGIAEVKATVCADALDACPDQVEAFDIEKVEDSILSELQTELNAPADKTYEDVLAFDAIYSETLSAFYAVPSDETHFKVCGFYSPAIERTNCWLRSTLIVMQSLPLEFKDLGMQKLWLSYKAGYDQCFVDKLVKSAPKSIILPQGGYVADFAYFFLSQCSFKVHANWRCLKCGMELKLQGLDAVFFYGDVVSHMCKCGNSMTLLSADIPYTFDFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVDGKQIDGKVVTKFNGDKFDFMVGHGMTFSMSPFEIAQLYGSCITPNVCFVKGDVIKVLRRVGAEVIVNPANGRMAHGAGVAGAIAKAAGKAFINETADMVKAQGVCQVGGCYESTGGKLCKKVLNIVGPDARGHGNECYSLLERAYQHINKCDNVVTTLISAGIFSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSFQLAKNLCRDVKFVTNACSSLFSESSFVSSYDVLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGEVFVSSQGKKFGYVQNGSFKEASVSQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIHKGKVFFQYSGLSAADLAAVKDAFGFDEPQLLQYYSMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWRRPGNEFRSGKPLRFVSLVLAKGSFKFNEPSDSTDFIRVELREADLSGATCDLEFICKCGVKQEQRKGVDAVMHFGTLDKSGLVKGYNIACTCGDKLVHCTQFNVPFLICSNTPEGKKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVSKVSEAKGNFTDCLYLKNLKQTFSSVLTTYYLDDVKCVAYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGHDIAEKLNAKLGFDCNSPFMEYKITEWPTATGDVVLASDDLYVSRYSGGCVTFGKPVIWRGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDRRPVPSAVLVTGAASGADASAISTEPGTAKEQKACASDSVEDQIVMEAQKKSSVTTVAVKEVKLNGVKKPVKWNCSVVVNDPTSETKVVKSLSIVDVYDMFLTGCRYVVWTANELSRLINSPTVREYVKWGMSKLIIPANLLLLRDEKQEFVAPKVVKAKAIACYGAVKWFLLYCFSWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPLPMFVGQIVAWVKTTFGVLTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYESINVVQHVVDRRVSFDYISLFKLVVELVIGYSLYTVCFYPLFVLVGMQLLTTWLPEFFMLGTMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMYGCSKPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVNPTDSAYYSVIEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLNAAVFYAQSLYRPMLMVEKKLITTANTGLSVSRTMFDLYVYSLLRHLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFVGCARRKCAIDSDVETKSITKSVMAAVNAGVEVTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQSNVAKAANVACIWSVDAFNQLSADLQHRLRKACVKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRVLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLYASFKVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLVYYRNSKACPVVVAVIDQDIGHTLFNVPTKVLRYGFHVLHFITHAFATDRVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGVMHNASLYSSLVPHVRYNLASSNGYIRFPEVVSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNSSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVQPIDFFALTASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVMHLQWLVMYGAIMPLWFCITYVAVVVSNHALWLFSYCRKIGTDVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYLSLYNKYRYFSGKMDTATYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCVVSVTYGNMTLNGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSDRMSLTVMSYQMQGSLLVLTVTLQNPNTPKYSFGVVKPGETFTVLAAYNGRPQGAFHVVMRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGPYRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLAAIKRLHSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHMLGVTLCALCFVIFAMLLIKHKHLYLTMYIMPVLCTLFYTNYLVVGYKQSFRGLAYAWLSYFVPAVDYTYMDEVLYGVVLLVAMVFVTMRSINHDVFSTMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTDIPQIKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPVIEVSQIQSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSVAFDKLAQLLVVLFANPAAVDSKCLASIEEVSDDYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPPLTSNTLTIIVPDKQVFDQVVDNVYVTYAPNVWHIQSIQDADGAVKQLNEIDVNSTWPLVISANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNIPTQCYYNTTGTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTVRLQAGTATEYASNSAILSLCAFSVDPKKTYLDYIQQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYCRSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNGFGVQV 4474 P0C6W0 Putative 2'-O-methyl transferase rep 693999 Yes SL-0382 [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}. UNIPROT P0C6W0 UNIPROT Q0Q467 Pfam PF13087 Pfam PF16348 Pfam PF06478 Pfam PF01661 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0008270 GO:0039520 GO:0032259 GO:0039648 GO:0039548 GO:0006351 GO:0019082 GO:0039694 MASNHISLAFANDEEISAIGFGSVEEAVSYYSDAAVNGFDQCRFVSLGLQDAVVGVEDDDVVMLITGVTQLRAYLGTFGDRPLNLRGWLLFSNCNYFLEELDLVFGRCGGTTIPVDQFMCGADGAPVIQEGDWTFMDYFQDSNQFTLNGITYVKAWDVDRKPNDYAKQNVTCIRRITYITDHRHVLADGTTMKTARHPKVNKSVVLDSPFDQIYKEVGSPFMGNGSTFVEMLKDPAFFHALITCECGRSEWTVGDWKGYNSLCCNIKCKPITIVTPKAVPGAVVITKAGIGAGLKCYNNVFLKHIIDLVVPGTNLGWGVWRIAKVQSKDDVATSGNVLVDDPEDRLDPCYFGNDGPFATKFKFQLLANSFDDEVKGAIVQGVVHVNTAICDVVKDILGLPWFVKKLGSLVTVMWDQFVAGVQSMKICTLKVVQLAKALSCATMSVVKGVITLVAEVPEIFKRLFYTLTSALKSLCTSSCDALVVAGKSFAKIGDYVLLPSALVRLVSSKVKGKAQSGIKQLQFATVVLGDTHKVESDRVEFSSVNLKMVDEEFPLNPVGHTVAVGNQAFFCSDGLYRFMADRDLVITSPIFKPELELEPIFECDAIPGFPKVAASNVAELCVKVDTLLFNYDKIYKKYSTIIKGDRCYIQCTHTFKAPSYYFDDDEFVELCTKYYKLPDFDAFYNAVHAATDMDQFCALCTSGFEVFIPRVPDCPPILNDIDGGSIWTSFILSVRSATDFIKTLKIDLGLNGVVVFVTKKFRKAGALLQKLYNAFLDTVTSFIKVAGVAFKYCATCVPKIVINGCYHTVTRLFAKDLQIPTEDGVADFNTFNHCVFPVNPTRIETDSLELEEVDFVEPGVDGKLVILDDYSFYSDGTNYYPSDGKGVVASCFKKKGGGVVTISDEVQVRTIDPVYKVRLEYEFEDETLVKVCEKAIGTKLKVTGDWSNLLETLEKAMDVVRQHLDVPDYFVYDEEGGTDLNLTIMVSQWPLSSDSEDDFKAVDDEPNANTDETVDTFAEDVAETQNVQQDVTQDEVEAVCDLVVKATEEGPIEHEELSEDQKEVQQALAFIEDKPVVVKPDVFAFSYASYGGLKVLNQSSNNCWVSSALVQLQLTGLLDSDEMQLFNAGRVSPMVKRCYESQRAIFGSLGDVSACLESLLKDRDGMSITCTIDCGCGPGVRVYENAIFRFTPLKTAFPMGRCLICSKTLMHTITQMKGTGIFCRDATALDVDTLVVKPLCAAVYVGAQDGGHYLTNMYDANMAVDGHGRHPIKFNTINTLCYKDVDWEVSNGSCDVKPFLTYKNIEFYQGELSALLSVNHDFVVNAANEQLSHGGGIAKALDDLTKGELQVLSNQYVSRNGSIKVGSGVLIKCKEHSILNVVGPRKGKHAAELLTKAYTFVFKQKGVPLMPLLSVGIFKVPITESLAAFLACVGDRVCKCFCYTDKERLAIQNFVTSFQTEQPVEPLPVIQEVKGVQLEKPVPDVKVENPCEPFRIEGDAKFYDLTPSMVQSLQVTRLVSFTNSDLCLGSFVRDCDGYVQGSLGGAIANYKKSNPVLPAGNCVTLKCDGFISFTFVILPKEGDTNYEKNFNRAIAKFLKLKGSLLVVVEDSSVFNKISHASVAGYVAKPALVDTLFEAKPVQVVVTQDQRSFHTVELSTSQTYGQQLGDCVVEDKKVTNLKPVSKDKVVSVVPNVDWDKHYGFVDAGIFHTLDHTMFVFDNNVVNGKRVLRTSDNNCWINAVCLQLQFANAKFKPKGLQQLWESYCTGDVAMFVHWLYWITGVEKGEPSDAENTLNIISRFLKPQGSVEMLRATSTTCDGTCSTKRVVSTPVVNASVLKVGLDDGNCVHGLPLVDRVVSVNGTVIITNVGDTPGKPVVATENLLLDGVSYTVFQDSTTGVGHYTVFDKEAKLMFDGDVLKPCDLNVSPVTSVVVCNNKKIVVQDPVKRVELDASKFLDTMNVASEKFFTFGDFVSRNIIVLIVYLFSLLAICFRALKKRDMKVMAGVPERTGIILKRSVKYNYKALKFFFRLKFQYIKVFLKFSLVLYTLYALMFMFIRFTPVGTPICKRYTDGYANSTFDKNDYCGNVLCKICLYGYEELSDFTHTRVIWQHLKDPLIGNILPLFYLVFLIIFGGFFVRIGITYFIMQYINAAGVALGYQDNVWLLHLLPFNSMGNIIVVAFIVTRILLFLKHVLFGCDKPSCIACSKSAKLTRVPLQTILQGVTKSFYVNANGGKKFCKKHNFFCVDCDSYGYGCTFINDVIAPELSNVTKLNVIPTGPATIIIDKVEFSNGFYYLYSGSTFWKYNFDITEAKYACKDVLKNCNILTDFVVFNNSGSNVTQVKNACVYFSQLLCKPIKLVDSALLASLNVDFSANLHKAFVEVLSNSFGKDLSNCSNMNECRESLGLSDVPEEEFSAAVSEAHRYDVLISDVSFNNLIVSYAKPEEKLAVHDIANCMRVGAKVVNHNVLTKDNVPVVWLAKDFIALSEEARKYIVRTTKTKGINFMLTFNDRRMHLTIPTISVANKKGAGLPSLFTRLYSFFWHLCVLIVVLFVATSLLDFSAQVTSDTQYDFKYIENGVLKVFEKPLDCVHNAFVNFNEWHNAKFGSIPTNSRRCPIVVGTSDEVRYIPGVPAGVFLYGKSLIFAMSTIFGTSGLCFDDRGLTDPDSCIFNSACTTLSGIGGRNVYCYREGVVDNAKLYSSLLPHSYYRLMDGNHIVLPEIITRGFGIRTIKTQAMTYCRTGECIDSQAGVCVGLDRFFVYSKTPGSDYVCGTGFFSLLFNVIGMFSNSIPVTVMSGQILLNCVVAFTAVMACFAFTKFKRLFGDMSFGVLSVGLCTVVNNLSYVVTQNSIGMLAYATLYFLCTKGVRYSWVWHVGFAISYCFLAPWWVVLAYLICALLEFLPNLFKLKVSTQLFEGDKFVGSFESAASGTFVLDMHSYQKLANSISTEKLKQYCASYNRYKYYSGSASEADYRLACFAHLAKAMSDFANDHMDKLYTPPTVSYNSTLQAGLRKMAQPSGIVEGCIVRVSYGNLTLNGLWLGDTVICPRHVIASNTTNVIDYDHAMSLVRLHNFSISSGNMFLGVISASMRGTLLHIKVNQSNVNTPNYTYKVLKPGDSFNILACYDGSAAGVYGVNMRTNYTIRGSFISGACGSPGYNINNGVVEFCYMHHLELGSGCHVGSDMDGTMYGKYEDQPTLQIEGASNLVTENVCSWLYGALINGDRWWLSSVSVGVDTYNEWALRNGMTALKNVDCFSLLVAKTGVDVGRLLASIQKLHGNFGGKSILGCTSLCDEFTLSEVVKQMYGVTLQSGKVSRAFRNASIVCCLLFLFLSEMLNHSKLFWINPGYITPVFLAIIVASSALMLLVKHKLLFLQLYLLPSLCIVSGYNIFKDYHFYTYMLEEFDYKVPFGGFNVTGVLNISLCCFVMGLHTFRFLQTPNKIFSYVVAVLTVLYTYYYSTDVLGLILTSMSGFTNYWFIGTATYKLATYVLPHTSLLDSFDAIKAVVFLYLLLGYCNCVYYGSLYWINRFCKLTLGCYEFKVSAAEFKYMVANGLRAPTGVFDALILSLKLIGVGGRKTIKISSVQSKLTDLKCTNVVLLGCLSNMNIAANSREWAYCVDLHNKINLCNDAEAAQEMLLALLAFFLSKNSAFGVDELLDSYFNDSSVLQSVAATYVNLPSYLAYETARQSYEDALANGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAASQMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILSLAKDGVVPLSIIPAVSATKLNIVVSDIESYSKIQREGCVHYAGVIWSVVDIKDNDGKPVHAKEVVTSNVESLAWPLFLNCERIIKLQNNEIIPSKIKQRPIKAEGEGVVADGNALYSNEGGRTFMYAFISDKPDLKVVKWEFDGGSNAIELEPPCKFLVEAPSGPVVKYLYFVRNLNNLRRGAVLGFIGATVRLQAGKQTEQATNSSLLTLCAFAVDPPKTYLDAVKSGHRPVGNCVKMLANGSGNGQAITNGVEASTNQDSYGGASVCLYCRAHVEHPDMDGFCKLRGKYVQVPLGTLDPIRFVLENTVCKVCGCWQANGCTCDRAVIQSVDSGYLNRVRGSSAARLEPLNGSDTHHVFRAFDVYNRDVACISKFLKVNCVRLKNLDKHDAFWIVKKCTKSVMEHEQSIYNLISDCGAVAKHDFFTWKEGRSVYGNVCRQDLTEYTMMDLCYALRNFDENNCETLKKILVVVGACDESYFDNKLWFDPVENEDVHRVYAKLGTIVARAMLKCVKYCDAMVEQGIVGVITLDNQDLNGDFYDFGDFVTSVKGMGVPICTSYYSYMMPVMGMTNCLASECFIKSDIFGEDFRTFDLLAYDFTEHKVNLFNKYFKHWGQTYHPNCEDCHDESCIVHCANFNTLFATTIPITAFGPLCRKCWIDGVPLVTTAGYHFKQLGIVWNKDLNLHSSRLTINELLQFCADPSLLIASSPALVDKRTVCFSVAALGTGMTNQTVKPGHFNREFYDFLRSQGFFEEGSELTLKHFFFAQKGDAAVRDFDYYRYNRTTVLDICQARVVYQIVQCYFGMYEGGCITAKEVIVNNLNKSAGYPFNKFGKAGLYYDSLSYEEQDDLYAYTKRNIIPTMTQLNLKYAISGKDRARTVGGVSLLSTMTTRQYHQKHLKSIVNTRGASVVIGTTKFYGGWDNMLKTLIKDVENPHLMGWDYPKCDRALPNMIRMISAMILGSKHVNCCSSSDRYYRLCNELAQVLTEMVYSNGGFYVKPGGTTSGDATTAYANSVFNIFQATSANVNRLLSVDSNTCNNIEVKQLQRKLYDCCYRSSSVDQSFVEEYFGYLRKHFSMMILSDDGVVCYNSEYAALGYVADLNAFKAVLYYQNNVFMSASKCWIEPDINKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGVFVDDIVKTDPVILLERYVSLAIDAYPLSKHDNPEYRRVFTVMLDWVKHLYKTLNQGVLDSFSVTLLEDATAKFWDESFYASMYEQSSVLQSAGLCVVCSSQTVLRCGDCIRRPMLCTKCAYDHVVSTSHKFILAITPYVCCSSGCGVSDVTKLYLGGLSYWCVDHKPRLSFPLCSSGNVFGLYKNSATGSPDVDDFNTLATSDWTDVKDYKLANDVKDSLRLFAAETIKAKEESVKSSYACATIHEVVGPKELVLKWEVGKPRPPLSRNSVFTCYHITKNTKFQVGEFTFEKLDYDNDAVSYKSTATTKLVPGMVFVLTSHNVQPLRAPTIINQERYSTLHKLRPAFNIHEDYSNLIPYYQLIGKQKLTTIQGPPGSGKSHCVIGLGLYFPGARIVFTACSHAAVDSLCVKAATAYSSDRCSRIIPQKARIECYDGFKSNNTSAQYLFSTVNALPEVNADICVVDEVSMCTNYDLSVINQRVNYRHIVYVGDPQQLPAPRVMITRGVLVPEDYNVVTRRMCVLKPDIFLHKCYRCPAEIVNTVSEMVYENQFVPVKSESKECFKIYCRGNVQVDNGSSINRRQLEVVRMFLAKNPKWAKAVFISPYNSQNYVAGRVLGLQIQTVDSSQGSEYDYVIYTQTSDTAHASNVNRFNVAITRAKKGILCIMCDRELFDILKFYELKLSDLQVGDGCGLFKDCYKGEDNLPPSHAPTFMSLSDNFKTDKDLAVQIGVNGPVKYEHVISFMGFRFDINVPNQHTLFCTRDFAMRNARGWLGFDVEGAHVIGSNVGTNVPLQLGFSNGVDFVVRPEGCVSTEVGDVIQPVRARAPPGDQFTHLLPLLRKGQPWSVIRRRIVQMCSDYLANLSDTLIFVLWSGGLELTTMRYFVKLGPVQTCDCGKRATCYNSTNHTFSCFRHALGSDYIYNCYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAAMTRCLAIHDCFVKNVDWSITYPFIANEQAINKSGRLVQSHVMRAVLKLYNPKAIHDVGNPKGIRCVVTDASWYCYDKNPTNTNVKMLEYDYITHGQLDGLCLFWNCNVDMYPEFSVVCRFDTRMRSTLNLEGCNGGSLYVNNHAFHTPAYDKRAFAKLKAMPFFFYDDSECEKLQDAVNYVPLRASNCITRCNVGGAVCSKHCALYHNYVMAYNTFTTAGFTIWVPNSFDMFNLWQTFKNSNVQGLENIAYNVVKKGSFVGVEGELPVAVVNDKVMVRDGVSDNVVFVNNTSLPTNVAFELYAKRKVGLTPPLTILKNLGVVCTSKCVLWDYEASRPLTTFTKDVCKYTDFDGDVCTLFDNSVPGAFERFTVTKNAVLISLTAVKKLTAIKLTYGYLNGVPVFTHEDKPFTWYIYTRKDGAFVEYPDGYFTQGRVISDFQPRSNMEEDFLNMDMGLFISKYGLEDYGFEHVVFGDVSKTTLGGLHLLISQIRLSKIGVLKVEDFVSSSDSTLKSCTVTYVDNPSSKMVCTYVDLLLDDFVNILKSVDLSVVSKVHEVVIDCKVWRWMLWCKDHKVQTFYPQLQSAEWKCGYSMPSIYKIQRMCLEPCNLYNYGSGLKLPDGIMFNVVKYTQLCQYLNSTTMCVPHHMRVLHLGAGSDKGVAPGTAVLRRWLPLDAVIVDNDVNDYVSDADFSYTGDCASMYLTDKFDLVISDMYDGRTKSCDGDNVSKEGFFPYINGVITEKLALGGTVAIKITEFSWNKKLYELIQKFEYWTLFCTSVNTSSSEAFLIGVHFLGDFSTNAIIDGNIMHANYIFWRNSTIMTMSYNSVLDLSKFSCKHKATVVVNLKDSSVTDLVLGLLKNGKLLIRNNGVVCGFSNHLVNSTK 6793 P0C6W4 2'-O-methyltransferase rep 694008 Yes SL-0382 [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}. UNIPROT P0C6W4 UNIPROT A3EXC9 Pfam PF13087 Pfam PF16348 Pfam PF06478 Pfam PF01661 Pfam PF16251 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF00680 Pfam PF11633 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0032259 GO:0039648 GO:0039579 GO:0039644 GO:0039502 GO:0006351 GO:0019082 GO:0039694 MSFVAGVAPQGARGKYRAELNTEKRTDHVSLKASLCDAGDLVLKISPWFMDGESAYKHVSEQLSKGSKLLFVPQTLKGFIRHLPGPRVYLVERLTGGTYSDPFMVNQLAYQNAAGEGVIGTTLQGKRVGMFFPFDADLVTGEFQFLLRKKGFGGNRFRDAPWDYNWTPYSDLMDALEADPCGKYSQSLLKKLVGGDFTPIDQYMCGKNGKPIAEFAALMASEGITKLADVEAEVKSRTDSDRYIVFKNKLYRIVWNVQRKDVAYSKQSAFTMNSIVQLDTMEDVPRHSFTIGSEIQVIAPSTAVQANGHLNLKQRLLYAFYGKQAVSEPNYIYHSAYVDCTSCGKGSWLTGNAVQGFACDCGAHYCANDVDLQSSGLVRKNAVLLTTCPCNKDGECKHTLPQLVSMMTDKCDVEVVGKTFILTYGGVIYAYMGCSGGTMHFIPRAKSCVSKIGDAIFTGCTGTWSKVCETANLFLERAQHAINFVNEFVLTETVVALLSGTTSSIEELRDLCRNATFEKVRDYLTPRGWIVTMGSYIEGVINVGAAGVCNAALNAPFIVLSGLGESFKKVAATPWKLCSSLRETLDHYADSITYRVFPYDIPCDVTDYTALLLDCAVLTGASAYFVARYVDEKVEQLTNLVFSSCQSAVAAFVQACMSTYKATAKFISDMFTLIKVVSERLYVYTSVGFVVVGDYSSQLLKQFMHILSKAMQLLHTTVSWAGSKLPSVVYNGRDSLVFPSGTYYCVSTQGRSLQDQFDLVIPGDLSKKQIGILEPTPNSTTVDKKINTNVVEVVVGQLEPTKEHSPELVVGDYVIISNKIFVRSVEDSETVFYPLCTDGKIVPTLFRLKGGAPPKGVKFGGEQTKEITAVRSVSVDYDVHPVLDALLAGSELATFTVEKDLPVKDFVDVVKDEVIELLSKLLRGYNVDGFDLEDFADTPCYVYNAEGDLAWSSTMTFSVNPVEEVEEECDDDYVEDEYLSEEMLVEEDENSWAAAVEAVIPMEDVQLDTLVAEIDVSEPADDVAEQASTEEVEVPSACVLEASQVANAAEVESCEAEVSSSIPLHEDANAAKANDCAEGMPALDSTETVSKLSVDTPVGDVTQDDATSSNATVISEDVHTATHSKGLVAVPEVVPEKALGTSVERMRSTSEWTVVETSLKQETAVIVKNDSSAKPQRVKKPKAENPLKNFKHIVLNNDVTLVFGDAIAVARATEDCILVNAANTHLKHGGGIAAAIDRASGGLVQAESDDYVNFYGPLNVGDSTLLKGHGLATGILHVVGPDARANQDIQLLKRCYKAFNKYPLVVSPLISAGIFCVEPRVSLEYLLSVVHTKTYVVVNSEKVYNDLAAPKPPTGLTYSHEGWRGIIRNAKSFGFTCFICTDQSANAKLLKGRGVDLTKKTQTVDGVKYYLYSSKDPLTDIITAANACKGICAMPIGYVTHGLDLAQAGQQVKKITVPYVCLLASKDQVPILNSDVAVQTPEQSFINTVIANGGYHCWHLVTGELIVKGVSYRKLLNWSDQTICYADNKFYVVKGQIALPFDSLEKCRTYLTSRAAQQKNVDVLVTIDGVNFRTVVLNNTTTYRVQLGSVFYKGSDISDTIPTEKMSGEAVYLADNLSEAEKAVLSEVYGTADTAFLHRYYSLLALVKKWKYTVHDGVKSLKLNSNNCYVNVTMLMLDMLKEIKFIVPALQAAYLKHKGGDSTEFIALIMAYGDCTYGEPDDASRLLHTILSKAELTTQAKMVWRQWCNVCGVQDTTTTGLKACIYVGMNSLDELHATHEECCQCGDVRKRQLVEHNAPWLLLSGLNEAKVMTPTSQSAGPDYTAFNVFQGVETSVGHYLHVRVKDNLLYKYDSGSLSKTSDMKCKMTDVYYPKQRYSADCNVVVYSLDGNTWADVDPDLSAFYMKDGKYFTKKPVIEYSPATILSGSVYTNSCLVGHDGTIGSDAISSSFNNLLGFDNSKPVSKKLTYSFFPDFEGDVILTEYSTYDPIYKNGAMLHGKPILWVNNSKFDSALNKFNRATLRQVYDIAPVTLENKYTVLQDNQIQQVEVEAPKEDAKPQSPVQVAEDIDNKLPIIKCKGLKKPFVKDGYSFVNDPQGVNVIDTLGIDDLRALYVDRNLRLIVLKENNWSALFNIHTVEKGDLSVIAASGSITRRVKILLGASSLFAQFASVTVNVTTAMGKALGRMTRNVITNTGIIGQGFALLKMLLILPFTFWKSKNQSTVKVEVGALRTAGIVTTNVVKQCASAAYDVLVVKFKRIDWKSTLRLLFLICTTGLLLSSLYYLFLFHQVLTSDVMLDGAEGMLATYRELRSYLGIHSLCDGMVEAYRNVSYDVNDFCSNRSALCNWCLIGQDSLTRYSAFQMIQTHVTSYVINIDWVWFVMEFALAYVLYTSTFNVLLLVVSSQYFFSYTGAFVNWRSYNYLVSGYFFCVTHIPLLGLVRIYNFLACLWFLRRFYNHVINGCKDTACLLCYKRNRLTRVEASTVVCGSKRTFYIVANGGTSFCCRHNWNCVDCDTAGIGNTFICEEVANDLTTSLRRLVKPTDKSHYYVESVTVKDSVVQLHYSREGASCYERYPLCYFTNLDKLKFKEVCKTPTGIPEHNFLIYDSSDRGQENLARSACVYYSQVLSKPMLLVDSNMVTTVGDSREIASKMLDSYVNSFISLFGVNRDKLDKLVATARDCVKRGDDFQTVIKTFTDAARGPAGVESDVETSSIVDALQYAYKHDLQLTTEGFNNYVPSYIKPDSVATADLGCLIDLNAASVNQTSIRNANGACIWNSSDYMKLSDSLKRQIRIACRKCNIPFRLTTSRLRSADNILSVKFSATKLSGGAPKWLLKLRDFTWKSYCVVTLVVFAMAVLSYLCLPAFNMSQVSFHEDRILTYKVVENGIIRDITPSDTCFANKYQSFSKWFNEHYGGLFNNDISCPVTVAVIAGVAGARVPNLPANVAWVGRQIVLFVSRVFASSNNVCYTPTAEIPYERFSDSGCVLASECTLFRDAEGKINPYCYDPTVLPGASAYDQMKPHVRYDMYDSDMYIKFPEVVFESTLRITKTLATRYCRFGSCEDANEGVCITTNGSWAIYNDHYANKPGVYCGDNYFDIVRRLGLSLFQPVTYFQLSTSLALGVMLCIFLTIAFYYVNKVKRALADYTQCAVVAVAAALLNSLCLCFVVSNPLLVLPYTALYYYATFYLTGEPAFVMHVSWFVMFGTVVPIWMVFAYIVGVCLRHLLWVMAYFSKKHVEVFTDGKLNCSFQDAAANIFVINKDTYVALRNSITQDSYNRYLSMFNKYKYYSGAMDTASYREASAAHLCKALQVYSETGSDVLFQPPNCSVTSSVLQSGLVKMAAPSGVVENCMVQVTCGSMTLNGLWLDNYVWCPRHVMCPADQLSDPNYDALLVSKTNLSFIVQKNVGAPANLRVVGHTMVGTLLKLTVESANPQTPAYTFTTVKPGASFSVLACYNGRPTGVFMVNMRQNSTIKGSFLCGSCGSVGYTQEGNVINFCYMHQMELSNGTHTGCAFDGVMYGAFEDRQVHQVQLSDKYCTINIVAWLYAAILNGCNWFVKPNKTGIATFNEWAMSNQFTEFIGTQSVDMLAHKTGVSVEQLLYAIQTLHKGFQGKTILGNSMLEDEFTPDDVNMQVMGVVMQSGVKRISYGLVHWLFTTLLLAYVATLQLTKFTIWNYLFEVIPLQLTPLVLCVMACVMLTVKHKHTFLTLFLLPTAICLTYANIVYEPQTPVSSALIAVANWLNPASVYMRTTHTDLGVYLSLCFALAVVVRRLYRPNASNLALALGSAMVWFYTYTTGDCSSPLTYLMFLTTLTSDYTVTVFLAVNVAKFFARVVFLYAPHAGFIFPEVKLVLLMYLAVGYFCTVYFGVFSLLNLKLRVPLGVYDYTVSTQEFRYLTGNGLHAPRNSWEALRLNMKLIGIGGTPCIKIASVQSKLTDLKCTSVVLLSVLQQLHLEANSKAWAHCVKLHNDILAATDPTEAFDNFVCLFATLMSFSANVDLEALASDLLDHPSVLQATLSEFSHLASYAELEAAQSSYQKALNSGDASPQVLKALQKAVNIAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVISNARNGCVPLSVVPLCASNKLRVVIPDITIWNKVVTWPSLSYAGALWDISLINNVDGEVVKSSDVTETNESLTWPLVLECTRAASSAVTLQNNEIRPSGLKTMVVSAGIDHANCNTSSLAYYEPVEGRKMLMGILSENAHLKWAKVEGRDGFVNIELQPPCKFLIAGPKGPEVRYLYFVKNLNNLHRGQLLGHIAATVRLQAGSNTEFAINSSVLSAVTFSVDPGKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAVSVKPEANADQDTYGGASVCLYCRAHIEHPDVTGVCKFKGKFVQVPLHIRDPVGFCLQNTPCNVCQFWIGHGCNCDALRGTTIPQSKDSNFLNRVRGSIVNARIEPCASGLTTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVEVDDEGHRLDSFFVVKRHTMENYELEKRCYDLVKDCDAVAVHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNNCEVLKSILVKYGCCDASYFDNKLWFDFVENPNVISVYHKLGERIRQAVLNTVKFCDQMVKSGLVGVLTLDNQDLNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCLAAETHRDCDLTKPLIEWPLLEYDYTDYKIGLFEKYFKXWDQQYHPNCVNCTDDRCVLHCANFNVLFSMTLPGTSFGPIVRKIFVDGVPFVISCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVRPGNFNKDFYDFVVSKGFFKEGSSVTLRHFFFAQDGHAAITDYSYYAYNLPTMCDIKQMLFCMEVVDRYFEIYDGGCLNASEVIVNNLDKSAGHPFNKFGKARVYYESLSYQEQDELFAMTKRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGSTCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHSTCCTNTDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNTIVDEEVKDMQFELYVNVYRKSQPDPKFVDRYYAFLNKHFSMMILSDDGVVCYNSDYATKGYIASIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLFIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHDDPEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEESFYRDLYTAPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCDVADVTKLYLGGMSYFCIDHRPVCSFPLCANGLVFGLYKNMCTGSPSVTEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERELLLVWEAGKAKPPLNRNYVFTGYHITKNSKVQLGEYVFERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLQAPTIVNQERYVKITGLYPTLTVPEEFANHVANFQKAGFSKFVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDQFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSVINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSVCYRCPEEIVNTVSALVYNNKLVAKKPASGQCFKILYKGSVTHDASSAINRPQLNFVKSFIAANPNWSKAVFISPYNSQNAVARSVLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNINRFNVAVTRAQKGILCVMTSQALFDSLEFAEVSLNNYKLQSQIVTGLYKDCSRESSGLHPAYAPTYVSVDDKYKTSDELCVNLNVPANVPYSRVISRMGFKLDASIPNYPKLFITRDEAIRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGSMLTSIAARPPPGEQFKHLVPLMNKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQRCCMCNRRASTYSSPLHSYACWSHSSGYDYVYNPFFVDVQQWGYIGNLATNHDRYCSVHQGAHVASNDAVMTRCLAIHDCFIERVEWDITYPYISHEKRLNSCCRAVERNVVRAALLAGRFERVYDIGNPKGIPIVDDPVVDWHYYDAQPLSKKVQQLFYTEDCAKNFSDGLCLFWNCNVPRYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDASAFRDLKPLPFFYYSTTPCEVHGNGNMLEDIDYVPLKSAVCITACNLGGAVCRKHAAEYRDYMEAYNLVSASGFRLWCYKTFDVYNLWSTFTKIQGLENIAYNVIKQGHFTGVEGELPVAVVNDKIYTKSDVNDVCIFENKTTLPTNIAFELYAKRAVRSHPDFNLLRNLEVDVCYKFVLWDYERSNIYGSATIGVCKYTDIDVNSALNICFDIRDNGSLERFMSLPNGILISDRKVKNYPCIVSSNYAYFNGTLIRDNTGNSQSSDGEVKQPVTFYIYKKVNNEFVQFTDTYYTLGRTVSDFTPVSEMEKDFLALDSDVFIKKYKLEAYAFEHVVYGDFSRTTLGGLHLLIGLYKKHQEGHIIMEEMLKERATVHNYFVTESNTASFKAVCSVIDLKLDDFVDIIKAMDLSVVSKVVKIPIDLTMIEFMLWCKDGQVQTFYPRLQAINDWKPGLAMPSLFKVQNSNLEPCMLPNYKQSIPMPQGVHMNIAKYMQLCQYLNTCTIAVPANMRVMHFGAGSDKGVAPGSSVLRQWLPTDAILIDNDLNEYVSDADITLFGDCVTVRVGQQVDLLISDMYDPSTKVVGETNEAKALFFVYLCNFIKNNLALGGSVAIKITEHSWSAELYELMGRFAWWTVFCTNANASSSEGFLIGINYLGELKEVIDGNVMHANYIFWRNTTLMNLSTYSLFDLSRFPLKLKGTPVLQLKESQINELVISLLSQGKLIIRDNDTLSVSTDVLVNFYRKPHKRSKC 7182 P0C6W5 2'-O-methyltransferase rep 694006 Yes SL-0382 [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}. UNIPROT P0C6W5 UNIPROT A3EXG5 PDB 5UTV Pfam PF13087 Pfam PF16348 Pfam PF06478 Pfam PF01661 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF00680 Pfam PF11633 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0032259 GO:0039648 GO:0039579 GO:0039644 GO:0039502 GO:0006351 GO:0019082 GO:0039694 MEGVPDPPKLKSMVVTTLKWCDPFANPNVTGWDIPIEEALEYAKQQLRTPEPQLVFVPYYLSHAPGISGDRVVITDSIWYATNFGWQPIRELAMDKDGVRYGRGGTHGVLLPMQDPSFIMGDIDIQIRKYGIGANSPPDVLPLWDGFSDPGPDVGPYLDFPDNCCPTKPKAKRGGDVYLSDQYGFDNNGILVEPVMKLLGVIKSDFTLEQLLAALGKYRTEDGYDLPDGYVKVAIKVGRKAVPVLKQSIFTVVGVTEQLVPGYYYPFSTSSVVEHTKPTRGGPVGKTVEAVMLSLYGTNNYNPATPVARLKCSYCDYYGWTPLKDIGTVNCLCGAEFQLTSSCVDAESAGVIKPGCVMLLDKSPGMRLIPGNRTYVSFGGAIWSPIGKVNGVTVWVPRAYSIVAGEHSGAVGSGDTVAINKELVEYLIEGIRVDADTLDNPTCATFIANLDCDTKAPVVHTVESLQGLCLANKIMLGDKPLPTDEFHPFIVGLAYHVQRACWYGALASRTFEAFRDFVRTEEERFAQFFGKVCAPINGCVYLAYTTGRVTLFSAYQVLNTAIAKSKDAFGGVAAIVVDMLKPILEWVLKKMSIAKGAWLPYAEGLLALFKAQFTVVKGKFQFLRASLNSKCHSLCDLLTTIMSKLLTSVKWAGCKVDALYTGTYYYFSRKGVLTEVQLCAKRLGLLLTPKQQKMEVEVLDGDFDAPVTLTDLELEECTGVLEEVFGASDVKLVKGTLVSLASKLFVRTEDGFLYRYVKSGGVLGKAFRLRGGGVSKVTFGDEEVHTIPNTVTVNFSYDVCEGLDAILDKVMAPFQVEEGTKLEDLACVVQKAVYERLSDLFSDCPAELRPINLEDFLTSECFVYSKDYEKILMPEMYFSLEDAVPVDDEMVDDIEDTVEQASDSDDQWLGDEGAEDCDNTIQDVDVATSMTTPCGYTKIAEHVYIKCADIVQEARNYSYAVLVNAANVNLHHGGGVAGALNRATNNAMQKESSEYIKANGSLQPGGHVLLSSHGLASHGILHVVGPDKRLGQDLALLDAVYAAYTGFDSVLTPLVSAGIFGFTVEESLCSLVKNVACTTYVVVYDRQLYERALATSFDVPGPQSSVQHVPAIDWAEAVEVQESIVDQVETPSLGAVDTVDSNADSGLNETARSPENVVGSVPDDVVADVESCVRDLVRQVVKKVKRDKRPPPIVPQQTVEQQPQEISSPGDCNTVLVDVVSMSFSAMVNFGKEKGLLIPVVIDYPAFLKVLKRFSPKEGLFSSNGYEFYGYSRDKPLHEVSKDLNSLGRPLIMIPFGFIVNGQTLAVSAVSMRGLTVPHTVVVPSESSVPLYRAYFNGVFSGDTTAVQDFVVDILLNGARDWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETKLCAPEPLIKVLTTVDGINYSTVLVSTAQSYRAQIGTVFCDGHDWSNKNPMPTDEGTHLYKQDNFSSAEVTAIREYYGVDDSNIIARAMSIRKTVQTWPYTVVDGRVLLAQRDSNCYLNVAISLLQDIDVSFSTPWVCRAYDALKGGNPLPMAEVLIALGKATPGVSDDAHMVLSAVLNHGTVTARRVMQTVCEHCGVSQMVFTGTDACTFYGSVVLDDLYAPVSVVCQCGRPAIRYVSEQKSPWLLMSCTPTQVPLDTSGIWKTAIVFRGPVTAGHYMYAVNGTLISVYDANTRRRTSDLKLPATDILYGPTSFTSDSKVETYYLDGVKRTTIDPDFSKYVKRGDYYFTTAPIEVVAAPKLVTSYDGFYLSSCQNPQLAESFNKAINATKTGPMKLLTMYPNVAGDVVAISDDNVVAHPYGSLHMGKPVLFVTRPNTWKKLVPLLSTVVVNTPNTYDVLAVDPLPVNNETSEEPISVKAPIPLYGLKATMVLNGTTYVPGNKGHLLCLKEFTLTDLQTFYVEGVQPFVLLKASHLSKVLGLRVSDSSLHVNHLSKGVVYAYAATRLTTRVTTSLLGGLVTRSVRKTADFVRSTNPGSKCVGLLCLFYQLFMRFWLLVKKPPIVKVSGIIAYNTGCGVTTCVLNYLRSRCGNISWSRLLKLLRYMLYIWFVWTCLTICGVWLSEPYAPSLVTRFKYFLGIVMPCDYVLVNETGTGWLHHLCMAGMDSLDYPALRMQQHRYGSPYNYTYILMLLEAFFAYLLYTPALPIVGILAVLHLIVLYLPIPLGNSWLVVFLYYIIRLVPFTSMLRMYIVIAFLWLCYKGFLHVRYGCNNVACLMCYKKNVAKRIECSTVVNGVKRMFYVNANGGTHFCTKHNWNCVSCDTYTVDSTFICRQVALDLSAQFKRPIIHTDEAYYEVTSVEVRNGYVYCYFESDGQRSYERFPMDAFTNVSKLHYSELKGAAPAFNVLVFDATNRIEENAVKTAAIYYAQLACKPILLVDKRMVGVVGDDATIARAMFEAYAQNYLLKYSIAMDKVKHLYSTALQQISSGMTVESVLKVFVGSTRAEAKDLESDVDTNDLVSCIRLCHQEGWEWTTDSWNNLVPTYIKQDTLSTLEVGQFMTANAKYVNANIAKGAAVNLIWRYADFIKLSESMRRQLKVAARKTGLNLLVTTSSLKADVPCMVTPFKIIGGHRRIVSWRRVLIHVFMLLVVLNPQWFTPWYIMRPIEYNVVDFKVIDNAVIRDITSADQCFANKFSAFENWYSNRYGSYVNSRGCPMVVGVVSDIVGSLVPGLPARFLRVGTTLLPLVNYGLGAVGSVCYTPHYAINYDVFDTSACVLAATCTLFSSASGERMPYCADAALIQNASRYDMLKPHVMYPFYEHSGYIRFPEVISAGVHIVRTMAMEYCKVGRCDVSEAGLCMSLQPRWVVNNAYFRQQSGVYCGTSAFDLFMNMLLPIFTPVGAVDITTSILMGALLAVVVSMSLYYLLRFRRAFGDYSGVIFTNILAFVLNVIVLCLEGPYPMLPSIYAMVFLYATCYFGSDIACMMHVSFLIMFAGVVPLWVTVLYIVVVLSRHILWFASLCTKRTVQVGDLAFHSFQDAALQTFMLDKEVFLRLKREISSDAYFKYLAMYNKYKYYSGPMDTAAYREAACSHLVMALEKYSNGGGDTIYQPPRCSVASAALQAGLTRMAHPSGLVEPCLVKVNYGSMTLNGIWLDNFVICPRHVMCSRDELANPDYPRLSMRAANYDFHVSQNGHNIRVIGHTMEGSLLKLTVDVNNPKTPAYSFIRVSTGQAMSLLACYDGLPTGVYTCTLRSNGTMRASFLCGSCGSPGFVMNGKEVQFCYLHQLELPNGTHTGTDFSGVFYGPFEDKQVPQLAAPDCTITVNVLAWLYAAVLSGENWFLTKSSISPAEFNNCAVKYMCQSVTSESLQVLQPLAAKTGISVERMLSALKVLLSAGFCGRTIMGSCSLEDEHTPYDIGRQMLGVKLQGKFQSMFRWTLQWFAIIFVLTILILLQLAQWTFVGALPFTLLLPLIGFVAVCVGFVSLLIKHKHTYLTVYLLPVAMVTAYYNFQYTPEGVQGYLLSLYNYVNPGRIDVIGTDLLTMLIISVACTLLSVRMVRTDAYSRIWYVCTAVGWLYNCWTGSADTVAISYLTFMVSVFTNYTGVACASLYAAQFMVWVLKFLDPTILLLYGRFRCVLVCYLLVGYLCTCYFGVFNLINRLFRCTLGNYEYVVSSQELRYMNSHGLLPPTNSWQALMLNIKLAGIGGIPIYRVSTIQSNMTDLKCTSVVLLSVLQQLRVESSSKLWALCVKLHNEILASNSPTEAFEAFVSLLSVLLSLPGAINLDELCSSILENNSVLQAVASEFSNLSSYVDYENAQKAYDTAVATGAPASTVNALKKAMNVAKSVLDKDVATTRKLERMSELAMTAMYKQARAEDRRSKVTAAMQTMLFNMIRRLDSDALSNILNNARNGVVPLGVIPRTAANKLLLVVPDFSVYTATITMPTLTYAGSAWDVMQVADADGKTVNATDITRENSVNLAWPLVVTAQRQQATSPVKLQNNELMPQTVKRMNVVAGVSQTACVTDAVAYYNATKEGRHVMAILADTDGLAFAKVEKSTGDGFVILELEPPCKFMVDTPKGPALKYLYFTKGLKNLCRGTVLGTLACTVRLHAGSATEVASNSSILSLCSFSVDPEATYKDYLDNGGSPIGNCVKMLTPHTGTGLAITAKPDANIDQESFGGASCCLYCRCHIEHPGASGVCKYKGKFVQIPLVGVNDPIGFCIRNVVCAVCNMWQGYGCPCSSLREINLQARDECFLNRVRGTSGVARLVPLGSGVQPDIVLRAFDICNTKVAGFGLHLKNNCCRYQELDADGTQLDSYFVVKRHTESNYLLEQRCYEKLKDCGVVARHDFFKFNIEGVMTPHVSRERLTKYTMADLVYSLRHFDNNNCDTLKEILVLRGCCTADYFDRKDWYDPVENPDIIRVYHNLGETVRKAVLSAVKMADSMVEQGLIGVLTLDNQDLNGQWYDFGDFIEGPAGAGVAVMDTYYSLAMPVYTMTNMLAAECHVDGDFSKPKRVWDICKYDYTQFKYSLFSKYFKYWDMQYHPNCVACADDRCILHCANFNILFSMVLPNTSFGPLVQKIYVDGVPFVVSTGYHYRELGVVMNQDIRQHAQRLSLRELLVYAADPAMHVAASNALADKRTVCMSVAAMTTGVTFQTVKPGQFNEDFYNFAVKCGFFKEGSTISFKHFFYAQDGNAAISDYDYYRYNLPTMCDIKQLLFSLEVVDKYFDCYDGGCLQASQVVVANYDKSAGFPFNKFGKARLYYESLSYADQDELFAYTKRNVLPTITQMNLKYAISAKNRARTVAGVSIASTMTNRQFHQKMLKSIAAARGASVVIGTTKFYGGWNRMLRTLCEGVENPHLMGWDYPKCDRAMPNLLRIFASLILARKHATCCNASERFYRLANECAQVLSEMVLCGGGFYVKPGGTSSGDSTTAYANSVFNICQAVSANLNTFLSIDGNKIYTTYVQELQRRLYLGIYRSNTVDNELVLDYYNYLRKHFSMMILSDDGVVCYNADYAQKGYVADIQGFKELLYFQNNVFMSESKCWVEPDITKGPHEFCSQHTMLVDMKGEQVYLPYPDPSRILGAGCFVDDLLKTDGTLMMERYVSLAIDAYPLTKHPDPEYQNVFWCYLQYIKKLHEELTGHLLDTYSVMLASDNASKYWEVEFYENMYMESATLQSVGTCVVCNSQTSLRCGGCIRRPFLCCKCCYDHVVSTTHKLVLSVTPYVCNNPSCDVADVTQLYLGGMSYYCRDHRPPISFPLCANGQVFGLYKNICTGSPDVADFNSLATCDWSNSKDYVLANTATERLKLFAAETLRATEENAKQAYASAVVKEVLSDRELVLSWETGKTRPPLNRNYVFTGFHITKNSKVQLGEYIFEKGDYGDVVNYRSSTTYKLQVGDYFVLTSHSVQPLSSPTLLPQERYTKLVGLYPAMNVPESFASNVVHYQRVGMSRYTTVQGPPGTGKSHLSIGLALYYPSAKIVYTACSHAAVDALCEKAHKNLPINRCSRIVPAKARVECFSKFKVNDVGAQYVFSTINALPETTADILVVDEVSMCTNYDLSMINARVRAKHIVYVGDPAQLPAPRTLLTKGTLAPEHFNSVCRLMVAVGPDIFLATCYRCPKEIVDTVSALVYDKKLKANKVTTGECYKCYYKGSVTHDSSSAINKPQLGLVKEFLIKNPKWQSAVFISPYNSQNSVARRMLGLQTQTVDSSQGSEFDYVIYCQTSDTAHALNVNRFNVAITRAKKGILCVMSDSTLYESLEFTPLDVNDYVKPKMQSEVTVGLFKDCAKAEPLGPAYAPTFVSVNDKFKLNESLCVHFDTTELQMPYNRLISKMGFKFDLNIPGYSKLFITREQAIREVRGWVGFDVEGAHACGPNIGTNLPLQIGFSTGVNFVVTPSGYIDTESGSRLANVVSKAPPGDQFKHLIPLMRKGEPWSVVRKRIVEMLCDTLDGVSDTVTFVTWAHGFELTTLHYFAKVGPERKCFMCPRRATLFSSVYGAYSCWSHHRHIGGADFVYNPFLVDVQQWGYVGNLQVNHDNVCDVHKGAHVASCDAIMTRCLAIHDCFCGEVNWDVEYPIIANELAINRACRSVQRVVLKAAVKALHIETIYDIGNPKAIKVYGVNVNNWNFYDTNPVVEGVKQLHYVYDVHRDQFKDGLAMFWNCNVDCYPHNALVCRFDTRVLSKLNLAGCNGGSLYVNQHAFHTDAFNKNAFVNLKPLPFFYYSDTACENATGVSTNYVSEVDYVPLKSNVCITRCNLGGAVCKKHADEYRNFLESYNTMVSAGFTLWVDKTFDVFNLWSTFVKLQSLENVAYNVLKSGHFTAVAGELPVAILNDRLYIKEDGADKLLFTNNTCLPTNVAFELWAKRSVNVVPEVKLLRNLGVTCTYNLVIWDYESNAPLVPNTVGICTYTDLTKLDDQVVLVDGRQLDAYSKFCQLKNAIYFSPSKPKCVCTRGPTHASINGVVVEAPDRGTAFWYAMRKDGAFVQPTDGYFTQSRTVDDFQPRTQLEIDFLDLEQSCFLDKYDLHDLGLEHIVYGQFDGTIGGLHLLIGAVRRKRTAHLVMETVLGTDTVTSYAVIDQPTASSKQVCSVVDIILDDFIALIKAQDRSVVSKVVQCCLDFKVFRFMLWCKGGKISTFYPQLQAKQDWKPGYSMPALYKVQNAVLEPCLLHNYGQAARLPSGTLMNVAKYTQLCQYLNTCSLAVPAKMRVMHFGAGSDKGVCPGTAVLKQWLPADAYLVDNDLCYCASDADSTYVGSCETFFSVNKWDFIFSDMYDARTKNTSGDNTSKEGFFTYLTGFIRSKLALGGSIAIKITEHSWSADLYAIMGHFNWWTCFCTSVNSSSSEAFLIGVNYIGVGALLDGWQMHANYVFWRNSTVMQLSSYSLYDLQRFPLRLKGTPVMSLKEDQLNELVLNLIRAGRLIVRDAVDIGVRGVACSGV 6930 P0C6X1 Putative 2'-O-methyl transferase rep 11137 Yes SL-0382 [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}. UNIPROT P0C6X1 UNIPROT Q05002 UNIPROT Q9DLN0 UNIPROT Q9DLN1 PDB 1P9S PDB 2J97 PDB 2J98 PDB 3EJG PDB 4RS4 PDB 4S1T Pfam PF13087 Pfam PF16348 Pfam PF06478 Pfam PF01661 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0008270 GO:0039520 GO:0032259 GO:0039648 GO:0039548 GO:0006351 GO:0019082 GO:0039694 MACNRVTLAVASDSEISANGCSTIAQAVRRYSEAASNGFRACRFVSLDLQDCIVGIADDTYVMGLHGNQTLFCNIMKFSDRPFMLHGWLVFSNSNYLLEEFDVVFGKRGGGNVTYTDQYLCGADGKPVMSEDLWQFVDHFGENEEIIINGHTYVCAWLTKRKPLDYKRQNNLAIEEIEYVHGDALHTLRNGSVLEMAKEVKTSSKVVLSDALDKLYKVFGSPVMTNGSNILEAFTKPVFISALVQCTCGTKSWSVGDWTGFKSSCCNVISNKLCVVPGNVKPGDAVITTQQAGAGIKYFCGMTLKFVANIEGVSVWRVIALQSVDCFVASSTFVEEEHVNRMDTFCFNVRNSVTDECRLAMLGAEMTSNVRRQVASGVIDISTGWFDVYDDIFAESKPWFVRKAEDIFGPCWSALASALKQLKVTTGELVRFVKSICNSAVAVVGGTIQILASVPEKFLNAFDVFVTAIQTVFDCAVETCTIAGKAFDKVFDYVLLDNALVKLVTTKLKGVRERGLNKVKYATVVVGSTEEVKSSRVERSTAVLTIANNYSKLFDEGYTVVIGDVAYFVSDGYFRLMASPNSVLTTAVYKPLFAFNVNVMGTRPEKFPTTVTCENLESAVLFVNDKITEFQLDYSIDVIDNEIIVKPNISLCVPLYVRDYVDKWDDFCRQYSNESWFEDDYRAFISVLDITDAAVKAAESKAFVDTIVPPCPSILKVIDGGKIWNGVIKNVNSVRDWLKSLKLNLTQQGLLGTCAKRFKRWLGILLEAYNAFLDTVVSTVKIGGLTFKTYAFDKPYIVIRDIVCKVENKTEAEWIELFPHNDRIKSFSTFESAYMPIADPTHFDIEEVELLDAEFVEPGCGGILAVIDEHVFYKKDGVYYPSNGTNILPVAFTKAAGGKVSFSDDVEVKDIEPVYRVKLCFEFEDEKLVDVCEKAIGKKIKHEGDWDSFCKTIQSALSVVSCYVNLPTYYIYDEEGGNDLSLPVMISEWPLSVQQAQQEATLPDIAEDVVDQVEEVNSIFDIETVDVKHDVSPFEMPFEELNGLKILKQLDNNCWVNSVMLQIQLTGILDGDYAMQFFKMGRVAKMIERCYTAEQCIRGAMGDVGLCMYRLLKDLHTGFMVMDYKCSCTSGRLEESGAVLFCTPTKKAFPYGTCLNCNAPRMCTIRQLQGTIIFVQQKPEPVNPVSFVVKPVCSSIFRGAVSCGHYQTNIYSQNLCVDGFGVNKIQPWTNDALNTICIKDADYNAKVEISVTPIKNTVDTTPKEEFVVKEKLNAFLVHDNVAFYQGDVDTVVNGVDFDFIVNAANENLAHGGGLAKALDVYTKGKLQRLSKEHIGLAGKVKVGTGVMVECDSLRIFNVVGPRKGKHERDLLIKAYNTINNEQGTPLTPILSCGIFGIKLETSLEVLLDVCNTKEVKVFVYTDTEVCKVKDFVSGLVNVQKVEQPKIEPKPVSVIKVAPKPYRVDGKFSYFTEDLLCVADDKPIVLFTDSMLTLDDRGLALDNALSGVLSAAIKDCVDINKAIPSGNLIKFDIGSVVVYMCVVPSEKDKHLDNNVQRCTRKLNRLMCDIVCTIPADYILPLVLSSLTCNVSFVGELKAAEAKVITIKVTEDGVNVHDVTVTTDKSFEQQVGVIADKDKDLSGAVPSDLNTSELLTKAIDVDWVEFYGFKDAVTFATVDHSAFAYESAVVNGIRVLKTSDNNCWVNAVCIALQYSKPHFISQGLDAAWNKFVLGDVEIFVAFVYYVARLMKGDKGDAEDTLTKLSKYLANEAQVQLEHYSSCVECDAKFKNSVASINSAIVCASVKRDGVQVGYCVHGIKYYSRVRSVRGRAIIVSVEQLEPCAQSRLLSGVAYTAFSGPVDKGHYTVYDTAKKSMYDGDRFVKHDLSLLSVTSVVMVGGYVAPVNTVKPKPVINQLDEKAQKFFDFGDFLIHNFVIFFTWLLSMFTLCKTAVTTGDVKIMAKAPQRTGVVLKRSLKYNLKASAAVLKSKWWLLAKFTKLLLLIYTLYSVVLLCVRFGPFNFCSETVNGYAKSNFVKDDYCDGSLGCKMCLFGYQELSQFSHLDVVWKHITDPLFSNMQPFIVMVLLLIFGDNYLRCFLLYFVAQMISTVGVFLGYKETNWFLHFIPFDVICDELLVTVIVIKVISFVRHVLFGCENPDCIACSKSARLKRFPVNTIVNGVQRSFYVNANGGSKFCKKHRFFCVDCDSYGYGSTFITPEVSRELGNITKTNVQPTGPAYVMIDKVEFENGFYRLYSCETFWRYNFDITESKYSCKEVFKNCNVLDDFIVFNNNGTNVTQVKNASVYFSQLLCRPIKLVDSELLSTLSVDFNGVLHKAYIDVLRNSFGKDLNANMSLAECKRALGLSISDHEFTSAISNAHRCDVLLSDLSFNNFVSSYAKPEEKLSAYDLACCMRAGAKVVNANVLTKDQTPIVWHAKDFNSLSAEGRKYIVKTSKAKGLTFLLTINENQAVTQIPATSIVAKQGAGDAGHSLTWLWLLCGLVCLIQFYLCFFMPYFMYDIVSSFEGYDFKYIENGQLKNFEAPLKCVRNVFENFEDWHYAKFGFTPLNKQSCPIVVGVSEIVNTVAGIPSNVYLVGKTLIFTLQAAFGNAGVCYDIFGVTTPEKCIFTSACTRLEGLGGNNVYCYNTALMEGSLPYSSIQANAYYKYDNGNFIKLPEVIAQGFGFRTVRTIATKYCRVGECVESNAGVCFGFDKWFVNDGRVANGYVCGTGLWNLVFNILSMFSSSFSVAAMSGQILLNCALGAFAIFCCFLVTKFRRMFGDLSVGVCTVVVAVLLNNVSYIVTQNLVTMIAYAILYFFATRSLRYAWIWCAAYLIAYISFAPWWLCAWYFLAMLTGLLPSLLKLKVSTNLFEGDKFVGTFESAAAGTFVIDMRSYEKLANSISPEKLKSYAASYNRYKYYSGNANEADYRCACYAYLAKAMLDFSRDHNDILYTPPTVSYGSTLQAGLRKMAQPSGFVEKCVVRVCYGNTVLNGLWLGDIVYCPRHVIASNTTSAIDYDHEYSIMRLHNFSIISGTAFLGVVGATMHGVTLKIKVSQTNMHTPRHSFRTLKSGEGFNILACYDGCAQGVFGVNMRTNWTIRGSFINGACGSPGYNLKNGEVEFVYMHQIELGSGSHVGSSFDGVMYGGFEDQPNLQVESANQMLTVNVVAFLYAAILNGCTWWLKGEKLFVEHYNEWAQANGFTAMNGEDAFSILAAKTGVCVERLLHAIQVLNNGFGGKQILGYSSLNDEFSINEVVKQMFGVNLQSGKTTSMFKSISLFAGFFVMFWAELFVYTTTIWVNPGFLTPFMILLVALSLCLTFVVKHKVLFLQVFLLPSIIVAAIQNCAWDYHVTKVLAEKFDYNVSVMQMDIQGFVNIFICLFVALLHTWRFAKERCTHWCTYLFSLIAVLYTALYSYDYVSLLVMLLCAISNEWYIGAIIFRICRFGVAFLPVEYVSYFDGVKTVLLFYMLLGFVSCMYYGLLYWINRFCKCTLGVYDFCVSPAEFKYMVANGLNAPNGPFDALFLSFKLMGIGGPRTIKVSTVQSKLTDLKCTNVVLMGILSNMNIASNSKEWAYCVEMHNKINLCDDPETAQELLLALLAFFLSKHSDFGLGDLVDSYFENDSILQSVASSFVGMPSFVAYETARQEYENAVANGSSPQIIKQLKKAMNVAKAEFDRESSVQKKINRMAEQAAAAMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILNMARNGVVPLSVIPATSAARLVVVVPDHDSFVKMMVDGFVHYAGVVWTLQEVKDNDGKNVHLKDVTKENQEILVWPLILTCERVVKLQNNEIMPGKMKVKATKGEGDGGITSEGNALYNNEGGRAFMYAYVTTKPGMKYVKWEHDSGVVTVELEPPCRFVIDTPTGPQIKYLYFVKNLNNLRRGAVLGYIGATVRLQAGKQTEFVSNSHLLTHCSFAVDPAAAYLDAVKQGAKPVGNCVKMLTNGSGSGQAITCTIDSNTTQDTYGGASVCIYCRAHVAHPTMDGFCQYKGKWVQVPIGTNDPIRFCLENTVCKVCGCWLNHGCTCDRTAIQSFDNSYLNRVRGSSAARLEPCNGTDIDYCVRAFDVYNKDASFIGKNLKSNCVRFKNVDKDDAFYIVKRCIKSVMDHEQSMYNLLKGCNAVAKHDFFTWHEGRTIYGNVSRQDLTKYTMMDLCFALRNFDEKDCEVFKEILVLTGCCSTDYFEMKNWFDPIENEDIHRVYAALGKVVANAMLKCVAFCDEMVLKGVVGVLTLDNQDLNGNFYDFGDFVLCPPGMGIPYCTSYYSYMMPVMGMTNCLASECFMKSDIFGQDFKTFDLLKYDFTEHKEVLFNKYFKYWGQDYHPDCVDCHDEMCILHCSNFNTLFATTIPNTAFGPLCRKVFIDGVPVVATAGYHFKQLGLVWNKDVNTHSTRLTITELLQFVTDPTLIVASSPALVDKRTVCFSVAALSTGLTSQTVKPGHFNKEFYDFLRSQGFFDEGSELTLKHFFFTQKGDAAIKDFDYYRYNRPTMLDIGQARVAYQVAARYFDCYEGGCITSREVVVTNLNKSAGWPLNKFGKAGLYYESISYEEQDAIFSLTKRNILPTMTQLNLKYAISGKERARTVGGVSLLATMTTRQFHQKCLKSIVATRNATVVIGTTKFYGGWDNMLKNLMADVDDPKLMGWDYPKCDRAMPSMIRMLSAMILGSKHVTCCTASDKFYRLSNELAQVLTEVVYSNGGFYFKPGGTTSGDATTAYANSVFNIFQAVSSNINCVLSVNSSNCNNFNVKKLQRQLYDNCYRNSNVDESFVDDFYGYLQKHFSMMILSDDSVVCYNKTYAGLGYIADISAFKATLYYQNGVFMSTAKCWTEEDLSIGPHEFCSQHTMQIVDENGKYYLPYPDPSRIISAGVFVDDITKTDAVILLERYVSLAIDAYPLSKHPKPEYRKVFYALLDWVKHLNKTLNEGVLESFSVTLLDEHESKFWDESFYASMYEKSTVLQAAGLCVVCGSQTVLRCGDCLRRPMLCTKCAYDHVFGTDHKFILAITPYVCNTSGCNVNDVTKLYLGGLNYYCVDHKPHLSFPLCSAGNVFGLYKSSALGSMDIDVFNKLSTSDWSDIRDYKLANDAKESLRLFAAETVKAKEESVKSSYAYATLKEIVGPKELLLLWESGKAKPPLNRNSVFTCFQITKDSKFQVGEFVFEKVDYGSDTVTYKSTATTKLVPGMLFILTSHNVAPLRAPTMANQEKYSTIYKLHPSFNVSDAYANLVPYYQLIGKQRITTIQGPPGSGKSHCSIGIGVYYPGARIVFTACSHAAVDSLCAKAVTAYSVDKCTRIIPARARVECYSGFKPNNNSAQYVFSTVNALPEVNADIVVVDEVSMCTNYDLSVINQRISYKHIVYVGDPQQLPAPRVLISKGVMEPIDYNVVTQRMCAIGPDVFLHKCYRCPAEIVNTVSELVYENKFVPVKEASKQCFKIFERGSVQVDNGSSINRRQLDVVKRFIHKNSTWSKAVFISPYNSQNYVAARLLGLQTQTVDSAQGSEYDYVIFAQTSDTAHACNANRFNVAITRAKKGIFCIMSDRTLFDALKFFEITMTDLQSESSCGLFKDCARNPIDLPPSHATTYLSLSDRFKTSGDLAVQIGNNNVCTYEHVISYMGFRFDVSMPGSHSLFCTRDFAMRHVRGWLGMDVEGAHVTGDNVGTNVPLQVGFSNGVDFVAQPEGCVLTNTGSVVKPVRARAPPGEQFTHIVPLLRKGQPWSVLRKRIVQMIADFLAGSSDVLVFVLWAGGLELTTMRYFVKIGAVKHCQCGTVATCYNSVSNDYCCFKHALGCDYVYNPYVIDIQQWGYVGSLSTNHHAICNVHRNEHVASGDAIMTRCLAVYDCFVKNVDWSITYPMIANENAINKGGRTVQSHIMRAAIKLYNPKAIHDIGNPKGIRCAVTDAKWYCYDKNPINSNVKTLEYDYMTHGQMDGLCLFWNCNVDMYPEFSIVCRFDTRTRSTLNLEGVNGGSLYVNNHAFHTPAYDKRAMAKLKPAPFFYYDDGSCEVVHDQVNYVPLRATNCITKCNIGGAVCSKHANLYRAYVESYNIFTQAGFNIWVPTTFDCYNLWQTFTEVNLQGLENIAFNVVNKGSFVGADGELPVAISGDKVFVRDGNTDNLVFVNKTSLPTNIAFELFAKRKVGLTPPLSILKNLGVVATYKFVLWDYEAERPLTSFTKSVCGYTDFAEDVCTCYDNSIQGSYERFTLSTNAVLFSATAVKTGGKSLPAIKLNFGMLNGNAIATVKSEDGNIKNINWFVYVRKDGKPVDHYDGFYTQGRNLQDFLPRSTMEEDFLNMDIGVFIQKYGLEDFNFEHVVYGDVSKTTLGGLHLLISQVRLSKMGILKAEEFVAASDITLKCCTVTYLNDPSSKTVCTYMDLLLDDFVSVLKSLDLTVVSKVHEVIIDNKPWRWMLWCKDNAVATFYPQLQSAEWKCGYSMPGIYKTQRMCLEPCNLYNYGAGLKLPSGIMFNVVKYTQLCQYFNSTTLCVPHNMRVLHLGAGSDYGVAPGTAVLKRWLPHDAIVVDNDVVDYVSDADFSVTGDCATVYLEDKFDLLISDMYDGRTKAIDGENVSKEGFFTYINGFICEKLAIGGSIAIKVTEYSWNKKLYELVQRFSFWTMFCTSVNTSSSEAFVVGINYLGDFAQGPFIDGNIIHANYVFWRNSTVMSLSYNSVLDLSKFNCKHKATVVVQLKDSDINEMVLSLVRSGKLLVRGNGKCLSFSNHLVSTK 6758 P0C6X2 2'-O-methyltransferase rep 443239 No SL-0382 [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}. UNIPROT P0C6X2 UNIPROT Q5MQD2 Pfam PF13087 Pfam PF16348 Pfam PF06478 Pfam PF11963 Pfam PF01661 Pfam PF16251 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF01831 Pfam PF05409 Pfam PF00680 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0008270 GO:0039595 GO:0039520 GO:0032259 GO:0039648 GO:0039579 GO:0039644 GO:0039502 GO:0006351 GO:0019079 GO:0019082 MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDIFVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFMPSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKLADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLSADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKAQSSGVIPENPVLFTNSTDTVNHDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALITHALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSYYLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATGWLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIPGFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLLDQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEHPVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEEIVTGDNDDQIVVTGDDVDDIESIYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGFVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGLDALFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELPQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWFCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQTMFDVYVDTFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDAFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFFVSLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVVVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMTLNGLWLDDKVYCPRHVICSSSNMNEPDYSALLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGNVKPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSTEDFNVWAMANGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGFTYVWLSYFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLSAIPALAANTLTIVIPDKQVFDKVVDNVYVTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYYNNGSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCVGSSVAVQSKDLNFLNRVRGTSVNARLVPCASGLSTDVQLRAFDICNTNRAGIGLYYKVNCCRFQRIDDDGNKLDKFFVVKRTNLEVYNKEKTYYELTKSCGVVAEHDFFTFDIDGSRVPHIVRRNLSKYTMLDLCYALRHFDRNDCSILCEILCEYADCKESYFSKKDWYDFVENPDIINIYKKLGPIFNRALLNTVIFADTLVEVGLVGVLTLDNQDLYGQWYDFGDFIQTAPGFGVAVADSYYSYMMPMLTMCHVLDCELFVNDSYRQFDLVQYDFTDYKLELFNKYFKYWGMKYHPNTVDCDNDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNLDVDTHRYRLSLKDLLLYAADPAMHVASASALLDLRTCCFSVAAITSGIKFQTVKPGNFNQDFYEFVKSKGLFKEGSTVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQNEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRHLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEFCCSHGDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVTANVCSLMACNGHKIEDLSIRNLQKRLYSNVYRTDYVDYTFVNEYYEFLCKHFSMMILSDDGVVCYNSDYASKGYIANISVFQQVLYYQNNVFMSESKCWVENDITNGPHEFCSQHTMLVKIDGDYVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVHHENEEYQKVFRVYLEYIKKLYNDLGTQILDSYSVILSTCDGLKFTEESFYKNMYLKSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATNHKYVLSVSPYVCNAPNCDVSDVTKLYLGGMSYYCENHKPHYSFKLVMNGMVFGLYKQSCTGSPYIDDFNKIASCKWTEVDDYVLANECIERLKLFAAETQKATEEAFKQSYASATIQEIVSDREVILCWETGKVKPPLNKNYVFTGYHFTSTGKTVLGEYVFDKSELTNGVYYRATTTYKLSIGDVFVLTSHSVASLSAPTLVPQENYASIRFSSVYSVPLVFQNNVANYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYYTARVVYTAASHAAVDALCEKAYKFLNINDCTRIIPAKVRVDCYDKFKINDTTCKYVFTTINALPELVTDIVVVDEVSMLTNYELSVINARIKAKHYVYIGDPAQLPAPRVLLSKGSLEPRHFNSITKIMCCLGPDIFLGNCYRCPKEIVETVSALVYDNKLKAKNDNSSLCFKVYFKGQTTHESSSAVNIQQIYLISKFLKANPVWNSAVFISPYNSQNYVAKRVLGVQTQTVDSAQGSEYDYVIYSQTAETAHSVNVNRFNVAITRAKKGIFCVMSNMQLFESLNFITLPLDKIQNQTLPRLHCTTNLFKDCSKSCLGYHPAHAPSFLAVDDKYKVNENLAVNLNICEPVLTYSRLISLMGFKLDLTLDGYSKLFITKDEAIKRVRGWVGFDVEGAHATRENIGTNFPLQIGFSTGVDFVVEATGLFAERDCYTFKKTVAKAPPGEKFKHLIPLMSKGQKWDIVRIRIVQMLSDYLLDLSDSVVFITWSASFELTCLRYFAKLGRELNCNVCSNRATCYNSRTGYYGCWRHSYTCDYVYNPLIVDIQQWGYTGSLTSNHDIICNVHKGAHVASADAIMTRCLAIYDCFCKSVNWNLEYPIISNEVSINTSCRLLQRVMLKAAMLCNRYNLCYDIGNPKGLACVKDYEFKFYDAFPVAKSVKQLFYVYDVHKDNFKDGLCMFWNCNVDKYPSNSIVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTNPFTRTVFENLKPMPFFYYSDTPCVYVDGLESKQVDYVPLRSATCITRCNLGGAVCSKHAEEYCNYLESYNIVTTAGFTFWVYKNFDFYNLWNTFTTLQSLENVIYNLVNVGHYDGRTGELPCAIMNDKVVVKINNVDTVIFKNNTSFPTNIAVELFTKRSIRHHPELKILRNLNIDICWKHVLWDYVKDSLFCSSTYGVCKYTDLKFIENLNILFDGRDTGALEAFRKARNGVFISTEKLSRLSMIKGPQRADLNGVIVDKVGELKVEFWFAMRKDGDDVIFSRTDSLCSSHYWSPQGNLGGNCAGNVIGNDALTRFTIFTQSRVLSSFEPRSDLERDFIDMDDNLFIAKYGLEDYAFDHIVYGSFNHKVIGGLHLLIGLFRRKKKSNLLIQEFLQYDSSIHSYFITDQECGSSKSVCTVIDLLLDDFVSIVKSLNLSCVSKVVNINVDFKDFQFMLWCNDNKIMTFYPKMQATNDWKPGYSMPVLYKYLNVPLERVSLWNYGKPINLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSDKEVAPGSAVLRQWLPSGSILVDNDLNPFVSDSLVTYFGDCMTLPFDCHWDLIISDMYDPLTKNIGDYNVSKDGFFTYICHLIRDKLSLGGSVAIKITEFSWNADLYKLMSCFAFWTVFCTNVNASSSEGFLIGINYLGKSSFEIDGNVMHANYLFWRNSTTWNGGAYSLFDMTKFSLKLAGTAVVNLRPDQLNDLVYSLIERGKLLVRDTRKEIFVGDSLVNTC 7182 P0C6Y3 Putative 2'-O-methyl transferase rep 11127 No SL-0382 [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}. UNIPROT P0C6Y3 UNIPROT Q0GNB9 UNIPROT Q0GNC0 UNIPROT Q5I5Y0 UNIPROT Q5I5Y1 PDB 2Q6D PDB 2Q6F PDB 5C94 Pfam PF16348 Pfam PF06478 Pfam PF01661 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF17896 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF00680 Pfam PF01443 Pfam PF08715 PROSITE PS51653 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 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}. GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004519 GO:0016896 GO:0008168 GO:0008242 GO:0003723 GO:0003724 GO:0003968 GO:0008270 GO:0039520 GO:0032259 GO:0006351 GO:0019082 GO:0039694 MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKITPGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMRRLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAGTCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQKAEIPVESEGWSAILGGHLCYVFKSGDRFYAAPLSGNFALHDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVAELVAAIKRGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLKLFQSARVKVEDVWSSLTEKSFEFWRLAYGKVRNLEEFVKTCFCKAQMAIVILATVLGEGIWHLVSQVIYKVGGLFTKVVDFCEKYWKGFCAQLKRAKLIVTETLCVLKGVAQHCFQLLLDAIQFMYKSFKKCALGRIHGDLLFWKGGVHKIIQEGDEIWFDAIDSIDVEDLGVVQEKLIDFDVCDNVTLPENQPGHMVQIEDDGKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVFIKVSIECCGEPWNTIFKKAYKEPIEVETDLTVEQLLSVVYEKMCDDLKLFPEAPEPPPFENVTLVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGDAEECDTNLECEEEDEDTKVLALIQDPASNKYPLPLDDDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKALPQKVIDVLGDWGEAVDAQEQLCQQESTRVISEKSVEGFTGSCDAMAEQAIVEEQEIVPVVEQSQDVVVFTPADLEVVKETAEEVDEFILISAVPKEEVVSQEKEEPQVEQEPTLVVKAQREKKAKKFKVKPATCEKPKFLEYKTCVGDLAVVIAKALDEFKEFCIVNAANEHMSHGGGVAKAIADFCGPDFVEYCADYVKKHGPQQKLVTPSFVKGIQCVNNVVGPRHGDSNLREKLVAAYKSVLVGGVVNYVVPVLSSGIFGVDFKISIDAMREAFKGCAIRVLLFSLSQEHIDYFDATCKQKTIYLTEDGVKYRSVVLKPGDSLGQFGQVFARNKVVFSADDVEDKEILFIPTTDKTILEYYGLDAQKYVTYLQTLAQKWDVQYRDNFVILEWRDGNCWISSAIVLLQAAKIRFKGFLAEAWAKLLGGDPTDFVAWCYASCNAKVGDFSDANWLLANLAEHFDADYTNALLKKCVSCNCGVKSYELRGLEACIQPVRAPNLLHFKTQYSNCPTCGASSTDEVIEASLPYLLLFATDGPATVDCDENAVGTVVFIGSTNSGHCYTQADGKAFDNLAKDRKFGRKSPYITAMYTRFSLRSENPLLVVEHSKGKAKVVKEDVSNLATSSKASFDDLTDFEQWYDSNIYESLKVQETPDNLDEYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFTYKLTPDTDENSKTPVYYPVLDSISLRAIWVEGSANFVVGHPNYYSKSLRIPTFWENAESFVKMGYKIDGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKILVKAATYVADKVGDGVVRNITDRIKGLCGFTRGHFEKKMSLQFLKTLVFFFFYFLKASSKSLVSSYKIVLCKVVFATLLIVWFIYTSNPVVFTGIRVLDFLFEGSLCGPYNDYGKDSFDVLRYCAGDFTCRVCLHDRDSLHLYKHAYSVEQIYKDAASGINFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLSSTVLQTGVGFLDWFVKTVFTHFNFMGAGFYFWLFYKIYVQVHHILYCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPTAYAYHVVYEACVVDDFVNLKYKAAIPGKDNASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKNAAVYYAQYLCKPILILDQALYEQLIVEPVSKSVIDKVCSILSNIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCHNHEVEYTGDGFTNVIPSYGMDTDKLTPRDRGFLINADASIANLRVKNAPPVVWKFSDLIKLSDSCLKYLISATVKSGGRFFITKSGAKQVISCHTQKLLVEKKAGGVINNTFKWFMSCFKWLFVFYILFTACCLGYYYMEMNKSFVHPMYDVNSTLHVEGFKVIDKGVIREIVSEDNCFSNKFVNFDAFWGKSYENNKNCPIVTVVIDGDGTVAVGVPGFVSWVMDGVMFVHMTQTDRRPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLIVPQQILHTPYIVKFVSDSYCRGSVCEYTKPGYCVSLDSQWVLFNDEYISKPGVFCGSTVRELMFNMVSTFFTGVNPNIYIQLATMFLILVVIVLIFAMVIKFQGVFKAYATIVFTIMLVWVINAFVLCVHSYNSVLAVILLVLYCYASMVTSRNTAIIMHCWLVFTFGLIVPTWLACCYLGFILYMYTPLVFWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGTEFVKLTNEIGDKFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEVVYTPPRYSIGVSRLQAGFKKLVSPSSAVEKCIVSVSYRGNNLNGLWLGDSIYCPRHVLGKFSGDQWGDVLNLANNHEFEVVTQNGVTLNVVSRRLKGAVLILQTAVANAETPKYKFVKANCGDSFTIACSYGGTVIGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSQPKWLESTTVSIEDYNRWASDNGFTPFSTSTAITKLSAITGVDVCKLLRTIMVKSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVPLKFYVHAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMLLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFMKLGFVIYTSSNTLTAYTEGNWELFFELVHTIVLANVSSNSLIGLIVFKCAKWMLYYCNATYFNNYVLMAVMVNGIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKVNPPKTVWEVFTTNILIQGIGGDRVLPIATVQSKLSDVKCTTVVLMQLLTKLNVEANSKMHAYLVELHNKILASDDVGECMDNLLGMLITLFCIDSTIDLGEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKSIYEKVLADSKNGGVTQQELAAYRKAANIAKSVFDRDLAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQANSGVVPLATVPIVCSNKLTLVIPDPETWVKCVEGVHVTYSTVVWNIDCVTDADGTELHPTSTGSGLTYCISGDNIAWPLKVNLTRNGHNKVDVALQNNELMPHGVKTKACVAGVDQAHCSVESKCYYTSISGSSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGDKVEVVYLYFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAITSKPSPTPDQDSYGGASVCLYCRAHIAHPGGAGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSLRQPKPSVQSVAVASGFDKNYLNRVRGSSEARLIPLANGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQEVRDTEDGNLEYCDSYFVVKQTTPSNYEHEKACYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEILVTYGCIEDYHPKWFEENKDWYDPIENPKYYAMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGDFQKTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQDLFQKYFKYWDQEYHPNCRDCSDDRCLIHCANFNILFSTLVPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALLVGTSNKLVDLRTSCFSVCALASGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRPTMFDIRQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFESTKKNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNAPVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKCDRAMPNLLRIAASLVLARKHTNCCTWSERVYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSANVARLLSVITRDIVYDDIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGFREVLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPRYLPYPDPSRILCACVFVDDLDKTESVAVMERYIALAIDAYPLVHHENEEYKKVFFVLLSYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNSQTILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQPGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVFGIYRANCAGSENVDDFNQLATTNWSTVEPYILANRCVDSLRRFAAETVKATEELHKQQFASAEVREVLSDRELILSWEPGKTRPPLNRNYVFTGFHFTRTSKVQLGDFTFEKGEGKDVVYYRATSTAKLSVGDIFVLTSHNVVSLIAPTLCPQQTFSRFVNLRPNVMVPACFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAAYFSNARVVFTACSHAAVDALCEKAFKFLKVDDCTRIVPQRTTIDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRTLLNGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRQCFKVIVNNGNSDVGHESGSAYNITQLEFVKDFVCRNKEWREATFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRAKRGILVVMRQRDELYSALKFIELDSVASLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITYKHLISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGNNFEPVNSKAPPGEQFNHLRALFKSAKPWHVVRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKDQVCSCGSRATTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASADAIMTRCLAINNAFCQDVNWDLTYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDLNFRFYDKNPIVPNVKQFEYDYNQHKDKFADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFHTPKFDRTSFRNLKAMPFFFYDSSPCETIQLDGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYADFVTSYNAAVTAGFTFWVTNNFNPYNLWKSFSALQSIDNIAYNMYKGGHYDAIAGEMPTIVTGDKVFVIDQGVEKAVFFNQTILPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYTNQTPLYRNTVKVCAYTDIEPNGLIVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGIPLKDGANLYVYKRVNGAFVTLPNTLNTQGRSYETFEPRSDVERDFLDMSEESFVEKYGKELGLQHILYGEVDKPQLGGLHTVIGMCRLLRANKLNAKSVTNSDSDVMQNYFVLADNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMAWFEDGIIKTCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGIALPSGIMMNVAKYTQLCQYLSKTTMCVPHNMRVMHFGAGSDKGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYKTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDVFIYLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLVGVNYLGASEKVKVSGKTLHANYIFWRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM 6631 P0C7N6 Nuclear protein localization protein 4 NPL4 321614 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT P0C7N6 UNIPROT Q0UV64 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0005789 GO:0031965 GO:0005634 GO:0048471 GO:0043130 GO:0031625 GO:0051028 GO:0015031 GO:0006511 MILRFVSKEGQFRLTVQPDSTFPELLAQIAEKLPKSVDLQSVTVSNRPQGGDARKISELKGVSFKQVGLSHGAQLFLGFEDQSTASNGHATAPTGANRLNGKVVEASDMPSVPLGSPTQVIKNPWEVVRQSPLDDKLDRQDGKIHRKRDARMCTHGPKGMCDYCMPLEPYAAAYLAEKKIKHLSFHSYLRKVNSAKNRPELGSSYIPPLTEPYYRVRPDCPSGHKPFPAGICTKCQPGAISLKPQEYRMVDHVEFASIQVVDDLINFWRNTGCQRLGFLYGRYEEYTEVPLGTKAVVETIYEPPQVNELDGISLGDWDNEKEIDEIAAQCGLQRVGVIFTDLLDADKGDGSVICKRHIDSYYLSSLEIAFAARYQAKYPRPTKWSETGKFGSNFVTCVISGDDQGQIGISSYQASNDAVEMVRADIIEPSAEPSVMLVQSEDDNEALNRARYIPEVFYRRINEHGANVQENAKPDFPVEYLFVTLTHGFPTQPNPLFTGGKFPIENREIMGEMPDVSALGKSLNAKANGLALNTTSGLNAISNFHMLCFIHNLGILSKDEESLLFKVASTHDTSEGSALQHTGGWATLLTILKESGERPPKRSYASPSFSATGRGAAHPGEKNRLMRQPSHGSDSDSVQLAKRLKGASLKGKE 653 P0C8N6 Nuclear envelope integral membrane protein 2 Nemp2 10116 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. UNIPROT P0C8N6 Pfam PF10225 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 MPPGSWWLVLWLPPLATLPAGAVPQEEAAMSVPRCKSLKETDLIKTSVSDCYCYNQHSQIEWTYMWSTVQVTVTSPGLLSIVYITGRHTCQHTETILSFLKCVTHNFWTAEEAKEVTIVFSPYGETVCFSVKPVGSLLTYAVSVNRNVVDFRLFLVFATGIFLFFYAKTLSQSPVFYYSSGTVLGILMTLVFVLLMTKKHIPKYSTFGALMIGCWFASVYVLCQLMENLKWLWCGNRIYVLGYVLVVGLCSFSACYSRGPPADEGSRDLLMWALRFLSLVLVYTGMAISQFAYAVMILLLLSWTRHYLLRAFSCLRWKVRQWFATRALVVRYLTDDEYREQAEAETASALEELRQACCRPDFPSWLAVSRLQAPKKFAEFVLGASHLSPEEVSTHEKQYGLGGAFLEEQLFSLQTESLPAS 421 P0CA01 p150 Ken 561445 No SL-0382 [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}. UNIPROT P0CA01 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}. GO:0042025 GO:0044220 GO:0019012 MGNRGSSTSSRPPLSSEANLYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIKAISKIGFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETICKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINSLTHGLRAEYLDVHGSIENTLENIKLLSDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFIDNILTPTQKELDKLKTDEVDIIKILNDTNSVLGTKNFGKVLSYTLCNLGIAATVANKINKALQRVGLKVEQYLHSKNWAEFDKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENNCAKKGGDGEKTPLDKRMEAQRLDRKHILMEFLNKSTQAYNDFLENVKKIGMKLVKEIALTPNITKLRDALSRINDMGTIALDLSLIGFYNNAAAREERETFLIQLTLVKNVLEELAKTDPNFKNLYDSCFRLLQIIDFYTDIVQKKYGGGEDCECTKVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYSNLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEVDWKATISAIELEYDVKRRFYRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEKVAAEIQQGRGVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQTVPMSPLQIYKTLLEYIQHSALSVGLKNLNQTQIGGQRVALAQTAEEASQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEPVYKLIPTRMILGGADELEPEVIPEAAGLYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRVIFMRPIELINIGDYSETEIRQLIKEINVIYQHFNLEYGEQEAVKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSILPDEDGYTQSSQLLPSDRFIGPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVSYQELIQQATNELKKEHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNTFRNNIKALDLDTIQKSIIEWLRETQAANVNRANLIDWLGRRHGDISEIRNPGLVIKANDARLSEVYPDPTTDATAPLDRNLVTETLFAWFTRFVGIPADGAVRPEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKLVQVRFPETSTAHVHLDFTGLISLIDSLMADTKYFLDLLRPHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYILLTKPYNVLQLRGGAQRGNAANIQINNNPEFSERYEQYGRVFSRLVFYDALIENSGLRVEQVALGDFRLSNLIRTNNAQEENALSFWTAVAPRAYANVNDAANNLRRYRLYGSDYGIRNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINTFANGNFSQAVMELGYAHPDLARDNTAFGHRGDPTEQSVLLLSLGLMLQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQYTKVQLARPNLTALLGANNDSIIYYNNNNVPNTGLTVGQAALRGIGSVFRPDITLMPLGNAQNNTNDVVRKRLIAVINGIIRGSLTLANSAMEVLHELTDHPIYFETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFKILYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYIHAIQALRFIINIRSFKTVMTYNENTFGGVNLIGEDRDDKPIITEGIGMNAVYSLRKTLQDVISFVESSYQEEQINNIHKIVSPRSQTRSLGSNRERERIFNLFDMNIMPINVNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLDTAAPQPDVAQVLNIPNRPPMNTREFMLKLLINPYVTVSITQYGNELLFRGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPGLAAGIQRGREQWGQPLSDYINQALHELVRTIRIIPQNIRVLRNIMVKNQLIADLAAIREQLVRMRREVENMVQTPEIQNNPTPEVIAAAQTWTQQYRARVDFLINFIGNAQQPNSLIQLIQNITPLTVRAQLTTVFIRHGLPVPDPDQALQTDDEATQWFMTNIINQPITMIIPFTDLADDLRIFLETMERYVFNVPRWLGPSTGRVARVPVNMAPGNIRYRTSYTENNVLTYIAEQNQEEGPWSIVKQVGVGIQKPALIQIGKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPNHIINPSITEYGFSITGPSETFSDKQYDSDIRIL 2475 P0CA05 p8 Ken 561445 No SL-0382 [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}. UNIPROT P0CA05 Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. GO:0044220 GO:0019012 MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILPFYIPTPMEFTGEIGSYTGVKLEVEKKEANKVILKNGEAVLIPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGNDPPVSKHISPYTPRTRIAIEVEKAFDECMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEPYKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADTATKEVDVPICYSDPETVHSYANHVRTEILHHNMVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIVRNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNDTQTGSQTSSLTDLVPTRLHSFLNHNLSKLKILNRAQQTVKNILSNDCLNQLKHYVKHTGKNEILKLLQE 534 P0CK47 Nuclear egress protein 1 NEC1 10377 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P0CK47 UNIPROT P03183 UNIPROT Q777G9 Pfam PF02718 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}. O15162 EBI-740019,EBI-2620189 P03185 EBI-2620196,EBI-2620189 Q9UBX5 EBI-947897,EBI-2620189 Q8N2S1 EBI-2620189,EBI-947718 P28799 EBI-2620189,EBI-747754 Q02818 EBI-2620189,EBI-2622179 Q12805 EBI-2620189,EBI-536772 P46379 EBI-2620189,EBI-347552 Q8WXE0 EBI-2622376,EBI-2620189 Q9Y228 EBI-2620189,EBI-765817 B2RCM5 EBI-2620189,EBI-2622428 Q9UEW3 EBI-2620189,EBI-2622414 A1L0V1 EBI-2620189,EBI-2622451 Q86V58 EBI-2620189,EBI-2622462 Q9NSC5 EBI-2620189,EBI-748420 P63279 EBI-80168,EBI-2620189 P55268 EBI-2529769,EBI-2620189 Q9UHF1 EBI-949532,EBI-2620189 Q6PKC3 EBI-2620189,EBI-749812 Q9UBP4 EBI-2620189,EBI-954409 Q93062 EBI-2620189,EBI-740322 Q96NA8 EBI-2620189,EBI-2622548 GO:0044201 GO:0016020 GO:0046872 GO:0046765 MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRSHFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEFSSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHIPETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ 318 P0CM10 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 214684 Yes SL-0178 SL-0182 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}. UNIPROT P0CM10 UNIPROT Q55XH5 UNIPROT Q5KMF9 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYCHGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNGPGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV 229 P0CP30 Nuclear protein localization protein 4 NPL4 214684 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT P0CP30 UNIPROT Q55VJ9 UNIPROT Q5KKN9 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0005789 GO:0031965 GO:0005634 GO:0048471 GO:0043130 GO:0031625 GO:0051028 GO:0015031 GO:0006511 MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLFLSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRHGDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICSTCQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTVETPWSDESRVQEIAKWCDKGLSVVGMIYTDLTPSPDDITKTLYKRHAQSYTASSLEMLLSAAYQLSHPLSTRMSPTGHYSSRFVTCCLTGDKDGGVDILAWQASEHAEAMVKAGIVEASVDPAVVRVRKPGEGEYVPEVFYSYKNEYGLQVKMPAKPTFPVEYLYVNITHGFPLAPSPLFLSNAFPTENRPGLHDQSMQVVITQLAAILKTSDAEIGDAGTWPGRIKKDVEKWLSDWHLVTFLCMQGLFSLKEQQILCRAATAHAHPNDTHALEELFASGGWQTLLTIVDSEASANARSNPPPTSSFNNLGIDSPAFAGPSTESSAPPSGPDSVGAGAGAGAGGGRERVCPHCTFVNEHGGSDCEICGLPLDG 693 P0CQ86 ATP-dependent RNA helicase DBP5 DBP5 214684 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P0CQ86 UNIPROT Q55NB1 UNIPROT Q5KBP4 UNIPROT Q5KBP5 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0003723 GO:0003724 GO:0016973 MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAGASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLMKGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVIDQIGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLPPNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVTADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETYIHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA 546 P0CS50 Protein transport protein SEC13 SEC13 214684 Yes SL-0178 SL-0185 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}. UNIPROT P0CS50 UNIPROT Q55MW6 UNIPROT Q5KB95 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0030127 GO:0005829 GO:0005789 GO:0000139 GO:0031080 GO:0005198 GO:0090114 GO:0051028 GO:1904263 GO:0015031 MCLWPLIQSAQASKPVPVETQHEDMIHDAQLDYYGKRLATCSSDRTIRIFNVIKGEAKGEPVILKGHTAAVWQVSWAHPSFGSILASCSYDGRVFIWKEVGQGQGKGSGGELQDGWERIKEHTLHTASVNSIAWAPYDLGPILACASSDGKVSVLSFQNDGSIEVNIFPAHGTGANAISWAPSVLSTVSGVSRSQQPSNSLAPQKRFVTAGSDNLIRIWGFDEEQKKWTEEETIKGHEDWVRDVAWAPNIGLPGMYIASASQDRTVLIHSRPSPSSSWTSAPLLPSLPQSQDPHFPDAVWRVSWSLAGNVLAVSCGDGKVSLWKEGVGKGWECVSDFSS 339 P0CU06 UPF0742 protein SPAC750.04c SPAC750 284812 Yes SL-0178 SL-0182 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}. UNIPROT P0CU06 UNIPROT Q9P332 Pfam PF09437 DE Reference Proteome: Yes; GO:0005737 GO:0016021 GO:0031965 MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR 146 P0DPK0 Protein CUSTOS custos 8355 No SL-0178 Nucleus envelope {ECO:0000269|PubMed:25157132}. UNIPROT P0DPK0 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}. GO:0005635 GO:0007275 GO:0030178 GO:0060061 GO:0016055 MAAPRRGTQKSDSDSSDEDLDRFREAAWVPPGAHQKVSDEQNEKIALPSLRVRPDCHEHDGNELQTTPEFRSHVAKKLAAILDSSIREVSQNEAVHISKAGNGDSEDEGFRLFRTSLPGEAGIVTSTIPRRKLASSSSEDSEEEQQRCREAAVSACDILRHSTLQQEPQSTPSNVCDNQPPKKKRKKKKKDRGDTSQINSVEETMHIEPGKNELQAKRKKKKKQKLEMAHCDELGNE 237 P0DPR2 E3 ubiquitin-protein ligase RNF43 rnf43 8364 Yes SL-0178 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}. UNIPROT P0DPR2 Pfam PF13639 Pfam PF18212 PROSITE PS50089 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}. GO:0005789 GO:0016021 GO:0005635 GO:0005886 GO:0046872 GO:0016740 GO:0007275 GO:0016567 GO:0016055 MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFHPLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWGPDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRRYQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPRPLAHRAPSQTQLWGRYPGSARLMSHLPPHGTPMVFPTPNNSLFLPRAPYYLDHTHHWQMPEQMAMQMRTHRRGAEGTRELGISPGCQDSSGYLPDDPGSDSSSGPCHGSSSENCTDISLHCLHGTSSSSVHSSQSNQEDSSPPALASYLLPQGELPALNPLLSTQASYASHVHFHQHRHHHYRRNQPSMSHSHPHRSKRRTKVSRADPSYYREHRHTTGANGELRSLMVRREPRPSCSRTCFDPRTNREHPRHQQSMPQAASVVQGSSEPDVATSLRGSRTDPPSRTYRKKKSSAPSHLPLLYSPRHCHPANSVQMSESSHPRWAEEVRLLHSRVNSHRENTAMMHLYHPPHHNQGATEEIEAVCEHAV 689 P0DTD1 2'-O-methyltransferase rep 2697049 Yes SL-0382 [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}. UNIPROT P0DTD1 PDB 5R7Y PDB 5R7Z PDB 5R80 PDB 5R81 PDB 5R82 PDB 5R83 PDB 5R84 PDB 5RE4 PDB 5RE5 PDB 5RE6 PDB 5RE7 PDB 5RE8 PDB 5RE9 PDB 5REA PDB 5REB PDB 5REC PDB 5RED PDB 5REE PDB 5REF PDB 5REG PDB 5REH PDB 5REI PDB 5REJ PDB 5REK PDB 5REL PDB 5REM PDB 5REN PDB 5REO PDB 5REP PDB 5RER PDB 5RES PDB 5RET PDB 5REU PDB 5REV PDB 5REW PDB 5REX PDB 5REY PDB 5REZ PDB 5RF0 PDB 5RF1 PDB 5RF2 PDB 5RF3 PDB 5RF4 PDB 5RF5 PDB 5RF6 PDB 5RF7 PDB 5RF8 PDB 5RF9 PDB 5RFA PDB 5RFB PDB 5RFC PDB 5RFD PDB 5RFE PDB 5RFF PDB 5RFG PDB 5RFH PDB 5RFI PDB 5RFJ PDB 5RFK PDB 5RFL PDB 5RFM PDB 5RFN PDB 5RFO PDB 5RFP PDB 5RFQ PDB 5RFR PDB 5RFS PDB 5RFT PDB 5RFU PDB 5RFV PDB 5RFW PDB 5RFX PDB 5RFY PDB 5RFZ PDB 5RG0 PDB 6LU7 PDB 6M03 PDB 6VWW PDB 6W01 PDB 6W02 PDB 6W61 PDB 6W63 PDB 6W6Y PDB 6W75 PDB 6Y2E PDB 6Y2F PDB 6Y2G PDB 6Y84 PDB 6YB7 Pfam PF13604 Pfam PF16348 Pfam PF06478 Pfam PF12379 Pfam PF01661 Pfam PF16251 Pfam PF11501 Pfam PF09401 Pfam PF06471 Pfam PF06460 Pfam PF12124 Pfam PF08716 Pfam PF08717 Pfam PF08710 Pfam PF05409 Pfam PF11633 Pfam PF08715 PROSITE PS00867 PROSITE PS51653 PROSITE PS00213 PROSITE PS51442 PROSITE PS51154 PROSITE PS51124 PROSITE PS51657 PROSITE PS50507 [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}. O75569 EBI-25475891,EBI-713955 O95831 EBI-25475880,EBI-356440 P04406 EBI-25475880,EBI-354056 P31689 EBI-25475871,EBI-347834 P35658 EBI-25475877,EBI-1222270 P37198 EBI-25475877,EBI-347978 P49454 EBI-25475888,EBI-968343 P57088 EBI-25475871,EBI-1048629 P61026 EBI-25475871,EBI-726075 P61970 EBI-25475891,EBI-591778 P63244 EBI-25475874,EBI-296739 Q06787 EBI-25492388,EBI-366305 Q15056 EBI-25475877,EBI-748492 Q5JTV8 EBI-25475871,EBI-2559665 Q6ZRP7 EBI-25475871,EBI-11127401 Q7Z3B4 EBI-25475877,EBI-741048 Q86UE4 EBI-25475891,EBI-1046588 Q8NC51 EBI-25475864,EBI-523558 Q8TEM1 EBI-25475862,EBI-372826 Q99567 EBI-25475877,EBI-726178 Q99720 EBI-25475868,EBI-3248663 Q9BV73 EBI-25475888,EBI-1053100 Q9BVL2 EBI-25475877,EBI-2811583 Q9H7Z7 EBI-25475871,EBI-681645 Q9UM54 EBI-25475864,EBI-350606 GO:0044172 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0003678 GO:0004519 GO:0004527 GO:0046872 GO:0008168 GO:0003723 GO:0003724 GO:0003968 GO:0036459 GO:0039595 GO:0039520 GO:0032259 GO:0039648 GO:0039579 GO:0039644 GO:0039502 MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDYVYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHMVVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPANSIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQSLENVAFNVVNKGHFDGQQGEVPVSIINNTVYTKVDGVDVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVDIAANTVIWDYKRDAPAHISTIGVCSMTDIAKKPTETICAPLTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPKQASLNGVTLIGEAVKTQFNYYKKVDGVVQQLPETYFTQSRNLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYGDFSHSQLGGLHLLIGLAKRFKESPFELEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVVKVTIDYTEISFMLWCKDGHVETFYPKLQSSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQKLALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN 7096 P10160 Eukaryotic translation initiation factor 5A-1 EIF5A 9986 Yes SL-0178 SL-0185 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}. UNIPROT P10160 Pfam PF01287 PROSITE PS00302 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}. GO:0005789 GO:0005643 GO:0043022 GO:0003746 GO:0051028 GO:0045727 GO:0045901 GO:0045905 GO:0015031 GO:0006452 MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDSGEEILITVLSAMTEEAAVAIKAMAK 154 P10204 Protein UL20 UL20 10299 Yes SL-0415 SL-0418 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}. UNIPROT P10204 Pfam PF04544 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}. P10221 EBI-7906325,EBI-6880600 P68331 EBI-7906325,EBI-7906305 GO:0044178 GO:0044200 GO:0016021 GO:0019012 GO:0019058 MTMRDDLPLVDRDLVDEAAFGGEEGELPLEEQFSLSSYGTSDFFVSSAYSRLPPHTQPVFSKRVILFLWSFLVLKPLEMVAAGMYYGLTGRVVAPACILAAIVGYYVTWAVRALLLYVNIKRDRLPLSAPVFWGMSVFLGGTALCALFAAAHETFSPDGLFHFIATNQMLPPTDPLRTRALGIACAAGASMWVAAADSFAASANFFLARFWTRAILNAPVAF 222 P10215 Nuclear egress protein 1 NEC1 10299 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P10215 PDB 4ZXS Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046802 GO:0046765 MYDTDPHRRGSRPGPYHGKERRRSRSSAAGGTLGVVRRASRKSLPPHARKQELCLHERQRYRGLFAALAQTPSEEIAIVRSLSVPLVKTTPVSLPFCLDQTVADNCLTLSGMGYYLGIGGCCPACNAGDGRFAATSREALILAFVQQINTIFEHRAFLASLVVLADRHNAPLQDLLAGILGQPELFFVHTILRGGGACDPRLLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPGYRFVAHVWQSTFVLVVRRNAEKPTDAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP 306 P10415 Apoptosis regulator Bcl-2 BCL2 9606 Yes SL-0178 SL-0182 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}. UNIPROT P10415 UNIPROT C9JHD5 UNIPROT P10416 UNIPROT Q13842 UNIPROT Q16197 PDB 1G5M PDB 1GJH PDB 1YSW PDB 2O21 PDB 2O22 PDB 2O2F PDB 2W3L PDB 2XA0 PDB 4AQ3 PDB 4IEH PDB 4LVT PDB 4LXD PDB 4MAN PDB 5AGW PDB 5AGX PDB 5FCG PDB 5JSN PDB 5VAU PDB 5VAX PDB 5VAY PDB 6GL8 PDB 6IWB PDB 6O0K PDB 6O0L PDB 6O0M PDB 6O0O PDB 6O0P Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 OMIM 151430 DisGeNET 596 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}.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}. O60238 EBI-77694,EBI-849893 Self EBI-77694,EBI-77694 P22736 EBI-721550,EBI-77694 Q07817-1 EBI-287195,EBI-77694 O43521-1 EBI-526416,EBI-77694 O43521-2 EBI-77694,EBI-526420 Q14790 EBI-77694,EBI-78060 Q9BXH1 EBI-519884,EBI-77694 P38398 EBI-77694,EBI-349905 P0DM65 EBI-77694,EBI-8839540 Q14457 EBI-77694,EBI-949378 A8MW95 EBI-77694,EBI-8839517 Q9NYF8 EBI-77694,EBI-437804 Q7CHR0 EBI-2853517,EBI-77694 Q16611 EBI-77694,EBI-519866 O43521 EBI-77694,EBI-526406 Q07812 EBI-77694,EBI-516580 P04637 EBI-366083,EBI-77694 P55957 EBI-519672,EBI-77694 O43521-4 EBI-6137933,EBI-77694 O43521-5 EBI-2123756,EBI-77694 O43521-6 EBI-2123760,EBI-77694 O43521-3 EBI-2123748,EBI-77694 Q96LC9 EBI-77694,EBI-3919268 Q61337 EBI-400328,EBI-77694 Q13323 EBI-700794,EBI-77694 Q13794 EBI-77694,EBI-707392 Q9C000 EBI-77694,EBI-1220518 P62136 EBI-77694,EBI-357253 P36873-1 EBI-356289,EBI-77694 P62140 EBI-352350,EBI-77694 Q86Y07 EBI-77694,EBI-1207615 Q91ZE9 EBI-708032,EBI-77694 P59635 EBI-25492879,EBI-77694 Q7L3V2 EBI-10697720,EBI-77694 Q92934 EBI-700771,EBI-77694 O54918 EBI-77694,EBI-526067 Q07813 EBI-700711,EBI-77694 P51572 EBI-77683,EBI-77694 Q9BXH1-1 EBI-519891,EBI-77694 Q9BXH1-2 EBI-519896,EBI-77694 GO:0005623 GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0016020 GO:0005741 GO:0005739 GO:0043209 GO:0031965 GO:0005654 GO:0005634 GO:0046930 GO:0032991 GO:0051434 GO:0015267 GO:0016248 GO:0042802 GO:0002020 GO:0046982 GO:0042803 GO:0051721 GO:0070491 GO:0043565 GO:0031625 GO:0007015 GO:0006915 GO:0031103 GO:0007409 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0001658 GO:0043375 GO:0007569 GO:0098609 GO:0006974 GO:0042149 GO:0071456 GO:0021747 GO:0019221 GO:0051607 GO:0048546 GO:0043583 GO:0032469 GO:0097192 GO:0008625 GO:0007565 GO:0048041 GO:0022612 GO:0032835 GO:0031069 GO:0048873 GO:0006959 GO:0008630 GO:0070059 GO:0008631 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:2000811 GO:0043066 GO:2001234 GO:0010507 GO:0010523 GO:0030308 GO:0030336 GO:0032848 GO:2001240 GO:2000134 GO:2001243 GO:1902166 GO:0051902 GO:0033033 GO:0043524 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0051402 GO:0048599 GO:0035265 GO:0001503 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0030890 GO:0043085 GO:0030307 GO:0008284 GO:2001244 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:1900740 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0051924 GO:0001952 GO:0010468 GO:0010559 GO:0046902 GO:0051881 GO:0006808 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0034097 GO:0042493 GO:0010332 GO:0051384 GO:0042542 GO:0010039 GO:0002931 GO:0035094 GO:0009314 GO:0009636 GO:0010224 GO:0048536 GO:0033077 GO:0043029 GO:0048538 MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK 239 P10536 Ras-related protein Rab-1B Rab1b 10116 Yes SL-0198 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}. UNIPROT P10536 Pfam PF00071 PROSITE PS51419 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}. P19357 EBI-915426,EBI-916259 GO:0012505 GO:0005793 GO:0048471 GO:0034045 GO:0045202 GO:0005525 GO:0003924 GO:0000045 GO:0006888 GO:0006886 GO:1903020 GO:0032482 GO:2000785 GO:0019068 MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC 201 P10544 E1B protein, small T-antigen E1BS 10524 No SL-0415 SL-0416 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}. UNIPROT P10544 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 MEFWSELQSYQSLRRLLELASARTSSCWRFIFGSTLTNVIYRAKEDYSSRFAELLSFNPGIFASLNLGHHSFFQEIVIKNLDFSSPGRTVSGLAFICFILDQWSAQTHLSEGYTLDYMTMALWRTLLRRKRVLGCSPAQPPHGLDPVREEEEEEEEEENLRAGLDPQTEL 170 P10687 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 Plcb1 10116 Yes SL-0178 SL-0182 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}. UNIPROT P10687 Pfam PF06631 Pfam PF09279 Pfam PF17787 Pfam PF00388 Pfam PF00387 Pfam PF08703 PROSITE PS50004 PROSITE PS50007 PROSITE PS50008 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. P51692 EBI-1186119,EBI-7551252 P17948 EBI-1026718,EBI-7551252 Q96T51 EBI-3941207,EBI-7551252 P54578 EBI-1048016,EBI-7551252 GO:0005623 GO:0005737 GO:0005829 GO:0098982 GO:0098978 GO:0016020 GO:0000790 GO:0031965 GO:0016607 GO:0005634 GO:0098794 GO:0032991 GO:0005509 GO:0005516 GO:0019899 GO:0005096 GO:0042802 GO:0005521 GO:0004435 GO:0005546 GO:0060466 GO:0007420 GO:1902618 GO:1905631 GO:1904637 GO:1904117 GO:0021987 GO:0045444 GO:0007213 GO:0000086 GO:0007215 GO:0032959 GO:0032957 GO:0048009 GO:0070498 GO:0035722 GO:0035723 GO:0007612 GO:0007613 GO:2000438 GO:0045892 GO:0031161 GO:0046488 GO:0048015 GO:2000344 GO:2000560 GO:0048639 GO:0040019 GO:1900087 GO:0032735 GO:0046330 GO:0045663 GO:0045893 GO:0099170 GO:0080154 GO:0008277 GO:0099178 GO:0051209 GO:0034284 GO:0010243 GO:0043434 MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFETSKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTATLAPKPPSQAPHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQMELEQEYQDKFKRLPLEILEFVQEAMKGKVSEDSNHGSAPPSLASDPAKVNLKSPSSEEVQGENAGREFDTPL 1216 P10909 Clusterin alpha chain CLU 9606 Yes SL-0198 [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}. UNIPROT P10909 UNIPROT B2R9Q1 UNIPROT B3KSE6 UNIPROT P11380 UNIPROT P11381 UNIPROT Q2TU75 UNIPROT Q5HYC1 UNIPROT Q7Z5B9 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 OMIM 185430 DisGeNET 1191 [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}. Self EBI-1104674,EBI-1104674 P62993 EBI-1104674,EBI-401755 Q5S007 EBI-5323863,EBI-1104674 Q9H4B6 EBI-1104674,EBI-1017775 Q92610 EBI-1210420,EBI-1104674 Q9Y2B5 EBI-9031083,EBI-1104674 P31321 EBI-2805516,EBI-1104674 Q9NPF5 EBI-399105,EBI-1104674 Q58WW2 EBI-2559044,EBI-1104674 Q6NUQ1 EBI-726876,EBI-1104674 Q9BXM7 EBI-2846068,EBI-1104674 Q07890 EBI-298181,EBI-1104674 Q99615 EBI-357552,EBI-1104674 P26640 EBI-355765,EBI-1104674 Q15059 EBI-1383460,EBI-1104674 Q9C093 EBI-1220460,EBI-1104674 Q9H974 EBI-1221028,EBI-1104674 Q96MT8 EBI-741977,EBI-1104674 Q14515 EBI-2682673,EBI-1104674 Q96K75 EBI-6660752,EBI-1104674 Q9Y6D5 EBI-2837511,EBI-1104674 Q15185 EBI-1049387,EBI-1104674 Q9UBU8 EBI-399246,EBI-1104674 Q96PY5 EBI-3438448,EBI-1104674 Q9NRI5 EBI-1104674,EBI-529989 Q06787 EBI-1104674,EBI-366305 Q9UKE5 EBI-1104674,EBI-1051794 P11766 EBI-717798,EBI-1104674 Q7Z699 EBI-5235340,EBI-1104674 P14868 EBI-358730,EBI-1104674 P36957 EBI-351007,EBI-1104674 Q7Z698 EBI-7082156,EBI-1104674 Q9UL68 EBI-1105008,EBI-1104674 O75592 EBI-1043774,EBI-1104674 Q86TG7 EBI-2858265,EBI-1104674 P02794 EBI-713259,EBI-1104674 Q6AI39 EBI-1012434,EBI-1104674 Q6GYQ0 EBI-3957100,EBI-1104674 Q96EK5 EBI-744150,EBI-1104674 Q00994 EBI-741753,EBI-1104674 F8VWT9 EBI-21378194,EBI-1104674 Q13439 EBI-1037845,EBI-1104674 P08238 EBI-352572,EBI-1104674 P07900 EBI-296047,EBI-1104674 Q6ZMI3 EBI-21379491,EBI-1104674 Q5SZL2 EBI-2514702,EBI-1104674 P26367 EBI-747278,EBI-1104674 Q9NR80 EBI-3389984,EBI-1104674 Q9UBW8 EBI-712982,EBI-1104674 Q9Y575 EBI-2875625,EBI-1104674 P48426 EBI-3924422,EBI-1104674 Q9BZ95 EBI-3390132,EBI-1104674 Q9NVR2 EBI-536703,EBI-1104674 Q9NWB6 EBI-2808785,EBI-1104674 Q5VTB9 EBI-949963,EBI-1104674 P53041 EBI-716663,EBI-1104674 Q9Y275 EBI-519169,EBI-1104674 Q14108 EBI-1564650,EBI-1104674 Q9NRD1 EBI-3938499,EBI-1104674 P17028 EBI-1104674,EBI-707773 P01100 EBI-852851,EBI-1104674 P37231 EBI-781384,EBI-1104674 P02866 EBI-2905940,EBI-1104674 P22736 EBI-1104674,EBI-721550 Q00987 EBI-1104674,EBI-389668 P04150 EBI-493507,EBI-1104674 O35638 EBI-2552452,EBI-1104674 P16104 EBI-494830,EBI-1104674 O15160 EBI-1104674,EBI-1055079 P05181 EBI-1104674,EBI-3907388 Q99708 EBI-1104674,EBI-745715 O14901 EBI-948266,EBI-1104674 Q14145 EBI-1104674,EBI-751001 Q9Y3Q8 EBI-739485,EBI-1104674 P51114-2 EBI-1104674,EBI-11022345 P30101 EBI-1104674,EBI-979862 Q96HP0 EBI-1104674,EBI-4401295 Q7Z333-3 EBI-1104674,EBI-11025482 Q5VW52 EBI-1104674,EBI-10973822 P27824 EBI-1104674,EBI-355947 Q07817-1 EBI-1104674,EBI-287195 Q9BWU1 EBI-394593,EBI-1104674 P45984 EBI-1104674,EBI-713568 P62829 EBI-1104674,EBI-353303 P46379 EBI-1104674,EBI-347552 P02647 EBI-701692,EBI-1104674 P01876 EBI-727651,EBI-1104674 P01857 EBI-356114,EBI-1104674 P27918 EBI-9038570,EBI-1104674 P37840 EBI-985879,EBI-1104674 A0A1J9WIU5 EBI-1104674,EBI-2811961 P03428 EBI-2547475,EBI-1104674 GO:0097440 GO:0072562 GO:0009986 GO:0042583 GO:0062023 GO:0005737 GO:0005829 GO:0070062 GO:0005576 GO:0005615 GO:0005794 GO:0043231 GO:0005743 GO:0005739 GO:0097418 GO:0005634 GO:0099020 GO:0048471 GO:0031093 GO:0032991 GO:0034366 GO:0045202 GO:0001540 GO:0051087 GO:0050750 GO:0051787 GO:0046982 GO:0044877 GO:0005102 GO:0048156 GO:0031625 GO:0051082 GO:0019730 GO:0000902 GO:0032286 GO:0051131 GO:0061077 GO:0061741 GO:0006956 GO:0006958 GO:0002434 GO:0045087 GO:0097193 GO:0006629 GO:0001774 GO:0061518 GO:1905907 GO:1902430 GO:0060548 GO:1905892 GO:1905895 GO:1902230 GO:0031333 GO:0090201 GO:1903573 GO:0002576 GO:1905908 GO:1902004 GO:0043065 GO:0010628 GO:2001244 GO:1902998 GO:1901216 GO:0051092 GO:0045429 GO:0032436 GO:0031334 GO:0048260 GO:1902949 GO:0032760 GO:2000060 GO:0017038 GO:0050821 GO:0061740 GO:1900221 GO:0042981 GO:0042127 GO:0030449 GO:1901214 GO:1902847 GO:0001836 GO:0051788 GO:0009615 GO:0043691 MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE 449 P10999 Lamin-L(III) LAML3 8355 No SL-0178 SL-0179 SL-0182 Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. UNIPROT P10999 UNIPROT P23420 UNIPROT Q6AZG7 Pfam PF00038 Pfam PF00932 PROSITE PS00226 PROSITE PS51842 PROSITE PS51841 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. GO:0005882 GO:0005637 MATSTPSRAREHASAAQSPGSPTRISRMQEKEDLRHLNDRLAAYIERVRSLEADKSLLKIQLEEREEVSSREVTNLRQLYETELADARKLLDQTANERARLQVELGKVREEYRQLQARNSKKENDLSLAQNQLRDLESKLNTKEAELATALSGKRGLEEQLQEQRAQIAGLESSLRDTTKQLHDEMLWRVDLENKMQTIREQLDFQKNIHTQEVKEIKKRHDTRIVEIDSGRRVEFESKLAEALQELRRDHEQQILEYKEHLEKNFSAKLENAQLAAAKNSDYASATREEIMATKLRVDTLSSQLNHYQKQNSALEAKVRDLQDMLDRAHDMHRRQMTEKDREVTEIRQTLQGQLEEYEQLLDVKLALDMEINAYRKMLEGEEQRLKLSPSPSQRSTVSRASTSQTSRLLRGKKRKLDETGRSVTKRSYKVVQQASSTGPVSVEDIDPEGNYVRLLNNTEEDFSLHGWVVKRMHMSLPEIAFKLPCRFILKSSQRVTIWAAGAGAVHSPPTDLVWKSQKTWGTGDNIKITLLDSTGEECAERTLYRVIGEEGETDEDFVEEEELERQFRSQSHQSVDPSCSIM 583 P11017 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 GNB2 9913 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P11017 UNIPROT A5D7A9 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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. GO:0005834 GO:0048471 GO:0003924 GO:0051020 GO:0044877 GO:0007165 MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN 340 P11048 Lamin-A lmna 8355 No SL-0178 Nucleus. Nucleus envelope {ECO:0000269|PubMed:25157132}. UNIPROT P11048 Pfam PF00038 Pfam PF00932 PROSITE PS00226 PROSITE PS51842 PROSITE PS51841 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. GO:0005882 GO:0005635 METPGQKRATRSTHTPLSPTRITRLQEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVISREVTGIKSAYETELADARKTLDSVAKERARLQLELSKIREEHKELKARNAKKESDLLTAQARLKDLEALLNSKDAALTTALGEKRNLENEIRELKAHIAKLEASLADTKKQLQDEMLRRVDTENRNQTLKEELEFQKSIYNEEMRETKRRHETRLVEVDNGRQREFESKLADALHELRAQHEGQIGLYKEELGKTYNAKLENAKQSAERNSSLVGEAQEEIQQSRIRIDSLSAQLSQLQKQLAAREAKLRDLEDAYARERDSSRRLLADKDREMAEMRARMQQQLDEYQELLDIKLALDMEINAYRKLLEGEEERLRLSPSPNTQKRSARTIASHSGAHISSSASKRRRLEEGESRSSSFTQHARTTGKVSVEEVDPEGKYVRLRNKSNEDQSLGNWQIKRQIGDETPIVYKFPPRLTLKAGQTVTIWASGAGATNSPPSDLVWKAQSSWGTGDSIRTALLTSSNEEVAMRKLVRTVVINDEDDEDNDDMEHHHHHHHHHHDGQNSSGDPGEYNLRSRTIVCTSCGRPAEKSVLASQGSGLVTGSSGSSSSSVTLTRTYRSTGGTSGGSGLGESPVTRNFIVGNGQRAQVAPQNCSIM 665 P11147 Heat shock 70 kDa protein cognate 4 Hsc70 7227 Yes SL-0198 Cytoplasm, perinuclear region. Nucleus. Note=Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress. UNIPROT P11147 UNIPROT Q3KN45 UNIPROT Q8SXQ4 UNIPROT Q9VFB0 Pfam PF00012 PROSITE PS00297 PROSITE PS00329 PROSITE PS01036 DE Reference Proteome: Yes; Q24133 EBI-75181,EBI-87640 P83949 EBI-75181,EBI-202590 P25439 EBI-868480,EBI-75181 Q9VRQ2 EBI-75181,EBI-169350 Q03751 EBI-75181,EBI-604931 Q9XZC2 EBI-75181,EBI-458892 Q24570 EBI-75181,EBI-167445 Q9VZF4 EBI-75181,EBI-138334 Q9VWE4 EBI-75181,EBI-122539 Q9VML8 EBI-75181,EBI-152952 Q9VU81 EBI-75181,EBI-179238 Q8IRH9 EBI-75181,EBI-162060 Q9VLG9 EBI-75181,EBI-86290 Q24216 EBI-139668,EBI-75181 Q9VNE0 EBI-75181,EBI-159712 Q9I7H9 EBI-139392,EBI-75181 Q9VRQ6 EBI-75181,EBI-194555 Q9VC50 EBI-75181,EBI-85761 Q9W5G1 EBI-75181,EBI-103112 Q9V3F2 EBI-75181,EBI-90755 Q9XYW6 EBI-75181,EBI-135209 P40301 EBI-98978,EBI-75181 Q7JXC4 EBI-75181,EBI-151216 Q9VUQ1 EBI-75181,EBI-162539 Q9W0B2 EBI-75181,EBI-89242 Q5BI03 EBI-102987,EBI-75181 Q9VRV9 EBI-181097,EBI-75181 Q9VIJ0 EBI-75181,EBI-94912 P29413 EBI-75181,EBI-192552 Q8IR79 EBI-149780,EBI-75181 Q9W3N7 EBI-75181,EBI-95849 Q9VIY9 EBI-75181,EBI-82519 Q9VJB0 EBI-75181,EBI-152945 Q9VMA3 EBI-75181,EBI-95398 Q9VNV2 EBI-75181,EBI-172319 Q9VI55 EBI-75181,EBI-172922 O96757 EBI-74922,EBI-75181 Q9VLI5 EBI-75181,EBI-154623 Q9VVC2 EBI-75181,EBI-141024 GO:0071013 GO:0005737 GO:0005829 GO:0005739 GO:0005634 GO:0005726 GO:0048471 GO:0005886 GO:0071011 GO:0098793 GO:0005524 GO:0016887 GO:0042623 GO:0051087 GO:0031072 GO:0051787 GO:0044183 GO:0051082 GO:0007411 GO:0007413 GO:0035967 GO:0034620 GO:0051085 GO:0061077 GO:0070868 GO:0061738 GO:0097753 GO:0000398 GO:0007399 GO:0007269 GO:0030707 GO:0106161 GO:0006457 GO:0042026 GO:0006986 GO:0016246 GO:0016192 MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDDAAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTHFVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKALRDAKLDKSVIHDIVLVGGSTRIPKVQRLLQDLFNGKELNKSINPDEAVAYGAAVQAAILHGDKSQEVQDLLLLDVTPLSLGIETAGGVMSVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVTALERSTNKENKITITNDKGRLSKEDIERMVNEAEKYRNEDEKQKETIAAKNGLESYCFNMKATLDEDNLKTKISDSDRTTILDKCNETIKWLDANQLADKEEYEHRQKELEGVCNPIITKLYQGAGFPPGGMPGGPGGMPGAAGAAGAAGAGGAGPTIEEVD 651 P11317 Early E3 9.0 kDa glycoprotein E311 45659 No SL-0415 SL-0418 Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT P11317 DE Reference Proteome: No; GO:0044200 GO:0016021 MILFQSNTTTSYAYTNIQPKYAMQLEITILIVIGILILSVILYFIFCRQIPNVHRNSKRRPIYSPMISRPHMALNEI 77 P11936 Deoxyribonuclease-1 DNASE1 9823 Yes SL-0178 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}. UNIPROT P11936 UNIPROT Q95KK2 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0005634 GO:0003779 GO:0004536 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQDDPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPSDAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAGPLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA 284 P12348 Period circadian protein per 46245 Yes SL-0198 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}. UNIPROT P12348 UNIPROT Q29I05 Pfam PF00989 PROSITE PS50112 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}. GO:0005634 GO:0048471 GO:0006355 GO:0048511 MEGESTESTQNTKVSDSAYSNSCSNSQSQRSGSSKSMLSGSHSSGSSGYGGKPSIQTSSSDMAIKRNKEKSRKKKKAKCTQAQATISSSLEGAEEQPHSSGTTCDQKILHVLATTQQLGDQPSSLDHKLGEQLEARHNCGVGKAEQPQSFSLPCPLSVSTLMPGIGVCHGGNAPGGKWEKTFESCKLDTGPAKTERVKEDSFCCVISMHDGIVLYTTPSITDVLGFPRDMWLGRSFIDFVHTKDRATFASQITTGIPIAESRCSMPKDARSTFCVMLRQYRGLQTSGYGVIGRSVNYEPFRLGMSFREAPEEERSDNYMVANSSNMLLVICATPIKSSYRVPEEIHSQRSPKFAIRHTAAGIISHVDSAAVSALGYLPQDLMGRSIMDLYHHDDLPVIKEIYESVMKKGQTAGASFCSKPYRFLIQNGCYILLETEWSSFVNPWSRKLEFVVGHHRVFQGPKICNVFETPPNSEPKIAEELQNKNTRIKEEIVNLLAEKVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPHHDYYDSKSSIETPPSYNQLNYNENLLRFFNSKPVTAPVEVDPPKVGSSDVSSTREDARSTLSPLNGFEGSGASGSSGHLTSGSNIHMSSATNTSNAGTGTGTVTGTGTIIATSGTGTVTCASGNMDANTSAAFNIAANTSAADNFGADTSAADTSGADTSAADNYAVDNYGPGNFGAENSCADNSGAENSCADNSGVDNSRPGNSGADNSAADNFGADNSGPDNSGADNSGPDNTGPDNSGAENSRAENSRADNSRPDHPRPDISGASNSRPDKTGPDKSGAENSASGSGSGTSGNEGPSSGGQDTRTTAGTPDSPPVSLTESLLNKHNDEMEKFMLKKHRESRGDRRTVEKNKNKTTNTIDSLKILEYSSTGPGHGTKRGGSYSWEGEGNKPKQQPTLNSVGVGTGAPEAPIPPVHPTHTTHTAIAQSSFSAQQSLFPTFYYIPATPLAASTPAPGALSPTPRNQKHHHHAHQHAPKVPDQASTSQQAAGPAAIPLQYVTGVMYPHPSLFYTHPAAAAATAMMYQPMPFPGIANAMQLPEQPSTSQSNYSKTVFSVIVAPPTITTTTATTTPKTQGAFHSITPAQLQRPSSQDTSVKTEPASNATPSHSSNKKKANSSIASGIGDYNSNQACSRNRANVKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDNDKEAKHRKLKNITRLSSKIMEHPEEDQTQHGDG 1271 P12349 Period circadian protein per 7244 No SL-0198 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}. UNIPROT P12349 Pfam PF00989 PROSITE PS50112 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}. GO:0005634 GO:0048471 GO:0006355 GO:0048511 MEGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMAVKRNKDKSRKKKKAKSPAQATAATTTTIKSLEQTEEPLLVKPNNGSCEQQLELQDAQQLGAPTPSDAHDAHGDKPQLDVDEQQDDPQAEQIQQLETATAATISPDTMSASVTVTIDGCTSMEKTCEWTDRPGRLEAHAACIGKQHVQQQQHDRVKEDSFCCVISMHDGVVLFTTANLNEMLGYPREMWLGRSFIDFVHIKDRATFASQITTGIPIAESRCSQSKDARTTFCVMLRRYRGLASGGFGIIGRPVSYAPFRLGLTFREAPEEVQPDGCTLSNATSMLLVISATPIKSCYKEPDEFLSPKGPKFAIQHTAAGIISHVDTAAVSALGYLPQDLIGRSILDFYHHEDLSDIKDIYEKVVKKGQTVGATFCSKPFRFLIQNGCYILLETEWTSFVNPWSRKLEFVVGHHRVFQGPKQCDVFEMSPNVTPNIPEDEQNRNACIKEDILKMMTETVTRPSDTVKQEVSRRCQALASFMETLMDEVARGDLKLDLPHETELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVDTDPPKMDSSYVSSAREDALSPVHGFEGSGGSGSSGNLTTASNVRMSSVTNTSNTGTGTSGGENSASGSSNPLPVNMTLTEILLNKHNDEMEKCMLKKHRESRGRTGDKTKKSVIEKMPEYSGPGHGQTMKRGGSHSWEGDANKPKQQLTLSAVVVAPTVSVSPAEDSQTTAKWQAPMTGSHLFQSSYNFPQSINLWPPFSLGLTTPTVHTTHTSMAQKSFSPQHNLFPAFYYIPAPLATATAGSAAAQTSVSSASAAQHSPKSSENPSTSQPEATAATAMPMPYMAGVMYPHPSLFYAYQPMPFPSVSGAVQMSVQSSGSQSNNNNKSIYTMAPASTTTQKPGAFHSITPAELNKPDAPDTLLHTETSPKISVQEAPKKELSDLPSTSARRGSSSDQRNNSNNPKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDNEKETKVHKLKPIVEHPEEDQTQHGDG 1087 P12478 C-terminal core protein nef 11683 No SL-0382 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}. UNIPROT P12478 PDB 5EO0 PDB 5EO1 Pfam PF00469 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}. GO:0005576 GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0005525 GO:0017124 GO:0030683 GO:0009405 MGGRWSKSSIVGWPAIRERIRRTDPAADGVGAVSRDLEKHGAITSSNTRGTNADCAWLEAQEESEEVGFPVRPQVPLRPMTYKGALDLSHFLKEKGG 97 P12683 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 HMG1 559292 Yes SL-0178 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope. UNIPROT P12683 UNIPROT D6W0K8 Pfam PF00368 Pfam PF13323 Pfam PF12349 PROSITE PS00066 PROSITE PS00318 PROSITE PS01192 PROSITE PS50065 PROSITE PS50156 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}. Self EBI-8377,EBI-8377 P12684 EBI-8377,EBI-8384 Q12329 EBI-8571,EBI-8377 Q08421 EBI-8377,EBI-762498 P38708 EBI-8377,EBI-24471 Q12447 EBI-8377,EBI-33397 P38219 EBI-8377,EBI-21409 P16140 EBI-8377,EBI-20254 P02557 EBI-8377,EBI-18986 P09733 EBI-8377,EBI-18976 P02994 EBI-8377,EBI-6314 P10592 EBI-8377,EBI-8603 P10659 EBI-8377,EBI-10789 P33299 EBI-8377,EBI-13910 P38764 EBI-8377,EBI-15913 P41940 EBI-8377,EBI-11191 P23641 EBI-8377,EBI-11178 P40069 EBI-8377,EBI-9166 P39993 EBI-8377,EBI-7547 P43535 EBI-8377,EBI-7423 P47912 EBI-8377,EBI-10095 P30822 EBI-8377,EBI-20589 P00330 EBI-8377,EBI-2218 P11484 EBI-8377,EBI-8627 P16370 EBI-8377,EBI-15773 P25454 EBI-8377,EBI-14709 P46985 EBI-8377,EBI-11052 P39925 EBI-2317,EBI-8377 GO:0005789 GO:0016021 GO:0005635 GO:0034399 GO:0005778 GO:0050662 GO:0004420 GO:0042282 GO:0015936 GO:0006696 GO:0019287 GO:0008299 GO:0016126 MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQCILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCSMYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLNLSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRIEDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTVISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLGDTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKSDVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATDINRLKDGSVTCIKS 1054 P12827 Protein E26 DA26 46015 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P12827 Pfam PF11050 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}. GO:0030430 GO:0044201 GO:0016020 GO:0019012 MESVQTRLCASSNQFAPFKKRQLAVPVGSVNSLTHTITSTTVTSVIPKNYQEKRQKICHIISSLRNTHLNFNKIQSVHKKKLRHLQNLLRKKNEIIAELVRKLESAQKKTTHRNISKPAHWKYFGVVRCDNTIRTIIGNEKFVRRRLAELCTLYNAEYVFCQARADGDKDRQALASLLTAAFGSRVIVYENSRRFEFINPDEIASGKRLIIKHLQDESQSDINAY 225 P13285 Latent membrane protein 2 LMP2 10377 Yes SL-0382 [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}. UNIPROT P13285 UNIPROT Q777H4 UNIPROT Q8AZK9 PDB 1UXS PDB 1UXW PDB 2JO9 PDB 3BVN PDB 3REW PDB 5GRD PDB 5GSD Pfam PF07415 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. GO:0033645 GO:0044220 GO:0020002 GO:0016021 GO:0039649 GO:0019042 MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLNLTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVAGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYCLTLESEERPPTPYRNTV 497 P14142 Solute carrier family 2, facilitated glucose transporter member 4 Slc2a4 10090 Yes SL-0198 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}. UNIPROT P14142 UNIPROT Q3TPK6 UNIPROT Q9JJN9 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 PROSITE PS00217 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}.Note=Defects in Slc2a4 may be the cause of certain post- receptor defects in non-insulin-dependent diabetes mellitus (NIDDM). GO:0009986 GO:0005905 GO:0030136 GO:0005737 GO:0030659 GO:0005829 GO:0012505 GO:0005768 GO:0009897 GO:0070062 GO:0032593 GO:0016021 GO:0005887 GO:0043231 GO:0016020 GO:0045121 GO:0005771 GO:0048471 GO:0005886 GO:0098793 GO:0042383 GO:0016529 GO:0030315 GO:0030140 GO:0012506 GO:0055056 GO:0005355 GO:0005360 GO:0010021 GO:0050873 GO:0071456 GO:0032869 GO:0071470 GO:0071356 GO:0042593 GO:0046323 GO:0044381 GO:1904659 GO:0098694 GO:0045471 MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQISAAFRRTPSLLEQEVKPSTELEYLGPDEND 509 P14733 Lamin-B1 Lmnb1 10090 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. UNIPROT P14733 UNIPROT Q61791 Pfam PF00038 Pfam PF00932 PROSITE PS00226 PROSITE PS51842 PROSITE PS51841 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. Q7TPH6 EBI-1811542,EBI-445247 Q80YT7 EBI-16726361,EBI-445247 P83510 EBI-7280013,EBI-445247 Q9Z0E3 EBI-80858,EBI-445247 Q01815 EBI-644904,EBI-445247 A2AKD7 EBI-20565907,EBI-445247 Q9D2G2 EBI-773210,EBI-445247 Q8K2B3 EBI-1219461,EBI-445247 Q60932 EBI-299577,EBI-445247 P08228 EBI-1635090,EBI-445247 Q01097 EBI-400125,EBI-445247 A3KGF7 EBI-681172,EBI-445247 GO:0005737 GO:0005638 GO:0005635 GO:0005637 GO:0005652 GO:0016363 GO:0031965 GO:0005654 GO:0005634 GO:0003690 GO:0008432 GO:0043274 GO:1990837 GO:1904609 GO:0010971 GO:0046330 MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSCAIM 588 P14906 Protein translocation protein SEC63 SEC63 559292 Yes SL-0178 SL-0179 SL-0182 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein. UNIPROT P14906 UNIPROT D6W2V5 UNIPROT Q08690 PDB 6N3Q PDB 6ND1 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. P32915 EBI-16400,EBI-16636 P33754 EBI-16636,EBI-16647 P39742 EBI-16636,EBI-16651 P21825 EBI-16632,EBI-16636 P37898 EBI-1998,EBI-16636 Q12168 EBI-32973,EBI-16636 P60010 EBI-2169,EBI-16636 P22108 EBI-2635,EBI-16636 P08566 EBI-2883,EBI-16636 Q06834 EBI-16636,EBI-33224 Q08347 EBI-16636,EBI-3763789 Q07457 EBI-16636,EBI-31563 P00549 EBI-16636,EBI-9890 Q12018 EBI-16636,EBI-4321 Q06697 EBI-16636,EBI-29913 P53197 EBI-23684,EBI-16636 P40094 EBI-16605,EBI-16636 Q01454 EBI-16636,EBI-5209 P38865 EBI-16636,EBI-5268 P31373 EBI-5473,EBI-16636 P32582 EBI-4167,EBI-16636 Q08496 EBI-16636,EBI-31943 P53759 EBI-16636,EBI-27885 Q06053 EBI-16636,EBI-27095 P38737 EBI-24359,EBI-16636 P36053 EBI-16636,EBI-26919 P00924 EBI-16636,EBI-6468 P00925 EBI-16636,EBI-6475 P45976 EBI-6940,EBI-16636 P15442 EBI-16636,EBI-330 Q12680 EBI-7727,EBI-16636 P32347 EBI-16636,EBI-5711 P28241 EBI-16636,EBI-8883 P53982 EBI-16636,EBI-8892 P47170 EBI-16636,EBI-25710 P32361 EBI-9364,EBI-16636 P48526 EBI-18725,EBI-16636 P38144 EBI-16636,EBI-21087 Q12494 EBI-16636,EBI-37528 P38853 EBI-16636,EBI-9619 Q02574 EBI-16636,EBI-10658 P00958 EBI-18762,EBI-16636 Q07980 EBI-33369,EBI-16636 Q02455 EBI-11009,EBI-16636 P40457 EBI-16636,EBI-25261 P48563 EBI-28333,EBI-16636 P30775 EBI-14964,EBI-16636 P53166 EBI-16636,EBI-23808 Q02950 EBI-16636,EBI-37241 P47047 EBI-16636,EBI-11592 P19524 EBI-16636,EBI-11659 P33420 EBI-16636,EBI-12049 Q01560 EBI-12114,EBI-16636 P38271 EBI-16636,EBI-12563 Q12451 EBI-16636,EBI-12621 P40960 EBI-16636,EBI-30551 P17558 EBI-16341,EBI-16636 P40433 EBI-16636,EBI-1956 P00560 EBI-16636,EBI-13275 P36093 EBI-16636,EBI-13366 P07271 EBI-16636,EBI-13404 P33334 EBI-465,EBI-16636 P52489 EBI-16636,EBI-9895 P38344 EBI-21136,EBI-16636 P29539 EBI-2083307,EBI-16636 P53552 EBI-16636,EBI-15475 P05748 EBI-14480,EBI-16636 P54780 EBI-14485,EBI-16636 P05749 EBI-16636,EBI-14552 Q12149 EBI-16636,EBI-1782 Q02206 EBI-16636,EBI-16204 P40482 EBI-16592,EBI-16636 P11075 EBI-16636,EBI-16882 P34223 EBI-16636,EBI-17093 Q06315 EBI-16636,EBI-34508 P39928 EBI-17357,EBI-16636 P32908 EBI-16636,EBI-17402 P25357 EBI-16636,EBI-17596 P36126 EBI-17726,EBI-16636 P25567 EBI-16636,EBI-18084 P36085 EBI-18340,EBI-16636 P08153 EBI-16636,EBI-18633 Q06510 EBI-2094606,EBI-16636 P00359 EBI-16636,EBI-7218 P02994 EBI-6314,EBI-16636 P32367 EBI-19150,EBI-16636 P40217 EBI-16636,EBI-8951 P35169 EBI-19374,EBI-16636 P40061 EBI-22621,EBI-16636 P53874 EBI-19873,EBI-16636 P07259 EBI-14372,EBI-16636 P34241 EBI-26595,EBI-16636 Q12339 EBI-16636,EBI-30231 Q06685 EBI-16636,EBI-35034 P22203 EBI-16636,EBI-20268 O13584 EBI-32314,EBI-16636 P33301 EBI-16636,EBI-20599 P19880 EBI-16636,EBI-31265 O13527 EBI-16636,EBI-33845 P87264 EBI-16636,EBI-3770432 P39991 EBI-3665883,EBI-16636 P38854 EBI-24799,EBI-16636 P34246 EBI-16636,EBI-26803 Q05948 EBI-16636,EBI-36984 Q06567 EBI-16636,EBI-27160 Q03153 EBI-28199,EBI-16636 Q12751 EBI-16636,EBI-27406 P42842 EBI-16636,EBI-28374 Q12697 EBI-16636,EBI-3770507 Q08748 EBI-16636,EBI-2050125 Q06813 EBI-16636,EBI-38252 P36019 EBI-16636,EBI-29415 P31111 EBI-29645,EBI-16636 P11484 EBI-8627,EBI-16636 P39079 EBI-19077,EBI-16636 P32589 EBI-16636,EBI-8648 P32447 EBI-3003,EBI-16636 P30822 EBI-16636,EBI-20589 P14922 EBI-16636,EBI-18215 P39704 EBI-6587,EBI-16636 P21268 EBI-16636,EBI-6780 P00927 EBI-16636,EBI-19200 P50946 EBI-28814,EBI-16636 Q12524 EBI-16636,EBI-27150 P54885 EBI-16636,EBI-13872 P06103 EBI-8973,EBI-16636 P40016 EBI-16636,EBI-15927 Q12250 EBI-15935,EBI-16636 Q05543 EBI-35018,EBI-16636 O94742 EBI-16636,EBI-31337 P31376 EBI-16636,EBI-20613 P38326 EBI-21031,EBI-16636 P38123 EBI-20881,EBI-16636 Q05471 EBI-22102,EBI-16636 Q04067 EBI-8958,EBI-16636 Q05946 EBI-34702,EBI-16636 P34110 EBI-16636,EBI-20415 P16521 EBI-6338,EBI-16636 P53719 EBI-28456,EBI-16636 P53740 EBI-28524,EBI-16636 P10591 EBI-16636,EBI-8591 P38788 EBI-24570,EBI-16636 P16140 EBI-16636,EBI-20254 P10592 EBI-16636,EBI-8603 P32629 EBI-2595,EBI-16636 Q02159 EBI-16636,EBI-19749 P47026 EBI-25989,EBI-16636 GO:0005783 GO:0016021 GO:0005739 GO:0005637 GO:0031207 GO:0008320 GO:0003723 GO:0046967 GO:0006620 GO:0031204 GO:0006614 MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDKNSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKGLTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVSRWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNNAKFRIVAKCHSLLHGLLDIACGFRNLDIALGAINTFKCIVQAVPLTPNCQILQLPNVDKEHFITKTGDIHTLGKLFTLEDAKIGEVLGIKDQAKLNETLRVASHIPNLKIIKADFLVPGENQVTPSSTPYISLKVLVRSAKQPLIPTSLIPEENLTEPQDFESQRDPFAMMSKQPLVPYSFAPFFPTKRRGSWCCLVSSQKDGKILQTPIIIEKLSYKNLNDDKDFFDKRIKMDLTKHEKFDINDWEIGTIKIPLGQPAPETVGDFFFRVIVKSTDYFTTDLDITMNMKVRDSPAVEQVEVYSEEDDEYSTDDDETESDDESDASDYTDIDTDTEAEDDESPE 663 P14907 Nucleoporin NSP1 NSP1 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P14907 UNIPROT D6VWE3 PDB 1O6O Pfam PF05064 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}. Q06142 EBI-9145,EBI-12265 P40368 EBI-12331,EBI-12265 P22696 EBI-6679,EBI-12265 Q02796 EBI-30514,EBI-12265 P15992 EBI-12265,EBI-8555 P11484 EBI-12265,EBI-8627 P10592 EBI-12265,EBI-8603 P40005 EBI-2342435,EBI-12265 P48363 EBI-12265,EBI-13239 P52553 EBI-12265,EBI-13260 P53900 EBI-13246,EBI-12265 P33416 EBI-12265,EBI-8680 P48353 EBI-8369,EBI-12265 P10591 EBI-12265,EBI-8591 P26448 EBI-3824,EBI-12265 P38915 EBI-17964,EBI-12265 P50875 EBI-17751,EBI-12265 Q02199 EBI-12315,EBI-12265 P39723 EBI-20675,EBI-12265 Q04477 EBI-27228,EBI-12265 Q14974 EBI-12265,EBI-286758 Q03330 EBI-7458,EBI-12265 Q02336 EBI-2186,EBI-12265 P50102 EBI-19863,EBI-12265 P48837 EBI-12265,EBI-12324 Q05166 EBI-12265,EBI-3035 Q8IYF3-3 EBI-12265,EBI-11523345 P40066 EBI-22648,EBI-12265 P34077 EBI-12056,EBI-12265 Q02630 EBI-11703,EBI-12265 P51998 EBI-12265,EBI-450 P40477 EBI-12265,EBI-11747 P22353 EBI-12265,EBI-407 Q06678 EBI-12265,EBI-392 P36516 EBI-12265,EBI-387 P36525 EBI-12265,EBI-15545 P36523 EBI-12265,EBI-15518 Q04599 EBI-12265,EBI-38719 P02829 EBI-12265,EBI-8659 P38305 EBI-20939,EBI-12265 Q12315 EBI-7635,EBI-12265 GO:0031965 GO:0034399 GO:0005643 GO:0044613 GO:0044615 GO:0005543 GO:0017056 GO:0007049 GO:0097064 GO:0006607 GO:0016973 GO:0006606 GO:0000055 GO:0000056 GO:0006405 GO:0006409 MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPTSNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGNANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFGSGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKPDENKASATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKSDEKKDSDSSKPAFSFGTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSFGSKPTGKEEGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSTADVKSSDSLKLNSKPVELKPVSLDNKTLDDLVTKWTNQLTESASHFEQYTKKINSWDQVLVKGGEQISQLYSDAVMAEHSQNKIDQSLQYIERQQDELENFLDNFETKTEALLSDVVSTSSGAAANNNDQKRQQAYKTAQTLDENLNSLSSNLSSLIVEINNVSNTFNKTTNIDINNEDENIQLIKILNSHFDALRSLDDNSTSLEKQINSIKK 823 P14998 Agnoprotein AGNO 10631 Yes SL-0415 SL-0418 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}. UNIPROT P14998 Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 MFCEPKNLVVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS 74 P15389 Sodium channel protein type 5 subunit alpha Scn5a 10116 Yes SL-0198 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}. UNIPROT P15389 UNIPROT Q925G6 PDB 6UZ0 PDB 6UZ3 Pfam PF00520 Pfam PF06512 Pfam PF11933 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}. GO:0005901 GO:0009986 GO:0005783 GO:0016021 GO:0014704 GO:0016328 GO:0048471 GO:0005886 GO:0042383 GO:0034706 GO:0030315 GO:0001518 GO:0030018 GO:0030506 GO:0005516 GO:0005261 GO:0019899 GO:0017134 GO:0044325 GO:0050998 GO:0019904 GO:0019901 GO:0097110 GO:0031625 GO:0005244 GO:0005248 GO:0086060 GO:0086061 GO:0086006 GO:0086062 GO:0086063 GO:0086014 GO:0086016 GO:0086067 GO:0003360 GO:0086043 GO:0055074 GO:0086002 GO:0060048 GO:0003231 GO:0071277 GO:0021549 GO:0051899 GO:0086010 GO:0098912 GO:0086045 GO:0086048 GO:0086012 GO:0086047 GO:0086046 GO:0019228 GO:0042475 GO:0045760 GO:0050679 GO:0010460 GO:0010765 GO:0060371 GO:0060372 GO:0086004 GO:0002027 GO:0086091 GO:1902305 GO:0060373 GO:0060307 GO:0014894 GO:0014070 GO:0086015 GO:0035725 GO:0006814 GO:0021537 GO:0086005 MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGLVWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERKSKRRKRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRTSLLVPWPLRHPSAQGQPGPGASAPGYVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSYLLRPMVLDRPPDTTTPSEEPGGPQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVKRTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRPGQGTPGDSEPVCVPIAVAESDTEDQEEDEENSLGTEEESSKQESQVVSGGHEPYQEPRAWSQVSETTSSEAGASTSQADWQQEQKTEPQAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQSPGKVWWRLRKTCYRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQRSVKHASFLFRQQAGGSGLSDEDAPEREGLIAYMMNGNFSRRSAPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSRSEDLADFPPSPDRDRESIV 2019 P15565 tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial TRM1 559292 Yes SL-0178 SL-0179 SL-0182 [Isoform 1]: Mitochondrion. [Isoform 2]: Mitochondrion. Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Predominantly targeted to the nucleus. UNIPROT P15565 UNIPROT D6VSA6 UNIPROT Q9URQ7 UNIPROT Q9URQ8 Pfam PF02005 PROSITE PS51626 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. P10591 EBI-19543,EBI-8591 P33416 EBI-8680,EBI-19543 P11484 EBI-8627,EBI-19543 P38788 EBI-24570,EBI-19543 P32589 EBI-19543,EBI-8648 P39101 EBI-19543,EBI-3949 P32527 EBI-29684,EBI-19543 P35177 EBI-17958,EBI-19543 P38915 EBI-17964,EBI-19543 P50875 EBI-17751,EBI-19543 Q12060 EBI-8287,EBI-19543 Q02336 EBI-2186,EBI-19543 P50102 EBI-19863,EBI-19543 Q05027 EBI-27500,EBI-19543 Q03330 EBI-7458,EBI-19543 GO:0005739 GO:0005635 GO:0005637 GO:0005634 GO:0004809 GO:0000049 GO:0030488 GO:0002940 MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAWDNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREVIANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCTDLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNVMSSTMTTYHCSRCGSYHNQPLGRISQREGRNNKTFTKYSVAQGPPVDTKCKFCEGTYHLAGPMYAGPLHNKEFIEEVLRINKEEHRDQDDTYGTRKRIEGMLSLAKNELSDSPFYFSPNHIASVIKLQVPPLKKVVAGLGSLGFECSLTHAQPSSLKTNAPWDAIWYVMQKCDDEKKDLSKMNPNTTGYKILSAMPGWLSGTVKSEYDSKLSFAPNEQSGNIEKLRKLKIVRYQENPTKNWGPKARPNTS 570 P16258 Oxysterol-binding protein 1 OSBP 9986 Yes SL-0198 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}. UNIPROT P16258 Pfam PF01237 Pfam PF00169 PROSITE PS01013 PROSITE PS50003 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}. GO:0005829 GO:0005789 GO:0000139 GO:0048471 GO:0005802 GO:0015485 GO:0070273 GO:0120015 GO:0032367 GO:0015918 MAATELRGVVGPGPAAIAAPGGGGAGPPVVGGGGGGRGDAGPGSGAASGTVAAAAAGGQGPGAGGVAAAAGPAPTPPAGGSGSSGTGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLVLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAFRGATVLPAHTSGSAGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFALLGTWDEKMDCFKVQPVSGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWEGGTAPTDSRLRPDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDWNSCPDIF 809 P16278 Beta-galactosidase GLB1 9606 Yes SL-0198 [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}. UNIPROT P16278 UNIPROT B2R7H8 UNIPROT B7Z6B0 UNIPROT P16279 PDB 3THC PDB 3THD PDB 3WEZ PDB 3WF0 PDB 3WF1 PDB 3WF2 PDB 3WF3 PDB 3WF4 Pfam PF13364 Pfam PF01301 PROSITE PS01182 OMIM 230500 OMIM 230600 OMIM 230650 OMIM 253010 OMIM 611458 DisGeNET 2720 [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}.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. P02866 EBI-2905940,EBI-989638 P16104 EBI-494830,EBI-989638 P01100 EBI-852851,EBI-989638 P62699 EBI-11721624,EBI-989638 P08670 EBI-353844,EBI-989638 Q9NQH7 EBI-989638,EBI-1171467 P10619 EBI-989638,EBI-989654 Q8NBJ4 EBI-712073,EBI-989638 P04985 EBI-989582,EBI-989638 Q99519 EBI-721517,EBI-989638 Q9NSA3 EBI-989638,EBI-747082 P30825 EBI-4289564,EBI-989638 Q3KNW5 EBI-18159983,EBI-989638 Q9BRI3 EBI-8644112,EBI-989638 Q8IWL3 EBI-1805738,EBI-989638 GO:0035578 GO:0005737 GO:0070062 GO:0005576 GO:1904813 GO:0005794 GO:0043231 GO:0043202 GO:0048471 GO:0005773 GO:0004565 GO:0016936 GO:0042803 GO:0044262 GO:0019388 GO:0006027 GO:0006687 GO:0042340 GO:0043312 GO:0051413 GO:1904016 MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV 677 P16733 Envelope glycoprotein M gM 10360 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P16733 UNIPROT Q7M6T7 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCYAVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVHFFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAVFVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVRYFRGRGSGSVKYQALATASGEEVAVLSHHDSLESRRLREEEDDDDDEDFEDA 372 P17698 Clusterin alpha chain CLU 9940 Yes SL-0198 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}. UNIPROT P17698 Pfam PF01093 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005576 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0051082 GO:0002434 GO:1905907 GO:0043065 GO:0048260 GO:0050821 GO:0042127 ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY 66 P17763 RNA-directed RNA polymerase NS5 POLG 11059 Yes SL-0382 [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}. UNIPROT P17763 UNIPROT P27910 UNIPROT P89313 UNIPROT P89314 PDB 3J8D PDB 3L6P PDB 3LKW PDB 4AL8 PDB 4GSX PDB 4GT0 PDB 4LCY PDB 4OIG PDB 5VIC PDB 5WJL PDB 5WKF Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0039714 GO:0005576 GO:0044167 GO:0033650 GO:0042025 GO:0044220 GO:0016021 GO:0044385 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0005216 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0075512 GO:0039654 GO:0039520 GO:0039707 GO:0051259 GO:0039545 GO:0039564 GO:0039574 GO:0039502 GO:0046762 GO:0039694 GO:0019062 MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKVLRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTTATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLTMEKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVTDKEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEVHTWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVSGILAQGKKMIRPQPMEHKYSWKSWGKAKIIGADVQNTTFIIDGPNTPECPDNQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQVCDHRLMSAAIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCIWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTAGPWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKTIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENLVKSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLTMGQLTWNDLIRLCIMVGANASDKMGMGTTYLALMATFRMRPMFAVGLLFRRLTSREVLLLTVGLSLVASVELPNSLEELGDGLAMGIMMLKLLTDFQSHQLWATLLSLTFVKTTFSLHYAWKTMAMILSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLITENKIWGRKSWPLNEGIMAVGIVSILLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTLTILLKATLLAISGVYPMSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRILQRGLLGRSQVGVGVFQEGVFHTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNAGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGAIALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYLPAIVREAIRRNVRTLVLAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYDWITDFPGKTVWFVPSIKSGNDIANCLRKNGKRVVQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILAGPMPVTVASAAQRRGRIGRNQNKEGDQYIYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLRGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEIWTKEGERKKLRPRWLDARTYSDPLALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGKAYRHAMEELPDTIETLMLLALIAVLTGGVTLFFLSGRGLGKTSIGLLCVIASSALLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMILTAAANEMGLLETTKKDLGIGHAAAENHHHAAMLDVDLHPASAWTLYAVATTIITPMMRHTIENTTANISLTAIANQAAILMGLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVFMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDLDPVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSLMKSLGGGRRGTGAQGETLGEKWKRQLNQLSKSEFNTYKRSGIIEVDRSEAKEGLKRGEPTKHAVSRGTAKLRWFVERNLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDIGESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNIVSAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKNGHKSTWHYDEDNPYKTWAYHGSYEVKPSGSASSMVNGVVRLLTKPWDVIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRNKKPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQNEAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGIFSPSELETPNLAERVLDWLKKHGTERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPFCSHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWVPTSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDRWCGSLIGLTARATWATNIQVAINQVRRLIGNENYLDFMTSMKRFKNESDPEGALW 3392 P18410 Sporulation-specific protein SPO7 SPO7 559292 Yes SL-0178 SL-0182 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}. UNIPROT P18410 UNIPROT D6VPK9 Pfam PF03907 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}. P38757 EBI-17857,EBI-24435 P10664 EBI-17857,EBI-15390 P16140 EBI-17857,EBI-20254 P32591 EBI-17857,EBI-18622 P32589 EBI-17857,EBI-8648 P11484 EBI-17857,EBI-8627 P10592 EBI-17857,EBI-8603 P02407 EBI-17857,EBI-14526 P05737 EBI-17857,EBI-15422 P05739 EBI-17857,EBI-15409 P49626 EBI-17857,EBI-15394 P04147 EBI-17857,EBI-12823 P12945 EBI-17857,EBI-11868 P32501 EBI-17857,EBI-6270 P38631 EBI-17857,EBI-7708 GO:0005783 GO:0005789 GO:0016021 GO:0071595 GO:0031965 GO:0019888 GO:0006629 GO:0071072 GO:0006998 GO:1903740 GO:0006470 GO:0071071 GO:0061709 GO:0030435 MEPESIGDVGNHAQDDSASIVSGPRRRSTSKTSSAKNIRNSSNISPASMIFRNLLILEDDLRRQAHEQKILKWQFTLFLASMAGVGAFTFYELYFTSDYVKGLHRVILQFTLSFISITVVLFHISGQYRRTIVIPRRFFTSTNKGIRQFNVKLVKVQSTWDEKYTDSVRFVSRTIAYCNIYCLKKFLWLKDDNAIVKFWKSVTIQSQPRIGAVDVKLVLNPRAFSAEIREGWEIYRDEFWAREGARRRKQAHELRPKSE 259 P18541 RING finger protein Z Z 11624 Yes SL-0382 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}. UNIPROT P18541 UNIPROT Q49K85 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGQGKSREEKGTNSTNRAEILPDTTYLGPLSCKSCWQKFDSLVRCHDHYLCRHCLNLLLSVSDRCPLCKYPLPTRLKISTAPSSPPPYEE 90 P19525 Interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2 9606 Yes SL-0198 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. UNIPROT P19525 UNIPROT A8K3P0 UNIPROT D6W584 UNIPROT E9PC80 UNIPROT Q52M43 UNIPROT Q7Z6F6 UNIPROT Q9UIR4 PDB 1QU6 PDB 2A19 PDB 2A1A PDB 3UIU PDB 6D3K PDB 6D3L Pfam PF00035 Pfam PF00069 PROSITE PS50137 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 176871 DisGeNET 5610 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}. O75569 EBI-640775,EBI-713955 Q5S007 EBI-5323863,EBI-640775 Q7KZN9 EBI-3248549,EBI-640775 P09622 EBI-353366,EBI-640775 P36957 EBI-351007,EBI-640775 P03372 EBI-78473,EBI-640775 Q16543 EBI-295634,EBI-640775 P60520 EBI-720116,EBI-640775 P35570 EBI-640775,EBI-520230 Q96FF9 EBI-718805,EBI-640775 P27635 EBI-352398,EBI-640775 Q6PFD6 EBI-11093565,EBI-640775 Q6PJG2 EBI-2795569,EBI-640775 Q14108 EBI-1564650,EBI-640775 Q99PL5 EBI-8361659,EBI-640775 Q9H444 EBI-749627,EBI-640775 Q14684 EBI-372051,EBI-640775 P04798 EBI-10194262,EBI-640775 P78563-4 EBI-12002366,EBI-640775 Q96C10 EBI-744193,EBI-640775 Q8IY81 EBI-640775,EBI-744088 P05455 EBI-640775,EBI-358037 P46087 EBI-640775,EBI-356811 Q9HCE1 EBI-640775,EBI-1055820 O00458 EBI-640775,EBI-726897 Q99848 EBI-640775,EBI-1048111 P07910 EBI-640775,EBI-357966 P56537 EBI-640775,EBI-372243 Q13310 EBI-640775,EBI-372844 Q9NUL3 EBI-640775,EBI-722938 Q9NZM5 EBI-640775,EBI-720156 Q9BZE4 EBI-640775,EBI-1056249 Q9H0E2 EBI-640775,EBI-74615 Q7L2E3 EBI-640775,EBI-1211456 Q9H0D6 EBI-640775,EBI-372110 P20248 EBI-640775,EBI-457097 Q9NSD9 EBI-640775,EBI-353803 O95793 EBI-640775,EBI-358174 O60812 EBI-640775,EBI-1046507 Q8WTT2 EBI-640775,EBI-2512539 Q9UPY3 EBI-640775,EBI-395506 Q9NX58 EBI-640775,EBI-713507 Q8N5Z5 EBI-640775,EBI-743960 Q96CT7 EBI-640775,EBI-5461329 Q00577 EBI-640775,EBI-1045860 P36873 EBI-640775,EBI-356283 Q15633 EBI-640775,EBI-978581 Q6P2E9 EBI-640775,EBI-1006038 Q9Y285 EBI-640775,EBI-725361 Q9UL40 EBI-640775,EBI-2462313 P16403 EBI-640775,EBI-358372 Q00526 EBI-640775,EBI-1245761 P11387 EBI-640775,EBI-876302 Q9BVP2 EBI-640775,EBI-641642 Q08211 EBI-640775,EBI-352022 P04591 EBI-640775,EBI-6179727 Q86VP6 EBI-456077,EBI-640775 Q13618 EBI-456129,EBI-640775 O00425 EBI-640775,EBI-1058566 Q9Y6M1 EBI-640775,EBI-1024419 P08238 EBI-352572,EBI-640775 P05198 EBI-640775,EBI-1056162 Q9UJU6 EBI-640775,EBI-751783 Q15628-2 EBI-640775,EBI-20868057 P51608 EBI-1189067,EBI-640775 Q96SL4 EBI-749411,EBI-640775 Q8N6M8-2 EBI-21771049,EBI-640775 Q27968 EBI-640793,EBI-640775 GO:0005737 GO:0005829 GO:0016020 GO:0005634 GO:0048471 GO:0005840 GO:0005524 GO:0003725 GO:0004694 GO:0042802 GO:0004715 GO:0004672 GO:0019888 GO:0004674 GO:0003723 GO:0000186 GO:0034198 GO:0051607 GO:0030968 GO:0045087 GO:0030683 GO:0043066 GO:0008285 GO:0033689 GO:0017148 GO:0045071 GO:0032722 GO:0001819 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0035455 GO:0009615 GO:0006412 MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC 551 P19811 Non-structural protein 12 rep 299386 Yes SL-0382 [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}. UNIPROT P19811 UNIPROT Q88625 UNIPROT Q8QZQ5 UNIPROT Q91DM2 PDB 1MBM PDB 2L8K PDB 4IUM PDB 4N0N PDB 4N0O PDB 5F17 PDB 5HBZ PDB 5HC1 Pfam PF16749 Pfam PF12581 Pfam PF14755 Pfam PF14754 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF17873 Pfam PF01443 Pfam PF17977 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 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}. GO:0033644 GO:0042025 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0070008 GO:0036459 GO:0008270 GO:0039648 GO:0039579 GO:0039502 GO:0006351 GO:0019082 GO:0039694 MATFSATGFGGSFVRDWSLDLPDACEHGAGLCCEVDGSTLCAECFRGCEGMEQCPGLFMGLLKLASPVPVGHKFLIGWYRAAKVTGRYNFLELLQHPAFAQLRVVDARLAIEEASVFISTDHASAKRFPGARFALTPVYANAWVVSPAANSLIVTTDQEQDGFCWLKLLPPDRREAGLRLYYNHYREQRTGWLSKTGLRLWLGDLGLGINASSGGLKFHIMRGSPQRAWHITTRSCKLKSYYVCDISEADWSCLPAGNYGGYNPPGDGACGYRCLAFMNGATVVSAGCSSDLWCDDELAYRVFQLSPTFTVTIPGGRVCPNAKYAMICDKQHWRVKRAKGVGLCLDESCFRGICNCQRMSGPPPAPVSAAVLDHILEAATFGNVRVVTPEGQPRPVPAPRVRPSANSSGDVKDPAPVPPVPKPRTKLATPNPTQAPIPAPRTRLQGASTQEPLASAGVASDSAPKWRVAKTVYSSAERFRTELVQRARSVGDVLVQALPLKTPAVQRYTMTLKMMRSRFSWHCDVWYPLAVIACLLPIWPSLALLLSFAIGLIPSVGNNVVLTALLVSSANYVASMDHQCEGAACLALLEEEHYYRAVRWRPITGALSLVLNLLGQVGYVARSTFDAAYVPCTVFDLCSFAILYLCRNRCWRCFGRCVRVGPATHVLGSTGQRVSKLALIDLCDHFSKPTIDVVGMATGWSGCYTGTAAMERQCASTVDPHSFDQKKAGATVYLTPPVNSGSALQCLNVMWKRPIGSTVLGEQTGAVVTAVKSISFSPPCCVSTTLPTRPGVTVVDHALYNRLTASGVDPALLRVGQGDFLKLNPGFRLIGGWIYGICYFVLVVVSTFTCLPIKCGIGTRDPFCRRVFSVPVTKTQEHCHAGMCASAEGISLDSLGLTQLQSYWIAAVTSGLVILLVCHRLAISALDLLTLASPLVLLVFPWASVGLLLACSLAGAAVKIQLLATLFVNLFFPQATLVTMGYWACVAALAVYSLMGLRVKVNVPMCVTPAHFLLLARSAGQSREQMLRVSAAAPTNSLLGVARDCYVTGTTRLYIPKEGGMVFEGLFRSPKARGNVGFVAGSSYGTGSVWTRNNEVVVLTASHVVGRANMATLKIGDAMLTLTFKKNGDFAEAVTTQSELPGNWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQGDAVVGVHTGSNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADVDAVPRSLAMLIDGLSNRESSLSGPQLLLIACFMWSYLNQPAYLPYVLGFFAANFFLPKSVGRPVVTGLLWLCCLFTPLSMRLCLFHLVCATVTGNVISLWFYITAAGTSYLSEMWFGGYPTMLFVPRFLVYQFPGWAIGTVLAVCSITMLAAALGHTLLLDVFSASGRFDRTFMMKYFLEGGVKESVTASVTRAYGKPITQESLTATLAALTDDDFQFLSDVLDCRAVRSAMNLRAALTSFQVAQYRNILNASLQVDRDAARSRRLMAKLADFAVEQEVTAGDRVVVIDGLDRMAHFKDDLVLVPLTTKVVGGSRCTICDVVKEEANDTPVKPMPSRRRRKGLPKGAQLEWDRHQEEKRNAGDDDFAVSNDYVKRVPKYWDPSDTRGTTVKIAGTTYQKVVDYSGNVHYVEHQEDLLDYVLGKGSYEGLDQDKVLDLTNMLKVDPTELSSKDKAKARQLAHLLLDLANPVEAVNQLNLRAPHIFPGDVGRRTFADSKDKGFVALHSRTMFLAARDFLFNIKFVCDEEFTKTPKDTLLGYVRACPGYWFIFRRTHRSLIDAYWDSMECVYALPTISDFDVSPGDVAVTGERWDFESPGGGRAKRLTADLVHAFQGFHGASYSYDDKVAAAVSGDPYRSDGVLYNTRWGNIPYSVPTNALEATACYRAGCEAVTDGTNVIATIGPFPEQQPIPDIPKSVLDNCADISCDAFIAPAAETALCGDLEKYNLSTQGFVLPSVFSMVRAYLKEEIGDAPPLYLPSTVPSKNSQAGINGAEFPTKSLQSYCLIDDMVSQSMKSNLQTATMATCKRQYCSKYKIRSILGTNNYIGLGLRACLSGVTAAFQKAGKDGSPIYLGKSKFDPIPAPDKYCLETDLESCDRSTPALVRWFATNLIFELAGQPELVHSYVLNCCHDLVVAGSVAFTKRGGLSSGDPITSISNTIYSLVLYTQHMLLCGLEGYFPEIAEKYLDGSLELRDMFKYVRVYIYSDDVVLTTPNQHYAASFDRWVPHLQALLGFKVDPKKTVNTSSPSFLGCRFKQVDGKCYLASLQDRVTRSLLYHIGAKNPSEYYEAAVSIFKDSIICCDEDWWTDLHRRISGAARTDGVEFPTIEMLTSFRTKQYESAVCTVCGAAPVAKSACGGWFCGNCVPYHAGHCHTTSLFANCGHDIMYRSTYCTMCEGSPKQMVPKVPHPILDHLLCHIDYGSKEELTLVVADGRTTSPPGRYKVGHKVVAVVADVGGNIVFGCGPGSHIAVPLQDTLKGVVVNKALKNAAASEYVEGPPGSGKTFHLVKDVLAVVGSATLVVPTHASMLDCINKLKQAGADPYFVVPKYTVLDFPRPGSGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILTQGRVKGYGDLNQLGCVGPASVPRNLWLRHFVSLEPLRVCHRFGAAVCDLIKGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYHKDRGLGHRTIDSIQGCTFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLLKFTKEAEAQDLIHGPPTACHLGQEIDLWSNEGLEYYKEVNLLYTHVPIKDGVIHSYPNCGPACGWEKQSNKISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDRYPNCLQITLQQVCELSKPCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKARALPDSLFSSGRFETNSRAFLDEAEEKFAAAHPHACLGEINKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAKAACSVVDVYAPSFEPYLHPETLSRVYKIMIDFKPCRLMVWRNATFYVQEGVDAVTSALAAVSKLIKVPANEPVSFHVASGYRTNALVAPQAKISIGAYAAEWALSTEPPPAGYAIVRRYIVKRLLSSTEVFLCRRGVVSSTSVQTICALEGCKPLFNFLQIGSVIGPV 3175 P20240 Otefin Ote 7227 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT P20240 UNIPROT Q9V8E5 Pfam PF03020 PROSITE PS50954 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}. P08928 EBI-115143,EBI-188444 Q24568 EBI-3406532,EBI-115143 P23572 EBI-108689,EBI-115143 Q94524 EBI-115143,EBI-158251 GO:0005694 GO:0005737 GO:0012505 GO:0005815 GO:0005641 GO:0005637 GO:0031965 GO:0034399 GO:0005654 GO:0000922 GO:0003714 GO:0008134 GO:0007049 GO:0051301 GO:0030718 GO:0060250 GO:0045892 GO:0031468 GO:0048477 GO:0030513 MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKVVEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQKYHIKSKLFIVLLVLLLIGVYYIFY 424 P20291 Arachidonate 5-lipoxygenase-activating protein Alox5ap 10116 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P20291 UNIPROT Q5RJL3 Pfam PF01124 PROSITE PS01297 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}. GO:0005829 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0005635 GO:0031965 GO:0005634 GO:0050544 GO:0008047 GO:0019899 GO:0004602 GO:0004364 GO:0042802 GO:0004464 GO:0047485 GO:0044877 GO:0071277 GO:0019370 GO:0002540 GO:0019372 GO:0002675 GO:0070207 MDQEAVGNVVLLAIVTLISVVQNAFFAHKVELESKAQSGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNHYLIFFFGSDFENYIRTITTTISPLLLIP 161 P20484 Protein MAK11 MAK11 559292 Yes SL-0178 SL-0182 Nucleus, nucleolus {ECO:0000269|PubMed:2826479}. Nucleus membrane {ECO:0000269|PubMed:2826479}; Peripheral membrane protein {ECO:0000269|PubMed:2826479}. Note=Membrane associated. UNIPROT P20484 UNIPROT D6VXR4 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. P10591 EBI-8591,EBI-10930 Q12329 EBI-8571,EBI-10930 Q06511 EBI-34602,EBI-10930 P0CX43 EBI-10930,EBI-7433060 Q07915 EBI-10930,EBI-35766 P36160 EBI-15881,EBI-10930 P53136 EBI-10930,EBI-23920 Q12024 EBI-10930,EBI-29589 P02994 EBI-10930,EBI-6314 Q05022 EBI-10930,EBI-16011 P49626 EBI-10930,EBI-15394 Q03532 EBI-10930,EBI-8170 P30822 EBI-20589,EBI-10930 P39014 EBI-10930,EBI-11507 GO:0016020 GO:0031965 GO:0005730 GO:0000466 GO:0000463 GO:0000027 GO:0042273 MSAIGDKNQFRIIVGSYEHNILCLSLDIPNQKENDAAKTPHFMPIFHFQAHSLSIKCLAVSRRYLVSGSNDEHIRIYDLQKRKELGTLLSHQGSITALQFSHPASSSEDAAVSKGSKNSKWLLSASEDHKIMVWRVKDWETVGTLKGHTARVNDVDIHPTNRIAISVSDDHSIRLWNLMTLRNAAVLKLRKYNTNGTCVRWLGAKGDYFAVGLRDRVLIYETGSAKVFKEIVFQRKTLMHIETHILPFDNKEYLSVGISDGNVHFYPCEELFEKVEENEKQEDDDDKEDISPAFSLLGHTNRIKDFKFYTNEFGTYLVTIGSDGKIVVWDMSTKEQVAVYDCGERLNCLTLCDESIEKYNTMKKRDAETADIGDQSEVESDTEELKKIMFGEKKKLNKKKRKQLKKSKVSVELE 414 P20592 Interferon-induced GTP-binding protein Mx2 MX2 9606 Yes SL-0178 SL-0185 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. UNIPROT P20592 UNIPROT B7Z5D3 UNIPROT D3DSI7 PDB 4WHJ PDB 4X0R PDB 5UOT Pfam PF01031 Pfam PF00350 Pfam PF02212 PROSITE PS00410 PROSITE PS51718 PROSITE PS51388 OMIM 147890 DisGeNET 4600 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}. A2ABF9 EBI-10174566,EBI-10200618 O75928 EBI-348555,EBI-10200618 Q8WXE1 EBI-10200618,EBI-747353 Q96KQ7 EBI-744366,EBI-10200618 GO:0030424 GO:0005737 GO:0031410 GO:0005829 GO:0043197 GO:0044327 GO:0016020 GO:0015630 GO:0031966 GO:0005643 GO:0005634 GO:0005886 GO:0014069 GO:0098844 GO:0045211 GO:0098793 GO:0045202 GO:0005525 GO:0003924 GO:0008017 GO:0006952 GO:0051607 GO:0061025 GO:0000266 GO:0051028 GO:0048285 GO:0098884 GO:0031623 GO:0051726 GO:0046822 GO:0050803 GO:0035455 GO:0009615 GO:0016185 GO:0060337 MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQPRAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH 715 P20676 Nucleoporin NUP1 NUP1 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. UNIPROT P20676 UNIPROT D6W2F9 PDB 4C31 PDB 4MBE PDB 5OWU 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}. Q06142 EBI-9145,EBI-12392 P16474 EBI-12392,EBI-7876 P36016 EBI-12392,EBI-10154 Q12329 EBI-12392,EBI-8571 P11484 EBI-12392,EBI-8627 P40150 EBI-12392,EBI-8632 P10591 EBI-12392,EBI-8591 P52297 EBI-618940,EBI-12392 P35177 EBI-17958,EBI-12392 P50102 EBI-19863,EBI-12392 P51116 EBI-12392,EBI-740459 Q08379 EBI-618309,EBI-12392 P10592 EBI-12392,EBI-8603 Q02821 EBI-12392,EBI-1797 P10081 EBI-12392,EBI-9017 P00359 EBI-12392,EBI-7218 P00560 EBI-12392,EBI-13275 P06168 EBI-12392,EBI-9082 P00950 EBI-12392,EBI-13517 P14540 EBI-12392,EBI-2447 P00925 EBI-12392,EBI-6475 P32324 EBI-12392,EBI-6333 P41832 EBI-12392,EBI-3692 P00330 EBI-12392,EBI-2218 Q03771 EBI-36525,EBI-12392 P28003 EBI-20647,EBI-12392 P38305 EBI-20939,EBI-12392 Q12315 EBI-7635,EBI-12392 GO:0031965 GO:0005643 GO:0044613 GO:0044615 GO:0008139 GO:0017056 GO:0006607 GO:0016973 GO:0006606 GO:0000055 GO:0006405 GO:0000972 MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTLHVNKRKRVSGTSQHSDSLTQNNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRNMRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTPSPIKNGSCTRQLAGKSGEDTNVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKTSENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPIQESFVPNSERSGTPTLKKNIEPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAVFKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTVPSTTLFNFGGKSDTVTSASQPFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNTKPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSSAQFTFGKAATAKETHTKPSETPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEERKSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTEPAQKDSSVVSEPKKPSFTFASSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTTTSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTPIPVLGKPTDATGNTTSKSAFSFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTNIAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAASNQSSFNFGNNGAGGLNPFTSATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSNNQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNVTNPSSIFGGAGGVPTTSFGQPQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR 1076 P20749 B-cell lymphoma 3 protein BCL3 9606 Yes SL-0198 Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Ubiquitination via 'Lys-63'- linked ubiquitin chains is required for nuclear accumulation. {ECO:0000250}. UNIPROT P20749 PDB 1K1A PDB 1K1B Pfam PF12796 PROSITE PS50297 PROSITE PS50088 OMIM 109560 DisGeNET 602 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}.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}. O95999 EBI-958922,EBI-958997 Q92598 EBI-958997,EBI-356829 Q00653 EBI-958997,EBI-307326 P19838 EBI-958997,EBI-300010 P17066 EBI-958997,EBI-355106 O15084 EBI-359567,EBI-958997 P56545 EBI-741533,EBI-958997 GO:0032996 GO:0033257 GO:0005737 GO:0005829 GO:0043231 GO:0030496 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0003700 GO:0030674 GO:0000978 GO:0008134 GO:0019730 GO:0006974 GO:0042742 GO:0042832 GO:0030330 GO:0030198 GO:0002268 GO:0002467 GO:0002455 GO:0007249 GO:0042771 GO:0051457 GO:0002315 GO:0043066 GO:0045415 GO:0046426 GO:0045892 GO:0042536 GO:0032729 GO:0045082 GO:0045944 GO:0045893 GO:0045727 GO:0042981 GO:0051101 GO:1901222 GO:0010225 GO:0009615 GO:0048536 GO:0042088 GO:0045064 GO:0006351 MPRCPAGAMDEGPVDLRTRPKAAGLPGAALPLRKRPLRAPSPEPAAPRGAAGLVVPLDPLRGGCDLPAVPGPPHGLARPEALYYPGALLPLYPTRAMGSPFPLVNLPTPLYPMMCPMEHPLSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPASTSQPDPSPDRSANTSPESSSRLSSNGLLSASPSSSPSQSPPRDPPGFPMAPPNFFLPSPSPPAFLPFAGVLRGPGRPVPPSPAPGGS 454 P21279 Guanine nucleotide-binding protein G(q) subunit alpha Gnaq 10090 Yes SL-0178 SL-0182 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}. UNIPROT P21279 UNIPROT Q6PFF5 PDB 2BCJ PDB 2RGN PDB 3AH8 PDB 3OHM PDB 4EKC PDB 4EKD PDB 4GNK PDB 4QJ3 PDB 4QJ4 PDB 4QJ5 PDB 5DO9 Pfam PF00503 PROSITE PS51882 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}. Q3UHD9 EBI-771911,EBI-771975 P62871 EBI-771975,EBI-357141 P63278-2 EBI-22091956,EBI-771975 Q9CQV8 EBI-771608,EBI-771975 GO:0005901 GO:0044297 GO:0005829 GO:0030425 GO:0005834 GO:0016020 GO:0031965 GO:0005886 GO:0032991 GO:0047391 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0044877 GO:0031826 GO:0001508 GO:0007202 GO:0007189 GO:0007188 GO:0048066 GO:0042733 GO:0021884 GO:0007186 GO:0007215 GO:0007507 GO:0042711 GO:0043066 GO:0043267 GO:0006469 GO:0016322 GO:0060158 GO:0007200 GO:0048661 GO:0009791 GO:0050821 GO:0060828 GO:0045634 GO:0001501 MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 P21818 Stathmin-2 Stmn2 10116 Yes SL-0198 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}. UNIPROT P21818 UNIPROT Q9ERH2 Pfam PF00836 PROSITE PS00563 PROSITE PS01041 PROSITE PS51663 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}. GO:0005737 GO:0005768 GO:0005794 GO:0030426 GO:0030027 GO:0016020 GO:0043005 GO:0043025 GO:0048471 GO:0031982 GO:0048306 GO:0015631 GO:1990090 GO:0007019 GO:0007026 GO:0031115 GO:0010977 GO:0031175 GO:0031117 GO:0010976 GO:0051493 GO:0031110 MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLSLEEIQKKLEAAEGRRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEKERHAAEVRRNKELQVELSG 179 P21910 Lamin-L(II) LAML2 8355 No SL-0178 SL-0179 SL-0182 Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. UNIPROT P21910 Pfam PF00038 Pfam PF00932 PROSITE PS00226 PROSITE PS51842 PROSITE PS51841 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. GO:0005882 GO:0005637 MATTTPSRSTRSSMQSPARGTSTPLSPTRISRLQEKEELRHLNDRLAVYIDRVRALELENDRLMVKISEKEEVTTREVSGIKNLYESELADARKVLDETARERARLQIELGKFRSDLDELNKNYKKKDADLSTAQGRIKDLEALFHRSEAELGTALGEKRSLEAEVADLRAQLSKTEDAHRVAKKQLEKETLMRVDFENRMQSLQEEMDFRKNIYEEESRETRKRHERRIVEVDRGHHYDYESKLAQALDELRKQHDEQVKMYKEELEQTYQAKLDNIKRSSDHNDKAANTALEELTERRMRIETLGYQLSGLQKQANAAEERIRELEELLSSDRDKYRKLLDSKEREMAEMRDQMQQQLNEYQELLDVKLALDLEINAYRKLLEGEEERLKLSPSPESRVTVSRATSSSSSATRTSRSKRRRVEEEYEEGGASTGFGAGHSLGSSRITASEGSSRTITSGQSSTTRFHLSQQASATGSISIEEIDLEGKYVHLKNNSDKDQSLGNWRLKRKIGEEEEIVYKFTPKYVLKAGQSVKIYSADAGVAHSPPSILVWKNQSSWGTGSNIRTYLVNTEEEEVAVRTVTKSVLRNVEEEEDEDADFGEEDLFHQQGDPRTTSRGCSVM 623 P22147 5'-3' exoribonuclease 1 XRN1 559292 Yes SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. UNIPROT P22147 UNIPROT D6VTX9 PDB 6Q8Y Pfam PF18129 Pfam PF18332 Pfam PF18334 Pfam PF18194 Pfam PF17846 Pfam PF03159 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}. P39523 EBI-27256,EBI-9642 P10591 EBI-8591,EBI-9642 P53940 EBI-2612341,EBI-9642 P39987 EBI-22339,EBI-9642 P32589 EBI-9642,EBI-8648 P11484 EBI-8627,EBI-9642 P10592 EBI-8603,EBI-9642 P33416 EBI-9642,EBI-8680 P38788 EBI-9642,EBI-24570 P02829 EBI-9642,EBI-8659 P53131 EBI-505,EBI-9642 P30822 EBI-20589,EBI-9642 P32495 EBI-12014,EBI-9642 P39715 EBI-6302,EBI-9642 P40070 EBI-188,EBI-9642 P53730 EBI-28496,EBI-9642 Q12180 EBI-37549,EBI-9642 P38112 EBI-10394,EBI-9642 P39730 EBI-8936,EBI-9642 Q12230 EBI-34978,EBI-9642 P50094 EBI-9195,EBI-9642 Q00539 EBI-11835,EBI-9642 P36520 EBI-15501,EBI-9642 P25644 EBI-204,EBI-9642 P07347 EBI-2796,EBI-9642 P39935 EBI-9002,EBI-9642 P33759 EBI-413,EBI-9642 P32588 EBI-14231,EBI-9642 P39928 EBI-17357,EBI-9642 P38934 EBI-3593,EBI-9642 P38996 EBI-11776,EBI-9642 P50095 EBI-9190,EBI-9642 P28007 EBI-7321,EBI-9642 P53917 EBI-28900,EBI-9642 Q07508 EBI-673,EBI-9642 P06102 EBI-12165,EBI-9642 P21954 EBI-8898,EBI-9642 P57743 EBI-10227,EBI-9642 P38199 EBI-21217,EBI-9642 P37838 EBI-12122,EBI-9642 P36160 EBI-15881,EBI-9642 P28003 EBI-20647,EBI-9642 P47017 EBI-174,EBI-9642 P53849 EBI-29244,EBI-9642 P07280 EBI-14536,EBI-9642 P39735 EBI-20627,EBI-9642 P04912 EBI-8076,EBI-9642 P10080 EBI-18146,EBI-9642 P53883 EBI-29032,EBI-9642 P38203 EBI-180,EBI-9642 Q03782 EBI-627,EBI-9642 P53617 EBI-12228,EBI-9642 P41544 EBI-25763,EBI-9642 P42846 EBI-28360,EBI-9642 P46677 EBI-18855,EBI-9642 Q06406 EBI-196,EBI-9642 P07260 EBI-150,EBI-9642 Q12339 EBI-30231,EBI-9642 P51998 EBI-450,EBI-9642 P27476 EBI-12274,EBI-9642 P31334 EBI-15497,EBI-9642 P46995 EBI-16985,EBI-9642 P38217 EBI-9152,EBI-9642 P53550 EBI-9642,EBI-270 Q12517 EBI-9642,EBI-38519 P53905 EBI-141,EBI-9642 P40089 EBI-10236,EBI-9642 P33322 EBI-4105,EBI-9642 P39998 EBI-22300,EBI-9642 P38789 EBI-18160,EBI-9642 P32357 EBI-340,EBI-9642 P20448 EBI-5612,EBI-9642 P07246 EBI-2227,EBI-9642 P23293 EBI-17078,EBI-9642 P32493 EBI-11898,EBI-9642 P07270 EBI-13378,EBI-9642 P14680 EBI-20777,EBI-9642 Q04264 EBI-13077,EBI-9642 GO:0005737 GO:0010494 GO:0005829 GO:0090512 GO:0005874 GO:0005634 GO:0000932 GO:0048471 GO:0004534 GO:0003682 GO:0003729 GO:0000741 GO:0061157 GO:0016242 GO:0070651 GO:0000956 GO:0000184 GO:0032968 GO:0060261 GO:0006364 GO:0043144 GO:0007089 GO:0016078 MGIPKFFRYISERWPMILQLIEGTQIPEFDNLYLDMNSILHNCTHGNDDDVTKRLTEEEVFAKICTYIDHLFQTIKPKKIFYMAIDGVAPRAKMNQQRARRFRTAMDAEKALKKAIENGDEIPKGEPFDSNSITPGTEFMAKLTKNLQYFIHDKISNDSKWREVQIIFSGHEVPGEGEHKIMNFIRHLKSQKDFNQNTRHCIYGLDADLIMLGLSTHGPHFALLREEVTFGRRNSEKKSLEHQNFYLLHLSLLREYMELEFKEIADEMQFEYNFERILDDFILVMFVIGNDFLPNLPDLHLNKGAFPVLLQTFKEALLHTDGYINEHGKINLKRLGVWLNYLSQFELLNFEKDDIDVEWFNKQLENISLEGERKRQRVGKKLLVKQQKKLIGSIKPWLMEQLQEKLSPDLPDEEIPTLELPKDLDMKDHLEFLKEFAFDLGLFITHSKSKGSYSLKMDLDSINPDETEEEFQNRVNSIRKTIKKYQNAIIVEDKEELETEKTIYNERFERWKHEYYHDKLKFTTDSEEKVRDLAKDYVEGLQWVLYYYYRGCPSWSWYYPHHYAPRISDLAKGLDQDIEFDLSKPFTPFQQLMAVLPERSKNLIPPAFRPLMYDEQSPIHDFYPAEVQLDKNGKTADWEAVVLISFVDEKRLIEAMQPYLRKLSPEEKTRNQFGKDLIYSFNPQVDNLYKSPLGGIFSDIEHNHCVEKEYITIPLDSSEIRYGLLPNAKLGAEMLAGFPTLLSLPFTSSLEYNETMVFQQPSKQQSMVLQITDIYKTNNVTLEDFSKRHLNKVIYTRWPYLRESKLVSLTDGKTIYEYQESNDKKKFGFITKPAETQDKKLFNSLKNSMLRMYAKQKAVKIGPMEAIATVFPVTGLVRDSDGGYIKTFSPTPDYYPLQLVVESVVNEDERYKERGPIPIEEEFPLNSKVIFLGDYAYGGETTIDGYSSDRRLKITVEKKFLDSEPTIGKERLQMDHQAVKYYPSYIVSKNMHLHPLFLSKITSKFMITDATGKHINVGIPVKFEARHQKVLGYARRNPRGWEYSNLTLNLLKEYRQTFPDFFFRLSKVGNDIPVLEDLFPDTSTKDAMNLLDGIKQWLKYVSSKFIAVSLESDSLTKTSIAAVEDHIMKYAANIEGHERKQLAKVPREAVLNPRSSFALLRSQKFDLGDRVVYIQDSGKVPIFSKGTVVGYTTLSSSLSIQVLFDHEIVAGNNFGGRLRTNRGLGLDASFLLNITNRQFIYHSKASKKALEKKKQSNNRNNNTKTAHKTPSKQQSEEKLRKERAHDLLNFIKKDTNEKNSESVDNKSMGSQKDSKPAKKVLLKRPAQKSSENVQVDLANFEKAPLDNPTVAGSIFNAVANQYSDGIGSNLNIPTPPHPMNVVGGPIPGANDVADVGLPYNIPPGFMTHPNGLHPLHPHQMPYPNMNGMSIPPPAPHGFGQPISFPPPPPMTNVSDQGSRIVVNEKESQDLKKFINGKQHSNGSTIGGETKNSRKGEIKPSSGTNSTECQSPKSQSNAADRDNKKDEST 1528 P23913 Delta(14)-sterol reductase LBR LBR 9031 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT P23913 PDB 2L8D Pfam PF01222 Pfam PF09465 PROSITE PS01017 PROSITE PS01018 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}. GO:0005737 GO:0005789 GO:0016021 GO:0005637 GO:0005634 GO:0050613 GO:0003677 GO:0070402 GO:0016627 GO:0006695 GO:0030223 GO:0016126 MPNRKYADGEVVMGRWPGSVLYYEVQVTSYDDASHLYTVKYKDGTELALKESDIRLQSSFKQRKSQSSSSSPSRRSRSRSRSRSPGRPAKGRRRSSSHSREHKEDKKKIIQETSLAPPKPSENNTRRYNGEPDSTERNDTSSKLLEQQKLKPDVEMERVLDQYSLRSRREEKKKEEIYAEKKIFEAIKTPEKPSSKTKELEFGGRFGTFMLMFFLPATVLYLVLMCKQDDPSLMNFPPLPALESLWETKVFGVFLLWFFFQALFYLLPIGKVVEGLPLSNPRKLQYRINGFYAFLLTAAAIGTLLYFQFELHYLYDHFVQFAVSAAAFSMALSIYLYIRSLKAPEEDLAPGGNSGYLVYDFFTGHELNPRIGSFDLKYFCELRPGLIGWVVINLAMLLAEMKIHNQSMPSLSMILVNSFQLLYVVDALWNEEAVLTTMDITHDGFGFMLAFGDLVWVPFVYSLQAFYLVGHPIAISWPVAAAITILNCIGYYIFRSANSQKNNFRRNPADPKLSYLKVIPTATGKGLLVTGWWGFVRHPNYLGDIIMALAWSLPCGFNHILPYFYVIYFICLLVHREARDEHHCKKKYGLAWERYCQRVPYTHISLHLLEHSTYLICKLKYTSHLCTWSVCYLGFKH 637 P24385 G1/S-specific cyclin-D1 CCND1 9606 Yes SL-0178 SL-0182 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}. UNIPROT P24385 UNIPROT Q6LEF0 PDB 2W96 PDB 2W99 PDB 2W9F PDB 2W9Z PDB 5VZU PDB 6P8E PDB 6P8F PDB 6P8G PDB 6P8H Pfam PF02984 Pfam PF00134 PROSITE PS00292 OMIM 168461 OMIM 254500 DisGeNET 595 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}.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. P11802 EBI-295644,EBI-375001 P38398 EBI-349905,EBI-375001 Q02224 EBI-375001,EBI-1375040 O95239 EBI-375001,EBI-1057516 O94880 EBI-375001,EBI-2680164 P38936 EBI-375077,EBI-375001 Q13761 EBI-925990,EBI-375001 Q00534 EBI-375001,EBI-295663 P42771 EBI-375053,EBI-375001 P49841 EBI-375001,EBI-373586 P11142 EBI-351896,EBI-375001 Q96TE0 EBI-10201595,EBI-375001 Q9BQA1 EBI-1237307,EBI-375001 O60477 EBI-375001,EBI-3904864 P06858 EBI-715909,EBI-375001 Q9H9Y6 EBI-355441,EBI-375001 P46527 EBI-375001,EBI-519280 P20020-6 EBI-375001,EBI-10972265 P05141 EBI-375001,EBI-355133 P43251 EBI-375001,EBI-2907478 P06493 EBI-375001,EBI-444308 O60673-2 EBI-375001,EBI-10977129 P24941 EBI-375096,EBI-375001 Q9UJK0 EBI-375001,EBI-11035689 Q07283 EBI-375001,EBI-1046116 Q00535 EBI-375001,EBI-1041567 P49918-2 EBI-375001,EBI-11103414 P42773 EBI-375001,EBI-711290 Q15276 EBI-447043,EBI-375001 P36873-1 EBI-375001,EBI-356289 P62140 EBI-352350,EBI-375001 P11802-1 EBI-22122649,EBI-375001 P06400 EBI-375001,EBI-491274 Q9UH17 EBI-2967317,EBI-375001 P49815 EBI-375001,EBI-396587 O43929 EBI-375001,EBI-374889 Q7L590 EBI-375001,EBI-374912 GO:0005923 GO:0000307 GO:0005737 GO:0005829 GO:0005622 GO:0031965 GO:0005654 GO:0005634 GO:0017053 GO:0016538 GO:0019899 GO:0042826 GO:0070064 GO:0004672 GO:0019901 GO:0044877 GO:0003714 GO:0008134 GO:0051301 GO:0006974 GO:0019221 GO:0030968 GO:0045444 GO:0000082 GO:0007595 GO:0033327 GO:0097421 GO:0060749 GO:0033598 GO:0044772 GO:0031571 GO:0071157 GO:0030857 GO:0000122 GO:0045787 GO:0045737 GO:1900087 GO:0010971 GO:0033601 GO:0001934 GO:0000320 GO:0000079 GO:0051592 GO:0051412 GO:0042493 GO:0032355 GO:0043627 GO:0045471 GO:0010039 GO:0044321 GO:0032026 GO:0010243 GO:0070141 GO:0033197 GO:0010165 GO:0006367 GO:0016055 MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI 295 P25028 Mitosis initiation protein fs(1)Ya fs 7227 Yes SL-0178 Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm. Note=In the nuclear envelope during interphase to metaphase. And in the nucleoplasm and cytoplasm during anaphase and telophase. UNIPROT P25028 UNIPROT Q8T057 UNIPROT Q9W4W0 UNIPROT Q9W4W1 PROSITE PS00028 Cell cycle-dependent nuclear envelope component required for embryonic mitosis. P08928 EBI-188444,EBI-106103 O61307 EBI-118556,EBI-106103 P02283 EBI-188137,EBI-106103 GO:0005737 GO:0005635 GO:0005652 GO:0005654 GO:0051301 GO:0006333 GO:0030261 GO:0006260 GO:0000278 GO:0006997 GO:0007344 MSFSNVLIMRQPDEGKCHICKRVFCCGKCRQKHQFKAHAIAVREPLGLRSAGGGIIEHRHQMESGATTIYVFCPICERRPLLLREEMHGELLAHIETCHLPLRCRKCQRNYTRVDDLREFSKCVDQQQSCTDVTGATETSKATLKKAANSTAISTQTSPSVTPISLINMRWKAKSRVTHEEFISDSVSSIRNLSSFSNSSIRRSIGQLGVNPSETMEKGKVIRSTSTPLHVESVFAKPKEPITFNASTGGHVSSIYHEEPSPTPESNPVQQQQQQQQPLQQRAWKMGARNKMSAATPLRQVMSKSIQKAFVEHGGMMVHQPPSAVVQRRVRLDLSEHSSHEAAGSSALDLRLSPAMRRTQSESSASEVNSGSSSSYSTSRNADLCKRQFLLSAQKLTTESIIITRTNSSSQKTSSTVYNSCESVEIIRSTSESAEVCHVPAITPIRVTGAGINKKQIKFETPPKSSQQMRSNGEGDETKDQFFTPEPGTPEIPERRHRQAIVPRQLSGEFSPKKDKPKEKGLAVMALISPPLQQPRVRPPLRECRQQRVYSGVQDVGEPEVVDAEEEDEVFRPTNASTCNDKKLEAPNSGRLWSLMSSMMRLPASLRGEREKDRDRDRDSDKENAGSGSLIRRCASIAGSLVRPSARDSSMEDQQCLKRKRTQTLDSQYCSPLSPSSSSKRYRIRPREPIERMRRQ 696 P25491 Mitochondrial protein import protein MAS5 YDJ1 559292 Yes SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrated in a perinuclear ring as well as in the cytoplasm. UNIPROT P25491 UNIPROT D6W1B6 PDB 1NLT PDB 1XAO PDB 5VSO Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. P06105 EBI-10420,EBI-16374 P06782 EBI-10420,EBI-17516 P12866 EBI-18383,EBI-10420 P40075 EBI-16735,EBI-10420 P04150 EBI-493507,EBI-10420 P10591 EBI-8591,EBI-10420 P31376 EBI-20613,EBI-10420 P08153 EBI-10420,EBI-18633 P40528 EBI-18696,EBI-10420 P40468 EBI-10420,EBI-18961 Q06510 EBI-10420,EBI-2094606 Q12466 EBI-10420,EBI-34614 Q03640 EBI-10420,EBI-27872 P38228 EBI-19039,EBI-10420 P00359 EBI-7218,EBI-10420 P02994 EBI-6314,EBI-10420 P41903 EBI-14154,EBI-10420 P36145 EBI-18907,EBI-10420 Q02939 EBI-2345544,EBI-10420 P32367 EBI-10420,EBI-19150 P14306 EBI-5916,EBI-10420 P10081 EBI-10420,EBI-9017 P34167 EBI-10420,EBI-9025 P40217 EBI-8951,EBI-10420 Q04067 EBI-10420,EBI-8958 P38431 EBI-10420,EBI-9038 Q01852 EBI-9141,EBI-10420 Q02208 EBI-27048,EBI-10420 P04786 EBI-19338,EBI-10420 P35169 EBI-19374,EBI-10420 P40032 EBI-22536,EBI-10420 P40414 EBI-10420,EBI-19419 P48561 EBI-10420,EBI-19525 P12685 EBI-19530,EBI-10420 Q04183 EBI-10420,EBI-32112 P40061 EBI-22621,EBI-10420 P09733 EBI-10420,EBI-18976 P09734 EBI-10420,EBI-18981 P52488 EBI-19710,EBI-10420 P25037 EBI-10420,EBI-19819 Q06682 EBI-32041,EBI-10420 P07259 EBI-10420,EBI-14372 P03962 EBI-14397,EBI-10420 P25386 EBI-20157,EBI-10420 P35194 EBI-10420,EBI-1871 P53254 EBI-1878,EBI-10420 Q06679 EBI-35712,EBI-10420 Q07468 EBI-20422,EBI-10420 P40522 EBI-10420,EBI-25035 Q06337 EBI-10420,EBI-35867 P40157 EBI-10420,EBI-29136 P40547 EBI-10420,EBI-24957 P16140 EBI-20254,EBI-10420 P23643 EBI-10420,EBI-20469 Q03433 EBI-10420,EBI-27814 P40438 EBI-3662633,EBI-10420 P40890 EBI-10420,EBI-26271 P33767 EBI-12658,EBI-10420 Q12416 EBI-10420,EBI-29963 P38749 EBI-10420,EBI-24313 O13527 EBI-33845,EBI-10420 P40017 EBI-2345299,EBI-10420 P34220 EBI-3759231,EBI-10420 P34225 EBI-10420,EBI-2344464 Q12491 EBI-10420,EBI-3767258 Q12193 EBI-10420,EBI-38876 P38219 EBI-21409,EBI-10420 P38266 EBI-21584,EBI-10420 P38331 EBI-21083,EBI-10420 P38332 EBI-21094,EBI-10420 P39109 EBI-10420,EBI-21779 P25616 EBI-21864,EBI-10420 Q06156 EBI-10420,EBI-4785 Q07349 EBI-10420,EBI-3698596 Q12516 EBI-10420,EBI-38546 Q06640 EBI-34097,EBI-10420 Q04411 EBI-10420,EBI-36153 Q3E7X8 EBI-3763343,EBI-10420 P40028 EBI-22514,EBI-10420 P40085 EBI-10420,EBI-22717 P43560 EBI-22832,EBI-10420 P43597 EBI-10420,EBI-22951 P53144 EBI-10420,EBI-23891 P53100 EBI-24104,EBI-10420 P53077 EBI-24169,EBI-10420 P53234 EBI-10420,EBI-23168 P53246 EBI-10420,EBI-23209 Q99315 EBI-3767461,EBI-10420 P50089 EBI-10420,EBI-23545 P53321 EBI-23598,EBI-10420 Q05900 EBI-10420,EBI-754 P0C2J7 EBI-10420,EBI-3761931 P38842 EBI-10420,EBI-24752 P47024 EBI-26039,EBI-10420 P47101 EBI-10420,EBI-25467 P28320 EBI-10420,EBI-26795 P34246 EBI-10420,EBI-26803 P34248 EBI-26807,EBI-10420 P28273 EBI-27022,EBI-10420 P36158 EBI-2936913,EBI-10420 Q07799 EBI-38901,EBI-10420 Q12244 EBI-10420,EBI-35601 Q12177 EBI-30090,EBI-10420 Q07897 EBI-10420,EBI-37851 Q12110 EBI-33635,EBI-10420 Q12288 EBI-10420,EBI-3767612 Q06247 EBI-10420,EBI-38452 Q06152 EBI-10420,EBI-35313 Q05867 EBI-10420,EBI-36496 Q06159 EBI-33888,EBI-10420 Q06479 EBI-35627,EBI-10420 Q06409 EBI-35964,EBI-10420 O13577 EBI-34501,EBI-10420 Q04533 EBI-10420,EBI-10803 Q04371 EBI-10420,EBI-28049 P0CF18 EBI-3767696,EBI-10420 Q03153 EBI-28199,EBI-10420 Q04471 EBI-10420,EBI-27220 Q03496 EBI-10420,EBI-3654556 P40168 EBI-10420,EBI-3767735 P53852 EBI-10420,EBI-29230 P53850 EBI-3767755,EBI-10420 P53837 EBI-10420,EBI-28271 P53756 EBI-10420,EBI-28581 P53757 EBI-10420,EBI-28586 Q99247 EBI-34003,EBI-10420 Q12496 EBI-29300,EBI-10420 Q08270 EBI-35014,EBI-10420 Q08457 EBI-36267,EBI-10420 Q12275 EBI-10420,EBI-33858 P53049 EBI-29324,EBI-10420 Q12032 EBI-32069,EBI-10420 Q08748 EBI-2050125,EBI-10420 Q02754 EBI-10420,EBI-34779 Q02895 EBI-35030,EBI-10420 Q08964 EBI-38118,EBI-10420 Q06813 EBI-38252,EBI-10420 Q06108 EBI-10420,EBI-38709 P01123 EBI-29496,EBI-10420 P51996 EBI-29384,EBI-10420 P36019 EBI-29415,EBI-10420 Q12159 EBI-10420,EBI-29516 P53819 EBI-2103894,EBI-10420 P40341 EBI-14858,EBI-10420 P40328 EBI-19022,EBI-10420 P40340 EBI-10420,EBI-19030 P31111 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EBI-18410,EBI-10420 P53101 EBI-10420,EBI-24097 P37297 EBI-10420,EBI-18454 P38198 EBI-10420,EBI-18463 P09064 EBI-10420,EBI-8920 P46676 EBI-10420,EBI-18547 P12385 EBI-6533,EBI-10420 P02829 EBI-8659,EBI-10420 A0A023PZA9 EBI-3862844,EBI-10420 P47171 EBI-10420,EBI-25715 Q03973 EBI-10420,EBI-33047 P32478 EBI-10420,EBI-4405 P04912 EBI-10420,EBI-8076 P07263 EBI-10420,EBI-18711 Q12692 EBI-8080,EBI-10420 P04807 EBI-10420,EBI-8738 P43579 EBI-10420,EBI-22775 P38286 EBI-10420,EBI-20857 P09436 EBI-18718,EBI-10420 P00927 EBI-19200,EBI-10420 P50095 EBI-10420,EBI-9190 P53115 EBI-24019,EBI-10420 P40006 EBI-2050819,EBI-10420 Q07821 EBI-10420,EBI-27136 P36132 EBI-10420,EBI-26411 P38217 EBI-9152,EBI-10420 Q08979 EBI-10420,EBI-9638 P22209 EBI-9730,EBI-10420 P40540 EBI-24977,EBI-10420 Q3E840 EBI-2055307,EBI-10420 P12695 EBI-10420,EBI-12469 P57743 EBI-10420,EBI-10227 P53905 EBI-10420,EBI-141 P48570 EBI-8502,EBI-10420 P49367 EBI-10276,EBI-10420 P11914 EBI-11205,EBI-10420 P39677 EBI-6361,EBI-10420 P24719 EBI-10690,EBI-10420 P00958 EBI-10420,EBI-18762 P53128 EBI-11572,EBI-10420 P33441 EBI-10841,EBI-10420 P09440 EBI-3903,EBI-10420 P53141 EBI-10988,EBI-10420 P25847 EBI-10420,EBI-11352 P32335 EBI-10420,EBI-11318 P47047 EBI-11592,EBI-10420 P19524 EBI-10420,EBI-11659 P38205 EBI-10420,EBI-11933 Q08972 EBI-10420,EBI-32014 P53081 EBI-12063,EBI-10420 P06102 EBI-10420,EBI-12165 P53164 EBI-10420,EBI-11856 P31378 EBI-10420,EBI-12294 P35172 EBI-10420,EBI-19513 P39705 EBI-20731,EBI-10420 P54784 EBI-12568,EBI-10420 P50874 EBI-12584,EBI-10420 P38826 EBI-12588,EBI-10420 Q12451 EBI-12621,EBI-10420 Q12447 EBI-10420,EBI-33397 P38254 EBI-10420,EBI-21533 Q04264 EBI-13077,EBI-10420 P42841 EBI-28378,EBI-10420 P47110 EBI-6084,EBI-10420 P39985 EBI-6120,EBI-10420 P23595 EBI-10420,EBI-12752 P32345 EBI-12759,EBI-10420 P53131 EBI-505,EBI-10420 P28708 EBI-9782,EBI-10420 Q12265 EBI-9886,EBI-10420 P41940 EBI-11191,EBI-10420 Q12335 EBI-10420,EBI-14064 Q12318 EBI-10420,EBI-37340 P09368 EBI-10420,EBI-14299 P06777 EBI-10420,EBI-14752 P32628 EBI-10420,EBI-14668 P32641 EBI-14675,EBI-10420 P06839 EBI-10420,EBI-14762 Q04231 EBI-10420,EBI-27726 P25454 EBI-10420,EBI-14709 P21538 EBI-10420,EBI-14905 P22336 EBI-10420,EBI-14971 P39083 EBI-10420,EBI-15044 Q00453 EBI-15073,EBI-10420 P16664 EBI-15080,EBI-10420 P48565 EBI-3664151,EBI-10420 Q07844 EBI-10420,EBI-27142 P21524 EBI-15234,EBI-10420 P32561 EBI-15864,EBI-10420 P32565 EBI-15919,EBI-10420 P40016 EBI-10420,EBI-15927 P40327 EBI-10420,EBI-13901 Q12754 EBI-10420,EBI-30678 P53236 EBI-16192,EBI-10420 Q05543 EBI-35018,EBI-10420 Q03940 EBI-10420,EBI-30712 P32368 EBI-10420,EBI-16210 Q08873 EBI-33137,EBI-10420 P40509 EBI-4884,EBI-10420 P38968 EBI-10420,EBI-20524 O94742 EBI-10420,EBI-31337 P46995 EBI-16985,EBI-10420 P53953 EBI-17006,EBI-10420 P23293 EBI-10420,EBI-17078 P51534 EBI-10420,EBI-17086 P11978 EBI-17237,EBI-10420 Q04195 EBI-10420,EBI-32913 P53327 EBI-10420,EBI-23623 P38989 EBI-10420,EBI-17412 P47037 EBI-17423,EBI-10420 P36048 EBI-243,EBI-10420 Q04053 EBI-10420,EBI-30464 P38633 EBI-10420,EBI-17658 P38863 EBI-17786,EBI-10420 P23561 EBI-18259,EBI-10420 P05453 EBI-6540,EBI-10420 P53201 EBI-10420,EBI-23061 P09959 EBI-18641,EBI-10420 Q05471 EBI-22102,EBI-10420 Q04175 EBI-10420,EBI-35508 Q12297 EBI-10420,EBI-36697 P33339 EBI-10420,EBI-19159 Q06339 EBI-29851,EBI-10420 P17423 EBI-9685,EBI-10420 P23254 EBI-19291,EBI-10420 P40462 EBI-25239,EBI-10420 P53840 EBI-10420,EBI-28257 Q03280 EBI-10420,EBI-36817 P06786 EBI-19352,EBI-10420 P43637 EBI-10420,EBI-9668 P06244 EBI-10420,EBI-9458 Q00764 EBI-10420,EBI-19430 P38426 EBI-19448,EBI-10420 P38811 EBI-24638,EBI-10420 Q07527 EBI-10420,EBI-36284 P00937 EBI-10420,EBI-19585 P38427 EBI-10420,EBI-19638 Q07381 EBI-10420,EBI-35023 P53378 EBI-19013,EBI-10420 P36164 EBI-10420,EBI-26527 Q08960 EBI-10420,EBI-29349 Q01476 EBI-19826,EBI-10420 P43593 EBI-19852,EBI-10420 P54860 EBI-10420,EBI-20003 P33202 EBI-20010,EBI-10420 P38067 EBI-10420,EBI-20027 P28274 EBI-20128,EBI-10420 P42945 EBI-10420,EBI-1884 Q05946 EBI-34702,EBI-10420 Q06078 EBI-359,EBI-10420 P53276 EBI-23301,EBI-10420 P32623 EBI-2098544,EBI-10420 P53076 EBI-24173,EBI-10420 Q12045 EBI-38784,EBI-10420 Q06685 EBI-35034,EBI-10420 P34110 EBI-10420,EBI-20415 Q12109 EBI-18832,EBI-10420 P39735 EBI-10420,EBI-20627 P46683 EBI-20829,EBI-10420 P38222 EBI-21417,EBI-10420 P38317 EBI-20989,EBI-10420 P25361 EBI-10420,EBI-21909 Q04093 EBI-30943,EBI-10420 Q04431 EBI-10420,EBI-32446 P16521 EBI-10420,EBI-6338 P43594 EBI-22936,EBI-10420 P53262 EBI-2061527,EBI-10420 P38829 EBI-10420,EBI-24704 P38833 EBI-24716,EBI-10420 P40533 EBI-24998,EBI-10420 P36114 EBI-10420,EBI-27086 Q05778 EBI-10420,EBI-33792 Q06188 EBI-35613,EBI-10420 Q04847 EBI-10420,EBI-27556 P53970 EBI-28642,EBI-10420 P42842 EBI-10420,EBI-28374 Q08206 EBI-38207,EBI-10420 Q08548 EBI-10420,EBI-38058 Q08822 EBI-10420,EBI-6705 P12688 EBI-29473,EBI-10420 Q08924 EBI-38332,EBI-10420 O13585 EBI-10420,EBI-33008 Q06109 EBI-10420,EBI-38369 Q08245 EBI-10420,EBI-32089 P53303 EBI-29657,EBI-10420 P11412 EBI-10420,EBI-7233 P15108 EBI-8666,EBI-10420 P47138 EBI-10420,EBI-25576 P39101 EBI-3949,EBI-10420 P46997 EBI-10420,EBI-26138 P25294 EBI-17244,EBI-10420 P38009 EBI-14223,EBI-10420 P07244 EBI-10420,EBI-323 P38972 EBI-10420,EBI-14246 P25376 EBI-2357,EBI-10420 P47019 EBI-10420,EBI-26061 P47771 EBI-10420,EBI-5772 P54115 EBI-10420,EBI-5798 P46682 EBI-2213,EBI-10420 P38328 EBI-2777,EBI-10420 Q12500 EBI-10420,EBI-38577 Q05029 EBI-27508,EBI-10420 P34730 EBI-3672,EBI-10420 P47039 EBI-25893,EBI-10420 Q07457 EBI-10420,EBI-31563 P32639 EBI-10420,EBI-861 P40096 EBI-10420,EBI-11908 P00812 EBI-10420,EBI-2856 P33322 EBI-10420,EBI-4105 P31384 EBI-4396,EBI-10420 Q03705 EBI-912262,EBI-10420 P19454 EBI-9548,EBI-10420 P53195 EBI-4847,EBI-10420 P30822 EBI-10420,EBI-20589 Q06440 EBI-4950,EBI-10420 P14922 EBI-18215,EBI-10420 P36009 EBI-5844,EBI-10420 Q04216 EBI-10420,EBI-27260 P54858 EBI-10420,EBI-6042 P32461 EBI-6090,EBI-10420 P53911 EBI-10420,EBI-28927 P47169 EBI-10420,EBI-25702 P38241 EBI-780,EBI-10420 Q04409 EBI-38225,EBI-10420 P00924 EBI-6468,EBI-10420 P38333 EBI-6482,EBI-10420 P43572 EBI-22792,EBI-10420 P32353 EBI-10420,EBI-6554 P39704 EBI-10420,EBI-6587 P38819 EBI-6603,EBI-10420 Q08649 EBI-10420,EBI-6648 P53743 EBI-10420,EBI-28537 Q12178 EBI-10420,EBI-6851 P39730 EBI-10420,EBI-8936 Q08193 EBI-29273,EBI-10420 P41814 EBI-8995,EBI-10420 P12754 EBI-6265,EBI-10420 P43535 EBI-10420,EBI-7423 Q05584 EBI-7672,EBI-10420 Q08220 EBI-7915,EBI-10420 P27472 EBI-8036,EBI-10420 P32190 EBI-7694,EBI-10420 Q12180 EBI-10420,EBI-37549 Q12341 EBI-8176,EBI-10420 P20448 EBI-10420,EBI-5612 P11353 EBI-8257,EBI-10420 Q04458 EBI-10420,EBI-27205 P61830 EBI-8098,EBI-10420 P25567 EBI-10420,EBI-18084 P0CS82 EBI-10420,EBI-5419 Q08273 EBI-31686,EBI-10420 P22146 EBI-10420,EBI-7327 P38085 EBI-20222,EBI-10420 P21147 EBI-2098,EBI-10420 P00830 EBI-3242,EBI-10420 P18239 EBI-2293,EBI-10420 GO:0005829 GO:0048471 GO:0072380 GO:0005524 GO:0001671 GO:0031072 GO:0046872 GO:0051082 GO:0006458 GO:0071470 GO:0051131 GO:0042026 GO:0045047 GO:0006626 GO:0009408 GO:0035719 GO:0030433 GO:0006511 MVKETKFYDILGVPVTATDVEIKKAYRKCALKYHPDKNPSEEAAEKFKEASAAYEILSDPEKRDIYDQFGEDGLSGAGGAGGFPGGGFGFGDDIFSQFFGAGGAQRPRGPQRGKDIKHEISASLEELYKGRTAKLALNKQILCKECEGRGGKKGAVKKCTSCNGQGIKFVTRQMGPMIQRFQTECDVCHGTGDIIDPKDRCKSCNGKKVENERKILEVHVEPGMKDGQRIVFKGEADQAPDVIPGDVVFIVSERPHKSFKRDGDDLVYEAEIDLLTAIAGGEFALEHVSGDWLKVGIVPGEVIAPGMRKVIEGKGMPIPKYGGYGNLIIKFTIKFPENHFTSEENLKKLEEILPPRIVPAIPKKATVDECVLADFDPAKYNRTRASRGGANYDSDEEEQGGEGVQCASQ 409 P27269 Protein V2 V2 66366 Yes SL-0382 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. UNIPROT P27269 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 MWDPLLNEFPESVHGFRCMLAIKYLQSVEETYEPNTLGHDLIRDLISVVRARDYVEATRRYNHFHARLEGSPKAELRQPIQQPCCCPHCPRHKQATIMDVQAHVPKAQNIQNVSKP 116 P27815 cAMP-specific 3',5'-cyclic phosphodiesterase 4A PDE4A 9606 Yes SL-0198 [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. UNIPROT P27815 UNIPROT O75522 UNIPROT O76092 UNIPROT Q16255 UNIPROT Q16691 UNIPROT Q5DM53 UNIPROT Q6PMT2 UNIPROT Q8IVA7 UNIPROT Q8WUQ3 UNIPROT Q9H3H2 PDB 2QYK PDB 3I8V PDB 3TVX Pfam PF18100 Pfam PF00233 PROSITE PS00126 PROSITE PS51845 OMIM 600126 DisGeNET 5141 Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:11566027, ECO:0000269|PubMed:17727341}. P27987 EBI-751388,EBI-1384345 P22626 EBI-299649,EBI-1384345 O75344 EBI-744771,EBI-1384345 GO:0005829 GO:0016020 GO:0005654 GO:0048471 GO:0005886 GO:0032587 GO:0004115 GO:0030552 GO:0046872 GO:0006198 GO:0035690 GO:0007186 GO:0043949 GO:0010738 GO:0007608 GO:0007165 MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQPHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGRSPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEIPSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTDQEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEEISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLTQQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLPSTAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT 886 P28491 Calreticulin CALR 9823 Yes SL-0198 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}. UNIPROT P28491 UNIPROT D4N5N1 Pfam PF00262 PROSITE PS00803 PROSITE PS00804 PROSITE PS00805 PROSITE PS00014 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}. GO:0005829 GO:0005789 GO:0044322 GO:0009897 GO:0005615 GO:0042824 GO:0005635 GO:0048471 GO:0005844 GO:0033018 GO:0050681 GO:0005509 GO:0030246 GO:0005178 GO:0003729 GO:0031625 GO:0051082 GO:0090398 GO:0030866 GO:0030968 GO:0071157 GO:0033144 GO:0045665 GO:0048387 GO:0000122 GO:0017148 GO:1901164 GO:0002502 GO:0008284 GO:2000510 GO:0010595 GO:0010628 GO:1901224 GO:0050766 GO:1900026 GO:0006611 GO:0006457 GO:0034504 GO:0050821 GO:0040020 MLLPVPLLLGLVGLAAAEPTIYFKEQFLDGDGWTDRWIESKHKPDFGRFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPDGLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAVKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDSNIYAYENFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEEKKRKEEEEVDKEDEEDKDEDEEEEDEKEEEEEEDAAAGQAKDEL 417 P28865 Nuclear egress protein 1 NEC1 10370 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P28865 UNIPROT Q69060 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MTVHKSRIRRSRSLSVTHRIQKRPDHREKTKLYLQLKLHDLHTVFNLFPEYEQKFLAIIKLPITGKEPIDVPFSLSNHHQHTCLEFSPYANEQISKSACLHCESVSVPTSSDAMVAHLNQVNNVMQNRLYFYGFRKDMELIRMSAKQPTIFQIFYIVHNTINNIFPIMFERKQKLGMHIVFQSRTLHIPCECIKQIVAVSSGYNVYLDILQESVILTVLCETLDTNTNIHIDIGMLQKKLEEMDIPNEISDRLEKYKGHLIGFH 264 P28948 Envelope glycoprotein M gM 31520 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P28948 UNIPROT Q6DLF9 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MARRGAAVAEEPLLPSSGIVGIGPIEGINWRTWLVQVFCFALTTSVLFITLVTASLPQTGYPCFYGSLVDYTQKNHSVVDGVWMRQIAGGVAPTLFLETTSLVAFLYYTTLVLVAISFYLIISAVLVRRYARGKECTAVAGCTRPTTTLIASHVTLVLGTLATWLLQVVILLLSHKQAVLGAAVYVVHFVSLVFFCMSFSGLGTASAQYSSNLRILKTNLPALHKMAGPGRAVMTNLGMGMLGISLPILSLMLGIILANSFHITLWQTVTVAVGVFVALGLMFLIIVELIVSHYVHVLVGPALAVLVASSTLAVATHSYFVHFHAMVSVQAPNLATASKAIVGIMAVISIIMLVVRLVRAIMFHKKRNTEFYGRVKTVSSKARRYANKVRGPRRNPQPLNVAESRGMLLAEDSETDAEEPIYDVVSEEFETEYYDDPQRVPERSHRREYR 450 P28951 Nuclear egress protein 1 NEC1 31520 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P28951 UNIPROT Q6DLI2 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MFDGRSDIYDSTSFAAELDDLYSCRSTGRENGRRSRVSTRGVHRDRCGSAAKRRSTKRRCELVARERDRYSLYLDYMASHPSDEISAVRELVVPLIKTTSITLPFDLNQTVADNCLSLSGMGYYLGIGGCCPTCTVSGEPRLHRADRAALILAYVQQLNNIYEYRGFLASVLAAAAQGDQAGVAASEGVQAERLLENVLAQPELFFAYHVLRDGGIQNVRVLFYRDLSVSGYMMYAVFPTKSVHLHYRLIDRLLAACPGYKIIAHVWQTAFVLVVRRDEGQQTDMDIPTVSAGDIYCKMCDLSFDGELLLEYKKLYAVFDDFLPPV 326 P28954 Nuclear egress protein 2 NEC2 31520 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P28954 UNIPROT Q6S6P5 Pfam PF04541 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}. GO:0044201 GO:0016021 MDSYNYRDFAVGGGLLQRIRLVVSGSLHCGESDATLNDPKHLPARCVFQFSGPDNNSVTFPIEYVLRLMKNWARSQCDPYIRIQNTGVSVLFQGFFFAPPNAPMASITSEHNNVILKSTHTTGLALSGIERVKRGGGLDLRPLQAMMQISCFTRMPVVQLSFRFMGPEDASRTQRLLERATSFGAMELHQKRTVDSCDRSNGIVSPREHRECRERQKRRPTPKRCASEVFASLASISSAFASERVKRRPVRIAAAILAFVFVAVILAIATKGRLF 275 P28971 Protein UL20 homolog 41 31520 Yes SL-0415 SL-0418 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}. UNIPROT P28971 UNIPROT Q6S6T0 Pfam PF04544 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}. GO:0044175 GO:0044178 GO:0044200 GO:0020002 GO:0016021 GO:0019012 GO:0019058 MPQVLMGNTRLHAPLEDGIPLIENDENSSQNEVDLYDYVSMSSYGGDNDFLISSAGGNITPENRPSFSAHVVLFAISALVIKPVCCFIFLNHYVITGSYDFAVAGGVCTVLYYMRLALTAWFMFRNIQSDMLPLNVWQQFVIGCMALGRTVAFMVVSYTTLFIRSELFFSMLAPNAGREYITPIIAHKLMPLISVRSAVCLVIISTAVYAADAICDTIGFTLPRMWMCILMRSSSVKRS 239 P30429 Cell death protein 4 ced 6239 Yes SL-0198 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}. UNIPROT P30429 UNIPROT Q5BHI5 PDB 2A5Y PDB 3LQQ PDB 3LQR PDB 4M9S PDB 4M9X PDB 4M9Y PDB 4M9Z Pfam PF00619 Pfam PF00931 PROSITE PS50209 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}. P42573 EBI-494118,EBI-494247 P41958 EBI-494118,EBI-494110 Q07817 EBI-78035,EBI-494118 O61667 EBI-494118,EBI-495949 GO:0008303 GO:0005623 GO:0005829 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0032991 GO:0043531 GO:0005524 GO:0051432 GO:0051434 GO:0089720 GO:0008656 GO:0061133 GO:0042802 GO:0000287 GO:0016505 GO:0030042 GO:0097202 GO:0006919 GO:0006915 GO:1902742 GO:0050829 GO:0009792 GO:0048598 GO:0046716 GO:0043066 GO:0043065 GO:1904747 GO:2001056 GO:0010954 GO:1905808 GO:0030155 GO:0008361 GO:0043281 GO:0040034 GO:0031647 MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQSHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGRAGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLLNFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDECYDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMALQRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDHIIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQKFYDSLKNFACC 571 P30822 Exportin-1 CRM1 559292 Yes SL-0198 Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14562095}. Note=Localized in the nucleus and at its periphery. UNIPROT P30822 UNIPROT D6VV01 PDB 3M1I PDB 3VYC PDB 3WYF PDB 3WYG PDB 4GMX PDB 4GPT PDB 4HAT PDB 4HAU PDB 4HAV PDB 4HAW PDB 4HAX PDB 4HAY PDB 4HAZ PDB 4HB0 PDB 4HB2 PDB 4HB3 PDB 4HB4 PDB 5DH9 PDB 5DHA PDB 5DHF PDB 5DI9 PDB 5DIF PDB 5JLJ PDB 5UWH PDB 5UWI PDB 5UWJ PDB 5UWO PDB 5UWP PDB 5UWQ PDB 5UWR PDB 5UWS PDB 5UWT PDB 5UWU PDB 5UWW PDB 5XOJ PDB 5YRO PDB 5YST PDB 5YSU PDB 5YTB PDB 5ZPU PDB 6A38 PDB 6A3A PDB 6A3B PDB 6A3C PDB 6A3E PDB 6CIT Pfam PF08767 Pfam PF18777 Pfam PF18784 Pfam PF18787 Pfam PF03810 Pfam PF08389 PROSITE PS50166 Receptor for the leucine-rich nuclear export signal (NES). P06782 EBI-20589,EBI-17516 P12683 EBI-8377,EBI-20589 P12684 EBI-8384,EBI-20589 P14906 EBI-16636,EBI-20589 P20484 EBI-20589,EBI-10930 P22147 EBI-20589,EBI-9642 P25491 EBI-10420,EBI-20589 Q02630 EBI-11703,EBI-20589 P39523 EBI-27256,EBI-20589 P10592 EBI-20589,EBI-8603 Q12329 EBI-20589,EBI-8571 P40150 EBI-20589,EBI-8632 P11484 EBI-8627,EBI-20589 P39079 EBI-20589,EBI-19077 P39076 EBI-19049,EBI-20589 P33416 EBI-20589,EBI-8680 P02829 EBI-8659,EBI-20589 P10591 EBI-8591,EBI-20589 P23641 EBI-11178,EBI-20589 P32364 EBI-20589,EBI-17497 P40078 EBI-20589,EBI-22681 P14127 EBI-20589,EBI-14531 P38284 EBI-20589,EBI-20849 Q99207 EBI-20589,EBI-35157 P53863 EBI-20589,EBI-29183 P38806 EBI-20589,EBI-24622 P38243 EBI-20589,EBI-3698417 P53107 EBI-20589,EBI-24056 P10080 EBI-20589,EBI-18146 Q01855 EBI-20589,EBI-16058 Q04660 EBI-20589,EBI-28098 P40010 EBI-20589,EBI-22449 P32357 EBI-20589,EBI-340 P47017 EBI-20589,EBI-174 P53550 EBI-20589,EBI-270 P47149 EBI-20589,EBI-12098 P47035 EBI-20589,EBI-25953 P05755 EBI-20589,EBI-16181 P34078 EBI-20589,EBI-10248 P30771 EBI-20589,EBI-11831 P25379 EBI-20589,EBI-3804607 P40348 EBI-20589,EBI-14992 P53935 EBI-20589,EBI-28788 Q06631 EBI-20589,EBI-36432 P21192 EBI-20589,EBI-2073 P38987 EBI-20589,EBI-19113 P49626 EBI-20589,EBI-15394 P32578 EBI-20589,EBI-17179 P24276 EBI-20589,EBI-18153 P48361 EBI-20589,EBI-2993 P26448 EBI-20589,EBI-3824 P37262 EBI-20589,EBI-17680 P25368 EBI-20589,EBI-16019 P28004 EBI-20589,EBI-20640 Q92331 EBI-20589,EBI-20483 P36080 EBI-20589,EBI-26762 P26321 EBI-20589,EBI-15398 Q12199 EBI-20589,EBI-38123 P36104 EBI-20589,EBI-26608 O13329 EBI-20589,EBI-7040 P47083 EBI-20589,EBI-11168 P23202 EBI-20589,EBI-20138 P21339 EBI-20589,EBI-11322 Q03063 EBI-20589,EBI-29752 P09032 EBI-20589,EBI-6275 P32501 EBI-20589,EBI-6270 P53830 EBI-20589,EBI-28299 P40523 EBI-20589,EBI-25031 P38254 EBI-20589,EBI-21533 P36041 EBI-20589,EBI-26995 P38835 EBI-20589,EBI-24724 P27515 EBI-20589,EBI-20151 P43639 EBI-20589,EBI-9563 Q01080 EBI-20589,EBI-15741 Q12532 EBI-20589,EBI-33283 P53104 EBI-20589,EBI-2657 P38856 EBI-20589,EBI-24811 P26784 EBI-20589,EBI-14508 Q03768 EBI-20589,EBI-7618 P40054 EBI-20589,EBI-16961 P40214 EBI-20589,EBI-27290 P19880 EBI-20589,EBI-31265 P32608 EBI-20589,EBI-16322 P25333 EBI-20589,EBI-16492 P08518 EBI-20589,EBI-15767 Q08909 EBI-20589,EBI-36654 P36000 EBI-20589,EBI-2206 Q04740 EBI-20589,EBI-15658 P20604 EBI-20589,EBI-13707 Q07953 EBI-20589,EBI-27124 P40531 EBI-20589,EBI-25006 P25502 EBI-20589,EBI-14307 Q12100 EBI-20589,EBI-36072 P25344 EBI-20589,EBI-18305 Q12453 EBI-20589,EBI-31271 P05453 EBI-20589,EBI-6540 P26570 EBI-20589,EBI-13807 P38970 EBI-20589,EBI-8142 P18899 EBI-20589,EBI-6165 P53297 EBI-20589,EBI-12961 P24309 EBI-20589,EBI-5648 P07266 EBI-20589,EBI-11278 P37263 EBI-20589,EBI-21659 P53836 EBI-20589,EBI-28275 P0CX52 EBI-20589,EBI-5234556 P34761 EBI-20589,EBI-20537 P35193 EBI-20589,EBI-29291 Q05672 EBI-20589,EBI-36115 Q12527 EBI-20589,EBI-31977 Q12221 EBI-20589,EBI-37840 P53309 EBI-20589,EBI-23557 Q00916 EBI-20589,EBI-724 Q03373 EBI-20589,EBI-34019 Q04429 EBI-20589,EBI-37461 Q04226 EBI-20589,EBI-18884 Q03833 EBI-20589,EBI-35786 P38070 EBI-20589,EBI-9524 P32481 EBI-20589,EBI-8924 P26786 EBI-20589,EBI-16161 P53686 EBI-20589,EBI-2070504 P32494 EBI-20589,EBI-2192 Q06511 EBI-20589,EBI-34602 P22517 EBI-20589,EBI-9600 P40466 EBI-20589,EBI-6965 Q3E7Y3 EBI-20589,EBI-783138 Q06512 EBI-20589,EBI-36459 P40992 EBI-20589,EBI-15990 P32491 EBI-20589,EBI-10973 P40210 EBI-20589,EBI-27280 P36123 EBI-20589,EBI-16392 Q00776 EBI-20589,EBI-2624 P53040 EBI-20589,EBI-18876 Q02931 EBI-20589,EBI-37773 P40160 EBI-20589,EBI-29124 P47049 EBI-20589,EBI-25866 P40357 EBI-20589,EBI-16904 P38333 EBI-20589,EBI-6482 P38961 EBI-20589,EBI-22139 P38861 EBI-20589,EBI-12077 P53972 EBI-20589,EBI-2883451 P53289 EBI-20589,EBI-23393 Q02197 EBI-20589,EBI-10924 P47019 EBI-20589,EBI-26061 P10664 EBI-20589,EBI-15390 Q07622 EBI-20589,EBI-38674 P40356 EBI-20589,EBI-13268 P53865 EBI-20589,EBI-29172 P53930 EBI-20589,EBI-28841 P35181 EBI-20589,EBI-2612 P38011 EBI-20589,EBI-7405 P53237 EBI-20589,EBI-23176 P53201 EBI-20589,EBI-23061 P20424 EBI-20589,EBI-17997 Q08972 EBI-20589,EBI-32014 P32524 EBI-20589,EBI-603 P29453 EBI-20589,EBI-15435 P48164 EBI-20589,EBI-16166 P47129 EBI-20589,EBI-25556 P06634 EBI-20589,EBI-5744 P32793 EBI-20589,EBI-24460 Q05775 EBI-20589,EBI-8944 Q04839 EBI-20589,EBI-27549 Q05518 EBI-20589,EBI-33452 Q04199 EBI-20589,EBI-3920 Q06412 EBI-20589,EBI-37117 Q03900 EBI-20589,EBI-38156 P39939 EBI-20589,EBI-14584 P39927 EBI-20589,EBI-23382 P42944 EBI-20589,EBI-8042 P38809 EBI-20589,EBI-24634 P39985 EBI-20589,EBI-6120 P20459 EBI-20589,EBI-8915 Q04305 EBI-20589,EBI-28183 Q08687 EBI-20589,EBI-34720 P27999 EBI-20589,EBI-15798 Q12102 EBI-20589,EBI-31412 P38882 EBI-20589,EBI-24892 P32913 EBI-20589,EBI-20366 Q06834 EBI-20589,EBI-33224 P38177 EBI-20589,EBI-21323 P32914 EBI-20589,EBI-17928 Q02796 EBI-20589,EBI-30514 P53272 EBI-20589,EBI-23284 P53091 EBI-20589,EBI-10556 P34758 EBI-20589,EBI-16685 Q12432 EBI-20589,EBI-6281 P33322 EBI-20589,EBI-4105 P43615 EBI-20589,EBI-23028 P47160 EBI-20589,EBI-25662 P38874 EBI-20589,EBI-9061 Q06410 EBI-20589,EBI-30856 P38817 EBI-20589,EBI-7569 P53136 EBI-20589,EBI-23920 P38789 EBI-20589,EBI-18160 P32328 EBI-20589,EBI-5588 P48415 EBI-20589,EBI-16551 P39108 EBI-20589,EBI-13183 P38282 EBI-20589,EBI-443 P32605 EBI-20589,EBI-680 P53094 EBI-20589,EBI-10651 P38687 EBI-20589,EBI-18004 P25343 EBI-20589,EBI-14490 Q02948 EBI-20589,EBI-2670 Q04868 EBI-20589,EBI-27653 Q12271 EBI-20589,EBI-36688 P15646 EBI-20589,EBI-6838 P38747 EBI-20589,EBI-3652313 P38630 EBI-20589,EBI-14985 P39517 EBI-20589,EBI-158 P05740 EBI-20589,EBI-14518 P54783 EBI-20589,EBI-2519 Q01919 EBI-20589,EBI-2610950 Q07655 EBI-20589,EBI-31312 P25367 EBI-20589,EBI-21708 Q08921 EBI-20589,EBI-37395 Q06436 EBI-20589,EBI-30241 P12904 EBI-20589,EBI-17537 P25567 EBI-20589,EBI-18084 Q03503 EBI-20589,EBI-10388 P20134 EBI-20589,EBI-17027 P38700 EBI-20589,EBI-2705 P36024 EBI-20589,EBI-17250 P12962 EBI-20589,EBI-9010 Q12194 EBI-20589,EBI-29434 P38990 EBI-20589,EBI-12863 P05756 EBI-20589,EBI-16054 Q12347 EBI-20589,EBI-30029 P25586 EBI-20589,EBI-21773 Q04067 EBI-20589,EBI-8958 Q03508 EBI-20589,EBI-27589 P40208 EBI-20589,EBI-27276 P39008 EBI-20589,EBI-13629 P38262 EBI-20589,EBI-17136 P32829 EBI-20589,EBI-11255 P53628 EBI-20589,EBI-17564 P53583 EBI-20589,EBI-11174 P40991 EBI-20589,EBI-12110 P53965 EBI-20589,EBI-28668 P39730 EBI-20589,EBI-8936 Q12428 EBI-20589,EBI-29344 Q12406 EBI-20589,EBI-2962 Q12502 EBI-20589,EBI-2113927 P40484 EBI-20589,EBI-11119 P36157 EBI-20589,EBI-26503 Q12024 EBI-20589,EBI-29589 Q00381 EBI-20589,EBI-2608 Q06108 EBI-20589,EBI-38709 P32342 EBI-20589,EBI-17984 P40099 EBI-20589,EBI-2059710 Q02939 EBI-20589,EBI-2345544 Q03497 EBI-20589,EBI-18285 P32607 EBI-20589,EBI-16312 P39016 EBI-20589,EBI-2052996 P04147 EBI-20589,EBI-12823 P32567 EBI-20589,EBI-17478 P36083 EBI-20589,EBI-26750 P32502 EBI-20589,EBI-6260 Q03208 EBI-20589,EBI-27965 Q12071 EBI-20589,EBI-36751 P07347 EBI-20589,EBI-2796 P40457 EBI-20589,EBI-25261 P53215 EBI-20589,EBI-23112 P32590 EBI-20589,EBI-8655 Q3E757 EBI-20589,EBI-783263 P38236 EBI-20589,EBI-11619 P40547 EBI-20589,EBI-24957 Q07084 EBI-20589,EBI-18184 P38682 EBI-20589,EBI-7679 P36103 EBI-20589,EBI-26614 P38151 EBI-20589,EBI-12968 P40017 EBI-20589,EBI-2345299 P16522 EBI-20589,EBI-4216 P26783 EBI-20589,EBI-16150 Q03776 EBI-20589,EBI-802 Q05543 EBI-20589,EBI-35018 P11746 EBI-20589,EBI-10528 P53734 EBI-20589,EBI-5625 Q12515 EBI-20589,EBI-38409 P15625 EBI-20589,EBI-18678 Q03088 EBI-20589,EBI-36005 Q04600 EBI-20589,EBI-38802 P38691 EBI-20589,EBI-9937 P47168 EBI-20589,EBI-25698 P50091 EBI-20589,EBI-23549 P53036 EBI-20589,EBI-16467 P05738 EBI-20589,EBI-15439 Q08096 EBI-20589,EBI-14892 P38112 EBI-20589,EBI-10394 P20433 EBI-20589,EBI-15777 P29468 EBI-20589,EBI-12917 Q99314 EBI-20589,EBI-31212 P42846 EBI-20589,EBI-28360 P43586 EBI-20589,EBI-22906 P28263 EBI-20589,EBI-19755 Q12417 EBI-20589,EBI-710 Q06671 EBI-20589,EBI-3685534 P15790 EBI-20589,EBI-9533 Q12099 EBI-20589,EBI-6776 P40007 EBI-20589,EBI-22439 O13516 EBI-20589,EBI-16176 P47122 EBI-20589,EBI-25534 P53327 EBI-20589,EBI-23623 P39936 EBI-20589,EBI-9006 Q07915 EBI-20589,EBI-35766 P53165 EBI-20589,EBI-23812 P38272 EBI-20589,EBI-21600 Q04461 EBI-20589,EBI-27209 Q08287 EBI-20589,EBI-12135 P52920 EBI-20589,EBI-11880 Q06709 EBI-20589,EBI-35391 Q02326 EBI-20589,EBI-15403 P32351 EBI-20589,EBI-9250 P47006 EBI-20589,EBI-26109 P18888 EBI-20589,EBI-17550 Q04934 EBI-20589,EBI-35255 P39516 EBI-20589,EBI-14464 Q12380 EBI-20589,EBI-2664 P40963 EBI-20589,EBI-16476 P15807 EBI-20589,EBI-10770 Q12454 EBI-20589,EBI-34560 Q00723 EBI-20589,EBI-841 P18961 EBI-20589,EBI-29484 Q12368 EBI-20589,EBI-252 P42223 EBI-20589,EBI-16498 P50111 EBI-20589,EBI-29626 Q05468 EBI-20589,EBI-32961 P22209 EBI-20589,EBI-9730 P38873 EBI-20589,EBI-24864 P36053 EBI-20589,EBI-26919 P38719 EBI-20589,EBI-5633 P32591 EBI-20589,EBI-18622 P38431 EBI-20589,EBI-9038 P39998 EBI-20589,EBI-22300 P14904 EBI-20589,EBI-2571 P19454 EBI-20589,EBI-9548 P32899 EBI-20589,EBI-9237 P11433 EBI-20589,EBI-4220 Q02864 EBI-20589,EBI-38920 P40070 EBI-20589,EBI-188 P53952 EBI-20589,EBI-2102292 P16370 EBI-20589,EBI-15773 Q02892 EBI-20589,EBI-12105 Q08689 EBI-20589,EBI-34404 P39955 EBI-20589,EBI-16463 P41903 EBI-20589,EBI-14154 P38315 EBI-20589,EBI-20985 P39015 EBI-20589,EBI-11238 P38041 EBI-20589,EBI-3719 P45976 EBI-20589,EBI-6940 P32497 EBI-20589,EBI-8965 P37304 EBI-20589,EBI-12870 P43597 EBI-20589,EBI-22951 Q12191 EBI-20589,EBI-32271 P38759 EBI-20589,EBI-13092 P53883 EBI-20589,EBI-29032 Q06706 EBI-20589,EBI-9068 P38712 EBI-20589,EBI-16007 P32495 EBI-20589,EBI-12014 Q03656 EBI-20589,EBI-9800 P38230 EBI-20589,EBI-3774859 P53316 EBI-20589,EBI-23586 P25390 EBI-20589,EBI-18129 Q03862 EBI-20589,EBI-31385 P25555 EBI-20589,EBI-7410 P0CX73 EBI-20589,EBI-11611501 P40453 EBI-20589,EBI-19857 P34253 EBI-20589,EBI-9950 P24784 EBI-20589,EBI-5596 P39525 EBI-20589,EBI-4467 P34239 EBI-20589,EBI-26951 P38200 EBI-20589,EBI-21213 Q12124 EBI-20589,EBI-37542 P53199 EBI-20589,EBI-6514 P47108 EBI-20589,EBI-25492 P47148 EBI-20589,EBI-25619 P05748 EBI-20589,EBI-14480 P12945 EBI-20589,EBI-11868 Q12163 EBI-20589,EBI-34713 P53063 EBI-20589,EBI-24206 Q08208 EBI-20589,EBI-35895 Q05949 EBI-20589,EBI-30948 Q03760 EBI-20589,EBI-27933 P36146 EBI-20589,EBI-10053 Q08732 EBI-20589,EBI-37488 Q07872 EBI-20589,EBI-38931 P35182 EBI-20589,EBI-12784 P25617 EBI-20589,EBI-375711 P35178 EBI-20589,EBI-16002 Q06078 EBI-20589,EBI-359 Q04418 EBI-20589,EBI-38743 Q04003 EBI-20589,EBI-38500 P32909 EBI-20589,EBI-17503 P23561 EBI-20589,EBI-18259 P15274 EBI-20589,EBI-2548 P53131 EBI-20589,EBI-505 P49704 EBI-20589,EBI-347 Q06315 EBI-20589,EBI-34508 P18494 EBI-20589,EBI-7657 P20447 EBI-20589,EBI-5608 P53145 EBI-20589,EBI-23885 Q04347 EBI-20589,EBI-28028 P25294 EBI-20589,EBI-17244 P40561 EBI-20589,EBI-25362 Q00816 EBI-20589,EBI-8270 Q03532 EBI-20589,EBI-8170 P43573 EBI-20589,EBI-22787 P25339 EBI-20589,EBI-23703 P39702 EBI-20589,EBI-20488 P50946 EBI-20589,EBI-28814 P48412 EBI-20589,EBI-20117 P21374 EBI-20589,EBI-9382 P38779 EBI-20589,EBI-24538 P03871 EBI-20589,EBI-14929 Q02554 EBI-20589,EBI-654 Q12460 EBI-20589,EBI-17148 P50109 EBI-20589,EBI-14050 P34241 EBI-20589,EBI-26595 P53892 EBI-20589,EBI-28987 P53914 EBI-20589,EBI-28914 P43572 EBI-20589,EBI-22792 Q12476 EBI-20589,EBI-31475 P48234 EBI-20589,EBI-23354 P38321 EBI-20589,EBI-21008 P53137 EBI-20589,EBI-23916 Q12378 EBI-20589,EBI-31807 P40956 EBI-20589,EBI-7968 Q04673 EBI-20589,EBI-18198 P40482 EBI-20589,EBI-16592 Q03758 EBI-20589,EBI-27941 P38823 EBI-20589,EBI-24686 P40559 EBI-20589,EBI-24915 Q07896 EBI-20589,EBI-36093 Q06211 EBI-20589,EBI-38894 P51534 EBI-20589,EBI-17086 P13186 EBI-20589,EBI-9723 P38281 EBI-20589,EBI-20838 P15303 EBI-20589,EBI-16584 Q08226 EBI-20589,EBI-30025 P12688 EBI-20589,EBI-29473 P36160 EBI-20589,EBI-15881 P32336 EBI-20589,EBI-12361 Q12060 EBI-20589,EBI-8287 P38697 EBI-20589,EBI-9186 Q06344 EBI-20589,EBI-34121 P32598 EBI-20589,EBI-13715 P29366 EBI-20589,EBI-3508 P34087 EBI-20589,EBI-15790 P38344 EBI-20589,EBI-21136 Q08649 EBI-20589,EBI-6648 Q04408 EBI-20589,EBI-36603 Q07381 EBI-20589,EBI-35023 P09064 EBI-20589,EBI-8920 P16892 EBI-20589,EBI-7193 P43612 EBI-20589,EBI-16370 P06103 EBI-20589,EBI-8973 P53251 EBI-20589,EBI-23221 P14126 EBI-20589,EBI-15364 Q04739 EBI-20589,EBI-7244 Q12343 EBI-20589,EBI-31503 P47170 EBI-20589,EBI-25710 P15624 EBI-20589,EBI-18684 P47050 EBI-20589,EBI-25861 Q08886 EBI-20589,EBI-3655948 P51862 EBI-20589,EBI-15702 P53941 EBI-20589,EBI-9243 P54113 EBI-20589,EBI-14213 Q12517 EBI-20589,EBI-38519 P30665 EBI-20589,EBI-4326 Q03785 EBI-20589,EBI-35568 P11745 EBI-20589,EBI-15648 P38249 EBI-20589,EBI-8981 P53855 EBI-20589,EBI-29212 P32786 EBI-20589,EBI-15986 P53604 EBI-20589,EBI-2086543 Q06628 EBI-20589,EBI-36188 Q08237 EBI-20589,EBI-30507 P39717 EBI-20589,EBI-20711 P53942 EBI-20589,EBI-15663 Q06218 EBI-20589,EBI-5640 P53893 EBI-20589,EBI-28980 Q12028 EBI-20589,EBI-33025 Q12321 EBI-20589,EBI-32854 P40217 EBI-20589,EBI-8951 Q07834 EBI-20589,EBI-36507 Q01477 EBI-20589,EBI-19834 Q03780 EBI-20589,EBI-30094 Q06632 EBI-20589,EBI-32872 Q02336 EBI-20589,EBI-2186 P38165 EBI-20589,EBI-16328 P47116 EBI-20589,EBI-2613227 P38696 EBI-20589,EBI-2920 P53949 EBI-20589,EBI-28725 P38180 EBI-20589,EBI-21315 Q04712 EBI-20589,EBI-27790 P39731 EBI-20589,EBI-11606 P53270 EBI-20589,EBI-23280 P08018 EBI-20589,EBI-12972 Q03769 EBI-20589,EBI-2055743 P40091 EBI-20589,EBI-13106 P37838 EBI-20589,EBI-12122 Q03735 EBI-20589,EBI-27955 P29055 EBI-20589,EBI-19123 P38065 EBI-20589,EBI-2181 P32047 EBI-20589,EBI-2611643 P42841 EBI-20589,EBI-28378 P53953 EBI-20589,EBI-17006 P27476 EBI-20589,EBI-12274 Q06132 EBI-20589,EBI-34377 P21373 EBI-20589,EBI-20174 Q03338 EBI-20589,EBI-421 P27692 EBI-20589,EBI-17937 P40693 EBI-20589,EBI-15415 P43603 EBI-20589,EBI-22980 P09734 EBI-20589,EBI-18981 Q07913 EBI-20589,EBI-30144 P06784 EBI-20589,EBI-18389 P38129 EBI-20589,EBI-18868 P53873 EBI-20589,EBI-29071 Q12159 EBI-20589,EBI-29516 P47048 EBI-20589,EBI-25870 Q02256 EBI-20589,EBI-14322 P38798 EBI-20589,EBI-12071 P25366 EBI-20589,EBI-22021 Q12522 EBI-20589,EBI-9046 Q12176 EBI-20589,EBI-10944 Q00539 EBI-20589,EBI-11835 Q12136 EBI-20589,EBI-36084 P46990 EBI-20589,EBI-14522 P40856 EBI-20589,EBI-16384 P38930 EBI-20589,EBI-9578 P04840 EBI-20589,EBI-13686 P14741 EBI-20589,EBI-6253 Q04410 EBI-20589,EBI-32083 P32523 EBI-20589,EBI-493 Q12504 EBI-20589,EBI-30749 P29295 EBI-20589,EBI-8536 P53742 EBI-20589,EBI-28532 P38701 EBI-20589,EBI-16081 Q02959 EBI-20589,EBI-8484 Q12523 EBI-20589,EBI-37062 P40535 EBI-20589,EBI-2052 P34167 EBI-20589,EBI-9025 Q02793 EBI-20589,EBI-17260 P36076 EBI-20589,EBI-26778 Q07825 EBI-20589,EBI-32387 P53088 EBI-20589,EBI-24137 P45978 EBI-20589,EBI-16691 Q12094 EBI-20589,EBI-29255 Q12421 EBI-20589,EBI-34768 P06843 EBI-20589,EBI-17914 P38738 EBI-20589,EBI-24355 P33400 EBI-20589,EBI-14422 P46675 EBI-20589,EBI-18471 Q07532 EBI-20589,EBI-33428 Q08726 EBI-20589,EBI-37977 Q08217 EBI-20589,EBI-9839 P25635 EBI-20589,EBI-14332 P33442 EBI-20589,EBI-16132 P38251 EBI-20589,EBI-15016 P05750 EBI-20589,EBI-16140 Q06205 EBI-20589,EBI-6956 P04803 EBI-20589,EBI-18837 P53238 EBI-20589,EBI-23185 Q07844 EBI-20589,EBI-27142 P39682 EBI-20589,EBI-612 P39744 EBI-20589,EBI-29259 P33201 EBI-20589,EBI-26590 P39969 EBI-20589,EBI-3727 Q06337 EBI-20589,EBI-35867 P14680 EBI-20589,EBI-20777 P38061 EBI-20589,EBI-15346 Q04511 EBI-20589,EBI-20020 Q12216 EBI-20589,EBI-11987 Q07821 EBI-20589,EBI-27136 P38213 EBI-20589,EBI-21385 P46682 EBI-20589,EBI-2213 P38153 EBI-20589,EBI-2710 Q12092 EBI-20589,EBI-38752 P39729 EBI-20589,EBI-20651 P41819 EBI-20589,EBI-5884 P42935 EBI-20589,EBI-23459 P47089 EBI-20589,EBI-5751 P38805 EBI-20589,EBI-24614 Q07533 EBI-20589,EBI-31510 P49960 EBI-20589,EBI-212 P42843 EBI-20589,EBI-28370 P0CX83 EBI-20589,EBI-7433003 P0CX36 EBI-20589,EBI-7433300 P0CX54 EBI-20589,EBI-7432640 P0CX38 EBI-20589,EBI-7432889 P0CX48 EBI-20589,EBI-7433392 P0CX46 EBI-20589,EBI-7433130 Q05937 EBI-20589,EBI-7766412 P0CX56 EBI-20589,EBI-7433160 P0CX32 EBI-20589,EBI-7432762 P0CX40 EBI-20589,EBI-7432610 Q06543 EBI-20589,EBI-33132 P40059 EBI-20589,EBI-6062 Q12049 EBI-20589,EBI-34263 Q12129 EBI-20589,EBI-30663 Q06188 EBI-20589,EBI-35613 P38985 EBI-20589,EBI-17977 Q12291 EBI-20589,EBI-31876 P27351 EBI-20589,EBI-2202 P38042 EBI-20589,EBI-4249 P04449 EBI-20589,EBI-14560 P38629 EBI-20589,EBI-15000 P30619 EBI-20589,EBI-16833 P23201 EBI-20589,EBI-17803 Q12224 EBI-20589,EBI-15468 P26785 EBI-20589,EBI-14513 Q12196 EBI-20589,EBI-15224 P47064 EBI-20589,EBI-2619 P12754 EBI-20589,EBI-6265 P40079 EBI-20589,EBI-10103 P50278 EBI-20589,EBI-17675 P32525 EBI-20589,EBI-26215 Q02908 EBI-20589,EBI-33957 Q06604 EBI-20589,EBI-37047 Q07418 EBI-20589,EBI-292 P27636 EBI-20589,EBI-4200 P20448 EBI-20589,EBI-5612 P40157 EBI-20589,EBI-29136 Q12090 EBI-20589,EBI-2083048 P23292 EBI-20589,EBI-4729 P47130 EBI-20589,EBI-763 Q99369 EBI-20589,EBI-3826891 P40021 EBI-20589,EBI-22484 P38089 EBI-20589,EBI-12814 P40013 EBI-20589,EBI-3614 P21304 EBI-20589,EBI-14328 P25042 EBI-20589,EBI-15714 P20434 EBI-20589,EBI-15781 P39743 EBI-20589,EBI-14500 Q03466 EBI-20589,EBI-31765 Q04377 EBI-20589,EBI-35652 Q05123 EBI-20589,EBI-2972 Q04372 EBI-20589,EBI-18926 P50094 EBI-20589,EBI-9195 P53901 EBI-20589,EBI-28955 P25559 EBI-20589,EBI-5661 P36049 EBI-20589,EBI-6289 Q07350 EBI-20589,EBI-688 P40335 EBI-20589,EBI-20373 Q12034 EBI-20589,EBI-17335 P15442 EBI-20589,EBI-330 Q3E705 EBI-20589,EBI-3666578 P34164 EBI-20589,EBI-17187 P29478 EBI-20589,EBI-16641 Q99216 EBI-20589,EBI-31176 P34072 EBI-20589,EBI-10978 Q02805 EBI-20589,EBI-15679 P23248 EBI-20589,EBI-16136 Q08444 EBI-20589,EBI-29777 P54000 EBI-20589,EBI-18492 Q02884 EBI-20589,EBI-35277 P10962 EBI-20589,EBI-10937 P49955 EBI-20589,EBI-664 Q08484 EBI-20589,EBI-8005 P47135 EBI-20589,EBI-9422 P53050 EBI-20589,EBI-10850 Q99186 EBI-20589,EBI-2715 P34110 EBI-20589,EBI-20415 Q08235 EBI-20589,EBI-3775 P40187 EBI-20589,EBI-13419 P07270 EBI-20589,EBI-13378 P32566 EBI-20589,EBI-17452 P46946 EBI-20589,EBI-16440 Q12481 EBI-20589,EBI-31770 Q04007 EBI-20589,EBI-35560 P48562 EBI-20589,EBI-4750 P25293 EBI-20589,EBI-11850 P32790 EBI-20589,EBI-17313 P50896 EBI-20589,EBI-14046 P80235 EBI-20589,EBI-3928 Q04304 EBI-20589,EBI-28179 P43563 EBI-20589,EBI-11125 P34243 EBI-20589,EBI-26601 Q02354 EBI-20589,EBI-22119 P53829 EBI-20589,EBI-28306 P53741 EBI-20589,EBI-28528 P39715 EBI-20589,EBI-6302 Q02875 EBI-20589,EBI-33176 Q03330 EBI-20589,EBI-7458 P17536 EBI-20589,EBI-19408 P38080 EBI-20589,EBI-9528 Q12213 EBI-20589,EBI-15427 Q12186 EBI-20589,EBI-34012 P53924 EBI-20589,EBI-28867 P39960 EBI-20589,EBI-3517 P47077 EBI-20589,EBI-25778 Q07807 EBI-20589,EBI-38012 P19524 EBI-20589,EBI-11659 P53894 EBI-20589,EBI-4110 P06844 EBI-20589,EBI-17921 P40084 EBI-20589,EBI-22713 P20053 EBI-20589,EBI-219 Q03233 EBI-20589,EBI-27402 P51401 EBI-20589,EBI-15443 P32794 EBI-20589,EBI-2310 Q12259 EBI-20589,EBI-30776 P22204 EBI-20589,EBI-5569 P53743 EBI-20589,EBI-28537 Q08951 EBI-20589,EBI-29702 P09959 EBI-20589,EBI-18641 Q12753 EBI-20589,EBI-8118 P36124 EBI-20589,EBI-16993 P25644 EBI-20589,EBI-204 P40339 EBI-20589,EBI-15009 P36115 EBI-20589,EBI-27090 Q08438 EBI-20589,EBI-30482 P38688 EBI-20589,EBI-18011 Q07362 EBI-20589,EBI-37896 P50079 EBI-20589,EBI-23505 P36119 EBI-20589,EBI-26366 P46654 EBI-20589,EBI-16037 P09547 EBI-20589,EBI-18617 P40449 EBI-20589,EBI-25311 P38263 EBI-20589,EBI-20304 P17076 EBI-20589,EBI-15431 P13663 EBI-5803,EBI-20589 P28496 EBI-26585,EBI-20589 P36013 EBI-10412,EBI-20589 P38085 EBI-20222,EBI-20589 P21147 EBI-2098,EBI-20589 Q07804 EBI-36254,EBI-20589 P33417 EBI-9401,EBI-20589 P38707 EBI-18775,EBI-20589 P38703 EBI-10035,EBI-20589 P0CI39 EBI-18360,EBI-20589 P52593 EBI-11763,EBI-20589 Q03529 EBI-16747,EBI-20589 P02994 EBI-20589,EBI-6314 P10659 EBI-20589,EBI-10789 Q01939 EBI-20589,EBI-13914 P33299 EBI-20589,EBI-13910 P41940 EBI-20589,EBI-11191 P40495 EBI-20589,EBI-25128 P15108 EBI-20589,EBI-8666 P33892 EBI-20589,EBI-7442 P00549 EBI-20589,EBI-9890 P16140 EBI-20589,EBI-20254 P07259 EBI-20589,EBI-14372 P02557 EBI-20589,EBI-18986 P09733 EBI-20589,EBI-18976 P10081 EBI-20589,EBI-9017 P32454 EBI-2641,EBI-20589 P40970 EBI-10067,EBI-20589 P38737 EBI-24359,EBI-20589 Q00955 EBI-4814,EBI-20589 P39722 EBI-20685,EBI-20589 P18239 EBI-2293,EBI-20589 P60010 EBI-2169,EBI-20589 GO:0005737 GO:0000776 GO:0005634 GO:0048471 GO:0005816 GO:0005049 GO:0061608 GO:0008536 GO:0006406 GO:0006611 GO:0034501 GO:0046825 GO:0000055 GO:0000056 MEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFSTNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKSDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAKALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELLSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLKATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELFKTTLDYWHNLVADLFYEVQRLPATEMSPLIQLSVGSQAISTGSGALNPEYMKRFPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENALMEQNRLEREKAAKIGGLLKPSELDD 1084 P31689 DnaJ homolog subfamily A member 1 DNAJA1 9606 Yes SL-0198 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}. UNIPROT P31689 UNIPROT Q5T7Q0 UNIPROT Q86TL9 PDB 2LO1 PDB 2M6Y PDB 6E8M Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 OMIM 602837 DisGeNET 3301 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}. A0A142I5B9 EBI-20625235,EBI-347834 O43542 EBI-2849976,EBI-347834 O95831 EBI-356440,EBI-347834 P00533 EBI-297353,EBI-347834 P04626 EBI-641062,EBI-347834 P05129 EBI-949799,EBI-347834 P13569 EBI-349854,EBI-347834 Q9H9G7 EBI-2267883,EBI-347834 Q9HCK5 EBI-2269696,EBI-347834 Q5S007 EBI-5323863,EBI-347834 P09622 EBI-353366,EBI-347834 P08559 EBI-715747,EBI-347834 O00429 EBI-724571,EBI-347834 Q6ZNJ1 EBI-2862306,EBI-347834 Q15077 EBI-10235794,EBI-347834 P03427 EBI-8430745,EBI-347834 Q9Y251 EBI-5453868,EBI-347834 Q9HC29 EBI-7445625,EBI-347834 Q8WW22 EBI-2555157,EBI-347834 Q96BE0 EBI-9356686,EBI-347834 Q9Y266 EBI-357298,EBI-347834 P21860 EBI-720706,EBI-347834 Q13043 EBI-367376,EBI-347834 Q16659 EBI-1384105,EBI-347834 P57078 EBI-4422308,EBI-347834 Q92769 EBI-301821,EBI-347834 Q9UBN7 EBI-301697,EBI-347834 Q969S8 EBI-301762,EBI-347834 Q96DB2 EBI-301713,EBI-347834 Q9H492 EBI-720768,EBI-347834 O95166 EBI-712001,EBI-347834 P60520 EBI-720116,EBI-347834 P05213 EBI-347834,EBI-2311600 P99024 EBI-350896,EBI-347834 Q9Z1B5 EBI-2552918,EBI-347834 P83887 EBI-2553410,EBI-347834 P68372 EBI-2553564,EBI-347834 P05214 EBI-10963854,EBI-347834 O75665 EBI-716327,EBI-347834 Q15468 EBI-7488405,EBI-347834 P35550 EBI-7817407,EBI-347834 Q6ZMQ8 EBI-2008380,EBI-347834 P10398 EBI-365961,EBI-347834 Q13418 EBI-747644,EBI-347834 P51617 EBI-358664,EBI-347834 P53671 EBI-1384350,EBI-347834 P04049 EBI-365996,EBI-347834 Q96FW1 EBI-1058491,EBI-347834 P03372 EBI-78473,EBI-347834 Q9BQE3 EBI-1103245,EBI-347834 Q71U36 EBI-302552,EBI-347834 Q9H9B4 EBI-355861,EBI-347834 Q14684 EBI-372051,EBI-347834 Q15051 EBI-2805823,EBI-347834 P07900 EBI-296047,EBI-347834 P0DOE9 EBI-6138585,EBI-347834 Q8JPQ9 EBI-6152703,EBI-347834 Q13617 EBI-456179,EBI-347834 Q13620 EBI-456067,EBI-347834 Q13616 EBI-359390,EBI-347834 Q93034 EBI-1057139,EBI-347834 Q92905 EBI-594661,EBI-347834 Q13618 EBI-456129,EBI-347834 Q77M19 EBI-6149376,EBI-347834 P15822 EBI-722264,EBI-347834 Q13042 EBI-347834,EBI-994830 Q9Y2Q3 EBI-347834,EBI-1053767 O00422 EBI-347834,EBI-1044156 P01889 EBI-347834,EBI-1046513 P31930 EBI-347834,EBI-1052596 Q92956 EBI-347834,EBI-1056653 O75365 EBI-347834,EBI-1043866 Q9NPF4 EBI-347834,EBI-1056510 Q8IXH7 EBI-347834,EBI-536725 P49703 EBI-347834,EBI-711726 P19256 EBI-347834,EBI-718785 P30408 EBI-347834,EBI-714256 Q9UM11 EBI-347834,EBI-724997 Q16526 EBI-741297,EBI-347834 P30530 EBI-2850927,EBI-347834 P61586 EBI-446668,EBI-347834 P06239 EBI-1348,EBI-347834 P41743 EBI-286199,EBI-347834 Q05513 EBI-295351,EBI-347834 P36507 EBI-1056930,EBI-347834 Q9H1R3 EBI-356910,EBI-347834 Q13882 EBI-1383632,EBI-347834 P15498 EBI-625518,EBI-347834 O15524 EBI-968198,EBI-347834 Q13163 EBI-307294,EBI-347834 Q13164 EBI-1213983,EBI-347834 P19419 EBI-726632,EBI-347834 Q13153 EBI-1307,EBI-347834 P41240 EBI-1380630,EBI-347834 P46734 EBI-602462,EBI-347834 Q02156 EBI-706254,EBI-347834 P83110-1 EBI-25469082,EBI-347834 P0DTD1 EBI-25475871,EBI-347834 P0DTC5 EBI-25475853,EBI-347834 P0DTC3 EBI-25475894,EBI-347834 P0DTD8 EBI-25475914,EBI-347834 P0DTC8 EBI-25475900,EBI-347834 Q7Z6J6 EBI-727282,EBI-347834 Q15334 EBI-299979,EBI-347834 P35240 EBI-1014472,EBI-347834 Q13509 EBI-350989,EBI-347834 Q14CZ7 EBI-10234819,EBI-347834 Q92834 EBI-6558417,EBI-347834 Q9C0F1 EBI-744115,EBI-347834 Q9NXB0 EBI-719269,EBI-347834 O14829 EBI-2931238,EBI-347834 Q9Y2T4-3 EBI-14013186,EBI-347834 Q6IQ23 EBI-2125301,EBI-347834 Q8IVT5 EBI-486984,EBI-347834 Q9BXB4 EBI-347834,EBI-2514786 Q96SU4-2 EBI-347834,EBI-12519654 Q14249 EBI-347834,EBI-9369928 O95714 EBI-347834,EBI-1058922 A0JLT2 EBI-394430,EBI-347834 Q9NX70 EBI-394656,EBI-347834 Q04206-2 EBI-347834,EBI-289947 Q13546 EBI-347834,EBI-358507 Q9Y572 EBI-347834,EBI-298250 Q15750 EBI-347834,EBI-358643 Q9NYJ8 EBI-347834,EBI-358708 O43318-2 EBI-347834,EBI-358700 P19438 EBI-347834,EBI-299451 P20333 EBI-347834,EBI-358983 Q13233 EBI-347834,EBI-49776 Q99759 EBI-347834,EBI-307281 Q00653 EBI-347834,EBI-307326 Q99558 EBI-347834,EBI-358011 Q15628 EBI-347834,EBI-359215 Q13077 EBI-347834,EBI-359224 Q12933 EBI-347834,EBI-355744 Q9Y4K3 EBI-347834,EBI-359276 Q9Y333 EBI-347834,EBI-347416 GO:0098554 GO:0005829 GO:0070062 GO:0016020 GO:0015630 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0055131 GO:0051087 GO:0001664 GO:0030544 GO:0050750 GO:0046872 GO:0030957 GO:0031625 GO:0051082 GO:0043066 GO:1903748 GO:0043508 GO:1905259 GO:0031397 GO:0043065 GO:0006457 GO:0070585 GO:0051223 GO:0009408 GO:0006986 MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 P32336 Protein NUD1 NUD1 559292 Yes SL-0178 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. UNIPROT P32336 UNIPROT D6W366 UNIPROT Q08895 PROSITE PS51450 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}. P30822 EBI-20589,EBI-12361 Q12411 EBI-36275,EBI-12361 Q08550 EBI-34513,EBI-12361 Q00684 EBI-4192,EBI-12361 P14832 EBI-5463,EBI-12361 P53865 EBI-29172,EBI-12361 P32472 EBI-2883297,EBI-12361 Q02796 EBI-30514,EBI-12361 P38265 EBI-21579,EBI-12361 P38890 EBI-24263,EBI-12361 P39987 EBI-22339,EBI-12361 P10592 EBI-12361,EBI-8603 P11484 EBI-12361,EBI-8627 P25294 EBI-17244,EBI-12361 P39101 EBI-12361,EBI-3949 P10591 EBI-8591,EBI-12361 Q07457 EBI-31563,EBI-12361 P26448 EBI-3824,EBI-12361 P39723 EBI-20675,EBI-12361 Q04477 EBI-27228,EBI-12361 P32337 EBI-9159,EBI-12361 Q02159 EBI-12361,EBI-19749 GO:0005623 GO:0005737 GO:0005635 GO:0061499 GO:0043014 GO:0045504 GO:0003774 GO:0035591 GO:0030953 GO:0051301 GO:0051293 GO:0000073 GO:0045132 GO:0031536 MDMDTQEAELSSQLENLTINSPRKLRSNAHSNSGKVFKEYESNHDFQDSNFTSQVVEPAISDSVKKPPTMTVLNNYSTVHQKVPSGFSGTTATSHQEAQWKQYFPGIGSGGGTNFGGAVGTANKVPESDLIVSDLVKDLSGVLETNTFKRHLDMKNKTTTMQTHENHDTISISHSKDFFNAEKVSSSFSDDSDSGPAAEAHDVFDGILQKQKSNYLVGSYPSNSNNKNNNNNNNNNNNNSININNKDNARTKEEDEEDTSNSFEFSSSSSMSSSQTQSGRKSKVLKKPPLNTISPGQLGYQFNHTHGAWDPPLNQGLDVSSSHSLDNTSSNQSQFATMVPTGDNHTNGKAPSILDKKAYELTSTKPGDVGYRQKKIQEEENLANSDDTPLDTPKFNDLFTKNGTRAKVKGQMRTSRSISNSNLLEAHKKLKTFPAERVEDITSISEVNTSFNETEKQLISILTSKLSGSPSYDSDWEKILKVDLSRGKLKNMFGMQRLLPNVLVLNLSDNEMNTLEGIPSNVVQLFCSNNKITSAHCSLAGFHDLECLDLSYNLLNTSLKFLSLCHHLQEVNLSYNSIQSLEGIGSSRMKKLNLSNNEINGIIDFEQLILTNNSVVGGWLTVEVLDLSNNNIIGVRNINCLPRLKVLNLNGNPLVSIVESSKMENGTLRALSIKNTGGALSKLQNYKLDDQFTFPYQNLKILKLDGFAQLSKWQKWPATLQILEINGGLASSLPRFSSLKSTNLYSLTIANVRDFTHLPVDLSKELPFLQELHLPGNNLQNAHKLTKTLPRQSVKFLDLRNNPITTPRHDRASTSLHYRQLLQLAGLCQQQCPALATLWLDDTPAPTATNL 851 P32499 Nucleoporin NUP2 NUP2 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. UNIPROT P32499 UNIPROT D6VYX5 UNIPROT Q06130 PDB 1UN0 PDB 2C1T Pfam PF08911 Pfam PF00638 PROSITE PS50196 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}. Self EBI-12401,EBI-12401 Q06142 EBI-9145,EBI-12401 P39705 EBI-12401,EBI-20731 P46673 EBI-12401,EBI-12345 P38181 EBI-12401,EBI-11756 Q12306 EBI-17490,EBI-12401 P16474 EBI-7876,EBI-12401 P0CS90 EBI-8637,EBI-12401 Q12329 EBI-8571,EBI-12401 P11484 EBI-12401,EBI-8627 P40150 EBI-8632,EBI-12401 P10592 EBI-8603,EBI-12401 P33416 EBI-8680,EBI-12401 P38788 EBI-12401,EBI-24570 P09435 EBI-12401,EBI-8611 P32589 EBI-8648,EBI-12401 P15108 EBI-12401,EBI-8666 P40358 EBI-12401,EBI-25940 P39101 EBI-12401,EBI-3949 P10591 EBI-12401,EBI-8591 P50875 EBI-17751,EBI-12401 Q02821 EBI-1797,EBI-12401 P50102 EBI-19863,EBI-12401 P38129 EBI-18868,EBI-12401 P32835 EBI-12401,EBI-7926 P16140 EBI-12401,EBI-20254 P09734 EBI-12401,EBI-18981 P02557 EBI-12401,EBI-18986 P02994 EBI-12401,EBI-6314 P10659 EBI-12401,EBI-10789 P40069 EBI-12401,EBI-9166 P00549 EBI-12401,EBI-9890 P00830 EBI-12401,EBI-3242 P00330 EBI-12401,EBI-2218 P53833 EBI-13638,EBI-12401 P32799 EBI-5070,EBI-12401 P19414 EBI-2104,EBI-12401 P28003 EBI-20647,EBI-12401 Q02159 EBI-12401,EBI-19749 GO:0000781 GO:0005737 GO:0005739 GO:0042564 GO:0031965 GO:0005643 GO:0044614 GO:0044615 GO:0005634 GO:0061676 GO:0008536 GO:0017056 GO:0030466 GO:0035392 GO:0031990 GO:0006607 GO:0016973 GO:0043547 GO:0000973 GO:0006611 GO:0006606 GO:0036228 GO:0000972 MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK 720 P32500 Nucleoporin NDC1 NDC1 559292 Yes SL-0178 SL-0182 SL-0185 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. UNIPROT P32500 UNIPROT D6VZE3 Pfam PF09531 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}. Q07457 EBI-31563,EBI-11950 Q04477 EBI-27228,EBI-11950 Q12315 EBI-7635,EBI-11950 P49687 EBI-11730,EBI-11950 Q05166 EBI-11950,EBI-3035 Q03790 EBI-11950,EBI-27321 P16521 EBI-11950,EBI-6338 P38219 EBI-11950,EBI-21409 P16140 EBI-11950,EBI-20254 P02994 EBI-11950,EBI-6314 P00359 EBI-11950,EBI-7218 P46654 EBI-11950,EBI-16037 P06169 EBI-11950,EBI-5687 P14742 EBI-11950,EBI-7557 P00330 EBI-11950,EBI-2218 P38305 EBI-20939,EBI-11950 GO:0005623 GO:0005737 GO:0016021 GO:0005635 GO:0031965 GO:0005643 GO:0070762 GO:0005816 GO:0017056 GO:0071790 GO:0051028 GO:0006999 GO:0006913 GO:0015031 GO:0030474 MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVTRKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVTDADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFITFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGNTWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDESPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSDESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSICALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLANWFLEVYASGNPNAT 655 P32567 Phosphatidic acid phosphohydrolase 1 PAH1 559292 Yes SL-0178 SL-0182 Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. UNIPROT P32567 UNIPROT D6VZY7 Pfam PF04571 Pfam PF08235 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}. P30822 EBI-20589,EBI-17478 P10591 EBI-17478,EBI-8591 P40150 EBI-17478,EBI-8632 P11484 EBI-17478,EBI-8627 Q06677 EBI-30084,EBI-17478 P10592 EBI-17478,EBI-8603 P16140 EBI-17478,EBI-20254 P07259 EBI-17478,EBI-14372 P02557 EBI-17478,EBI-18986 P09733 EBI-17478,EBI-18976 P00549 EBI-17478,EBI-9890 GO:0005737 GO:0005829 GO:0005789 GO:0019898 GO:0005811 GO:0031965 GO:0005634 GO:0005773 GO:0008195 GO:0044212 GO:0009060 GO:0009062 GO:0034389 GO:0008654 GO:0006276 GO:0019432 GO:0042144 MQYVGRALGSVSKTWSSINPATLSGAIDVIVVEHPDGRLSCSPFHVRFGKFQILKPSQKKVQVFINEKLSNMPMKLSDSGEAYFVFEMGDQVTDVPDELLVSPVMSATSSPPQSPETSILEGGTEGEGEGENENKKKEKKVLEEPDFLDINDTGDSGSKNSETTGSLSPTESSTTTPPDSVEERKLVEQRTKNFQQKLNKKLTEIHIPSKLDNNGDLLLDTEGYKPNKNMMHDTDIQLKQLLKDEFGNDSDISSFIKEDKNGNIKIVNPYEHLTDLSPPGTPPTMATSGSVLGLDAMESGSTLNSLSSSPSGSDTEDETSFSKEQSSKSEKTSKKGTAGSGETEKRYIRTIRLTNDQLKCLNLTYGENDLKFSVDHGKAIVTSKLFVWRWDVPIVISDIDGTITKSDALGHVLAMIGKDWTHLGVAKLFSEISRNGYNILYLTARSAGQADSTRSYLRSIEQNGSKLPNGPVILSPDRTMAALRREVILKKPEVFKIACLNDIRSLYFEDSDNEVDTEEKSTPFFAGFGNRITDALSYRTVGIPSSRIFTINTEGEVHMELLELAGYRSSYIHINELVDHFFPPVSLDSVDLRTNTSMVPGSPPNRTLDNFDSEITSGRKTLFRGNQEEKFTDVNFWRDPLVDIDNLSDISNDDSDNIDEDTDVSQQSNISRNRANSVKTAKVTKAPQRNVSGSTNNNEVLAASSDVENASDLVSSHSSSGSTPNKSTMSKGDIGKQIYLELGSPLASPKLRYLDDMDDEDSNYNRTKSRRASSAAATSIDKEFKKLSVSKAGAPTRIVSKINVSNDVHSLGNSDTESRREQSVNETGRNQLPHNSMDDKDLDSRVSDEFDDDEFDEDEFED 862 P32767 Importin beta-like protein KAP122 KAP122 559292 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10617640}. UNIPROT P32767 UNIPROT D6VUC1 PDB 6Q82 PDB 6Q83 PDB 6Q84 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}. P25491 EBI-10420,EBI-13044 P16140 EBI-13044,EBI-20254 P07259 EBI-13044,EBI-14372 P09734 EBI-13044,EBI-18981 P02557 EBI-13044,EBI-18986 P02994 EBI-13044,EBI-6314 P11484 EBI-13044,EBI-8627 P10592 EBI-13044,EBI-8603 Q04062 EBI-13044,EBI-15944 P41940 EBI-13044,EBI-11191 P40495 EBI-13044,EBI-25128 P00549 EBI-13044,EBI-9890 P00830 EBI-13044,EBI-3242 P50085 EBI-23530,EBI-13044 Q00955 EBI-4814,EBI-13044 P39925 EBI-2317,EBI-13044 Q06625 EBI-37861,EBI-13044 GO:0005737 GO:0005635 GO:0005634 GO:0061608 GO:0006606 GO:0008361 MSSIHEVVALIEELYSPHPKHDVNQIQQSLQSIQKSEQGFHLANELLSDDKYSANVKYFGALTLTVQLNTRGENDYETLWNVFRSNLLYLTKFSTLYVSNPNMYGQSLIIIKKLMSNLSLIFTKINDPQLNNAGNENMIKQWNNPINTFIQLMSVQNQNINADQLLLDSINCSLTYEQLSQFVSLSQKHNELALTFTEVIVEDLTKFQTKRHSMSQIHEVVHEHLYISTMALINLNLTAQAVFNPTVFDCITAWINYISLTRSVSSSGRMDLSEIFQNLIDLMYQSTEGSDGYENAEKILTIFGNVFANDPLLMSYDLRQQIECIFLGVVRPDSGITDISNKNSWMLQYMNYLVTNDFFSELKELAICIVDFLQINTLSVCNKLFTNIQAADNGQVQDEYIQEYIKVLLQMTNFPLTPVLQEFFSVRMVDFWLDLSDAYTNLASETLRPNSIELSTQIFQQLINIYLPKISLSVKQRIIEEEGESTSVNEFEDFRNAVSDLAQSLWSILGNDNLTNVLIDGMGQMPAASDETLIIKDTDVLFRIETMCFVLNTILVDMTLSESPWIKNIVDANKFFNQNVISVFQTGFQTSASTKVSQILKLDFVRTSTTLIGTLAGYFKQEPFQLNPYVEALFQGLHTCTNFTSKNEQEKISNDKLEVMVIKTVSTLCETCREELTPYLMHFISFLNTVIMPDSNVSHFTRTKLVRSIGYVVQCQVSNGPEEQAKYILQLTNLLSGSIEHCLASSVQLQEQQDYINCLLYCISELATSLIQPTEIIENDALLQRLSEFQSFWSSDPLQIRSKIMCTIDKVLDNSIYCKNSAFVEIGCLIVGKGLNLPDGEPYFLKYNMSEVMNFVLRHVPNCELATCLPYFVYLLEKLISEFRKELTPQEFDFMFEKILLVYYDAYIINDPDLLQMTIGFVNNVLDVKPGLAIGSKHWTSFILPQFLKLIPSREKFTIVAVAKFWTKLINNKKYNQEELTTVRQQVSSIGGDLVYQIMYGLFHTQRSDLNSYTDLLRALVAKFPIEAREWLVAVLPQICNNPAGHEKFINKLLITRGSRAAGNVILQWWLDCTTLPNYQG 1081 P34077 Nucleoporin NIC96 NIC96 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P34077 UNIPROT D6VTN2 PDB 2QX5 PDB 2RFO Pfam PF04097 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}. P14907 EBI-12056,EBI-12265 Q02630 EBI-11703,EBI-12056 Q02629 EBI-11698,EBI-12056 P48837 EBI-12056,EBI-12324 P51998 EBI-12056,EBI-450 Q00684 EBI-4192,EBI-12056 P22696 EBI-6679,EBI-12056 P02293 EBI-8088,EBI-12056 P38265 EBI-21579,EBI-12056 P26448 EBI-3824,EBI-12056 P47054 EBI-12056,EBI-25846 Q03790 EBI-12056,EBI-27321 P52593 EBI-11763,EBI-12056 Q02199 EBI-12315,EBI-12056 P39723 EBI-20675,EBI-12056 Q04477 EBI-27228,EBI-12056 P46675 EBI-18471,EBI-12056 Q7Z3B4 EBI-741048,EBI-12056 Q05166 EBI-3035,EBI-12056 P53863 EBI-29183,EBI-12056 P07259 EBI-12056,EBI-14372 P10592 EBI-12056,EBI-8603 P40069 EBI-12056,EBI-9166 P40066 EBI-22648,EBI-12056 Q07953 EBI-27124,EBI-12056 P38305 EBI-20939,EBI-12056 Q12315 EBI-7635,EBI-12056 GO:0031965 GO:0005643 GO:0044612 GO:0044615 GO:0017056 GO:0006999 GO:0016973 GO:0006606 GO:0000055 MLETLRGNKLHSGTSKGANKKLNELLESSDNLPSASSELGSIQVSINELRRRVFQLRSKNKASKDYTKAHYLLANSGLSFEDVDAFIKDLQTNQFLEPNPPKIIESEELEFYIRTKKEENILMSIEQLLNGATKDFDNFINHNLNLDWAQHKNEVMKNFGILIQDKKTVDHKKSISSLDPKLPSWGNKGNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEFISILSSANGTRNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGLATNVNKIKSFIDTKLKKADKSWKISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKANIKKVEQSFLTYFKAYASSKDHGLPVEYSTKLHTEYNQHIKSSLDGDPYRLAVYKLIGRCDLSRKNIPAVTLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYYLQTLLLSGLYGLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANILANYTKSFRYSDPRVAVEYLVLITLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGARIPGVIEERQPLLHVRDEKEFLHTITEQAARRADEDGRIYDSILLYQLAEEYDIVITLVNSLLSDTLSASDLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLLNISSIRELYFNKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIITLSCISNMIHILNESKYQSSTKGQQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVSL 839 P34160 Nuclear cap-binding protein complex subunit 1 STO1 559292 Yes SL-0198 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}. UNIPROT P34160 UNIPROT D6VZU8 PDB 3UKY PDB 6N7P Pfam PF02854 Pfam PF09088 Pfam PF09090 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}. P06105 EBI-745,EBI-16374 P10591 EBI-8591,EBI-745 P39987 EBI-745,EBI-22339 P16474 EBI-7876,EBI-745 P0CS90 EBI-8637,EBI-745 P36016 EBI-10154,EBI-745 P33416 EBI-745,EBI-8680 P11484 EBI-745,EBI-8627 P10592 EBI-8603,EBI-745 P39076 EBI-745,EBI-19049 P39101 EBI-3949,EBI-745 Q06677 EBI-745,EBI-30084 P53207 EBI-736,EBI-745 Q00539 EBI-11835,EBI-745 Q02554 EBI-654,EBI-745 Q00916 EBI-724,EBI-745 P39935 EBI-9002,EBI-745 P32588 EBI-14231,EBI-745 P38996 EBI-11776,EBI-745 Q07508 EBI-673,EBI-745 P38199 EBI-21217,EBI-745 P32605 EBI-680,EBI-745 P54999 EBI-770,EBI-745 P10080 EBI-18146,EBI-745 P40204 EBI-637,EBI-745 P32639 EBI-861,EBI-745 Q03782 EBI-627,EBI-745 P53617 EBI-12228,EBI-745 P28320 EBI-26795,EBI-745 P07260 EBI-150,EBI-745 Q03776 EBI-802,EBI-745 Q04493 EBI-13253,EBI-745 P32561 EBI-15864,EBI-745 P11633 EBI-12028,EBI-745 Q08920 EBI-33556,EBI-745 Q12046 EBI-553,EBI-745 P36036 EBI-745,EBI-27015 P39936 EBI-745,EBI-9006 P02994 EBI-745,EBI-6314 Q02821 EBI-745,EBI-1797 P25567 EBI-745,EBI-18084 P43321 EBI-745,EBI-529 Q06217 EBI-745,EBI-235 Q02260 EBI-745,EBI-585 P23293 EBI-745,EBI-17078 Q00416 EBI-745,EBI-16945 Q04693 EBI-745,EBI-519 P0C0W1 EBI-745,EBI-16090 P53552 EBI-745,EBI-15475 P33334 EBI-745,EBI-465 P33203 EBI-745,EBI-701 P04147 EBI-745,EBI-12823 P40965 EBI-745,EBI-11371 Q06142 EBI-745,EBI-9145 P38697 EBI-745,EBI-9186 P04911 EBI-745,EBI-8072 Q05949 EBI-745,EBI-30948 Q12492 EBI-745,EBI-32227 Q12476 EBI-745,EBI-31475 Q05900 EBI-754,EBI-745 P32357 EBI-340,EBI-745 P33322 EBI-4105,EBI-745 P47130 EBI-763,EBI-745 P40018 EBI-432,EBI-745 Q02159 EBI-745,EBI-19749 P53854 EBI-29221,EBI-745 GO:0000243 GO:0005845 GO:0005846 GO:0005634 GO:0048471 GO:0005844 GO:0003729 GO:0000339 GO:0006370 GO:0045292 GO:0000398 GO:0051028 GO:0000184 GO:0006970 MFNRKRRGDFDEDENYRDFRPRMPKRQRIPPVVQLCKEMMPDIRTIGESVKAFEDDIKFLSEAIMNEYGHEDYFNNALLSTLNAVVVEQPQKQAAIALLTMVVNSKNNVAGKSIINYFFEELQKWCKQTYNDEFKSTSNETGPWNKIKLILRFLSILSPMFLVDELINIYKSLFELSIELNNLDPGNRVPLSEAIYTNTLLNIPYLFFFNRNNDGLRTKVEELLAYVEQNYLVKTTDINLLREYNGEPPYEMVELVRVVLPNVKKALINNLEQLNELFPDWNHLLTPQTGDEGFNDALTLPSVDDLKSFVRLNKNFGSVDSMWKTPRYAFHVYLPNSAGNFETVVPISTYAGQLFNDIIIDLVESLEFNRKEVARQVITLDLFFKAGIFTEPGESIAQLIATYEENPLAPTFKIEDLAIETILGLIFKLPSVSQPFAYFYTLLVDICQNSPKAIAPVFGRAFRFFYSHLDSLDFELKLRYLDWFSIQMSNFNFSWKWNEWEDDSIKFGKYFYNPKVNFAKNLIQKELRLTSNFSEVEDSLPQEFTKYLDTSYIPRDQLINYYQSLFTGYTVEEDSVRKNDLYFRQEGVPMENTVRKILDYTHKANNSREVTELESILGELKNEYGSIISDFNRFVIILLVQAVTDSGSRSLSHANKYINDLKEDLKTIFAKIELDIETKEYIIIEAVLTFWNANPQTGFLVADAFKYAGLLTSRTIFTFIFNETGLKNNGLIEATAIEAVFRNLSQQISEENESGNNFEFVFERLCTIANSTIDLLDVNADEDIEIPKVNGEMDIDDIEDDKLDLKWKYFTVIGFIKSILRRYSHEYRELADKFIANIDNAIPHESTRRTISNWIQETKEV 861 P34343 Nuclear pore complex protein 15 npp 6239 Yes SL-0178 SL-0185 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}. UNIPROT P34343 UNIPROT Q5WRU8 Pfam PF03177 Pfam PF08801 Important for early nematode development. {ECO:0000269|PubMed:12937276}. GO:0000776 GO:0031965 GO:0005643 GO:0031080 GO:0017056 GO:0051028 GO:0007275 GO:0031081 GO:0006606 GO:0006355 GO:0006405 GO:0000972 MSGRDLELTLDRVSSIEYPALVKEAFLNNWHASAHRSEVTSNCASLNDRYCWVLSRNQIFIWERAKSSHRAIIPTQLPLPTSGLPRSVKCVVVYDGVHRGANKTPCPGILVVSPEGVLRHWTSIESQTYIEEVLDINNEVALRVELTDEPIDGKSASFLLTTTSGTVYFLNGKGQDSAKTGALECNKVAGREAHGFRRRLSSIMFGGESKESTSLITNSFQHQSKDLLVVTVSPDVLTVYNMYTPCELWSLKTKEFFQPKIASFFEADLKRTPLKVRARLIDAAVFRDGLMILIGGTHEESQSVHMFMVWMSANWQTEQPTGVVWSARVPMNEHRALFSKIDDSIYSNLTLCIPKNTAESKKADRTDGIIIINPYFAVSLYLPFDLAKPKKPESLYRHVSIPPRDQLLGYAICSQYVYIMMLESGVSTIRLLPRGFADSSIYTHEQVVVPSLSVGTDDWPILSELLSEMVASGLPKTPLYQSLHRAFELFAEKHMAESEEELKAIIKMPDQEIARIVSQFLYAIIDYSDAANKTDTELHAKRVLTSRIMLFLKHMGVYERIISSPLGISRGGILSLRVGGTMLGEVSERVAASTAIWTWKTSNETNSAVFDAIIEKVLRIPEVQDLGLKDKDALFGRCGLVHHIPVVAAQQLEKNVIGKTKSHRFEVFHAVCELLSGIKETIISWRNCRTKVAIPKFPIWWTLETFASCYRDVAEKIIEELKNGSSTDSERARLLMYILSIYDFYLSESDSQPDNDKVLQEMIALGKPADAMELAEKHKDFGTLVKNYLTTDVGTRQKTFERYKKMFEKDDFEMYLCDYLKEHGRNDVLLQQGGSRVDAYLDNFKELRYSREIANKQFGKAALTLMSLADAETKSFSKFVEFLTRAYYCACSSIDGTDVSEVLDFYKRRYPEMKHRKRIPTEILKICFGNDLDAMMSVEDMLEWNMAVQPNDEASVEGFARAFHLLADLLAVHPDSDELKKKIDKTWKALVDYDEWNRVRSKEDVEKKTIFGKFCNYLINSYPADKGDSFPIWMPISRRLIFPTDIDTVLDECIANTTGNHLSWIKGHLKWIGEQLCKQALLPKSAFFRPDMKQVGSISQAALEAFGPILQRREQRFIDQLNRDSMMET 1129 P34454 Uncharacterized protein F54F2.9 F54F2 6239 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00624}; Single-pass membrane protein {ECO:0000305}. UNIPROT P34454 Pfam PF00226 Pfam PF00249 PROSITE PS50076 PROSITE PS50090 PROSITE PS51293 DE Reference Proteome: Yes; GO:0016021 GO:0031965 GO:0003677 MRVILLLAFLISLTECQWTSEDLALYDLVEEVGVNFYEWFDIPRDASSNQVKKAYRKLTLEWHPDRNSAPDATEKFRQVAGIYEVLKTTELREKYDNVLENGLPSWRHPMYYYRRMRKLAWYEGILVLLFIGTIAHYLMMWAAYFEKTLVYKQNVKKSRKSKKEDPAEAEKLMKQALEEYLPKYSELLPIILARGTVTLFKNLALTAKDAMTPKEVEPEEPTEEELAQQRRQQRAAAAPQQLEFKFEVAQGMKAVSTNDPEMEKKYAAENEVVAQKQSGATWTPDELASLVRLSTEKYPAGTPNRWEQMGRVLNRSAEDVIAMAGKMKQMKQEDYTKLLMTTIQQSVPVEEKSEDDWSQAEQKAFETALQKYPKGTDERWERISEEIGSKTKKQVMVRFKQLAEMIRKKKTNDT 414 P34561 Vacuolar protein sorting-associated protein 53 homolog vps 6239 Yes SL-0198 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}. UNIPROT P34561 UNIPROT E5QCF9 Pfam PF04100 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}. GO:0005829 GO:0010008 GO:0000938 GO:0043204 GO:0048471 GO:1904810 GO:1904811 GO:0090326 GO:0060378 GO:0042147 MEEPTTSELKLSDNVMNEISDMCITEYCKPNMSLMAQINELFPTEQSLTQLDSIIASVEGEIGELDNELAYLVETNANVSERGEEALKHAQDAMIELEKSIGSIRERTKSSDEIVREMTRDIKQLDIAKRNLTASITTLHHLHILLTGVESLGAWVDKKDYSSIARQLPAILNVLQLFDAYKESDQIANLSGQLDKLKASLTIQLAKDLKNAFQTGQLSDRITDMCRVAAALEGNVKENFVKWFIEQQLSEYVIIYADNEEGAWLDKVDDRYKWFVRKLTDFERAGLSNIFPADWHMGRRLTSEFCTVTRDILYRIMTRRRQDLDWKLLGHAIQHTKMFEALLTKRFPEKDGISFEKAIWSVFDTFLDVFINAQEKTLNEFLDTCASKIRSGEEKPSRESSTHAVPFPSSADMFLLLKKVITESSKLSSEPDALIRDVIGVVRVCLRGYATSCLVAFLPSLGSQQSGAANLFSLIREEIAYPRLTPDQQFLVCCILATADWCAETSIQLQEKLSQRIPGVDISQETEAFYSITNQSLQVLVQDVESTCDAALQSISKVNWTAVDCVGDESPFIGSMRAHLRQAVPLIRDMLSDRRKYFAHFCLKLATQLAHKFVGSLFRCRTISTHGAEQLLLDTHSLKTFLLSVPSIDSIINSKPPTAYVTSVNAALTKAEMILKVVMCSLETVDEFVEQYIKLLPASDAAEMQKVLEMKGVKRQEHSAVLNAYRLKIGASGSDPIQQSNSLTSRIGGALPTVGSAASVSEAFNAVVSMAADGLSDQAVTSSIDKLKRFERLVKRQL 798 P34609 JNK-interacting protein unc 6239 Yes SL-0198 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. UNIPROT P34609 UNIPROT A7LPE3 UNIPROT A7LPE4 UNIPROT C0P271 UNIPROT C7FZT6 UNIPROT Q95V72 UNIPROT S6EZN6 UNIPROT S6EZP3 UNIPROT S6F548 UNIPROT S6F556 UNIPROT S6FD02 UNIPROT S6FN04 UNIPROT S6FN08 UNIPROT S6FWP4 UNIPROT S6FWP6 UNIPROT U4MKU8 Pfam PF16471 Pfam PF09744 PROSITE PS51776 PROSITE PS51777 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}. P46822 EBI-315684,EBI-315578 H2L0F6 EBI-315684,EBI-329192 P34686 EBI-332095,EBI-315684 Q93345 EBI-322409,EBI-315684 Q18668 EBI-317396,EBI-315684 Q5WRT0 EBI-315684,EBI-322655 GO:0030424 GO:0043194 GO:0043679 GO:0005623 GO:0044297 GO:0005737 GO:0048471 GO:0008432 GO:0019900 GO:0019894 GO:0005078 GO:0030159 GO:0007257 GO:0030421 GO:0040011 GO:0018991 GO:0046328 GO:0048489 GO:0016192 MACNLSPVNEMADSITSSTPSEIVYGGPGSPDEHRTMSDKVQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTKYLMGSEKFELMQNMPLPNMQLRNKMGMAASVDASSIRGVSDLISAHMTQSTTMDVNLANHITNEDWQDEFSSDIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQSEEEEADETTSVDPKENNDLLGADLTDDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSLGMGREVENLIKENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLMELEESIKWTEMQRAKKMQQQQQNVNQKKSGGIWEFFSSLLGDSVTPPASSRGNRASSSRGKMTRSVEYIDPDMISERRAAERREQYKLVREHVKKEDGRIEAYGWSLPNVEAEVSSVPIPVCCRPLLDNEPSLKIWCATGVVLRGGRDERGQWIVGDPIYFAPASMKKTKTSNHRPELEDEIKRARNLDARESELDEWQSSSLVWVVSSNQGKSLIAVLDANNPNNIIETFPACDSHLLCIQAVSGVMEGEPEMNEEQSKKYLSGGGKIKDLPEGLDGTDLGACEWVELRKMEDSEDGVPTYCSNDMKPSPKRTRDFSISEVAPVDSSAPVKEDPLPPPANRPGGRAALPPHIRDAMSKYDGVSGQMSGALPTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPDAVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSATSSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVDIEPYVTKMLGTSKLDFSYMRTTALLVSNRRLWIGTGTGVIISVPFSGQLEKKIETKDSKRPAGPGGLVRVYGATSENATNDEKTNDDFIPYCNLAHAQLSFHGHKDSVKFFLGVPGASKNGEDESAEVTLRRMLIMSGGDGYIDFRIGEENEPELTGQSIRPRDMSHLIIWEVDAELPILSK 1190 P34689 ATP-dependent RNA helicase glh-1 glh 6239 Yes SL-0198 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}. UNIPROT P34689 UNIPROT Q22873 UNIPROT Q7KQH5 UNIPROT Q9TXH4 Pfam PF00270 Pfam PF00271 Pfam PF00098 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 PROSITE PS50158 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}. GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0005524 GO:0017151 GO:0008432 GO:0043621 GO:0003723 GO:0003724 GO:0008270 GO:0030154 GO:0007276 GO:0007281 GO:0009791 GO:0016070 MSDGWSDSESAAKAKTGFGSGGGFGGGNNGGSGFGGGKNGGTGFGGGNTGGSGFGGGNTGGSGFGGGKTGGSGFGGGNTCGSGFGGGSTGGSPYGGASSGFGGSTATSGFGSGEKSSAFGGSGGFGGSATGFGSGGGSFGGGNSGFGEGGHGGGERNNNCFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDGGFGGGEERGPMKCFNCKGEGHRSAECPEPPRGCFNCGEQGHRSNECPNPAKPREGVEGEGPKATYVPVEDNMEDVFNMQKISEGLMFNKFFDAEVKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDAMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAIDKIGAANKCVLQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDCSLLSELVGVLADAQQIVPDWMQGAAGGNYGASGFGSSVPTQVPQDEEGW 763 P35197 ADP-ribosylation factor GTPase-activating protein GCS1 GCS1 559292 Yes SL-0198 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. UNIPROT P35197 UNIPROT D6VRC9 PDB 5FJX Pfam PF01412 PROSITE PS50115 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}. P32589 EBI-8648,EBI-7475 P11484 EBI-8627,EBI-7475 P10592 EBI-7475,EBI-8603 P10591 EBI-7475,EBI-8591 P16140 EBI-7475,EBI-20254 P53919 EBI-7475,EBI-28887 GO:0005856 GO:0005829 GO:0005768 GO:0000139 GO:0005739 GO:0048471 GO:0005802 GO:0003779 GO:0005096 GO:0046872 GO:0030037 GO:0048205 GO:0006888 GO:0043001 GO:0006890 MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRMEKGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREGTPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQADPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAEDSSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF 352 P35233 Tyrosine-protein phosphatase non-receptor type 2 Ptpn2 10116 Yes SL-0178 SL-0182 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}. UNIPROT P35233 Pfam PF00102 PROSITE PS00383 PROSITE PS50056 PROSITE PS50055 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}. GO:0005829 GO:0005783 GO:0005793 GO:0031965 GO:0005654 GO:0005634 GO:0005886 GO:0003677 GO:0005178 GO:0004726 GO:0019901 GO:0004725 GO:0030971 GO:0097677 GO:0019905 GO:0030183 GO:0030218 GO:0042593 GO:0008286 GO:0008285 GO:0050922 GO:0042059 GO:0070373 GO:0050728 GO:0046627 GO:0060336 GO:1902206 GO:1902215 GO:0070104 GO:0010888 GO:1902227 GO:0045650 GO:2000587 GO:1902233 GO:0061099 GO:0050860 GO:0000122 GO:0010804 GO:0060339 GO:0042532 GO:0035335 GO:1902237 GO:0045722 GO:1903899 GO:0006470 GO:1902202 GO:0030217 MSATIEREFEELDAQCRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTRAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQILLSMRKYRMGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWKELSKEDLSPVCRHSQNRTMTEKYNGKRIGSEDEKLTGLSSKVPDTVEESSESILRKRIREDRKATTAQKVQQMRQRLNETERKRKRWLYWQPILTKMGFVSVILVGALVGWTLLFQLNVLPRLTDT 416 P35240 Merlin NF2 9606 Yes SL-0198 [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. UNIPROT P35240 UNIPROT O95683 UNIPROT Q8WUJ2 UNIPROT Q969N0 UNIPROT Q969Q3 UNIPROT Q96T30 UNIPROT Q96T31 UNIPROT Q96T32 UNIPROT Q96T33 UNIPROT Q9BTW3 UNIPROT Q9UNG9 UNIPROT Q9UNH3 UNIPROT Q9UNH4 PDB 1H4R PDB 3U8Z PDB 4ZRI PDB 4ZRJ PDB 6CDS Pfam PF00769 Pfam PF09380 Pfam PF00373 Pfam PF09379 PROSITE PS00660 PROSITE PS00661 PROSITE PS50057 OMIM 101000 OMIM 156240 OMIM 162091 OMIM 607379 DisGeNET 4771 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}.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. P31689 EBI-1014472,EBI-347834 Self EBI-1014472,EBI-1014472 Q9BZE4 EBI-1056249,EBI-1014472 Q9Y6K9 EBI-81279,EBI-1014472 Q92844 EBI-356349,EBI-1014472 Q8NFZ5 EBI-359372,EBI-1014472 O14964 EBI-740220,EBI-1014472 Q9Y2J4 EBI-746752,EBI-1014472 P46937 EBI-1044059,EBI-1014472 O95835 EBI-1014472,EBI-444209 P57078 EBI-4422308,EBI-1014472 Q4VCS5 EBI-2511319,EBI-1014472 Q4VCS5-2 EBI-1014472,EBI-3891843 Q4VCS5-1 EBI-3903812,EBI-1014472 Q68EM7-1 EBI-3957761,EBI-1014472 Q8NI35 EBI-724390,EBI-1014472 Q8N3R9 EBI-2513978,EBI-1014472 Q13153 EBI-1014472,EBI-1307 D4A9Q2 EBI-3892226,EBI-1014472 Q8IY63 EBI-1014472,EBI-1057112 P35240-2 EBI-1014505,EBI-1014472 Q14324 EBI-1014472,EBI-5653200 Q9H204 EBI-514199,EBI-1014472 O14745 EBI-1014472,EBI-349787 Q10728 EBI-1014472,EBI-918263 P11279 EBI-2805407,EBI-1014472 Q92918 EBI-881,EBI-1014472 P52272 EBI-486809,EBI-1014472 O14964-1 EBI-21239519,EBI-1014472 Q01082 EBI-351561,EBI-1014472 O60884 EBI-1014472,EBI-352957 Q9BQE3 EBI-1014472,EBI-1103245 P34932 EBI-1014472,EBI-356933 Q92598 EBI-1014472,EBI-356829 P63167 EBI-1014472,EBI-349105 GO:0005912 GO:0045177 GO:0044297 GO:0032154 GO:0030864 GO:0005737 GO:0005856 GO:0005829 GO:0005769 GO:0031527 GO:0030027 GO:0016020 GO:0043005 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0032587 GO:0003779 GO:0030036 GO:0045216 GO:0007398 GO:0021766 GO:0070306 GO:0001707 GO:0030336 GO:0008285 GO:0022408 GO:0001953 GO:0043409 GO:0006469 GO:0046426 GO:0042532 GO:0042475 GO:0045597 GO:0051496 GO:0042981 GO:0051726 GO:0014013 GO:0035330 GO:2000177 GO:1900180 GO:0031647 GO:0072091 GO:0014010 MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL 595 P35281 Ras-related protein Rab-10 Rab10 10116 Yes SL-0198 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}. UNIPROT P35281 Pfam PF00071 PROSITE PS51419 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}. P19357 EBI-915426,EBI-917314 GO:0098993 GO:0005929 GO:0012505 GO:0005789 GO:0071782 GO:0005768 GO:0070382 GO:0005794 GO:0032593 GO:0016020 GO:0048471 GO:0030670 GO:0005886 GO:0055037 GO:0055038 GO:0008021 GO:0005802 GO:0019003 GO:0051021 GO:0005525 GO:0003924 GO:0031489 GO:0019882 GO:0007409 GO:0071236 GO:0032869 GO:0071786 GO:0016197 GO:0045200 GO:0097051 GO:0090150 GO:0043001 GO:0006893 GO:0006886 GO:0030859 GO:1903361 GO:0072659 GO:0009306 GO:0032482 GO:0045055 GO:0017157 GO:0006904 GO:0016192 MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIEIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDQHANEDVERMLLRNKCDMDHKRVVPKGKGEQIAREHRIRFFETSAKANINIEKAFLTLPEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC 200 P35368 Alpha-1B adrenergic receptor ADRA1B 9606 Yes SL-0178 SL-0182 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. UNIPROT P35368 UNIPROT B0LPE1 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 OMIM 104220 DisGeNET 147 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}. P25106 EBI-490017,EBI-1965291 P35348 EBI-489756,EBI-490017 Self EBI-490017,EBI-490017 P61073 EBI-490017,EBI-489411 P25100 EBI-489993,EBI-490017 P02768 EBI-714423,EBI-490017 P01857 EBI-356114,EBI-490017 Q14315 EBI-490017,EBI-489954 GO:0005901 GO:0005623 GO:0005737 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0004935 GO:0004937 GO:0046982 GO:0071880 GO:0007188 GO:0007267 GO:0007186 GO:0042593 GO:0035556 GO:0150099 GO:0001994 GO:0007200 GO:0007204 GO:0043410 GO:0045987 GO:0045907 GO:0055117 MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLTEPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF 520 P35508 Casein kinase I isoform delta CSNK1D 9913 Yes SL-0198 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}. UNIPROT P35508 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005737 GO:0000139 GO:0005815 GO:0005634 GO:0048471 GO:0005886 GO:0005876 GO:0005524 GO:0004672 GO:0004674 GO:0050321 GO:0032922 GO:1905515 GO:0018105 GO:0090263 GO:0032436 GO:0006468 GO:0042752 GO:0051225 GO:0016055 MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR 415 P35658 Nuclear pore complex protein Nup214 NUP214 9606 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:8108440}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000269|PubMed:8108440}. UNIPROT P35658 UNIPROT A6NFQ0 UNIPROT Q15010 UNIPROT Q3KQZ0 UNIPROT Q5JUP7 UNIPROT Q75R47 UNIPROT Q86XD3 PDB 2OIT PDB 3FHC PDB 3FMO PDB 3FMP PDB 5DIS Pfam PF18617 OMIM 114350 OMIM 618426 DisGeNET 8021 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}.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. Q6UXB4 EBI-2114729,EBI-1222270 Q9GZM8 EBI-1222270,EBI-928842 Q9UPY3 EBI-395506,EBI-1222270 Q9H0R8 EBI-746969,EBI-1222270 P25054 EBI-727707,EBI-1222270 Q5NFS5 EBI-1222270,EBI-2797271 Q80U93 EBI-2551193,EBI-1222270 Q07832 EBI-2552999,EBI-1222270 Q9UN86 EBI-1044298,EBI-1222270 Q13283 EBI-1047359,EBI-1222270 P24386 EBI-2515129,EBI-1222270 Q9H492 EBI-720768,EBI-1222270 P19320 EBI-6189824,EBI-1222270 Q13617 EBI-456179,EBI-1222270 Q13618 EBI-456129,EBI-1222270 Q8D1L8 EBI-1222270,EBI-2862395 Q81KT8 EBI-1222270,EBI-2809955 Q5NGV7 EBI-2796192,EBI-1222270 A0A2S9PJQ7 EBI-2846239,EBI-1222270 A0A2P0HLN8 EBI-1222270,EBI-2810906 P01857 EBI-356114,EBI-1222270 Q99567 EBI-726178,EBI-1222270 P0DTD1 EBI-25475877,EBI-1222270 Q15811 EBI-602041,EBI-1222270 Q3KR16-1 EBI-25408239,EBI-1222270 Q9Y4F1 EBI-5235630,EBI-1222270 Q63358 EBI-6251137,EBI-1222270 GO:1990876 GO:0005829 GO:0043657 GO:0005643 GO:0005654 GO:0005049 GO:0008139 GO:0017056 GO:0075733 GO:0000278 GO:0006406 GO:0006611 GO:0006606 GO:0016925 GO:0051726 GO:1900034 GO:0060964 GO:0006110 GO:0043488 GO:0046822 GO:0006405 GO:0006409 GO:0016032 GO:0019083 MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGLVFAGGASGLQIFPTKNLLIQNKPGDDPNKIVDKVQGLLVPMKFPIHHLALSCDNLTLSACMMSSEYGSIIAFFDVRTFSNEAKQQKRPFAYHKLLKDAGGMVIDMKWNPTVPSMVAVCLADGSIAVLQVTETVKVCATLPSTVAVTSVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHPVRVLDVLWIGTYVFAIVYAAADGTLETSPDVVMALLPKKEEKHPEIFVNFMEPCYGSCTERQHHYYLSYIEEWDLVLAASAASTEVSILARQSDQINWESWLLEDSSRAELPVTDKSDDSLPMGVVVDYTNQVEITISDEKTLPPAPVLMLLSTDGVLCPFYMINQNPGVKSLIKTPERLSLEGERQPKSPGSTPTTPTSSQAPQKLDASAAAAPASLPPSSPAAPIATFSLLPAGGAPTVFSFGSSSLKSSATVTGEPPSYSSGSDSSKAAPGPGPSTFSFVPPSKASLAPTPAASPVAPSAASFSFGSSGFKPTLESTPVPSVSAPNIAMKPSFPPSTSAVKVNLSEKFTAAATSTPVSSSQSAPPMSPFSSASKPAASGPLSHPTPLSAPPSSVPLKSSVLPSPSGRSAQGSSSPVPSMVQKSPRITPPAAKPGSPQAKSLQPAVAEKQGHQWKDSDPVMAGIGEEIAHFQKELEELKARTSKACFQVGTSEEMKMLRTESDDLHTFLLEIKETTESLHGDISSLKTTLLEGFAGVEEAREQNERNRDSGYLHLLYKRPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDQHLEQKKKQRHLLVPERETLFNTLANNREIINQQRKRLNHLVDSLQQLRLYKQTSLWSLSSAVPSQSSIHSFDSDLESLCNALLKTTIESHTKSLPKVPAKLSPMKQAQLRNFLAKRKTPPVRSTAPASLSRSAFLSQRYYEDLDEVSSTSSVSQSLESEDARTSCKDDEAVVQAPRHAPVVRTPSIQPSLLPHAAPFAKSHLVHGSSPGVMGTSVATSASKIIPQGADSTMLATKTVKHGAPSPSHPISAPQAAAAAALRRQMASQAPAVNTLTESTLKNVPQVVNVQELKNNPATPSTAMGSSVPYSTAKTPHPVLTPVAANQAKQGSLINSLKPSGPTPASGQLSSGDKASGTAKIETAVTSTPSASGQFSKPFSFSPSGTGFNFGIITPTPSSNFTAAQGATPSTKESSQPDAFSSGGGSKPSYEAIPESSPPSGITSASNTTPGEPAASSSRPVAPSGTALSTTSSKLETPPSKLGELLFPSSLAGETLGSFSGLRVGQADDSTKPTNKASSTSLTSTQPTKTSGVPSGFNFTAPPVLGKHTEPPVTSSATTTSVAPPAATSTSSTAVFGSLPVTSAGSSGVISFGGTSLSAGKTSFSFGSQQTNSTVPPSAPPPTTAATPLPTSFPTLSFGSLLSSATTPSLPMSAGRSTEEATSSALPEKPGDSEVSASAASLLEEQQSAQLPQAPPQTSDSVKKEPVLAQPAVSNSGTAASSTSLVALSAEATPATTGVPDARTEAVPPASSFSVPGQTAVTAAAISSAGPVAVETSSTPIASSTTSIVAPGPSAEAAAFGTVTSGSSVFAQPPAASSSSAFNQLTNNTATAPSATPVFGQVAASTAPSLFGQQTGSTASTAAATPQVSSSGFSSPAFGTTAPGVFGQTTFGQASVFGQSASSAASVFSFSQPGFSSVPAFGQPASSTPTSTSGSVFGAASSTSSSSSFSFGQSSPNTGGGLFGQSNAPAFGQSPGFGQGGSVFGGTSAATTTAATSGFSFCQASGFGSSNTGSVFGQAASTGGIVFGQQSSSSSGSVFGSGNTGRGGGFFSGLGGKPSQDAANKNPFSSASGGFGSTATSNTSNLFGNSGAKTFGGFASSSFGEQKPTGTFSSGGGSVASQGFGFSSPNKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAFTSPLGSTGGKVFGEGTAAASAGGFGFGSSSNTTSFGTLASQNAPTFGSLSQQTSGFGTQSSGFSGFGSGTGGFSFGSNNSSVQGFGGWRS 2090 P35729 Nucleoporin NUP120 NUP120 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P35729 UNIPROT D6VXN0 UNIPROT P35730 PDB 3F7F PDB 3H7N PDB 3HXR PDB 4XMM PDB 4XMN 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}. Self EBI-11713,EBI-11713 Q02630 EBI-11703,EBI-11713 Q02629 EBI-11698,EBI-11713 P22696 EBI-6679,EBI-11713 P39987 EBI-22339,EBI-11713 P11484 EBI-11713,EBI-8627 P53900 EBI-13246,EBI-11713 P46673 EBI-12345,EBI-11713 Q04477 EBI-27228,EBI-11713 P49687 EBI-11713,EBI-11730 P55735 EBI-11713,EBI-1046596 P53011 EBI-11713,EBI-16940 Q8WUM0 EBI-11713,EBI-295695 P52891 EBI-11713,EBI-12337 P47054 EBI-25846,EBI-11713 Q04439 EBI-11687,EBI-11713 P10592 EBI-11713,EBI-8603 Q06488 EBI-11713,EBI-16198 Q04491 EBI-16529,EBI-11713 P32582 EBI-4167,EBI-11713 P38305 EBI-20939,EBI-11713 Q12315 EBI-7635,EBI-11713 GO:0000781 GO:0031965 GO:0005643 GO:0031080 GO:0042802 GO:0017056 GO:0006302 GO:0035392 GO:0006406 GO:0031990 GO:0000122 GO:0031081 GO:0045944 GO:0045893 GO:0000973 GO:0006611 GO:0006606 GO:0000055 GO:0034398 MACLSRIDANLLQYYEKPEPNNTVDLYVSNNSNNNGLKEGDKSISTPVPQPYGSEYSNCLLLSNSEYICYHFSSRSTLLTFYPLSDAYHGKTINIHLPNASMNQRYTLTIQEVEQQLLVNVILKDGSFLTLQLPLSFLFSSANTLNGEWFHLQNPYDFTVRVPHFLFYVSPQFSVVFLEDGGLLGLKKVDGVHYEPLLFNDNSYLKSLTRFFSRSSKSDYDSVISCKLFHERYLIVLTQNCHLKIWDLTSFTLIQDYDMVSQSDSDPSHFRKVEAVGEYLSLYNNTLVTLLPLENGLFQMGTLLVDSSGILTYTFQNNIPTNLSASAIWSIVDLVLTRPLELNVEASYLNLIVLWKSGTASKLQILNVNDESFKNYEWIESVNKSLVDLQSEHDLDIVTKTGDVERGFCNLKSRYGTQIFERAQQILSENKIIMAHNEDEEYLANLETILRDVKTAFNEASSITLYGDEIILVNCFQPYNHSLYKLNTTVENWFYNMHSETDGSELFKYLRTLNGFASTLSNDVLRSISKKFLDIITGELPDSMTTVEKFTDIFKNCLENQFEITNLKILFDELNSFDIPVVLNDLINNQMKPGIFWKKDFISAIKFDGFTSIISLESLHQLLSIHYRITLQVLLTFVLFDLDTEIFGQHISTLLDLHYKQFLLLNLYRQDKCLLAEVLLKDSSEFSFGVKFFNYGQLIAYIDSLNSNVYNASITENSFFMTFFRSYIIENTSHKNIRFFLENVECPFYLRHNEVQEFMFAMTLFSCGNFDQSYEIFQLHDYPEAINDKLPTFLEDLKSENYHGDSIWKDLLCTFTVPYRHSAFYYQLSLLFDRNNSQEFALKCISKSAEYSLKEIQIEELQDFKEKQHIHYLNLLIHFRMFEEVLDVLRLGHECLSDTVRTNFLQLLLQEDIYSRDFFSTLLRLCNAHSDNGELYLRTVDIKIVDSILSQNLRSGDWECFKKLYCFRMLNKSERAAAEVLYQYILMQADLDVIRKRKCYLMVINVLSSFDSAYDQWILNGSKVVTLTDLRDELRGL 1037 P35845 Oxysterol-binding protein homolog 1 SWH1 559292 Yes SL-0178 SL-0182 SL-0183 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. UNIPROT P35845 UNIPROT D6VPN6 UNIPROT P39555 UNIPROT P80234 UNIPROT Q86ZC4 UNIPROT Q86ZS1 PDB 5H28 PDB 5H2C Pfam PF01237 Pfam PF00169 PROSITE PS50297 PROSITE PS50088 PROSITE PS01013 PROSITE PS50003 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}. Self EBI-12611,EBI-12611 P10591 EBI-12611,EBI-8591 P39987 EBI-22339,EBI-12611 P33416 EBI-12611,EBI-8680 P11484 EBI-8627,EBI-12611 P10592 EBI-8603,EBI-12611 P40150 EBI-12611,EBI-8632 P32589 EBI-12611,EBI-8648 P43613 EBI-23020,EBI-12611 P40564 EBI-12611,EBI-25380 P35177 EBI-17958,EBI-12611 Q03330 EBI-7458,EBI-12611 P40075 EBI-16735,EBI-12611 P29056 EBI-19142,EBI-12611 P00359 EBI-12611,EBI-7218 P32324 EBI-12611,EBI-6333 P32794 EBI-12611,EBI-2310 P38881 EBI-24885,EBI-12611 P12385 EBI-6533,EBI-12611 P40510 EBI-12611,EBI-16821 P07259 EBI-12611,EBI-14372 P02994 EBI-12611,EBI-6314 P26786 EBI-12611,EBI-16161 P23248 EBI-12611,EBI-16136 P41805 EBI-12611,EBI-15270 P41940 EBI-12611,EBI-11191 P32317 EBI-12611,EBI-2306 P53919 EBI-12611,EBI-28887 P38829 EBI-12611,EBI-24704 GO:0005829 GO:0005769 GO:0005783 GO:0000139 GO:0000138 GO:0043231 GO:0016020 GO:0005635 GO:0005640 GO:0071561 GO:0005545 GO:0008289 GO:0008142 GO:0032934 GO:0120015 GO:0015248 GO:0006897 GO:0006887 GO:0030011 GO:0034727 GO:0015918 MEQPDLSSVAISKPLLKLKLLDALRQGSFPNLQDLLKKQFQPLDDPNVQQVLHLMLHYAVQVAPMAVIKEIVHHWVSTTNTTFLNIHLDLNERDSNGNTPLHIAAYQSRGDIVAFLLDQPTINDCVLNNSHLQAIEMCKNLNIAQMMQVKRSTYVAETAQEFRTAFNNRDFGHLESILSSPRNAELLDINGMDPETGDTVLHEFVKKRDVIMCRWLLEHGADPFKRDRKGKLPIELVRKVNENDTATNTKIAIDIELKKLLERATREQSVIDVTNNNLHEAPTYKGYLKKWTNFAQGYKLRWFILSSDGKLSYYIDQADTKNACRGSLNMSSCSLHLDSSEKLKFEIIGGNNGVIRWHLKGNHPIETNRWVWAIQGAIRYAKDREILLHNGPYSPSLALSHGLSSKVSNKENLHATSKRLTKSPHLSKSTLTQNDHDNDDDSTNNNNNKSNNDYDDNNNNNNNDDDDYDDDDESRPLIEPLPLISSRSQSLSEITPGPHSRKSTVSSTRAADIPSDDEGYSEDDSDDDGNSSYTMENGGENDGDEDLNAIYGPYIQKLHMLQRSISIELASLNELLQDKQQHDEYWNTVNTSIETVSEFFDKLNRLTSQREKRMIAQMTKQRDVNNVWIQSVKDLEMELVDKDEKLVALDKERKNLKKMLQKKLNNQPQVETEANEESDDANSMIKGSQESTNTLEEIVKFIEATKESDEDSDADEFFDAEEAASDKKANDSEDLTTNKETPANAKPQEEAPEDESLIVISSPQVEKKNQLLKEGSFVGYEDPVRTKLALDEDNRPKIGLWSVLKSMVGQDLTKLTLPVSFNEPTSLLQRVSEDIEYSHILDQAATFEDSSLRMLYVAAFTASMYASTTNRVSKPFNPLLGETFEYARTDGQYRFFTEQVSHHPPISATWTESPKWDFYGECNVDSSFNGRTFAVQHLGLWYITIRPDHNISVPEETYSWKKPNNTVIGILMGKPQVDNSGDVKVTNHTTGDYCMLHYKAHGWTSAGAYEVRGEVFNKDDKKLWVLGGHWNDSIYGKKVTARGGELTLDRIKTANSATGGPKLDGSKFLIWKANERPSVPFNLTSFALTLNALPPHLIPYLAPTDSRLRPDQRAMENGEYDKAAAEKHRVEVKQRAAKKEREQKGEEYRPKWFVQEEHPVTKSLYWKFNGEYWNKRKNHDFKDCADIF 1188 P35930 RNA-directed RNA polymerase POL1 12262 No SL-0382 [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}. UNIPROT P35930 UNIPROT Q66182 Pfam PF00548 Pfam PF00680 Pfam PF00910 PROSITE PS51874 PROSITE PS50507 PROSITE PS51218 [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}. GO:0044165 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003723 GO:0003724 GO:0003968 GO:0018144 GO:0006351 GO:0039694 MYMLTFEPGLCVAGIIRQVRSNPFMHVVQAYARTTETYREDIEMTKSMLKLKADEPLLVMSIVAAAMDFQTMVMAPIEMEASEFLYGFYAERMSYIVTNRGMSELHEYIQLQCQRHLLVKVEIDGQYLVQEHEYEAQGFNIKRVKELITDVATWVPKKVKGMIGWSVDAVLDSFQEYFYKVITERIPMAMKVCSWVATVWDQIKTWIEDAMTAMSSFLQGCNELLTWGLATLAACCALNVLERILIFMEFLDESIDIAGIFLRTGVVAAACYHFSSTAKGFTEMMSVLSVATTAVAAVVCANYFGGSKTKKVNAQGNPVDLLERIAAGLSSISQDSLVSLGKSCSAINSIATSYGHLRNFAGRVLTMLRDFAWKILGLETRFLADAALVFGEDVDGWLQRISALREAYVSKAYSSQDEVFEMNVLLERGYKMRHLMATGSRVSPAIGNMLMQGLADLERLHRNAAVQGVKGVRKIPFTVFAHGNSRCGKSLLIGKLISDFQEHKGLGEDTVYSRNTTETHWSGYRRQPIVVIDDFAAVESDISAEAQLINLVSSTPYSVVMAAIEEKGMTFDSQFIFASTNFLEVSPNGKIRCDDAFRNRRHVLIDVKLKPEVEYQSDDFTANQSYNILEHSHGRYNVVATFDNYEELLAYCLTKHEQHEAEQEANLAKLRRTNKFESHFKKFEQVLQLSTYFSSSIERIKREALATTDGADDYHLLYVVPRNGSYLHVAANKDFQIQQWYGPVEEVAEEDILRASERMLLGAYEFLLLSTELNVVVKNHLPELICTDNYDHNLEFCGVVGDPVYHQQLLKNIRALKPWHRAVLFGIGTLMGAKNPTPWYKRMWEGIKDVLYKAYSTEISQWPVPLKITCGIVLVGIVGAGFWKTVSVLTNAGNGAGLVGAAVNSFSVVSTAEAQSRKPNRFEVQQYRYKNVPLTRRSWGNAQMSLDQSTVSILNKCHAKFIIASQHAQIVLVPGRRFIGYSHFFCNLKHPLMVQIETADRTYFHRYQPENMEYIEDSELCVYHSSCLEDISHSCWDLFCWDPDKELPKKFSADFVSCKYNTWTKSVEPTWANVDAEVIKEDFTICDGEYRNTVSTSIRYEAPTVMSDCGSMIITNVGGKTKIVGIHVAGRDNKIGMASLLPPLLPCAQAQGAEKYFNFYPIEYDAAEGIARVGELKPKLYIPLPKKTSLVKTPEEWHLGTPCDKVPSILVKGDPRLADTVHADYDPCLSGLTKYSTPMSPLDSVLLGETCQEILDEWFDCLPEGFELGEVTINEALNGVDGVDYMDRIPLATSEGFPHVMSREQGEKGKQRFVQGDGHIVSLIPGTSVHEAYETLSRTIATEVPTLVGIECPKDEKLPFRKVFTKPKTRNFTILPMEYNILVRQYFLNFVRFIMKKRDVLPCQVGINPYSMEWSIVASRLKSQGNDILCCDYSSFDGLLSKQIMEMMADMINRFCGGGTLICAKRKNLLMACCSRLAISRDSVWRIECGIPSGFPLTVICNSIFNEILVRYHYKLLLQEHNAPNMYVQSFKNLISMVTYGDDNLISVNAVVKPYFDGTKLKQAMARNGIIITDGKDKTSATLEFRRLEDCDFLKRGFLKRSSVLWDAPEEKASLWAQLHYVNVNNCEMQVAYMTNLVNVLRELYMHDPTEMVEFRRLALKSIPWLNTTDLPTLYQVKEFYAEQRLRNIPDHNDSLDMLTSVDLLGPAILGEGVPQEALVLSELLEVRDLRYHTVPDNDNGKEVWILFNTMYPQKLLPSNCHSFTWNCGQGRGGLPTQHWLATNVTRTDSKLNKLIRTAVAANKKIVLATKDNILPINVIAVLLAARNKVMPSLATNALLTYVIGAAKKLNFLTSECQFAFFNV 1864 P36137 Protein UIP5 UIP5 559292 Yes SL-0178 SL-0182 Nucleus membrane; Single-pass type I membrane protein. UNIPROT P36137 UNIPROT D6VXA6 Pfam PF03388 DE Reference Proteome: Yes; P02829 EBI-26427,EBI-8659 GO:0030134 GO:0005789 GO:0005793 GO:0000324 GO:0000139 GO:0016021 GO:0005635 GO:0031965 GO:0005537 GO:0007029 GO:0006888 GO:0007030 MSRDVRAEKLAISLLILSLFLIFQLVAEIYLNNGDQYHTETSPFTRGRSHVTRVPNHDASLSIPFLDKINQFWHVGGATQIRNIQSIKLTQDRDQDKHGLVLSNGIGDNTINDFEIVFTFRISHDPTTQLTGDGMCFAITPENGFLTQNLQSSYAKKQYMMNSQGVIADNTDLMGFPKNLPGLFIVLDTYRNQGHDHKEVPFMDVFINVAPESDWYDINSDGELSTSLRLNSRGHIKLKKNALWNRVTKLRIIYLESISFLKIDVQYAKEGNYWIELFQTTENLYLPKNMHTGQRYIGCSALNGQLTETVELLDVSTSEFHWNDMDASIEDTYDYAKEAELFLEQEFGEVLDREPDEFTKWKMIKAQPNIKTGSQSAEQKTSNNPHSRLFKVVLTIWHYSEILLLIMGIYLFSACIRVFQRRFKKIRSRRKRAGSHSVGLLPM 443 P36161 Nucleoporin NUP133 NUP133 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P36161 UNIPROT D6VXE2 PDB 3KFO Pfam PF08801 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}. P39523 EBI-27256,EBI-11722 P22696 EBI-6679,EBI-11722 Q12329 EBI-11722,EBI-8571 P11484 EBI-8627,EBI-11722 P10592 EBI-8603,EBI-11722 P33416 EBI-8680,EBI-11722 P48363 EBI-13239,EBI-11722 P47079 EBI-11722,EBI-19072 P40150 EBI-11722,EBI-8632 P02829 EBI-8659,EBI-11722 P32589 EBI-8648,EBI-11722 P15108 EBI-11722,EBI-8666 P31539 EBI-11722,EBI-8050 Q04432 EBI-11722,EBI-35591 P38181 EBI-11722,EBI-11756 P52891 EBI-12337,EBI-11722 Q04477 EBI-27228,EBI-11722 P16140 EBI-11722,EBI-20254 P0CS90 EBI-11722,EBI-8637 P10591 EBI-11722,EBI-8591 P46673 EBI-11722,EBI-12345 P38305 EBI-20939,EBI-11722 Q12315 EBI-7635,EBI-11722 GO:0000781 GO:0005829 GO:0031965 GO:0005643 GO:0031080 GO:0005634 GO:0017056 GO:0030466 GO:0006302 GO:0035392 GO:0031990 GO:0000122 GO:0031081 GO:0016973 GO:0045944 GO:0045893 GO:0000973 GO:0006606 GO:0006355 GO:0006405 GO:0034398 GO:0000972 GO:0006409 MSEKKVHLRLRKELSVPIAVVENESLAQLSYEEESQASLMDISMEQQQLRLHSHFDNSKVFTENNRYIVKTLQTDYSSGFSNDDELNGYIDMQIGYGLVNDHKKVYIWNIHSTQKDTPYITVPFRSDDNDEIAVAPRCILTFPATMDESPLALNPNDQDETGGLIIIKGSKAIYYEDINSINNLNFKLSEKFSHELELPINSSGGEKCDLMLNCEPAGIVLSTNMGRIFFITIRNSMGKPQLKLGKLLNKPFKLGIWSKIFNTNSSVVSLRNGPILGKGTRLVYITTNKGIFQTWQLSATNSHPTKLIDVNIYEAILESLQDLYPFAHGTLKIWDSHPLQDESSQLFLSSIYDSSCNETYYILSTIIFDSSSNSFTIFSTYRLNTFMESITDTKFKPKIFIPQMENANDTNEVTSILVMFPNAVVITQVNSKLDSSYSMRRKWEDIVSLRNDIDIIGSGYDSKSLYVLTKQMGVLQFFVKENEETNSKPEVGFVKSHVDQAVYFSKINANPIDFNLPPEISLDQESIEHDLKLTSEEIFHSNGKYIPPMLNTLGQHLSVRKEFFQNFLTFVAKNFNYKISPELKLDLIEKFEILNCCIKFNSIIRQSDVLNDIWEKTLSNYNLTQNEHLTTKTVVINSPDVFPVIFKQFLNHVVFVLFPSQNQNFKLNVTNLINLCFYDGILEEGEKTIRYELLELDPMEVDTSKLPWFINFDYLNCINQCFFDFTFACEEEGSLDSYKEGLLKIVKILYYQFNQFKIWINTQPVKSVNANDNFININNLYDDNHLDWNHVLCKVNLKEQCIQIAEFYKDLSGLVQTLQTLDQNDSTTVSLYETFFNEFPKEFSFTLFEYLIKHKKLNDLIFRFPQQHDVLIQFFQESAPKYGHVAWIQQILDGSYADAMNTLKNITVDDSKKGESLSECELHLNVAKLSSLLVEKDNLDINTLRKIQYNLDTIDAEKNISNKLKKGEVQICKRFKNGSIREVFNILVEELKSTTVVNLSDLVELYSMLDDEESLFIPLRLLSVDGNLLNFEVKKFLNALVWRRIVLLNASNEGDKLLQHIVKRVFDEELPKNNDFPLPSVDLLCDKSLLTPEYISETYGRFPIDQNAIREEIYEEISQVETLNSDNSLEIKLHSTIGSVAKEKNYTINYETNTVEY 1157 P36268 Inactive glutathione hydrolase 2 GGT2 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:23682772}. Endoplasmic reticulum {ECO:0000269|PubMed:23682772}. Note=Co-localizes with calnexin in the endoplasmic reticulum. UNIPROT P36268 PROSITE PS00462 OMIM 137181 DisGeNET 728441 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}. GO:0005783 GO:0070062 GO:0048471 GO:0005886 GO:0000048 GO:0006751 GO:1901750 GO:0031179 GO:0006508 GO:0002682 GO:0050727 GO:0032355 GO:0032496 GO:0034612 GO:0007283 MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAMAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTGKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLWYVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNEWTTSALPAFTNEFGAPPSPANFIQPGKQPLLSMCLTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAALDSRKGGEPAGY 569 P36312 RNA-directed RNA polymerase POL1 31716 No SL-0382 [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}. UNIPROT P36312 Pfam PF00548 Pfam PF00680 Pfam PF00910 PROSITE PS51874 PROSITE PS50507 PROSITE PS51218 [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}. GO:0044165 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003723 GO:0003724 GO:0003968 GO:0018144 GO:0006351 GO:0039694 MKFFAGQTVMDVLQHVSSPTTNLRLLSYCNLKKEEDGKMMLAIKEQRHRRLLTLSYGAMCFQFSNSVGDEGIEVDDDELMFEIFDALLRTKISNSKGMTHLYSWMRGVYLSTFKVEVQCDDYNSNLLEKDLAGEAQGLSQFVSGLADWIPSRVKTLAGYAAEGIIEAFKKHFDKLLVEYCPMAVAACSWITTVWTTIKEWVQSAMDAMSWIMAGCTELISWGMCVIAGSCALSLLEKALVAMGLISSSFDLAGIFVRSAVVGAFCLTVVNKRSRNCAELLQLVSLAVGAVSSATSSCFQSPVGQATDVSAESQSGGVEMLESLAKNLTNFCDGTLVSIGKTCNAVNSINTAAGTIKNLVGRLLSMLSNFAYKLLGLESTFLRDASVVFSENVDGWLKQISWCQDQFLAKAYINQDELMVLRSLITRGEVMQREMIMGGMKVSPTVCGLINKGCTDLAKLMAGAVMHGTSGTRKIPFVVYAHGASRVGKTMVINRLIEDFRKELELGEDCVYPRNVVDDYWSGYKRQPIVVIDDFGAVSSDPSAEAQLIPLISSAPYPLNMADLSEKGMHFDSAIVMCSSNFIECSPESKVRDEMAFRNRRHVLFTVSLDPNIPYDGDDITKNQIYEIKTWFHDSYHVEATFTSYGDLLAYCKNKWVEHNTEQEANLKQLGVKKESVAFQQFRSILDLAVFVNQDAENFKQRLETPDGRCHFVSCYDKSGILRHYTIDATGDVQEMEKVDSSLDDILLEKTNKMVLAAYKMIKYHKDTNLVIKTQLADLVDPTKYTADFQFDGVIGSPLFSSQVMPSVKALPLWQRMVLYTVGQNLGRTHSSWYEGIKDKCMLALSKAYSTEIKDWPVALKIVVGVILATVAGKAFWRFYASMADAGNGGHFVGAVASAFAGSQAVVAQSRKPNRFDVAQYRYRNIPLRKRNWAEGQMSLDQSTMLIMEKCKANFVFSNISCQIVMLPGRQFLCYKHVFASLNSPMYVDIYTANKKYKLYYKPQNRVYFETDSEIMLYKDASLEDIPASCWDLFCFDAEKSLPRGSFPAEILSCKLDRTTNQHIPEWADISARTVNQKLDVEFGEYQTIFYSYLQYDVSTKAEDCGSLIIATIDGRKKIIGIHTAGRANRSGFASYMPQVEIPVQAQAAEKFFDFLEKEQHVTEGIGKVGNLKKGVWVPLPTKTNLVETPKEWHLGTEKTKEPSILSSTDLRLGDKQYDPFVGGIQKYAEPMGILDDEVLRHVATDIVEEWFDCVDPQEDTFEEVDLQVAINGLEGMEYMERVPMATSEGFPHILTRKSGEKGKGRFVYGDGEIFDLIPGTSVHEAYLTLEETCADTVPALVGIECPKDEKLPLRKIYEKPKTRCFTVLPMEYNLVVRRKFLKFVVFIMKNRHRLSCQVGINPYGMEWSRLAMSLLEKGNNILCCDYSSFDGLLTKQVMHLMSEMINELCGGSSRLKQQRTNLLMACCSRYALCKGEVWRVECGIPSGFPLTVICNSIFNELLVRYSYIKICQQARVPATITYGFSTFVKMVTYGDDNLLSVQSAITHVFDGTKLKEFLKLNGITITDGKDKTSPVLNFRNLEDCDFLKRGFKKESDVVWVGPEEKESLWAQLHYVTTNNLEKHEAYLVNVVNVIRELYLHDPREAAELRRKAIQNVDFLKENPKDLPTMAAIKEFYNMQRQQQFVDSNDNLDSLLNPDFLFVAPHRKMHEAEMELVPKWYLRDLGKAPINVLTGEADRICVLVNASIPDHLLPEKVVNISWPYGPGRGGLPTHGWAQANLYNPNSAVVKKLRTLVNQNPDDRVDICFRHDAVPVAIATIIFLVHLGKVKGRSANEYLTKIIDSAKSLKFLPKECDIIF 1858 P38114 Uncharacterized transcriptional regulatory protein TBS1 TBS1 559292 Yes SL-0178 SL-0182 Nucleus membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. UNIPROT P38114 UNIPROT D6VQE5 UNIPROT E9PAD3 Pfam PF04082 Pfam PF00172 PROSITE PS00463 PROSITE PS50048 Involved in tolerance to thiabendazole. {ECO:0000269|PubMed:10628851}. Q12343 EBI-20833,EBI-31503 Q12180 EBI-20833,EBI-37549 P10591 EBI-8591,EBI-20833 P11484 EBI-8627,EBI-20833 P38788 EBI-24570,EBI-20833 P02829 EBI-20833,EBI-8659 P53900 EBI-13246,EBI-20833 P39078 EBI-19054,EBI-20833 P32589 EBI-20833,EBI-8648 Q12329 EBI-8571,EBI-20833 P10592 EBI-8603,EBI-20833 GO:0005737 GO:0016021 GO:0031966 GO:0005739 GO:0031965 GO:0005634 GO:0000981 GO:0043565 GO:0008270 GO:0006351 MNMDSGITSSHGSMDKTQKQSSEWAANQKHNQRVENTRVLMGPAVPAMPPVPSNFPPVPTGTIMSPQLSPFPDHRLRHHPLAHMMPADKNFLAYNMESFKSRVTKACDYCRKRKIRCTEIEPISGKCRNCIKYNKDCTFHFHEELKRRREEALNNKGNGKSVKKPRLDKENKFKDENFDIAVRSRNTSSTDSSPKLHTNLSQEYIGVSAGKSASDKEDTWPDFVPIDRTVLEKIELNHTKVAGKVFVLEEICKNMKGTIEKLAEKSKIDVIDKEYMKRPKRKQYSKALLTKQKMFHFRQNVLSHLTDEEFLSPINEMFTTTFKYSILQTKLVLDFSFRSASSPSSDNILYPLPRLAIAKRLLKNIKCPSLASLLHIVDVDQCLQFADVHFDPAKGRLTSSQAFLLNICLCLGATVTNFEEKQELVDEDNHETYYFEKFELWRLRSFTFLNSVYYYHKLSVARADMTALKALLLLAKFAQQKISASSAVKVLSVAIKVALDLRLNLHSTYEDLELDEIIKRRRLWCYCFSTDKFFSVVLSRPPFLKEENTDVLTDESYVELFRDKILPNLSIKYDDSKLEGVKDIVSVVNLLANHLEYVPYIQSYFLSRLSLIESQIYYSCFSIRTTLDDTLDEIIENVLENQKALDRMRDDLPTILSLENYKENMRILSLDSSKLDFEVSCCTTILLHLRWYHQKITLSLFVISIIGDNLDQRESSRHDIAEIIRRSRLDFKRNCIEVLNILKDFEYYPTVQNEFLYFSLTTVFSMFLYLSEIMVNDEHAMETGYIIGLLRDTHTRMLGSEERCLSVHNLKWQTSLFFYTFFLRSTMEKFNLTSKYAKFYAFDSNYYEGVLNRLVKHTRESKDDMVELLKTSFINKEKMAAFGSFVTEDQEKMEVSFNIFNEITIQDLNFLQFSSIPKLWENKTLEPGEEYHHSNGTNTDNNETTGADDTDDNNNNNNNNNKNGNNSSSTINNNNNNYSNSNNNDNDNNINDDDDDDDDDDDDDDDDDDDDDNDDDYSNNGADDDEEDDDYDRSLFPTGLASLLDASYPERTANDYRDENEQSNKLFEKIEGHLEHGVFFYDRDFFFKNVCVKM 1094 P38181 Nucleoporin NUP170 NUP170 559292 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P38181 UNIPROT D6VPS4 PDB 3I5P PDB 3I5Q Pfam PF03177 Pfam PF08801 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}. P25491 EBI-10420,EBI-11756 P32499 EBI-12401,EBI-11756 P36161 EBI-11722,EBI-11756 Self EBI-11756,EBI-11756 Q02630 EBI-11703,EBI-11756 Q02629 EBI-11698,EBI-11756 P48837 EBI-11756,EBI-12324 P32597 EBI-18410,EBI-11756 Q03790 EBI-27321,EBI-11756 P11938 EBI-14821,EBI-11756 P11978 EBI-11756,EBI-17237 Q00684 EBI-4192,EBI-11756 P14832 EBI-5463,EBI-11756 P22696 EBI-6679,EBI-11756 P10591 EBI-8591,EBI-11756 P11484 EBI-8627,EBI-11756 P40358 EBI-11756,EBI-25940 P39929 EBI-11756,EBI-17554 Q03281 EBI-22131,EBI-11756 Q03707 EBI-11756,EBI-18064 P40064 EBI-11740,EBI-11756 P49687 EBI-11756,EBI-11730 Q04477 EBI-27228,EBI-11756 P38305 EBI-20939,EBI-11756 Q12315 EBI-7635,EBI-11756 GO:0031965 GO:0005643 GO:0044611 GO:0003682 GO:1990841 GO:0044877 GO:0017056 GO:0006342 GO:0007059 GO:0016458 GO:0070869 GO:0051028 GO:0051292 GO:0006913 GO:0016584 GO:0006606 GO:0036228 GO:0006405 GO:0034398 GO:0000972 MFQSFFHNNGPAAAGETFSDSRSYPLTNHQEVPRNGLNELASSATKAQQQPTHILNSYPITGSNPLMRASAMGATSGSINPNMSNMNEHIRVSGMGTSKPLDLAGKYIDHLQHKDSNTPVLDERSYYNSGVDYNFSREKNGLGAFTPFEKQDVFNIPDEILHEFSTSQTKTDMGIFPELNRCWITIDNKLILWNINNDNEYQVVDDMKHTIQKVALVRPKPNTFVPAVKHLLLISTTMELFMFAISLDKATNELSVFNTHLSVPVQGIDVIDIVSHERSGRIFFAGQASGLNIWELHYSGSDDWFNSKCSKVCLTKSALLSLLPTNMLSQIPGVDFIQALFEDNSNGNGGFSQETITQLTIDQQRGIIYSLSSKSTIRAYVITEKSLEGPMSIEPAYISRIIGTTTARAAPILGPKYLKIVKISSVAPEENNNLFLVALTVGGVRLYFNGSMGRFNIEALRLESIKFPPSSVTPEVIQQELLHQQQEQAKRSFPFFSNLMSSEPVLLKFQKKSSVLLETTKASTIISPGIFFSAVIKSSQQTHQQEKKENSSVTGTTATAGSKTVKQQPVTLQHKLFVSVPDYGILKTHGKYVENATFLETAGPVQQIIPLSGLFNATTKPQGFANEFATQYTSETLRVAVLTSTSIEIYKYRTPDEIFEDLIDNPLPFVLNYGAAEACSTALFVTCKSNKSEKLRSNALTFLTMGIPGVVDIKPVYNRYSVSTVSSLLSKPTLSTATTNLQQSITGFSKPSPANKEDFDLDDVILSPRFYGIALLITRLLRDIWGRHVFMTFTDNRVTSHAFISSSDPITPSINNLKSDEISQNRNIISKVSISKDCIEYYLSSINILNEFFITYGDSISQISAPYVLANNSNGRVIDKTEEVANQAESIAINAMIKMVQSIKEGLSFLNVLYEESEVEGFDNQYLGFKDIISFVSLDVQKDLVKLDFKDLFAPNDKTKSLIREILLSIINRNITKGASIEYTATALQERCGSFCSASDILGFRAIEHLRRAKEIGLRNYDSLNYHLKNATALLEQIVDDLSIEKLKEAVSMMLSVNYYPKSIEFLLNIANSMDKGKLACQYVANGFLENDDRKQYYDKRILVYDLVFDTLIKVDELAEKKQSSKTQNQISISNDDEVKLRQKSYEAALKYNDRLFHYHMYDWLVSQNREEKLLDIETPFILPYLMEKAGSSLKISNILWVYYSRRSKFFESAEILYRLATSNFDITLFERIEFLSRANGFCNSVSPLSQKQRIVQLASRIQDACEVAGIQGDILSLVYTDARIDSAIKDELIKTLDGKILSTSELFNDFAVPLSYHEIALFIFKIADFRDHEVIMAKWDELFQSLRMEFNNTGKKEDSMNFINLLSNVLIKIGKNVQDSEFIFPIFELFPIVCNFFYETLPKEHIVSGSIVSIFITAGVSFNKMYYILKELIETSDSDNSVFNKEMTWLIHEWYKSDRKFRDIISYNDIIHLKEYKIDNDPIEKYVKNSGNNLGICFYKE 1502 P38217 Importin subunit beta-2 KAP104 559292 Yes SL-0178 SL-0185 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}. UNIPROT P38217 UNIPROT D6VQ19 Pfam PF02985 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}. P22147 EBI-9152,EBI-9642 P25491 EBI-9152,EBI-10420 P10591 EBI-8591,EBI-9152 P32589 EBI-9152,EBI-8648 P46988 EBI-9152,EBI-13224 P33416 EBI-8680,EBI-9152 P11484 EBI-8627,EBI-9152 P40150 EBI-9152,EBI-8632 P25303 EBI-16711,EBI-9152 P23641 EBI-11178,EBI-9152 P32340 EBI-11961,EBI-9152 P04840 EBI-13686,EBI-9152 P50085 EBI-23530,EBI-9152 P53045 EBI-6506,EBI-9152 Q04182 EBI-13072,EBI-9152 Q99190 EBI-31149,EBI-9152 P18414 EBI-6526,EBI-9152 P53217 EBI-23120,EBI-9152 P16140 EBI-9152,EBI-20254 P07259 EBI-9152,EBI-14372 P02557 EBI-9152,EBI-18986 P09733 EBI-9152,EBI-18976 P02994 EBI-9152,EBI-6314 P10592 EBI-9152,EBI-8603 P05756 EBI-9152,EBI-16054 P46654 EBI-9152,EBI-16037 P05317 EBI-9152,EBI-15447 P26321 EBI-9152,EBI-15398 P41940 EBI-9152,EBI-11191 P32505 EBI-9152,EBI-11770 P40069 EBI-9152,EBI-9166 Q99383 EBI-9152,EBI-11783 P33892 EBI-9152,EBI-7442 P38737 EBI-9152,EBI-24359 Q03690 EBI-9152,EBI-8989 P40035 EBI-22551,EBI-9152 P40970 EBI-10067,EBI-9152 P19414 EBI-2104,EBI-9152 P37898 EBI-1998,EBI-9152 GO:0005935 GO:0005934 GO:0005737 GO:0005829 GO:0005643 GO:0005634 GO:0061608 GO:0008139 GO:0010458 GO:0051028 GO:0006606 MASTWKPAEDYVLQLATLLQNCMSPNPEIRNNAMEAMENFQLQPEFLNYLCYILIEGESDDVLKQHYSLQDLQNNRATAGMLLKNSMLGGNNLIKSNSHDLGYVKSNIIHGLYNSNNNLVSNVTGIVITTLFSTYYRQHRDDPTGLQMLYQLLELTSNGNEPSIKALSKIMEDSAQFFQLEWSGNTKPMEALLDSFFRFISNPNFSPVIRSESVKCINTVIPLQTQSFIVRLDKFLEIIFQLAQNDENDLVRAQICISFSFLLEFRPDKLVSHLDGIVQFMLHLITTVNEEKVAIEACEFLHAFATSPNIPEHILQPYVKDIVPILLSKMVYNEESIVLLEASNDDDAFLEDKDEDIKPIAPRIVKKKEAGNGEDADDNEDDDDDDDDEDGDVDTQWNLRKCSAATLDVMTNILPHQVMDIAFPFLREHLGSDRWFIREATILALGAMAEGGMKYFNDGLPALIPFLVEQLNDKWAPVRKMTCWTLSRFSPWILQDHTEFLIPVLEPIINTLMDKKKDVQEAAISSVAVFIENADSELVETLFYSQLLTSFDKCLKYYKKKNLIILYDAIGRFAEKCALDETAMQIILPPLIEKWALLSDSDKELWPLLECLSCVASSLGERFMPMAPEVYNRAFRILCHCVELEAKSHQDPTIVVPEKDFIITSLDLIDGLVQGLGAHSQDLLFPQGTKDLTILKIMLECLQDPVHEVRQSCFALLGDIVYFFNSELVIGNLEDFLKLIGTEIMHNDDSDGTPAVINAIWALGLISERIDLNTYIIDMSRIILDLFTTNTQIVDSSVMENLSVTIGKMGLTHPEVFSSGAFANDSNWNKWCLSVNALDDVEEKSSAYMGFLKIINLTSTEVTMSNDTIHKIVTGLSSNVEANVFAQEIYTFLMNHSAQISAINFTPDEISFLQQFTS 918 P38242 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 559292 Yes SL-0178 SL-0182 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}. UNIPROT P38242 UNIPROT D6VQ69 Pfam PF08660 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}. P11484 EBI-8627,EBI-21477 P32589 EBI-21477,EBI-8648 P10591 EBI-21477,EBI-8591 P25294 EBI-21477,EBI-17244 P10592 EBI-21477,EBI-8603 P40069 EBI-21477,EBI-9166 GO:0030176 GO:0031227 GO:0031965 GO:0042175 GO:0043541 GO:0043495 GO:0006488 MKTAYLASLVLIVSTAYVIRLIAILPFFHTQAGTEKDTKDGVNLLKIRKSSKKPLKIFVFLGSGGHTGEMIRLLENYQDLLLGKSIVYLGYSDEASRQRFAHFIKKFGHCKVKYYEFMKAREVKATLLQSVKTIIGTLVQSFVHVVRIRFAMCGSPHLFLLNGPGTCCIISFWLKIMELLLPLLGSSHIVYVESLARINTPSLTGKILYWVVDEFIVQWQELRDNYLPRSKWFGILV 237 P38757 Nuclear envelope morphology protein 1 NEM1 559292 Yes SL-0178 SL-0182 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}. UNIPROT P38757 UNIPROT D3DKU7 Pfam PF03031 PROSITE PS50969 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}. P18410 EBI-17857,EBI-24435 P38074 EBI-8394,EBI-24435 GO:0005789 GO:0016021 GO:0005811 GO:0005739 GO:0071595 GO:0031965 GO:0004721 GO:0071072 GO:0006998 GO:1903740 GO:0006470 GO:0071071 MNALKYFSNHLITTKKQKKINVEVTKNQDLLGPSKEVSNKYTSHSENDCVSEVDQQYDHSSSHLKESDQNQERKNSVPKKPKALRSILIEKIASILWALLLFLPYYLIIKPLMSLWFVFTFPLSVIERRVKHTDKRNRGSNASENELPVSSSNINDSSEKTNPKNCNLNTIPEAVEDDLNASDEIILQRDNVKGSLLRAQSVKSRPRSYSKSELSLSNHSSSNTVFGTKRMGRFLFPKKLIPKSVLNTQKKKKLVIDLDETLIHSASRSTTHSNSSQGHLVEVKFGLSGIRTLYFIHKRPYCDLFLTKVSKWYDLIIFTASMKEYADPVIDWLESSFPSSFSKRYYRSDCVLRDGVGYIKDLSIVKDSEENGKGSSSSLDDVIIIDNSPVSYAMNVDNAIQVEGWISDPTDTDLLNLLPFLEAMRYSTDVRNILALKHGEKAFNIN 446 P38770 Nucleus export protein BRL1 BRL1 559292 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:15882446}; Multi-pass membrane protein {ECO:0000269|PubMed:15882446}. UNIPROT P38770 UNIPROT D3DKY3 Pfam PF10104 Involved in mRNA and protein export from nucleus. {ECO:0000269|PubMed:15882446}. P46985 EBI-24507,EBI-11052 Q12329 EBI-8571,EBI-24507 P32589 EBI-24507,EBI-8648 P11484 EBI-24507,EBI-8627 P33416 EBI-24507,EBI-8680 P10592 EBI-24507,EBI-8603 P10591 EBI-24507,EBI-8591 Q9BXL8 EBI-1773949,EBI-24507 Q9UJW9 EBI-24507,EBI-748621 P02829 EBI-24507,EBI-8659 P16140 EBI-24507,EBI-20254 P09733 EBI-24507,EBI-18976 P12709 EBI-24507,EBI-7238 P06169 EBI-24507,EBI-5687 P04147 EBI-24507,EBI-12823 P15108 EBI-24507,EBI-8666 P47088 EBI-24507,EBI-26307 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 GO:0015031 MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRNTLDFSAAKADEEEDDRMEIDEVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQKQEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAATKVEGVVPLPPSANQDDNESSNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNTHNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQLFLNAITTVVIFSFILSFIIALQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPALGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFIDPLNWKTLFVIFCGVITWCFSSNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ 471 P39015 Suppressor protein STM1 STM1 559292 Yes SL-0198 Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Concentrated in the perinuclear region. UNIPROT P39015 UNIPROT D6VYE5 PDB 4U3M PDB 4U3N PDB 4U3U PDB 4U4N PDB 4U4O PDB 4U4Q PDB 4U4R PDB 4U4U PDB 4U4Y PDB 4U4Z PDB 4U50 PDB 4U51 PDB 4U52 PDB 4U53 PDB 4U55 PDB 4U56 PDB 4U6F PDB 4V88 PDB 4V8Y PDB 4V8Z PDB 5DAT PDB 5DC3 PDB 5DGE PDB 5FCI PDB 5FCJ PDB 5I4L PDB 5LYB PDB 5NDG PDB 5NDV PDB 5NDW PDB 5OBM PDB 5TGA PDB 5TGM PDB 6HHQ Pfam PF09598 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}. P30822 EBI-20589,EBI-11238 P39940 EBI-11238,EBI-16219 P43582 EBI-11238,EBI-22766 P40318 EBI-11238,EBI-18208 P46995 EBI-11238,EBI-16985 P22696 EBI-11238,EBI-6679 P33203 EBI-11238,EBI-701 Q06525 EBI-11238,EBI-35138 P10591 EBI-8591,EBI-11238 P40454 EBI-25278,EBI-11238 P11484 EBI-11238,EBI-8627 P38788 EBI-11238,EBI-24570 P40150 EBI-11238,EBI-8632 P22943 EBI-8548,EBI-11238 P25294 EBI-17244,EBI-11238 Q08687 EBI-34720,EBI-11238 P32790 EBI-17313,EBI-11238 P38199 EBI-21217,EBI-11238 P07280 EBI-14536,EBI-11238 P38968 EBI-20524,EBI-11238 P11632 EBI-12019,EBI-11238 P38700 EBI-2705,EBI-11238 P32357 EBI-340,EBI-11238 P38285 EBI-20853,EBI-11238 P40522 EBI-11238,EBI-25035 Q12389 EBI-5644,EBI-11238 P00330 EBI-2218,EBI-11238 Q02486 EBI-2028,EBI-11238 P02293 EBI-8088,EBI-11238 P38822 EBI-3889,EBI-11238 Q12114 EBI-4640,EBI-11238 P07270 EBI-13378,EBI-11238 P22082 EBI-17526,EBI-11238 GO:0005737 GO:0005634 GO:0048471 GO:0005844 GO:0003677 GO:0043022 GO:0042162 GO:0045142 GO:0043066 GO:0043558 GO:0000723 GO:0031929 GO:0006414 MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA 273 P39547 ULP1-interacting protein 3 UIP3 559292 Yes SL-0178 SL-0182 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}. UNIPROT P39547 UNIPROT D6VPM9 Pfam PF00674 DE Reference Proteome: Yes; Self EBI-20760,EBI-20760 Q12743 EBI-33192,EBI-20760 O13540 EBI-31374,EBI-20760 P39548 EBI-20760,EBI-2344928 P47111 EBI-20760,EBI-25497 P53868 EBI-2490,EBI-20760 P38226 EBI-20760,EBI-21429 P06197 EBI-13458,EBI-20760 Q02724 EBI-20050,EBI-20760 Q06144 EBI-34916,EBI-20760 P40107 EBI-7764,EBI-20760 P40857 EBI-20760,EBI-26003 P46956 EBI-20760,EBI-13337 P53142 EBI-20760,EBI-23899 P32453 EBI-3306,EBI-20760 P53845 EBI-28230,EBI-20760 P53337 EBI-20760,EBI-23662 P32621 EBI-20760,EBI-7511 Q12016 EBI-20760,EBI-29309 Q03860 EBI-37537,EBI-20760 Q04767 EBI-20760,EBI-28141 P47088 EBI-26307,EBI-20760 Q8TGQ7 EBI-20760,EBI-2343396 Q04969 EBI-27827,EBI-20760 P02829 EBI-8659,EBI-20760 Q9BSE2 EBI-8649725,EBI-20760 GO:0005783 GO:0000329 GO:0005794 GO:0016021 GO:0005635 GO:0031965 GO:0005886 GO:0016050 MQTPSENTDVKLDTLDEPSAHLIEENVALPEDTFNSYWSYILNEIARCKPLMIMFLIPVCLVLLITFFHDIKGILVFLVISLILSIIILLIGITAFVSETLNKGFIIKLLVEVITRKPAVGGKEWRIIAYNMNQYLFDHGIWHTPYYFFCEHRCHKFFKSLIKQTRSNAHLSSPTNGAENTQSNTPAKEVSNEMVKPYIFSSDPVLEAYLIKAAEIHKEAEFEYWRKQYPEVDLP 235 P39685 Nucleoporin POM152 POM152 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex. UNIPROT P39685 UNIPROT D6VZV2 PDB 5TVZ 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}. P11484 EBI-12739,EBI-8627 P39102 EBI-12739,EBI-20578 P39078 EBI-19054,EBI-12739 P32589 EBI-8648,EBI-12739 P15108 EBI-8666,EBI-12739 P10592 EBI-8603,EBI-12739 P40358 EBI-25940,EBI-12739 P10591 EBI-12739,EBI-8591 P02994 EBI-6314,EBI-12739 Q12158 EBI-16655,EBI-12739 P38305 EBI-20939,EBI-12739 GO:0071944 GO:0016021 GO:0005739 GO:0005641 GO:0031965 GO:0034399 GO:0005643 GO:0070762 GO:0043495 GO:0017056 GO:0051028 GO:0006999 GO:0006913 GO:0006606 GO:0030474 MEHRYNVFNDTPRGNHWMGSSVSGSPRPSYSSRPNVNTTRRFQYSDDEPAEKIRPLRSRSFKSTESNISDEKSRISERDSKDRYINGDKKVDIYSLPLISTDVLEISKQRTFAVILFLIIQCYKIYDLVILKSGLPLSGLLFKNYRFNFISKYFIIDSFFLYVLPSFNIPRLTFKPWVVYLQILAMLLLNIFISSDHEFVLISLIMTTWRKLYTKELSVTGSAINHHRIFDSSAHFKGALTIKILPENTAMFNPLHESYCLPMDTNLFKINSIDVPIRINSTEEIEYIELEYRDLYTNSVELRSLSKKDFKIIDNPKSFLKKDQSVLKSHSNDFEEGSTIRYLAVTLQDIGFYQIKKIVDSKKLNLKIHQSHLVVPYCPIASITGTGSNDRCIGDSDNVSFEIQGVPPMKLAYSKIVNGQTFSYVDSSLQPEYFESPLQSSKSKQSFTQGELNDLKWGRNQPVNINLDSSITQDGKFAYKIDKITDGLGNVVDFTSLPEELKKRYDLSYNFNVHEVPRAALEERFDPKSPTKRSIAIVFEEIKNWISDIPYVISLSYTDAQDKSKKIMNVTTDSLTKVLQADLPGSYNLEYIESKFCPGEIVGKSNVLVTMPVAPTMEVKSFPILDQCVGQVGLNFELSFTGAPPYYYNTKIYKLENGERKLYDAKRYTSEGTRNRFSYSPPKEGNYEIVFDTVSNKLFTEPIKLEPVKEYTFKTSMRVKPSASLKLHHDLKLCLGDHSSVPVALKGQGPFTLTYDIIETFSSKRKTFEIKEIKTNEYVIKTPVFTTGGDYILSLVSIKDSTGCVVGLSQPDAKIQVRRDIPSAAFNFFEPIKEAKIKHGSVTEIPLKLSGEGPFTVKFKHMDYDGNIVKEFENKFQNSYKPALKVSKEGLYQLVDIRDSSCQGNVIYRNSLYKVSFLEKPKFAIQDNHHITKVTENLFSKEEVCQGMEGTVDLALFGSPPFILEYDLMAPNGHISTKKIQVATKYASLKLPNQIPGEYITTIKAIFDGNYGESDIHFREHQSELIIKQTVHPIPDVAFADGGKTLRACAANVDQISFLEPINLKFLQGESPFSITFSVYHESTSRTDQYTIDNIDSENFSFEKLYEGMKLGNHAITIDSVVDANGCVNSLISGPRNQILVSITDAPKIHILDPSTEYCVGDYVAYQLNGVAPFMIKYEFNGIPLKSKERSSQFVRLASEPGIISITSLQDSSSQCIVDFTNPKLKSEFDDLSLNIHPIPSVTVSQGNYVTEDIREGDQAEVIFSFEGTPPFSLTYVRTEETDGKHGKRRSQVVETHKVTDIYSHEYKVITSLQGTYEAIEITDAYCFAKNDLFFNN 1337 P39705 Nucleoporin NUP60 NUP60 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Nuclear basket. UNIPROT P39705 UNIPROT D6VPL6 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}. P25491 EBI-20731,EBI-10420 P32499 EBI-12401,EBI-20731 Q06142 EBI-9145,EBI-20731 P36016 EBI-20731,EBI-10154 P11484 EBI-20731,EBI-8627 P10592 EBI-8603,EBI-20731 P33416 EBI-8680,EBI-20731 P40358 EBI-20731,EBI-25940 P10591 EBI-20731,EBI-8591 Q02336 EBI-2186,EBI-20731 P50102 EBI-19863,EBI-20731 Q02821 EBI-20731,EBI-1797 P40069 EBI-9166,EBI-20731 Q12449 EBI-37072,EBI-20731 P28003 EBI-20647,EBI-20731 P38305 EBI-20939,EBI-20731 Q12315 EBI-7635,EBI-20731 GO:0005829 GO:0031965 GO:0005643 GO:0044613 GO:0044615 GO:0005634 GO:0005543 GO:0017056 GO:0030466 GO:0051276 GO:0006302 GO:0008298 GO:0031990 GO:0006607 GO:0006913 GO:0016973 GO:0000973 GO:0006611 GO:0060188 GO:0034398 GO:0000972 MHRKSLRRASATVPSAPYRKQIISNAHNKPSLFSKIKTFFTQKDSARVSPRNNVANKQPRNESFNRRISSMPGGYFHSEISPDSTVNRSVVVSAVGEARNDIENKEEEYDETHETNISNAKLANFFSKKGNEPLSEIEIEGVMSLLQKSSKSMITSEGEQKSAEGNNIDQSLILKESGSTPISISNAPTFNPKYDTSNASMNTTLGSIGSRKYSFNYSSLPSPYKTTVYRYSAAKKIPDTYTANTSAQSIASAKSVRSGVSKSAPSKKISNTAAALVSLLDENDSKKNNAASELANPYSSYVSQIRKHKRVSPNAAPRQEISEEETTVKPLFQNVPEQGEEPMKQLNATKISPSAPSKDSFTKYKPARSSSLRSNVVVAETSPEKKDGGDKPPSSAFNFSFNTSRNVEPTENAYKSENAPSASSKEFNFTNLQAKPLVGKPKTELTKGDSTPVQPDLSVTPQKSSSKGFVFNSVQKKSRSNLSQENDNEGKHISASIDNDFSEEKAEEFDFNVPVVSKQLGNGLVDENKVEAFKSLYTF 539 P39929 Vacuolar-sorting protein SNF7 SNF7 559292 Yes SL-0178 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}. UNIPROT P39929 UNIPROT D6VY27 UNIPROT E9P8V6 PDB 5FD7 PDB 5FD9 PDB 5T8L PDB 5T8N Pfam PF03357 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}. P38181 EBI-11756,EBI-17554 Self EBI-17554,EBI-17554 Q04272 EBI-17554,EBI-28157 Q02796 EBI-30514,EBI-17554 Q07979 EBI-36549,EBI-17554 P40340 EBI-19030,EBI-17554 P10591 EBI-17554,EBI-8591 P11484 EBI-17554,EBI-8627 Q05931 EBI-17554,EBI-35227 P10592 EBI-8603,EBI-17554 P32447 EBI-3003,EBI-17554 Q12495 EBI-3913,EBI-17554 Q03281 EBI-22131,EBI-17554 Q03707 EBI-17554,EBI-18064 P48582 EBI-17554,EBI-3768 P36108 EBI-26574,EBI-17554 Q12483 EBI-17554,EBI-30277 P47142 EBI-17554,EBI-25595 Q06696 EBI-17554,EBI-36540 P08539 EBI-17554,EBI-7376 P52917 EBI-20475,EBI-17554 Q08817 EBI-17554,EBI-30849 GO:0005737 GO:0000815 GO:0005635 GO:0005886 GO:0042802 GO:1904669 GO:0071454 GO:1904902 GO:0070676 GO:0045324 GO:0015031 GO:0061709 GO:0043162 MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKVEGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDEDELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL 240 P39962 Casein kinase I homolog 3 YCK3 559292 Yes SL-0178 SL-0182 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. UNIPROT P39962 UNIPROT D3DM29 Pfam PF00069 PROSITE PS50011 PROSITE PS00108 Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. P50222 EBI-748397,EBI-4740 GO:0005737 GO:0000324 GO:0000329 GO:0031965 GO:0005634 GO:0005886 GO:0005524 GO:0004672 GO:0004674 GO:0018105 GO:0006468 GO:0016192 MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRILNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQYQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLGHVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALRLNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKSRISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTNLANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC 524 P39996 Glutathione transferase 3 GTT3 559292 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. UNIPROT P39996 UNIPROT D3DLN3 DE Reference Proteome: Yes; P48363 EBI-13239,EBI-22308 P40150 EBI-8632,EBI-22308 P02829 EBI-8659,EBI-22308 Q8N6G5 EBI-22308,EBI-10267100 Q8N6L0 EBI-749265,EBI-22308 P00359 EBI-22308,EBI-7218 P32324 EBI-22308,EBI-6333 P00330 EBI-22308,EBI-2218 P47088 EBI-22308,EBI-26307 Q02159 EBI-22308,EBI-19749 GO:0016021 GO:0016020 GO:0031965 GO:0034399 MPTKSTFSRWKKADLIDLANKLEIDGFPNYAKKSDMIDYLESHLNHLEKPVDFKDDYPELRSFYESMTVDQSKDERNEYGSGSGNGSGSGSCDTATNDSDLEKAYIKEDDDEKPQSGDETSATKPLSSRNANSNAKTNFNLLDFSTDNDSSTSAFTKFKFNFQEYLSDIRYQTQKLNENVQDYLSTISAVDTIFSLLEFSFLVRNILAAGQPTSSSSLASSLEAAVAAHNKYQYTLDFCLPILTWLLFFRGIPTLVSYYINFIRYDLNIELDPMTFNLTKFLISLAIFKTCNNKNIDFHSFRCVNQLWTQLCTVNRSLGMVPLVFSMVSCLLTLYVL 337 P40064 Nucleoporin NUP157 NUP157 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P40064 UNIPROT D3DM12 PDB 4MHC Pfam PF03177 Pfam PF08801 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}. P25491 EBI-11740,EBI-10420 P38181 EBI-11740,EBI-11756 P11978 EBI-11740,EBI-17237 P11484 EBI-8627,EBI-11740 P32589 EBI-11740,EBI-8648 P02829 EBI-8659,EBI-11740 P10591 EBI-11740,EBI-8591 Q03790 EBI-27321,EBI-11740 P39081 EBI-11740,EBI-12980 P47007 EBI-11740,EBI-26105 Q08817 EBI-11740,EBI-30849 P38305 EBI-20939,EBI-11740 Q12315 EBI-7635,EBI-11740 GO:0031965 GO:0005643 GO:0044611 GO:0003677 GO:0003723 GO:0017056 GO:0051028 GO:0051292 GO:0006913 GO:0000973 GO:0006606 GO:0036228 GO:0006405 GO:0000972 MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHVKISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIKSDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDRTHELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPSIPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLSNRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDTGPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTALLDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEACSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLFSQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALILLINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTSADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQPKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLKKRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALASSDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVLPLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTDVVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGSIAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK 1391 P40066 Nucleoporin GLE2 GLE2 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P40066 UNIPROT D3DM14 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. P14907 EBI-22648,EBI-12265 P34077 EBI-22648,EBI-12056 P22696 EBI-6679,EBI-22648 P38915 EBI-17964,EBI-22648 P53040 EBI-18876,EBI-22648 P38129 EBI-18868,EBI-22648 P35177 EBI-17958,EBI-22648 Q03330 EBI-7458,EBI-22648 P11484 EBI-22648,EBI-8627 P10591 EBI-22648,EBI-8591 P40368 EBI-22648,EBI-12331 P40477 EBI-22648,EBI-11747 Q02630 EBI-22648,EBI-11703 P10592 EBI-22648,EBI-8603 P47054 EBI-22648,EBI-25846 P48837 EBI-22648,EBI-12324 Q04599 EBI-22648,EBI-38719 P36516 EBI-22648,EBI-387 P22353 EBI-22648,EBI-407 P36523 EBI-22648,EBI-15518 P36525 EBI-22648,EBI-15545 Q06678 EBI-22648,EBI-392 P38305 EBI-20939,EBI-22648 Q12315 EBI-7635,EBI-22648 GO:0005737 GO:0031965 GO:0005643 GO:0003723 GO:0043130 GO:0031081 GO:0016973 GO:0000973 GO:2000728 GO:0006405 GO:0000972 MSFFNRSNTTSALGTSTAMANEKDLANDIVINSPAEDSISDIAFSPQQDFMFSASSWDGKVRIWDVQNGVPQGRAQHESSSPVLCTRWSNDGTKVASGGCDNALKLYDIASGQTQQIGMHSAPIKVLRFVQCGPSNTECIVTGSWDKTIKYWDMRQPQPVSTVMMPERVYSMDNKQSLLVVATAERHIAIINLANPTTIFKATTSPLKWQTRCVACYNEADGYAIGSVEGRCSIRYIDDGMQKKSGFSFKCHRQTNPNRAPGSNGQSLVYPVNSIAFHPLYGTFVTAGGDGTFNFWDKNQRHRLKGYPTLQASIPVCSFNRNGSVFAYALSYDWHQGHMGNRPDYPNVIRLHATTDEEVKEKKKR 365 P40069 Importin subunit beta-4 KAP123 559292 Yes SL-0178 SL-0185 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}. UNIPROT P40069 UNIPROT D3DM16 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. P12683 EBI-8377,EBI-9166 P12684 EBI-8384,EBI-9166 P32499 EBI-12401,EBI-9166 P34077 EBI-12056,EBI-9166 P38217 EBI-9152,EBI-9166 P38242 EBI-21477,EBI-9166 P39705 EBI-9166,EBI-20731 P10591 EBI-8591,EBI-9166 P02309 EBI-8113,EBI-9166 P61830 EBI-8098,EBI-9166 P04912 EBI-8076,EBI-9166 Q12692 EBI-8080,EBI-9166 Q12529 EBI-2887498,EBI-9166 P40340 EBI-19030,EBI-9166 P11484 EBI-9166,EBI-8627 P32835 EBI-7926,EBI-9166 Q04477 EBI-27228,EBI-9166 P46675 EBI-18471,EBI-9166 P52910 EBI-2136,EBI-9166 P42842 EBI-28374,EBI-9166 P11075 EBI-16882,EBI-9166 P38152 EBI-19672,EBI-9166 P25360 EBI-13344,EBI-9166 P35200 EBI-11337,EBI-9166 P39004 EBI-8790,EBI-9166 P40319 EBI-6423,EBI-9166 P32340 EBI-11961,EBI-9166 P39715 EBI-6302,EBI-9166 P07246 EBI-2227,EBI-9166 Q05881 EBI-37369,EBI-9166 P32502 EBI-6260,EBI-9166 Q12449 EBI-37072,EBI-9166 P25454 EBI-14709,EBI-9166 P21304 EBI-14328,EBI-9166 P46956 EBI-13337,EBI-9166 P13663 EBI-5803,EBI-9166 P32476 EBI-6545,EBI-9166 P32467 EBI-8774,EBI-9166 P32803 EBI-6431,EBI-9166 P38853 EBI-9619,EBI-9166 P28496 EBI-26585,EBI-9166 P04840 EBI-13686,EBI-9166 P53965 EBI-28668,EBI-9166 P22211 EBI-12207,EBI-9166 P00546 EBI-4253,EBI-9166 P40499 EBI-25109,EBI-9166 P53045 EBI-6506,EBI-9166 Q04182 EBI-13072,EBI-9166 Q02336 EBI-2186,EBI-9166 P40495 EBI-25128,EBI-9166 P50108 EBI-11043,EBI-9166 P33748 EBI-11407,EBI-9166 P46985 EBI-11052,EBI-9166 P22202 EBI-8621,EBI-9166 P32903 EBI-13545,EBI-9166 Q02785 EBI-13065,EBI-9166 P38310 EBI-20959,EBI-9166 P36013 EBI-10412,EBI-9166 P38085 EBI-20222,EBI-9166 P20107 EBI-29667,EBI-9166 P53742 EBI-28532,EBI-9166 P07262 EBI-5823,EBI-9166 P32454 EBI-2641,EBI-9166 P35723 EBI-26730,EBI-9166 P32905 EBI-16032,EBI-9166 P33441 EBI-10841,EBI-9166 P21147 EBI-2098,EBI-9166 P39522 EBI-9078,EBI-9166 P48563 EBI-28333,EBI-9166 P40416 EBI-3181,EBI-9166 P41940 EBI-11191,EBI-9166 P32629 EBI-2595,EBI-9166 P28003 EBI-20647,EBI-9166 Q07560 EBI-5153,EBI-9166 P16550 EBI-2631,EBI-9166 P38687 EBI-18004,EBI-9166 P23500 EBI-11297,EBI-9166 P05626 EBI-9166,EBI-3264 P53881 EBI-29042,EBI-9166 Q07084 EBI-18184,EBI-9166 Q07804 EBI-36254,EBI-9166 P38707 EBI-18775,EBI-9166 P36148 EBI-26471,EBI-9166 P12385 EBI-6533,EBI-9166 P54837 EBI-6642,EBI-9166 P38703 EBI-10035,EBI-9166 P29496 EBI-10549,EBI-9166 Q99190 EBI-31149,EBI-9166 P32798 EBI-5006,EBI-9166 P18414 EBI-6526,EBI-9166 P40060 EBI-22617,EBI-9166 Q12029 EBI-34730,EBI-9166 Q04013 EBI-24564,EBI-9166 Q12345 EBI-35758,EBI-9166 Q06616 EBI-36065,EBI-9166 P36008 EBI-6329,EBI-9166 P53217 EBI-23120,EBI-9166 P39704 EBI-6587,EBI-9166 P32843 EBI-15626,EBI-9166 P0CI39 EBI-18360,EBI-9166 Q12680 EBI-7727,EBI-9166 P22215 EBI-17397,EBI-9166 Q03771 EBI-36525,EBI-9166 Q02821 EBI-1797,EBI-9166 P38719 EBI-5633,EBI-9166 P35191 EBI-10603,EBI-9166 P39743 EBI-14500,EBI-9166 P40541 EBI-16667,EBI-9166 P33333 EBI-13494,EBI-9166 Q04062 EBI-15944,EBI-9166 P27929 EBI-11843,EBI-9166 P38689 EBI-9877,EBI-9166 P40081 EBI-22701,EBI-9166 P51998 EBI-450,EBI-9166 P47054 EBI-25846,EBI-9166 P52593 EBI-11763,EBI-9166 Q03529 EBI-16747,EBI-9166 P32492 EBI-11681,EBI-9166 P41805 EBI-9166,EBI-15270 P40010 EBI-9166,EBI-22449 Q06142 EBI-9166,EBI-9145 P25605 EBI-9166,EBI-9087 P28241 EBI-9166,EBI-8883 P33892 EBI-9166,EBI-7442 Q12159 EBI-9166,EBI-29516 P07259 EBI-9166,EBI-14372 P10081 EBI-9166,EBI-9017 P02994 EBI-9166,EBI-6314 P40150 EBI-9166,EBI-8632 P10592 EBI-9166,EBI-8603 Q12464 EBI-9166,EBI-31814 P26783 EBI-9166,EBI-16150 P23248 EBI-9166,EBI-16136 P33442 EBI-9166,EBI-16132 P32566 EBI-17452,EBI-9166 P39011 EBI-3544,EBI-9166 Q04305 EBI-28183,EBI-9166 P39969 EBI-3727,EBI-9166 P40035 EBI-22551,EBI-9166 Q12296 EBI-33338,EBI-9166 P40970 EBI-10067,EBI-9166 P38264 EBI-13350,EBI-9166 P39676 EBI-6905,EBI-9166 P19262 EBI-12464,EBI-9166 Q06338 EBI-33582,EBI-9166 P54115 EBI-5798,EBI-9166 P18239 EBI-2293,EBI-9166 P16522 EBI-4216,EBI-9166 P53012 EBI-16742,EBI-9166 P36046 EBI-26978,EBI-9166 Q02776 EBI-30302,EBI-9166 P47077 EBI-25778,EBI-9166 P47026 EBI-25989,EBI-9166 P38720 EBI-1965,EBI-9166 GO:0005737 GO:0010494 GO:0005643 GO:0005634 GO:0061608 GO:0008139 GO:0008536 GO:0051028 GO:0006607 GO:0006606 GO:2000220 MDQQFLSQLEQTLHAITSGVGLKEATKTLQTQFYTQPTTLPALIHILQNGSDDSLKQLAGVEARKLVSKHWNAIDESTRASIKTSLLQTAFSEPKENVRHSNARVIASIGTEELDGNKWPDLVPNLIQTASGEDVQTRQTAIFILFSLLEDFTSSLSGHIDDFLALFSQTINDPSSLEIRSLSAQALNHVSALIEEQETINPVQAQKFAASIPSVVNVLDAVIKADDTMNAKLIFNCLNDFLLLDSQLTGNFIVDLIKLSLQIAVNSEIDEDVRVFALQFIISSLSYRKSKVSQSKLGPEITVAALKVACEEIDVDDELNNEDETGENEENTPSSSAIRLLAFASSELPPSQVASVIVEHIPAMLQSANVFERRAILLAISVAVTGSPDYILSQFDKIIPATINGLKDTEPIVKLAALKCIHQLTTDLQDEVAKFHEEYLPLIIDIIDSAKNIVIYNYATVALDGLLEFIAYDAIAKYLDPLMNKLFYMLESNESSKLRCAVVSAIGSAAFAAGSAFIPYFKTSVHYLEKFIQNCSQIEGMSEDDIELRANTFENISTMARAVRSDAFAEFAEPLVNSAYEAIKTDSARLRESGYAFIANLAKVYGENFAPFLKTILPEIFKTLELDEYQFNFDGDAEDLAAFADSANEEELQNKFTVNTGISYEKEVASAALSELALGTKEHFLPYVEQSLKVLNEQVDESYGLRETALNTIWNVVKSVLLASKVEPESYPKGIPASSYVNADVLAVIQAARETSMGNLSDEFETSMVITVMEDFANMIKQFGAIIIMDNGDSSMLEALCMQVLSVLKGTHTCQTIDIEEDVPRDEELDASETEATLQDVALEVLVSLSQALAGDFAKVFDNFRPVVFGLFQSKSKNKRSSAVGAASELALGMKEQNPFVHEMLEALVIRLTSDKSLEVRGNAAYGVGLLCEYASMDISAVYEPVLKALYELLSAADQKALAAEDDEATREIIDRAYANASGCVARMALKNSALVPLEQTVPALLAHLPLNTGFEEYNPIFELIMKLYQENSPVITNETPRIIEIFSAVFTKENDRIKLEKESTLGREENMERLKQFQTEEMKHKVIELLKYLNTTYNGIVAQNPVLAAVIA 1113 P40075 Vesicle-associated membrane protein-associated protein SCS2 SCS2 559292 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Nucleus membrane; Single-pass type IV membrane protein. UNIPROT P40075 UNIPROT D3DM26 Pfam PF00635 PROSITE PS50202 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}. P25491 EBI-16735,EBI-10420 P35845 EBI-16735,EBI-12611 P39523 EBI-16735,EBI-27256 Q07657 EBI-22083,EBI-16735 Q00402 EBI-16735,EBI-12386 Q08229 EBI-16735,EBI-36841 P41940 EBI-16735,EBI-11191 P07149 EBI-16735,EBI-6795 P00330 EBI-16735,EBI-2218 P18759 EBI-16735,EBI-16565 P22137 EBI-16735,EBI-4766 P38616 EBI-16735,EBI-24029 P00950 EBI-16735,EBI-13517 Q03661 EBI-16735,EBI-2346381 P19097 EBI-16735,EBI-6806 P28834 EBI-16735,EBI-8878 P02557 EBI-16735,EBI-18986 P10592 EBI-16735,EBI-8603 P47079 EBI-16735,EBI-19072 P41277 EBI-16735,EBI-7829 P28241 EBI-16735,EBI-8883 P07259 EBI-16735,EBI-14372 P22203 EBI-16735,EBI-20268 P34216 EBI-16735,EBI-21243 P25694 EBI-16735,EBI-4308 P16140 EBI-16735,EBI-20254 P34760 EBI-16735,EBI-19623 P32610 EBI-16735,EBI-20264 P00549 EBI-16735,EBI-9890 P00358 EBI-16735,EBI-7212 Q12230 EBI-16735,EBI-34978 P53252 EBI-16735,EBI-23225 P15108 EBI-16735,EBI-8666 P10591 EBI-16735,EBI-8591 Q06385 EBI-16735,EBI-35395 P11484 EBI-16735,EBI-8627 P19882 EBI-16735,EBI-8586 Q12377 EBI-16735,EBI-308 P00925 EBI-16735,EBI-6475 P00359 EBI-16735,EBI-7218 P60010 EBI-16735,EBI-2169 P21672 EBI-16735,EBI-15246 P38713 EBI-12630,EBI-16735 O15209 EBI-16735,EBI-723574 Q08984 EBI-16735,EBI-3719178 Q12451 EBI-16735,EBI-12621 P21957 EBI-12555,EBI-16735 P37297 EBI-16735,EBI-18454 P38886 EBI-16735,EBI-15949 P49626 EBI-16735,EBI-15394 P38631 EBI-16735,EBI-7708 P12385 EBI-6533,EBI-16735 P47088 EBI-16735,EBI-26307 GO:0005935 GO:0005934 GO:0000781 GO:0005783 GO:0005789 GO:0030176 GO:0005635 GO:0031965 GO:0071561 GO:0005886 GO:0033149 GO:0035091 GO:0006348 GO:0048309 GO:0090158 GO:0061163 GO:0061817 GO:0042308 GO:0008654 GO:0032377 GO:0060304 MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFKCRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPAVVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLGWFYR 244 P40305 Interferon alpha-inducible protein 27, mitochondrial IFI27 9606 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT P40305 UNIPROT A0A087WZF8 UNIPROT A8K0H0 UNIPROT Q53YA6 UNIPROT Q6IEC1 UNIPROT Q7Z5R0 UNIPROT Q7Z5R1 UNIPROT Q7Z5R2 UNIPROT Q96BK3 UNIPROT Q9H4B1 Pfam PF06140 OMIM 600009 DisGeNET 3429 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}. P05549-1 EBI-2805952,EBI-9678982 Q92754 EBI-2805952,EBI-937309 A0A384KLT9 EBI-2805952,EBI-2853974 Q0WHE4 EBI-2840791,EBI-2805952 P17778 EBI-2805952,EBI-2842665 A0A384KST0 EBI-2845592,EBI-2805952 Q8ZG09 EBI-2842762,EBI-2805952 Q8ZHF1 EBI-2805952,EBI-2849437 Q81KT8 EBI-2805952,EBI-2809955 A0A1Q4LWR1 EBI-2831752,EBI-2805952 A0A0F7RKM4 EBI-2812285,EBI-2805952 Q81VA8 EBI-2812761,EBI-2805952 Q5NGF6 EBI-2805952,EBI-2798182 Q8ZCW0 EBI-2842923,EBI-2805952 GO:0005789 GO:0016021 GO:0031966 GO:0005741 GO:0005739 GO:0005635 GO:0005637 GO:0042802 GO:0005521 GO:0001102 GO:0006915 GO:0097190 GO:0051607 GO:0097191 GO:0045087 GO:0044827 GO:0000122 GO:0043161 GO:0070936 GO:0046825 GO:0060337 GO:0016032 MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGGGVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY 122 P40318 ERAD-associated E3 ubiquitin-protein ligase DOA10 SSM4 559292 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT P40318 UNIPROT D6VVQ1 PDB 2M6M Pfam PF12906 PROSITE PS51292 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}. P39015 EBI-11238,EBI-18208 P47137 EBI-25572,EBI-18208 P40513 EBI-10316,EBI-18208 P06738 EBI-13389,EBI-18208 P38758 EBI-24443,EBI-18208 P39683 EBI-12218,EBI-18208 P16467 EBI-5696,EBI-18208 P11154 EBI-14358,EBI-18208 P33399 EBI-10046,EBI-18208 P25617 EBI-18208,EBI-375711 P32288 EBI-7665,EBI-18208 P53982 EBI-8892,EBI-18208 P10963 EBI-18208,EBI-13770 P00925 EBI-18208,EBI-6475 P40825 EBI-18648,EBI-18208 P30952 EBI-10428,EBI-18208 Q04697 EBI-27807,EBI-18208 P32835 EBI-7926,EBI-18208 P23542 EBI-2002,EBI-18208 P38998 EBI-10264,EBI-18208 P38720 EBI-1965,EBI-18208 P35202 EBI-19195,EBI-18208 P80210 EBI-14267,EBI-18208 P40217 EBI-8951,EBI-18208 P38009 EBI-14223,EBI-18208 Q04458 EBI-27205,EBI-18208 P40959 EBI-11636,EBI-18208 Q05979 EBI-10016,EBI-18208 P40892 EBI-26263,EBI-18208 P08524 EBI-7069,EBI-18208 P25561 EBI-21696,EBI-18208 P38787 EBI-12913,EBI-18208 P46655 EBI-18665,EBI-18208 P38158 EBI-10326,EBI-18208 P38081 EBI-21453,EBI-18208 Q01454 EBI-5209,EBI-18208 Q08968 EBI-29375,EBI-18208 P41816 EBI-12734,EBI-18208 P46151 EBI-11567,EBI-18208 P54885 EBI-13872,EBI-18208 Q08686 EBI-19264,EBI-18208 Q08444 EBI-29777,EBI-18208 P50278 EBI-17675,EBI-18208 P37254 EBI-12831,EBI-18208 Q10740 EBI-10175,EBI-18208 P50101 EBI-19898,EBI-18208 P00331 EBI-2222,EBI-18208 P16862 EBI-9435,EBI-18208 P46680 EBI-2406,EBI-18208 Q04212 EBI-28073,EBI-18208 P15274 EBI-2548,EBI-18208 P54007 EBI-18208,EBI-27168 Q99260 EBI-29503,EBI-18208 Q04491 EBI-16529,EBI-18208 P31539 EBI-8050,EBI-18208 P10592 EBI-8603,EBI-18208 P41903 EBI-14154,EBI-18208 P38716 EBI-24682,EBI-18208 P17076 EBI-15431,EBI-18208 P53051 EBI-10464,EBI-18208 P53265 EBI-23264,EBI-18208 P53101 EBI-24097,EBI-18208 P53183 EBI-23747,EBI-18208 P10356 EBI-22726,EBI-18208 P21524 EBI-15234,EBI-18208 P25044 EBI-14183,EBI-18208 Q07505 EBI-5951,EBI-18208 P16120 EBI-19259,EBI-18208 P25576 EBI-21752,EBI-18208 P17967 EBI-13012,EBI-18208 P00817 EBI-9338,EBI-18208 P12866 EBI-18383,EBI-18208 P32589 EBI-8648,EBI-18208 Q04228 EBI-27730,EBI-18208 P38428 EBI-18208,EBI-27580 P38911 EBI-18208,EBI-6951 P25694 EBI-18208,EBI-4308 GO:0000837 GO:0005783 GO:0030176 GO:0016021 GO:0005635 GO:0005637 GO:0061630 GO:0004842 GO:0008270 GO:0030433 MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNIDISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMMLDGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPRLSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLRHVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQNEFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAVVFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNGYTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPILAGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKILHDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESSSYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVRDVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPDFRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCLSKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSKLNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES 1319 P40358 DnaJ-like chaperone JEM1 JEM1 559292 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000269|PubMed:9148890}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9148890}. Nucleus membrane {ECO:0000269|PubMed:15282802}. UNIPROT P40358 UNIPROT D6VWB0 Pfam PF00226 PROSITE PS50076 Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating. {ECO:0000269|PubMed:9148890}. P32499 EBI-12401,EBI-25940 P38181 EBI-11756,EBI-25940 P39685 EBI-25940,EBI-12739 P39705 EBI-20731,EBI-25940 P80210 EBI-25940,EBI-14267 P38009 EBI-25940,EBI-14223 P53730 EBI-25940,EBI-28496 P36000 EBI-2206,EBI-25940 P38328 EBI-25940,EBI-2777 Q12386 EBI-25940,EBI-2967 P32447 EBI-25940,EBI-3003 P43583 EBI-25940,EBI-22761 P48361 EBI-2993,EBI-25940 P14682 EBI-19730,EBI-25940 P53622 EBI-4860,EBI-25940 P53859 EBI-1731,EBI-25940 Q03375 EBI-30409,EBI-25940 P40487 EBI-25162,EBI-25940 P32898 EBI-25940,EBI-22092 P32461 EBI-25940,EBI-6090 P40557 EBI-24929,EBI-25940 P53743 EBI-28537,EBI-25940 P53849 EBI-25940,EBI-29244 P25569 EBI-21727,EBI-25940 P20448 EBI-25940,EBI-5612 P61830 EBI-25940,EBI-8098 P00815 EBI-25940,EBI-8334 P17629 EBI-8526,EBI-25940 Q06706 EBI-9068,EBI-25940 P50094 EBI-9195,EBI-25940 P25642 EBI-25940,EBI-9217 P40089 EBI-25940,EBI-10236 P40070 EBI-188,EBI-25940 P35192 EBI-10346,EBI-25940 Q12387 EBI-5736,EBI-25940 P46151 EBI-11567,EBI-25940 P33441 EBI-25940,EBI-10841 P09440 EBI-3903,EBI-25940 Q00539 EBI-25940,EBI-11835 P12945 EBI-11868,EBI-25940 Q07896 EBI-25940,EBI-36093 P53742 EBI-25940,EBI-28532 Q12499 EBI-12126,EBI-25940 P53261 EBI-13145,EBI-25940 Q01560 EBI-25940,EBI-12114 P50874 EBI-12584,EBI-25940 P32896 EBI-25940,EBI-13004 P16861 EBI-25940,EBI-9428 P16862 EBI-25940,EBI-9435 P00560 EBI-13275,EBI-25940 P32345 EBI-25940,EBI-12759 P32263 EBI-25940,EBI-13885 Q12417 EBI-25940,EBI-710 P40164 EBI-29107,EBI-25940 P06777 EBI-14752,EBI-25940 Q04231 EBI-27726,EBI-25940 P12753 EBI-25940,EBI-14700 P22336 EBI-25940,EBI-14971 P26754 EBI-25940,EBI-14976 P21524 EBI-15234,EBI-25940 P27999 EBI-15798,EBI-25940 P07703 EBI-15831,EBI-25940 P38764 EBI-25940,EBI-15913 Q05022 EBI-16011,EBI-25940 P40856 EBI-25940,EBI-16384 Q12745 EBI-31898,EBI-25940 Q03067 EBI-25940,EBI-34550 P39000 EBI-25940,EBI-22627 Q12460 EBI-25940,EBI-17148 P17883 EBI-25940,EBI-1861 P32908 EBI-17402,EBI-25940 P43321 EBI-529,EBI-25940 P32558 EBI-4334,EBI-25940 P32585 EBI-25940,EBI-18032 P36008 EBI-6329,EBI-25940 P43637 EBI-9668,EBI-25940 P22515 EBI-19703,EBI-25940 P39538 EBI-25940,EBI-19884 P50101 EBI-19898,EBI-25940 P54860 EBI-20003,EBI-25940 P32861 EBI-25940,EBI-19987 P39735 EBI-25940,EBI-20627 Q12457 EBI-25940,EBI-33699 P40521 EBI-3655056,EBI-25940 P40566 EBI-25940,EBI-3657860 P36076 EBI-26778,EBI-25940 P38746 EBI-27201,EBI-25940 Q07825 EBI-32387,EBI-25940 Q08422 EBI-30793,EBI-25940 Q12532 EBI-25940,EBI-33283 P46951 EBI-25940,EBI-23455 P53900 EBI-13246,EBI-25940 GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0042175 GO:0051087 GO:0051787 GO:0051082 GO:0000742 GO:0034975 GO:0030433 MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIYYKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDVSVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNSDASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDTNFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCKKSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSESTNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFKMNFGL 645 P40368 Nucleoporin NUP82 NUP82 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. UNIPROT P40368 UNIPROT D6VWC1 PDB 3PBP PDB 3TKN 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}. P14907 EBI-12331,EBI-12265 P37198 EBI-12331,EBI-347978 P40066 EBI-22648,EBI-12331 Q06410 EBI-30856,EBI-12331 P22696 EBI-6679,EBI-12331 P11484 EBI-12331,EBI-8627 P48363 EBI-13239,EBI-12331 Q04477 EBI-27228,EBI-12331 Q02199 EBI-12331,EBI-12315 P40477 EBI-12331,EBI-11747 P46673 EBI-12331,EBI-12345 Q03790 EBI-12331,EBI-27321 P49687 EBI-12331,EBI-11730 Q02630 EBI-12331,EBI-11703 Q02629 EBI-12331,EBI-11698 Q9BQD3 EBI-739657,EBI-12331 Q9HCM9-2 EBI-12331,EBI-11523450 Q9Y3C0 EBI-12331,EBI-712969 Q12443 EBI-12331,EBI-32591 P10591 EBI-12331,EBI-8591 P40150 EBI-12331,EBI-8632 P38305 EBI-20939,EBI-12331 Q12315 EBI-7635,EBI-12331 GO:0005829 GO:0031965 GO:0005643 GO:0044614 GO:0044612 GO:0005634 GO:0017056 GO:0006406 GO:0006611 GO:0006606 GO:0000055 GO:0000056 MSQSSRLSALPIFQASLSASQSPRYIFSSQNGTRIVFIQDNIIRWYNVLTDSLYHSLNFSRHLVLDDTFHVISSTSGDLLCLFNDNEIFVMEVPWGYSNVEDVSIQDAFQIFHYSIDEEEVGPKSSIKKVLFHPKSYRDSCIVVLKEDDTITMFDILNSQEKPIVLNKPNNSFGLDARVNDITDLEFSKDGLTLYCLNTTEGGDIFAFYPFLPSVLLLNEKDLNLILNKSLVMYESLDSTTDVIVKRNVIKQLQFVSKLHENWNSRFGKVDIQKEYRLAKVQGPFTINPFPGELYDYTATNIATILIDNGQNEIVCVSFDDGSLILLFKDLEMSMSWDVDNYVYNNSLVLIERVKLQREIKSLITLPEQLGKLYVISDNIIQQVNFMSWASTLSKCINESDLNPLAGLKFESKLEDIATIERIPNLAYINWNDQSNLALMSNKTLTFQNISSDMKPQSTAAETSISTEKSDTVGDGFKMSFTQPINEILILNDNFQKACISPCERIIPSADRQIPLKNEASENQLEIFTDISKEFLQRIVKAQTLGVSIHNRIHEQQFELTRQLQSTCKIISKDDDLRRKFEAQNKKWDAQLSRQSELMERFSKLSKKLSQIAESNKFKEKKISHGEMKWFKEIRNQILQFNSFVHSQKSLQQDLSYLKSELTRIEAETIKVDKKSQNEWDELRKMLEIDSKIIKECNEELLQVSQEFTTKTQ 713 P40383 5'-3' exoribonuclease 1 exo2 284812 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. UNIPROT P40383 Pfam PF18129 Pfam PF18332 Pfam PF18334 Pfam PF17846 Pfam PF03159 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}. GO:0005737 GO:0010494 GO:0005829 GO:0005874 GO:0000932 GO:0048471 GO:0004534 GO:0000287 GO:0004540 GO:0003723 GO:0000741 GO:0000184 GO:0090502 GO:0006364 MGIPKFFRWMSERYPLCSQLIENDRIPEFDNLYLDMNGILHNCTHKNDDHSSPPLPEEEMYIAIFNYIEHLFEKIKPKKLLYMAVDGCAPRAKMNQQRSRRFRTAKDAHDARLKAERNGEDFPEEQFDSNCITPGTTFMERVSRQLYYFIHKKVTNDSQWQNIEVIFSGHDCPGEGEHKIMEYIRTQKAQPSYNPNTRHCLYGLDADLIMLGLLSHDPHFCLLREEVTFGPASRNRSKELAHQKFYLLHLSLLREYLEFEFQECRSTFTFKYDLEKILDDFILLAFFVGNDFLPHLPGLHINEGALALMFSIYKKVMPSAGGYINEKGVINMARLELILLELENFEKEIFKAEVSETKNNGNSDKPSFDFLKYITESTNDIKAMTGEQKNYFLQIKKFLSSREPFIDFSANISSVDQRFLRRLCNDLHLSFSKIIKVDGTHLLRITFRDLEFNDEDEDEIEQDEIERVLQKYDNIPLLNEEQALKEKNVEKDFIQWKDDYYRSKVGFSYYDEEALKAMAERYVEGLQWVLFYYYRGCQSWGWYYNYHFAPKISDVLKGLDVKIDFKMGTPFRPFEQLMAVLPARSQALVPPCFRDLMVNSESPIIDFYPENFALDQNGKTASWEAVVIIPFIDETRLIDALASKDKFLTEEERKRNSFNAPTVFSLAEDYTSFYPSSLPSLFPDLVTRCIQKPYSLPSMEGKEYLVGLCPGVFLGAFGMVGFPSFHTLKHKAELVYHGINVFGNESRNPSVIVNVEDVKSALTSEQIAMQYVGKRIFVDWPYLREAYVESAMDESYMYLASNSTIEKRDLAEIEKSQWGRKCSHKIREYSKRFGVLFGDISLLLQVRPIKGLEYTREGALVKIFNESVLEDYPAQLVVEKIAIDDPRFTEREAPPVEVEYPPGTKAFHLGEYNYGRPAQITGCKDNKLIIWLSTAPGLDAQWGRVLVNDSKSKEKYYPSYIVAKLLNIHPLLLSKITSSFLISNGTKRENIGLNLKFDARNQKVLGFSRKSTKGWEFSNKTVALVKEYINTFPQLFNILTTHATKDNLTVKDCFPKDDTQQLAAVKHWIKEKGINSLTRVSLDEDALDSDIIKLIEEKASTIDSTYQVPKKVFGVPRYALLKPSQTRGILHSQEFALGDRVVYVQDSGKVPIAAYGTVVGIMLHHLDVVFDLPFMSGTTLDGRCSPYHGMQVEVSMVLNVTNPQFVVNTRAGKNRKTNVSANNVSQGTDSRLVTKPTSTFPSPPSPPSSSVWNKREHHPKPFSLHQVPPPESLIHKSKSKFSKGNHHSTNGTQSIRGRGGKRGKPLRSKELNRKHDHIVQPMGKLQIN 1328 P40477 Nucleoporin NUP159 NUP159 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. UNIPROT P40477 UNIPROT D6VVH2 PDB 1XIP PDB 3PBP PDB 3RRM PDB 3TKN PDB 4DS1 Pfam PF16755 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}. P14907 EBI-12265,EBI-11747 P40066 EBI-22648,EBI-11747 P40368 EBI-12331,EBI-11747 Q06142 EBI-11747,EBI-9145 P22696 EBI-6679,EBI-11747 P10591 EBI-11747,EBI-8591 Q12329 EBI-8571,EBI-11747 P47138 EBI-25576,EBI-11747 P39076 EBI-11747,EBI-19049 P39987 EBI-11747,EBI-22339 P38788 EBI-24570,EBI-11747 P11484 EBI-11747,EBI-8627 P40150 EBI-11747,EBI-8632 P32589 EBI-8648,EBI-11747 P02829 EBI-11747,EBI-8659 P10592 EBI-11747,EBI-8603 Q12046 EBI-11747,EBI-553 P38305 EBI-20939,EBI-11747 Q12315 EBI-7635,EBI-11747 GO:0031965 GO:0005643 GO:0044613 GO:0044614 GO:0005634 GO:0000774 GO:0017056 GO:0003714 GO:0097064 GO:0006607 GO:0031081 GO:0016973 GO:0006611 GO:0000055 GO:0000056 MSSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKAVVGELQLLRDHITSDSTPLTFKWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFRTVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQLAQNVTSFDVTNSQLAVLLKDRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDDEVSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASSCSSEVSIWDSKQVIEPSQDSERAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTIERLPLVYILNNEGSLQIVGLFHVAAIKSGHYSINLESLEHEKSLSPTSEKIPIAGQEQEEKKKNNESSKALSENPFTSANTSGFTFLKTQPAAANSLQSQSSSTFGAPSFGSSAFKIDLPSVSSTSTGVASSEQDATDPASAKPVFGKPAFGAIAKEPSTSEYAFGKPSFGAPSFGSGKSSVESPASGSAFGKPSFGTPSFGSGNSSVEPPASGSAFGKPSFGTPSFGSGNSSAEPPASGSAFGKPSFGTSAFGTASSNETNSGSIFGKAAFGSSSFAPANNELFGSNFTISKPTVDSPKEVDSTSPFPSSGDQSEDESKSDVDSSSTPFGTKPNTSTKPKTNAFDFGSSSFGSGFSKALESVGSDTTFKFGTQASPFSSQLGNKSPFSSFTKDDTENGSLSKGSTSEINDDNEEHESNGPNVSGNDLTDSTVEQTSSTRLPETPSDEDGEVVEEEAQKSPIGKLTETIKKSANIDMAGLKNPVFGNHVKAKSESPFSAFATNITKPSSTTPAFSFGNSTMNKSNTSTVSPMEEADTKETSEKGPITLKSVENPFLPAKEERTGESSKKDHNDDPKDGYVSGSEISVRTSESAFDTTANEEIPKSQDVNNHEKSETDPKYSQHAVVDHDNKSKEMNETSKNNERSGQPNHGVQGDGIALKKDNEKENFDSNMAIKQFEDHQSSEEDASEKDSRQSSEVKESDDNMSLNSDRDESISESYDKLEDINTDELPHGGEAFKAREVSASADFDVQTSLEDNYAESGIQTDLSESSKENEVQTDAIPVKHNSTQTVKKEAVDNGLQTEPVETCNFSVQTFEGDENYLAEQCKPKQLKEYYTSAKVSNIPFVSQNSTLRLIESTFQTVEAEFTVLMENIRNMDTFFTDQSSIPLVKRTVRSINNLYTWRIPEAEILLNIQNNIKCEQMQITNANIQDLKEKVTDYVRKDIAQITEDVANAKEEYLFLMHFDDASSGYVKDLSTHQFRMQKTLRQKLFDVSAKINHTEELLNILKLFTVKNKRLDDNPLVAKLAKESLARDGLLKEIKLLREQVSRLQLEEKGKKASSFDASSSITKDMKGFKVVEVGLAMNTKKQIGDFFKNLNMAK 1460 P40532 Nuclear membrane organization protein APQ12 APQ12 559292 Yes SL-0178 SL-0182 Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. UNIPROT P40532 UNIPROT D6VVP2 Pfam PF12716 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}. P32589 EBI-8648,EBI-25002 P11484 EBI-8627,EBI-25002 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGIYMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK 138 P40548 HSP70 co-chaperone SNL1 SNL1 559292 Yes SL-0178 SL-0182 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}. UNIPROT P40548 UNIPROT D6VVR3 Pfam PF02179 PROSITE PS51035 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}. Q06247 EBI-24950,EBI-38452 P02557 EBI-24950,EBI-18986 P09733 EBI-24950,EBI-18976 P02994 EBI-24950,EBI-6314 P00359 EBI-24950,EBI-7218 P40150 EBI-24950,EBI-8632 P11484 EBI-24950,EBI-8627 P10591 EBI-24950,EBI-8591 P11075 EBI-24950,EBI-16882 P23248 EBI-24950,EBI-16136 P14127 EBI-24950,EBI-14531 P06367 EBI-24950,EBI-14460 P05756 EBI-24950,EBI-16054 P05317 EBI-24950,EBI-15447 P29453 EBI-24950,EBI-15435 P05739 EBI-24950,EBI-15409 P49626 EBI-24950,EBI-15394 P14120 EBI-24950,EBI-15333 P38754 EBI-24950,EBI-14475 P40212 EBI-24950,EBI-14456 P50108 EBI-24950,EBI-11043 P38631 EBI-24950,EBI-7708 GO:0005789 GO:0016021 GO:0005739 GO:0005635 GO:0031965 GO:0051087 GO:0043022 GO:0006999 GO:0006457 MSHNAMEHWKSKLSKTSTSTYVLLAVIAVVFLVTIRRPNGSKGKSSKKRASKKNKKGKNQFEKAPVPLTLEEQIDNVSLRYGNELEGRSKDLINRFDVEDEKDIYERNYCNEMLLKLLIELDSIDLINVDESLRRPLKEKRKGVIKEIQAMLKSLDSLK 159 P41208 Centrin-2 CETN2 9606 Yes SL-0178 SL-0185 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}. UNIPROT P41208 UNIPROT B2R4T4 UNIPROT Q53XW1 PDB 1M39 PDB 1ZMZ PDB 2A4J PDB 2GGM PDB 2K2I PDB 2OBH Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 300006 DisGeNET 1069 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}. P03372 EBI-78473,EBI-1789926 Q8NA72 EBI-2561090,EBI-1789926 Q2NKQ1-4 EBI-10182463,EBI-1789926 Q96PV4 EBI-1789926,EBI-10171633 A8K8P3 EBI-743371,EBI-1789926 Q70CQ1 EBI-2511022,EBI-1789926 Q9H0E7 EBI-2512823,EBI-1789926 Q9R1K9 EBI-2553037,EBI-1789926 O43303 EBI-1566217,EBI-1789926 P15289 EBI-1789926,EBI-2117357 Q96LA8 EBI-1789926,EBI-912440 Q6P5D4 EBI-647072,EBI-1789926 P52732 EBI-355697,EBI-1789926 O14640 EBI-1789926,EBI-723489 Q8N0X7 EBI-1789926,EBI-2643803 P53680 EBI-1789926,EBI-297662 P50991 EBI-1789926,EBI-356876 P49368 EBI-1789926,EBI-356673 P20290 EBI-1789926,EBI-1054687 Q99832 EBI-1789926,EBI-357046 Q9UNY4 EBI-1789926,EBI-2322921 Q16513 EBI-1789926,EBI-2511350 Q9BYS8 EBI-1789926,EBI-5665279 P78371 EBI-1789926,EBI-357407 P48643 EBI-1789926,EBI-355710 P17987 EBI-1789926,EBI-356553 Q8WUY9 EBI-1789926,EBI-3924857 Q01831 EBI-1789926,EBI-372610 Q9NYP9 EBI-1789926,EBI-1104552 P40227 EBI-1789926,EBI-356687 P35606 EBI-1789926,EBI-1056534 O14737 EBI-1789926,EBI-712290 P54727 EBI-1789926,EBI-954531 Q8WU90 EBI-1789926,EBI-1042636 Q6PD62 EBI-1019583,EBI-1789926 P48754 EBI-6876136,EBI-1789926 O88286 EBI-5737907,EBI-1789926 Q14103 EBI-299674,EBI-1789926 Q3V6T2 EBI-2266839,EBI-1789926 P29341 EBI-773902,EBI-1789926 Q9NTX7-2 EBI-11750630,EBI-1789926 P15927-2 EBI-21839513,EBI-1789926 Q8IW19 EBI-1256044,EBI-1789926 Q96DD0-2 EBI-21832535,EBI-1789926 Q8NEE6-2 EBI-1789926,EBI-21867651 O14874 EBI-1046765,EBI-1789926 Q8NA72-3 EBI-11751537,EBI-1789926 Q5VW00 EBI-3951747,EBI-1789926 P08887-2 EBI-16630231,EBI-1789926 Q0VDD8-2 EBI-21543829,EBI-1789926 Q16526 EBI-741297,EBI-1789926 P16104 EBI-494830,EBI-1789926 Q96A08 EBI-3951855,EBI-1789926 Q12798 EBI-2512818,EBI-1789926 Q9BQ69 EBI-5324932,EBI-1789926 Q6ZNE5 EBI-2690371,EBI-1789926 Q99598 EBI-742638,EBI-1789926 GO:0005814 GO:0005813 GO:0036064 GO:0005829 GO:0005622 GO:0044615 GO:0005654 GO:0032391 GO:0070390 GO:0071942 GO:0005509 GO:0031683 GO:0032795 GO:0008017 GO:0051301 GO:0007099 GO:0097711 GO:0000086 GO:0070911 GO:0000278 GO:0051028 GO:0006289 GO:0000715 GO:0000717 GO:0006294 GO:0015031 GO:0032465 GO:0010389 GO:0007283 MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY 172 P41391 Ran GTPase-activating protein 1 rna1 284812 Yes SL-0198 Cytoplasm. Cytoplasm, perinuclear region {ECO:0000305}. Note=Possibly enriched in the nuclear periphery. UNIPROT P41391 PDB 1K5D PDB 1K5G PDB 1YRG PDB 2CA6 GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state. P62826 EBI-286642,EBI-1032893 GO:0005737 GO:0005829 GO:0031965 GO:0005634 GO:0048471 GO:0005096 GO:0046827 MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIPEALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPPLRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIALKSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDDVVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI 386 P41917 GTP-binding nuclear protein Ran-2 RAN2 3702 Yes SL-0178 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. UNIPROT P41917 UNIPROT Q0WVD9 UNIPROT Q94K33 Pfam PF00071 PROSITE PS51418 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}. Q8RWG8 EBI-2325867,EBI-2325919 Q9LMK7 EBI-2325844,EBI-2325919 GO:0005737 GO:0005794 GO:0005635 GO:0005730 GO:0005634 GO:0009536 GO:0005525 GO:0003924 GO:0006606 GO:0046686 GO:0000054 MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNFEKPFLYLARKLAGDQNLHFVESPALAPPEVHLDIAAQQQNEADLAAAAAQPLPDDDDDAFE 221 P41933 Nuclear hormone receptor family member odr-7 odr 6239 Yes SL-0198 Nucleus. Cytoplasm, perinuclear region. UNIPROT P41933 UNIPROT C3U4U8 UNIPROT C3U4U9 UNIPROT C3U4V2 Pfam PF00105 PROSITE PS00031 PROSITE PS51030 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}. G5EFI7 EBI-6731836,EBI-6731843 O45291 EBI-6736645,EBI-6731836 Q19418 EBI-2315670,EBI-6731836 Q22289 EBI-6731836,EBI-6726526 Q9NAE4 EBI-332523,EBI-6731836 Q9TXN8 EBI-6726742,EBI-6731836 GO:0005634 GO:0048471 GO:0001228 GO:0003700 GO:0043565 GO:0008270 GO:0022401 GO:0050918 GO:0045944 GO:0006357 GO:0007608 MIVPDTEGLLIYSYGLMYGSYCMACQMLIPHFQCIPGIFPNFRISTELIKTMTDKLEQPNNNVPQQPWGPFPPAFGGRPSGEQTDGNPGEFDNDAAHQQTAPFMTHFFPRIGLQFPDFTEYQRFNGFQRNAFFPNPFGSQFTGQAFAQSFPLHNSMTTMDGFNLTHAPHPFSTNTNSTKPKDIENTVQSTIKHSSENIQDKPPVLSVEYPVKYDSELKFDANVDFTAVPKQESSDDSTLKNLKKSDQQLQQPQQFTFPPPLLAEKSFEQPRMREDVLPFHPQFYPAPLDMGTNFKQEMRTPPIDGHIDYRKFDASGKRMEFQPPGALHDCQVCLSTHANGLHFGARTCAACAAFFRRTISDDKRYVCKRNQRCNNASRDGTGYRKICRSCRMKRCLEIGMLPENVQHKRNRRDSGSPPRKTPFDTFFNGFYPSFQPSGSAAQPITVSSSESPRHTTN 457 P42001 Protection of telomeres homolog 1 pot 6239 Yes SL-0178 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}. UNIPROT P42001 UNIPROT A0A2K5ATS5 UNIPROT A0A2K5ATS9 UNIPROT A0A2K5ATU9 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}. GO:0000784 GO:0005635 GO:0043047 GO:1904357 MQYTYQHIQDLVPGPTPQNFYGKIIFIKKKINQIVVLIKDETQSIYLRVIPKEDQELEFQLRQVVRVHRCKIQSILNSKEGIAQIGLFGCHLIAWSQSGKVDNPVIISSRSWTKSDEDSERLQTLRKLGKSRRKSGRKTSVDTMANKLIERREAMFADTFIKSLFNKIALSRKEHLSRNARELFYHRPGDIVETQNLLEIDDSWFNDENSEQFVQYVLNCTTCHVEYNHVEYAQNNIPTNCRFCQEAMESFHAAFRIRISIETYGVFLTIPLELIKTELDICEDWDSESNIVEEEEKVTRFKKNIQEKVRDASIVHIKGISSLLLIIMLNINSISLVNNITENKRILLQKSNVPSSLQLKILITPFVIVVVRFFGITWIYSGSSCIEEVLNLIDNCSRRR 400 P42167 Thymopentin TMPO 9606 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane; Single-pass type II membrane protein. Note=Tightly associated with the nuclear lamina. [Isoform Zeta]: Cytoplasm {ECO:0000269|PubMed:18403046}. UNIPROT P42167 UNIPROT A2T926 UNIPROT Q14861 Pfam PF03020 Pfam PF08198 PROSITE PS50954 PROSITE PS50955 OMIM 188380 DisGeNET 7112 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. O43542 EBI-2849976,EBI-455283 P00519 EBI-375543,EBI-455283 P02545 EBI-455283,EBI-351935 P20700 EBI-455283,EBI-968218 P06241 EBI-455283,EBI-515315 P62993 EBI-455283,EBI-401755 P16333 EBI-455283,EBI-389883 Q00005 EBI-1052159,EBI-455283 Q9NQB0 EBI-924724,EBI-455283 O95229 EBI-1001132,EBI-455283 O14862 EBI-6253193,EBI-455283 O14646-2 EBI-455283,EBI-10961487 Q6IE81-2 EBI-455283,EBI-10986812 Q7KZ85 EBI-455283,EBI-2515547 P35232 EBI-455283,EBI-354213 Q99623 EBI-455283,EBI-358348 Q9BXS6-2 EBI-455283,EBI-10969852 P98160 EBI-455283,EBI-947664 P62807 EBI-455283,EBI-354552 O95696-2 EBI-455283,EBI-11017508 P26640 EBI-455283,EBI-355765 P49916 EBI-455283,EBI-1753381 P61421 EBI-455283,EBI-954063 P17480 EBI-455283,EBI-396235 Q10589 EBI-455283,EBI-2476339 Q14978-2 EBI-455283,EBI-396172 P46100 EBI-455283,EBI-396461 P55197 EBI-455283,EBI-1104952 B4E2V5 EBI-455283,EBI-10977770 Q9P2E9 EBI-455283,EBI-2371806 Q8WWQ0 EBI-455283,EBI-722984 E7ESK6 EBI-455283,EBI-10986808 Q9BW71 EBI-455283,EBI-723624 P42766 EBI-455283,EBI-356819 O95251 EBI-455283,EBI-473199 P23258 EBI-455283,EBI-302589 Q96B26 EBI-455283,EBI-371922 Q8NHU3 EBI-455283,EBI-10977284 Q969G5 EBI-455283,EBI-3893101 Q5T3F8 EBI-2553509,EBI-455283 Q9Y587 EBI-2115780,EBI-455283 P27824 EBI-355947,EBI-455283 P68431 EBI-79722,EBI-455283 P11279 EBI-2805407,EBI-455283 Q77M19 EBI-6149376,EBI-455283 P06821 EBI-2547404,EBI-455283 P27105 EBI-1211440,EBI-455283 Q8WZ60 EBI-6426464,EBI-455283 Q8NBJ4 EBI-712073,EBI-455283 Q99JP4 EBI-2554171,EBI-455283 C5E524 EBI-12561527,EBI-455283 C5E519 EBI-12562139,EBI-455283 P03496 EBI-2547442,EBI-455283 GO:0005737 GO:0016021 GO:0016020 GO:0005635 GO:0005637 GO:0031965 GO:0005634 GO:0003677 GO:0005521 MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSGAAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTISSSAENTRQNGSNDSDRYSDNEEDSKIELKLEKREPLKGRAKTPVTLKQRRVEHNQSYSQAGITETEWTSGSSKGGPLQALTRESTRGSRRTPRKRVETSEHFRIDGPVISESTPIAETIMASSNESLVVNRVTGNFKHASPILPITEFSDIPRRAPKKPLTRAEVGEKTEERRVERDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYVPLADVKSEKTKKGRSIPVWIKILLFVVVAVFLFLVYQAMETNQVNPFSNFLHVDPRKSN 454 P42674 Blastula protease 10 BP10 7656 No SL-0198 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. UNIPROT P42674 Pfam PF01400 Pfam PF00431 PROSITE PS51864 PROSITE PS01180 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 PROSITE PS00142 Could be involved in the differentiation of ectodermal lineages and subsequent patterning of the embryo. GO:0005938 GO:0005615 GO:0048471 GO:0004222 GO:0008270 MKLILFLSGLVSLVLCTLAAPTGDQKEIHTETPPPKKPSETTTPGALKTPQPEPKDEEPTPGAFQGDMMLTEDQQRESKEAIDDEMTGRKKRKATIYESQRWPYKVIPYVISPSSSGQSSLIRNAMDHWEQNTCLRFEPRTSSHSRQLGHNAYLSFFRGSGCWSYVGKAFNGEQQISIGNGCAYFGTIVHEIGHAIGFHHEQSRPDRDDYINVLYQNIQSGRQHNFAKYTWGRVTSRNVEYDVGSIMHYGGYGFSSNGRPTITTRDPRLNSRLGQRIALSPADIELANLIYECDDIEDCAGANECLNGGYHDTECNCVCPSGYNGDLCEDAVTTTRPDCSERFTEMTGVITSPNWPGRYEDNMACVYQIEGPPGSTIELTFTEMNIENHAACRYDAVEVRKDDINSDGEKFCGNTLPAVQISSGNQMLISFTSDPSITGRGFRATYRIVILTTTQIPDTTTISTTTPVPTTTQATTDETVVGSCGGSFGGTQGRVATPNYPNNYDNDLECVYVIEVEIGRRVELDFIDFVLEDETNCRWDSLSINLGDGIKIDMKMCGREYPAASLVSIGNNMELTLISDRSVTDRGFMADYRAIDL 597 P42704 Leucine-rich PPR motif-containing protein, mitochondrial LRPPRC 9606 Yes SL-0178 SL-0179 SL-0182 SL-0183 Mitochondrion. Nucleus, nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note=Seems to be predominantly mitochondrial. UNIPROT P42704 UNIPROT A0PJE3 UNIPROT A8K1V1 UNIPROT Q53PC0 UNIPROT Q53QN7 UNIPROT Q6ZUD8 UNIPROT Q7Z7A6 UNIPROT Q96D84 Pfam PF01535 Pfam PF13812 Pfam PF17177 PROSITE PS51375 OMIM 220111 OMIM 607544 DisGeNET 10128 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}.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. P04626 EBI-641062,EBI-1050853 O14880 EBI-724754,EBI-1050853 Q15118 EBI-7016221,EBI-1050853 P08559 EBI-715747,EBI-1050853 O95714 EBI-1058922,EBI-1050853 P10809 EBI-352528,EBI-1050853 Q9NWT8 EBI-448665,EBI-1050853 Q9H1C4 EBI-4401271,EBI-1050853 O95183 EBI-10191195,EBI-1050853 P21860 EBI-720706,EBI-1050853 Q9BSB4 EBI-2946739,EBI-1050853 O94966 EBI-2511895,EBI-1050853 Q70CQ1 EBI-2511022,EBI-1050853 Q9NXR7 EBI-949389,EBI-1050853 P01106 EBI-447544,EBI-1050853 Q9Y6E7 EBI-2606540,EBI-1050853 A2APR8 EBI-10973834,EBI-1050853 Q8VC57 EBI-2551470,EBI-1050853 P09803 EBI-984420,EBI-1050853 P47755 EBI-762451,EBI-1050853 P51149 EBI-1056089,EBI-1050853 Q9GZT3 EBI-1050853,EBI-1050793 P42768 EBI-1050853,EBI-346375 Q96EB6 EBI-1050853,EBI-1802965 Q9HBM1 EBI-1050853,EBI-999909 Q14573 EBI-1050853,EBI-351055 P28715 EBI-1050853,EBI-765885 Q9NPL8 EBI-1050853,EBI-6268651 Q9BZQ6 EBI-1050853,EBI-2556756 J3KS15 EBI-1050853,EBI-11073518 A8K7Q2 EBI-1050853,EBI-10971637 Q9P2K8-2 EBI-1050853,EBI-10988447 J3QL56 EBI-1050853,EBI-11137054 Q6UB35 EBI-1050853,EBI-1046835 P38117 EBI-1050853,EBI-1056543 Q6PJT7-9 EBI-1050853,EBI-10963388 Q02224 EBI-1050853,EBI-1375040 B4DR80 EBI-1050853,EBI-11056323 P39748 EBI-1050853,EBI-707816 P36776 EBI-1050853,EBI-357448 Q9H6K4 EBI-8477908,EBI-1050853 Q9BVS5 EBI-3197877,EBI-1050853 P63000 EBI-1050853,EBI-413628 O75381 EBI-594898,EBI-1050853 Q6QDQ4 EBI-5276623,EBI-1050853 Q15327 EBI-5653378,EBI-1050853 P05919 EBI-6248147,EBI-1050853 P19320 EBI-6189824,EBI-1050853 P0DOE9 EBI-6138585,EBI-1050853 Q77M19 EBI-6149376,EBI-1050853 Q9Z381 EBI-1050853,EBI-2865275 Q81ME0 EBI-2813646,EBI-1050853 P11171 EBI-1050853,EBI-1050906 Q9Y2Q3 EBI-1050853,EBI-1053767 Q14164 EBI-1050853,EBI-307369 Q9Y5V3 EBI-1050853,EBI-716006 P01889 EBI-1050853,EBI-1046513 P43360 EBI-1050853,EBI-1045155 Q9UBN6 EBI-1050853,EBI-1044859 P62330 EBI-1050853,EBI-638181 P23508 EBI-1050853,EBI-307531 Q9Y4K3 EBI-1050853,EBI-359276 Q9HC98 EBI-1050853,EBI-740364 P60520 EBI-1050853,EBI-720116 P78396 EBI-1050853,EBI-375065 P19532 EBI-1050853,EBI-1048957 O75365 EBI-1050853,EBI-1043866 Q9Y5J5 EBI-1050853,EBI-1055859 Q9P2S5 EBI-1050853,EBI-1054904 Q13480 EBI-517684,EBI-1050853 Q15256 EBI-2265659,EBI-1050853 P27361 EBI-73995,EBI-1050853 Q16828 EBI-746870,EBI-1050853 P28562 EBI-975493,EBI-1050853 O94776 EBI-1783035,EBI-1050853 P08631 EBI-346340,EBI-1050853 O15530 EBI-717097,EBI-1050853 Q14CZ7 EBI-10234819,EBI-1050853 Q96KR7 EBI-717068,EBI-1050853 Q9NZI8 EBI-1053892,EBI-1050853 O14829 EBI-2931238,EBI-1050853 Q8IWL3 EBI-1805738,EBI-1050853 Q6IQ23 EBI-2125301,EBI-1050853 Q9Y6K9 EBI-1050853,EBI-81279 Q15653 EBI-1050853,EBI-352889 P60709 EBI-353944,EBI-1050853 GO:0000794 GO:0005856 GO:0016020 GO:0005874 GO:0042645 GO:0005739 GO:0005637 GO:0005640 GO:0005654 GO:0005634 GO:0048471 GO:1990904 GO:0048487 GO:0008017 GO:0003723 GO:0003697 GO:0031625 GO:0047497 GO:0051028 GO:0000961 GO:0070129 MAALLRSARWLLRAGAAPRLPLSLRLLPGGPGRLHAASYLPAARAGPVAGGLLSPARLYAIAAKEKDIQEESTFSSRKISNQFDWALMRLDLSVRRTGRIPKKLLQKVFNDTCRSGGLGGSHALLLLRSCGSLLPELKLEERTEFAHRIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMDRDLLQIIFSFSKAGYPQYVSEILEKVTCERRYIPDAMNLILLLVTEKLEDVALQILLACPVSKEDGPSVFGSFFLQHCVTMNTPVEKLTDYCKKLKEVQMHSFPLQFTLHCALLANKTDLAKALMKAVKEEGFPIRPHYFWPLLVGRRKEKNVQGIIEILKGMQELGVHPDQETYTDYVIPCFDSVNSARAILQENGCLSDSDMFSQAGLRSEAANGNLDFVLSFLKSNTLPISLQSIRSSLLLGFRRSMNINLWSEITELLYKDGRYCQEPRGPTEAVGYFLYNLIDSMSDSEVQAKEEHLRQYFHQLEKMNVKIPENIYRGIRNLLESYHVPELIKDAHLLVESKNLDFQKTVQLTSSELESTLETLKAENQPIRDVLKQLILVLCSEENMQKALELKAKYESDMVTGGYAALINLCCRHDKVEDALNLKEEFDRLDSSAVLDTGKYVGLVRVLAKHGKLQDAINILKEMKEKDVLIKDTTALSFFHMLNGAALRGEIETVKQLHEAIVTLGLAEPSTNISFPLVTVHLEKGDLSTALEVAIDCYEKYKVLPRIHDVLCKLVEKGETDLIQKAMDFVSQEQGEMVMLYDLFFAFLQTGNYKEAKKIIETPGIRARSARLQWFCDRCVANNQVETLEKLVELTQKLFECDRDQMYYNLLKLYKINGDWQRADAVWNKIQEENVIPREKTLRLLAEILREGNQEVPFDVPELWYEDEKHSLNSSSASTTEPDFQKDILIACRLNQKKGAYDIFLNAKEQNIVFNAETYSNLIKLLMSEDYFTQAMEVKAFAETHIKGFTLNDAANSRLIITQVRRDYLKEAVTTLKTVLDQQQTPSRLAVTRVIQALAMKGDVENIEVVQKMLNGLEDSIGLSKMVFINNIALAQIKNNNIDAAIENIENMLTSENKVIEPQYFGLAYLFRKVIEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLVDAGKVDDARALLQRCGAIAEQTPILLLFLLRNSRKQGKASTVKSVLELIPELNEKEEAYNSLMKSYVSEKDVTSAKALYEHLTAKNTKLDDLFLKRYASLLKYAGEPVPFIEPPESFEFYAQQLRKLRENSS 1394 P45436 Cell death protein 3 subunit p13 ced 31234 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT P45436 UNIPROT E3M6B9 Pfam PF00619 PROSITE PS50209 PROSITE PS01122 PROSITE PS01121 PROSITE PS50207 PROSITE PS50208 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}. GO:0008303 GO:0005623 GO:0030054 GO:0005739 GO:0031965 GO:0043204 GO:0048471 GO:0098793 GO:0008656 GO:0097200 GO:0042802 GO:0030042 GO:0097202 GO:1902742 GO:0050829 GO:0009792 GO:0046716 GO:1905803 GO:1904747 GO:1905845 GO:0043525 GO:1901046 GO:0010954 GO:1905808 GO:0016540 GO:0030163 GO:0030155 GO:0042659 GO:0040034 GO:0040012 GO:0031647 GO:0040028 MMRQDRRNLLERNILVFSNKLQSEQILEVLIAKQILNADNGDVINSCRTERDKRKEIVKAVQRRGDVAFDAFYDALRDTGHHELAAVLEPLARTIDFITPRDLECPMSPASHRRSRALSPSTFSSPTRVHRDSVSSVSSFTSTYQDVYTRARSTSRSSRPLHASDRHNYVSPSNSFQSQPSSANSSFTGCSSLGYSSSRTRSYSKASAHSQYIFHEEDMNYVDAPTIHRVFDEKTMYRNFSTPRGLCLIINNEHFEQMPTRNGTKADKDNISNLFRCMGYIVHCKDNLTGRAMMLTIRDFAKNETHGDSAILVILSHGEENVIIGVDDVSVNVHEIYDLLNAANAPRLANKPKLVFVQACRGERRDNGFPVLDSVDGVPALIRPRGWDKGDGPLFNFLGCVRPQAQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSLHAKDMDVVELLTEVNKKVACGFQTSQGANILKQMPELTSRLLKKFYFWPEDRNRSSAV 508 P46061 Ran GTPase-activating protein 1 Rangap1 10090 Yes SL-0178 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}. UNIPROT P46061 UNIPROT Q60801 UNIPROT Q6NZB5 PDB 1KPS Pfam PF13516 Pfam PF07834 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}. P35922 EBI-645094,EBI-1033051 Q61584 EBI-8350418,EBI-1033051 P52927 EBI-912574,EBI-1033051 P63279 EBI-80168,EBI-1033051 Q9EPK7 EBI-6908541,EBI-1033051 GO:0016235 GO:1904115 GO:0000777 GO:0005737 GO:1990723 GO:0005829 GO:0030425 GO:0043231 GO:0072686 GO:0005635 GO:0031965 GO:0005643 GO:0044614 GO:0005654 GO:0005634 GO:0048471 GO:0005096 GO:0008536 GO:0003723 GO:0031625 GO:0090630 GO:0071375 GO:1904117 GO:0046826 GO:0048678 GO:0007165 MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI 589 P46673 Nucleoporin NUP85 NUP85 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P46673 UNIPROT D6VWL3 PDB 3EWE PDB 3F3F PDB 3F3G PDB 3F3P PDB 4XMM PDB 4XMN Pfam PF07575 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}. P32499 EBI-12401,EBI-12345 P35729 EBI-12345,EBI-11713 P36161 EBI-11722,EBI-12345 P40368 EBI-12331,EBI-12345 P53011 EBI-12345,EBI-16940 Q02630 EBI-11703,EBI-12345 Q02629 EBI-11698,EBI-12345 P22696 EBI-6679,EBI-12345 Q03790 EBI-12345,EBI-27321 Q05166 EBI-12345,EBI-3035 Q8WUM0 EBI-295695,EBI-12345 P49687 EBI-11730,EBI-12345 P52891 EBI-12337,EBI-12345 P51862 EBI-15702,EBI-12345 Q04491 EBI-16529,EBI-12345 Q07622 EBI-38674,EBI-12345 P32582 EBI-4167,EBI-12345 P38305 EBI-20939,EBI-12345 Q12315 EBI-7635,EBI-12345 GO:0031965 GO:0005643 GO:0031080 GO:0017056 GO:0006406 GO:0031081 GO:0045893 GO:0006606 GO:0000055 MTIDDSNRLLMDVDQFDFLDDGTAQLSNNKTDEEEQLYKRDPVSGAILVPMTVNDQPIEKNGDKMPLKFKLGPLSYQNMAFITAKDKYKLYPVRIPRLDTSKEFSAYVSGLFEIYRDLGDDRVFNVPTIGVVNSNFAKEHNATVNLAMEAILNELEVFIGRVKDQDGRVNRFYELEESLTVLNCLRTMYFILDGQDVEENRSEFIESLLNWINRSDGEPDEEYIEQVFSVKDSTAGKKVFETQYFWKLLNQLVLRGLLSQAIGCIERSDLLPYLSDTCAVSFDAVSDSIELLKQYPKDSSSTFREWKNLVLKLSQAFGSSATDISGELRDYIEDFLLVIGGNQRKILQYSRTWYESFCGFLLYYIPSLELSAEYLQMSLEANVVDITNDWEQPCVDIISGKIHSILPVMESLDSCTAAFTAMICEAKGLIENIFEGEKNSDDYSNEDNEMLEDLFSYRNGMASYMLNSFAFELCSLGDKELWPVAIGLIALSATGTRSAKKMVIAELLPHYPFVTNDDIEWMLSICVEWRLPEIAKEIYTTLGNQMLSAHNIIESIANFSRAGKYELVKSYSWLLFEASCMEGQKLDDPVLNAIVSKNSPAEDDVIIPQDILDCVVTNSMRQTLAPYAVLSQFYELRDREDWGQALRLLLLLIEFPYLPKHYLVLLVAKFLYPIFLLDDKKLMDEDSVATVIEVIETKWDDADEKSSNLYETIIEADKSLPSSMATLLKNLRKKLNFKLCQAFM 744 P46674 Nuclear mRNA export protein SAC3 SAC3 559292 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores. UNIPROT P46674 UNIPROT D6VSD9 PDB 3FWB PDB 3FWC PDB 3T5V PDB 4C31 PDB 4MBE PDB 4TRQ PDB 5G5P PDB 5L3T Pfam PF12209 Pfam PF03399 PROSITE PS50250 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}. P25491 EBI-16425,EBI-10420 Q06410 EBI-16425,EBI-30856 P10591 EBI-8591,EBI-16425 Q06677 EBI-16425,EBI-30084 P39987 EBI-22339,EBI-16425 P38788 EBI-24570,EBI-16425 P11484 EBI-16425,EBI-8627 P47079 EBI-16425,EBI-19072 P40150 EBI-8632,EBI-16425 P32589 EBI-8648,EBI-16425 Q05027 EBI-27500,EBI-16425 Q6WNK7 EBI-1251050,EBI-16425 P38129 EBI-18868,EBI-16425 Q08231 EBI-32097,EBI-16425 GO:0005737 GO:0044614 GO:0005634 GO:0070390 GO:0030029 GO:0000278 GO:0031124 GO:0006406 GO:0071033 GO:0000973 GO:0006611 GO:0042274 GO:0006283 MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKKSQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSIMEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVFARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENMLLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDNLASSVYVKDPKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTSPKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVHGDLSEQKQQQIKTVTDGGSPFVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQENADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQASYSQAKKNRILEEKKREEIKLVSHQLGVPGFKKSTCLFRTPYKGNVNSSFMLSSSDKNLIFSPVNDEFNKFATHLTKISKLWRPLEMQSIYYDNLTKKFPSNSLTPANLFIYAKDWTSLSNRWILSKFNLQTAQDSKKFSNNIISSRIICIDDEYEPSDFSDLQLLIFNTGVTNPDIFDLEMKLKDDGEELIKLITGISLNTNICFSLLIIYWESAENTLSESTIKHLLKLNRISKNYSSVIERIDLMNLTEESPHKCLEDKLSEISHSYVYKLTERGKYDKTLRQKRSLAGIHSRSTQLQTTKDIDQKMKKMLEKEKNKYQQQIGERNTYAHLESHIDASPRSKKRKLPILLSTSHSSQFKTPLASRLNTSGSSTSPPLPSHLAMKFRKNSRVTSLHTVLPVSTPSHSNNIPAASFSGNNTTDIQSQQLIENQKSTSVYLNNVSERILGNQEICQTPINPVTPVLDGADQGKEDIPDSILELKILIDSVKKKVNND 1301 P46822 Kinesin light chain klc 6239 Yes SL-0178 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}. UNIPROT P46822 UNIPROT Q18088 UNIPROT Q6BEW4 UNIPROT Q8I7M2 UNIPROT Q8TA80 UNIPROT Q95QV1 PROSITE PS01160 PROSITE PS50005 PROSITE PS50293 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}. P34609 EBI-315684,EBI-315578 Self EBI-315578,EBI-315578 Q23064-3 EBI-2902257,EBI-315578 Q23130 EBI-315578,EBI-328747 G5EFD7 EBI-315578,EBI-322609 O01482 EBI-315611,EBI-315578 Q17581 EBI-315606,EBI-315578 P91001 EBI-313007,EBI-315578 Q93228 EBI-315621,EBI-315578 G5EBU5 EBI-315617,EBI-315578 P25807 EBI-315630,EBI-315578 P91131 EBI-315625,EBI-315578 Q95Y99 EBI-315648,EBI-315578 H2L044 EBI-315644,EBI-315578 O01802 EBI-312854,EBI-315578 Q9XW20 EBI-315668,EBI-315578 Q9TZH8 EBI-315663,EBI-315578 P34540 EBI-315657,EBI-315578 Q95XR0 EBI-314404,EBI-315578 Q966C7 EBI-315672,EBI-315578 GO:0005623 GO:0005737 GO:0016938 GO:0005874 GO:0005635 GO:0019894 GO:0003777 GO:0048675 GO:0051295 GO:0040011 GO:0002119 GO:0030473 GO:0040038 GO:0048489 MSNMSQDDVTTGLRTVQQGLEALREEHSTISNTLETSVKGVKEDEAPLPKQKLSQINDNLDKLVCGVDETSLMLMVFQLTQGMDAQHQKYQAQRRRLCQENAWLRDELSSTQIKLQQSEQMVAQLEEENKHLKYMASIKQFDDGTQSDTKTSVDVGPQPVTNETLQELGFGPEDEEDMNASQFNQPTPANQMAASANVGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAANLLNEALSIREKCLGESHPAVAATLNNLAVLFGKRGKFKDAEPLCKRALEIREKVLGDDHPDVAKQLNNLALLCQNQGKYEEVEKYYKRALEIYESKLGPDDPNVAKTKNNLSSAYLKQGKYKEAEELYKQILTRAHEREFGQISGENKPIWQIAEEREENKHKGEGATANEQAGWAKAAKVDSPTVTTTLKNLGALYRRQGKYEAAETLEDVALRAKKQHEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS 540 P46892 Cyclin-dependent kinase 11B Cdk11b 10116 Yes SL-0178 SL-0182 SL-0198 Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cytoplasm, perinuclear region. UNIPROT P46892 Pfam PF00069 PROSITE PS50011 PROSITE PS00108 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}. GO:0031965 GO:0005634 GO:0048471 GO:0005524 GO:0004693 GO:0004674 GO:0001824 GO:0007049 GO:2001234 GO:0006468 GO:0001558 GO:0010468 GO:0007346 GO:0007088 GO:0050684 MKSEKSRTTSWLFQSHEVTEILGRVKKNRKKLVKGLHRAGPPPEKNYLPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPLTSIREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLSGVKHLHDNWILHRDLKTSNLLLTHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTACDMWSVGCIFGELLTQKPLFPGKSDIDQINKIFKDIGTPSEKIWPGYSELPAVKKMTFSELPYNNLRKRFGALLSDQGFDLMNKFLTYYPGRRINAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQCVKRGTSPKPPEGGLGYSQLGDDDLKETGFHLTTTNDGAVSCRPWCSLLF 436 P47054 Nucleoporin NUP192 NUP192 559292 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution). UNIPROT P47054 UNIPROT D6VWE4 PDB 4IFQ Pfam PF11894 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}. P34077 EBI-12056,EBI-25846 P35729 EBI-25846,EBI-11713 P40066 EBI-22648,EBI-25846 P40069 EBI-25846,EBI-9166 P22696 EBI-6679,EBI-25846 P32472 EBI-2883297,EBI-25846 P10591 EBI-25846,EBI-8591 P38788 EBI-25846,EBI-24570 P40150 EBI-8632,EBI-25846 P32589 EBI-8648,EBI-25846 P02829 EBI-25846,EBI-8659 Q12329 EBI-25846,EBI-8571 P10592 EBI-8603,EBI-25846 Q05166 EBI-25846,EBI-3035 Q04477 EBI-27228,EBI-25846 P23641 EBI-11178,EBI-25846 Q02630 EBI-11703,EBI-25846 P49687 EBI-25846,EBI-11730 Q03790 EBI-27321,EBI-25846 P02994 EBI-25846,EBI-6314 P38708 EBI-25846,EBI-24471 P02557 EBI-25846,EBI-18986 P09733 EBI-25846,EBI-18976 P00359 EBI-25846,EBI-7218 P41940 EBI-25846,EBI-11191 P00330 EBI-25846,EBI-2218 P38737 EBI-24359,EBI-25846 Q06625 EBI-37861,EBI-25846 P43587 EBI-22913,EBI-25846 P47087 EBI-26303,EBI-25846 P38305 EBI-20939,EBI-25846 Q12315 EBI-7635,EBI-25846 GO:0005643 GO:0044611 GO:0005634 GO:0017056 GO:0051028 GO:0006999 GO:0015031 GO:0046822 MKWSAIPFQTLYRSIESGEFDFDLFKEVLPDLQNLNLNTDKLKNNASRSQLEKGEIELSDGSTFKVNQEFIFEAISLSDELNLDEIVACELILSGDTTANNGKVQYFLRRQYILQIVSFIVNCFHEDTELYQELIKNGALVSNILSAFKFIHTQLSEIKQQINKAQILENYNALFQQNIKFRRDFLLREYDILSQILYGLVDKGAIMKNKDFILSLLHHVSELDSNDFFIIYYTPAFFHLFASLRVLPDADVKLLHSQFMKDLKDDSIYTKPVKVALIFIFFAYFIGWCKEDPKRRADTMDFKTDVDEPMTSAVELGAIEQILIFAADTSIVEQDKSMELFYDIRSLLERHIPRLIPKQLLDDEKIFSQTTNSTYNPASATDNMSGRGLWNPSYPGMMSTTGTARLNSMPNNVNEYSYTTIVLSDQTQEFFLSSFDDVLQTIITDCAFLLTKIKDAEEDSLLSGEDLTLDDISLKADLERFFLSIYFFYASRPEYSCTFWSDKESNAYGFIEWCSRCNDNLMRSCFYLMVSSLSFGPENALNVYHYFGENSSISWKNIAQCLSDYTKKISNFNSSLHKRQQFSESTHNDIDSTAVALEEGLNEEAVIFLSSLLTLVGSVTYQVDEDVKSSLSKVFSDVLFEFTKINTPLVGAAFKVISNLVPKLESSRTKFWSFLDSLIFKDSSLNYSSESYRNAFTNVLTKYSDVLGFLQLFHNLISIHSRENNSEYMVFGKLAFPTRLGQGYRKVGIWPYFDYIFNDILAHVDQIVDIRNKRAVQLPILKIIYTGLCSFDYSVILNSIPAAANLDALVDCENFFNYVQECPAIPIFNYIFTEKIYKSIFNVVDVGVDQLSIELEGGKNQAELLQLAVKIINKVLDYQETYVEELFPIVKKHGKTDYFLPKNYSLHGLRSFYDAIFFNIPLVAHLGLYVGVDDQILATNSLRILAKLSERSNGSVASLSKRNKLLTIFDSVDESARIKDAFITQLESSITDAGVLALKLELLDFLTSNLSNYSRTMTISHLLLGFQVSNVISLGPNLATFISSGTSLLDSLISVLEASLNSITKDNIDYAPMRLATAALEIILKLCRNPLTSGLLYSYLIKENFFERIMILDPQVTRFTTWNGSPFDNSTEEKCKNFIESESVGAFLSFLAYRNYWTQYLGLFIHKISFSGTKSEVLTYVNYLISNTMYSVRLFSFLDPLNYGNICEPKETLSIFTNVPLNLEQVTLNKYCSGNIYDFHKMENLMRLIKRVRAESLHSNSFSLTVSKEQFLKDADVECIKAKSHFTNIISRNKALELNLSVLHSWVQLVQIIVTDGKLEPSTRSNFILEVFGTIIPKISDYIEFNITFSEELVSLAVFLFDIYNRDRKLITDKGTVDGRLYQLFKTCIQGINSPLSSVALRSDFYILANHYLSRVLSDQVGSEKVLQDLRLGSKKLVEIIWNDVVYGEGTSRVTGILLLDSLIQLANRSKENFILDSLMKTTRLLLIIRSLKNTDALLNSTTEHINIDDLLYELTAFKATVFFLIRVAETRGGASALIENNLFRIIAELSFLKVDPDLGLDLMFDEVYVQNSKFLKVNVTLDNPLLVDKDANGVSLFELIVPIFQLISAVLVSMGSSNKAVVQTVKGLLNTYKRLVIGIFKRDLLREKEDKKNSSDPNNQSLNEMVKLIVMLCTLTGYQNND 1683 P47069 Spindle pole body assembly component MPS3 MPS3 559292 Yes SL-0178 SL-0182 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. UNIPROT P47069 UNIPROT D6VWG1 UNIPROT P47070 PROSITE PS51469 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}. Self EBI-25811,EBI-25811 Q08955 EBI-25811,EBI-31728 Q12366 EBI-25811,EBI-34568 P40348 EBI-25811,EBI-14992 Q12743 EBI-25811,EBI-33192 P53966 EBI-9999,EBI-25811 Q12404 EBI-25811,EBI-11184 P06197 EBI-25811,EBI-13458 Q06616 EBI-36065,EBI-25811 P32562 EBI-4440,EBI-25811 P43605 EBI-25811,EBI-22988 Q12692 EBI-8080,EBI-25811 Q03362 EBI-25811,EBI-2057915 P28791 EBI-25811,EBI-16572 P40504 EBI-10011,EBI-25811 Q04477 EBI-27228,EBI-25811 P40857 EBI-25811,EBI-26003 P47007 EBI-25811,EBI-26105 GO:0005623 GO:0005737 GO:0005825 GO:0016021 GO:0034993 GO:0000784 GO:0005635 GO:0031965 GO:0034399 GO:0005816 GO:0005524 GO:0043495 GO:0006348 GO:0034087 GO:0000741 GO:0045141 GO:0007064 GO:0006998 GO:0000743 GO:0030474 GO:0007129 GO:0034398 MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLDFPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGLFFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLPSNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSALISDVIESPGIGTAGSAESRWEYDLNRYVKEILSNELQYIDKDYFIQEMNRRLQSNKQEIWEEITNRLETQQQQQQQQVQQDYSNVPQQYSSILMKRLIHQIYNSNQHQWEDDLDFATYVQGTKLLNHLTSPTWRQGSGVQPIELLTDSKQSSSTYWQCENEPGCSWAIRFKTPLYLTKISYMHGRFTNNLHIMNSAPRLISLYVKLSQTKEIKALQTLANQYGFGQHHKRDRNYIKIAKFEYRLTDSRIRQQMYLPPWFIQLKPLVRSIVFQVDENYGNKKFISLRKFIINGVTPQDLQIIENNEFPVLLGDTPEYGVTQNTDEGKRKVLLSKPPYASSSTSTKFHPASNVPSFGQDELDQ 682 P48837 Nucleoporin NUP57 NUP57 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P48837 UNIPROT D6VUQ0 Pfam PF13634 Pfam PF13874 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}. P14907 EBI-12265,EBI-12324 P34077 EBI-12056,EBI-12324 P37198 EBI-347978,EBI-12324 P38181 EBI-11756,EBI-12324 P40066 EBI-22648,EBI-12324 Self EBI-12324,EBI-12324 Q02630 EBI-12324,EBI-11703 Q02629 EBI-12324,EBI-11698 Q06142 EBI-9145,EBI-12324 P49686 EBI-12310,EBI-12324 P49687 EBI-12324,EBI-11730 Q02199 EBI-12324,EBI-12315 P52891 EBI-12324,EBI-12337 Q06410 EBI-30856,EBI-12324 P10591 EBI-8591,EBI-12324 P22696 EBI-6679,EBI-12324 Q02959 EBI-8484,EBI-12324 P38265 EBI-21579,EBI-12324 P09435 EBI-8611,EBI-12324 P11484 EBI-12324,EBI-8627 P10592 EBI-12324,EBI-8603 P32589 EBI-12324,EBI-8648 P35177 EBI-17958,EBI-12324 Q04477 EBI-27228,EBI-12324 Q03330 EBI-7458,EBI-12324 Q6WNK7 EBI-1251050,EBI-12324 P53165 EBI-23812,EBI-12324 Q9NPJ6 EBI-12324,EBI-394607 P19012 EBI-12324,EBI-739566 P43365 EBI-12324,EBI-749530 Q08379 EBI-618309,EBI-12324 Q7Z6G3-2 EBI-12324,EBI-10172876 P13196 EBI-12324,EBI-3905054 Q5JR59-3 EBI-12324,EBI-11522433 Q8N6Y0 EBI-739895,EBI-12324 P02829 EBI-12324,EBI-8659 P38305 EBI-20939,EBI-12324 Q12315 EBI-7635,EBI-12324 GO:0031965 GO:0005643 GO:0044613 GO:0042802 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0006606 GO:0036228 MFGFSGSNNGFGNKPAGSTGFSFGQNNNNTNTQPSASGFGFGGSQPNSGTATTGGFGANQATNTFGSNQQSSTGGGLFGNKPALGSLGSSSTTASGTTATGTGLFGQQTAQPQQSTIGGGLFGNKPTTTTGGLFGNSAQNNSTTSGGLFGNKVGSTGSLMGGNSTQNTSNMNAGGLFGAKPQNTTATTGGLFGSKPQGSTTNGGLFGSGTQNNNTLGGGGLFGQSQQPQTNTAPGLGNTVSTQPSFAWSKPSTGSNLQQQQQQQIQVPLQQTQAIAQQQQLSNYPQQIQEQVLKCKESWDPNTTKTKLRAFVYNKVNETEAILYTKPGHVLQEEWDQAMEKKPSPQTIPIQIYGFEGLNQRNQVQTENVAQARIILNHILEKSTQLQQKHELDTASRILKAQSRNVEIEKRILKLGTQLATLKNRGLPLGIAEEKMWSQFQTLLQRSEDPAGLGKTNELWARLAILKERAKNISSQLDSKLMVFNDDTKNQDSMSKGTGEESNDRINKIVEILTNQQRGITYLNEVLEKDAAIVKKYKNKT 541 P49021 Protein timeless tim 7227 Yes SL-0198 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. UNIPROT P49021 UNIPROT A4V040 UNIPROT B7Z007 UNIPROT B7Z008 UNIPROT C9QPB7 UNIPROT M9MRE9 UNIPROT O44380 UNIPROT Q1WWF5 UNIPROT Q59E16 UNIPROT Q8I037 UNIPROT Q95U67 UNIPROT Q9VQR6 UNIPROT Q9VQR7 Pfam PF04821 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}. O77059 EBI-266295,EBI-94117 P07663 EBI-266295,EBI-496170 Q9VDY1 EBI-3414232,EBI-266295 M9NFI9 EBI-9933576,EBI-266295 Q24568 EBI-3406532,EBI-266295 Q9V480 EBI-171262,EBI-266295 Q9VQ30 EBI-93669,EBI-266295 Q960S0 EBI-160404,EBI-266295 P51123 EBI-499582,EBI-266295 Q24432 EBI-133159,EBI-266295 O61735 EBI-266295,EBI-143834 P18431 EBI-266295,EBI-242141 GO:0005737 GO:0005829 GO:0000790 GO:0000228 GO:0005654 GO:0005634 GO:0048471 GO:0032991 GO:0031298 GO:0003677 GO:0046982 GO:0008134 GO:0071482 GO:0048512 GO:0003053 GO:0007623 GO:0060086 GO:0007620 GO:0006281 GO:0000076 GO:0008062 GO:0009649 GO:0045475 GO:0007617 GO:0046957 GO:0000122 GO:2000678 GO:0009648 GO:0050766 GO:0006606 GO:0042749 GO:0045187 GO:0050764 GO:0042306 GO:0043111 GO:0048478 GO:0007622 GO:0030431 MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQNVRSDLIPLLENAKDDAVLESVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLYTSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNCLLLLRNILHIPETHAHCVMPMMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTLQKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMREGTAATLQEVSRKGQEYQNAMARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMDDGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPLNLTQQPADKVNNTTNPTSSAPQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKGKCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKPRTIMSPMDKKELRRKKLVKRSKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYLVEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDMEHIDTILTYDVLSYLTYEGVSLCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHITQFATLEVMHYYGILLEDFNNNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIWEADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEMTKEHNQEHTVCSWSQEEMDTLYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCFVKLTLRSGLKVPEGDHIMEPVAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQLPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDASELEDATASSPSRYHHTGPRNSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYTPDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTSMSTVNPTTTLSLNMLNTFMGSHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEMDVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEKEKELNSDNVSLASDLTRMYVSDEDDRLERTEIRVPHYH 1398 P49454 Centromere protein F CENPF 9606 Yes SL-0198 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. UNIPROT P49454 UNIPROT Q13171 UNIPROT Q13246 UNIPROT Q5VVM7 Pfam PF10490 Pfam PF10473 Pfam PF10481 OMIM 243605 OMIM 600236 DisGeNET 1063 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}.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. P43034 EBI-720620,EBI-968343 P32121 EBI-714559,EBI-968343 Q9GZM8 EBI-928842,EBI-968343 Q9NXR1 EBI-941227,EBI-968343 Q02224 EBI-968343,EBI-1375040 Q96JN8-2 EBI-16811547,EBI-968343 Q9NRI5 EBI-968343,EBI-529989 Q5S007 EBI-5323863,EBI-968343 A2AUM9 EBI-2554268,EBI-968343 P63005 EBI-917499,EBI-968343 Q8BZQ7 EBI-11026797,EBI-968343 Q96FF9 EBI-718805,EBI-968343 Q7TSY8 EBI-2552468,EBI-968343 Q99PT9 EBI-11092400,EBI-968343 Q13283 EBI-1047359,EBI-968343 Q08AG7 EBI-2637198,EBI-968343 P01106 EBI-447544,EBI-968343 Q9QYY8 EBI-11090415,EBI-968343 P70399 EBI-769130,EBI-968343 Q71F23 EBI-2515234,EBI-968343 Q8CI51 EBI-299301,EBI-968343 Q9Y253 EBI-2827270,EBI-968343 P25963 EBI-307386,EBI-968343 P46013 EBI-876367,EBI-968343 Q8TDR4 EBI-3923210,EBI-968343 Q96A37 EBI-2130320,EBI-968343 Q96AP7 EBI-4314670,EBI-968343 Q9UPY6 EBI-3907133,EBI-968343 Q7L5N1 EBI-486838,EBI-968343 Q15714 EBI-968343,EBI-712609 Q02539 EBI-932603,EBI-968343 Q9BYW2 EBI-968343,EBI-945869 P30040 EBI-946830,EBI-968343 P0DTD1 EBI-25475888,EBI-968343 Q9UQN3 EBI-718324,EBI-968343 P49356 EBI-602349,EBI-968343 Q96KS9 EBI-10290462,EBI-968343 Q96EY4 EBI-1045338,EBI-968343 Q9HD26-2 EBI-11102276,EBI-968343 Q96T17-2 EBI-16399739,EBI-968343 Q9UKA1 EBI-2692340,EBI-968343 Q9Y6K9-2 EBI-21581164,EBI-968343 Q9H2F9 EBI-2813327,EBI-968343 Q9Y2V7 EBI-3866319,EBI-968343 Q8N5R6-4 EBI-21699064,EBI-968343 GO:0005930 GO:0005623 GO:0005813 GO:0000775 GO:0036064 GO:0097539 GO:0000940 GO:0005737 GO:0005829 GO:0000776 GO:0030496 GO:0005635 GO:0016363 GO:0005654 GO:0005634 GO:0048471 GO:0045120 GO:0005819 GO:0000922 GO:0003682 GO:0070840 GO:0008022 GO:0042803 GO:0008134 GO:0030154 GO:0051301 GO:0007059 GO:0071897 GO:0001822 GO:0051382 GO:0051310 GO:0000278 GO:0007094 GO:0007517 GO:0045892 GO:0015031 GO:0051726 GO:0010389 GO:0016202 GO:0042493 GO:0021591 MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKTEGTNLKRENQRLMEICESLEKTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKRCKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYSGSKYEDLKEKYNKEVEERKRLEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRDFSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELRLQGHEKEMKGQVNKFQELQLQLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTALEQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEELSRQQRSFQTLDQECIQMKARLTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRSMEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDLQEKINQQENSLTLEKLKLAVADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLSALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENLQSKINHLETCLKTQQIKSHEYNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIENMCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDHQRSLLAFDQQPAMHHSFANIIGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLESQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAETSQRISKLQEDTSAHQNVVAETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSSIISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQEKLILLQRCEETGNAYEDLSQKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAKEHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNNSKSEAGGLKQEIMTLKEEQNKMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKEISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISGLKDCEIDAEEKYISGPHELSTSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTELNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGELVEDIPGGEFGEQPNEQHPVSLAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVDSLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGAVSANQCSVDEVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQELEQLLSSERQELDCLRKQYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQLQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSETTERTPKHDVHQICDKDAQQDLNLDIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPMDFLGNQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEACIELEKIVGELKKENSDLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGDNVAKVNDSWKERFLDVENELSRIRSEKASIEHEALYLEADLEVVQTEKLCLEKDNENKQKVIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLHCIQVAEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKEKELLVKESESLQARLSESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKLRVRIEADEKKQLHIAEKLKERERENDSLKDKVENLERELQMSEENQELVILDAENSKAEVETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLLEEKEQAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIEKLRARLEADEKKQLCVLQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKGEVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNELQKEQERISELEIINSSFENILQEKEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLELEKAQLLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQVEGEHQLWKEQNLELRNLTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDKMSFVEKVNKMTAKETELQREMHEMAQKTAELQEELSGEKNRLAGELQLLLEEIKSSKDQLKELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQYEVEIQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQLKKENERAQGKMKLLIKSCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIKELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEMLETQVAHLCSQQSKQDSRGSPLLGPVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKAVMSGIHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSPLSLGKENLAESSKPTAGGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSPREGLRVKRGRLVPSPKAGLESNGSENCKVQ 3114 P49686 Nucleoporin NUP42 NUP42 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. UNIPROT P49686 UNIPROT D6VSH5 PDB 6B4E 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}. P48837 EBI-12310,EBI-12324 Self EBI-12310,EBI-12310 Q06142 EBI-12310,EBI-9145 Q02630 EBI-12310,EBI-11703 Q02629 EBI-12310,EBI-11698 P49687 EBI-11730,EBI-12310 Q02199 EBI-12310,EBI-12315 Q05166 EBI-12310,EBI-3035 P52891 EBI-12310,EBI-12337 Q12315 EBI-7635,EBI-12310 Q03330 EBI-7458,EBI-12310 P38305 EBI-20939,EBI-12310 GO:0031965 GO:0005643 GO:0044613 GO:0044614 GO:0005634 GO:0017056 GO:0003714 GO:0071472 GO:0031990 GO:0006607 GO:0016973 GO:0000973 GO:0000972 MSAFGNPFTSGAKPNLSNTSGINPFTNNAASTNNMGGSAFGRPSFGTANTMTGGTTTSAFGMPQFGTNTGNTGNTSISAFGNTSNAAKPSAFGAPAFGSSAPINVNPPSTTSAFGAPSFGSTGFGAMAATSNPFGKSPGSMGSAFGQPAFGANKTAIPSSSVSNSNNSAFGAASNTPLTTTSPFGSLQQNASQNASSTSSAFGKPTFGAATNTQSPFGTIQNTSTSSGTGVSPFGTFGTNSNNKSPFSNLQSGAGAGSSPFGTTTSKANNNNNVGSSAFGTTNNQSPFSGGSGGTFGSASNLNKNTNGNFQSSFGNKGFSFGITPQNDANKVSQSNPSFGQTMPNTDPNISLKSNGNATSFGFGQQQMNATNVNANTATGKIRFVQGLSSEKDGILELADLAEETLKIFRANKFELGLVPDIPPPPALVA 430 P49687 Nucleoporin NUP145C NUP145 559292 Yes SL-0178 SL-0182 SL-0185 [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. UNIPROT P49687 UNIPROT D6VU53 PDB 3BG0 PDB 3BG1 PDB 3IKO PDB 3JRO PDB 3JRP PDB 3KEP PDB 3KES PDB 4XMM PDB 4XMN Pfam PF04096 Pfam PF13634 Pfam PF12110 PROSITE PS51434 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}. P32500 EBI-11730,EBI-11950 P35729 EBI-11713,EBI-11730 P38181 EBI-11756,EBI-11730 P40368 EBI-12331,EBI-11730 P46673 EBI-11730,EBI-12345 P47054 EBI-25846,EBI-11730 P48837 EBI-12324,EBI-11730 P49686 EBI-11730,EBI-12310 Self EBI-11730,EBI-11730 Q04491 EBI-11730,EBI-16529 P55735 EBI-1046596,EBI-11730 Q06142 EBI-9145,EBI-11730 Q02630 EBI-11703,EBI-11730 Q02629 EBI-11698,EBI-11730 P22696 EBI-6679,EBI-11730 P11484 EBI-8627,EBI-11730 P25294 EBI-17244,EBI-11730 P10591 EBI-11730,EBI-8591 P52891 EBI-12337,EBI-11730 Q04477 EBI-27228,EBI-11730 Q02199 EBI-11730,EBI-12315 P10592 EBI-11730,EBI-8603 P53011 EBI-11730,EBI-16940 P32582 EBI-4167,EBI-11730 Q03718 EBI-27756,EBI-11730 P53230 EBI-23156,EBI-11730 Q06411 EBI-576,EBI-11730 P47077 EBI-25778,EBI-11730 P38305 EBI-20939,EBI-11730 Q12315 EBI-7635,EBI-11730 GO:0000781 GO:0031965 GO:0005643 GO:0044613 GO:0044614 GO:0031080 GO:0016787 GO:0008139 GO:0003723 GO:0017056 GO:0006302 GO:0035392 GO:0006607 GO:0031081 GO:0016973 GO:0045893 GO:0000973 GO:0006606 GO:0036228 GO:0046822 GO:0006405 GO:0034398 GO:0006409 MFNKSVNSGFTFGNQNTSTPTSTPAQPSSSLQFPQKSTGLFGNVNVNANTSTPSPSGGLFNANSNANSISQQPANNSLFGNKPAQPSGGLFGATNNTTSKSAGSLFGNNNATANSTGSTGLFSGSNNIASSTQNGGLFGNSNNNNITSTTQNGGLFGKPTTTPAGAGGLFGNSSSTNSTTGLFGSNNTQSSTGIFGQKPGASTTGGLFGNNGASFPRSGETTGTMSTNPYGINISNVPMAVADMPRSITSSLSDVNGKSDAEPKPIENRRTYSFSSSVSGNAPLPLASQSSLVSRLSTRLKATQKSTSPNEIFSPSYSKPWLNGAGSAPLVDDFFSSKMTSLAPNENSIFPQNGFNFLSSQRADLTELRKLKIDSNRSAAKKLKLLSGTPAITKKHMQDEQDSSENEPIANADSVTNIDRKENRDNNLDNTYLNGKEQSNNLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAAVSNFVIGRRGYGCITFQHDVDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKKTKKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFSIWGLVNEEDAEIDEDDLSKQEDGGEQPLRKVRTLAQSKPSDKEVILKTDGTFGTLSGKDDSIVEEKAYEPDLSDADFEGIEASPKLDVSKDWVEQLILAGSSLRSVFATSKEFDGPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEIEKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVSQIGPEIEEKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSIDKNISKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKFSLPYDDPIGVIFQLYAANENTEKLYKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMREITLLRASTNDHILNRLKIPSQLIFNAQALKDRYEGNYLSEVQNLLLGSSYDLAEMAIVTSLGPRLLLSNNPVQNNELKTLREILNEFPDSERDKWSVSINVFEVYLKLVLDNVETQETIDSLISGMKIFYDQYKHCREVAACCNVMSQEIVSKILEKNNPSIGDSKAKLLELPLGQPEKAYLRGEFAQDLMKCTYKI 1317 P49790 Nuclear pore complex protein Nup153 NUP153 9606 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P49790 UNIPROT B4DIK2 UNIPROT E7EPX5 UNIPROT F6QR24 UNIPROT Q4LE47 UNIPROT Q5T9I7 UNIPROT Q7Z743 PDB 2EBQ PDB 2EBR PDB 2EBV PDB 2GQE PDB 4U0C PDB 4U0D PDB 5TSV PDB 5TSX PDB 6AYA Pfam PF08604 Pfam PF10599 Pfam PF00641 PROSITE PS01358 PROSITE PS50199 OMIM 603948 DisGeNET 9972 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}. A8CG34 EBI-286779,EBI-2880179 O15504 EBI-286779,EBI-2515057 P02545 EBI-351935,EBI-286779 P12270 EBI-286779,EBI-1048528 P46060 EBI-286779,EBI-396091 Q9UPY3 EBI-395506,EBI-286779 Q92973 EBI-286779,EBI-286693 Q14974 EBI-286779,EBI-286758 Q8WUF5 EBI-5550163,EBI-286779 Q13625 EBI-77642,EBI-286779 P62826 EBI-286642,EBI-286779 Q96DB2 EBI-301713,EBI-286779 Q5S007 EBI-5323863,EBI-286779 P25054 EBI-727707,EBI-286779 Q9Y2K6 EBI-2511991,EBI-286779 Q8IY92 EBI-2370740,EBI-286779 P03372 EBI-78473,EBI-286779 Q9QWT9 EBI-2552204,EBI-286779 E9PVX6 EBI-2553009,EBI-286779 P51784 EBI-306876,EBI-286779 Q8BH74 EBI-2554056,EBI-286779 Q9ERU9 EBI-643756,EBI-286779 E9PUA5 EBI-10972016,EBI-286779 Q6PFD9 EBI-646104,EBI-286779 P57740 EBI-295687,EBI-286779 Q9BPU9 EBI-6958971,EBI-286779 Q8VE37 EBI-8006911,EBI-286779 P63280 EBI-80180,EBI-286779 Q80U93 EBI-2551193,EBI-286779 Q96EE3 EBI-922818,EBI-286779 O14862 EBI-6253193,EBI-286779 P18754 EBI-286779,EBI-992720 O00629 EBI-286779,EBI-396343 Q8TEM1 EBI-286779,EBI-372826 Q9H9A5 EBI-286779,EBI-1054261 Q53GS7 EBI-286779,EBI-1955541 P78406 EBI-286779,EBI-724495 Q8NFH5 EBI-286779,EBI-9050429 Q8IXQ5-2 EBI-286779,EBI-10981566 Q9NXE4-2 EBI-286779,EBI-10966436 J3KMX2 EBI-286779,EBI-11076792 P52948-5 EBI-286779,EBI-5280407 P52292 EBI-286779,EBI-349938 P63165 EBI-286779,EBI-80140 Q8WUM0 EBI-286779,EBI-295695 Q9NRG9 EBI-286779,EBI-3912901 Q69YH5 EBI-286779,EBI-6911908 P61956-2 EBI-286779,EBI-10966382 Q96HA1 EBI-286779,EBI-739990 Q9UKX7 EBI-286779,EBI-2371082 P33991 EBI-286779,EBI-374938 P62136 EBI-286779,EBI-357253 O14715 EBI-286779,EBI-2560912 O00505 EBI-286779,EBI-358297 P63279 EBI-286779,EBI-80168 Q9BW27 EBI-286779,EBI-716392 Q03188 EBI-286779,EBI-295799 Q8NFH4 EBI-286779,EBI-2563158 P49792 EBI-286779,EBI-973138 Q8NFH3 EBI-286779,EBI-1059321 Q969G3 EBI-286779,EBI-455078 Q9UBU9 EBI-286779,EBI-398874 O60684 EBI-286779,EBI-359923 O95373 EBI-286779,EBI-286735 Q99567 EBI-286779,EBI-726178 Q86XI6 EBI-286779,EBI-3918864 Q9BTX1-2 EBI-286779,EBI-10966386 Q8N1F7 EBI-286779,EBI-1042703 Q9HC62 EBI-286779,EBI-714881 Q96SK2 EBI-286779,EBI-10963859 P52294 EBI-286779,EBI-358383 Q8TAQ2 EBI-286779,EBI-357418 Q96EE3-1 EBI-286779,EBI-10966390 Q92621 EBI-286779,EBI-1045046 Q9P0U3-2 EBI-286779,EBI-10967520 Q5SRE5 EBI-286779,EBI-1049404 Q12769 EBI-286779,EBI-295715 Q9BW19 EBI-286779,EBI-2107279 E9PF10 EBI-286779,EBI-10966422 Q6NUQ4 EBI-286779,EBI-372318 P35658-2 EBI-286779,EBI-10969485 Q9UN86-2 EBI-11035716,EBI-286779 Q05322 EBI-6153153,EBI-286779 Q13618 EBI-456129,EBI-286779 A0A0F7R9Q0 EBI-2815990,EBI-286779 A0A0F7RG11 EBI-2815999,EBI-286779 Q9ZC54 EBI-2846248,EBI-286779 P01106 EBI-447544,EBI-286779 Q8WUY9 EBI-3924857,EBI-286779 P36873-2 EBI-3964623,EBI-286779 Q9GZY0 EBI-444173,EBI-286779 Q8N9Q2 EBI-10268630,EBI-286779 Q2NL82 EBI-358058,EBI-286779 Q9UKX7-2 EBI-10966378,EBI-286779 Q9BXS6-2 EBI-10969852,EBI-286779 GO:0005829 GO:0043657 GO:0016020 GO:0042405 GO:0031965 GO:0034399 GO:0005643 GO:0044613 GO:0044615 GO:0005730 GO:0005654 GO:0003677 GO:0042802 GO:0046872 GO:0008139 GO:0043495 GO:0017056 GO:0075733 GO:0006406 GO:0046832 GO:0051292 GO:0006606 GO:0016925 GO:1900034 GO:0060964 GO:0006110 GO:0006405 GO:0006409 GO:0046718 GO:0075732 GO:0016032 GO:0019083 MASGAGGVGGGGGGKIRTRRCHQGPIKPYQQGRQQHQGILSRVTESVKNIVPGWLQRYFNKNEDVCSCSTDTSEVPRWPENKEDHLVYADEESSNITDGRITPEPAVSNTEEPSTTSTASNYPDVLTRPSLHRSHLNFSMLESPALHCQPSTSSAFPIGSSGFSLVKEIKDSTSQHDDDNISTTSGFSSRASDKDITVSKNTSLPPLWSPEAERSHSLSQHTATSSKKPAFNLSAFGTLSPSLGNSSILKTSQLGDSPFYPGKTTYGGAAAAVRQSKLRNTPYQAPVRRQMKAKQLSAQSYGVTSSTARRILQSLEKMSSPLADAKRIPSIVSSPLNSPLDRSGIDITDFQAKREKVDSQYPPVQRLMTPKPVSIATNRSVYFKPSLTPSGEFRKTNQRIDNKCSTGYEKNMTPGQNREQRESGFSYPNFSLPAANGLSSGVGGGGGKMRRERTRFVASKPLEEEEMEVPVLPKISLPITSSSLPTFNFSSPEITTSSPSPINSSQALTNKVQMTSPSSTGSPMFKFSSPIVKSTEANVLPPSSIGFTFSVPVAKTAELSGSSSTLEPIISSSAHHVTTVNSTNCKKTPPEDCEGPFRPAEILKEGSVLDILKSPGFASPKIDSVAAQPTATSPVVYTRPAISSFSSSGIGFGESLKAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPGTKSGFKGFDTSSSSSNSAASSSFKFGVSSSSSGPSQTLTSTGNFKFGDQGGFKIGVSSDSGSINPMSEGFKFSKPIGDFKFGVSSESKPEEVKKDSKNDNFKFGLSSGLSNPVSLTPFQFGVSNLGQEEKKEELPKSSSAGFSFGTGVINSTPAPANTIVTSENKSSFNLGTIETKSASVAPFTCKTSEAKKEEMPATKGGFSFGNVEPASLPSASVFVLGRTEEKQQEPVTSTSLVFGKKADNEEPKCQPVFSFGNSEQTKDENSSKSTFSFSMTKPSEKESEQPAKATFAFGAQTSTTADQGAAKPVFSFLNNSSSSSSTPATSAGGGIFGSSTSSSNPPVATFVFGQSSNPVSSSAFGNTAESSTSQSLLFSQDSKLATTSSTGTAVTPFVFGPGASSNNTTTSGFGFGATTTSSSAGSSFVFGTGPSAPSASPAFGANQTPTFGQSQGASQPNPPGFGSISSSTALFPTGSQPAPPTFGTVSSSSQPPVFGQQPSQSAFGSGTTPNSSSAFQFGSSTTNFNFTNNSPSGVFTFGANSSTPAASAQPSGSGGFPFNQSPAAFTVGSNGKNVFSSSGTSFSGRKIKTAVRRRK 1475 P49903 Selenide, water dikinase 1 SEPHS1 9606 Yes SL-0178 SL-0182 [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}. UNIPROT P49903 UNIPROT B4DWK0 UNIPROT D3DRS9 UNIPROT D6PSQ9 UNIPROT Q5T5U8 UNIPROT Q5T5U9 UNIPROT Q9BVT4 PDB 3FD5 PDB 3FD6 Pfam PF00586 Pfam PF02769 OMIM 600902 DisGeNET 22929 Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}. P32456 EBI-714388,EBI-714091 Self EBI-714091,EBI-714091 Q9NRI5 EBI-714091,EBI-529989 Q2TAL8 EBI-714091,EBI-2798044 P24278 EBI-714091,EBI-739899 Q6GPH4 EBI-2815120,EBI-714091 Q13618 EBI-456129,EBI-714091 O60739 EBI-714091,EBI-1043343 Q9UBN6 EBI-714091,EBI-1044859 P21673 EBI-714091,EBI-711613 Q8N357 EBI-713484,EBI-714091 Q96ID5 EBI-713314,EBI-714091 Q13432 EBI-711260,EBI-714091 Q96E40 EBI-722584,EBI-714091 Q8TF50 EBI-11035148,EBI-714091 O95125 EBI-751960,EBI-714091 Q6S9Z5 EBI-17269964,EBI-714091 Q8N554 EBI-750821,EBI-714091 Q9UPG8 EBI-2876622,EBI-714091 Q6IQ23 EBI-2125301,EBI-714091 Q14774 EBI-6678255,EBI-714091 Q9UKR5 EBI-711490,EBI-714091 Q14194 EBI-473101,EBI-714091 GO:0005737 GO:0031965 GO:0005886 GO:0005524 GO:0005525 GO:0042802 GO:0046982 GO:0042803 GO:0004756 GO:0006464 GO:0016260 MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS 392 P50393 Lysophospholipase Pla2g4a 10116 No SL-0178 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}. UNIPROT P50393 Pfam PF00168 Pfam PF01735 PROSITE PS50004 PROSITE PS51210 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}. GO:0005737 GO:0005829 GO:0005783 GO:0005794 GO:0043231 GO:0005634 GO:0048471 GO:0042588 GO:0005509 GO:0047498 GO:0005544 GO:0035035 GO:0004622 GO:0004623 GO:0102567 GO:0102568 GO:0007568 GO:0019369 GO:0050482 GO:0071236 GO:0046697 GO:0046475 GO:0046456 GO:0001554 GO:0001542 GO:0043065 GO:0030501 GO:0008284 GO:0031622 GO:0050729 GO:0031394 GO:0031340 GO:0042127 GO:0051592 GO:0051384 GO:0009408 GO:0009725 GO:0042542 GO:0032496 GO:0010226 GO:0051597 GO:0010033 GO:0010243 GO:0033280 GO:0043129 MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRRQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSTTLSSLKEKVSAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEDAEREYQNDNQASWVHRMLMALVSDSALFNTREGRAGKEHNFMLGLNLNTSYPLSPLRDFSPQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQNPSRCSVSLSNVEARKFFNKEFLSKPTAESI 752 P50613 Cyclin-dependent kinase 7 CDK7 9606 Yes SL-0198 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. UNIPROT P50613 UNIPROT Q9BS60 UNIPROT Q9UE19 PDB 1LG3 PDB 1PA8 PDB 1UA2 PDB 2HIC PDB 6O9L Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 601955 DisGeNET 1022 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}. O15027 EBI-1245958,EBI-357515 P12270 EBI-1245958,EBI-1048528 P32121 EBI-714559,EBI-1245958 Q16543 EBI-1245958,EBI-295634 Q14684 EBI-1245958,EBI-372051 Q14241 EBI-1245958,EBI-742350 Q13889 EBI-1245958,EBI-6380459 Q13888 EBI-1245958,EBI-1565170 Q13823 EBI-1245958,EBI-1043365 Q13610 EBI-1245958,EBI-1050630 Q13011 EBI-1245958,EBI-711968 P55199 EBI-1245958,EBI-1245868 P51948 EBI-1245958,EBI-716139 P51946 EBI-1245958,EBI-741406 P46013 EBI-1245958,EBI-876367 P32780 EBI-1245958,EBI-715539 P29083 EBI-1245958,EBI-5462215 P28715 EBI-1245958,EBI-765885 P21127 EBI-1245958,EBI-1298 P19447 EBI-1245958,EBI-1183307 P18074 EBI-1245958,EBI-6380590 O75683 EBI-1245958,EBI-2691252 O00541 EBI-1245958,EBI-1053271 Q9Y5Q9 EBI-1245958,EBI-1054873 Q9Y5Q8 EBI-1245958,EBI-1045409 Q9Y4W2 EBI-1245958,EBI-1051591 Q9Y2X9 EBI-1245958,EBI-396200 Q9Y2G7 EBI-1245958,EBI-16770406 Q9H9Y6 EBI-1245958,EBI-355441 Q9H9B1 EBI-1245958,EBI-766087 Q9BYE7 EBI-1245958,EBI-1048026 Q9BTC8 EBI-1245958,EBI-2461787 Q8IWI9 EBI-1245958,EBI-2815196 Q6P1X5 EBI-1245958,EBI-1560063 Q5UIP0 EBI-1245958,EBI-711331 Q15542 EBI-1245958,EBI-1560145 Q13206 EBI-1245958,EBI-2514399 Q12789 EBI-1245958,EBI-357956 P62891 EBI-1245958,EBI-8830744 P49848 EBI-1245958,EBI-1560206 P49642 EBI-1245958,EBI-726050 P38432 EBI-1245958,EBI-945751 P29084 EBI-1245958,EBI-2853321 P21675 EBI-1245958,EBI-491289 O95602 EBI-1245958,EBI-359472 O00268 EBI-1245958,EBI-1034261 Q9NXF1 EBI-1245958,EBI-2371062 Q96PZ0 EBI-1245958,EBI-1052964 Q8WUA4 EBI-1245958,EBI-1237062 Q7Z4V5 EBI-1245958,EBI-1049136 O15355 EBI-1245958,EBI-725702 Q13042 EBI-1245958,EBI-994830 Q8N1G0 EBI-1245958,EBI-1210558 P30260 EBI-1245958,EBI-994813 Q96ME7 EBI-1245958,EBI-10986895 Q8TDI0 EBI-1245958,EBI-1042816 Q7Z5K2 EBI-1245958,EBI-1022242 Q9NW82 EBI-1245958,EBI-2515581 Q9Y3C7 EBI-1245958,EBI-394707 Q9Y2R4 EBI-1245958,EBI-395458 Q9UK58 EBI-1245958,EBI-2836773 Q9NY93 EBI-1245958,EBI-372376 Q9NX58 EBI-1245958,EBI-713507 Q9NW13 EBI-1245958,EBI-2878099 Q9NVC6 EBI-1245958,EBI-394562 Q9H0A0 EBI-1245958,EBI-876527 Q9BZE4 EBI-1245958,EBI-1056249 Q96S94 EBI-1245958,EBI-1045974 Q92759 EBI-1245958,EBI-6380495 Q92621 EBI-1245958,EBI-1045046 Q8TF01 EBI-1245958,EBI-3437793 Q8IY81 EBI-1245958,EBI-744088 Q8IX01 EBI-1245958,EBI-949116 Q6ZYL4 EBI-1245958,EBI-6380438 Q6PD62 EBI-1245958,EBI-1019583 P03372 EBI-78473,EBI-1245958 Q01094 EBI-448924,EBI-1245958 A0A0H2W2U3 EBI-2845132,EBI-1245958 P51659 EBI-1245958,EBI-358398 P01909 EBI-1245958,EBI-713389 P15927 EBI-1245958,EBI-621404 P56270 EBI-1245958,EBI-1809742 P0DMV8 EBI-1245958,EBI-11052499 Q7Z739 EBI-1245958,EBI-2849837 Q709F0 EBI-1245958,EBI-2880718 P62633 EBI-1245958,EBI-1047529 O15235 EBI-1245958,EBI-712205 Q6P1K8 EBI-8469755,EBI-1245958 P14635 EBI-1245958,EBI-495332 Q58FG0 EBI-1245958,EBI-11323222 Q9UBF8-2 EBI-1245958,EBI-16107849 Q96NH3-4 EBI-1245958,EBI-21548859 Q8IZL9 EBI-1245958,EBI-6128565 Q58FG1 EBI-1245958,EBI-6916562 Q58FF7 EBI-1245958,EBI-9996483 Q58FF6 EBI-1245958,EBI-6916503 Q13451 EBI-1245958,EBI-306914 Q13137 EBI-1245958,EBI-739580 P46527 EBI-1245958,EBI-519280 P24864 EBI-1245958,EBI-519526 P20248 EBI-1245958,EBI-457097 P08238 EBI-1245958,EBI-352572 P07900-2 EBI-1245958,EBI-6190772 P24941 EBI-375096,EBI-1245958 P01023 EBI-1245958,EBI-640741 P48740 EBI-1245958,EBI-6380536 P23634 EBI-1245958,EBI-1174388 P78362 EBI-593303,EBI-1245958 Q96SB4 EBI-539478,EBI-1245958 Q02539 EBI-932603,EBI-1245958 O96006 EBI-740037,EBI-1245958 GO:0019907 GO:0005737 GO:0005654 GO:0005634 GO:0048471 GO:0005675 GO:0070985 GO:0050681 GO:0005524 GO:0004693 GO:0008094 GO:0016301 GO:0008022 GO:0004672 GO:0004674 GO:0008353 GO:0003713 GO:0006370 GO:0030521 GO:0007050 GO:0051301 GO:0000082 GO:0000086 GO:0006294 GO:0045944 GO:0045893 GO:0006468 GO:0050821 GO:0000079 GO:0042795 GO:0006363 GO:0006366 GO:0006362 GO:0006368 GO:0006361 GO:0006367 GO:0006283 MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF 346 P50995 Annexin A11 ANXA11 9606 Yes SL-0178 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}. UNIPROT P50995 UNIPROT B4DVE7 Pfam PF00191 PROSITE PS00223 PROSITE PS51897 OMIM 602572 OMIM 617839 DisGeNET 311 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}.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. O15162 EBI-715243,EBI-740019 O75340 EBI-352915,EBI-715243 Q8IUH5 EBI-715243,EBI-524753 Q9WVM1 EBI-2552104,EBI-715243 Q80UG5 EBI-772170,EBI-715243 Q91ZJ0 EBI-11131709,EBI-715243 Q15828 EBI-7163527,EBI-715243 Q93034 EBI-1057139,EBI-715243 Q81ZA2 EBI-2811440,EBI-715243 Q0WDP0 EBI-715243,EBI-2843240 Q5NHS4 EBI-2798955,EBI-715243 P31942 EBI-715243,EBI-711437 Q53EZ4 EBI-747776,EBI-715243 Q92734 EBI-715243,EBI-357061 P60033 EBI-712921,EBI-715243 Q96AE4-2 EBI-12121668,EBI-715243 Q8NI38 EBI-10271199,EBI-715243 Q52LG2 EBI-11953846,EBI-715243 P15289 EBI-2117357,EBI-715243 Q9NZC7-5 EBI-12040603,EBI-715243 Q3LI66 EBI-11962084,EBI-715243 P09104 EBI-715243,EBI-713154 GO:0042582 GO:0062023 GO:0005737 GO:0005829 GO:0070062 GO:0042470 GO:0016020 GO:0030496 GO:0005635 GO:0005654 GO:0045335 GO:0042581 GO:0005819 GO:0005509 GO:0005544 GO:0048306 GO:0023026 GO:0008429 GO:0003723 GO:0044548 GO:0032506 GO:0006909 GO:0051592 MSYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDYLSGMAANMSGTFGGANMPNLYPGAPGAGYPPVPPGGFGQPPSAQQPVPPYGMYPPPGGNPPSRMPSYPPYPGAPVPGQPMPPPGQQPPGAYPGQPPVTYPGQPPVPLPGQQQPVPSYPGYPGSGTVTPAVPPTQFGSRGTITDAPGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDIYEIKEAIKGVGTDEACLIEILASRSNEHIRELNRAYKAEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLAQRDAQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEEGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSETDLLDIRSEYKRMYGKSLYHDISGDTSGDYRKILLKICGGND 505 P52297 Importin subunit beta kpnb1 8355 No SL-0178 Cytoplasm {ECO:0000250|UniProtKB:Q14974}. Nucleus envelope {ECO:0000250|UniProtKB:Q14974}. UNIPROT P52297 UNIPROT B0LM40 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000269|PubMed:7878057}. P20676 EBI-618940,EBI-12392 A5XAW2 EBI-3511040,EBI-618940 A0A1L8G4G8 EBI-3645294,EBI-618940 Q6PAY1 EBI-6285025,EBI-618940 Q91349 EBI-6285043,EBI-618940 Q6DCP4 EBI-619012,EBI-618940 P62826 EBI-286642,EBI-618940 GO:0005737 GO:0005635 GO:0008536 GO:0006606 MELVTILEKTVSPDRNELEAAQKFLEQAAVENLPTFVVELSKVLANPANSQVARVAAGLQIKNPLTSRDPDVKAQYQQRWLAIDASARGEIKTYVLRTLGTESYRPSSASQCVAGIACAEITVNQWPQLIPQLVANVTDPNSTERMKESTLEAIGYICQDIDPEQLQHKSNEILTAIIQGMRKEEPSNNVRLAATNALLNSLEFTKANFDKESERHYIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITVEAMKNEIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPESCQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLGAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPSSYCLSSSFEVIVQKLLETTDRPDGHQNNLRSAAYEALMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQVESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGAEFLKYMEAFKPFLTIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEMMQFLLENLGNENVHRSVKPQILSVFGDVALAIGGEFKKYLDVVLNTLQQASQAQVDKSDYDMVDYLNELREGCIEAYTGIIQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDSVVACGAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKTKTLATWATKELRKLKNQA 876 P52302 Protein lethal(3)malignant blood neoplasm 1 l 7227 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:8174791}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8174791}. Note=Mainly around the nucleus. UNIPROT P52302 UNIPROT Q59E19 UNIPROT Q8MS87 UNIPROT Q9VRU6 Pfam PF00379 PROSITE PS51155 Required for differentiation of the phagocytic blood-cell type, the plasmatocyte. {ECO:0000269|PubMed:8174791}. GO:0062129 GO:0048471 GO:0005886 GO:0008010 GO:0040003 MSLKLMAFVCALLLLCTLTHVLSAATTVRPYKFGFTIDEQQHRAEKRDERGIIMGEFGFITADGIYHVTVYATDEEGKFRIISMKSYPYAGPVGSKSVPVTTTPKVLLPAAPVALPKYNFNSEACSGCFLKKSPPKTEIRTLSQPLAPVQPGKPDGSSDIGLNVQLPFRESIAQTVASRLGLLQDTLQTSNTNTNAPNTKTIELGLNIAMSTYYTTKNAVTGHVSTQTSNSQTPSANTKIDYNVGVVEKASPPVYRPLNIRLNEDVMRQAITYGNTIPGHVPLPNQPLVETSLLPASQVKIFALDGNAKVPLASNIQSVAQHPNAGLNAKVPLASNIQSVAQHPNAGLNAKVPLASNIQSVAQHPNAGLKNINRSGVSSAKTLANTKTRPPHTFNPHQTPLLSSATAPGISGVTANTPTGNVPSNGGGIAAGKAPGNPQAGGSGGIIGAGAPGGRKVSAGGIGSGSAIGGVSGGSKASGNGGAIGSGSAIGGGATGSKASGFGFGSNIGGGVSGSKPSGFGSESKIGGPDSGSKALGFGSGSKIGGGITGTKASGFGGEIGSGRGSASSATGDLYKFKYILDYNGHEETGGRNGDKQGSYFAIGEDAVQRTIEYIANEFGFQPHVSWRKLDAKEALPEENSLKHYEFKWFNQE 653 P52370 Envelope glycoprotein M gM 10323 No SL-0415 SL-0418 SL-0419 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}. UNIPROT P52370 UNIPROT O39493 Pfam PF01528 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}. GO:0044175 GO:0044177 GO:0044178 GO:0033644 GO:0044201 GO:0016021 GO:0019031 GO:0019012 GO:0055036 MAGSAQPAAVHWRLWLAQVGVFAGLALLLLITLIGAASPGAGLPCFYAAIVNYNARNLSADGGAWAQRELGARHPALFLETPTTAAFSAYTAVVLLAVAAFDVAAAIIIRRENSGGFAAAYHMNALATLATPPGALLLGALAAWTLQAAVLLLSHKIMVLAAATYLAHLAPPAAFVGLFCTAGLPGAEYAQAVHALRERSPRAHRLLGPGRAVMINLAGGLLALIIGTAPLMLGQLLGAGLGLSLAQTVVAGVTVFCLAAVLFLVLTELVLSRYTQVLPGPAFGTLVAASCIAVASHDYFHQLRGVVRTQAPRAAARVKLALAGVALLAVAMLVLRLVRACLHHRRKGSAFYGHVSAARQQAARYIARARSSRGMAPLEGDAAALLDRGVASDDEEAVYEAHAPPRPPTIPLRRPEVPHSRASHPRPPPRSPPPAHVK 438 P52371 Envelope glycoprotein M gM 82831 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P52371 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MKSSKSDLFIYKTWFKLLVLYFVMFVLSATVPIAASFPGLGFPCYYNALVNYSAINLTERNVAKHLTPTLYLEEPEMFAYMTFTFLVDCFAAVYYFLGALAIMLAKRHFVVSLTTLSQWIAMVGTPTLILIGMWRMWTIQLFIQTLSYKHIYLSAFVYLIHFLLSFLHTQCYISRNSQLWSLKVLEQGIPPNTLLDTVVFTIKPLLANCQLFCLGLEMLVFSLSFMMAIGNSFYVLVSDIVFGAINLYLALVLFWVLLTELYLVKYMTFVMGFYLGGLIGCIFLLVPLWRYEQIFVAANLRSPILINILVIFFLCTLSALVRLLRMTWFSPTKPSYEPIQLKNIKHRRVKLQSPSGPSILEEGSSDEGSEDSEEEEEL 378 P52372 Envelope glycoprotein M gM 57278 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P52372 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MALSRVDVINMRIWVLSIICACLTYVNVTVHLVAVHFPNLGFPCAYYEINDMKAINLSIRNDIRSLTPQLYLNPIQLICYVVFMDICFFFILVYYIVCCVKVFSSEKTPNINQSTRDITWMGDSLSCFQFVLTMDTYQFFVTCLSFRLVTLAAFTYCLFFICFTAFTLTMITQYQSSERSFFVLKRIHPKLKGTIKYKTIIINMIELMLGFSSMVFAITICLGLGNNFYIKSSTVAFASINTFFVMSFVYSLVIELILHQYVKVQFGLHFGILFGILGLTYPILKYDSLFKTEWTVKFIVNLAVITIVCLSFIICRLIRFFMRKHHNYKKLPTTVEDLDVLEEANE 346 P52373 Envelope glycoprotein M gM 69156 No SL-0415 SL-0418 SL-0419 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}. UNIPROT P52373 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MAKAGVMTLSHVDRMNLRTWTMAIACCLLSFVNIVVFSVAAHFPGIGFPCYYPRIIDFDNMNLTMYNAIHHLTPQLFLDPVQLIVYVIFTELIFFCVLSYYIVCWVQIYFRSEHGTQVNQSTRDINFMGDSATCFTFVLTMDTFQIFLLSLSFRLPSMVAFSKCMYFMCLTAFVVTLVTHYESRERSAFALSKIHPKLQGTIRYRTAVVNLTQLILGFATMVLAMSLALGFGNSFFVKTAHVVFGAMVAFAIVACVYFSIIESVLSRYMKVQFGYHIGTILGVCGAMYPIIRYEALNASSYARDINIGITVLLLLCVAFSVIRTVRFLLRRNKRYRALALDNEEIRALRSDAE 353 P52449 Envelope glycoprotein M gM 36351 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P52449 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MASSRVDTINLRIWLVSIICAALSFINVTVHLIAINFPNLGFPCAYFEINDLKAVNLSANNEIYQMTHQLYINPVQIICYVLIMAILFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYSIFFVCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLSELMLGYSTMFLGITTCLGVGNSIYIRSITVAFSSINTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLSVVAIISIGFIICRLVRYLVKKKRRYKQLLNAESSSLMDENE 344 P52465 Nuclear egress protein 2 NEC2 10370 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P52465 Pfam PF04541 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}. GO:0044201 GO:0016021 MANVLKEKMYDELLSATCRILKLGSHDYRITERNLLSKNPKFPLCDIILKLDYAYNLEYLLSLWEHVTKQEPRFVFKNTGGAVSMSCYLHAPVKVEGHHAVRECNILRVNECLTVRMSDIVAMKPSTFAVFTKCIIRRNRDDTYVVEFVAFGPENESEYISLLKAIFLKKCSMGKQHLESNRFCQGLRRRSSHVLEKGRFESSGKVVNKASAVVTSQESIKQFYEKEKSLLSGVKFWRLSERHCRFALVGICFLLALYFCYVLLKKTPTPASGSVV 276 P52466 Nuclear egress protein 2 NEC2 57278 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P52466 Pfam PF04541 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}. GO:0044201 GO:0016021 MLKEKMYDELILSTCRVLKLGPADFRVTDKNLFSKNPKFPLCDILLKLDFAYSLEYLLSLWEDLTKQEARFIFKNTGGAVSMSCYLHAPIKQESQNIVKECNILNVNECLSVCLNDIEAIKPSSSGVLTKCIIRRNRDAAFIVEFVAFGPESESEYIALLKAIILKKKFLERQDLEKHRAARHIKKPLRLQLKSVGEMTSFRSINYMGNTKDAAVFPVTVPIFARRNNILCGFLVAALLIVCYVIFKEFALSADFSAV 258 P52590 Nuclear pore complex protein Nup107 Nup107 10116 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P52590 Pfam PF04121 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}. GO:0000777 GO:0031965 GO:0034399 GO:0005643 GO:0031080 GO:0017056 GO:0008585 GO:0006406 GO:0072006 GO:0051292 GO:0000973 GO:0006606 GO:0006355 MDRSGFGGMSSPVIRDPEVTRTARKHSAHKRVLIQANQDENFGTTTPRSQIIPRTPSSFRQPFTPPSRSLLRHPDISYIFGTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGFYTNTEHHSMTEDINLSTVMLREDDPGEAASMSMFSDFLQSFLKHSSTTVFDLVEEYENICASQVNILSKIVSRATRWDWQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENMFAIAGINASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGDFSDNIEFYAKSVYWENTLHSLKQRQLLSYIGSTRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLHHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTLDETEELPREYMEANWTLEKVFEELQATDKKRVLEENQEHYHVVQKFLILGDIDGLMDEFSKWLSKSRSSLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLINEKHTNLIAFYTCHLPQDLAVAQYALFLEGVTECEQRHQCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPSLDTATTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDSIAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNERFKHMNSAPQKPTLLSQATFTEKVAHEHKEKKYEMDHNIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEEDPERAHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS 926 P52593 Nucleoporin NUP188 NUP188 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P52593 UNIPROT D6W0I1 Pfam PF10487 Pfam PF18378 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. P30822 EBI-11763,EBI-20589 P34077 EBI-11763,EBI-12056 P40069 EBI-11763,EBI-9166 P22696 EBI-6679,EBI-11763 Q12329 EBI-11763,EBI-8571 Q06677 EBI-30084,EBI-11763 P46988 EBI-13224,EBI-11763 P11484 EBI-8627,EBI-11763 P40150 EBI-8632,EBI-11763 P10591 EBI-11763,EBI-8591 Q04477 EBI-27228,EBI-11763 Q02629 EBI-11763,EBI-11698 Q02630 EBI-11763,EBI-11703 Q08959 EBI-11763,EBI-38526 P38708 EBI-11763,EBI-24471 P16140 EBI-11763,EBI-20254 P07259 EBI-11763,EBI-14372 P02557 EBI-11763,EBI-18986 P09733 EBI-11763,EBI-18976 P02994 EBI-11763,EBI-6314 P00359 EBI-11763,EBI-7218 P10592 EBI-11763,EBI-8603 P32905 EBI-11763,EBI-16032 P05317 EBI-11763,EBI-15447 P49626 EBI-11763,EBI-15394 P41940 EBI-11763,EBI-11191 P23641 EBI-11763,EBI-11178 Q12134 EBI-11763,EBI-37262 P00549 EBI-11763,EBI-9890 P00330 EBI-11763,EBI-2218 P53201 EBI-23061,EBI-11763 P53877 EBI-29063,EBI-11763 P38305 EBI-20939,EBI-11763 Q12315 EBI-7635,EBI-11763 GO:0031965 GO:0005643 GO:0044611 GO:0017056 GO:0031990 GO:0006999 GO:0006606 GO:0006405 MATPSFGNSSPQLTFTHVANFMNDAAADVSAVDAKQLAQIRQFLKANKTNLIESLNTIRQNVTSSGDHNKLRSTIANLLQINVDNDPFFAQSEDLSHAVEFFMSERSSRLHIVYSLLVNPDIDLETYSFIDNDRFNVVGKLISIISSVIQNYDIITASSLAHDYNNDQDMFTIVSLVQLKKFSDLKFILQILQILNLMILNTKVPVDIVNQWFLQYQNQFVEFCRNINSTDKSIDTSSLQLYKFQNFQDLSYLSETLISRISSLFTITTILILGLNTSIAQFDIQSPLYMDTETFDTVNSALENDVATNIVNEDPIFHPMIHYSWSFILYYRRALQSSESFDDSDITKFALFAESHDVLQKLNTLSEILSFDPVYTTVITVFLEFSLNFIPITASTSRVFAKIISKAPEQFIENFLTNDTFEKKLSIIKAKLPLLNESLIPLINLALIDTEFANFELKDICSFAVTKSSLNDLDYDLIADTITNSSSSSDIIVPDLIELKSDLLVAPPLENENSNCLLSIPKSTKGKILTIKQQQQQQQQQNGQQPPTTSNLIIFLYKFNGWSLVGRILQNLLHSYMEKGTQLDDLQHELMISIIKLVTNVVDPKTSIEKSSEILSYLSNSLDTSASTINGASIIQVIFEIFEISLQRKDYTSIVQCCEFMTMLTPNYLHLVSSYLNKSDLLDKYGKTGLSNMILGSVELSTGDYTFTIQLLKLTKVFIRESLSLKNIHISKRSKIDIINKLILHAIHIFESYYNWKYNNFLQKFEIAFHLTLIFYDVLHDVFTINPHQKDQLIISSSANKLLQLFLTPMDSIDLAPNTLTNILISPLNTTTKILGDKILGNLYSKVMNNSFKLCTLLIAIRGSNRDLKPSNLEKLLFINSSKLVDVYTLPSYVHFKVQIIELLSYLVEAPWNDDYPFLLSFLGEAKSMAFLKEVLSDLSSPVQDWNLLRSLYIFFTTLLESKQDGLSILFLTGQFASNKKINDESSIDKKSSILTVLQKNSLLLDSTPEEVSCKLLETITYVLNTWTNSKIFIKDPKFVNSLLAKLKDSKKLFQKKENLTRDETVSLIKKYKLISRIVEIFALCIYNSTDSNSEILNFLNQEDLFELVHHFFQIDGFNKTFHDELNLKFKEKWPSLELQSFQKIPLSRINENENFGYDIPLLDIVLKADRSWNEPSKSQTNFKEEITDASLNLQYVNYEISTAKAWGALITTFVKRSTVPLNDGFVDLVEHFLKLNIDFGSDKQMFTQIYLERIELSFYILYSFKLSGKLLKEEKIIELMNKIFTIFKSGEIDFIKNIGKSLKNNFYRPLLRSVLVLLELVSSGDRFIELISDQLLEFFELVFSKGVYLILSEILCQINKCSTRGLSTDHTTQIVNLEDNTQDLLLLLSLFKKITNVNPSKNFNVILASSLNEVGTLKVILNLYSSAHLIRINDEPILGQITLTFISELCSIEPIAAKLINSGLYSVLLESPLSVAIQQGDIKPEFSPRLHNIWSNGLLSIVLLLLSQFGIKVLPETCLFVSYFGKQIKSTIYNWGDNKLAVSSSLIKETNQLVLLQKMLNLLNYQELFIQPKNSDDQQEAVELVIGLDSEHDKKRLSAALSKFLTHPKYLNSRIIPTTLEEQQQLEDESSRLEFVKGISRDIKALQDSLFKDV 1655 P52891 Nucleoporin NUP84 NUP84 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT P52891 UNIPROT D6VRN4 PDB 3IKO PDB 3JRO PDB 4XMM PDB 4XMN Pfam PF04121 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}. P35729 EBI-11713,EBI-12337 P36161 EBI-12337,EBI-11722 P46673 EBI-12337,EBI-12345 P48837 EBI-12324,EBI-12337 P49686 EBI-12310,EBI-12337 P49687 EBI-12337,EBI-11730 Q02630 EBI-11703,EBI-12337 Q02629 EBI-11698,EBI-12337 P22696 EBI-6679,EBI-12337 P33416 EBI-12337,EBI-8680 P11484 EBI-8627,EBI-12337 P10591 EBI-12337,EBI-8591 Q05166 EBI-12337,EBI-3035 Q8WUM0 EBI-295695,EBI-12337 P16140 EBI-12337,EBI-20254 P02994 EBI-12337,EBI-6314 P10592 EBI-12337,EBI-8603 P53011 EBI-12337,EBI-16940 Q04491 EBI-12337,EBI-16529 P34232 EBI-12337,EBI-11585 Q99257 EBI-12337,EBI-11642 P32582 EBI-4167,EBI-12337 P38305 EBI-20939,EBI-12337 Q12315 EBI-7635,EBI-12337 GO:0000781 GO:0031965 GO:0005643 GO:0031080 GO:0042802 GO:0017056 GO:0006974 GO:0030466 GO:0006302 GO:0035392 GO:0006406 GO:0031990 GO:0031081 GO:0045944 GO:0045893 GO:0000973 GO:0006606 GO:0006355 GO:0034398 MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDESNVISSKDWELEARFWHLVELLLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDFPLRENTNVLDVKDKEEDHIFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKHSLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIENYLLENNQVGTDELILPLPSHALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIINPGSVEEVDKSKLITTYISLLKLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTTQRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLNGRVKALEQFMERNNIGEICKNYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEWQKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTSSNFADSADYEILYEIRALYTPFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVARTATLSN 726 P52948 Nuclear pore complex protein Nup96 NUP98 9606 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P52948 UNIPROT Q8IUT2 UNIPROT Q8WYB0 UNIPROT Q96E54 UNIPROT Q9H3Q4 UNIPROT Q9NT02 UNIPROT Q9UF57 UNIPROT Q9UHX0 UNIPROT Q9Y6J4 UNIPROT Q9Y6J5 PDB 1KO6 PDB 2Q5X PDB 2Q5Y PDB 3MMY PDB 4OWR PDB 5A9Q PDB 6BZM Pfam PF04096 Pfam PF12110 PROSITE PS51434 OMIM 601021 DisGeNET 4928 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}.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}. A0A142I5B9 EBI-20625235,EBI-295727 P02545 EBI-351935,EBI-295727 Q5S007 EBI-5323863,EBI-295727 Q9UKE5 EBI-295727,EBI-1051794 Q9UPY3 EBI-395506,EBI-295727 Q16543 EBI-295634,EBI-295727 Q9BY41 EBI-6598095,EBI-295727 Q96DB2 EBI-301713,EBI-295727 P25054 EBI-295727,EBI-727707 Q93009 EBI-302474,EBI-295727 Q80U93 EBI-2551193,EBI-295727 P24386 EBI-2515129,EBI-295727 Q8BH74 EBI-2554056,EBI-295727 Q6ZQH8 EBI-2554037,EBI-295727 Q6PFD9 EBI-646104,EBI-295727 P01106 EBI-447544,EBI-295727 Q99P88 EBI-2551981,EBI-295727 Q9ERU9 EBI-643756,EBI-295727 Q9BPU9 EBI-6958971,EBI-295727 P45983 EBI-286483,EBI-295727 Q6ZYL4 EBI-6380438,EBI-295727 Q9H444 EBI-749627,EBI-295727 Q15388 EBI-711636,EBI-295727 P27824 EBI-355947,EBI-295727 Q14684 EBI-372051,EBI-295727 P21698 EBI-6148916,EBI-295727 Q8ZIC6 EBI-2860508,EBI-295727 Q9H0J4 EBI-1053637,EBI-295727 Q9H8S9 EBI-748229,EBI-295727 Q93079 EBI-352469,EBI-295727 Q16695 EBI-358900,EBI-295727 Q92623 EBI-295727,EBI-20865549 P0DTC6 EBI-25475897,EBI-295727 B2RTY4 EBI-355398,EBI-295727 Q8IW93-1 EBI-25410216,EBI-295727 P57740 EBI-295687,EBI-295727 Q8WUM0 EBI-295695,EBI-295727 Q8WYP5 EBI-396018,EBI-9032368 Q9BW27 EBI-716392,EBI-9032368 GO:0005829 GO:0043657 GO:0043231 GO:0016604 GO:0005635 GO:0042405 GO:0031965 GO:0034399 GO:0005643 GO:0044614 GO:0044615 GO:0031080 GO:0005654 GO:1990904 GO:0003729 GO:0008139 GO:1990841 GO:0003723 GO:0008236 GO:0017056 GO:0003713 GO:0005215 GO:0075733 GO:0006406 GO:0051292 GO:0006999 GO:0006913 GO:0048026 GO:0000973 GO:0006606 GO:0016925 GO:1900034 GO:0060964 GO:0006110 GO:0006405 GO:0034398 GO:0006409 GO:0016032 GO:0019083 MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFGAPQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLDTMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSKTRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEKLSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLALLLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTASISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWAKETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLSLHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL 1817 P53011 Nucleoporin SEH1 SEH1 559292 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT P53011 UNIPROT D6VU45 PDB 3EWE PDB 3F3F PDB 3F3G PDB 3F3P PDB 4XMM Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. P35729 EBI-11713,EBI-16940 P46673 EBI-12345,EBI-16940 P49687 EBI-11730,EBI-16940 P52891 EBI-12337,EBI-16940 Q02630 EBI-11703,EBI-16940 P47170 EBI-25710,EBI-16940 P39923 EBI-12212,EBI-16940 P38742 EBI-24336,EBI-16940 Q08281 EBI-2047093,EBI-16940 Q03897 EBI-32422,EBI-16940 P38164 EBI-21365,EBI-16940 P32472 EBI-2883297,EBI-16940 Q06677 EBI-30084,EBI-16940 P38788 EBI-24570,EBI-16940 P39078 EBI-16940,EBI-19054 P31539 EBI-16940,EBI-8050 Q03330 EBI-7458,EBI-16940 Q8WUM0 EBI-295695,EBI-16940 P18888 EBI-17550,EBI-16940 P09440 EBI-3903,EBI-16940 P41543 EBI-12651,EBI-16940 P41811 EBI-4898,EBI-16940 P32639 EBI-861,EBI-16940 P32357 EBI-340,EBI-16940 Q04491 EBI-16529,EBI-16940 P32582 EBI-4167,EBI-16940 P40018 EBI-432,EBI-16940 P53919 EBI-16940,EBI-28887 P38305 EBI-20939,EBI-16940 Q12315 EBI-7635,EBI-16940 GO:0097042 GO:0031965 GO:0005643 GO:0031080 GO:0035859 GO:0017056 GO:0034629 GO:0051028 GO:0006913 GO:1904263 GO:0015031 MQPFDSGHDDLVHDVVYDFYGRHVATCSSDQHIKVFKLDKDTSNWELSDSWRAHDSSIVAIDWASPEYGRIIASASYDKTVKLWEEDPDQEECSGRRWNKLCTLNDSKGSLYSVKFAPAHLGLKLACLGNDGILRLYDALEPSDLRSWTLTSEMKVLSIPPANHLQSDFCLSWCPSRFSPEKLAVSALEQAIIYQRGKDGKLHVAAKLPGHKSLIRSISWAPSIGRWYQLIATGCKDGRIRIFKITEKLSPLASEESLTNSNMFDNSADVDMDAQGRSDSNTEEKAELQSNLQVELLSEHDDHNGEVWSVSWNLTGTILSSAGDDGKVRLWKATYSNEFKCMSVITAQQ 349 P53062 Nucleus export protein BRR6 BRR6 559292 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}. UNIPROT P53062 UNIPROT D6VV88 Pfam PF10104 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}. P25611 EBI-2347150,EBI-22052 P11484 EBI-2347150,EBI-8627 GO:0071944 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNLKLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRSFLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA 197 P53067 Importin subunit beta-5 KAP114 559292 Yes SL-0178 SL-0185 Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:14562095}. UNIPROT P53067 UNIPROT D6VV94 PDB 6AHO Pfam PF03810 PROSITE PS50166 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}. P04912 EBI-8076,EBI-9174 Q12692 EBI-8080,EBI-9174 P38910 EBI-4553,EBI-9174 P32589 EBI-8648,EBI-9174 P11484 EBI-8627,EBI-9174 P10592 EBI-9174,EBI-8603 P46988 EBI-9174,EBI-13224 P33416 EBI-9174,EBI-8680 P13393 EBI-19129,EBI-9174 P25635 EBI-14332,EBI-9174 P02293 EBI-8088,EBI-9174 P25293 EBI-11850,EBI-9174 P16140 EBI-9174,EBI-20254 P07259 EBI-9174,EBI-14372 P02994 EBI-9174,EBI-6314 P41940 EBI-9174,EBI-11191 P02557 EBI-9174,EBI-18986 P09733 EBI-9174,EBI-18976 P12709 EBI-7238,EBI-9174 Q02486 EBI-2028,EBI-9174 P49956 EBI-4560,EBI-9174 P02294 EBI-8094,EBI-9174 Q02159 EBI-9174,EBI-19749 GO:0005737 GO:0005829 GO:0005635 GO:0005643 GO:0005634 GO:0061608 GO:0008536 GO:0051028 GO:0006606 MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLSLRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISAVDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEIVFKVLNTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGNVDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTESEPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFVSKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYLLQCILLNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPLTSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQVSSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQECLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLKKKPNDGFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLERLLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVLCFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLNDKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQSKQPNPEQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMDVKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL 1004 P53148 Spindle pole body component SPC105 SPC105 559292 Yes SL-0178 SL-0182 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. UNIPROT P53148 UNIPROT D6VU52 PDB 4BL0 Pfam PF08317 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}. Q04431 EBI-32446,EBI-23870 P40568 EBI-25398,EBI-23870 Q12143 EBI-33666,EBI-23870 P39731 EBI-11606,EBI-23870 P40460 EBI-23870,EBI-25247 P33895 EBI-23870,EBI-12377 P36016 EBI-23870,EBI-10154 P11484 EBI-23870,EBI-8627 P40150 EBI-23870,EBI-8632 Q06677 EBI-30084,EBI-23870 P32589 EBI-23870,EBI-8648 Q04477 EBI-27228,EBI-23870 P14693 EBI-23870,EBI-24602 GO:0005623 GO:0000941 GO:0000778 GO:0005739 GO:0031617 GO:0031965 GO:0005816 GO:0008017 GO:1990758 GO:0007094 GO:0034501 GO:0031134 MNVDERSRIGGREKDAGPGKGILKQNQSSQMTSSFLENPGVRIPTRIITKKEVLDGSNTTSRINTSNLQSMVKRRVSFAPDVTLHSFTFVPEQNNEIKEPRRRKTSTNSPTKISSQEEPLVTSTQIDDARTEEKTAAEEDPDTSGMELTEPIVATPDSNKASQHDPTSMEMTEVFPRSIRQKNPDVEGESIESSQQIDDVEAVREETMELTAIHNVHDYDSISKDTVEGEPIDLTEYESKPYVPNSVSRSTGKSSDYSVERSNDKSDLSKSENKTNSSQPMEITDIFHADPQNPMSLHSDNNINNDGNEMELTQIQTNFDRDNHHIDESPSEKHAFSSNKRRKLDTVSDYAASVTTPVKEAKDTSGEDNDGDLEMMEKMSPITFSDVDNKIGTRSNDVFTIEPGTEDTGMQTATDDEEDGENVDDNGNKIVEKTRLPEIDKEGQSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKVNFPLNSFNFVENQRIDNVFSAFYIDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLMRDQLQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIRKLNEAIKEEIRSLKNLPSDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKLAIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKLRDTLKILESLTGVRFLKFSKATLSIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDSMLSNLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFAQGVFSENGQIPMKVHISTQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT 917 P53541 Putative meiotic phospholipase SPO1 SPO1 559292 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. UNIPROT P53541 UNIPROT D6W1G5 Pfam PF01735 PROSITE PS51210 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}. P11484 EBI-17851,EBI-8627 P32589 EBI-8648,EBI-17851 P10592 EBI-17851,EBI-8603 GO:0071944 GO:0005737 GO:0005783 GO:0005789 GO:0005576 GO:0000324 GO:0016021 GO:0043231 GO:0031965 GO:0005634 GO:0005886 GO:0005628 GO:0004623 GO:0004620 GO:0032120 GO:0046475 GO:0030474 GO:0070583 MQKLLFVFSVLLTVVLATAPFQVQCPSSPLIREAKHELCPEETLYLKKKKIKTKNKLIQFLKSLTEAKFSSKFYKRVLKDPPKIGIAISGGGYRSMLVGTGFISQMNDYGLFEYSDYIAGLSGGSWILMDLVVQNFEVKSLLQEWDLEEDLLLGIPEFDISEEEIVTNAKKEYNDNDLKMKKRQGGSLITSSSNFYEQIEEIMNSIEEIPEDYMITKRNLNPLARLKKIFFPNNTFTGTDAKIETFKKVLDFYKSLHLKIKPKKMEGFQISFTDYWGKAIVQRLKKNFDDDPNHSFSFSKLVNSSKKFKECSVPIPIFVANCKNGLLSNVIFEFTPFEFGSWENILRLFVKLPYLGSKIVSGKAEKCINNFDDLGFITATSSSIFNNVLIFIWNLASQSSREAMKALNMVMGIFGLGKEEIFSISKDSSRLETDYAVYQPNPFYLYPEKDNVLTNKNHLYLVDGGEDGENIPLRTLVIPERELDVIFVLDSSSDIDNYPNGSKLKRIFEKLDEENVHYQFPNNVKTFTHPIVIGCNATKRTGHDSFLPIIIYHANANHGNASNTSTFKITYNQSEVSSMLPTGRGVFSNDYDLYYKNCLGCILTKRTMDRLPRKKKFSPFCLQCFKDYCYS 631 P53694 Reticulon-like protein 1 rtn1 284812 Yes SL-0178 SL-0182 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. UNIPROT P53694 Pfam PF02453 PROSITE PS50845 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}. GO:0005623 GO:0032153 GO:0032541 GO:0005789 GO:0016021 GO:0031965 GO:0007049 GO:0051301 GO:1990809 GO:0071790 MSEQHSLNPFESGSVTASDVAAAKSGAEDLVNTLTAHTVHPSTELPSATSFPSALPNSENPVIQNISSSSSEPHHTSQSTPGETSSPVCPVSGAHGGADKKCPALEAGCPFTNTTKQNVDPEISNALWSVLTWKNTSCSFSTLMSILALVYVPSWINLPRLFFRTFRYVFLITSIIEFGGLFASNGKRGVLSHFRSSYITCDSKALDRIVNSIVDIFNVMLIQFQRILFAESPILTFTASVAAFIEFFLSGFLSYKSLFVWNVLFAFILPRLYVCNERSIKHLVASLERSGDKLKKQATETINTTVNK 308 P53816 Phospholipase A and acyltransferase 3 PLAAT3 9606 Yes SL-0198 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}. UNIPROT P53816 UNIPROT B2R7Q4 UNIPROT B7XAK5 UNIPROT Q3SYI3 UNIPROT Q9HDD1 PDB 2KYT PDB 4DOT PDB 4FA0 PDB 4Q95 Pfam PF04970 OMIM 613867 DisGeNET 11145 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}. Q9NRR5 EBI-711226,EBI-746318 Q9UMX0-2 EBI-10173939,EBI-746318 Q9UMX0 EBI-746318,EBI-741480 P30153 EBI-746318,EBI-302388 Q9UHD9 EBI-947187,EBI-746318 GO:0005829 GO:0005783 GO:0016021 GO:0048471 GO:0005778 GO:0005777 GO:0005886 GO:0052740 GO:0016410 GO:0052739 GO:0008970 GO:0004623 GO:0102567 GO:0102568 GO:0046485 GO:0016042 GO:0070292 GO:0045786 GO:0007031 GO:0036151 GO:0036152 GO:0036149 GO:0036150 GO:0008654 GO:0006644 GO:1904177 GO:0009617 GO:0006641 GO:0016032 MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ 162 P53895 Protein ASI2 ASI2 559292 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:17085444}. UNIPROT P53895 UNIPROT D6W124 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}. P25294 EBI-17244,EBI-28975 P10592 EBI-28975,EBI-8603 P10614 EBI-28975,EBI-5127 P53983 EBI-28603,EBI-28975 P54074 EBI-27241,EBI-28975 P38074 EBI-28975,EBI-8394 GO:0097658 GO:0005783 GO:0016021 GO:0005637 GO:0071230 GO:0036369 GO:0006511 MARPQNHRRSNWTERDDNDDYLFQRFLEESETRHSREPSPVTEQSQQELQQDVQQAIDGIFNSLRRNMSSTSNINRAANMDATTNGNGGINADTIRATNANTADSPFTARQQSPLRTFLRNLFILDYFIGLILFPFSVYNILRSGFNSMTFSENDFIIEIVGYWKFAKIFGSGGTTLIAYKDTGKLGLLGKFHNIIVFYSSPVIKHIMKSRDGNEPNLNWIRLMFAKAFELFVKVSTILIYLAYGVSGTVYMVTAGFFFVLCLLFTVIRRYKGVHRMLVSQRITGPGVF 289 P53903 Processing of GAS1 and ALP protein 2 PGA2 559292 Yes SL-0178 SL-0182 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}. UNIPROT P53903 UNIPROT D6W133 Pfam PF07543 Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins. {ECO:0000269|PubMed:16943325}. Q12154 EBI-2344998,EBI-2989 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0015031 MSEVAETWVDTWMAKLVNYDYKHFIRLVIIVGGYLLLRNIASRELAKKQLAAQVEKDKRDKEEKRSKDLIDKPDDAATAETTSFGWGKKTRRRVKRQQELFENALEEAKRRNQGLDPDSDADIEELLEE 129 P53983 Protein ASI3 ASI3 559292 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}. UNIPROT P53983 UNIPROT D6W1G9 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}. P25491 EBI-10420,EBI-28603 P53895 EBI-28603,EBI-28975 P11484 EBI-28603,EBI-8627 P39077 EBI-28603,EBI-19063 P10591 EBI-28603,EBI-8591 P25294 EBI-28603,EBI-17244 P54074 EBI-28603,EBI-27241 P10614 EBI-5127,EBI-28603 P49626 EBI-28603,EBI-15394 Q02159 EBI-28603,EBI-19749 GO:0097658 GO:0016021 GO:0005637 GO:0034399 GO:0046872 GO:0004842 GO:0071230 GO:0036369 GO:0006511 MSTNILQHVKQLLHNRDVFSFFHNKTGNLNYLDNTTQKPEVFVSPNSTIVSAPTLDSFQALMEKGNFTTLQLAKVGIRMFFSYSVSKYAVLCFSTAIILNRLTVMSSLRSNSTNIRLPLWSKTLLHLVATLSLVKALLQILSQFGLMHELHVSDTDFYALSVYLFVALSDCIEIFISSTTNVPSLICSDFSIWGLSLNLYIISKMPAGQQHIGDNVELLGAVFHRLVIHLVELFHIRAYRLCGEVILNAGFFTAFVTRTYLNGLDFINICLIHNYFPGFFYISTILLASIGIFLKALFTSNPFRSLYSRYKNLEKWWRSNNYNGEEEFNEIALSLCLLLTSNDYKIFKKSDNVKSVDEVAAFSNSYVVSGHLNQLQSTPEDLLSRKEMTTDSQLPGFARTYLGLFELVRTIILTYSRLLKNLLWSKNFESSIDKKPRVGKRKKRDLNKYVTEKNYKKFLYKPDVKELNIESDLRSLELLLPEDDSSKDYFPPRKIDESVSDEEFDSDMESQLIIDEEKELTHLSSNAVDSDDLEEIAWNISMWSILNYEMDVHNKVNGPLTRSQYGKRNPQGVLVDVVIERLLHHTNSRYMYKRLNMKDDDKLEFKFDFAFDSCDEVEEMDLSCLICKVNKRNIVTWPCRCLALCDDCRISLGYKGFATCVSCDSEVKGYSKLNIV 676 P54074 Protein ASI1 ASI1 559292 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT P54074 UNIPROT D6VZU2 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}. P53895 EBI-27241,EBI-28975 P53983 EBI-28603,EBI-27241 P02829 EBI-27241,EBI-8659 P10614 EBI-27241,EBI-5127 Q969F0 EBI-743099,EBI-27241 GO:0097658 GO:0016021 GO:0005637 GO:0034399 GO:0046872 GO:0004842 GO:0071230 GO:0036369 GO:0006511 MNSSTSSENVFINSFSYLNQTSQAVISGNSTFANVINFPYRLGLSFIGAVNLQYEQTVKSEEIPPTLRSVFDTIGFFFSPYAIFCFVIAIVLNRFVVFYAVLNNGSRRTLPLWLSNVFHVSAVVVLAMVSLGPLTLGKDFKILGDPAFAQEKFLLNIFYAFAYSYCVETIFTIMRNSSPLEGTDYSLFELSIQFYTMTNNNTKFLDSPDYIIDCSMAILSRILIHLVEIFRLRNYRLLFSTIMNLCHICYLGIRVKQGGWKSLPFSVKFRHFPKLFSVSIICLSLLIFKLSCLIRWDPFGKSRNSCELLQFYPLSRNWKKYLNYTGEEDFSAMATKFALLLCSGTELMEKGIRREFPAINIPDNVNEKFFISGYLNELSKPYKENTSISFPKKNSSILKQRFFLMFPKSIIWIMKKLVGQVFFGFRDNKDEDIPDNDPSKMLKITKTNSLNNSAGHKEDIELELLNTSDDEYSEDYEPSEVESLGDSDEENLEEDSLIFNETRDALLDLFSSEDNEVHTDYNWIMSTSRILQQKLLSDKTLTRASILDTKLSEVDETFGTESDFDLSCAVCKVNERNTVLWPCRCFAICEDCRISLGLRGFSTCVCCRSKVHGYCKVHPVSDSK 624 P54217 Spermatocyte protein spe-11 spe 6239 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:8565851}. Note=Localized to the perinuclear region of sperm. UNIPROT P54217 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}. GO:0005634 GO:0048471 GO:0030703 GO:0007275 GO:0060468 GO:0007283 MSDEEIDISTALNNKTTPKKKSLKRNSNSQEGYESPEEREIVYPSVFGAIGTPMAKSDNAKEWDEWKEKERKKDKAEWKRYLRSKWDMTQGHLPLVSDSEFLKGRKEHKEYNSKARMDILDGLDEVNEGFFNCGKGAAMNIRYNDKNVSKKGAKKFVATVETAMKKAGNPTMEQMMTDDLDEDEARAEAEWERQREQRKLASRAYDAAMDEREDDAKYVPWDEYCQEMEELGKELKIGEKHYKKWLEKKMDENKVTHKFNAYQLDLKCLDEDAFSNKKSLKSVVRNVQKFYRKMREPKK 299 P54259 Atrophin-1 ATN1 9606 Yes SL-0198 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}. UNIPROT P54259 UNIPROT Q99495 UNIPROT Q99621 UNIPROT Q9UEK7 Pfam PF03154 OMIM 125370 OMIM 607462 OMIM 618494 DisGeNET 1822 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}.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. O15162 EBI-740019,EBI-945980 Self EBI-945980,EBI-945980 Q9P2R6 EBI-945980,EBI-948076 Q9HAU0 EBI-945934,EBI-945980 Q15654 EBI-742327,EBI-945980 Q9NWB1 EBI-945980,EBI-945906 Q9UQB8 EBI-945980,EBI-525456 Q06455 EBI-945980,EBI-743342 Q01844 EBI-945980,EBI-739737 Q96CN9 EBI-945980,EBI-746252 Q96PV6 EBI-739546,EBI-945980 Q99750 EBI-945980,EBI-724076 Q9BSW2 EBI-945980,EBI-739773 O43639 EBI-945980,EBI-713635 P61964 EBI-945980,EBI-540834 O00308 EBI-945980,EBI-743923 Q9BQ66 EBI-739863,EBI-945980 P61289 EBI-355546,EBI-945980 Q93062 EBI-740322,EBI-945980 O00468 EBI-947482,EBI-945980 P46379 EBI-347552,EBI-945980 Q02641 EBI-947514,EBI-945980 O43439 EBI-748628,EBI-945980 Q9HC77 EBI-946194,EBI-945980 Q9H2X0 EBI-947551,EBI-945980 P52943 EBI-947590,EBI-945980 O14641 EBI-740850,EBI-945980 Q12805 EBI-536772,EBI-945980 O95967 EBI-743414,EBI-945980 O75095 EBI-947597,EBI-945980 Q7Z7M0 EBI-947617,EBI-945980 P23142 EBI-726652,EBI-945980 Q5ZEY4 EBI-947655,EBI-945980 P28799 EBI-747754,EBI-945980 P98160 EBI-947664,EBI-945980 Q9Y219 EBI-946223,EBI-945980 O60290 EBI-310635,EBI-945980 Q14766 EBI-947693,EBI-945980 Q8N2S1 EBI-947718,EBI-945980 P02686 EBI-947410,EBI-945980 A6BM72 EBI-947743,EBI-945980 Q92832 EBI-947754,EBI-945980 Q99435 EBI-946274,EBI-945980 O75420 EBI-945980,EBI-947774 P17858 EBI-487243,EBI-945980 Q96PM5 EBI-947779,EBI-945980 O75093 EBI-947791,EBI-945980 Q6ZWJ1 EBI-947833,EBI-945980 Q86TM6 EBI-947849,EBI-945980 Q99973 EBI-947859,EBI-945980 Q9ULU4 EBI-765834,EBI-945980 P98175 EBI-721525,EBI-945980 Q9NP73 EBI-947892,EBI-945980 Q9UBX5 EBI-947897,EBI-945980 P98164 EBI-947916,EBI-945980 Q92824 EBI-945980,EBI-751290 P25788 EBI-348380,EBI-945980 Q9H0M0 EBI-742157,EBI-945980 Q08117 EBI-717810,EBI-945980 P61204 EBI-641535,EBI-945980 P48634 EBI-347545,EBI-945980 Q9H9J5 EBI-947238,EBI-945980 Q09013 EBI-692774,EBI-945980 Q16610 EBI-945980,EBI-947964 P98095 EBI-947973,EBI-945980 Q3KQU3 EBI-713229,EBI-945980 Q5JSZ5 EBI-744891,EBI-945980 A7E2V4 EBI-947995,EBI-945980 Q15323 EBI-948001,EBI-945980 Q92794 EBI-948013,EBI-945980 Q8WYB5 EBI-948029,EBI-945980 O43251 EBI-746056,EBI-945980 Q96EP0 EBI-948111,EBI-945980 Q8IUQ4 EBI-747107,EBI-945980 O43255 EBI-948141,EBI-945980 Q96R06 EBI-413317,EBI-945980 Q9Y4B4 EBI-948156,EBI-945980 Q70EL1 EBI-946185,EBI-945980 A0A384KST0 EBI-2845592,EBI-945980 A0A2S9PJQ7 EBI-2846239,EBI-945980 A0A384LHY7 EBI-2850412,EBI-945980 Q8ZA76 EBI-945980,EBI-2846943 A0A1Q4M0N4 EBI-945980,EBI-2817814 A0A0F7R9Q0 EBI-945980,EBI-2815990 A0A384LQ43 EBI-2848562,EBI-945980 O75081 EBI-1190217,EBI-945980 Q14457 EBI-949378,EBI-945980 GO:0030054 GO:0005737 GO:0016363 GO:0005654 GO:0005634 GO:0048471 GO:0003677 GO:0019904 GO:0001085 GO:0003714 GO:0007417 GO:0000122 GO:0051402 MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL 1190 P54265 Myotonin-protein kinase Dmpk 10090 Yes SL-0178 SL-0182 SL-0183 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. UNIPROT P54265 Pfam PF08826 Pfam PF00069 PROSITE PS51285 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005623 GO:0005829 GO:0005789 GO:0031307 GO:0016020 GO:0031965 GO:0005640 GO:0005886 GO:0033017 GO:0005524 GO:0046872 GO:0017020 GO:0004674 GO:0006874 GO:0035556 GO:0010657 GO:0006998 GO:0018105 GO:0006468 GO:0014853 GO:0008016 GO:0010830 GO:0014722 GO:0002028 GO:0051823 MSAEVRLRQLQQLVLDPGFLGLEPLLDLLLGVHQELGASHLAQDKYVADFLQWVEPIAARLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVKGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLQPDGMVRSLVAVGTPDYLSPEILQAVGGGPGAGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYAKIVHYREHLSLPLADTVVPEEAQDLIRGLLCPAEIRLGRGGAGDFQKHPFFFGLDWEGLRDSVPPFTPDFEGATDTCNFDVVEDRLTAMVSGGGETLSDMQEDMPLGVRLPFVGYSYCCMAFRDNQVPDPTPMELEALQLPVSDLQGLDLQPPVSPPDQVAEEADLVAVPAPVAEAETTVTLQQLQEALEEEVLTRQSLSRELEAIRTANQNFSSQLQEAEVRNRDLEAHVRQLQERMEMLQAPGAAAITGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARIPRPGLSEARCLLLFAAALAAAATLGCTGLVAYTGGLTPVWCFPGATFAP 631 P54811 Transitional endoplasmic reticulum ATPase homolog 1 cdc 6239 Yes SL-0198 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}. UNIPROT P54811 Pfam PF00004 Pfam PF17862 Pfam PF02933 Pfam PF02359 Pfam PF09336 PROSITE PS00674 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}. Self EBI-320245,EBI-320245 Q17425 EBI-2411422,EBI-320245 Q94230 EBI-320245,EBI-895916 O17850 EBI-320245,EBI-320650 P54812 EBI-320265,EBI-320245 Q9TXH9 EBI-320245,EBI-320236 Q22557 EBI-2412448,EBI-320245 Q22560 EBI-2002088,EBI-320245 G5EC44 EBI-320245,EBI-323732 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0034098 GO:0005524 GO:0016887 GO:0042802 GO:0031593 GO:0044877 GO:0097352 GO:0008340 GO:0009792 GO:0071712 GO:0016236 GO:0051228 GO:0045977 GO:0032436 GO:1905634 GO:0030970 GO:0030433 MASVPTHQSEKEKKNDELSTAILKDKVKPNRLIVDQSEQDDNSVIAVSQAKMDELGLFRGDAVILKGKKRKESVAIIVSDESCPNEKVRMNRVVRNNLRIRLGDVVSITPAPNLSYGTRIHVLPIDDTIEGLTGNLFDVFLKPYFLEAYRPLHKGDIFTVQAAMRTVEFKVVETEPAPACIVSPDTMIHYEGDPIKREEEEESMNDIGYDDLGGVRKQLAQIKEMVELPLRHPQLFKAIGIKPPRGILLFGPPGTGKTLIARAVANETGSFFFLINGPEVMSKMSGESESNLRKAFEECEKNQPAILFIDEIDAIAPKREKTNGEVERRIVSQLLTLMDGVKGRSNLVVIAATNRPNSIDGALRRFGRFDREIDIGIPDAVGRLEILRIHTKNMKLADDVDLEQIANECHGFVGADLASLCSEAALQQIREKMELIDLEDDQIDAEVLNSLAVTMENFRFAQGKSSPSALREAVVETPNTTWSDIGGLQNVKRELQELVQYPVEHPEKYLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRDVFDKARAAAPCVLFFDELDSIAKARGGGAGGDGGGASDRVINQVLTEMDGMNAKKNVFIIGATNRPDIIDPAVLRPGRLDQLIYIPLPDEASRHQILKASLRKTPLSKDLDLTFLAKNTVGFSGADLTEICQRACKLAIRESIEKEIRIEKERQDRQARGEELMEDDAVDPVPEITRAHFEEAMKFARRSVTDNDIRKYEMFAQTLQQSRGFGNNFKFPGEQRGSDAPSAPVPAQDDDDLYN 809 P55735 Protein SEC13 homolog SEC13 9606 Yes SL-0178 SL-0185 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}. UNIPROT P55735 UNIPROT A8MV37 UNIPROT B4DXJ1 UNIPROT Q5BJF0 UNIPROT Q9BRM6 UNIPROT Q9BUG7 PDB 3BG0 PDB 3BG1 PDB 5A9Q Pfam PF00400 PROSITE PS50082 PROSITE PS50294 OMIM 600152 DisGeNET 6396 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}. O14976 EBI-714707,EBI-1046596 O15027 EBI-357515,EBI-1046596 O15504 EBI-2515057,EBI-1046596 P00533 EBI-297353,EBI-1046596 P02545 EBI-351935,EBI-1046596 P35729 EBI-11713,EBI-1046596 P37198 EBI-347978,EBI-1046596 P49687 EBI-1046596,EBI-11730 Self EBI-1046596,EBI-1046596 O94979 EBI-1046596,EBI-1767898 Q15436 EBI-81088,EBI-1046596 Q5T011 EBI-10749411,EBI-1046596 Q9NXC5 EBI-2515122,EBI-1046596 Q96S15 EBI-746424,EBI-1046596 Q6PJI9 EBI-2515073,EBI-1046596 P03372 EBI-78473,EBI-1046596 Q12824 EBI-358419,EBI-1046596 Q9Y2H1 EBI-991501,EBI-1046596 Q9UPY3 EBI-395506,EBI-1046596 O00463 EBI-1046596,EBI-523498 Q96JE7-2 EBI-10215083,EBI-1046596 P04792 EBI-1046596,EBI-352682 Q8WYP5 EBI-396018,EBI-1046596 Q9BW27 EBI-716392,EBI-1046596 P43351 EBI-706448,EBI-1046596 Q8BH74 EBI-2554056,EBI-1046596 Q6PFD9 EBI-646104,EBI-1046596 P56749 EBI-1046596,EBI-723005 Q9ERU9 EBI-643756,EBI-1046596 P57740 EBI-295687,EBI-1046596 Q9BPU9 EBI-6958971,EBI-1046596 P63280 EBI-80180,EBI-1046596 P21333 EBI-350432,EBI-1046596 Q91X51 EBI-2553222,EBI-1046596 P56377 EBI-1054374,EBI-1046596 Q9Z1Z0 EBI-7597484,EBI-1046596 Q96EE3 EBI-922818,EBI-1046596 P58043 EBI-9638431,EBI-1046596 Q92731 EBI-78505,EBI-1046596 G3X972 EBI-11079353,EBI-1046596 P09497 EBI-726598,EBI-1046596 Q9NYZ3 EBI-2511327,EBI-1046596 Q13492 EBI-2803688,EBI-1046596 Q00610 EBI-354967,EBI-1046596 Q9CWZ3 EBI-1993805,EBI-1046596 O43493 EBI-1752146,EBI-1046596 O15155 EBI-749204,EBI-1046596 P49336 EBI-394377,EBI-1046596 Q15075 EBI-298113,EBI-1046596 Q8NFH3 EBI-1059321,EBI-1046596 O94979-2 EBI-17482477,EBI-1046596 Q92734 EBI-357061,EBI-1046596 Q13618 EBI-456129,EBI-1046596 P48729 EBI-1383726,EBI-1046596 P49674 EBI-749343,EBI-1046596 A0A0F7RLQ7 EBI-2814703,EBI-1046596 A0A0H2W3Z6 EBI-2841276,EBI-1046596 P01889 EBI-1046596,EBI-1046513 P56537 EBI-1046596,EBI-372243 P78396 EBI-1046596,EBI-375065 P23508 EBI-1046596,EBI-307531 P62330 EBI-638181,EBI-1046596 Q96JE7 EBI-749897,EBI-1046596 Q8IZD9 EBI-1752361,EBI-1046596 Q8NFH4 EBI-2563158,EBI-1046596 Q96HA1 EBI-739990,EBI-1046596 Q6P5F9 EBI-2550236,EBI-1046596 Q6IQ23 EBI-2125301,EBI-1046596 Q9BW85 EBI-1046596,EBI-10300345 Q96EA4 EBI-1046596,EBI-715381 Q96CP2 EBI-1046596,EBI-9394506 Q96BP3 EBI-1046596,EBI-2827139 Q8WUM0 EBI-1046596,EBI-295695 Q8NAV1 EBI-1046596,EBI-715374 Q12769 EBI-1046596,EBI-295715 Q03154 EBI-1046596,EBI-742064 P58004 EBI-1046596,EBI-3939642 P52948-5 EBI-1046596,EBI-5280407 P11274 EBI-1046596,EBI-712838 O15400-2 EBI-1046596,EBI-11042829 O15062 EBI-1046596,EBI-722671 O15027-2 EBI-1046596,EBI-11079342 Q9NYJ8 EBI-1046596,EBI-358708 GO:0030127 GO:0005829 GO:0005789 GO:0012507 GO:0070062 GO:0061700 GO:0000139 GO:0043657 GO:0043231 GO:0005765 GO:0005635 GO:0031080 GO:0005654 GO:0042802 GO:0005198 GO:0019886 GO:0002474 GO:0048208 GO:0090114 GO:0090110 GO:0006886 GO:0075733 GO:0006406 GO:0032008 GO:1904263 GO:0032527 GO:1900034 GO:0060964 GO:0006110 GO:0006409 GO:0016032 GO:0019083 MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQNEQ 322 P55820 Synaptosomal-associated protein 25 SNAP25 9986 Yes SL-0198 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}. UNIPROT P55820 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}. GO:0030054 GO:0005737 GO:0016020 GO:0043005 GO:0048471 GO:0001917 GO:0005886 GO:0031201 GO:0045202 GO:0017075 GO:0005249 MLQLVEESSKDAGIRXLVMLDEQGEQLERVVDEREQMAISGGFIRIMEKMLGSG 54 P57088 Transmembrane protein 33 TMEM33 9606 Yes SL-0178 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}. UNIPROT P57088 UNIPROT B3KSS8 UNIPROT Q9H953 Pfam PF03661 OMIM 618515 DisGeNET 55161 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}. A0A142I5B9 EBI-20625235,EBI-1048629 P04626 EBI-641062,EBI-1048629 P13569 EBI-349854,EBI-1048629 E9PS44 EBI-21260290,EBI-1048629 O94966 EBI-2511895,EBI-1048629 P62263 EBI-1048629,EBI-352783 Q6NUS6 EBI-11278332,EBI-1048629 Q9CR14 EBI-7529579,EBI-1048629 Q99549 EBI-2653928,EBI-1048629 O55143 EBI-770763,EBI-1048629 O15155 EBI-749204,EBI-1048629 Q14684 EBI-372051,EBI-1048629 Q77M19 EBI-6149376,EBI-1048629 Q8ZC32 EBI-2852171,EBI-1048629 Q5NIP6 EBI-2796567,EBI-1048629 P48039 EBI-1188238,EBI-1048629 Q9BUV8 EBI-1048629,EBI-1050079 Q14164 EBI-1048629,EBI-307369 P11171 EBI-1048629,EBI-1050906 P62140 EBI-1048629,EBI-352350 Q9Y5J5 EBI-1048629,EBI-1055859 Q99608 EBI-1048629,EBI-718177 Q9P1U1 EBI-1047175,EBI-1048629 Q9UET6 EBI-1048629,EBI-1055987 P01106 EBI-1048629,EBI-447544 Q15714 EBI-1048629,EBI-712609 Q9HAW0 EBI-1048629,EBI-1055224 O75365 EBI-1048629,EBI-1043866 Q15008 EBI-1048629,EBI-359701 Q71U36 EBI-302552,EBI-1048629 P30086 EBI-716384,EBI-1048629 P04049 EBI-365996,EBI-1048629 Q13547 EBI-301834,EBI-1048629 P51636 EBI-603607,EBI-1048629 P61586 EBI-446668,EBI-1048629 P15056 EBI-365980,EBI-1048629 P15498 EBI-625518,EBI-1048629 Q13164 EBI-1213983,EBI-1048629 P19419 EBI-726632,EBI-1048629 Q13153 EBI-1307,EBI-1048629 P49023 EBI-702209,EBI-1048629 Q99558 EBI-358011,EBI-1048629 Q6KAU7-1 EBI-25408849,EBI-1048629 P0DTD1 EBI-25475871,EBI-1048629 P0DTC3 EBI-25475894,EBI-1048629 P0DTD8 EBI-25475914,EBI-1048629 P0DTD3 EBI-25475917,EBI-1048629 Q96FB2 EBI-1048629,EBI-2857623 Q8IVT5 EBI-486984,EBI-1048629 GO:0005783 GO:0005789 GO:0030176 GO:0042470 GO:0005635 GO:0071786 GO:0061024 GO:1903896 GO:1903899 GO:1903371 GO:0034976 MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLSRAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDARGSNSLPLLRSVLDKLSANQQNILKFIACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRTLFNELRIVVEHIIMKPACPLFVRRLCLQSIAFISRLAPTVP 247 P58195 Phospholipid scramblase 1 Plscr1 10116 Yes SL-0198 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}. UNIPROT P58195 Pfam PF03803 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}. GO:0062023 GO:0005737 GO:0005829 GO:0005794 GO:0005887 GO:0016020 GO:0045121 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0005509 GO:0042609 GO:0003677 GO:0001228 GO:0019899 GO:0005154 GO:0017128 GO:0017124 GO:0006953 GO:0006915 GO:0071345 GO:0071222 GO:0051607 GO:0006955 GO:0097193 GO:0030099 GO:0032091 GO:0045071 GO:0006659 GO:0070782 GO:0015914 GO:0017121 GO:0043065 GO:2000373 GO:0010628 GO:0045089 GO:1902231 GO:0045944 GO:0060368 GO:0033003 GO:0035455 GO:0035456 MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDPSGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEKRQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNEEQRSGVW 335 P58546 Myotrophin MTPN 9606 Yes SL-0198 Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P58546 PDB 3AAA Pfam PF12796 PROSITE PS50297 PROSITE PS50088 OMIM 606484 DisGeNET 136319 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}. Q9H8T0 EBI-711399,EBI-1051736 P00441 EBI-990792,EBI-1051736 P13569 EBI-349854,EBI-1051736 P60520 EBI-720116,EBI-1051736 P28482 EBI-1051736,EBI-959949 Q9UPV0 EBI-3937015,EBI-1051736 Q14203 EBI-724352,EBI-1051736 O15078 EBI-1811944,EBI-1051736 Q5SW79 EBI-1104799,EBI-1051736 Q66GS9 EBI-1046993,EBI-1051736 Q96FW1 EBI-1058491,EBI-1051736 Q6XUX3 EBI-1051736,EBI-1049520 Q14164 EBI-1051736,EBI-307369 Q9Y4K3 EBI-1051736,EBI-359276 P01889 EBI-1051736,EBI-1046513 P11171 EBI-1051736,EBI-1050906 Q9Y478 EBI-1051736,EBI-719769 Q9UBN6 EBI-1051736,EBI-1044859 Q9UET6 EBI-1051736,EBI-1055987 P40337 EBI-1051736,EBI-301246 Q9NRY4 EBI-766200,EBI-1051736 Q3KRB8 EBI-25411786,EBI-1051736 Q8N0Z3 EBI-2361917,EBI-1051736 Q8N137 EBI-947360,EBI-1051736 Q96Q45 EBI-2602465,EBI-1051736 Q6UVJ0 EBI-1570153,EBI-1051736 Q7Z7A1 EBI-2563266,EBI-1051736 Q8IVT5 EBI-486984,EBI-1051736 GO:0030424 GO:0005829 GO:0008290 GO:0005634 GO:0048471 GO:0043565 GO:0006584 GO:0071260 GO:0021707 GO:0030182 GO:0010613 GO:0030307 GO:0010557 GO:0051092 GO:0051247 GO:2000812 GO:0008361 GO:0016202 GO:0006417 GO:0043403 GO:0051146 MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ 118 P58742 Aladin Aaas 10090 Yes SL-0178 SL-0185 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}. UNIPROT P58742 UNIPROT Q544M6 Pfam PF00400 PROSITE PS00678 PROSITE PS50294 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}. P45561-1 EBI-22092288,EBI-21917416 GO:0005813 GO:0005829 GO:0072686 GO:0005635 GO:0031965 GO:0005643 GO:0005654 GO:0000922 GO:0009566 GO:0007612 GO:0001578 GO:0090307 GO:0051028 GO:0006913 GO:0015031 MCSLGLFPPPPPRGQVTLYEHNNELVTGNSYESPPPDFRGQWINLPVLHLTKDPLKAPGRLDHGTRTAFIHHREQVWKRCINVWHDVGLFGVLNEIANSEEEVFEWVKTACSWALALCGRASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSIRVYNANSTIVPSLKHRLQRNVAALAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPNGGWLLSASPVDAVILVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKVLATTPSAVFRVWEAQMWTCEAWPTLSGRCQTGCWSPDGNRLLFTVLGEALIYSLSFPERCGTGKGHVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGNPQVQDGNPVILLFRTRNSPVFELLPCGIIQGEPGAQAQLITFHPSFNKGALLSVCWSTGRITHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHEVPLFTETSPTSAPWDPLPGQSSAQPHSPHSHL 546 P59044 NACHT, LRR and PYD domains-containing protein 6 NLRP6 9606 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:12387869}. Inflammasome {ECO:0000269|PubMed:12387869}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Nucleus membrane {ECO:0000250|UniProtKB:Q63035}. UNIPROT P59044 UNIPROT A8K9F3 UNIPROT E9PJZ8 PDB 6NCV PDB 6NDJ Pfam PF05729 Pfam PF17776 Pfam PF17779 Pfam PF02758 PROSITE PS50824 PROSITE PS50837 OMIM 609650 DisGeNET 171389 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}. GO:0061702 GO:0031965 GO:0005886 GO:0005524 GO:0005000 GO:0006954 GO:0045087 GO:0070373 GO:0043124 GO:0002862 GO:0034122 GO:0010506 GO:0050727 GO:0070255 GO:0009617 GO:0042060 MDQPEAPCSSTGPRLAVARELLLAALEELSQEQLKRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQERRLQRLGLGSGTLLSVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEAMGPAEEPEPGRARRSDTHTFNRLFRRDEEGRRPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVDFAFFMPCGELLERPGTRSLADLILDQCPDRGAPVPQMLAQPQRLLFILDGADELPALGGPEAAPCTDPFEAASGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFSDKDKKKYFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRTSKTTTSVYLLFITSVLSSAPVADGPRLQGDLRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPGVLETEVTYQFIDQSFQEFLAALSYLLEDGGVPRTAAGGVGTLLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSERVKQEALRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMDVAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLFQAMTDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQCRVQTVRVQLPDPQRGLQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDGHPQPPKELISTF 892 P59235 Nucleoporin Nup43 Nup43 10090 Yes SL-0178 SL-0185 Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. UNIPROT P59235 UNIPROT E9QPN3 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. P52927 EBI-912574,EBI-8460031 P61021 EBI-8320093,EBI-8460031 GO:0000777 GO:0031080 GO:0007049 GO:0051301 GO:0007059 GO:0051028 GO:0015031 MEEIYAKFVSQKISKTRWRPVPSGSLQTTETFATGSWDNEENCVSLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDLQFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWPAAHYHTGPSSPSYSSAPCTGIVCDNPEIVTVGEDGRINLFRVDHKEAVRTIDNADSSTLHAVTFLRTPEIVTVNSIGQLKIWDFRQQGSEPCQILSLTGDRVPLHCVDRHPDQQHVVATGGQDGMLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPDHLFTCSEDGSLWHWDASTDAPEKSSLFHQGGRSSTFLSHSLSNQAGVHQSLVSSWLSTDPAKDRIEITSLLPSRTLSVNSLDVLGPCLVCGTDAEAIYVTRQLFS 380 P59595 Nucleoprotein N 694009 Yes SL-0382 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}. UNIPROT P59595 UNIPROT Q7T3Z4 UNIPROT Q7TA14 UNIPROT Q7TF99 UNIPROT Q80E50 PDB 1SSK PDB 1X7Q PDB 2CJR PDB 2GIB PDB 2JW8 PDB 2OFZ PDB 2OG3 PDB 3I6L PDB 6IEX Pfam PF00937 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}. Self EBI-7602718,EBI-7602718 P61769 EBI-714718,EBI-7602718 P59596 EBI-7602718,EBI-25487824 P63279 EBI-7602718,EBI-80168 Q05639 EBI-7602718,EBI-354943 P62937 EBI-7602718,EBI-437708 GO:0044172 GO:0044177 GO:0044220 GO:0019013 GO:0003723 MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA 422 P60321 Nanos homolog 2 NANOS2 9606 Yes SL-0198 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}. UNIPROT P60321 UNIPROT Q17R30 UNIPROT Q4G0P8 Pfam PF05741 PROSITE PS51522 OMIM 608228 DisGeNET 339345 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}. O95273 EBI-10216569,EBI-748961 P43365 EBI-749530,EBI-10216569 Q9UIV1 EBI-10216569,EBI-2105113 Q9C0C2 EBI-10216569,EBI-2104458 Q9UKZ1 EBI-10216569,EBI-2562014 Q9UHA7 EBI-10216569,EBI-13385196 Q9UFF9 EBI-10216569,EBI-742299 Q9NZN8-4 EBI-10216569,EBI-21546893 Q9HC44 EBI-10216569,EBI-746674 Q9H9A5-2 EBI-10216569,EBI-21502930 Q9H2K2 EBI-10216569,EBI-4398527 Q96LI5 EBI-10216569,EBI-1046635 Q92600 EBI-10216569,EBI-357079 Q8N4C8-2 EBI-10216569,EBI-10988882 Q14201-2 EBI-10216569,EBI-21547457 Q14192 EBI-10216569,EBI-701903 Q14106 EBI-10216569,EBI-2562000 O95819-2 EBI-10216569,EBI-21536929 O75175 EBI-10216569,EBI-743073 D6R9H6 EBI-10216569,EBI-21546884 A5YKK6-2 EBI-10216569,EBI-16057352 P60903 EBI-717048,EBI-10216569 GO:0005737 GO:0005634 GO:0000932 GO:0048471 GO:0003729 GO:0008270 GO:0030154 GO:0030718 GO:0006402 GO:0007275 GO:0045835 GO:0017148 GO:1900153 GO:0007283 MQLPPFDMWKDYFNLSQVVWALIASRGQRLETQEIEEPSPGPPLGQDQGLGAPGANGGLGTLCNFCKHNGESRHVYSSHQLKTPDGVVVCPILRHYVCPVCGATGDQAHTLKYCPLNGGQQSLYRRSGRNSAGRRVKR 138 P60763 Ras-related C3 botulinum toxin substrate 3 RAC3 9606 Yes SL-0198 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. UNIPROT P60763 UNIPROT O14658 UNIPROT Q5U0M8 PDB 2C2H PDB 2G0N PDB 2IC5 PDB 2OV2 PDB 2QME PDB 6TM1 Pfam PF00071 PROSITE PS51420 OMIM 602050 OMIM 618577 DisGeNET 5881 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}.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. Q9P013 EBI-767084,EBI-2371709 Q9Y5V0 EBI-2690918,EBI-767084 Q7L014 EBI-767084,EBI-2555356 P19338 EBI-767084,EBI-346967 Q96IZ7 EBI-767084,EBI-712189 Q9HB71 EBI-1047302,EBI-767084 P55209 EBI-767084,EBI-356392 P07197 EBI-767084,EBI-1105035 Q9H446 EBI-767084,EBI-748952 P07195 EBI-767084,EBI-358748 P31629 EBI-2514157,EBI-767084 Q96IZ5 EBI-767084,EBI-740773 Q92581 EBI-21492614,EBI-767084 P63000-2 EBI-11049550,EBI-767084 P15153 EBI-489652,EBI-767084 Q9BYG5 EBI-767084,EBI-295391 P53365 EBI-767084,EBI-638194 Q8WUI4-6 EBI-767084,EBI-12094670 P30825 EBI-4289564,EBI-767084 P52306 EBI-746389,EBI-767084 Q9UHY1 EBI-767084,EBI-749731 GO:0005938 GO:0071944 GO:0042995 GO:0005737 GO:0031410 GO:0005856 GO:0005829 GO:0012505 GO:0070062 GO:0031941 GO:0030426 GO:0043231 GO:0030027 GO:0043005 GO:0043025 GO:0048471 GO:0005886 GO:0045202 GO:0048306 GO:0005525 GO:0003924 GO:0019901 GO:0030036 GO:0007015 GO:0030031 GO:0021894 GO:0030865 GO:0007163 GO:0048873 GO:0035556 GO:0050885 GO:0031175 GO:0033630 GO:1900026 GO:0032956 GO:0008360 GO:0014041 GO:0051056 GO:0007266 GO:0051932 GO:0016055 MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF 192 P60877 Synaptosomal-associated protein 25 SNAP25 9544 Yes SL-0198 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}. UNIPROT P60877 UNIPROT P13795 UNIPROT P36974 UNIPROT P70557 UNIPROT P70558 UNIPROT Q8IXK3 UNIPROT Q96FM2 UNIPROT Q9BR45 Pfam PF00835 PROSITE PS50192 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}. GO:0030054 GO:0005737 GO:0016020 GO:0043005 GO:0048471 GO:0001917 GO:0005886 GO:0098793 GO:0031201 GO:0070032 GO:0005484 GO:0019905 GO:0017075 GO:0005249 GO:0006887 GO:0031629 GO:0016082 GO:0006906 MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG 206 P61204 ADP-ribosylation factor 3 ARF3 9606 Yes SL-0198 Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. UNIPROT P61204 UNIPROT A8K6G8 UNIPROT B7ZB63 UNIPROT P16587 PDB 6II6 Pfam PF00025 PROSITE PS51417 OMIM 103190 DisGeNET 377 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. P54259 EBI-641535,EBI-945980 O15264 EBI-2116951,EBI-641535 Q5S007 EBI-5323863,EBI-641535 Q14186 EBI-749713,EBI-641535 O35071 EBI-2366194,EBI-641535 P97302 EBI-2552417,EBI-641535 Q8VD62 EBI-762039,EBI-641535 Q5PRE5 EBI-2553990,EBI-641535 Q8TBB1 EBI-739832,EBI-641535 P53365 EBI-638194,EBI-641535 GO:0005737 GO:0070062 GO:0000139 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006661 GO:0006890 GO:0016192 MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 P61809 Cyclin-dependent kinase 5 activator 1, p25 Cdk5r1 10090 Yes SL-0198 [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}. UNIPROT P61809 UNIPROT Q62938 Pfam PF03261 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}. GO:0030424 GO:0043292 GO:0005737 GO:0005829 GO:0030425 GO:0043197 GO:0030426 GO:0043231 GO:0016020 GO:0031594 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0098793 GO:0016533 GO:0003779 GO:0051015 GO:0045296 GO:0005509 GO:0061575 GO:0008092 GO:0046875 GO:0051879 GO:0035255 GO:0016301 GO:0002020 GO:0019901 GO:0043539 GO:0007411 GO:0007413 GO:0007420 GO:0021549 GO:0021799 GO:0009792 GO:0048013 GO:0007213 GO:0021766 GO:0035235 GO:0021819 GO:0030517 GO:0045892 GO:0007158 GO:0030182 GO:0001764 GO:0031175 GO:0018105 GO:0018107 GO:0071158 GO:0045348 GO:0043525 GO:0045860 GO:0090314 GO:0010870 GO:0032956 GO:0061001 GO:0070507 GO:0098693 GO:0048511 GO:0042501 GO:0021722 MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR 307 P61970 Nuclear transport factor 2 NUTF2 9606 Yes SL-0178 SL-0179 SL-0182 SL-0183 SL-0185 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}. UNIPROT P61970 UNIPROT B2R4G7 UNIPROT P13662 UNIPROT Q6IB67 PDB 1GY5 Pfam PF02136 PROSITE PS50177 OMIM 605813 DisGeNET 10204 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}. P37198 EBI-591778,EBI-347978 Self EBI-591778,EBI-591778 Q5S007 EBI-5323863,EBI-591778 P62826 EBI-591778,EBI-286642 Q8WUF5 EBI-5550163,EBI-591778 Q13625 EBI-77642,EBI-591778 Q5T751 EBI-12224199,EBI-591778 Q08117-2 EBI-11741437,EBI-591778 Q5TCM9 EBI-11955689,EBI-591778 Q9Y383 EBI-352851,EBI-591778 P01889 EBI-1046513,EBI-591778 Q9UET6 EBI-591778,EBI-1055987 Q8WTR7 EBI-751409,EBI-591778 P0DTD1 EBI-25475891,EBI-591778 P12004 EBI-358311,EBI-591778 Q8NCX0-3 EBI-12235840,EBI-591778 Q9NP66 EBI-740641,EBI-591778 Q8WTV1 EBI-17438286,EBI-591778 Q9BWC9 EBI-711501,EBI-591778 Q14847-2 EBI-9088686,EBI-591778 Q16740 EBI-1056029,EBI-591778 Q9NSI6-4 EBI-10693038,EBI-591778 Q9NQ35 EBI-10311735,EBI-591778 Q9C004 EBI-354861,EBI-591778 Q9BYU1 EBI-10302990,EBI-591778 Q8IY57-5 EBI-12111538,EBI-591778 Q96I34 EBI-710402,EBI-591778 Q8TDC0 EBI-5662487,EBI-591778 Q9Y247 EBI-742802,EBI-591778 Q5T0J7-2 EBI-12833746,EBI-591778 Q96NC0 EBI-2682299,EBI-591778 Q13555-5 EBI-12020154,EBI-591778 O00746 EBI-744871,EBI-591778 Q5T6F2 EBI-2514383,EBI-591778 Q96BZ8 EBI-726510,EBI-591778 Q7Z7F0-4 EBI-9089060,EBI-591778 Q9NX63 EBI-743375,EBI-591778 Q9NQG5 EBI-747925,EBI-591778 Q8N7W2-2 EBI-10181188,EBI-591778 Q9BY43-2 EBI-12178895,EBI-591778 O43790 EBI-9996498,EBI-591778 Q6NTE8 EBI-2857471,EBI-591778 P12532 EBI-1050662,EBI-591778 P15531 EBI-741141,EBI-591778 Q3KNR5 EBI-10240813,EBI-591778 Q9H0A9-2 EBI-11995806,EBI-591778 Q9UIL8 EBI-2861403,EBI-591778 Q9BYQ0 EBI-11958364,EBI-591778 Q01813 EBI-359022,EBI-591778 Q7Z3B4 EBI-741048,EBI-591778 Q9P0W2 EBI-713401,EBI-591778 P46527 EBI-519280,EBI-591778 GO:0005829 GO:0070062 GO:0005637 GO:0031965 GO:0005640 GO:0044613 GO:0005654 GO:0042802 GO:0061608 GO:0008536 GO:0017056 GO:0051028 GO:1904046 GO:0006913 GO:0042307 GO:0006611 GO:0006606 GO:0090204 MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSCIISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG 127 P62166 Neuronal calcium sensor 1 NCS1 9606 Yes SL-0198 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}. UNIPROT P62166 UNIPROT E9PAY3 UNIPROT P36610 UNIPROT Q9UK26 PDB 1G8I PDB 2LCP PDB 4GUK PDB 5O9S PDB 6QI4 Pfam PF00036 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 603315 DisGeNET 23413 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}. Q9BYM8 EBI-2340624,EBI-746987 Q9H0F6 EBI-3942966,EBI-746987 Q92844 EBI-356349,EBI-746987 Q12933 EBI-355744,EBI-746987 Q8NFZ5 EBI-359372,EBI-746987 P21554 EBI-746987,EBI-2909859 Q9BXU9 EBI-12187137,EBI-746987 Q86UW9 EBI-746987,EBI-740376 P41271 EBI-746987,EBI-10208650 Q96ST8 EBI-2799206,EBI-746987 P37058 EBI-2932988,EBI-746987 P08637 EBI-2833956,EBI-746987 Q9UPU5 EBI-746987,EBI-1642365 Q9BV23 EBI-746987,EBI-3916106 Q5W0U4 EBI-746987,EBI-5884190 P30419-2 EBI-746987,EBI-21690011 P04183 EBI-746987,EBI-712550 O75175 EBI-746987,EBI-743073 O60551 EBI-746987,EBI-3920273 Q96ST8-3 EBI-11144046,EBI-746987 Q6FHY5 EBI-16439278,EBI-746987 Q9UKN5 EBI-2803427,EBI-746987 P78358 EBI-1188472,EBI-746987 P10451 EBI-723648,EBI-746987 O60930 EBI-2372399,EBI-746987 O95868 EBI-12382527,EBI-746987 Q8IWL1 EBI-12350685,EBI-746987 Q9BXJ5 EBI-2817707,EBI-746987 Q03060-25 EBI-12884642,EBI-746987 A0A1U9X8X8 EBI-17234977,EBI-746987 Q8TDS5 EBI-12813389,EBI-746987 Q9Y336 EBI-746987,EBI-12857926 O75084 EBI-746987,EBI-746917 Q96C03-3 EBI-746987,EBI-11988931 Q7Z698 EBI-7082156,EBI-746987 Q96K80 EBI-746987,EBI-742550 Q6P5F9 EBI-2550236,EBI-746987 Q8N5S1 EBI-21587304,EBI-746987 P05362 EBI-1035358,EBI-746987 Q8NFB2 EBI-21757569,EBI-746987 GO:0044305 GO:0030054 GO:0005737 GO:0030425 GO:0031045 GO:0098978 GO:0005794 GO:0043231 GO:0048471 GO:0005886 GO:0099524 GO:0014069 GO:0099523 GO:0005509 GO:0000287 GO:0019901 GO:0005245 GO:0099626 GO:0048015 GO:0045921 GO:0010975 GO:2000300 MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGSKADPSIVQALSLYDGLV 190 P62833 Ras-related protein Rap-1A RAP1A 9913 Yes SL-0198 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}. UNIPROT P62833 UNIPROT A4IFG1 UNIPROT P10113 Pfam PF00071 PROSITE PS51421 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}. GO:0030054 GO:0005737 GO:0005769 GO:0098978 GO:0032045 GO:0005770 GO:0043005 GO:0048471 GO:0005886 GO:0019003 GO:0005525 GO:0003924 GO:0044877 GO:0017034 GO:0071320 GO:1990090 GO:0061028 GO:2000301 GO:0038180 GO:0070374 GO:0043547 GO:0010976 GO:0045860 GO:2001214 GO:0072659 GO:0032486 GO:1901888 GO:0098696 MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL 184 P63243 Receptor of activated protein C kinase 1, N-terminally processed RACK1 9913 Yes SL-0198 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}. UNIPROT P63243 UNIPROT P25388 UNIPROT P99049 UNIPROT Q3T0R8 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. GO:0005623 GO:0005737 GO:0005829 GO:0022627 GO:0030425 GO:1990630 GO:0030496 GO:0005739 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0001891 GO:0051434 GO:0030332 GO:0008656 GO:0019899 GO:0008200 GO:0042803 GO:0005080 GO:0019903 GO:0030292 GO:0030971 GO:0043022 GO:0042169 GO:0035591 GO:0007049 GO:0071333 GO:0071363 GO:0007369 GO:0030308 GO:0010629 GO:1903208 GO:0033137 GO:0050765 GO:0032091 GO:0051898 GO:0030178 GO:0043473 GO:0043065 GO:0030335 GO:0051343 GO:2000543 GO:0042998 GO:0043547 GO:2001244 GO:0051901 GO:0032436 GO:0001934 GO:0031334 GO:0016567 GO:0051726 GO:0051302 GO:2000114 GO:0032880 GO:0072344 GO:0048511 MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR 317 P70245 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Ebp 10090 Yes SL-0178 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}. UNIPROT P70245 UNIPROT Q9CSP4 Pfam PF05241 PROSITE PS51751 Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}.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. GO:0031410 GO:0005783 GO:0005789 GO:0016021 GO:0043231 GO:0005635 GO:0000247 GO:0047750 GO:0004769 GO:0006695 GO:0030097 GO:0016126 MTTNTVPLHPYWPRHLKLDNFVPNDLPTSHILVGLFSISGGLIVITWLLSSRASVVPLGAGRRLALCWFAVCTFIHLVIEGWFSLYNGILLEDQAFLSQLWKEYSKGDSRYILSDSFVVCMETVTACLWGPLSLWVVIAFLRQQPFRFVLQLVVSMGQIYGDVLYFLTELHEGLQHGEIGHPVYFWFYFVFLNAVWLVIPSILVLDAIKHLTSAQSVLDSKVMKIKSKHN 230 P70496 Phospholipase D1 Pld1 10116 Yes SL-0198 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. UNIPROT P70496 UNIPROT O08959 UNIPROT O35856 UNIPROT O54765 UNIPROT P70497 UNIPROT Q9QWJ6 Pfam PF00169 Pfam PF00614 Pfam PF13091 Pfam PF00787 PROSITE PS50003 PROSITE PS50035 PROSITE PS50195 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}. GO:0016324 GO:0098981 GO:0030139 GO:0005789 GO:0005768 GO:0005794 GO:0031985 GO:0000139 GO:0043231 GO:0030027 GO:0031902 GO:0048471 GO:0045202 GO:0031982 GO:0070290 GO:0035091 GO:0004630 GO:0048870 GO:0050830 GO:0048017 GO:0006654 GO:0008654 GO:0009395 GO:0030335 GO:0032534 GO:0098693 GO:0043434 MSLRSEARVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPTAQEACIPFSSIYNTQGFKEPNIQIYLSGCPVKAQVLEVERFTSTSRMPSVNLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREMPSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTDFLKDHRFGSYAAVHENILAKWYVNAKGYFEDIANAMEGATEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGQSLGSLTAASVESMESLSLKDKHQSHKNEPVLKSVNDTDMKLKGIGKSRKFSKFSLYRQLHRRNLHNSDSISSVDSASSYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSADTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQATAHELRYQVPGAVHAKAQLLRSAADWSAGIKHHEESIHAAYTHVIENSKHYIYIENQFFISCADDKVVFNKVGNAIAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFAQGLRLECFRLVLGYLSDPSEDIQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDRLRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT 1074 P70582 Nuclear pore complex protein Nup54 Nup54 10116 Yes SL-0178 SL-0182 SL-0185 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. UNIPROT P70582 PDB 3T97 PDB 3T98 PDB 4J3H Pfam PF13874 Pfam PF18437 Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000269|PubMed:8707840}. GO:0005635 GO:0031965 GO:0005643 GO:0044613 GO:0032991 GO:0042802 GO:0044877 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0006913 GO:0036228 GO:0006605 GO:0042306 MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTSTGTGTGLGTGLGTGLGFGGFNTQQQQQQQQTSLGGLFSQPAQAPAQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNNNIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQTEVVIYIVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNPDSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMDLSHRTLQVLIKQEIQRKSGYAIQAEEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHLISIIKDDLEDIKLVEHGLNETIHSRGGVFS 510 P70600 Protein-tyrosine kinase 2-beta Ptk2b 10116 Yes SL-0198 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. UNIPROT P70600 UNIPROT O88489 UNIPROT Q3T1H4 UNIPROT Q63201 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. Q9WUD9 EBI-8651342,EBI-7784541 GO:0097440 GO:0030424 GO:0005623 GO:0044297 GO:0005938 GO:0042995 GO:0005856 GO:0030425 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0030426 GO:0030027 GO:0045121 GO:0043025 GO:0017146 GO:0005634 GO:0048471 GO:0098794 GO:0014069 GO:0043423 GO:0005524 GO:0004683 GO:0019899 GO:0004715 GO:0008022 GO:0004672 GO:0044877 GO:0031625 GO:0007015 GO:0090630 GO:0042976 GO:0002250 GO:0001525 GO:0043534 GO:0045453 GO:0007155 GO:0030154 GO:0007166 GO:0006968 GO:0071498 GO:0071300 GO:0070098 GO:0086100 GO:0007173 GO:0048041 GO:0014009 GO:0007229 GO:0035235 GO:0060292 GO:0060291 GO:0000165 GO:0002315 GO:0043066 GO:0030502 GO:0008285 GO:0010656 GO:0045638 GO:0043524 GO:0030279 GO:0043267 GO:0031175 GO:0001556 GO:0038083 GO:0018108 GO:0030838 GO:0045766 GO:2000538 GO:0030307 GO:0030335 GO:0008284 GO:0001954 GO:0032270 GO:0007204 GO:2000573 GO:0010595 GO:0070374 GO:2000463 GO:0046330 GO:0043507 GO:0010976 GO:0045429 GO:0051000 GO:0050731 GO:0043552 GO:0045860 GO:2000379 GO:0051968 GO:0045727 GO:2000060 GO:0006468 GO:2000249 GO:0050848 GO:0030155 GO:0008360 GO:0010752 GO:2000114 GO:0032960 GO:0010758 GO:0045428 GO:2000310 GO:0051279 GO:2000058 GO:0051592 GO:0051591 GO:0042220 GO:0042493 GO:0045471 GO:0009749 GO:0009725 GO:0042542 GO:0001666 GO:0035902 GO:0010226 GO:0009612 GO:0010243 GO:0006970 GO:0000302 GO:0007172 GO:0002040 GO:0043149 GO:0033209 GO:0048010 MSGVSEPLSRVKVGTLRPPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIIHAKKDGEKRNSLPQIPTLNLESRRSHLSESCSIESDIYAEIPDETLRRPGGPQYGVAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIVMELYPYGELGHYLERNKNSLKVPTLVLYALQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMERDIAIEQERNARYRPPKILEPTAFQEPPPKPSRPKYKHPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAEKIKMRQVLDRQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYHNVMTLVEAVLELKNKLSQLPPEEYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE 1009 P80303 Nesfatin-1 NUCB2 9606 Yes SL-0178 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. UNIPROT P80303 UNIPROT A8K642 UNIPROT D3DQX5 UNIPROT Q8NFT5 UNIPROT V9HW75 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 608020 DisGeNET 4925 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}. Q99IB8 EBI-6927928,EBI-2296670 Q3KSU8 EBI-2621128,EBI-2296670 Q2MV58 EBI-11333674,EBI-2296670 Q6NUS6 EBI-11278332,EBI-2296670 Q9NQH7 EBI-1171467,EBI-2296670 O75489 EBI-1224896,EBI-2296670 Q13617 EBI-456179,EBI-2296670 Q96GM5 EBI-358489,EBI-2296670 O14980 EBI-2296670,EBI-355867 P24522 EBI-448167,EBI-2296670 P08754 EBI-2296670,EBI-357563 P84996 EBI-2680244,EBI-2296670 GO:0005829 GO:0005783 GO:0005793 GO:0070062 GO:0005615 GO:0005794 GO:0005640 GO:0005886 GO:0005509 GO:0003677 GO:0001965 GO:0005085 GO:0032099 GO:0007264 MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADIEEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIKAATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQGIPPSGPAGELKFEPHI 420 P83722 Nuclear pore complex protein Nup160 nup160 8355 No SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:11684705}. Cytoplasm {ECO:0000269|PubMed:11684705}. UNIPROT P83722 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}. GO:0005737 GO:0031080 GO:0051028 GO:0015031 PVNIYVIMADQGPAHLPVSLAVHTDMLEYVPVSKDEYFQKLKKA 44 P85091 Cytoplasmic FMR1-interacting protein 1 CYFIP1 9913 Yes SL-0198 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}. UNIPROT P85091 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}. GO:0030054 GO:0030027 GO:0005845 GO:0043005 GO:0048471 GO:0001726 GO:0045202 GO:0051015 GO:0048365 GO:0048675 GO:0030032 GO:0008360 GO:0031529 MYLTPSEKRINLSKVHPTDKLADQIFAYYKEGERDGKDEIIKNVPLKRIRK 51 P86172 NmrA-like family domain-containing protein 1 Nmral1 10116 Yes SL-0198 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}. UNIPROT P86172 Pfam PF05368 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}. GO:0005634 GO:0048471 GO:0042802 KLVVVFGATGAQGGSVARTLLEDGTFRVRVVTRNPEQKLLADLAKRLGLHYVVYSGLENIKKLAAGHFDGKGEVEEYFRKPEEYIGQNVGLSTCRTTPEEYEKLGFQGAQDLANMFRFYALKPDRNIDLTLRAQTLDQWLEQHKGDFAHL 150 P87170 CTP-dependent diacylglycerol kinase 1 ptp4 284812 Yes SL-0178 SL-0182 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}. UNIPROT P87170 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}. GO:0005783 GO:0000139 GO:0030176 GO:0031965 GO:0004143 GO:0006654 GO:0016192 MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRESEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYWGLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM 218 P87310 Mediator of RNA polymerase II transcription subunit 10 med10 284812 Yes SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT P87310 PDB 5N9J Pfam PF09748 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. GO:0005829 GO:0016592 GO:0005635 GO:0005634 GO:0003713 GO:0003712 GO:0045944 GO:0060261 GO:0006357 MLPQDDMTDEMKSLASRLEDTTQAFYDLALIVYNLEDTTPSDAIPESLDTLIRDLKSLPDISRKVNNLIPQDVLEYIEQGRNPDVYARQFSELVQKDNQYVNGKLYAIEGFQKAFAEEIKQAYPEVSSVVDKILNEGKVESTVS 144 P89457 Nuclear egress protein 2 NEC2 10315 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT P89457 Pfam PF04541 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}. GO:0044201 GO:0016021 GO:0046765 MAGMGKPYGGRPGDAFEGLVQRIRLIVPATLRGGGGESGPYSPSNPPSRCAFQFHGQDGSDEAFPIEYVLRLMNDWADVPCNPYLRVQNTGVSVLFQGFFNRPHGAPGGAITAEQTNVILHSTETTGLSLGDLDDVKGRLGLDARPMMASMWISCFVRMPRVQLAFRFMGPEDAVRTRRILCRAAEQALARRRRSRRSQDDYGAVVVAAAHHSSGAPGPGVAASGPPAPPGRGPARPWHQAVQLFRAPRPGPPALLLLAAGLFLGAAIWWAVGARL 276 P90897 DEAD-box ATP-dependent RNA helicase rde-12 rde 6239 Yes SL-0198 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}. UNIPROT P90897 UNIPROT G3MU56 UNIPROT G3MU57 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0043186 GO:0000932 GO:0048471 GO:0031332 GO:0005524 GO:0019899 GO:0003723 GO:0003724 GO:0030422 GO:0006417 GO:0043330 MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYRGQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHRSDGSNSEGVNAPVRAPRDWVPVTRDIDELVRETADRLADCDVGQDRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPLGHLGAIIKDAGFMESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVNLEFFECKGLAEKNAKLREILKQNVNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDQGADTFIHRAGRTGRTGRKENGLCVSFVDPQSDRDSLLAPKLVELIISQNLPDLKVPDFLDAMAKSSRGKSGTSGFGQRGGYGGRGGGFGGTGRGRGGGVFGGGGRGGDFGGSGNFGGSGGGGSFGGSGGGGGFGGVKPSGFGGSRNNAEPTSSGGGFGAPKAPTGFPSDNNDASEDAPAAGGFGFSTKAAQDAKKAEESATLGSSTFGTANNADEEPTETGADGNDDDEW 959 P91193 Macoilin maco 6239 Yes SL-0178 SL-0182 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}. UNIPROT P91193 Pfam PF09726 Plays a role in the regulation of neuronal activity. {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}. GO:0016021 GO:0043025 GO:0005635 GO:0031965 GO:0005791 GO:0030867 GO:0051015 GO:0008017 GO:0006935 GO:0040011 GO:0023041 GO:0043052 MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESIQMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWPIVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDVSNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTTSSRKKKHNGNSGFNSTPPNDKKKGKSIRDVDMDDGDDSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAWLFSFVFESSTPSENSLSNQQIDDDEDYEDGDGDKKNGRTDSMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNHQKSNGNSNGHARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQIKNGSSIGGGSSETLMNGRSSTEANNENDTTASDQSSPHQHSAMGSPVPFAKMPLSVNVSNRHGSPFNGKVSPIASIGSVLAAAGGPAPPDYMMAVGANVTATTGPVPQKQPRAGFHGISRYNEFTNIASGGEHRLFDTPASAISASAINGSNPEDDFLMNKGKFGAPSQPAARLA 897 Q00613 Heat shock factor protein 1 HSF1 9606 Yes SL-0198 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}. UNIPROT Q00613 UNIPROT A8K4L0 UNIPROT A8MW26 UNIPROT Q53XT4 PDB 2LDU PDB 5D5U PDB 5D5V PDB 5HDG PDB 5HDN Pfam PF00447 Pfam PF06546 PROSITE PS00434 OMIM 140580 DisGeNET 3297 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}. O60271 EBI-719620,EBI-1023301 Self EBI-719620,EBI-719620 Q96MT8-2 EBI-719620,EBI-21369329 O00505 EBI-719620,EBI-358297 O95817 EBI-719620,EBI-747185 O95757 EBI-719620,EBI-358652 Q9NZL4 EBI-719620,EBI-356763 Q03933 EBI-719620,EBI-2556750 P22392 EBI-719620,EBI-713693 P04792 EBI-719620,EBI-352682 O00629 EBI-719620,EBI-396343 Q9ULV5 EBI-766428,EBI-719620 P14618-1 EBI-719620,EBI-4304679 Q04759 EBI-719620,EBI-374762 Q9CQU5 EBI-2551595,EBI-719620 O43529 EBI-719620,EBI-3910509 Q9UKN8 EBI-719620,EBI-1237240 Q9UBC2 EBI-719620,EBI-2556746 Q96SB8 EBI-719620,EBI-605415 Q8NET4 EBI-3951768,EBI-719620 Q8NEH6 EBI-719620,EBI-743811 Q5VZK9 EBI-719620,EBI-2563775 Q15555 EBI-719620,EBI-739717 Q15029 EBI-719620,EBI-357897 Q14C86 EBI-719620,EBI-1049788 Q14683 EBI-719620,EBI-80690 Q14566 EBI-719620,EBI-374900 P61962 EBI-719620,EBI-359808 P53350 EBI-719620,EBI-476768 P51157 EBI-719620,EBI-11898753 P49736 EBI-719620,EBI-374819 P34931 EBI-719620,EBI-354912 P33991 EBI-719620,EBI-374938 O43683 EBI-719620,EBI-748936 Q9Y4E8 EBI-719620,EBI-1043104 Q9Y6Y0 EBI-719620,EBI-715774 Q9Y6A4 EBI-719620,EBI-1046872 Q00534 EBI-295663,EBI-719620 Q81JT7 EBI-719620,EBI-2811219 Q81VE1 EBI-719620,EBI-2811760 P49137 EBI-993299,EBI-719620 P09104 EBI-719620,EBI-713154 Q53FA3 EBI-10972046,EBI-719620 GO:0005813 GO:0101031 GO:0000777 GO:0005737 GO:0005829 GO:0000791 GO:0000792 GO:0000776 GO:0097431 GO:0000790 GO:0097165 GO:0005654 GO:0005634 GO:0048471 GO:0016605 GO:0045120 GO:1990904 GO:0031490 GO:0003677 GO:0003700 GO:0000981 GO:0001227 GO:0031072 GO:0051879 GO:0042802 GO:1990841 GO:0046982 GO:0019901 GO:0043621 GO:0000978 GO:0001162 GO:0043565 GO:0098847 GO:0097677 GO:0061770 GO:0034622 GO:1904385 GO:0071276 GO:0071280 GO:0072738 GO:0071392 GO:0071480 GO:0034605 GO:0070301 GO:1904845 GO:0071222 GO:1904843 GO:0035865 GO:1903936 GO:0034620 GO:0006952 GO:0006281 GO:0001892 GO:0060136 GO:0007143 GO:0000165 GO:0006397 GO:0009299 GO:0051028 GO:0010667 GO:0008285 GO:2001033 GO:0090084 GO:1901215 GO:0031333 GO:0000122 GO:0032720 GO:1902512 GO:0008284 GO:0120162 GO:0043280 GO:0090261 GO:1904528 GO:0045931 GO:1900365 GO:0040018 GO:0045944 GO:0061408 GO:0042531 GO:1900034 GO:0043618 GO:0014823 GO:1990910 GO:1990911 GO:0033574 GO:0007283 GO:0016032 MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS 529 Q00702 Protein UL20 UL20 10349 No SL-0415 SL-0418 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}. UNIPROT Q00702 Pfam PF04544 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}. GO:0044175 GO:0044178 GO:0044200 GO:0020002 GO:0016021 GO:0019012 GO:0019058 MEDAAADVDAAADAKLTGENDALLSSAFVGARPPRPRFSSHVVSLLALALALRPACCLVLALHGSRATLAALLTALAFYARAAVCAVLVARNVARDRMPLSPAQQAALGLLAAARLAFLYVALDAGRHYAPALAGALYGADCVCDALAFLLPRAYARSIMH 161 Q01017 Envelope glycoprotein M gM 10383 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q01017 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MMKASRSDTFMLRTWIQLLVLFVIMFIMSAILPIAASVEGLGFPCYFPNLVDYSLLNLTLRNAAKHLTPTLFLEAPELFVYITWSVLVDLASAIYYVVGALAILQARKTHLTSMITLQTWINLVGSHTMLFIGIARMWTLQLFIHVLSYKHVMLAAFIYFLHFCLSYMHTLSLVSRNSPKWSVLLMEQHIPKQSLLSTILDYGKPLCVNMYLSLLALEMLVFSLGFMMAIGNSFYILVSDTVLASINLYFVLTTFWYMMTEMFLQDYLKLQFGFYLGVFSGSLILLLPVLRYEAVFVSANLHKTVAVNIAMIPAMCVIAMMFRLFRYSQQVRKPENSYTPLPKRFKKRRQKQDQQLIMVETSDEEL 366 Q01041 Nuclear egress protein 1 NEC1 10383 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q01041 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MSSRSVKSRKSTKSRRHHPYVKLTDKMFFSAISSKKELGTDFLREMDAPICTSKTILLPLDLNSISPGRCIYLSPFGHSSNMEFQCEKCTESKNKGSGDVSQNHDLYSVTLVFYKNVDKVVKHKAFYLSLLSHSMENLKKSFTQPELLYAYVVVKEAGHNVFPIFFEKDDCLSICLTFKCQTLHIGESCLRMLMDNLPNYKISIDYIKDVYAMTFTQCFAIQRNISIAEDTICESVSTLDCTDELREEIVKGINALQIKDI 261 Q01045 Nuclear egress protein 2 NEC2 10383 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q01045 Pfam PF04541 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}. GO:0044201 GO:0016021 MNSTRLVYELCDIVNLYLCQPGVQIDVDRCASGPHVFTKGGTEAICTVKLSHGLVYNIEFVYKFWAHKLESVKYPFSPCFIISNNGLATTLKCFLSRPRNVNHFGHVLNIDSDVYLTKNTSVILSQDDFVKFKTNLVFSKDLDVFHSMVVFRTYLIEHRQALQFLVVKPRSSKRVNSILSSVAKTASQNFILDPPRRSEETRVCIKPWTLSKKNIWTIILSLVAVVAIILKWREL 235 Q02199 Nucleoporin NUP49/NSP49 NUP49 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT Q02199 UNIPROT D6VTY0 Pfam PF13634 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}. P14907 EBI-12315,EBI-12265 P34077 EBI-12315,EBI-12056 P40368 EBI-12331,EBI-12315 P48837 EBI-12324,EBI-12315 P49686 EBI-12310,EBI-12315 P49687 EBI-11730,EBI-12315 Q06142 EBI-9145,EBI-12315 Q02630 EBI-11703,EBI-12315 Q02629 EBI-12315,EBI-11698 P22696 EBI-6679,EBI-12315 P38265 EBI-21579,EBI-12315 P07259 EBI-12315,EBI-14372 P10592 EBI-12315,EBI-8603 P16861 EBI-12315,EBI-9428 Q04477 EBI-27228,EBI-12315 Q05166 EBI-12315,EBI-3035 Q7Z3B4 EBI-12315,EBI-741048 Q06411 EBI-12315,EBI-576 P38305 EBI-20939,EBI-12315 Q12315 EBI-7635,EBI-12315 GO:0005635 GO:0031965 GO:0005643 GO:0044613 GO:0042802 GO:0017056 GO:0006607 GO:0006999 GO:0016973 GO:0006606 GO:0036228 GO:0000055 GO:0006409 MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGSATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSLFGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQQLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSESATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNGIDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI 472 Q02629 Nucleoporin NUP100/NSP100 NUP100 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side. UNIPROT Q02629 UNIPROT D6VXL9 Pfam PF04096 Pfam PF13634 PROSITE PS51434 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}. P34077 EBI-11698,EBI-12056 P35729 EBI-11698,EBI-11713 P38181 EBI-11698,EBI-11756 P40368 EBI-12331,EBI-11698 P46673 EBI-11698,EBI-12345 P48837 EBI-12324,EBI-11698 P49686 EBI-12310,EBI-11698 P49687 EBI-11698,EBI-11730 P52593 EBI-11763,EBI-11698 P52891 EBI-11698,EBI-12337 Q02199 EBI-12315,EBI-11698 Self EBI-11698,EBI-11698 Q02630 EBI-11698,EBI-11703 Q06142 EBI-9145,EBI-11698 Q05166 EBI-11698,EBI-3035 P40482 EBI-16592,EBI-11698 P53038 EBI-11698,EBI-19106 P43603 EBI-22980,EBI-11698 P22696 EBI-6679,EBI-11698 P11484 EBI-8627,EBI-11698 P40150 EBI-11698,EBI-8632 Q02159 EBI-11698,EBI-19749 P53035 EBI-11698,EBI-10919 P38305 EBI-20939,EBI-11698 Q12315 EBI-7635,EBI-11698 GO:0031965 GO:0005643 GO:0044613 GO:0044614 GO:0008139 GO:0003723 GO:0017056 GO:0006406 GO:0031990 GO:0006607 GO:0045893 GO:0000973 GO:0006606 GO:0036228 GO:0006405 GO:0034398 MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFGQSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFGGQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLGGSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLFGKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPAGTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNTASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSSAVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKRNSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLNVINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISSKVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSIYENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT 959 Q02630 Nucleoporin NUP116/NSP116 NUP116 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side. UNIPROT Q02630 UNIPROT D6VZM2 PDB 1O6P PDB 2AIV PDB 3PBP Pfam PF04096 Pfam PF13634 PROSITE PS51434 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}. P14907 EBI-11703,EBI-12265 P30822 EBI-11703,EBI-20589 P34077 EBI-11703,EBI-12056 P35729 EBI-11703,EBI-11713 P38181 EBI-11703,EBI-11756 P40066 EBI-22648,EBI-11703 P40368 EBI-12331,EBI-11703 P46673 EBI-11703,EBI-12345 P47054 EBI-11703,EBI-25846 P48837 EBI-12324,EBI-11703 P49686 EBI-12310,EBI-11703 P49687 EBI-11703,EBI-11730 P52593 EBI-11763,EBI-11703 P52891 EBI-11703,EBI-12337 P53011 EBI-11703,EBI-16940 Q02199 EBI-11703,EBI-12315 Q02629 EBI-11698,EBI-11703 Self EBI-11703,EBI-11703 Q06142 EBI-9145,EBI-11703 Q05166 EBI-11703,EBI-3035 Q04934 EBI-35255,EBI-11703 P53038 EBI-19106,EBI-11703 P40054 EBI-16961,EBI-11703 P45819 EBI-24068,EBI-11703 P39723 EBI-20675,EBI-11703 P35177 EBI-17958,EBI-11703 Q03330 EBI-7458,EBI-11703 P50102 EBI-19863,EBI-11703 Q12443 EBI-11703,EBI-32591 P32589 EBI-11703,EBI-8648 P11484 EBI-11703,EBI-8627 P10592 EBI-11703,EBI-8603 P38305 EBI-20939,EBI-11703 Q12315 EBI-7635,EBI-11703 GO:0031965 GO:0005643 GO:0044613 GO:0044614 GO:0051117 GO:0042802 GO:0008139 GO:0003723 GO:0017056 GO:0006406 GO:0006999 GO:0016973 GO:0000973 GO:0006606 GO:0000055 GO:0006405 GO:0034398 GO:0006409 MFGVSRGAFPSATTQPFGSTGSTFGGQQQQQQPVANTSAFGLSQQTNTTQAPAFGNFGNQTSNSPFGMSGSTTANGTPFGQSQLTNNNASGSIFGGMGNNTALSAGSASVVPNSTAGTSIKPFTTFEEKDPTTGVINVFQSITCMPEYRNFSFEELRFQDYQAGRKFGTSQNGTGTTFNNPQGTTNTGFGIMGNNNSTTSATTGGLFGQKPATGMFGTGTGSGGGFGSGATNSTGLFGSSTNLSGNSAFGANKPATSGGLFGNTTNNPTNGTNNTGLFGQQNSNTNGGLFGQQQNSFGANNVSNGGAFGQVNRGAFPQQQTQQGSGGIFGQSNANANGGAFGQQQGTGALFGAKPASGGLFGQSAGSKAFGMNTNPTGTTGGLFGQTNQQQSGGGLFGQQQNSNAGGLFGQNNQSQNQSGLFGQQNSSNAFGQPQQQGGLFGSKPAGGLFGQQQGASTFASGNAQNNSIFGQNNQQQQSTGGLFGQQNNQSQSQPGGLFGQTNQNNNQPFGQNGLQQPQQNNSLFGAKPTGFGNTSLFSNSTTNQSNGISGNNLQQQSGGLFQNKQQPASGGLFGSKPSNTVGGGLFGNNQVANQNNPASTSGGLFGSKPATGSLFGGTNSTAPNASSGGIFGSNNASNTAATTNSTGLFGNKPVGAGASTSAGGLFGNNNNSSLNNSNGSTGLFGSNNTSQSTNAGGLFQNNTSTNTSGGGLFSQPSQSMAQSQNALQQQQQQQRLQIQNNNPYGTNELFSKATVTNTVSYPIQPSATKIKADERKKASLTNAYKMIPKTLFTAKLKTNNSVMDKAQIKVDPKLSISIDKKNNQIAISNQQEENLDESILKASELLFNPDKRSFKNLINNRKMLIASEEKNNGSQNNDMNFKSKSEEQETILGKPKMDEKETANGGERMVLSSKNDGEDSATKHHSRNMDEENKENVADLQKQEYSEDDKKAVFADVAEKDASFINENYYISPSLDTLSSYSLLQLRKVPHLVVGHKSYGKIEFLEPVDLAGIPLTSLGGVIITFEPKTCIIYANLPNRPKRGEGINVRARITCFNCYPVDKSTRKPIKDPNHQLVKRHIERLKKNPNSKFESYDADSGTYVFIVNHAAEQT 1113 Q02821 Importin subunit alpha SRP1 559292 Yes SL-0198 Cytoplasm, perinuclear region. Note=Mainly localized at the periphery of the nucleus. UNIPROT Q02821 UNIPROT D6W0Z8 PDB 1BK5 PDB 1BK6 PDB 1EE4 PDB 1EE5 PDB 1UN0 PDB 1WA5 PDB 2C1T PDB 4PVZ PDB 4XZR PDB 5H2W PDB 5H2X PDB 5T94 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. P20591 EBI-1797,EBI-929476 P20676 EBI-12392,EBI-1797 P32499 EBI-1797,EBI-12401 P34160 EBI-745,EBI-1797 P39705 EBI-20731,EBI-1797 P40069 EBI-1797,EBI-9166 P32562 EBI-4440,EBI-1797 Q08904 EBI-32829,EBI-1797 P53184 EBI-1797,EBI-23741 P51601 EBI-1797,EBI-7429 P25367 EBI-21708,EBI-1797 P08536 EBI-10753,EBI-1797 Q03063 EBI-29752,EBI-1797 P17423 EBI-9685,EBI-1797 P60010 EBI-1797,EBI-2169 P38821 EBI-6008,EBI-1797 Q02895 EBI-1797,EBI-35030 Q12306 EBI-17490,EBI-1797 Q06549 EBI-1797,EBI-4455 P32318 EBI-1797,EBI-19215 P43619 EBI-11793,EBI-1797 Q03373 EBI-34019,EBI-1797 P09201 EBI-1797,EBI-6744 Q12189 EBI-15898,EBI-1797 P15202 EBI-4061,EBI-1797 P18759 EBI-1797,EBI-16565 P38716 EBI-24682,EBI-1797 Q12206 EBI-1797,EBI-20571 P33307 EBI-5168,EBI-1797 Q02796 EBI-30514,EBI-1797 P22216 EBI-17843,EBI-1797 P36124 EBI-16993,EBI-1797 Q04116 EBI-2889005,EBI-1797 P10591 EBI-8591,EBI-1797 P11484 EBI-1797,EBI-8627 P25303 EBI-1797,EBI-16711 P32447 EBI-3003,EBI-1797 Q12495 EBI-3913,EBI-1797 P53131 EBI-505,EBI-1797 P50875 EBI-17751,EBI-1797 Q05027 EBI-27500,EBI-1797 P22579 EBI-17160,EBI-1797 P50102 EBI-19863,EBI-1797 P38129 EBI-18868,EBI-1797 P35177 EBI-17958,EBI-1797 Q03330 EBI-7458,EBI-1797 Q9HAN9 EBI-1797,EBI-3917542 Q9NS73 EBI-1797,EBI-741953 Q9NS73-5 EBI-10182361,EBI-1797 Q9NVV9 EBI-741515,EBI-1797 P22234 EBI-1797,EBI-712261 O00635 EBI-1797,EBI-2130415 P35520 EBI-740135,EBI-1797 P63261 EBI-1797,EBI-351292 A0A0C4DGF1 EBI-10188476,EBI-1797 Q7Z6G3-2 EBI-1797,EBI-10172876 Q96A10 EBI-1797,EBI-10486892 P13196 EBI-3905054,EBI-1797 P60709 EBI-1797,EBI-353944 Q13137 EBI-739580,EBI-1797 Q13557-8 EBI-1797,EBI-11534483 Q13867 EBI-1797,EBI-718504 Q15038 EBI-1797,EBI-724310 Q15041 EBI-1797,EBI-714543 Q8WVF5 EBI-1797,EBI-741463 Q14974 EBI-1797,EBI-286758 Q12449 EBI-37072,EBI-1797 P27466 EBI-9592,EBI-1797 P46948 EBI-1788,EBI-1797 Q12149 EBI-1782,EBI-1797 Q02724 EBI-20050,EBI-1797 Q12124 EBI-37542,EBI-1797 P13259 EBI-5254,EBI-1797 P53256 EBI-1842,EBI-1797 P53881 EBI-29042,EBI-1797 Q08278 EBI-10674,EBI-1797 P53833 EBI-13638,EBI-1797 P50111 EBI-29626,EBI-1797 P22215 EBI-17397,EBI-1797 P53866 EBI-1797,EBI-29168 P32337 EBI-1797,EBI-9159 P41940 EBI-1797,EBI-11191 Q06142 EBI-1797,EBI-9145 P00330 EBI-1797,EBI-2218 P38792 EBI-1757,EBI-1797 P32799 EBI-5070,EBI-1797 P53859 EBI-1731,EBI-1797 Q08285 EBI-1831,EBI-1797 Q05636 EBI-1810,EBI-1797 Q08920 EBI-33556,EBI-1797 Q12464 EBI-31814,EBI-1797 Q06218 EBI-5640,EBI-1797 P28003 EBI-20647,EBI-1797 P15108 EBI-8666,EBI-1797 GO:0005737 GO:0005829 GO:0042564 GO:0005643 GO:0005654 GO:0005634 GO:0048471 GO:0032991 GO:0097718 GO:0061608 GO:0008139 GO:0044877 GO:0006607 GO:0031144 GO:0006612 MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN 542 Q03001 Dystonin DST 9606 Yes SL-0178 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}. UNIPROT Q03001 UNIPROT B7Z3H1 UNIPROT E7ERU0 UNIPROT O94833 UNIPROT Q12825 UNIPROT Q13266 UNIPROT Q13267 UNIPROT Q13775 UNIPROT Q5TBT0 UNIPROT Q5TBT2 UNIPROT Q5TF23 UNIPROT Q5TF24 UNIPROT Q8N1T8 UNIPROT Q8N8J3 UNIPROT Q8WXK8 UNIPROT Q8WXK9 UNIPROT Q96AK9 UNIPROT Q96DQ5 UNIPROT Q96J76 UNIPROT Q96QT5 UNIPROT Q9H555 UNIPROT Q9UGD7 UNIPROT Q9UGD8 UNIPROT Q9UN10 PDB 3GJO Pfam PF00307 Pfam PF13499 Pfam PF02187 Pfam PF00681 Pfam PF17902 Pfam PF00435 Pfam PF18373 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 PROSITE PS51460 PROSITE PS50002 OMIM 113810 OMIM 614653 OMIM 615425 DisGeNET 667 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.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. O95295 EBI-296723,EBI-310758 P04626 EBI-310758,EBI-641062 P51151 EBI-4401353,EBI-310758 P03372 EBI-78473,EBI-310758 Q9NRI5 EBI-310758,EBI-529989 Q8TDR0-2 EBI-310758,EBI-11946508 Q9UKE5 EBI-310758,EBI-1051794 Q96AC1 EBI-310758,EBI-4399465 Q99459 EBI-310758,EBI-374880 O60239 EBI-310758,EBI-624860 Q96MT8-2 EBI-310758,EBI-21369329 P61764 EBI-310758,EBI-960169 Q9NV70 EBI-310758,EBI-1045313 Q96BS2 EBI-310758,EBI-740653 Q9BY11 EBI-310758,EBI-721769 P13569 EBI-349854,EBI-310758 Q14108 EBI-1564650,EBI-310758 Q96GC9 EBI-2800296,EBI-310758 Q9H8S9 EBI-748229,EBI-310758 Q7L9L4 EBI-2558745,EBI-310758 Q99IB8 EBI-310758,EBI-6927928 P29991 EBI-310758,EBI-8826488 Q13951 EBI-310758,EBI-718750 P25054 EBI-310758,EBI-727707 Q16659 EBI-1384105,EBI-310758 Q13952 EBI-310758,EBI-389755 Q13177 EBI-310758,EBI-1045887 Q15691 EBI-310758,EBI-1004115 P19838 EBI-300010,EBI-310758 Q9NQW6 EBI-2553589,EBI-310758 Q5JU00 EBI-11335160,EBI-310758 Q61166 EBI-2027055,EBI-310758 Q3UH45 EBI-11090767,EBI-310758 Q9D6P8 EBI-11062253,EBI-310758 P35579 EBI-350338,EBI-310758 P46013 EBI-876367,EBI-310758 Q15388 EBI-711636,EBI-310758 Q9NS69 EBI-1047508,EBI-310758 O43493 EBI-1752146,EBI-310758 P15311 EBI-1056902,EBI-310758 P49841 EBI-373586,EBI-310758 O15155 EBI-749204,EBI-310758 P11279 EBI-2805407,EBI-310758 P43355 EBI-740978,EBI-310758 O75386 EBI-5357290,EBI-310758 Q14324 EBI-310758,EBI-5653200 Q96CV9 EBI-748974,EBI-310758 Q9UKG1 EBI-741243,EBI-310758 Q8IZP0 EBI-375446,EBI-310758 Q15327 EBI-5653378,EBI-310758 P0C862 EBI-310758,EBI-5654640 Q8N3C7 EBI-310758,EBI-5655540 Q13188 EBI-992580,EBI-310758 Q8TDR0 EBI-310758,EBI-928811 Q9UHX1 EBI-1053259,EBI-310758 Q15287 EBI-310758,EBI-395959 P15121 EBI-310758,EBI-1052491 O76021 EBI-358028,EBI-310758 P50993 EBI-2952691,EBI-310758 P05455 EBI-358037,EBI-310758 Q12996 EBI-1056775,EBI-310758 P49286 EBI-1188341,EBI-310758 Q86X19 EBI-11343485,EBI-310758 Q9H9Q2 EBI-2510162,EBI-310758 Q9NYQ7 EBI-310758,EBI-308417 Q9HCM3 EBI-310758,EBI-311350 P62993 EBI-401755,EBI-310758 GO:0015629 GO:0030424 GO:1904115 GO:0009925 GO:0005604 GO:0005938 GO:0031252 GO:0005737 GO:0031410 GO:0005829 GO:0005789 GO:0005925 GO:0031673 GO:0030056 GO:0016021 GO:0005882 GO:0045111 GO:0016020 GO:0015630 GO:0035371 GO:0005635 GO:0005654 GO:0005634 GO:0030018 GO:0003779 GO:0005509 GO:0005178 GO:0008017 GO:0051010 GO:0008022 GO:0042803 GO:0005198 GO:0007155 GO:0048870 GO:0031122 GO:0007010 GO:0031581 GO:0007229 GO:0045104 GO:0030011 GO:0000226 GO:0009611 GO:0008090 GO:0042060 MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVTTMSERTFPNNPVELKALYNQYLQFKETEIPPKETEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLEMLQQIANRVQRDSVICEDKLILAGNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNECSSVYSKGRILTTEQTKLMISGITQSLNSGFAQTLHPSLTSGLTQSLTPSLTSSSMTSGLSSGMTSRLTPSVTPAYTPGFPSGLVPNFSSGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEINMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTAPLKLTYAEKLHRLESQYAKLLNTSRNQERHLDTLHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEEKEELLQYKSTIANLMGKAKTIIQLKPRNSDCPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDLANRIEQQYQNVLTLWHESHINMKSVVSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKELERLKDDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQVYSMSSTYIDKLKTVNLVLKNTQAAEALVKLYETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVERWQNVHVQIDNRLRDLEGIGKSLKYYRDTYHPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSATVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSADLIIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKKEQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSGDVKVEEKLDKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTGIRLLETQLMISGLISPELRKCFDLKDAKSHGLIDEQILCQLKELSKAKEIISAASPTTIPVLDALAQSMITESMAIKVLEILLSTGSLVIPATGEQLTLQKAFQQNLVSSALFSKVLERQNMCKDLIDPCTSEKVSLIDMVQRSTLQENTGMWLLPVRPQEGGRITLKCGRNISILRAAHEGLIDRETMFRLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSILTYQVQTGGIIQSNPAKRLTVDEAVQCDLITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKILNGRQKIAALYIPESSQVIGLDAAKQLGIIDNNTASILKNITLPDKMPDLGDLEACKNARRWLSFCKFQPSTVHDYRQEEDVFDGEEPVTTQTSEETKKLFLSYLMINSYMDANTGQRLLLYDGDLDEAVGMLLEGCHAEFDGNTAIKECLDVLSSSGVFLNNASGREKDECTATPSSFNKCHCGEPEHEETPENRKCAIDEEFNEMRNTVINSEFSQSGKLASTISIDPKVNSSPSVCVPSLISYLTQTELADISMLRSDSENILTNYENQSRVETNERANECSHSKNIQNFPSDLIENPIMKSKMSKFCGVNETENEDNTNRDSPIFDYSPRLSALLSHDKLMHSQGSFNDTHTPESNGNKCEAPALSFSDKTMLSGQRIGEKFQDQFLGIAAINISLPGEQYGQKSLNMISSNPQVQYHNDKYISNTSGEDEKTHPGFQQMPEDKEDESEIEEYSCAVTPGGDTDNAIVSLTCATPLLDETISASDYETSLLNDQQNNTGTDTDSDDDFYDTPLFEDDDHDSLLLDGDDRDCLHPEDYDTLQEENDETASPADVFYDVSKENENSMVPQGAPVGSLSVKNKAHCLQDFLMDVEKDELDSGEKIHLNPVGSDKVNGQSLETGSERECTNILEGDESDSLTDYDIVGGKESFTASLKFDDSGSWRGRKEEYVTGQEFHSDTDHLDSMQSEESYGDYIYDSNDQDDDDDDGIDEEGGGIRDENGKPRCQNVAEDMDIQLCASILNENSDENENINTMILLDKMHSCSSLEKQQRVNVVQLASPSENNLVTEKSNLPEYTTEIAGKSKENLLNHEMVLKDVLPPIIKDTESEKTFGPASISHDNNNISSTSELGTDLANTKVKLIQGSELPELTDSVKGKDEYFKNMTPKVDSSLDHIICTEPDLIGKPAEESHLSLIASVTDKDPQGNGSDLIKGRDGKSDILIEDETSIQKMYLGEGEVLVEGLVEEENRHLKLLPGKNTRDSFKLINSQFPFPQITNNEELNQKGSLKKATVTLKDEPNNLQIIVSKSPVQFENLEEIFDTSVSKEISDDITSDITSWEGNTHFEESFTDGPEKELDLFTYLKHCAKNIKAKDVAKPNEDVPSHVLITAPPMKEHLQLGVNNTKEKSTSTQKDSPLNDMIQSNDLCSKESISGGGTEISQFTPESIEATLSILSRKHVEDVGKNDFLQSERCANGLGNDNSSNTLNTDYSFLEINNKKERIEQQLPKEQALSPRSQEKEVQIPELSQVFVEDVKDILKSRLKEGHMNPQEVEEPSACADTKILIQNLIKRITTSQLVNEASTVPSDSQMSDSSGVSPMTNSSELKPESRDDPFCIGNLKSELLLNILKQDQHSQKITGVFELMRELTHMEYDLEKRGITSKVLPLQLENIFYKLLADGYSEKIEHVGDFNQKACSTSEMMEEKPHILGDIKSKEGNYYSPNLETVKEIGLESSTVWASTLPRDEKLKDLCNDFPSHLECTSGSKEMASGDSSTEQFSSELQQCLQHTEKMHEYLTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLAEEFLKSLPSDFPRGHVEELSISHQSLKTAFSSLSNVSSERTKQIMLAIDSEMSKLAVSHEEFLHKLKSFSDWVSEKSKSVKDIEIVNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQDLSPNQSKQLLRLLNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQACEATASKHLSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKEQGQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTDPSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNNSGISLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEEFWANKGLTSIKKDMTDISHGYEDLGLLLKDKIAELNTKLSKLQKAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLQGIGHFQNTIREMFSQFAEFDDELDSMAPVGRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLATEETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHSRSELLQQALCNAKIFGEDEVELMNWLNEVHDKLSKLSVQDYSTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEASQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAILRSQQFDQAADAELSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERAQSLVNQFWETYEELWPWLTETQSIISQLPAPALEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLYSQIKEDVKKRAVALDEAISQSTQFHDKIDQILESLERIVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGTDKDISAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVMELAEKFWCDHMSLIVTIKDTQDFIRDLEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVFDWVDIAGGKLASMSPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKHTVQDPLMELKLIWDSLEERIINRQHKLEGALLALGQFQHALDELLAWLTHTEGLLSEQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQQWLTDTERHLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEALNLAMEFHNSLQDFINWLTQAEQTLNVASRPSLILDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWSKLMEWLEESEKSLDSELEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSLADDNLKLDDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQELSTRWETVCALSISKQTRLEAALRQAEEFHSVVHALLEWLAEAEQTLRFHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASALAGLIAKQELLEALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEEMTRKQPDVDKVTKTYKRRAADPSSLQSHIPVLDKGRAGRKRFPASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKMLRSESNSSITTTQPTIAKGRTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSVSSQAAQAASPQVPATTTPKGTPIQGSKLRLPGYLSGKGFHSGEDSGLITTAAARVRTQFADSKKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEIQSVCSDVETVPQTHRPTPRAGSRPSTAKPSKIPTPQRKSPASKLDKSSKR 7570 Q03281 Inner nuclear membrane protein HEH2 HEH2 559292 Yes SL-0178 SL-0179 SL-0182 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. UNIPROT Q03281 UNIPROT D6VT82 PDB 4PVZ Pfam PF12949 Pfam PF09402 DE Reference Proteome: Yes; P38181 EBI-22131,EBI-11756 P39929 EBI-22131,EBI-17554 P11484 EBI-22131,EBI-8627 P32589 EBI-8648,EBI-22131 P02829 EBI-8659,EBI-22131 P52917 EBI-20475,EBI-22131 P32462 EBI-6502,EBI-22131 P47088 EBI-22131,EBI-26307 GO:0016021 GO:0005635 GO:0005637 GO:0034399 MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKSKKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSELETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETRNESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIWLWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEPGYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWESQREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLGVLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQSENIELYLLEENGEIMTCWEWKE 663 Q03297 Period circadian protein per 7260 No SL-0198 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}. UNIPROT Q03297 UNIPROT O18421 UNIPROT O18422 UNIPROT P91721 UNIPROT P91722 Pfam PF00989 PROSITE PS50112 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}. GO:0005634 GO:0048471 GO:0006355 GO:0048511 NKDKSRKKKKPKCIALATATAVSLEGTRESPLPASGSCEKVLQELQDTQQLGEPLVVTETQLSEQLLETEQNEDQNKSEQLAQFPLPTPIVTTLSPGIGPGHDCVGGASGGAVAGGCLVVGAGTDKTSELIPGKLESAGTKPSQERPKEESFCCVISMHDGIVLYTTPSISDVLGFPRDMWLGRSFVDFVHHKDRATFASQITTGIPIAESRGCMPKDARSTFCVMLRRYRGLNSGGFGVIGRAVNYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAAVSALGYLPQDLIGRSIMDFYHHEDLSVMKDTYETVMKKGQTAGASFCSKPYRFLIQNGCFVLLETEWTSFVNPWSRKLEFVVGHHRVFQGPKLCNVFETSVSAKPKISEEAQNRNARIKEDIVKLLAETVSRPSDTVKQEVSRRCQALANFMETLMDEITRADLKLDLPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLHMSSVTNTSNAGTGTSGTGNSGDGGGGGGADGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGDKNKKSANEAMKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTGGGGGGGGGGGGGGGGGLPLFLDVTHTSSSSQNKGPTGVAAGGAGGGVGGGGGSCSGLGGNGNVGSGNGNNSQPSTNQYTQSGLPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFPTFYYIPASIAASSPSSTNTNPNRPHKHAHVHSSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMVYQPVPFAGVANPMQLPEQASKNVYTTQPVMVAPPTATNKTQGAFHSITPAPPQRPSSQATSVKAETGSNVAPSDTSKKEVPDSPITPTMGDFTLDQPCNNNATTLKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPENDKDAKHRKLKSLDQSDNKIVEHPEEDQTQHG 1093 Q03427 Lamin-C LamC 7227 Yes SL-0178 SL-0180 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}. UNIPROT Q03427 UNIPROT Q24374 UNIPROT Q9V729 Pfam PF00038 Pfam PF00932 PROSITE PS51842 PROSITE PS51841 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}. O76417 EBI-498761,EBI-498159 Q8T0N1 EBI-498761,EBI-499087 Q9VJ29 EBI-498761,EBI-153860 GO:0005638 GO:0016020 GO:0005635 GO:0005652 GO:0034399 GO:0070732 GO:0005200 GO:0006325 GO:0006342 GO:0007112 GO:0060415 GO:0031081 GO:0030833 GO:0035989 MSARRVTLNTRVSRASTSTPVGGASTSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEERRLNIESPGRPTTDSGISSNGSHLTASASSRSGRVTPSGRRSATPGISGSSAVKRRRTVIDESEDRTLSEYSVNAAAKGDLEIIEADVEGRFIKLHNKGTEEINLTGWQLTRIAGDEELAFKFSRGSKVLGGASVTIWSVDAGTAHDPPNNLVMKKKWPVANSMRSVLANADKEDVASYDRVRANVSSHTSRHRSSGTPSTGFTLGSGAGSTGVRSLFSLLF 621 Q03455 Probable zinc transporter MSC2 MSC2 559292 Yes SL-0178 SL-0182 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}. UNIPROT Q03455 UNIPROT D6VSI6 Pfam PF01545 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}. P53735 EBI-28507,EBI-34990 Q06677 EBI-34990,EBI-30084 P53919 EBI-28887,EBI-34990 GO:0005623 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0005385 GO:0006882 GO:0055085 GO:0006829 MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFNFINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPSFDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIVNKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFNEITSSIKTDLLSLLFVVVAEYVSSFSNKQPDSHSHNHAHHHSHLTDSLPLENESMFKQMALNKDTRSIFSFLLLNTAFMFVQLLYSFRSKSLGLLSDSLHMALDCTSLLLGLIAGVLTKKPASDKFPFGLNYLGTLAGFTNGVLLLGIVCGIFVEAIERIFNPIHLHATNELLVVATLGLLVNLVGLFAFDHGAHDHGGTDNENMKGIFLHILADTLGSVGVVISTLLIKLTHWPIFDPIASLLIGSLILLSALPLLKSTSANILLRLDDKKHNLVKSALNQISTTPGITGYTTPRFWPTESGSSGHSHAHTHSHAENHSHEHHHDQKNGSQEHPSLVGYIHVQYVDGENSTIIKKRVEKIFENVSIKAWVQVEPQNSTCWCRATSMNTISANPNSLPLQPIAN 724 Q03707 Inner nuclear membrane protein SRC1 SRC1 559292 Yes SL-0178 SL-0179 SL-0182 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. UNIPROT Q03707 UNIPROT D6VZE1 UNIPROT Q03712 PDB 4XZR Pfam PF12949 Pfam PF09402 Plays a role in sister chromatid separation. {ECO:0000269|PubMed:11754482}. P25491 EBI-18064,EBI-10420 P38181 EBI-11756,EBI-18064 P39929 EBI-17554,EBI-18064 P10591 EBI-8591,EBI-18064 P11484 EBI-8627,EBI-18064 P38788 EBI-18064,EBI-24570 P40150 EBI-18064,EBI-8632 P32589 EBI-8648,EBI-18064 P33416 EBI-8680,EBI-18064 Q12329 EBI-8571,EBI-18064 P10592 EBI-8603,EBI-18064 Q12159 EBI-18064,EBI-29516 Q12066 EBI-18064,EBI-35877 Q12213 EBI-18064,EBI-15427 P06169 EBI-18064,EBI-5687 GO:0016021 GO:0005635 GO:0005637 GO:0034399 GO:0034087 GO:0043007 GO:0000070 MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSSPSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNKSDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVKTPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEVEQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTEKDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRLLIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDDKKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQLSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKVIEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNIKSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI 834 Q03760 Pre-mRNA leakage protein 39 PML39 559292 Yes SL-0178 SL-0182 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. UNIPROT Q03760 UNIPROT D6W0H7 Pfam PF07967 Involved in the nuclear retention of improperly spliced pre- mRNAs. {ECO:0000269|PubMed:16162818}. P30822 EBI-20589,EBI-27933 P40150 EBI-8632,EBI-27933 GO:0031965 GO:0008270 GO:0051237 GO:0051028 MEKDALEVRLKSIRHSLDKNTKLLPGKYRNTLGERLITKWRYKKKSHNGSSMLPEKCKSHVQLYDDLVQESSKHFVGFRLHDLRALLKRICSIQNYTRHVLIEWDVRWVNPLTLASKGWEPYQSASQSQVPFKCCCCHAIMTIPLLKNGDDVADYTMKLNEKIWNSNIIGNHLQKCPWRENQVDLNKEYYLSSQNLIREIERIHTEIDRIVSGSNEFSLKRNSSRIFHYLSEKEIQKLAFFFDCKDYSLVGLLLLGYTKFQKDDLVQCTACFHRASLKKLEYTEFNGHALWCRYYNKELLPTMLLELIGKEDKLITKLGVGERLNKLEAVLQTL 334 Q03790 Nucleoporin NUP53 NUP53 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT Q03790 UNIPROT D6VZX4 PDB 3W3Y PDB 5UAZ Pfam PF05172 PROSITE PS51472 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}. P32500 EBI-11950,EBI-27321 P34077 EBI-12056,EBI-27321 P38181 EBI-27321,EBI-11756 P40064 EBI-27321,EBI-11740 P40368 EBI-12331,EBI-27321 P46673 EBI-12345,EBI-27321 P47054 EBI-27321,EBI-25846 Self EBI-27321,EBI-27321 Q06142 EBI-9145,EBI-27321 Q05166 EBI-27321,EBI-3035 P32597 EBI-18410,EBI-27321 P11938 EBI-14821,EBI-27321 P38265 EBI-21579,EBI-27321 P11484 EBI-27321,EBI-8627 P10592 EBI-8603,EBI-27321 P32589 EBI-27321,EBI-8648 P10591 EBI-27321,EBI-8591 Q04477 EBI-27228,EBI-27321 Q05359 EBI-6581,EBI-27321 P16140 EBI-27321,EBI-20254 Q12398 EBI-27321,EBI-32583 P00925 EBI-27321,EBI-6475 P38305 EBI-20939,EBI-27321 Q12315 EBI-7635,EBI-27321 GO:0031965 GO:0005643 GO:0044613 GO:0044615 GO:0042802 GO:0005543 GO:0003697 GO:0017056 GO:0007049 GO:0051301 GO:0051028 GO:0006607 GO:0006999 GO:0045893 GO:0006606 GO:0034501 GO:0007088 GO:0060188 GO:0006355 GO:0072417 MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFNNPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDSNEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGSKEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKSELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKVRNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL 475 Q03963 Interferon-induced, double-stranded RNA-activated protein kinase Eif2ak2 10090 Yes SL-0198 Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q03963 UNIPROT Q61742 UNIPROT Q62026 PDB 1X48 PDB 1X49 Pfam PF00035 Pfam PF00069 PROSITE PS50137 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. P35569 EBI-2603444,EBI-400825 P35570 EBI-520230,EBI-2603444 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0005524 GO:0003725 GO:0004694 GO:0042802 GO:0004715 GO:0004672 GO:0000186 GO:0034198 GO:0051607 GO:0030968 GO:0045087 GO:0043066 GO:0033689 GO:0017148 GO:0045071 GO:0043065 GO:0032722 GO:0001819 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0035455 GO:0032496 GO:0009636 GO:0009615 GO:0033197 GO:0006412 MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKVDCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKLLKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNSDFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYKTRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATALENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLKKLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC 515 Q04175 Importin beta SMX1 SXM1 559292 Yes SL-0178 SL-0185 Cytoplasm. Nucleus, nuclear pore complex. UNIPROT Q04175 UNIPROT D6VT29 Pfam PF08506 Pfam PF03810 PROSITE PS50166 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}. P25491 EBI-10420,EBI-35508 P22696 EBI-6679,EBI-35508 Q03833 EBI-35786,EBI-35508 P53688 EBI-2066550,EBI-35508 P10591 EBI-8591,EBI-35508 P39987 EBI-35508,EBI-22339 P11484 EBI-8627,EBI-35508 P40564 EBI-35508,EBI-25380 P53131 EBI-505,EBI-35508 P39715 EBI-6302,EBI-35508 P16140 EBI-35508,EBI-20254 P36144 EBI-35508,EBI-26459 P07259 EBI-35508,EBI-14372 P02994 EBI-35508,EBI-6314 P10592 EBI-35508,EBI-8603 P46654 EBI-35508,EBI-16037 P26785 EBI-35508,EBI-14513 P0C0W9 EBI-35508,EBI-15275 P41940 EBI-35508,EBI-11191 P40495 EBI-35508,EBI-25128 P33399 EBI-35508,EBI-10046 P33892 EBI-35508,EBI-7442 P00549 EBI-35508,EBI-9890 P32357 EBI-340,EBI-35508 P38697 EBI-9186,EBI-35508 P07702 EBI-10271,EBI-35508 P36000 EBI-2206,EBI-35508 Q03862 EBI-31385,EBI-35508 P53230 EBI-35508,EBI-23156 GO:0005737 GO:0005829 GO:0005635 GO:0005643 GO:0005634 GO:0061608 GO:0008536 GO:0006406 GO:0006606 MVQEQAILSCIEQTMVADAKIIKEAEQQLFEFQKQPGFTSFLLNIVSDDNFALNVRLSSAIYLKNKIHRSWDTKREDGIKADEKLSIKERLIETLVKNCENNHIRPILTETINGILVGQEDWDLAPIIKNLLSSGDASYIYPGLLLLFQLCKAHRWDMVGSRDYIDSVIEELFPIVEGIASNIGSQTDYRSNEILYLILKSFKYACLNNLPQYFSQPERIMSWVQLHLYLCSKPLPVEVMELDPADRSLDKRVKVNKWGFGNLNRFLQRYNKITKAITKEFIDYIFNTIVPIILREFFKDIEAWGNNSLWLSDSSLYFLISFLEKCVTIDQLYPLIEPHLQIIFENVIFPCLCANEQSIELLEDDQEEYTRRYFDINREGSTPDAASADFIFLIGSKRPEKLNNILPFINDIFTRFDANSSDINMAFKEEGALRTLSNLFSFIDEPSVLENIFGHFIVPLLSQDKYMFLVARSLETIALYSEEFKDMNILSQLFELTYTNFLNSNVLPVQIEAADAIKCLIVSNPQIHPAVSAHVPGMMEKLLKLSKIFEIDILSEVMEALVERFSDELSPFAKDLASNLVEQFLRIAQALVENPSETYSASDQEQEIQASGLLQTMTTMVMSMNKVPLIESLAPVVKFVVLHAQISFITEAVDLLDALTISSHLLYNQIAPPIWELLHDILDSFQTYAMDYFEAYSIFFETIVMTGFPQDQTYVQPLLEILSAKLESEVDYDIEHVMQILMYFALSMRDIPLFSKAIKVSTNDELGLDSKCIVKLGLANLFAKPIETLQIMENEGFTINFFTNWFNEKFYSVFAIKLQVLVILTLLKMPEVPNSVSPLLNNLTNKLVELTLSLPKAIRNRDAVTEGKSLEGDLTPEEEEEYFIECDDDMKETVLDQINVFQEVHTFFKNLQNEDAGKYEKIINYLDESKRDSLQVILEFVSQH 944 Q04537 Period circadian protein per 7274 No SL-0198 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}. UNIPROT Q04537 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}. GO:0005634 GO:0048471 GO:0048511 EGSGGSGSSGHFTTGSNVHMSSVTNTSNGGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTASGTATGTASGTATGTANGTGTGKGTDTHTAGSGSGSGTGTGTGTGTTTTTTTGNNSSSSTPPVTLTESLLNK 141 Q04561 Non-structural protein 12 rep 11049 Yes SL-0382 [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}. UNIPROT Q04561 Pfam PF16749 Pfam PF14757 Pfam PF14758 Pfam PF05410 Pfam PF05411 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF01443 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 [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}. GO:0030430 GO:0044165 GO:0033644 GO:0042025 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0004521 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0036459 GO:0008270 GO:0039520 GO:0039648 GO:0039579 GO:0039514 GO:0039545 GO:0039522 GO:0039644 GO:0039563 GO:0039502 GO:0006351 GO:0019082 GO:0039694 MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVDLADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRGIRAVVDPDGPIHVEALSCPQSWIRHLTLDDDVTPGFVRLTSLRIVPNTEPTTSRIFRFGAHKWYGAAGKRARAKRAAKSEKDSAPTPKVALPVPTCGITTYSPPTDGSCGWHVLAAIMNRMINGDFTSPLTQYNRPEDDWASDYDLVQAIQCLRLPATVVRNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIADFLANPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFIYAVERMLKDCPSSKQAMALLAKIKVPSSKAPSVSLDECFPTDVLADFEPASQERPQSSGAAVVLCSPDAKEFEEAAPEEVQESGHKAVHSALLAEGPNNEQVQVVAGEQLKLGGCGLAVGNAHEGALVSAGLINLVGGNLSPSDPMKENMLNSREDEPLDLSQPAPASTTTLVREQTPDNPGSDAGALPVTVREFVPTGPILCHVEHCGTESGDSSSPLDLSDAQTLDQPLNLSLAAWPVRATASDPGWVHGRREPVFVKPRNAFSDGDSALQFGELSESSSVIEFDRTKDAPVVDAPVDLTTSNEALSVVDPFEFAELKRPRFSAQALIDRGGPLADVHAKIKNRVYEQCLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVAQWDRKLSVTPPPKPVGPVLDQIVPPPTDIQQEDVTPSDGPPHAPDFPSRVSTGGSWKGLMLSGTRLAGSISQRLMTWVFEVFSHLPAFMLTLFSPRGSMAPGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVGSSCDHDSPECHAELLALEQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRYLWHVLLRLCMLADLALSLVYVVSQGRCHKCWGKCIRTAPAEVALNVFPFSRATRVSLVSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKMSAQTVVAVPYDPSQAIKCLKVLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRVVVDSDTFVAAVRCGYSTAQLVLGRGNFAKLNQTPPRNSISTKTTGGASYTLAVAQVSAWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPTYGPGVVCSSRLCVSADGVTLPLFSAVAQLSGREVGIFILVLVSLTALAHRMALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHPLTMLWVHSFLVFCLPAAGILSLGITGLLWAIGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRTLIFTPSAVGSLLEGAFRTHKPCLNTVNVVGSSLGSGGVFTIDGRRTVVTAAHVLNGDTARVTGDSYNRMHTFKTNGDYAWSHADDWQGVAPVVKVAKGYRGRAYWQTSTGVEPGIIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPEGETCTIKETKLSDLSRHFAGPSVPLGDIKLSPAIIPDVTSIPSDLASLLASVPVVEGGLSTVQLLCVFFLLWRMMGHAWTPIVAVGFFLLNEILPAVLVRAVFSFALFVLAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGTFAGRLSELSQALSTYCFLPRVLAMTSCVPTIIIGGLHTLGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMNNESLTAALACKLSQADLDFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQIDKMKGVLSKLEAFAETATPSLDIGDVIVLLGQHPHGSILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRSEEDDLKVERMKKHCVSLGFHNINGKVYCKIWDKSTGDTFYTDDSRYTQDHAFQDRSADYRDRDYEGVQTTPQQGFDPKSETPVGTVVIGGITYNRYLIKGKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLKRIISQLQGLTTEQALNCLLAASGLTRCGRGGLVVTETAVKIIKYHSRTFTLGPLDLKVTSEVEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGLDTIPGIQPGHGAGNMGVDGSIWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHKGRLINTRFGDLPYKTPQDTKSAIHAACCLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQKYDLSTQGFVLPGVLRLVRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTPCTLKKQYCSKPKTRTILGTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAIVRWFVANLLYELAGCEEYLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSALKMGHEIGLKFLEEQLKFEDLLEIQPMLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNRDRILAALAYHMKAQNASEYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKKFRHCGICDAKADYASACGLDLCLFHSHFHQHCPVTLSCGHHAGSKECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKVGNKTTALDPGRYQSRRGLVAVKRGIAGNEVDLSDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQVQDDDVIYTPTHQTMFDIVSALKVCRYSIPGASGLPFPPPARSGPWVRLIASGHVPGRVSYLDEAGYCNHLDILRLLSKTPLVCLGDLQQLHPVGFDSYCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTRPVAFGQVLTPYHKDRIGSAITIDSSQGATFDIVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLTPERTDCNLVFSRGDELVVLNADNAVTTVAKALETGPSRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPTFAPLPKELAPHWPVVTHQNNRAWPDRLVASMRPIDARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAEEEAAKELPHAFIGDVKGTTVGGCHHITSKYLPRSLPKDSVAVVGVSSPGRAAKAVCTLTDVYLPELRPYLQPETASKCWKLKLDFRDVRLMVWKGATAYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQNILTTAWFEDLGPQWKILGLQPFRRAFGFENTEDWAILARRMNDGKDYTDYNWNCVRERPHAIYGRARDHTYHFAPGTELQVELGKPRLPPGQVP 3855 Q04839 mRNA transport factor GFD1 GFD1 559292 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q04839 UNIPROT D6W081 PDB 3LCN Pfam PF17331 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}. P30822 EBI-20589,EBI-27549 P11484 EBI-27549,EBI-8627 P10591 EBI-27549,EBI-8591 Q12315 EBI-27549,EBI-7635 GO:0005737 GO:0031965 GO:0005643 GO:0044877 GO:0006406 MPLESIWADAPDEEPIKKQKPSHKRSNNNKKNNNSRWSNESSSNNKKKDSVNKVKNNKGNHESKTKNKIKETLPREKKPPHSQGKISPVSESLAINPFSQKATEISPPPVSPSKMKTTKTQSKQDTASKMKLLKKKIEEQREILQKTHHKNQQQQVLMDFLNDEGSSNWVDDDEEELILQRLKTSLKI 188 Q05166 Nucleoporin ASM4 ASM4 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. UNIPROT Q05166 UNIPROT D6VRR0 UNIPROT E9P903 UNIPROT Q12456 Pfam PF05172 PROSITE PS51472 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}. P14907 EBI-12265,EBI-3035 P32500 EBI-11950,EBI-3035 P34077 EBI-3035,EBI-12056 P46673 EBI-12345,EBI-3035 P47054 EBI-25846,EBI-3035 P49686 EBI-12310,EBI-3035 P52891 EBI-12337,EBI-3035 Q02199 EBI-12315,EBI-3035 Q02629 EBI-11698,EBI-3035 Q02630 EBI-11703,EBI-3035 Q03790 EBI-27321,EBI-3035 Self EBI-3035,EBI-3035 Q06142 EBI-9145,EBI-3035 P22696 EBI-6679,EBI-3035 Q04947 EBI-38020,EBI-3035 Q03718 EBI-3035,EBI-27756 Q06344 EBI-34121,EBI-3035 P38305 EBI-20939,EBI-3035 Q12315 EBI-7635,EBI-3035 GO:0031965 GO:0005643 GO:0044613 GO:0044615 GO:0005543 GO:0003697 GO:0017056 GO:0007049 GO:0051301 GO:0031990 GO:0006607 GO:0006999 GO:0006355 MFGIRSGNNNGGFTNLTSQAPQTTQMFQSQSQLQPQPQPQPQQQQQHLQFNGSSDASSLRFGNSLSNTVNANNYSSNIGNNSINNNNIKNGTNNISQHGQGNNPSWVNNPKKRFTPHTVIRRKTTKQNSSSDINQNDDSSSMNATMRNFSKQNQDSKHNERNKSAANNDINSLLSNFNDIPPSVTLQDWQREDEFGSIPSLTTQFVTDKYTAKKTNRSAYDSKNTPNVFDKDSYVRIANIEQNHLDNNYNTAETNNKVHETSSKSSSLSAIIVFGYPESISNELIEHFSHFGHIMEDFQVLRLGRGINPNTFRIFHNHDTGCDENDSTVNKSITLKGRNNESNNKKYPIFTGESWVKLTYNSPSSALRALQENGTIFRGSLIGCIPYSKNAVEQLAGCKIDNVDDIGEFNVSMYQNSSTSSTSNTPSPPNVIITDGTLLREDDNTPAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQNAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL 528 Q05655 Protein kinase C delta type catalytic subunit PRKCD 9606 Yes SL-0198 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}. UNIPROT Q05655 UNIPROT B0KZ81 UNIPROT B2R834 UNIPROT Q15144 UNIPROT Q86XJ6 PDB 1YRK PDB 2YUU Pfam PF00130 Pfam PF00069 Pfam PF00433 PROSITE PS51285 PROSITE PS50004 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 PROSITE PS00479 PROSITE PS50081 OMIM 176977 OMIM 615559 DisGeNET 5580 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}.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. P17677 EBI-1267511,EBI-704279 P11388 EBI-704279,EBI-539628 Q02880 EBI-704279,EBI-2307774 P78527-2 EBI-704279,EBI-7195896 P78527-1 EBI-704279,EBI-3952976 P04637 EBI-366083,EBI-704279 Q96A56 EBI-704279,EBI-9986117 P57078 EBI-4422308,EBI-704279 P41594 EBI-6595175,EBI-704279 P06241 EBI-704279,EBI-515315 P29353 EBI-78835,EBI-704279 P19878 EBI-704279,EBI-489611 Q9GZU8 EBI-704279,EBI-2371956 P51114-2 EBI-704279,EBI-11022345 A5PLN9-2 EBI-704279,EBI-10985648 Q13523 EBI-704279,EBI-395940 E7EVG6 EBI-704279,EBI-11134881 Q562R1 EBI-704279,EBI-1773495 P29401 EBI-704279,EBI-1050560 Q9BRD0 EBI-704279,EBI-2561235 O60231 EBI-704279,EBI-311446 Q9P013 EBI-704279,EBI-2371709 Q3L8U1-2 EBI-704279,EBI-10965785 P61513 EBI-704279,EBI-356793 Q8IV50 EBI-704279,EBI-11021255 O60814 EBI-704279,EBI-4409738 P52739 EBI-704279,EBI-2849346 Q8N5V2 EBI-718372,EBI-704279 Q9NYF8 EBI-437804,EBI-704279 P05771 EBI-704279,EBI-706216 Q04759 EBI-704279,EBI-374762 P24001-2 EBI-704279,EBI-8800907 P33993 EBI-355924,EBI-704279 Q9BXL7 EBI-7006141,EBI-704279 Q9UDY8 EBI-704279,EBI-1047372 Q9Y4K3 EBI-704279,EBI-359276 GO:0035578 GO:0005911 GO:0005737 GO:0005829 GO:0005783 GO:0070062 GO:0005576 GO:0016363 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0005524 GO:0004698 GO:0004699 GO:0008047 GO:0019899 GO:0043560 GO:0019900 GO:0046872 GO:0004715 GO:0004672 GO:0019901 GO:0004697 GO:0004674 GO:0032147 GO:0006915 GO:0042100 GO:0060326 GO:0007049 GO:1904385 GO:0070301 GO:0071447 GO:0090398 GO:0042742 GO:0038096 GO:0016572 GO:0016064 GO:0060333 GO:0032613 GO:0032615 GO:0035556 GO:0008631 GO:0030837 GO:0051490 GO:0034351 GO:0050728 GO:0046627 GO:0043407 GO:0050732 GO:0090331 GO:0032091 GO:0042119 GO:0043312 GO:0018105 GO:0018107 GO:0030168 GO:2001235 GO:2000304 GO:0032079 GO:2000753 GO:1900163 GO:0035307 GO:0042307 GO:2001022 GO:2000755 GO:0032930 GO:0006468 GO:0050821 GO:0032956 GO:0043488 GO:0010469 GO:0007165 GO:0002223 GO:0023021 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 676 Q05B45 Transmembrane protein 120A TMEM120A 9913 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q05B45 Pfam PF07851 Necessary for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}. GO:0016021 GO:0005637 GO:0045444 GO:0051291 GO:0051260 MHPPPPGPLGDCLRDWEELQQDFHGIQETHRLYRLKLEELTKLQNSCTSSITRQKKRLQELALVLRKCKPSLPSEAEEAARELENQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLGNFFTTLRVVHQKFHNQLHGSKKE 343 Q05B54 Transmembrane protein 134 TMEM134 9913 Yes SL-0198 Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6X4}. UNIPROT Q05B54 Pfam PF05915 DE Reference Proteome: Yes; GO:0016021 GO:0048471 MSASRPQFSIDDAFELSLEDTGPGLEPSGVARFGPLHFERRARFEVADEDKQSRLRYQNLENDEDGAQASPEPDGGVSSRDSGQTSIRSSQWSFSSISSSTQRSYNACCSWTQHPLIQKNHRVVLASFLLLLLGLVLILTGVGLEVAPSPGVSSAIFFVPGFLLLVPGVYHVIFIYCAVKGHRGFQFFYLPYFEK 195 Q06142 Importin subunit beta-1 KAP95 559292 Yes SL-0178 SL-0185 Cytoplasm {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. UNIPROT Q06142 UNIPROT D6VYY6 PDB 2BKU PDB 3EA5 PDB 3ND2 PDB 5OWU Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. P14907 EBI-9145,EBI-12265 P20676 EBI-9145,EBI-12392 P32499 EBI-9145,EBI-12401 P34160 EBI-745,EBI-9145 P39705 EBI-9145,EBI-20731 P40069 EBI-9166,EBI-9145 P40477 EBI-11747,EBI-9145 P48837 EBI-9145,EBI-12324 P49686 EBI-12310,EBI-9145 P49687 EBI-9145,EBI-11730 Q02199 EBI-9145,EBI-12315 Q02629 EBI-9145,EBI-11698 Q02630 EBI-9145,EBI-11703 Q02821 EBI-1797,EBI-9145 Q03790 EBI-9145,EBI-27321 Q05166 EBI-9145,EBI-3035 P32562 EBI-4440,EBI-9145 P53687 EBI-8705,EBI-9145 P22216 EBI-17843,EBI-9145 P36124 EBI-16993,EBI-9145 Q04116 EBI-2889005,EBI-9145 P11484 EBI-9145,EBI-8627 P40150 EBI-9145,EBI-8632 P10592 EBI-9145,EBI-8603 P39079 EBI-9145,EBI-19077 P33416 EBI-8680,EBI-9145 P32589 EBI-8648,EBI-9145 P15108 EBI-9145,EBI-8666 P32527 EBI-9145,EBI-29684 P39101 EBI-9145,EBI-3949 P10591 EBI-8591,EBI-9145 P32447 EBI-3003,EBI-9145 Q12495 EBI-3913,EBI-9145 Q12529 EBI-2887498,EBI-9145 P39723 EBI-20675,EBI-9145 P27692 EBI-17937,EBI-9145 P39004 EBI-8790,EBI-9145 P28496 EBI-26585,EBI-9145 Q04182 EBI-13072,EBI-9145 Q04673 EBI-18198,EBI-9145 Q12149 EBI-1782,EBI-9145 Q12476 EBI-31475,EBI-9145 Q02724 EBI-20050,EBI-9145 P13259 EBI-5254,EBI-9145 Q04779 EBI-28153,EBI-9145 P38703 EBI-10035,EBI-9145 P53833 EBI-13638,EBI-9145 Q00578 EBI-14683,EBI-9145 P38262 EBI-17136,EBI-9145 Q12504 EBI-30749,EBI-9145 P50111 EBI-29626,EBI-9145 P26755 EBI-14981,EBI-9145 P22336 EBI-14971,EBI-9145 Q08920 EBI-33556,EBI-9145 P32337 EBI-9159,EBI-9145 P38111 EBI-6668,EBI-9145 P14832 EBI-5463,EBI-9145 Q06218 EBI-5640,EBI-9145 P19414 EBI-2104,EBI-9145 P28003 EBI-20647,EBI-9145 P38219 EBI-9145,EBI-21409 P07259 EBI-9145,EBI-14372 P02557 EBI-9145,EBI-18986 P02994 EBI-9145,EBI-6314 P00359 EBI-9145,EBI-7218 P18888 EBI-9145,EBI-17550 P19358 EBI-9145,EBI-10795 P10659 EBI-9145,EBI-10789 P46654 EBI-9145,EBI-16037 P41940 EBI-9145,EBI-11191 P33892 EBI-9145,EBI-7442 P47077 EBI-25778,EBI-9145 P47026 EBI-25989,EBI-9145 P53911 EBI-28927,EBI-9145 GO:0005737 GO:0042564 GO:0005643 GO:0005634 GO:0097718 GO:0061676 GO:0061608 GO:0008139 GO:0044877 GO:0005087 GO:0051028 GO:0006607 GO:0051292 GO:0006656 GO:0006606 GO:0006612 GO:0046822 GO:0060188 MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRILAALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIAAIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNILIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEVQAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDIAYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQNCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLMNDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINLVEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSASISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMGLFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAVGFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPYLNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIFQFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLFSQATKDTARWAREQQKRQLSL 861 Q06148 Non-homologous end-joining protein 1 NEJ1 559292 Yes SL-0178 SL-0182 Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. UNIPROT Q06148 UNIPROT D6VYR3 UNIPROT Q0P6Z6 UNIPROT Q0P6Z7 UNIPROT Q0P707 Pfam PF09302 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}. P10592 EBI-34047,EBI-8603 P11484 EBI-34047,EBI-8627 P32589 EBI-8648,EBI-34047 P25294 EBI-34047,EBI-17244 P38316 EBI-34047,EBI-2692 GO:0005737 GO:0032807 GO:0016021 GO:0070419 GO:0031965 GO:0005634 GO:0045027 GO:0006303 GO:0045002 GO:0035825 MDSELKGQQLSDAEWCVKKINGEGNCLLLFLPMSSPTTIVMIVLVSLERLVPYVFKLSQTQLSQQCQSQGFTDSISLNLIKLKLMDILQAPQEINQIGLVDSNLVFSFDVSADITVSINSVPSHVTKDMFYMILQSLCMLLLKLVNLSTQYHYVQRDILNEKQKCLDFLLISLRDLDGGSKVISQWAPENSKNYESLQQCTDDDIIKKLLHKGKFQHQEFLADSLKTLLSLRNKFQDVSRFEESGELNKKERVRFPAVNHFYNDDFELQADPTNEARPNSRGKIKPKTDFKPKSRESSTSSQLRLENFSESEATPEKTKSSSSLVEEYPQKKRKFGKVRIKN 342 Q06502 Non-structural protein 12 rep 300015 No SL-0382 [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}. UNIPROT Q06502 UNIPROT Q06503 Pfam PF16749 Pfam PF12581 Pfam PF05410 Pfam PF05411 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF01443 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 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}. GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0070008 GO:0008270 GO:0006351 GO:0019082 GO:0039694 MQSGFDRCLCTPNARVFWERGQVYCTRCLAARPLLPLSQQHPRLGALGLFYRPASPLSWEAPVTYPTKECRPGGMCWLSSIYPIARMTSGNHNFQARLNFIASVVYRDGKLTSKHLEEDFEVYSRGCRWYPITGPVPGIALYANAVHVSDESFPGATHVLSNLPLPQQPLRKGLCPFADARANVWRYKGNTVFVSPQGYLWTTGSNDSVPEPWGEDRRLCEKIISSLPADHLVKINFSNYPFDYSFTGGDGAGFVVFPCKERDTKFSKCWEKIFEDHSGWMAACEEADLADRMGYRTPAGVAGPYLARRLQVRGLRAVVKPENNDYIVWALGVPESYIRHVSRAGEPVEEFFVKVGEFSIVSNCVVTPHPKFRFQTRKYYGYSPPGDGACGLHCISAMLNDIFGDSFTTRLGKCSRDSSEWLSDQDLYQLVMTANLPATIGHCPSAIYKLDCVNQHWTVTKRKGDRAVGRLAPDCLRGVCGECEMGIHIGADTDLSPIVELQLAQDVSPRPGALLWFLELHELCVVDDDFAHAIARAGEEYRRAMGIPRDDWVILAELMTENCRTRHQVLEKLQRGLQLQASSRPSSPASVSPASSVDLSAAGLLLSGTESDKEAVVAVNDGCYTVLGFDKNEATKSEQDLATDLFCDLVKPMETSTTKLESRKILEAAAKALESCKPKRKRSRKKKTRTPSPTCSVDAAVAEPTSVNSLGNQDTRETCASEKKAEKCPTPTPPPRPKRAALKNSNSGCVLKDIIWNQTGPGVKCLTIVEDVRAFLKGITPPGGVLSTRSRITKHIVDHFHSICEQTPELVLAHAEHQAKNLHELLASETAKLILGIGEDPLKKLVGSQRSLPRRLGFGAWLGGQQKTSGGCGEREFKDVGRKSGAERTPSKRDLGVSLGDQLSQDGARRLSSSTACEIKESVPPIIDSGGGLSQKFMAWLNHQVFVLSSHLLAVWSFIFGSRQVLGVFDYVYTLFCLCCVLLCFYLPAIGFMTLVGCVFGSPWRVRLSVFSVWLCVAVVVFQEVLPEPGAVCTSASAERAAALERYTSNGVHRPVNHLSVGLVGTVAGFVARSVGGPRRYWFYFLRLMVLLDLGLVFLAVALRGSCKKCFCKCVRTASHEVQLRVFPSTKVARTTLEAICDMYSAPRVDPIFIATGVRGCWTGSVSPHQVTEKPVSYSNLDDKKISNKTVVPPPTDPQQAVRCLKVLQCGGSIQDVSVPEVKKVTKVPFKAPFFPNVTIDPECYIVVDPVTYSAAMRGGYGVSHLIVGLGDFAEVNGLRFVSGGQIADFVCLGLYVLLNFLLSAWLSSPVSCGRGTNDPWCRNPFSYPVVGQGVMCNSHLCVAEDGLTSPMTLSYSLIDWALMVAIMATVAIFFAKISLLVDVVCVFCCLLMYAFPSLSIAAFGFPFVLCKVSLHPITLVWVQFFLLAVNVWAGVASVVVLISSWFLARATSSLGLITPYDVHMITATPRGASSLASAPEGTYLAAVRRSALTGRCCMFVPTNFGSVLEGSLRTRGCAKNVVSVFGSASGSGGVFTINGNPVVVTASHLLSDGKARVSCVGFSQCLDFKCAGDYAFARVANWKGDAPKAELSHRRGRAYCSPLVGLSLDLLGKNSAFCFTKCGDSGSPVVDEDGNLLGIHTGSNKRGSGMVTTHGGKTLGMANVKLSEMCPHYSGPGVPVSTVKLPKHLVVDVETVSSDLVAVVESLPALEGALSSMQLLCVFFFLWRLIHVPDVPVIRIAFFFLNEILPVMLARLMFSFALSLFFCVHWLFCSSVAVAFGDCCSKSVTGYSVQVLLLRLVIAALNRPCGPFGFSLLGQLSQCCLMLCLLDIELQLLGCLYLGQLLMWPPKEIFFHPTGQFMFLPLFLSLFKRNALADMLVGNGCFDAAFFLKYFAEGNLRDGVSDSCNMTPEGLTAALAITLSDDDLEFLQRHSEFKCFVSASNMRNGAKEFIESAYARALRAQLAATDKIKASKSILAKLESFAGGVVTQVEPGDVVVVLGKKVIGDLVEVVINDAKHVIRVIETRTMAGTQFSVGTICGDLENACEDPSGLVKTSKKQARRQKRTGLGTEVVGTVVIDGVSYNKVWHIATGDVTYEGCLVTENPQLRPLGMTTIGRFQEFIRKHGEKVKTSVEKYPVGKKKSVEFNITTYLLDGEEYDVPDHEPLEWTITIGESDLEAERLTVDQALRHMGHDSLLTAKEKEKLARIIESLNGLQQASALNCLATSGLDRCTRGGLTVSGDAVKLVRYHSRTFSIGDVNLKVMGREEYGRTVGKQGHCLVANLVDGVVVMRKHEPSLVDVLLTGEDADLISPTHGPGNTGVHGFTWDFEAPPTDLELELSEQIITACSIRRGDAPSLDLPYKLHPVRGNPYRDRGVLYNTRFGDIKYLTPQKTKEPLHAAACFNPKGVPVSDSETLVATTLPHGFELYVPTIPQSVLEYLDSRPMHRKCCVRAVVRGLAECDLQKFDLSRQGFVLPGVLYMVRRYLCRLVGIRRRLFLPSTYPAKNSMAGINGNRFPTHVVQSHPDIDALCERACKEHWQTVTPCTLKKQYCSKAKTRTILGTNNFVALGLRSALSGVTQGFMRKGIGSPICLGKNKFTPLPTKVSGRCLEADLASCDRSTPAIIRWFTTNLLFELAGPEEWIPSYVLNCCHDAVSTMSGCFDKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSAFRCGHKVGGLFLRDSLEMEQLFELQPLLVYSDDVVLYDESSELPNYHFFVDHLDLMLGFKTDRSKTVITSDPQFPGCRIAAGRVLVPQRDRILAALAYHMKASCVSDYFASAAAILMDACACCDYDEDWYFDLVCGIADCARKEGFRFPGPSFYVDMWKRLSVEEKKKCRTCAHCGAPSTLVSSCGLNLCDYHGHGHPHCPVVLPCGHAVGSGVCDGCSSPVMSLNTELDKLLACVPYHPPKVELLSVNDGVSSLPPGRYQARGGVVSVRRDILGNVVDLPDGDYQVMKVAQTCADICMVSINSHILRSQFITGAPGTGKTTYLLSVVRDDDVIYTPTHRTMLDVVKALGTCRFDPPKDTPLEFPVPSRTGPCVRLIRAGFIPGRVSYLDEAAYCNPLDVLKILSKTPLVCVGDLNQLPPVDFIGPCYAFALMLGRQLIEVFRFGPSIVNPIKKFYREELVSRGPDTGVKFLKSYQPYGQVLTPYHRDRVDGAITIDSSQGCTYDVITVYLPTPKSLNSARALVAITRARFYVFVYDPHNQLEQYLNMSEHEPAGAVAFWCGEQPMMISEGRVQRLSGPAQTTDPKLQQLMGLEGTASPLPQVAHNLGFYYSPDLVQFARIPSELCKHWPVVTAQNRTDWPDRLVCSMSKIDKCSRAIFCAGYHVGPSVFLGVPGVVSYYLTKFLKGKPVPLPDSLMSTGRIALNVREYLDEKEMEFSSRCPHAFIGEVKGSNVGGCHHVTSRYLPPVLVPGSVVKIGVSCPGKAAKELCTVTDVYLPELDPYLNPPTKSMDYKLLVDFQPVKLMVWKDATAYFHEGIRPMESMSRFLKVPQEEGVFFDLDEFVTNAKVSKLPCKYSVSANQFLTDVVLSMTHPSLAPPDYELLFARAYCVPGLDVGTLNAYIYRRGPSTYTTSNIARLVKDICCPVGCKGSGYMFPK 3637 Q06616 Nuclear envelope protein YPR174C YPR174C 559292 Yes SL-0178 SL-0182 Nucleus membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. UNIPROT Q06616 UNIPROT D6W4H5 Pfam PF08537 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}. P40069 EBI-36065,EBI-9166 P47069 EBI-36065,EBI-25811 P08456 EBI-14055,EBI-36065 P32562 EBI-36065,EBI-4440 P40578 EBI-10855,EBI-36065 Q03860 EBI-36065,EBI-37537 P53174 EBI-6200,EBI-36065 Q5SW96 EBI-36065,EBI-747813 Q8N6L0 EBI-749265,EBI-36065 Q969F0 EBI-36065,EBI-743099 P07259 EBI-36065,EBI-14372 Q12449 EBI-37072,EBI-36065 P28003 EBI-20647,EBI-36065 GO:0005737 GO:0005635 GO:0031965 GO:0034399 GO:0005816 MGIQEKTLGIRKERKLVVVPRERNHVRHASQRTRSKNYKNISKKRAQQHAFGFNIAKTLAKIQAFVWGSPADEEEESVVPLSKNSQDCVPLQWQAKFAQLRQQLHSTQKELQFVKEKCHLLQSVLDDANIDQRYLESRRDMKNIERDNLKPTENLPPSPVRAVNPLVTSSPIHMSPLQSRQRPVSSLQPPKGPNFYAKYPKLPQTNILRESPTEDSVPHAE 221 Q06787 Synaptic functional regulator FMR1 FMR1 9606 Yes SL-0198 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}. UNIPROT Q06787 UNIPROT A6NNH4 UNIPROT D3DWT0 UNIPROT D3DWT1 UNIPROT D3DWT2 UNIPROT G8JL90 UNIPROT Q16578 UNIPROT Q5PQZ6 UNIPROT Q99054 PDB 2BKD PDB 2FMR PDB 2LA5 PDB 2QND PDB 4OVA PDB 4QVZ PDB 4QW2 PDB 5DE5 PDB 5DE8 PDB 5DEA PDB 5UWJ PDB 5UWO Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 OMIM 300623 OMIM 300624 OMIM 309550 OMIM 311360 OMIM 616034 DisGeNET 2332 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}.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. P10909 EBI-1104674,EBI-366305 P63165 EBI-80140,EBI-366305 Self EBI-366305,EBI-366305 P63073 EBI-2000006,EBI-366305 Q5S007 EBI-5323863,EBI-366305 P09622 EBI-353366,EBI-366305 P36957 EBI-351007,EBI-366305 P08559 EBI-715747,EBI-366305 Q6ZNJ1 EBI-2862306,EBI-366305 Q12824 EBI-358419,EBI-366305 O75925 EBI-629434,EBI-366305 Q92538 EBI-359050,EBI-366305 P52179 EBI-5353249,EBI-366305 P12814 EBI-351710,EBI-366305 O15379 EBI-607682,EBI-366305 O14617 EBI-1051639,EBI-366305 O75928 EBI-348555,EBI-366305 O60229 EBI-949233,EBI-366305 Q8WV44 EBI-725997,EBI-366305 P54296 EBI-5357134,EBI-366305 Q9NYA4 EBI-1052346,EBI-366305 Q13023 EBI-1056102,EBI-366305 Q9NRD5 EBI-79165,EBI-366305 Q9UII2 EBI-718459,EBI-366305 O15066 EBI-3931791,EBI-366305 O75376 EBI-347233,EBI-366305 Q9Y4A8 EBI-10890629,EBI-366305 Q5JY77 EBI-2514717,EBI-366305 P50749 EBI-960081,EBI-366305 P43243 EBI-352602,EBI-366305 Q9UKI8 EBI-740492,EBI-366305 Q16181 EBI-2009373,EBI-366305 O43295 EBI-368166,EBI-366305 Q8N5U6 EBI-714023,EBI-366305 Q96IV0 EBI-6165879,EBI-366305 P10644 EBI-476431,EBI-366305 P05771 EBI-706216,EBI-366305 Q9Y5G2 EBI-21384271,EBI-366305 Q9UHQ4 EBI-2548400,EBI-366305 Q8NFW8 EBI-2816175,EBI-366305 Q9NQZ6 EBI-747993,EBI-366305 Q5T6F2 EBI-2514383,EBI-366305 Q2TAA8 EBI-6872498,EBI-366305 P17980 EBI-359720,EBI-366305 Q9NR46 EBI-749607,EBI-366305 Q9NRA8 EBI-301024,EBI-366305 Q6PEZ3 EBI-21384744,EBI-366305 O00231 EBI-357816,EBI-366305 Q8N2N9 EBI-2876112,EBI-366305 Q9P246 EBI-448891,EBI-366305 Q9Y2V7 EBI-3866319,EBI-366305 Q9NS37 EBI-632965,EBI-366305 P15622 EBI-739678,EBI-366305 Q9UNH7 EBI-949294,EBI-366305 Q53G59 EBI-740929,EBI-366305 Q15424 EBI-348298,EBI-366305 P62979 EBI-357375,EBI-366305 P62750 EBI-353254,EBI-366305 P35268 EBI-354533,EBI-366305 Q9C0C9 EBI-2339946,EBI-366305 Q9H2G4 EBI-947459,EBI-366305 P23246 EBI-355453,EBI-366305 Q96BJ3 EBI-4401674,EBI-366305 Q2KHR2 EBI-1222187,EBI-366305 Q86XZ4 EBI-6164306,EBI-366305 P28370 EBI-2822460,EBI-366305 P51532 EBI-302489,EBI-366305 Q14527 EBI-1045161,EBI-366305 P18583 EBI-1053513,EBI-366305 Q13813 EBI-351450,EBI-366305 P21579 EBI-524909,EBI-366305 P21675 EBI-491289,EBI-366305 Q14241 EBI-742350,EBI-366305 Q15906 EBI-399189,EBI-366305 P10600 EBI-1033020,EBI-366305 P10828 EBI-78558,EBI-366305 P05452 EBI-1047626,EBI-366305 P09936 EBI-714860,EBI-366305 P63279 EBI-80168,EBI-366305 Q15361 EBI-7239664,EBI-366305 O96028 EBI-2693298,EBI-366305 P52746 EBI-3444189,EBI-366305 Q99676 EBI-3907489,EBI-366305 P21506 EBI-1105324,EBI-366305 Q06732 EBI-474142,EBI-366305 Q06730 EBI-3951772,EBI-366305 Q13029 EBI-2686075,EBI-366305 Q86XK2 EBI-1047804,EBI-366305 Q6ZS17 EBI-2806927,EBI-366305 A6NKB5 EBI-21311109,EBI-366305 P51114 EBI-713291,EBI-366305 P45974 EBI-741277,EBI-366305 Q8IZ26 EBI-10264496,EBI-366305 Q9UQM7 EBI-1383687,EBI-366305 Q6PIJ6 EBI-2513135,EBI-366305 Q9H7E2 EBI-3938232,EBI-366305 Q9BZR9 EBI-2340370,EBI-366305 P51784 EBI-306876,EBI-366305 P04632 EBI-711828,EBI-366305 Q2LD37 EBI-2683809,EBI-366305 Q9BSF8 EBI-720180,EBI-366305 Q86W92 EBI-1045582,EBI-366305 Q5VT25 EBI-689171,EBI-366305 Q96JF6 EBI-723614,EBI-366305 Q5H9K5 EBI-2818620,EBI-366305 Q9BR77 EBI-7851256,EBI-366305 O95267 EBI-1054956,EBI-366305 Q9NP66 EBI-740641,EBI-366305 Q7L5Y9 EBI-10984762,EBI-366305 O60884 EBI-352957,EBI-366305 Q9Y6X2 EBI-2803703,EBI-366305 Q9BSL1 EBI-749370,EBI-366305 P40123 EBI-1051165,EBI-366305 Q99784 EBI-1105073,EBI-366305 Q9UQB8 EBI-525456,EBI-366305 Q14919 EBI-712941,EBI-366305 O00471 EBI-949824,EBI-366305 Q14314 EBI-21370828,EBI-366305 Q9UBU8 EBI-399246,EBI-366305 Q8N5Y2 EBI-2560796,EBI-366305 Q13438 EBI-725454,EBI-366305 O14647 EBI-1210503,EBI-366305 P61964 EBI-540834,EBI-366305 Q9UKN5 EBI-2803427,EBI-366305 Q9UNN5 EBI-718246,EBI-366305 Q9Y496 EBI-1104844,EBI-366305 Q96RF0 EBI-298169,EBI-366305 Q9C026 EBI-720828,EBI-366305 Q96CW1 EBI-297683,EBI-366305 Q96N64 EBI-6597774,EBI-366305 Q96PV6 EBI-739546,EBI-366305 Q96PY5 EBI-3438448,EBI-366305 Q00610 EBI-354967,EBI-366305 Q8N1A0 EBI-8473062,EBI-366305 Q12860 EBI-5564336,EBI-366305 Q14194 EBI-473101,EBI-366305 Q96L42 EBI-21372247,EBI-366305 Q8N3I7 EBI-2892592,EBI-366305 P29400 EBI-726908,EBI-366305 Q8WXF8 EBI-5278558,EBI-366305 Q8TF20 EBI-20859557,EBI-366305 Q6PEW1 EBI-748373,EBI-366305 Q1L5Z9 EBI-2510853,EBI-366305 Q12882 EBI-2839838,EBI-366305 Q14204 EBI-356015,EBI-366305 P29692 EBI-358607,EBI-366305 O43491 EBI-366305,EBI-1052044 Q9H4G0 EBI-465536,EBI-366305 O60293 EBI-746701,EBI-366305 P33121 EBI-2838799,EBI-366305 P42566 EBI-396684,EBI-366305 Q9Y483 EBI-725816,EBI-366305 Q70YC4 EBI-21374257,EBI-366305 Q9UPW8 EBI-311017,EBI-366305 Q9UPY8 EBI-726739,EBI-366305 Q96RU3 EBI-1111248,EBI-366305 Q9UBB6 EBI-1053490,EBI-366305 P21333 EBI-350432,EBI-366305 Q9Y2J2 EBI-310986,EBI-366305 O60333 EBI-465633,EBI-366305 Q9BT88 EBI-751770,EBI-366305 Q9Y5W8 EBI-3917449,EBI-366305 O95490 EBI-2865302,EBI-366305 Q9UJ04 EBI-308511,EBI-366305 Q9C040 EBI-749840,EBI-366305 O94874 EBI-1048088,EBI-366305 Q7Z460 EBI-913476,EBI-366305 Q96JC1 EBI-1050197,EBI-366305 O75044 EBI-1051034,EBI-366305 Q8N488 EBI-752324,EBI-366305 O75533 EBI-876542,EBI-366305 Q9UPN3 EBI-366305,EBI-522925 Q9ULA0 EBI-748356,EBI-366305 Q6PID6 EBI-2555404,EBI-366305 Q8NAP3 EBI-5235984,EBI-366305 Q8TF01 EBI-3437793,EBI-366305 Q96DZ5 EBI-12823145,EBI-366305 O43166 EBI-310678,EBI-366305 Q9Y4E5 EBI-747230,EBI-366305 Q9NUQ6 EBI-5280638,EBI-366305 Q9ULX6 EBI-357530,EBI-366305 Q96NJ3 EBI-18064466,EBI-366305 Q06210 EBI-1055540,EBI-366305 Q9UHB7 EBI-395282,EBI-366305 Q9ULD5 EBI-11975599,EBI-366305 Q9UMS4 EBI-395746,EBI-366305 P38159 EBI-743526,EBI-366305 Q86WH2 EBI-2845202,EBI-366305 Q9HBT6 EBI-21378130,EBI-366305 Q5JPE7 EBI-2680477,EBI-366305 Q8N660 EBI-2863570,EBI-366305 Q6NZI2 EBI-2559016,EBI-366305 P07305 EBI-725224,EBI-366305 Q9BWC9 EBI-711501,EBI-366305 Q00341 EBI-1049478,EBI-366305 P61978 EBI-304185,EBI-366305 P11021 EBI-354921,EBI-366305 Q5HYM0 EBI-21379449,EBI-366305 P78318 EBI-1055954,EBI-366305 Q13123 EBI-713456,EBI-366305 O14782 EBI-1104854,EBI-366305 A6QL64 EBI-21379797,EBI-366305 O60282 EBI-717170,EBI-366305 P33176 EBI-355878,EBI-366305 Q12840 EBI-713468,EBI-366305 A8MQT2 EBI-21380453,EBI-366305 Q15784 EBI-7399633,EBI-366305 Q14494 EBI-2804436,EBI-366305 Q9UQ80 EBI-924893,EBI-366305 P67809 EBI-354065,EBI-366305 Q16656 EBI-2547810,EBI-366305 Q6P4R8 EBI-2511210,EBI-366305 P05165 EBI-2211679,EBI-366305 Q15154 EBI-741421,EBI-366305 Q9UJX3 EBI-1384164,EBI-366305 O95071 EBI-358329,EBI-366305 Q9UBS4 EBI-713113,EBI-366305 Q7LFL8 EBI-3940093,EBI-366305 Q99719 EBI-373345,EBI-366305 Q9NZR2 EBI-1642131,EBI-366305 Q9H0C5 EBI-935503,EBI-366305 Q00169 EBI-1042490,EBI-366305 O43236 EBI-1047513,EBI-366305 P46100 EBI-396461,EBI-366305 Q5T0N5 EBI-714058,EBI-366305 Q6ZN54 EBI-2857145,EBI-366305 Q8WUP2 EBI-3864120,EBI-366305 Q8NDB2 EBI-2837677,EBI-366305 Q8TEP8 EBI-2339778,EBI-366305 Q8TC92 EBI-713221,EBI-366305 Q8NEU8 EBI-741261,EBI-366305 Q15172 EBI-641666,EBI-366305 Q9P0M6 EBI-3922608,EBI-366305 Q6VMQ6 EBI-928732,EBI-366305 Q3V6T2 EBI-2266839,EBI-366305 Q96S59 EBI-636085,EBI-366305 Q9UPY3 EBI-395506,EBI-366305 Q9NWT6 EBI-745632,EBI-366305 P38919 EBI-299104,EBI-366305 Q13131 EBI-1181405,EBI-366305 Q92731 EBI-78505,EBI-366305 P03372 EBI-78473,EBI-366305 Q9Y2D8 EBI-2212028,EBI-366305 P46013 EBI-876367,EBI-366305 Q13137 EBI-739580,EBI-366305 A7MCY6 EBI-359969,EBI-366305 Q9UHD2 EBI-356402,EBI-366305 P48059 EBI-306928,EBI-366305 Q6QDQ4 EBI-5276623,EBI-366305 Q13617 EBI-456179,EBI-366305 Q86VP6 EBI-456077,EBI-366305 Q13618 EBI-456129,EBI-366305 A0A384KBR0 EBI-366305,EBI-2851265 Q13428 EBI-396105,EBI-366305 P0DTD1 EBI-25492388,EBI-366305 P61326 EBI-299134,EBI-366305 Q9UJV9 EBI-1046350,EBI-366305 O95793 EBI-358174,EBI-366305 GO:0030424 GO:0043679 GO:0015030 GO:0030054 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0005829 GO:0030425 GO:1902737 GO:0043197 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0016020 GO:1990124 GO:0005845 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0035770 GO:0045202 GO:0019034 GO:0003682 GO:0070840 GO:0002151 GO:0042802 GO:0044325 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0043022 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0031369 GO:0045182 GO:0030371 GO:0006974 GO:0072711 GO:0034644 GO:0098586 GO:0031047 GO:0007215 GO:0044830 GO:0006397 GO:0051028 GO:2000766 GO:1900453 GO:1902373 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0060999 GO:0051491 GO:2000637 GO:0033129 GO:1901254 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 GO:0016032 MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP 632 Q06833 Nucleus-vacuole junction protein 2 NVJ2 559292 Yes SL-0178 SL-0182 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}. UNIPROT Q06833 UNIPROT D6W491 Pfam PF10296 Pfam PF00169 PROSITE PS51847 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}. P10591 EBI-8591,EBI-37290 P10592 EBI-37290,EBI-8603 P11484 EBI-8627,EBI-37290 P40150 EBI-8632,EBI-37290 P39743 EBI-37290,EBI-14500 P43603 EBI-37290,EBI-22980 Q02159 EBI-37290,EBI-19749 GO:0071944 GO:0005783 GO:0005789 GO:0016021 GO:0071561 GO:0008289 GO:0035621 MASLKVFLAVYLLGGITFLPLVLFTLYKIHLLYSNLKSASKKELDHDTADEIDEKTRLLARDIDPEFKARKLEEQLGVKVFNKGWITVTKQYYYHSSEVAVILKNSNNNKDSDTALQEQILQRTDLKKKQRFFAVLRHGNLFLYKDDSQNANLVHAISLQNRFITIWPRFDELGKEELPDASLFTKRTCIAIFKNDLVSIDSKNHNVILPHFDPLTSAESNNGDISTNDTTHEYQSQFHSSNQFFLYFDNNMDKEDWYYQLINASKNSNSLSTGLLDPNVSANAAHLKTKDMLQLIQDINSTENQLTTKWLNALLGRLFLSLQQTDTLNKFIHEKICKKLNKIKTPGFLDDLVVEKVDVGDSAPLFTSPELLELSPEGSTKIAIDVQYRGNLTIIIATKASINLGSRFKQREVSLQLSIKIKEFSGPLLFLIKPPPSNRIWYAFRTEPIMDFEIEPIVSSSKLSYNVVTNAIKSKFAEAVKESLVVPFMDDIVFYPTPNEVYRGGIWEEQDPEAAARARTAAAASDMNNTSAKEHLEALQEGGMKTQSRIKKALRPERKKENLKDLVDASGVATKTTTQTTVTTATNDDVSSSENSTKSRKYFKNSIKKIGRWYKDNVGNSSDTEDMDEIDVQDKKNDDSADERESDNPILTSNPKMISNRRPVPRRPSQPLNTLSPKLEGRKEKDTENFPVPPSASNMNASKMFANKENRKFSVSSNDSQNSLKNGDPHVKASKLESSQAFVKKTSQNRFNDGFFKQDLEFEEQREPKL 770 Q06BI3 Calcium-binding protein 8 Caln1 10116 Yes SL-0198 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}. UNIPROT Q06BI3 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 MPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME 219 Q07065 Cytoskeleton-associated protein 4 CKAP4 9606 Yes SL-0198 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. UNIPROT Q07065 UNIPROT Q504S5 UNIPROT Q53ES6 OMIM 618595 DisGeNET 10970 High-affinity epithelial cell surface receptor for APF. Mediates the anchoring of the endoplasmic reticulum to microtubules. A0A142I5B9 EBI-20625235,EBI-702400 O43542 EBI-2849976,EBI-702400 O76050 EBI-702400,EBI-2129917 P00519 EBI-375543,EBI-702400 P00533 EBI-297353,EBI-702400 Self EBI-702400,EBI-702400 P49407 EBI-743313,EBI-702400 P08559 EBI-715747,EBI-702400 Q9HBL7 EBI-714824,EBI-702400 P51151 EBI-4401353,EBI-702400 P31040 EBI-1057265,EBI-702400 P36957 EBI-351007,EBI-702400 P25100 EBI-489993,EBI-702400 Q9H1C4 EBI-4401271,EBI-702400 Q15077 EBI-10235794,EBI-702400 P63208 EBI-307486,EBI-702400 O75807 EBI-714746,EBI-702400 Q8IYT8 EBI-714340,EBI-702400 P40692 EBI-744248,EBI-702400 P60520 EBI-720116,EBI-702400 Q70EL3 EBI-2512953,EBI-702400 P01106 EBI-447544,EBI-702400 P36895 EBI-2551936,EBI-702400 Q9P0N5 EBI-721260,EBI-702400 Q2MV58 EBI-11333674,EBI-702400 Q5HYA8 EBI-11334880,EBI-702400 Q6NUS6 EBI-11278332,EBI-702400 Q9Y3E0 EBI-4402607,EBI-702400 Q96GX1 EBI-11349465,EBI-702400 Q96Q45 EBI-2602465,EBI-702400 Q86UK5 EBI-7260649,EBI-702400 Q86X19 EBI-11343485,EBI-702400 O75787 EBI-2512037,EBI-702400 P35278 EBI-2551532,EBI-702400 Q3UJU9 EBI-2554307,EBI-702400 Q9R0Q3 EBI-998894,EBI-702400 F8VQC7 EBI-11104531,EBI-702400 O60307 EBI-311420,EBI-702400 P51148 EBI-1054923,EBI-702400 P51149 EBI-1056089,EBI-702400 Q9D8B3 EBI-8322817,EBI-702400 Q16513 EBI-2511350,EBI-702400 Q5T3F8 EBI-2553509,EBI-702400 Q9P0L0 EBI-1059156,EBI-702400 Q15006 EBI-359031,EBI-702400 Q8N4V1 EBI-6163737,EBI-702400 P09450 EBI-5347760,EBI-702400 O00400 EBI-11135403,EBI-702400 Q96FW1 EBI-1058491,EBI-702400 O43493 EBI-1752146,EBI-702400 P11279 EBI-2805407,EBI-702400 Q9NS69 EBI-1047508,EBI-702400 P27824 EBI-355947,EBI-702400 Q96I36 EBI-6570698,EBI-702400 P13073 EBI-1056574,EBI-702400 O15155 EBI-749204,EBI-702400 Q99689 EBI-396435,EBI-702400 O95274 EBI-2561547,EBI-702400 Q9Y6Z7 EBI-21859492,EBI-702400 Q9BZR6 EBI-5240240,EBI-702400 Q5BJH7-3 EBI-11127237,EBI-702400 P50876 EBI-702400,EBI-2340657 O60858-3 EBI-21523829,EBI-702400 Q9NVF7 EBI-740282,EBI-702400 P08842 EBI-7183227,EBI-702400 P51888 EBI-2827057,EBI-702400 P04578 EBI-6163496,EBI-702400 Q13618 EBI-456129,EBI-702400 Q92905 EBI-594661,EBI-702400 P17568 EBI-1246238,EBI-702400 Q14764 EBI-2816254,EBI-702400 P18848 EBI-492498,EBI-702400 Q9Y3C0 EBI-712969,EBI-702400 P81172 EBI-702400,EBI-3942179 Q6I9Y2 EBI-716286,EBI-702400 Q9H1I8 EBI-702400,EBI-711197 P21675 EBI-702400,EBI-491289 P16403 EBI-358372,EBI-702400 Q6NUK1 EBI-702400,EBI-4289949 Q8IVJ8 EBI-702400,EBI-20844837 Q96NB3 EBI-702400,EBI-3920997 Q9UKU6 EBI-702400,EBI-2679650 Q8WXX0 EBI-702400,EBI-1046155 P04275 EBI-702400,EBI-981819 A6NNW6 EBI-702400,EBI-20833177 Q9ULG1 EBI-702400,EBI-769345 P29475 EBI-7164065,EBI-702400 Q640N3-2 EBI-25409036,EBI-702400 Q5FWK3 EBI-17170552,EBI-702400 Q6IQ23 EBI-2125301,EBI-702400 Q92633 EBI-3908414,EBI-702400 Q9H8X2 EBI-8786596,EBI-702400 Q16581 EBI-21515121,EBI-702400 Q6P5W5-2 EBI-21515953,EBI-702400 Q9UGM1 EBI-9008641,EBI-702400 Q13503 EBI-394678,EBI-702400 P30825 EBI-4289564,EBI-702400 A2A2Y4-2 EBI-21527498,EBI-702400 O75326 EBI-1753538,EBI-702400 Q8WWF3 EBI-17280858,EBI-702400 P49796-4 EBI-12006708,EBI-702400 Q86Y78 EBI-14035066,EBI-702400 O14763-2 EBI-21548444,EBI-702400 Q16322 EBI-12265328,EBI-702400 O94766 EBI-3917958,EBI-702400 Q99871-2 EBI-21525681,EBI-702400 Q7LGA3 EBI-5461291,EBI-702400 Q99598 EBI-742638,EBI-702400 GO:0035577 GO:0036464 GO:0005856 GO:0005829 GO:0005783 GO:0005788 GO:0005789 GO:0070062 GO:0016021 GO:0042599 GO:0005811 GO:0016020 GO:0016607 GO:0048471 GO:0005886 GO:0005791 GO:0035579 GO:0003723 GO:0044267 GO:0043312 GO:0043687 MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV 602 Q074N0 RNA-directed RNA polymerase NS5 POLG 407141 No SL-0382 [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}. UNIPROT Q074N0 Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0005525 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0075512 GO:0039654 GO:0039520 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MSGRKAQGKTLGVNMVRRGARSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKLTTHLKRLWRMLDPRQGLAVLRKVKRVVASLMIGLSSRKRRSNEMAMMPLLILSMVILAGGVTLVRKNRWLLLNVTAEDLGKTFSLGTGNCTTNILEAKYWCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGRCDAVGRSKRSRRAIDLPTHENHGLKTRQEKWMAGRMGERQLQKIERWLVRNPFFAITALAIAYLVGNNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQGKCVTVMAPDKPSLDISLQTVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENDGDNACKRTYSDRGWGNGCGLFGKGSIVACAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYIAEMEKDSWIVDRQWAQDLTLPWQSGSGGIWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDENDNNLYKLHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAVNKGILVTVNPIASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIHTVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAVNFGKRELKCGDGIFVFRDSDDWLTKYSYYPEDPVKLASIIKASHEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISVVVQDPKNIYQRGTHPFSRIRDGLQYGWKTWGKNLIFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGMGVFTTRVFMDAVFDYSVDCDGAILGAAVNGKKSAHGSPTFWMGSHEVNGTWMVHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKVQTNGPWMQVPLEVRREPCPGTSVVLDTGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTHESHLVRSWVTAGEVHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGIILLGAMLVGQVTVLDLVKLIVAVGLHFHEINNGGDAMYMALIASFSIRPGLLVGFGLRTLWSPRERLVMAFGAAMVEVALGGMMGGLWQYLNAVSLCVLTINAISSRKASNAVLPLMALLTPVTMHEVRMATMLFCTVVIVGVLHQNAKDTSMQKTIPIVALTLTSYMGLTQPFLGLCAYMSTQVFGRRSIPVNEALAAAGLVGVLAGLAFQDMENFLGPIAVGGILMMLVSVAGKVDGLELKKLGEVSWEEEAEISGSSSRYDVALSEQGEFKLLSEDKVPWDQIVMTSLALVGAAIHPFALLLVLGGWVLHIKGARRSGDVLWDIPTPKVIEECEYLEDGIYGIFQSTFLGASQRGVGVAQGGVFHTMWHVTRGAFLLRNGKKLVPSWASVKEDLVAYGGSWKLDGKWDGEEEVQLIAAVPGKAVVNVQTKPSVFKVRNGGEIGAVALDYPSGTSGSPIVNRSGEVVGLYGNGILVGDNSFVSAISQTEVKEESKEELQEIPTMLKKGMTTILDFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLEPTRAVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWTSGHEWILADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEKEYPTIKQKRPDFILATDIAEMGANLCVERVLDCRTAYKPVLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIEGTKTPVSPGEMRLRDDQRRVFRELVRGCDLPVWLSWQVAKPGLKTNDRKWCFEGPEEHEILNDNGETVKCRSPGGAKKALRPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVVLTELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTIVMLFILAGLLTSGMVIFFMSPKGMSRMSMAMGTMAGSGYLMFLGGVKPTHISYVMLIFFVLMVVIIPEPGQQRTIQDNQVAYLIIGILTLLSIVAANELGMLEKTKEDFFGRRNIATSGGTIPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGNLSLSGIAQSASVLSFMDKGIPFMKMNISVVILLVSGWNSITVIPLLCGVGGAMLHWTLILPGIKAQQSKLAQKRVFHGVAKNPVVDGNPTADIEEAPEMPALYEKKLALYLLLALSLMSVAMCRTPFSLAEGIVLSSAALGPLIEGNTSLLWNGPMAVSMTGVMRGNYYAFVGVMYNLWKMKTGRRGSASGKTLGEVWKRELNLLDKQQFELYKRTDITEVDRDMARRHLAEGKVDTGVAVSRGTAKLRWFHERGYVKLEGRVMDLGCGRGGWCYYAAAQKEVSGVKGYTLGRDGHEKPMNVQSLGWNIVTFKDKTDIHRLEPAKCETLLCDIGESSPSSVTEGERTLRVLETIEKWLACGVDNFCVKVLAPYMPDVIEKLELLQRRFGGTIIRNPLSRNSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEPDVILPIGTRSVETDKGPLDRDAIEERVERIKTEYAATWFYDNDNPYRTWHYCGSYITKTSGSAASMINGVIKILTFPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKIMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAVGAFLEEQEQWKTANEAVQDPKFWEMVDAERKLHQQGRCQSCVYNMMGKREKKLSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIKDLSTKEGGGFYADDTAGWDTRITEADLDDEQEIMSYMNAEQRKLAWAVMEMTYKNKVVKVLRPAPGGKAFMDIISRRDQRGSGQVVTYALNTITNLKVQLIRMAEAEMVINHQHVNECDEGVLARLDAWLAENGCDRLARMAVSGDDCVVRPVDDRFGLALSHLNAMSKVRKDISEWQPSKEWTDWENVPFCSHHFHELVLKDGRKVVVPCRDQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKRDMRLLSFAVSSAVPMAWVPSGRTTWSVHGKGEWMTTQDMLDVWNRVWVLNNPHMKDKTTVKEWRDVPYLTKRQDKLCGSLIGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI 3412 Q07912 Activated CDC42 kinase 1 TNK2 9606 Yes SL-0198 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. UNIPROT Q07912 UNIPROT Q6ZMQ0 UNIPROT Q8N6U7 UNIPROT Q96H59 PDB 1CF4 PDB 1U46 PDB 1U4D PDB 1U54 PDB 3EQP PDB 3EQR PDB 4EWH PDB 4HZR PDB 4HZS PDB 4ID7 PDB 5ZXB Pfam PF09027 Pfam PF11555 Pfam PF07714 Pfam PF14604 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50002 OMIM 606994 DisGeNET 10188 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}. O14976 EBI-714707,EBI-603457 P00533 EBI-297353,EBI-603457 Self EBI-603457,EBI-603457 Q12913 EBI-2264500,EBI-603457 Q05209 EBI-603457,EBI-2266035 P08575 EBI-1341,EBI-603457 P60953-1 EBI-3625591,EBI-603457 Q96JZ2 EBI-3919324,EBI-603457 Q8WXH5 EBI-603457,EBI-3942425 Q9HC98 EBI-603457,EBI-740364 P29972 EBI-745213,EBI-603457 O60880 EBI-6983382,EBI-603457 P07902 EBI-750827,EBI-603457 Q7Z3S9 EBI-945833,EBI-603457 P60953 EBI-81752,EBI-603457 P62993 EBI-603457,EBI-401755 P16333 EBI-389883,EBI-603457 G3X972 EBI-11079353,EBI-603457 Q9NYZ3 EBI-2511327,EBI-603457 Q00610 EBI-354967,EBI-603457 O95817 EBI-747185,EBI-603457 P08238 EBI-603457,EBI-352572 Q8IUQ4 EBI-603457,EBI-747107 P85968 EBI-603457,EBI-22237670 G3V7X3 EBI-603457,EBI-22085594 D4A3M8 EBI-603457,EBI-21231408 P97573 EBI-603457,EBI-8008869 O35244 EBI-603457,EBI-915490 Q7Z7F7 EBI-603457,EBI-7825445 P07900 EBI-603457,EBI-296047 Q58FF7 EBI-603457,EBI-9996483 P10809 EBI-603457,EBI-352528 P17987 EBI-603457,EBI-356553 P40227 EBI-603457,EBI-356687 P48643 EBI-603457,EBI-355710 P50991 EBI-603457,EBI-356876 P78371 EBI-603457,EBI-357407 Q16543 EBI-603457,EBI-295634 P05141 EBI-603457,EBI-355133 P49368 EBI-603457,EBI-356673 P49411 EBI-603457,EBI-359097 P50990 EBI-603457,EBI-356507 Q58FF8 EBI-603457,EBI-2961708 P60953-2 EBI-603457,EBI-287394 GO:0005912 GO:0005905 GO:0030136 GO:0097268 GO:0005737 GO:0030659 GO:0005768 GO:0031234 GO:0070436 GO:0016020 GO:0005634 GO:0048471 GO:0005886 GO:0005524 GO:0005154 GO:0005095 GO:0042802 GO:0046872 GO:0004715 GO:0004674 GO:0004712 GO:0004713 GO:0005102 GO:0031625 GO:0050699 GO:0030154 GO:0007166 GO:0006897 GO:0038083 GO:0016310 GO:0050731 GO:0042127 GO:2000369 GO:0007264 GO:0007169 MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR 1038 Q07937 Nanos homolog 1 nanos1 8355 No SL-0198 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. UNIPROT Q07937 Pfam PF05741 PROSITE PS51522 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}. GO:0005737 GO:0060293 GO:0048471 GO:0003723 GO:0030371 GO:0008270 GO:0007281 GO:0008354 MDGGLCFDSWSDYLGLSSLISRGLQPQREGERPRWDVLSPASAEPLPSNESVGHKGCGFCRSNREALSLYTSHRLRALDGRVLCPVLRGYTCPLCGANGDWAHTMRYCPLRRLLRDPQSNSNNPKLRH 128 Q08231 Nuclear mRNA export protein THP1 THP1 559292 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores. UNIPROT Q08231 UNIPROT D6W1Z5 PDB 3T5V PDB 4TRQ PDB 5G5P PDB 5L3T PDB 5UBP Pfam PF01399 PROSITE PS50250 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}. P46674 EBI-32097,EBI-16425 P10591 EBI-8591,EBI-32097 P33416 EBI-8680,EBI-32097 P11484 EBI-32097,EBI-8627 Q05931 EBI-32097,EBI-35227 P40150 EBI-8632,EBI-32097 P10592 EBI-32097,EBI-8603 P32589 EBI-32097,EBI-8648 Q6WNK7 EBI-1251050,EBI-32097 P21576 EBI-32097,EBI-20460 GO:0005635 GO:0005634 GO:0070390 GO:0003690 GO:0044877 GO:0003723 GO:0000282 GO:0031124 GO:0006406 GO:0071033 GO:0016973 GO:0000973 GO:0006368 GO:0006283 MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTRFKIMCTSFLNYARDVDPWSAWSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFIINLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPRGNASSTNIPGKQRILLYLVNKLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAFVQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWSVLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQNKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLINLGLLRANCFPQLQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW 455 Q08920 Nuclear cap-binding protein subunit 2 CBC2 559292 Yes SL-0198 Nucleus. Cytoplasm, perinuclear region. Note=Predominantly nuclear, is able to exit the nucleus in an RNA- dependent manner. UNIPROT Q08920 UNIPROT D6W3J0 PDB 6N7P Pfam PF00076 PROSITE PS50102 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}. P34160 EBI-33556,EBI-745 Q02821 EBI-33556,EBI-1797 Q06142 EBI-33556,EBI-9145 P53316 EBI-23586,EBI-33556 P39987 EBI-33556,EBI-22339 P0CS90 EBI-33556,EBI-8637 P10592 EBI-33556,EBI-8603 Q12329 EBI-33556,EBI-8571 P11484 EBI-33556,EBI-8627 P39078 EBI-33556,EBI-19054 P12612 EBI-33556,EBI-19045 P39076 EBI-33556,EBI-19049 P10591 EBI-33556,EBI-8591 P25303 EBI-16711,EBI-33556 P53207 EBI-736,EBI-33556 Q00539 EBI-11835,EBI-33556 P38996 EBI-11776,EBI-33556 P32605 EBI-680,EBI-33556 P39936 EBI-33556,EBI-9006 Q03782 EBI-33556,EBI-627 Q00916 EBI-33556,EBI-724 Q06217 EBI-33556,EBI-235 Q04693 EBI-33556,EBI-519 P33334 EBI-33556,EBI-465 P04147 EBI-33556,EBI-12823 P53617 EBI-33556,EBI-12228 Q01560 EBI-33556,EBI-12114 Q03735 EBI-33556,EBI-27955 Q07508 EBI-33556,EBI-673 P50094 EBI-33556,EBI-9195 P50095 EBI-33556,EBI-9190 Q12476 EBI-31475,EBI-33556 P32357 EBI-340,EBI-33556 P20448 EBI-5612,EBI-33556 P47130 EBI-763,EBI-33556 P40018 EBI-432,EBI-33556 Q03330 EBI-7458,EBI-33556 P38074 EBI-33556,EBI-8394 GO:0000243 GO:0005846 GO:0048471 GO:0000339 GO:0045292 GO:0000398 GO:0051028 GO:0000184 MSLEEFDEVKYDHSTKRLDTPSRYLLRKARRNPNGLQELRESMKSSTIYVGNLSFYTSEEQIYELFSKCGTIKRIIMGLDRFKFTPCGFCFIIYSCPDEALNALKYLSDTKLDEKTITIDLDPGFEDGRQFGRGKSGGQVSDELRFDFDASRGGFAIPFAERVGVPHSRFDNSSSQSNTNNYIPPPDAMGTFRPGFDEEREDDNYVPQ 208 Q08926 ULP1-interacting protein 4 UIP4 559292 Yes SL-0178 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}. UNIPROT Q08926 UNIPROT D6W3I3 DE Reference Proteome: Yes; Q07549 EBI-2044051,EBI-22078 GO:0005783 GO:0005789 GO:0005741 GO:0005635 MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDEHSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKERKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTDMSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS 304 Q08931 Pheromone-regulated membrane protein 3 PRM3 559292 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane; Single-pass membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. UNIPROT Q08931 UNIPROT D6W3H6 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}. P40857 EBI-36479,EBI-26003 P47088 EBI-36479,EBI-26307 P38074 EBI-36479,EBI-8394 GO:0005737 GO:0031316 GO:0016021 GO:0005635 GO:0034399 GO:0005816 GO:0000742 GO:0048288 MTAMKEDNAALITLKKNNDQEKLRVHKLTDASSNSADGFVINKAKNGGPLNKKSLVNNEQHIKKAVSPGRVRKHKTTTSSTKSRTKSKKKDASESKVQRENKGSFYQGAIFGSFLGAAVTTVLSNLAVKALQN 133 Q08955 Chromosome segregation in meiosis protein 4 CSM4 559292 Yes SL-0178 SL-0182 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}. UNIPROT Q08955 UNIPROT D6W3G9 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}. P47069 EBI-25811,EBI-31728 GO:0005623 GO:0005789 GO:0016021 GO:0000784 GO:0031965 GO:0045132 GO:0045141 GO:0010520 GO:0030435 GO:0007129 MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKEMIAFLESQLFCTTQNFVAQETHDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIYLSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV 156 Q08CK7 Insulin-like growth factor 2 mRNA-binding protein 1 igf2bp1 7955 Yes SL-0198 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}. UNIPROT Q08CK7 Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 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}. GO:0070937 GO:0030175 GO:0030426 GO:0030027 GO:0005634 GO:0048471 GO:0003730 GO:0051028 GO:0003407 GO:0006417 MNKLYIGNLNEKVTAEDLVKTFEDYKIPYSGQFLMKTGYASVDCPDDQWAMKAIETFSGKVELHGKRIEVEHSVPKKQRTRKLQIRNIPPHLQWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYGTREQARQAIQKLNGYQFDNNALRVSYIPDENSEVDSQRGPDNGRRPGYGPRGTSRQMSPGSGIPSKHQHADIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKPISIHSTPEGCSAACRMILEIMNQEAKDTKTADEVPLKVLAHNNFVGRLIGKEGRNLKKVEQDTDTKITISPLQDLTLYNPERTITVKGSIEACCLAEQEIMKKVREAYDNDIAAMNQQTHLIPGLNLGAIGLFPPSSAMPPPALGNSVPGPPYGPMGASEQETVHVYIPAQAVGALIGKKGQHIKQLSRFAGASIKIAPAEAPDSKMRMVIVTGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIKVAAAAAGRVIGKGGKTVNELQNLTAAEVVVPREQTPDEHDQVIVKIIGHFYASQLAQRKIRDILTQVKQQQKGGGMGTPQGPHPQGMTELGSPQGLAQEPRRK 598 Q08DM1 Dematin DMTN 9913 Yes SL-0198 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}. UNIPROT Q08DM1 Pfam PF16182 Pfam PF02209 PROSITE PS51089 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}. GO:0015629 GO:0005884 GO:0031253 GO:0031410 GO:0005829 GO:0012505 GO:0048471 GO:0005886 GO:0031095 GO:0014731 GO:0003779 GO:0051015 GO:0043621 GO:0005102 GO:0030507 GO:0030036 GO:0051017 GO:0051693 GO:0090527 GO:0035585 GO:0035584 GO:0071277 GO:0071320 GO:0048821 GO:0030032 GO:0010812 GO:0051895 GO:0033137 GO:0010801 GO:0050732 GO:0090315 GO:1900025 GO:0030194 GO:0010763 GO:2001046 GO:1901731 GO:1900026 GO:0090303 GO:0070560 GO:0065003 GO:0032956 GO:0008360 GO:0051489 GO:0010591 MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWAESRSPGTISQASAPRTAGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRAESTGGSPQSKHPIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHAGTSKSSSLPAYGRTTLSRLQSTDFSPSGSEAESPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNRGRTKLPPGVDRMRLERHLSAEDFSRVFSMSPEEFGKLALWKRNELKKKASLF 406 Q09349 Ubiquitin conjugation factor E4 ufd-2 ufd 6239 Yes SL-0178 SL-0182 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}. UNIPROT Q09349 UNIPROT Q6BEV4 UNIPROT Q95QB5 Pfam PF04564 Pfam PF10408 PROSITE PS51698 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}. P90879 EBI-2417964,EBI-317233 G5EEM6 EBI-317233,EBI-317215 GO:0005737 GO:0031965 GO:0005730 GO:0005634 GO:0000151 GO:0051087 GO:0031625 GO:0034450 GO:0008340 GO:0032436 GO:0051865 GO:0000209 GO:0016567 GO:0030433 MIEDEKAGLQPMDISDASVFFFQADVESKDFLTSLFDCEGKSDDRMLRYADAIIDVQNLNFDVSPQCLQSNIAEIITKFVLLSQDGSRRGLSRSFNFIDPDIIAGCREEDAIEFLLINFVRCHHELGKSGTSNCYKKTLESTRKAVFSVFVMIQRGYLESQLRSQHASLVFTKRLLEDTVSNVFLRTLVEYLASTDECDEDAITETFNPIFGILRSGIICQRFEDNKDEIVRQILRVMNLLLSIRLPSNGPRPLSNLLVNREDFLPTPSEKIQGREFGLMSFLGPFFSYGLESSARRPNHRVFVDCEEDARKYDGSVNTEQKLYFQRMDPIRTMLHQLMLPLASDQGSRNKTLRWIATIISTNDIRTRSHYDPSDVLCDHYMTNFLSVMYMFSEKIDLSKIIVDYPFLPSSLINISKETRLKMDESGAVAFASQFADRPDEYHFSTVCFFLTIAAQRLVIPPLMNQISEYSRHLKELKHKINALKEKLNTVSGFERAEVEKKLNYETEHWKLMSRHLLCVKTQAQDPALMASSMDFVDKQMKFILNLLCDNLDLLGDDSQLPTEVSQMFCALPEYFLEDALDFYIFAISNGMKLLMERNADWISRLTVLFTQYHYIKSPFLVSKLVRVLSSIQPPLWFNVVRLRMAQENLLMCMIKFYSDFEDNGDFYEKFNVRGNIQYMLEKMEEDMFYKGKFMDMARECGAEFIRFVNMVINDATWCIDESLSGLKSIHDVEKKMANKVEWDNTDQEIRNQDLGVYEEAKRKVKGWLGTAKSNLKLLLSITVNSPEPFRTPVLGERLAAMLNHNLSQLIGSKASELKVKDPRSYGWEPREFVSLLISIYLKLNMPAFVKYIAYDERTYSPEFFHNAIECMRKNSIVGFSQLESFEHLAEDVKKEYEAKAELEEEYDDVPEEFKDPIMDAIMVDPVKLPSGHVMDRAVIERHLLSTPNNPFNRAPLSHNELSPDSELKAKIQEWICQKRNSKK 984 Q09353 Sentrin-specific protease ulp 6239 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:25475837}. UNIPROT Q09353 UNIPROT Q8IU18 Pfam PF02902 PROSITE PS50600 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}. GO:0005635 GO:0005634 GO:0008234 GO:0009792 GO:1904333 GO:0016926 GO:0032880 MSRRSDLSDKDSQSRKRHWLTDQAVTNEEKEQSPTKRTRKTKSQGLGGLFNTFFGMFVSSNSGEKEKTEVSGEVQVQEDDEIIVEGTTRRVAENKKYMIFLNEDAPVRANAGSEENEVIIEKHVQKNVEIRNDEEKQEVQGDLVLTLSSSPKSPKNLEKSFEVQQDDEEPDVLFEKVVKTPNKQLQEARRFQNELIFLNDNPDTPDDVSVISDSRSKEFISPTPDDSVSRPITPSLSSLSNYTSNNVRDYWRRNSAKKPEVLRRVPVRHQFKHSTSVRKMNTIIDLKKIKNHLSSRDRLLQGVVASGQYEAKAISGIVEKKPKKMQRTSSTDILARAKNKIAELGGSRSNTPSLLSREPSIIIDSEESTSSSYRQHARSNSSESDSYRKLNDILSQINSLGIGSAYRGPQRYQNSYQLSKQKEDKLLEEARIREGHRSQTRGDRLEDVRKRLELQGIAIRPKVEKKKVDDFMALPDAADALVERAWSGGNPNEQFVDAFSIQICKKDLATLSGLHWLNDEIINFYLQLICDRSNGDSKYPKIYAFNTFFYSNIVSKGYASVKRWTRKVDIFAFDIVLVPVHLGMHWCMAVIDMGEKKIEFYDSLYDGNTAVLPALRGYLEAESLDKKKTAMNFSGWTIQQMTDIPRQQNGSDCGVFSCQFGEWASRRTTPRFTQKNMPYYRKRMVYEIVSKKLLATI 697 Q09601 Nucleoporin NUP35 npp 6239 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000269|PubMed:12937276}. UNIPROT Q09601 UNIPROT O62340 Pfam PF05172 PROSITE PS51472 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}. Q09601-1 EBI-6455756,EBI-2004755 Q9BKT9 EBI-2004755,EBI-2005827 Q95Y13 EBI-6456240,EBI-2004755 H2KYA1 EBI-11466183,EBI-2004755 GO:0005635 GO:0031965 GO:0005643 GO:0044613 GO:0044615 GO:0005543 GO:0003697 GO:0017056 GO:0007049 GO:0051301 GO:0009792 GO:0051028 GO:0006607 GO:0006999 GO:0006997 GO:0007096 GO:0006355 MFSHLNQNTSGRHNSMDLNNSSISNFGTPVEQSTPALLFGKRKATVPSSYTASPLNTASAPCSDIFAVSAPAVPQHLKDTPGSKSVHWSPSLVQSGEKSAAQTQNTPANLSFGGNSSFSAPTKPAPQSIQTSSFGGQAMHAPPLRSLRDKVEPAKKISRRNTFTARSTPLSTPITQRVTSRLAEAEEQPMEEEADAADTWVTVFGFQPSQVSILLNLFSRHGEVVSHQTPSKGNFIHMRYSCVTHAQQAISRNGTLLDQDTFIGVVQCTNKDVINGSASGIVARSSNIAAAANRSASMYNSFVENDMADQSVNHNENSVLNSSNVFDANNSLNSSRISVRSGVGMRPLAADQRTNILQGTPSVRKAPDGLLNKFWNTIGLN 381 Q09684 Nuclear fusion protein tht1 tht1 284812 Yes SL-0178 SL-0182 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}. UNIPROT Q09684 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:9442101}. GO:0005737 GO:0005789 GO:0005794 GO:0031301 GO:0031965 GO:0000742 GO:0048288 MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLLNTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEVNMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEILSTIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSVQSNIDFVNSGFQPLYDLTIQLKEELQSLKRLSSEQQNLQHEQILQWKSDFLNVSKDHLKVLQQLRPLIDIVEKFMNVYFKGLSNIISSFAFIGFTLFATLSSLFFKVLKIHRRPIIVFGSLSIIFIHIYCFKITSWVNLYGWITCTIARTLSFIKLNIRTFYLTAFLCALLNFLRYLKYRNSKKDTELSLFLPAPEECNIYHNEHIQVQEDNYLCPIENSLIDLFGSENNKEKLGKQENVRFAFLNSESLEQSPWWD 577 Q09747 ATP-dependent RNA helicase dbp5 dbp5 284812 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q09747 PDB 3FHO Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0005829 GO:0005635 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0003723 GO:0003724 GO:0002184 GO:0006406 GO:0016973 MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQSENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGTVMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEELSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRVGTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQRPITRVPTDDYEELEKVVKNALKM 503 Q09793 Nucleoporin nup45 nup45 284812 Yes SL-0178 SL-0185 Cytoplasm. Nucleus, nuclear pore complex. UNIPROT Q09793 Pfam PF13634 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}. GO:0005737 GO:0034399 GO:0005643 GO:0005634 GO:0008139 GO:0017056 GO:0051028 GO:0006913 GO:0015031 GO:0010389 MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPGLNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTTGGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNANTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISSRILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALSNRFAQVHDEVKRLQVNTSTSLPFIS 425 Q09825 Spindle pole body-associated protein sad1 sad1 284812 Yes SL-0178 SL-0182 Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Single-pass membrane protein. UNIPROT Q09825 UNIPROT Q9UU40 PDB 6A6W Pfam PF07738 PROSITE PS51469 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}. O13712 EBI-1542405,EBI-929731 Self EBI-929731,EBI-929731 Q92358 EBI-929731,EBI-929655 Q9US52 EBI-929731,EBI-929651 O13787 EBI-21242328,EBI-929731 Q10322 EBI-1125055,EBI-929731 P10815 EBI-929731,EBI-1187843 GO:0005623 GO:0005737 GO:0061497 GO:0005639 GO:0031021 GO:0034993 GO:0035974 GO:0005874 GO:0044732 GO:0071958 GO:0005635 GO:0071957 GO:0035861 GO:0043495 GO:0051301 GO:0072766 GO:0071790 GO:0032121 GO:0006998 MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSNIRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRKSQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKVGGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLSTGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEHVQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQVRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS 514 Q09877 Sad1-interacting factor 3 sif3 284812 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. UNIPROT Q09877 UNIPROT O94555 Pfam PF02582 DE Reference Proteome: Yes; GO:0016021 GO:0005759 GO:0031965 GO:0005634 GO:0140053 MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHAAAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVKHFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISEIFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAMSHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLPLYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR 472 Q09904 Nucleoporin nup124 nup124 284812 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:10409764}. UNIPROT Q09904 Pfam PF08604 Pfam PF10599 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}. GO:0005635 GO:0005643 GO:0044613 GO:0044615 GO:0008139 GO:0017056 GO:0051028 GO:0006606 GO:0000054 GO:0006405 MPPVSKNTRTSSKTVKKPYDPPQGSSRPFFTVLKRAFSSVLHPFTSGLDEKASGTASKDRKSGRAGTKSLLTPELTPHYLGKSPRIIRVSNRSHVRTIDGIEEKVHTNTFEPRKPKQKQDYTNSPTLFKRHDELSLKSLNSLHPSSALSKKLGSTSQHQIATPKSSASLLNILRSLHDEQKNTLNISSVKQDRITEANPTCEKRKPSRSPSPMLSKKKSVARASENEPSAKQNKSFSGNDSHKSLTDIRDKENGETEVSAKNHVPHRSSRRRRRHQRLIPIIYETLEQMDLRKPVLVNAEVQTDSNPGNTMFIDKQDIYHRLSTPTSRKRQTLEKGHIKAFSAVDEDLDEIFACEDDVHYTALPKQNPKSERILEPIIASPKDNTSDKGLLTKSAPTFEELQASITPKPVKTSPNDTALTLANAEDNKTFEHQPLSKDTEAPKSQFSSSPTKESTTRKSEVEPPSPSKEIKSSHFSVPEFKFEPKTEATTDKKLNVPKFEFKPTATADVQTNRLKENEPKPTFFAQLPSKTQETPSITENKPSFFSQLSPKREETEKKDNAPSAPASTSGFSFGGFAPKTLEEKEETKAPTFNFSLNNASSTQDTTKPTLQFNFGSSFGKPTSNIFNDKKTSENGLASSTVASESKPSAPESKPSSGFGNTAGSSPFSFNLTKESKEVPPTNSFSFAKKGKDEANDSLSAKASTPFSFAKPNTENVTTTAPQFSFNFTKPNTDAKTNLLPEKTFNEEAVKQKETEKEVPPTGPKASEIKDSVSSNNAVPSSTFNFVSPFAAVSEKTNENNIPNDTTKTNGNATKRTLEQTEDAKPFAFSFGSTTEQANKKASTSNETTKPQLDTSSKTDGVTANAPFSFASAFNAPKPSTNTADGKDSASNLTTPSPAFSFGNNSGVKASSNNNPSTNSSTAPFSFGTSNKPAFSFGSATSKTTSEGTAPAASASAPAPTTSAFSFGASNSSMNKEENTPMAKDAGDTAPASGFKSGFSFGANNSPQPASMFGTSTPAPSSAFAFGNQSGTNPAAPAGFGGITNTATNNPPSTGFTFTPSNAGSTAAPMFGAGNTPNPSGSINNASQAFAFGSGEPSNPASNPPSTGFSFGAATPSAFNASASQSPAPNGIQFNLGSSNSQTNAPPGRKIAVPRSRRKR 1159 Q0CHM0 Protein transport protein sec13 sec13 341663 Yes SL-0178 SL-0185 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}. UNIPROT Q0CHM0 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0030127 GO:0005789 GO:0000139 GO:0005643 GO:0005198 GO:0090114 GO:0051028 GO:1904263 GO:0015031 MAAAQVISNSGHEDMIHDAGLDYYGRRLATCSSDKTIKVFEIEGEAHRLVETLKGHEGAVWCVAWAHPKFGTILASSSYDGKVLIWREQHQNTTSPAAGSAWTKVFDFSLHTASVNMVSWAPHESGCLLGCASSDGHVSVLEFQDNSWTHQIFHAHGMGVNSISWAPAAAPGSLISANPGPGQQRRFVTGGSDNLLKIWDYNPETKTYNLSQTLEGHSDWVRDVAWSPSILSKSYIASASQDKTVRIWTSDASNPGQWTSQQLEFDSVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE 309 Q0GNC1 Inverted formin-2 Inf2 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q0GNC1 UNIPROT Q14C56 UNIPROT Q499F7 UNIPROT Q6P9T3 Pfam PF06367 Pfam PF06371 Pfam PF02181 Pfam PF02205 PROSITE PS51444 PROSITE PS51232 PROSITE PS51082 Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000269|PubMed:16818491}. P52927 EBI-912574,EBI-6908712 GO:0048471 GO:0003779 GO:0017048 GO:0030036 GO:0032535 GO:0090140 MSVKEGAQRKWAALKEKLGPQDSDPTEANLESAEPELCIRLLQMPSVVNYSGLRKRLESSDGGWMVQFLEQSGLDLLLEALARLSGRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHALTLDALDHYKMVCSQQYRFSVIMSELSDSDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRLRDLEDADLLIQLEAFEEAKAEDEEELQRISDGINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLLWEALENLVNRAVLLASDAQACTLEEVVERLLSIKGRPRPSPLDKAHKSVQTNSVQNQGSSSQNTTTPTTKVEGQQPVVASPCQHVGSIQSSSVDIAPQPVALEQCITALPLPTPPLSSSTPVLPPTPPPLPGPGATSPLPPPPPPLPPPLPGSGTTSPPPPPPPPPPLPPPLPGSGTISPPPPPPPPPLPGTGAVSPPPPPPLPSLPDSHKTQPPPPPPPPLPGMCPVPPPPPLPRAGQIPPPPPLPGFSVPSMMGGVEEIIVAQVDHSLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVARERNSMWATLGSPCTAAVEPDFSSIEQLFSFPTAKPKEPSAAPARKEPKEVTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMMLCEGTAIVLDMVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASANLKKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTEASGRVAPTDPPKATEPATASNPTQGTNHPASEPLDTTAADEPQGWDLVDAVTPSPQPSKEEDGPPALERRSSWYVDAIDFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPGVKSSHQDATDPEALWGVHQTEADSTSEGPEDEAQRGQSTHLPRTGPGEDEDGEDTAPESALDTSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEEFVPDSDDIKAKRLCVIQ 1273 Q0IHC4 Myelin-associated neurite-outgrowth inhibitor fam168b 8355 No SL-0198 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}. UNIPROT Q0IHC4 Pfam PF14944 Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQQELEHPAHVSSGVQMFMFGHAFSVARNGAIPSGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPFYAAPPHVIHHTTVVQPNGMPATMYPAPIQSPRGNGVAMGMVAGTTMAMSAGTLLTSHYPSPVAPQVTMPTYRPPGTPTYSYVPPQW 225 Q0IIE8 DnaJ homolog subfamily B member 14 DNAJB14 9913 Yes SL-0178 SL-0182 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}. UNIPROT Q0IIE8 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0030544 GO:0034622 GO:0071218 GO:0051085 GO:0030433 MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGGGDQSKPNCTKDSSSGSGESGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNQQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSNQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVIYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYHDERLRRKAEALSMDNCKELERLTSIYKGG 379 Q0IIG6 RISC-loading complex subunit TARBP2 TARBP2 9913 Yes SL-0198 Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034}. UNIPROT Q0IIG6 Pfam PF00035 PROSITE PS50137 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}. GO:0005737 GO:0016604 GO:0048471 GO:0016442 GO:0070578 GO:0003725 GO:0019899 GO:0035198 GO:0070883 GO:0042803 GO:0047485 GO:0035197 GO:0035280 GO:0035264 GO:0050689 GO:0061351 GO:0051149 GO:0045727 GO:0045070 GO:0031054 GO:0030422 GO:1903798 GO:0090065 GO:0046782 GO:0007338 GO:0035087 GO:0043403 GO:0007286 GO:0030423 MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDVPVFTAAAAATPVPSAVPTRSSPMEVQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEPEDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCSVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCHGSAATREAARGEAARRALQYLKIMAGSK 366 Q0P4G6 Solute carrier family 2, facilitated glucose transporter member 10 slc2a10 8364 Yes SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT Q0P4G6 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}. GO:0012505 GO:0005887 GO:0048471 GO:0005351 GO:0046323 MGLSSPTLILAATVSLLGGIVFGYELGIISGALLVLKTVYQLTCFEQEALVSAVLFGALLASLIGGIIIDRWGRRTAILASNLVVLAGSIILIATSTFWWLIVGRVTIGFAISISSMACCIYVSEIVRPHQRGMLVSLYETGITVGILISYAMNYFLSGVNESWKYMFGLAIVPAAFQFISILFLPSKPHKLNFWEQDTDDGFIELEETGEAGEFKPDTYDRQYTFLDLFRSKDNMRTRTLLGLGLVLFQQFTGQPNVLYYASTIFQSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAITGIGIVSFTVKMDSHRDCGSVTGRNMSSGESNVSQLLGIVHAETSTINTLDNSVHQLAMAIRSPSLANSASSNHKDLISQNSTVLPASPELPSNYTILNWITLLSMMAFVSAFSIGFGPMTWIVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLDVIASIGLSWTFLLYGVVGLLAIAFIYFFIPETKGQSLEEIDKQFSTKRILQKRETSKGVGKRPSSGPPYQRIGKASPS 555 Q0P5M9 Major facilitator superfamily domain-containing protein 10 MFSD10 9913 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D2V8}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q0P5M9 Pfam PF07690 PROSITE PS50850 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}. GO:0031526 GO:0016021 GO:0005637 GO:0022857 GO:0006915 MGCGAGGSCTPRPPIRQQQAPETRVVAVVFLGLLLDLLAFTLLLPLLPGLLESHGRAHDPLYGSWQRGVDWFAAAIGMPAEKRYNSVLFGGLIGSVFSLLQFLSAPLTGALSDCLGRRPGMLLSLAGVATSYAVWAASKSFAAFLASRVIGGISKGNVSLCTAIVADLGSPSARSKGMAVIGVAFSLGFTLGPTLGAFLPSETVPWLALLFAVSDLLFIWCFLPETLPPEKRAPSVTLGFRAAADLLSPLALLRFSAVARGPDPPTGVRLGSLRGLGLVYFLYLFLFSGLEFTLSFLVHQRFRFSRVEQGKMFFFIGLTMATIQGAYARRIRPGREIAAVKQAILLLIPASLFVGWGHTLPILGLGLLLYSWAAAVVVPCLSSVVAGYGSPGQKGTVMGTLRSLGALARAVGPVVAASAYWLAGARVCYTVCAALFLLPFSILRTLSPPARTLKAE 456 Q0VBZ8 Proline-rich protein 14 PRR14 9913 Yes SL-0178 SL-0180 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}. UNIPROT Q0VBZ8 UNIPROT Q58D02 Pfam PF15386 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}. GO:0005694 GO:0005652 GO:0005654 GO:0007517 MDLPGDSSTPGRQRLCRQPHAGALWGAKSPKRPKLQPLGAPSPLEKASRRVLAVVLEDVMAARMVPLEPQEESSTPRHHSNHRDSVRSQPPASPPRQAMWSPQARPPDPLHLCREPLSRIRRPPSTPRRQSRTTPGPDEGPSQKVDQVHQPTLVVMLQDIASSRPRAEGFADEAPNFIIPARRAEPKVMVHQPKPPSRDLPAPSRPSALSANPLASPPPAPDPVLEPPSTPPPSSLLRPRLSPWGLAPLFHSVRSKLESFADIFLTPNKAPRPPPPSPPMKLELKIAISEAGQPGASEGTVTVSPRPPIRQWRAQDQNPSATLTKPSLGRSHSCPDLGPPGPDPCSWPPVPAPSSRPRPRRHTVGGGEMAKAPPPPRPCLRKEVFPLGGVGASPPLVTSCSSTASTSSFSEPAEPRLSSTKRKEPRAPEDQVLPDSETKTIGKVSRFRIRRTPARSQINLTPMGLPRPVRLNKKEFSLEEIYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRTVEFRDSSLPRSRRPSRGARATAGRTLPPSLAPSPDVEPLLQQRLQELDASLLEEEEEGDQDQPHRT 587 Q0VCW8 Phosducin-like protein 3 PDCL3 9913 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}. UNIPROT Q0VCW8 Pfam PF02114 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}. GO:0005783 GO:0048471 GO:0001525 GO:0006915 MQDPNADTEWNDILRKKGILPSKEDLKDLEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEFNEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIKTSLEENPKKPVEDVLLSAVRCSVPAKRDSDSEDD 240 Q0VGK4 Lysophospholipase D GDPD1 Gdpd1 10116 Yes SL-0198 Membrane {ECO:0000250|UniProtKB:Q9CRY7}; Multi- pass membrane protein {ECO:0000250|UniProtKB:Q9CRY7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CRY7}. UNIPROT Q0VGK4 Pfam PF03009 PROSITE PS51704 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}. GO:0005789 GO:0016021 GO:0016020 GO:0048471 GO:0047391 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 GO:0006644 MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVSELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHIISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNNMSA 314 Q0WPU1 Myosin-15 XI 3702 Yes SL-0178 SL-0182 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}. UNIPROT Q0WPU1 UNIPROT Q9SMY9 Pfam PF01843 Pfam PF00612 Pfam PF00063 Pfam PF02736 PROSITE PS51126 PROSITE PS50096 PROSITE PS51456 PROSITE PS51844 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}. GO:0005737 GO:0016459 GO:0031965 GO:0051015 GO:0005524 GO:0005516 GO:0003774 GO:0007015 GO:0030048 GO:0007097 GO:2000769 MRNCLPMELNLRKGDKVWVEDKDLAWIAADVLDSFDNKLHVETSTGKKVFVSPEKLFRRDPDDEEHNGVDDMTKLTYLHEAGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSKLGLGNYQLGRTKVFLRAGQIGILDSRRAEVLDASARLIQRRLRTFVTHQNFISARASAISIQAYCRGCLSRNAYATRRNAAAAVLVQKHVRRWLSRCAFVKLVSAAIVLQSCIRADSTRLKFSHQKEHRAASLIQAHWRIHKFRSAFRHRQSSIIAIQCRWRQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARLATINECNKNAVLEKQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEEKLSHLENENQVLMQKTLITSPERIGQILGEKHSSAVVPAQNDRRSVFETPTPSKHIMPFSHSLSESRRSKLTAERNLENYELLSRCIKENLGFNDDKPLAACVIYKCLLHWRAFESESTAIFNIIIEGINEALKGGDENGVLPYWLSNASALLCLLQRNLRSNSFLNASAQRSGRAAYGVKSPFKLHGPDDGASHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPLLGSCIQAPKASRGIAGKSRSPGGVPQQSPSSQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNGEYVKSGISELEKWIANAKEEFAGTSWHELNYIRQAVGFLVIHQKKKKSLDEIRQDLCPVLTIRQIYRISTMYWDDKYGTQSVSSEVVSQMRVLVDKDNQKQTSNSFLLDDDMSIPFSAEDIDKAIPVLDPSEIEPPKFVSEYTCAQSLVKKPSIASTSKQII 1522 Q0WPZ7 Protein GLE1 GLE1 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q0WPZ7 UNIPROT Q9SAE5 Pfam PF07817 Required for seed viability. {ECO:0000269|PubMed:22898497}. GO:0005737 GO:0005635 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0006446 GO:0006449 GO:0048316 MGIVLEPPCPKSVDGISIDPEPNWNFESLVAEIASVEKKLNGFSMYPQPITNTTLRMGRRGGGFVMHVSEDEMESDEGEESDDEEEEEDHSQICTAGKRFACDELYLSDESDEEFDHEPEYMMNKLGLAESALYEVINDHQTEIKDDIRNQVSVVETEIMNEIETSLSAIARVEKYSETRKEVERKLDLQYQRKVAEALDTHLTAVQREHKIKSQIEERKIRSEEAQEEARRKERAHQEEKIRQEKARAEAQMLAKIRAEEEKKEVERKAAREVAEKEVADRKAAEQKLAEQKAVIESVTGSSATSNAQAGGNSIRAAESALILENHRLKKLEELETTNQSLKSRSNENFSSFEKHIGRVIRQISGTKDSVSGKINDIVKIFKDPRCPVSISIAAFAKKMVTTKEKPNPFACSYVIVYINSQFPQVMDILLAEFHKACIYTVPKHIVNSQSAWDSDAYERLDSIMRLYGALVQTDIRVGNATNVHGIEHGWAWLARFLNKIPANRATATALNSFLQTAGFGLHQRYKSQFLKVVNVVREHFLQKLRAKKDTSDLLVIIAEITAYLDDRMYLKEPEGRAMKTTSTLSSELTAELNQPNYNQNYQRNDYRNYY 611 Q0WSX8 TIR domain-containing protein TIK 3702 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q0WSX8 UNIPROT Q9FLA6 Pfam PF01582 PROSITE PS50104 Could play a role in nuclear morphology, specifically nuclear size. {ECO:0000269|PubMed:25217773}. GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0050135 GO:0061809 GO:0043621 GO:0007165 MDEQVQEPLSDQVFINFRGDELREIFVNHLELQLRNAGINVFIDTKEQKGRRLQYLFTRIKKSKIALAIFSKRYCESKWCLDELVTMNEQMKEKKLVVIPIFYNVRSDDVKRAANPDGEGNLDGEFSLPFKQLKQNHAGEPERVEGWERALRSVTKRIGFSRSNSKYKHDTDFVLDIVKEVKKQLNIPTDNSWSAIGVAFLAITINLIFSFFIAPKYLPDQKFFQTPEWFIGTLAVVLASWFWYKNNQNKAPPPS 255 Q10099 Nucleoporin seh1 seh1 284812 Yes SL-0178 SL-0185 Cytoplasm. Nucleus, nuclear pore complex. UNIPROT Q10099 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0005829 GO:0034399 GO:0005643 GO:0031080 GO:0005634 GO:0035859 GO:0005198 GO:0034629 GO:0051028 GO:1904263 GO:0015031 MDDISATTIQTNHQDLVNDVTYDFYGRRMVSCSADQRVKVYDFNDDTETWAITSEWRAGDASLMRVAWAHPSFGQVLAVCSLDRGVRIYEEQKKNFESKTWVEVAKLMDARSAVLDISFCPFQHGCKLAAVSADATLRIYEAMEPGNLTYWTLMNEIALMPSPPSRNEQPAFCVNWCPSRWREQYIAVGCMNDAYIYKQNSHGKWKKVAELPGHTDLIRDICWAPSMGSSYYLIATACKDGNVRIFKVETLCEEVFQEEEDAGNSMTEDSNFNLNSLKVELIGEYDNHKCQVWRCRFNVTGTILSSSGDDGCVRLWKASYANLFKCISVVSLEKKPEKL 339 Q10109 Lap-Emerin-Man domain protein 2 lem2 284812 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}. UNIPROT Q10109 PDB 5YCA Pfam PF12949 Pfam PF09402 Nucleus inner membrane protein involved in meiosis. {ECO:0000269|PubMed:20404563}. GO:0005623 GO:0061638 GO:0034506 GO:0034507 GO:0099115 GO:0005639 GO:0044732 GO:1904834 GO:0005635 GO:0031965 GO:0031618 GO:1902377 GO:0005724 GO:0097038 GO:1990578 GO:0003682 GO:0072766 GO:0030702 GO:1990141 GO:0000183 GO:0030466 GO:0099114 GO:0097240 GO:0070197 GO:0006998 GO:0071765 GO:0031937 GO:0097355 GO:0034398 MDNWEDPNFELRNLRVIDLKKILHESGVSFPVNARKIEYIRMVDRIRKNKLSSGPQHLLSHLQKEENSNTSKASSSEDEIAPKYLYPSSPSKSTKKPHNETEPLLSPQFIDKPSNIETPVKIESPHVSQNNTFQSYSELSPNVETSLTMKTPPAHASTPKFRSHKSHRVAVPMSFMDSSALHTSPAFSERLKLLSSSNNFSPQLRSPKISHRLQTSATSSPLQHKRPFTNVPERVSRDIEFAPLDSARPSESSSPYSEVDSAEEDDELFQNYVLQQTRKESKLWSFIKKVFHDIKYANYRLLHNLRAFPGISAISSSYLVHIFMILLGVVAAIFLALLREKMFTAGFCDSGASGSSASILGISFPSLCRTCPPNAICPSPNYVECKPGYVLYEPWYSSLGFWPSKYCVSDTSREESVNIFREECLSVLRSWNAILHCSNNSSDLLERNMSYNAHPYVADNLNISSDHISFPSKPFALGLLHDTLLERKSPTLGLEMFEDLFKASLAVLSETNEVVMDSKLICYDSWAGIPLRCRLKQQLIKFVWRNKVFLFGILALSGVIFKLINFFRTRSIVAKYLPSASRFCVESLKRQKANYQMSRSQEPVIPLIEMHDILFHGNGPLEQIHMTKATARTLWEAIVERVEQVGSVRTRESEVDGEWTRVWEWVGTNTLDFQTDRSFINTTSPLRE 688 Q10168 Nucleoporin nsp1 nsp1 284812 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q10168 Pfam PF05064 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}. GO:0005635 GO:0031965 GO:0034399 GO:0005643 GO:0044613 GO:0044615 GO:0005543 GO:0017056 GO:0000917 GO:0051028 GO:0006606 GO:0010389 GO:0000054 GO:0006405 MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNSTNASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTNTTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSNTTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFTKPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPSAKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRIDDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISEIVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF 598 Q10283 3-hydroxy-3-methylglutaryl-coenzyme A reductase hmg1 284812 Yes SL-0178 Endoplasmic reticulum membrane {ECO:0000269|PubMed:19486165}; Multi-pass membrane protein {ECO:0000269|PubMed:19486165}. Nucleus envelope {ECO:0000269|PubMed:19486165}. UNIPROT Q10283 UNIPROT O74425 Pfam PF00368 Pfam PF12349 PROSITE PS00066 PROSITE PS00318 PROSITE PS50065 PROSITE PS50156 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0042175 GO:0005778 GO:0050662 GO:0004420 GO:0042282 GO:0015936 GO:0006696 GO:0010142 GO:0019287 GO:0008299 GO:0016126 MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQIPAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDSSSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVLLSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRHFSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGNDSSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAISSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPEKKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDVTRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTMRGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRFCTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTVEDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPATDALKSVNSRVPGR 1053 Q10331 Nucleoporin nup107 nup107 284812 Yes SL-0178 SL-0182 SL-0185 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:15226438}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11309419, ECO:0000269|PubMed:15226438}. UNIPROT Q10331 UNIPROT O94351 Pfam PF04121 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}. Q9P797 EBI-295788,EBI-295769 Q9UTH0 EBI-295788,EBI-295780 GO:0005829 GO:0031965 GO:0034399 GO:0005643 GO:0031080 GO:0005634 GO:0017056 GO:0006406 GO:0016973 GO:0000973 GO:0006606 GO:0006355 GO:0006407 MACCCYSTILTHTRLDFKTMHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEKFNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAVLEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRLDERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTKNKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSNSSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSDSIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSVSPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDGEPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHPSTLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAGECSLSTPNGLFSL 813 Q10475 Eukaryotic translation initiation factor 4 gamma tif471 284812 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:12581158}. Note=Localized to the perinuclear region, the growing tips and septum. UNIPROT Q10475 UNIPROT P78832 Pfam PF12152 Pfam PF08017 Pfam PF02854 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}. Q9USV1 EBI-927233,EBI-2477564 Q9UUB7 EBI-926902,EBI-2477564 GO:0005737 GO:0010494 GO:0005829 GO:0016281 GO:0005634 GO:0048471 GO:0003729 GO:0005198 GO:0003743 GO:0002183 GO:0042273 MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNSSKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPVSTVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNTNTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHYQHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQYIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIVNPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEENAKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAPLASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQFITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRSGSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKPDPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRKENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKANLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVNIDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSSGRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALRREQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS 1403 Q12063 Dehydrodolichyl diphosphate synthase complex subunit NUS1 NUS1 559292 Yes SL-0178 SL-0182 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}. UNIPROT Q12063 UNIPROT D6VRG0 PDB 6JCN 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}. P15108 EBI-34546,EBI-8666 P32589 EBI-8648,EBI-34546 Q04432 EBI-35591,EBI-34546 P02829 EBI-34546,EBI-8659 GO:1904423 GO:0005783 GO:0005789 GO:0016021 GO:0005811 GO:0005635 GO:0031965 GO:0016765 GO:0019408 GO:0006486 MPTMIKKDDKAMEPPNEKPHRKIERDDVPESSNHIPPPESGVLKGGKVNSKTRALKAVTSIIADADENPQKKVNNETNGVQKQKTEDLSKRIGKFEYLFYKFLLVLLYICFGLFRYGQYQYNKMKLRIFSIIYNHAYTPQLIRQDVIPLKKIPKRLAAILEVKPVGDVGGGVTGLLNDASEIVCWTVSAGIKHLMLYDYDGILQRNVPELRMEIHSNLAKYFGPAHVPNYAVKIPHSNKIFYNLDGIETETDVGNEIEANQEKDKIAIEISLLSNRDGRETIVDLTKTMAELCAVNELSVSDITMDLVDSELKQLVGPEPDLLLYFGPSLDLQGFPPWHIRLTEFYWEKDNNEVIYSVFIRGLRQYAGCKVNVGK 375 Q12123 Inactive diphosphatase DCS2 DCS2 559292 Yes SL-0198 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. UNIPROT Q12123 UNIPROT D6W2M9 Pfam PF05652 PROSITE PS00892 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}. Q06151 EBI-38701,EBI-38973 Self EBI-38701,EBI-38701 P11484 EBI-8627,EBI-38701 P37366 EBI-4385,EBI-38701 Q06218 EBI-5640,EBI-38701 P40024 EBI-22498,EBI-38701 Q08004 EBI-35455,EBI-38701 P07245 EBI-3897,EBI-38701 P38829 EBI-38701,EBI-24704 GO:0005737 GO:0005634 GO:0000932 GO:0048471 GO:0004857 GO:0050072 GO:0046982 GO:0042803 GO:0000340 GO:0031670 GO:0009267 GO:0000290 GO:0000184 GO:0090342 GO:0009408 GO:0007584 GO:0006970 GO:0006979 MGSQDLASLIGRFKYVRVLDSNPHTKVISLLGSIDGKDAVLTAEKTHFIFDETVRRPSQSGRSTPIFFHREIDEYSFLNGITDLKELTSNDIYYWGLSVLKQHILHNPTAKVNLIWPASQFHIKGYDQQDLHVVRETPDMYRNIVVPFIQEMCTSERMKWVNNILYEGAEDDRVVYKEYSSRNKEDGFVILPDMKWDGINIDSLYLVAIVYRDDIKSLRDLNPNHRDWLIRLNKKIKTIIPQHYDYNVNPDELRVFIHYQPSYYHFHVHIVNIRHPGVGEERGSGMTILLEDVIEALGFLGPEGYMKKTLTYVIGENHDLWKKGFKEEVEKQLKHDGIATSPEKGSGFNTNLG 353 Q12144 Pore and endoplasmic reticulum protein of 33 kDa PER33 559292 Yes SL-0178 SL-0185 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex. UNIPROT Q12144 UNIPROT D6VY65 DE Reference Proteome: Yes; P10591 EBI-37691,EBI-8591 P11484 EBI-37691,EBI-8627 P10592 EBI-37691,EBI-8603 P25294 EBI-37691,EBI-17244 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0005643 GO:0071786 GO:0061024 GO:0051028 GO:0015031 MTVPRNRPMAPFGTIIKSRIKQPQFYWFIGHFLTIFNFIQFHLSITSKQNQLSCYRRSLFYISVTYAIVLYQFFKSDQLKFNFTLLRQEMKKLDNLQYFAMLFILFLLSQFNIIISGSLYSPVIFSIFHFLNYFKENLLPFLPLIPLNLKNLLNSKITVFIQNYNGFFLQMAQVFEIICGLRVGLFLVPFNFFLLLVRRANVSFEVVGTMLAGLTYVWFFKLRYLQSESMRQIFKQYVLRLDAYVSRTLPPYCSRLWNGYKNFVMTVFWKIPV 273 Q12164 Pore membrane protein of 33 kDa POM33 559292 Yes SL-0178 SL-0185 Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex. UNIPROT Q12164 UNIPROT D6VXY1 Pfam PF03661 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}. P10591 EBI-30000,EBI-8591 P11484 EBI-30000,EBI-8627 P10592 EBI-8603,EBI-30000 P32589 EBI-8648,EBI-30000 P32793 EBI-30000,EBI-24460 P43603 EBI-30000,EBI-22980 GO:0005783 GO:0005789 GO:0031309 GO:0005635 GO:0005643 GO:0071786 GO:0061024 GO:0051028 GO:0031081 GO:0006999 GO:0015031 MSSRPANNQGPPNLPARDKSLVQRFMAVAKSLQFAWFTGHSVVLISSILYLLKMSEFYYRSAYLGVIESFGIIIYQQFFTRNEPLQTQDAAATKASIKSRVAGLLKSEDVLYLVLANFWLFTPRFSFSLIPFFAFAVFHVLIYVEKVLLPKVFHLSSKDSSKILSFIDKFVVQYNDLCMHWVGTAELLIFILVLFRAILCFQRSWIILVVYAIFIKLRYENSKYMKAAFAQWRVRMDGIISHPSIPPFVKRAYNAIKMSLIRLSEYRLSGAPQVTKKQN 279 Q12315 Nucleoporin GLE1 GLE1 559292 Yes SL-0178 SL-0182 SL-0185 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. UNIPROT Q12315 UNIPROT D6VRE7 PDB 3PEU PDB 3PEV PDB 3RRM PDB 3RRN PDB 6B4E Pfam PF07817 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}. P14907 EBI-7635,EBI-12265 P20676 EBI-7635,EBI-12392 P32500 EBI-7635,EBI-11950 P34077 EBI-7635,EBI-12056 P35729 EBI-7635,EBI-11713 P36161 EBI-7635,EBI-11722 P38181 EBI-7635,EBI-11756 P39705 EBI-7635,EBI-20731 P40064 EBI-7635,EBI-11740 P40066 EBI-7635,EBI-22648 P40368 EBI-7635,EBI-12331 P40477 EBI-7635,EBI-11747 P46673 EBI-7635,EBI-12345 P47054 EBI-7635,EBI-25846 P48837 EBI-7635,EBI-12324 P49686 EBI-7635,EBI-12310 P49687 EBI-7635,EBI-11730 P52593 EBI-7635,EBI-11763 P52891 EBI-7635,EBI-12337 P53011 EBI-7635,EBI-16940 Q02199 EBI-7635,EBI-12315 Q02629 EBI-7635,EBI-11698 Q02630 EBI-7635,EBI-11703 Q03790 EBI-7635,EBI-27321 Q04839 EBI-27549,EBI-7635 Q05166 EBI-7635,EBI-3035 Self EBI-7635,EBI-7635 P12385 EBI-7635,EBI-6533 P05453 EBI-7635,EBI-6540 P06103 EBI-8973,EBI-7635 Q04067 EBI-8958,EBI-7635 P38074 EBI-7635,EBI-8394 Q02159 EBI-7635,EBI-19749 P38305 EBI-20939,EBI-7635 Q12445 EBI-7635,EBI-34287 GO:0005737 GO:0005739 GO:0031965 GO:0005643 GO:0044614 GO:0008047 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0006397 GO:0016973 GO:0006446 GO:0006449 GO:0006409 MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLIPINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQRKRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLGKAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGDSLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGWKRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAAAVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP 538 Q12445 Nucleoporin POM34 POM34 559292 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex. UNIPROT Q12445 UNIPROT D6VY20 UNIPROT E9P8U3 UNIPROT Q7LGY6 Pfam PF08058 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. Q12315 EBI-7635,EBI-34287 P11484 EBI-34287,EBI-8627 P38305 EBI-20939,EBI-34287 GO:0031309 GO:0034399 GO:0005643 GO:0070762 GO:0017056 GO:0051028 GO:0006999 GO:0006913 GO:0006606 GO:0030474 MKIQAGQLGLDDNDVPGPLPDTDSKPSSQSQNDTPMFKLGNFESPVLKELSRRTVNKEMETQRIMTNVIAFAFWNLLVKFIKFFWNNTHVGRQFCNRLSRIHLYMLTFHTLKKANIIYHTTFSWLNAELLDYLFHLLISLNILFSLWKLLSTVKVSDLNLTDRQKKLLGVDMQSSVDTGLQPQHPHYVSTSKISQMAQNKTHIPQTNLKNHPAYLFKGLETPLKARQREMAEEQTKLQSQSLHTKNVFGTLQRHSGISSTLVSANNDNNSPHTPVTRKGYIPSSKYAYMMNSQSPRGKI 299 Q12769 Nuclear pore complex protein Nup160 NUP160 9606 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. UNIPROT Q12769 UNIPROT B4DYE8 UNIPROT B4E2J9 UNIPROT Q08AD3 UNIPROT Q7Z5X6 UNIPROT Q96GB3 UNIPROT Q9H660 PDB 5A9Q OMIM 607614 OMIM 618178 DisGeNET 23279 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}.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. A0A142I5B9 EBI-20625235,EBI-295715 P02545 EBI-351935,EBI-295715 P49790 EBI-286779,EBI-295715 P55735 EBI-1046596,EBI-295715 P57740 EBI-295687,EBI-295715 Q5S007 EBI-5323863,EBI-295715 Q9NRI5 EBI-295715,EBI-529989 P62508 EBI-295715,EBI-2834260 Q7TSJ6 EBI-6305003,EBI-295715 Q8WYP5 EBI-396018,EBI-295715 Q9BW27 EBI-716392,EBI-295715 Q9P2Y5 EBI-2952704,EBI-295715 O94966 EBI-2511895,EBI-295715 O75317 EBI-2511507,EBI-295715 Q8BH74 EBI-2554056,EBI-295715 Q6PFD9 EBI-646104,EBI-295715 Q9ERU9 EBI-643756,EBI-295715 Q9BPU9 EBI-6958971,EBI-295715 Q8VE37 EBI-8006911,EBI-295715 P63280 EBI-80180,EBI-295715 Q80U93 EBI-2551193,EBI-295715 Q14974 EBI-286758,EBI-295715 Q96EE3 EBI-922818,EBI-295715 Q15388 EBI-711636,EBI-295715 P27824 EBI-355947,EBI-295715 Q14684 EBI-372051,EBI-295715 Q8NBZ7-2 EBI-21514721,EBI-295715 A8K8V0-2 EBI-21612038,EBI-295715 Q8NFH3 EBI-1059321,EBI-295715 P04049 EBI-365996,EBI-295715 Q13618 EBI-456129,EBI-295715 Q9Y5V3 EBI-295715,EBI-716006 P63000 EBI-413628,EBI-295715 Q6EMK4 EBI-10249550,EBI-295715 C5E526 EBI-12577179,EBI-295715 I6T1Z2 EBI-12561553,EBI-295715 P0C0U1 EBI-12579807,EBI-295715 P32970 EBI-18539709,EBI-295715 Q9H813 EBI-4319734,EBI-295715 Q8N7X8 EBI-18052611,EBI-295715 Q9Y3B2 EBI-295715,EBI-371892 Q8WUM0 EBI-295695,EBI-295715 GO:0005829 GO:0043657 GO:0005635 GO:0005643 GO:0031080 GO:0017056 GO:0075733 GO:0006406 GO:0072006 GO:0016925 GO:1900034 GO:0060964 GO:0006110 GO:0006409 GO:0016032 GO:0019083 MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYSESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQTVHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFVLKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLMVADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFALTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFCRGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLLKKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAEQILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGVHKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLSVLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRLQYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHDPSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL 1436 Q12840 Kinesin heavy chain isoform 5A KIF5A 9606 Yes SL-0198 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}. UNIPROT Q12840 UNIPROT A6H8M5 UNIPROT Q4LE26 PDB 4UXT PDB 4UXY PDB 4UY0 Pfam PF00225 PROSITE PS00411 PROSITE PS50067 OMIM 602821 OMIM 604187 OMIM 617235 OMIM 617921 DisGeNET 3798 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}.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}. P02545 EBI-351935,EBI-713468 Q06787 EBI-713468,EBI-366305 P31946-2 EBI-10770173,EBI-713468 P61981 EBI-359832,EBI-713468 Q9NV70 EBI-713468,EBI-1045313 Q8TDR0-2 EBI-713468,EBI-11946508 P61457 EBI-740475,EBI-713468 O95819 EBI-2511133,EBI-713468 Q9Y4G8 EBI-307079,EBI-713468 Q00987 EBI-389668,EBI-713468 P28702 EBI-748576,EBI-713468 P06213 EBI-10818032,EBI-713468 Q4G0F5 EBI-6151831,EBI-713468 Q04917 EBI-306940,EBI-713468 P63104 EBI-347088,EBI-713468 O60296 EBI-2851680,EBI-713468 P27348 EBI-359854,EBI-713468 Q96NW4 EBI-6125599,EBI-713468 Q8TDR0 EBI-928811,EBI-713468 Q9BYV6 EBI-713468,EBI-2341179 Q92731 EBI-78505,EBI-713468 Q96EV8-2 EBI-16749183,EBI-713468 Q1K9H5 EBI-6050669,EBI-713468 P03431 EBI-2547514,EBI-713468 Q9UGM1 EBI-9008641,EBI-713468 Q15654 EBI-742327,EBI-713468 P13497 EBI-489827,EBI-713468 Q07866-2 EBI-11979975,EBI-713468 P12524-2 EBI-18936665,EBI-713468 Q8N205-2 EBI-12099160,EBI-713468 Q9NV70-2 EBI-10961687,EBI-713468 Q9Y2V7 EBI-3866319,EBI-713468 Q15811 EBI-713468,EBI-602041 Q13625 EBI-713468,EBI-77642 GO:1904115 GO:0005623 GO:0035253 GO:0005829 GO:0032839 GO:0005871 GO:0016020 GO:0005874 GO:0043204 GO:0048471 GO:0045202 GO:0005524 GO:0008574 GO:0016887 GO:0019894 GO:0008017 GO:0003777 GO:0003774 GO:0099641 GO:0098971 GO:0019886 GO:0007411 GO:0007268 GO:0030705 GO:0007018 GO:1990049 GO:0006890 GO:0048489 GO:0016192 MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS 1032 Q12912 Processed lymphoid-restricted membrane protein LRMP 9606 Yes SL-0178 [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}. UNIPROT Q12912 UNIPROT A0AVM2 UNIPROT B4E077 UNIPROT Q8N301 Pfam PF05781 OMIM 602003 DisGeNET 4033 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. P62258 EBI-2839307,EBI-356498 Q9H4A3 EBI-457907,EBI-2839307 A0A0F7RGS7 EBI-2839307,EBI-2816751 A0A0F7RC41 EBI-2839328,EBI-2839307 A0A0F7R429 EBI-2839307,EBI-2814691 Q81JR3 EBI-2839354,EBI-2839307 Q9ULV4 EBI-351384,EBI-2839307 GO:0035577 GO:0005623 GO:0005694 GO:0005789 GO:0016021 GO:0005887 GO:0016020 GO:0005815 GO:0005635 GO:0005886 GO:0000922 GO:0043312 GO:0007338 GO:0006906 GO:0006903 MESTPFSGVANQIHTLCERPTYGEVKDGALDVKRQHKCPGPTSGPSPGTNLSGCIRMNDDPSMEENGVERVCPESLLQSREYSSLPLPRHTSSTDGTITSSDPGLEILNMASCDLDRNSLCKKEEDTRSASPTIEAQGTSPAHDNIAFQDSTSKDKTILNLEAKEEPETIEEHKKEHASGDSVVSPLPVTTVKSVNLRQSENTSANEKEVEAEFLRLSLGFKCDWFTLEKRVKLEERSRDLAEENLKKEITNCLKLLESLTPLCEDDNQAQEIIKKLEKSIKFLSQCAARVASRAEMLGAINQESRVSKAVEVMIQHVENLKRMYAKEHAELEELKQVLLQNERSFNPLEDDDDCQIKKRSASLNSKPSSLRRVTIASLPRNIGNAGMVAGMENNDRFSRRSSSWRILGSKQSEHRPSLPRFISTYSWADAEEEKCELKTKDDSEPSGEETVERTRKPSLSEKKNNPSKWDVSSVYDTIASWATNLKSSIRKANKALWLSIAFIVLFAALMSFLTGQLFQKSVDAAPTQQEDSWTSLEHILWPFTRLRHNGPPPV 555 Q13023 A-kinase anchor protein 6 AKAP6 9606 Yes SL-0178 SL-0182 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. UNIPROT Q13023 UNIPROT A7E242 UNIPROT A7E2D4 UNIPROT O15028 OMIM 604691 DisGeNET 9472 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. P00519 EBI-375543,EBI-1056102 P12931 EBI-621482,EBI-1056102 Q06787 EBI-1056102,EBI-366305 P06241 EBI-515315,EBI-1056102 P62993 EBI-1056102,EBI-401755 P16333 EBI-389883,EBI-1056102 P27986 EBI-79464,EBI-1056102 P46108 EBI-886,EBI-1056102 Q99459 EBI-1056102,EBI-374880 Q9NRI5 EBI-1056102,EBI-529989 Q8TDR0-2 EBI-1056102,EBI-11946508 Q96CV9 EBI-748974,EBI-1056102 A0A2B6C7C6 EBI-2816451,EBI-1056102 Q96EV8 EBI-465804,EBI-1056102 GO:0034704 GO:0005901 GO:0005623 GO:0005737 GO:0014704 GO:0014701 GO:0005635 GO:0031965 GO:0048471 GO:0016529 GO:0030315 GO:0008179 GO:0044325 GO:0060090 GO:0051018 GO:0034237 GO:0043495 GO:0001508 GO:0019933 GO:0071320 GO:0071345 GO:0070886 GO:0030307 GO:0061051 GO:1902261 GO:1901381 GO:0051281 GO:0060316 GO:0006605 GO:0060306 GO:0010738 GO:0010880 MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGLGDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPGLTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEETFKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISSSLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQRSWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDILSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDSINEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAPSSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNSGSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKVGDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQPDVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSINEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPSDTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENLGSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSDALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENEVAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACVEGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAENLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR 2319 Q13177 PAK-2p34 PAK2 9606 Yes SL-0198 [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. UNIPROT Q13177 UNIPROT Q13154 UNIPROT Q6ISC3 PDB 3PCS Pfam PF00786 Pfam PF00069 PROSITE PS50108 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 605022 DisGeNET 5062 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}. O60711 EBI-744222,EBI-1045887 Q03001 EBI-310758,EBI-1045887 Self EBI-1045887,EBI-1045887 P60953-1 EBI-3625591,EBI-1045887 Q9NRI5 EBI-1045887,EBI-529989 P14618-1 EBI-4304679,EBI-1045887 Q9BUB5 EBI-1045887,EBI-73837 P42574 EBI-524064,EBI-1045887 O60504 EBI-741237,EBI-1045887 P60953 EBI-1045887,EBI-81752 Q9H4E5 EBI-1045887,EBI-6285694 P15056 EBI-1045887,EBI-365980 Q09472 EBI-447295,EBI-1045887 P63000 EBI-1045887,EBI-413628 Q9WVM1 EBI-2552104,EBI-1045887 Q96NL6 EBI-2514016,EBI-1045887 Q3THE2 EBI-770040,EBI-1045887 Q9Y2X7-3 EBI-1045887,EBI-11070376 Q14161 EBI-1045887,EBI-1046878 P63208 EBI-1045887,EBI-307486 Q9NVF7 EBI-1045887,EBI-740282 Q14155-1 EBI-1045887,EBI-717540 Q14161-4 EBI-1045887,EBI-11070380 B7Z6G2 EBI-1045887,EBI-11070369 Q9Y2X7 EBI-1045887,EBI-466061 Q9NXV6 EBI-2559836,EBI-1045887 P02675 EBI-1034445,EBI-1045887 P48431 EBI-6124081,EBI-1045887 O60404 EBI-21879932,EBI-1045887 Q9H4E5-2 EBI-21868147,EBI-1045887 Q15052-2 EBI-21521235,EBI-1045887 P55210 EBI-1045887,EBI-523958 P42858 EBI-466029,EBI-1045887 Q13153 EBI-1307,EBI-1045887 O14730 EBI-1045887,EBI-1047061 P53667 EBI-1045887,EBI-444403 P04049 EBI-1045887,EBI-365996 P24666 EBI-717701,EBI-1045887 Q14697 EBI-348004,EBI-1045887 Q9UNM6 EBI-356070,EBI-1045887 Q13347 EBI-354047,EBI-1045887 P25787 EBI-603262,EBI-1045887 P62910 EBI-438408,EBI-1045887 P00505 EBI-720214,EBI-1045887 P62750 EBI-353254,EBI-1045887 P61224 EBI-358143,EBI-1045887 P27695 EBI-1048805,EBI-1045887 P07355 EBI-352622,EBI-1045887 P06730 EBI-73440,EBI-1045887 Q13263 EBI-78139,EBI-1045887 Q16630 EBI-358410,EBI-1045887 Q04637 EBI-73711,EBI-1045887 Q13526 EBI-714158,EBI-1045887 P27797 EBI-1049597,EBI-1045887 Q00005 EBI-1052159,EBI-1045887 P20290 EBI-1054687,EBI-1045887 P50395 EBI-1049143,EBI-1045887 Q99436 EBI-603319,EBI-1045887 P83731 EBI-353146,EBI-1045887 P22061 EBI-353343,EBI-1045887 P07237 EBI-395883,EBI-1045887 P25205 EBI-355153,EBI-1045887 P23526 EBI-1053240,EBI-1045887 P35580 EBI-351758,EBI-1045887 P30084 EBI-719602,EBI-1045887 P54819 EBI-1056291,EBI-1045887 Q9Y266 EBI-357298,EBI-1045887 P21266 EBI-350350,EBI-1045887 Q13404 EBI-1050671,EBI-1045887 Q15019 EBI-741220,EBI-1045887 O00264 EBI-1045534,EBI-1045887 P04179 EBI-716989,EBI-1045887 P25786 EBI-359352,EBI-1045887 O75534 EBI-719186,EBI-1045887 P30086 EBI-716384,EBI-1045887 P49023 EBI-702209,EBI-1045887 Q15052-1 EBI-25409944,EBI-1045887 Q14155-4 EBI-25410853,EBI-1045887 O43639 EBI-713635,EBI-1045887 Q9NYB9-2 EBI-11096309,EBI-1045887 P16333 EBI-389883,EBI-1045887 Q15052 EBI-1642523,EBI-1045887 Q8WVK2 EBI-2512550,EBI-1045887 P05362 EBI-1035358,EBI-1045887 Q9NYY3 EBI-721354,EBI-1045887 Q96K76 EBI-2514143,EBI-1045887 Q01968-2 EBI-11749425,EBI-1045887 Q92845 EBI-954040,EBI-1045887 Q9BTV5 EBI-722073,EBI-1045887 GO:0005911 GO:0005737 GO:0005829 GO:0098978 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0005524 GO:0045296 GO:0042802 GO:0004672 GO:0019901 GO:0004674 GO:0030296 GO:0048365 GO:0031267 GO:0032147 GO:0034333 GO:0006915 GO:0070830 GO:0071407 GO:0060996 GO:0038095 GO:0035722 GO:0043066 GO:2001271 GO:0006469 GO:0051497 GO:0018105 GO:0016310 GO:2001238 GO:0050731 GO:0046777 GO:0150105 GO:0006468 GO:0051493 GO:0050690 GO:0040008 GO:0007346 GO:0007165 GO:0023014 GO:0002223 GO:0031098 GO:0031295 GO:0050852 GO:0048010 MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR 524 Q13261 Soluble interleukin-15 receptor subunit alpha IL15RA 9606 Yes SL-0178 SL-0182 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}. UNIPROT Q13261 UNIPROT B4E2C2 UNIPROT Q3B769 UNIPROT Q5JVA1 UNIPROT Q5JVA2 UNIPROT Q5JVA4 UNIPROT Q6B0J2 UNIPROT Q7LDR4 UNIPROT Q7Z609 PDB 2ERS PDB 2Z3Q PDB 2Z3R PDB 4GS7 PROSITE PS50923 OMIM 601070 DisGeNET 3601 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}. O95999 EBI-958922,EBI-980354 P11802 EBI-295644,EBI-980354 P24941 EBI-980354,EBI-375096 P35243 EBI-954661,EBI-980354 O14936 EBI-1215506,EBI-980354 Q8N2W9 EBI-980354,EBI-473160 P40933 EBI-980354,EBI-980274 GO:0009986 GO:0030659 GO:0005789 GO:0005768 GO:0005615 GO:0000139 GO:0016021 GO:0031965 GO:0005886 GO:0004896 GO:0042010 GO:0019901 GO:0035723 GO:0050766 MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL 267 Q13330 Metastasis-associated protein MTA1 MTA1 9606 Yes SL-0178 [Isoform Short]: Cytoplasm. [Isoform Long]: Nucleus. Nucleus envelope. Cytoplasm. Cytoplasm, cytoskeleton. Note=Associated with microtubules. Localization at the nuclear envelope is TPR-dependent. UNIPROT Q13330 UNIPROT A5PLK4 UNIPROT Q86SW2 UNIPROT Q8NFI8 UNIPROT Q96GI8 PDB 4BKX PDB 4PBY PDB 4PBZ PDB 4PC0 PDB 5FXY PDB 5ICN PDB 6G16 Pfam PF01426 Pfam PF01448 Pfam PF00320 Pfam PF17226 Pfam PF00249 PROSITE PS51038 PROSITE PS51156 PROSITE PS51293 OMIM 603526 DisGeNET 9112 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}. P36957 EBI-351007,EBI-714236 Q12873 EBI-523590,EBI-714236 Q14839 EBI-372916,EBI-714236 P03372 EBI-78473,EBI-714236 Q13547 EBI-301834,EBI-714236 Q09028 EBI-620823,EBI-714236 Q16576 EBI-352227,EBI-714236 Q5S007 EBI-714236,EBI-5323863 Q92769 EBI-301821,EBI-714236 P43364-2 EBI-714236,EBI-10178634 P60410 EBI-714236,EBI-10171774 Q13422 EBI-714236,EBI-745305 Q5VWX1 EBI-714236,EBI-742808 Q6A162 EBI-10171697,EBI-714236 Q6FGM0 EBI-10173690,EBI-714236 P21673 EBI-714236,EBI-711613 Q7Z3S9 EBI-945833,EBI-714236 O00505 EBI-358297,EBI-714236 Q9BRK4 EBI-714236,EBI-741037 Q99497 EBI-1164361,EBI-714236 Q9BTC8 EBI-2461787,EBI-714236 O60341 EBI-710124,EBI-714236 Q96KQ7 EBI-744366,EBI-714236 Q92560 EBI-714236,EBI-1791447 P62805 EBI-714236,EBI-302023 Q86YP4 EBI-714236,EBI-726224 P11142 EBI-714236,EBI-351896 Q13620 EBI-714236,EBI-456067 P52732 EBI-714236,EBI-355697 O60315 EBI-714236,EBI-717614 P04004 EBI-714236,EBI-1036653 O14744 EBI-714236,EBI-351098 Q8WXI9 EBI-714236,EBI-923440 O95983 EBI-714236,EBI-1783068 O35207 EBI-11100491,EBI-714236 O14862 EBI-6253193,EBI-714236 O14519 EBI-1052532,EBI-714236 P04040 EBI-2432181,EBI-714236 Q08379 EBI-618309,EBI-714236 P68431 EBI-79722,EBI-714236 P0DPK4 EBI-714236,EBI-22310682 A8E1C4 EBI-6148716,EBI-714236 Q77M19 EBI-6149376,EBI-714236 Q9NVP1 EBI-714236,EBI-724378 O15530 EBI-717097,EBI-714236 P46734 EBI-602462,EBI-714236 O00629 EBI-396343,EBI-714236 Q15323 EBI-948001,EBI-714236 A8MQ03 EBI-3867333,EBI-714236 Q99961 EBI-697911,EBI-714236 Q9NRD5 EBI-79165,EBI-714236 Q58EX7 EBI-949255,EBI-714236 P26358 EBI-719459,EBI-714236 Q8IXH7 EBI-714236,EBI-536725 P32249 EBI-714236,EBI-715171 GO:0005737 GO:0005829 GO:0043231 GO:0005874 GO:0005635 GO:0005654 GO:0005634 GO:0016581 GO:0003682 GO:0042826 GO:0000978 GO:0001103 GO:0003713 GO:0003714 GO:0008270 GO:0032922 GO:0006302 GO:0043153 GO:0016575 GO:0045475 GO:0000122 GO:1902499 GO:0043161 GO:0040029 GO:0010212 GO:0007165 MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED 715 Q13459 Unconventional myosin-IXb MYO9B 9606 Yes SL-0198 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}. UNIPROT Q13459 UNIPROT O75314 UNIPROT Q9NUJ2 UNIPROT Q9UHN0 PDB 5C5S PDB 5HPY Pfam PF00612 Pfam PF00063 Pfam PF00788 Pfam PF00620 PROSITE PS50096 PROSITE PS51456 PROSITE PS50200 PROSITE PS50238 PROSITE PS00479 PROSITE PS50081 OMIM 602129 OMIM 609753 DisGeNET 4650 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}.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. Q5NID9 EBI-721429,EBI-2798201 P01106 EBI-447544,EBI-721429 Q15345 EBI-721429,EBI-721408 Q9Y3A3 EBI-721429,EBI-713935 Q15651 EBI-1758705,EBI-721429 P16401 EBI-5327611,EBI-721429 P16403 EBI-358372,EBI-721429 Q15293 EBI-948278,EBI-721429 Q15155 EBI-373107,EBI-721429 GO:0015629 GO:0005884 GO:0005938 GO:0005737 GO:0005829 GO:0016020 GO:0016459 GO:0048471 GO:0003779 GO:0043531 GO:0005524 GO:0016887 GO:0005516 GO:0005096 GO:0046872 GO:0000146 GO:0017048 GO:0048495 GO:0030048 GO:0035023 GO:0051056 GO:0007266 GO:0035385 MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGTKCYVLVEVKESGGEEWVLDANDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKYVHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEGNLLKNLKHRFLQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVSYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPEDYFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQIFAVLSAILYLGNVTYKKRATGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFNQHIFKLEQEEYQGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGAQSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKSKGIKQKQIIPKNLLDSKSLKLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKILLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQASWRGYWQRKLYRHQKQSIIRLQSLCRGHLQRKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGGQQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEAPSPEKTLPPQKTVAAESHEKVPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESREDETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRVSPPAPGSAPETPEDKSKPCGSPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVAAASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDVSKLLPSLAKAQPAAETTDGERSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENAVSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRESVFRQITNANELKYLDEFLLNKINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHVGYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFTRGYTKNDFEPVKQSKAQKKKRKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSHCSYTYGRKGEPGVEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLENFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNAPWPLKLGFSSPYEGVLNKSPKTRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKEDITYRLPELDPRGSDEENLDSETSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPTVAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHLPRWAPGAREAAAPVRRREPPARRPDQIHSVYITPGADLPVQGALEPLEEDGQPPGAKRRYSDPPTYCLPPASGQTNG 2157 Q13530 Serine incorporator 3 SERINC3 9606 Yes SL-0198 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}. UNIPROT Q13530 UNIPROT B4DUE9 UNIPROT O43717 UNIPROT Q9BR33 Pfam PF03348 OMIM 607165 DisGeNET 10955 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}. P62841 EBI-372635,EBI-1045571 A0A286YCX6 EBI-11119299,EBI-1045571 O95393 EBI-3922513,EBI-1045571 P53985 EBI-1054708,EBI-1045571 P45880 EBI-354022,EBI-1045571 Q9HAV4 EBI-517949,EBI-1045571 Q9P035 EBI-359013,EBI-1045571 Q9Y277 EBI-354196,EBI-1045571 P33947 EBI-1056498,EBI-1045571 O15260 EBI-1045571,EBI-1044848 P24390 EBI-1043076,EBI-1045571 Q99623 EBI-358348,EBI-1045571 Q13263 EBI-78139,EBI-1045571 GO:0000139 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0051607 GO:0009597 GO:0045087 GO:0006564 GO:0006658 GO:1902237 GO:0006665 GO:0016032 MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS 473 Q13625 Apoptosis-stimulating of p53 protein 2 TP53BP2 9606 Yes SL-0198 Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42. UNIPROT Q13625 UNIPROT B4DG66 UNIPROT Q12892 UNIPROT Q86X75 UNIPROT Q96KQ3 PDB 1YCS PDB 2UWQ PDB 4A63 PDB 4IRV PDB 6GHM PDB 6HKP Pfam PF12796 Pfam PF00018 PROSITE PS50297 PROSITE PS50088 PROSITE PS50002 OMIM 602143 DisGeNET 7159 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}. P49790 EBI-77642,EBI-286779 P61970 EBI-77642,EBI-591778 P62826 EBI-77642,EBI-286642 Q12840 EBI-713468,EBI-77642 O15265 EBI-77642,EBI-708350 P46108 EBI-886,EBI-77642 Q04917 EBI-306940,EBI-77642 P61981 EBI-359832,EBI-77642 Q05086-2 EBI-10175863,EBI-77642 P04637 EBI-366083,EBI-77642 Q6NSK7 EBI-77642,EBI-21369851 P31946 EBI-359815,EBI-77642 Q9Y2J4 EBI-746752,EBI-77642 P46937 EBI-1044059,EBI-77642 Q7TSJ6 EBI-6305003,EBI-77642 Q4VCS5 EBI-2511319,EBI-77642 P29991 EBI-77642,EBI-8826488 Q14457 EBI-949378,EBI-77642 Q9BYG5 EBI-295391,EBI-77642 Q9Y2D8 EBI-2212028,EBI-77642 Q9Y2I6 EBI-719716,EBI-77642 O60308 EBI-2685240,EBI-77642 O75665 EBI-716327,EBI-77642 O94986 EBI-311012,EBI-77642 Q15154 EBI-741421,EBI-77642 Q5BJF6 EBI-8744243,EBI-77642 Q5JU00 EBI-11335160,EBI-77642 Q5TB80 EBI-1059012,EBI-77642 Q66GS9 EBI-1046993,EBI-77642 Q68CZ1 EBI-5235485,EBI-77642 Q8N4C6 EBI-1164022,EBI-77642 Q8TES7 EBI-2350063,EBI-77642 Q96KN7 EBI-1050213,EBI-77642 Q96NL6 EBI-2514016,EBI-77642 Q96ST8 EBI-2799206,EBI-77642 Q6ZU80 EBI-2873150,EBI-77642 Q7Z7A1 EBI-2563266,EBI-77642 P63104 EBI-347088,EBI-77642 Q9NPB6 EBI-81876,EBI-77642 Q9JK83 EBI-81861,EBI-77642 P46938 EBI-1211949,EBI-77642 Q8NHQ8 EBI-306805,EBI-77642 Q96NE9-2 EBI-13213391,EBI-77642 Q15435 EBI-77642,EBI-1024281 P36873-1 EBI-77642,EBI-356289 P36873-2 EBI-3964623,EBI-77642 P62136 EBI-357253,EBI-77642 P36873 EBI-77642,EBI-356283 Q8IUQ4 EBI-77642,EBI-747107 Q81ZG1 EBI-2815760,EBI-77642 Q9BYC9 EBI-714361,EBI-77642 Q13107 EBI-723290,EBI-77642 Q9NU19 EBI-8787464,EBI-77642 P04637-1 EBI-3895849,EBI-77642 Q53HC0 EBI-719994,EBI-77642 P16403 EBI-358372,EBI-77642 Q15149 EBI-297903,EBI-77642 Q8TEW0 EBI-77642,EBI-81968 A6NKD9 EBI-77642,EBI-2561671 P41236 EBI-77642,EBI-1056517 O75901 EBI-77642,EBI-6871931 Q9H3G5 EBI-77642,EBI-357542 P34932 EBI-77642,EBI-356933 P62140 EBI-77642,EBI-352350 Q92598 EBI-77642,EBI-356829 Q02833 EBI-77642,EBI-929013 Q15834 EBI-77642,EBI-739674 P04083 EBI-77642,EBI-354007 A6NK89 EBI-6912267,EBI-77642 Q8N137 EBI-947360,EBI-77642 Q8N960 EBI-2563015,EBI-77642 Q8IW35 EBI-1566210,EBI-77642 Q9C0F1 EBI-744115,EBI-77642 Q9HC77 EBI-946194,EBI-77642 P68104 EBI-352162,EBI-77642 P21246 EBI-473725,EBI-77642 Q9BVJ6 EBI-473284,EBI-77642 Q13432 EBI-711260,EBI-77642 P05067 EBI-77613,EBI-77642 GO:0030054 GO:0005737 GO:0005829 GO:0005739 GO:0005654 GO:0005634 GO:0048471 GO:0042802 GO:0051059 GO:0002039 GO:0017124 GO:0005070 GO:0007049 GO:0072332 GO:0045786 GO:1900119 GO:1901216 GO:1900740 GO:0042981 GO:1901796 GO:0007165 MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLKQQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQTKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQSSEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIPSVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPHFSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEVVSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPEGPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA 1128 Q13875 Myelin-associated oligodendrocyte basic protein MOBP 9606 Yes SL-0198 Cytoplasm, perinuclear region. Note=Present in the major dense line of CNS myelin. {ECO:0000250}. UNIPROT Q13875 UNIPROT A8K2C2 UNIPROT G5E945 UNIPROT Q13874 UNIPROT Q6DHZ6 UNIPROT Q8TBJ1 Pfam PF02318 OMIM 600948 DisGeNET 4336 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}. P60370 EBI-10230628,EBI-10172150 P60409 EBI-10172290,EBI-10230628 P60411 EBI-10172052,EBI-10230628 P36957 EBI-351007,EBI-10230628 Q6A162 EBI-10171697,EBI-10230628 P60410 EBI-10171774,EBI-10230628 Q6FHY5 EBI-16439278,EBI-10230628 GO:0030864 GO:0005739 GO:0048471 GO:0003779 GO:0017022 GO:0017137 GO:0019911 GO:0007399 MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRPKQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQPRSSPLRGPGASRGGSPVKASRFW 183 Q14244 Ensconsin MAP7 9606 Yes SL-0198 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. UNIPROT Q14244 UNIPROT B7Z290 UNIPROT B7Z400 UNIPROT B7Z5S7 UNIPROT B7Z9U7 UNIPROT C9JPS0 UNIPROT E9PCP3 UNIPROT F5H1E2 UNIPROT Q7Z6S0 UNIPROT Q8TAU5 UNIPROT Q9NY82 UNIPROT Q9NY83 Pfam PF05672 OMIM 604108 DisGeNET 9053 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}. O15027 EBI-357515,EBI-2211064 Q14203 EBI-724352,EBI-2211064 P61981 EBI-359832,EBI-2211064 P03372 EBI-78473,EBI-2211064 Q86V81 EBI-347640,EBI-2211064 P61457 EBI-740475,EBI-2211064 E9QKK1 EBI-10967445,EBI-2211064 Q2KHM9 EBI-2805604,EBI-2211064 Q86VQ0 EBI-6658186,EBI-2211064 Q9Z2X1 EBI-4283704,EBI-2211064 P62714 EBI-1044367,EBI-2211064 Q8TF05 EBI-1056262,EBI-2211064 G3X972 EBI-11079353,EBI-2211064 Q9D8B3 EBI-8322817,EBI-2211064 Q9Y3M2 EBI-2211064,EBI-947308 O95273 EBI-748961,EBI-2211064 Q6NSX1 EBI-6873045,EBI-2211064 Q8N3C7 EBI-2211064,EBI-5655540 Q71U36 EBI-302552,EBI-2211064 Q8N0Z3 EBI-2361917,EBI-2211064 Q8NC26 EBI-2211064,EBI-10265237 GO:0030424 GO:0016323 GO:0005829 GO:0005874 GO:0005875 GO:0015630 GO:0048471 GO:0005102 GO:0005198 GO:0007163 GO:0000226 GO:0072659 GO:0006970 MAELGAGGDGHRGGDGAVRSETAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPKARQPARSRLWLPSKSLPHLPGTPRPTSSLPPGSVKAAPAQVRPPSPGNIRPVKREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPEVGPAAPAMAPAPASAPAPASAPAPAPVPTPAMVSAPSSTVNASASVKTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQRQAEERALREREEAERAQRQKEEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATDKKTSDQRNGDIAKGALTGGTEVSALPCTTNAPGNGKPVGSPHVVTSHQSKVTVESTPDLEKQPNENGVSVQNENFEEIINLPIGSKPSRLDVTNSESPEIPLNPILAFDDEGTLGPLPQVDGVQTQQTAEVI 749 Q14517 Protocadherin Fat 1, nuclear form FAT1 9606 Yes SL-0198 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}. UNIPROT Q14517 Pfam PF00028 Pfam PF00008 Pfam PF02210 PROSITE PS00010 PROSITE PS00232 PROSITE PS50268 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 PROSITE PS01187 PROSITE PS50025 OMIM 600976 DisGeNET 2195 Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact. {ECO:0000250}. P13569 EBI-349854,EBI-1171918 P09055 EBI-644224,EBI-1171918 Q9JLV5 EBI-2551335,EBI-1171918 Q13418 EBI-747644,EBI-1171918 Q15349 EBI-1384149,EBI-1171918 Q15910 EBI-530054,EBI-1171918 Q8K1S6 EBI-11147680,EBI-1171918 Q9BPW8 EBI-307125,EBI-1171918 Q13291 EBI-4315002,EBI-1171918 Q86WN2 EBI-21641408,EBI-1171918 Q92187 EBI-21513582,EBI-1171918 Q99445 EBI-21642183,EBI-1171918 Q9HD64 EBI-2340004,EBI-1171918 P01127 EBI-1554925,EBI-1171918 P83916 EBI-78129,EBI-1171918 Q02750 EBI-492564,EBI-1171918 P61586 EBI-446668,EBI-1171918 Q05513 EBI-295351,EBI-1171918 Q13322 EBI-80275,EBI-1171918 P46734 EBI-602462,EBI-1171918 P19419 EBI-726632,EBI-1171918 P10644 EBI-476431,EBI-1171918 P63000 EBI-413628,EBI-1171918 Q9UQ74 EBI-21595127,EBI-1171918 Q8N6T7 EBI-712415,EBI-1171918 Q9UK85 EBI-1753048,EBI-1171918 O95156 EBI-21767608,EBI-1171918 Q96LS8 EBI-21767722,EBI-1171918 Q76B58 EBI-21759044,EBI-1171918 GO:0016324 GO:0005911 GO:0070062 GO:0030175 GO:0005925 GO:0005887 GO:0030027 GO:0005634 GO:0048471 GO:0005886 GO:0005509 GO:0007015 GO:0009653 GO:0048593 GO:0007155 GO:0016477 GO:0098609 GO:0007267 GO:0003382 GO:0007163 GO:0045197 GO:0007156 MGRHLALLLLLLLLFQHFGDSDGSQRLEQTPLQFTHLEYNVTVQENSAAKTYVGHPVKMGVYITHPAWEVRYKIVSGDSENLFKAEEYILGDFCFLRIRTKGGNTAILNREVKDHYTLIVKALEKNTNVEARTKVRVQVLDTNDLRPLFSPTSYSVSLPENTAIRTSIARVSATDADIGTNGEFYYSFKDRTDMFAIHPTSGVIVLTGRLDYLETKLYEMEILAADRGMKLYGSSGISSMAKLTVHIEQANECAPVITAVTLSPSELDRDPAYAIVTVDDCDQGANGDIASLSIVAGDLLQQFRTVRSFPGSKEYKVKAIGGIDWDSHPFGYNLTLQAKDKGTPPQFSSVKVIHVTSPQFKAGPVKFEKDVYRAEISEFAPPNTPVVMVKAIPAYSHLRYVFKSTPGKAKFSLNYNTGLISILEPVKRQQAAHFELEVTTSDRKASTKVLVKVLGANSNPPEFTQTAYKAAFDENVPIGTTVMSLSAVDPDEGENGYVTYSIANLNHVPFAIDHFTGAVSTSENLDYELMPRVYTLRIRASDWGLPYRREVEVLATITLNNLNDNTPLFEKINCEGTIPRDLGVGEQITTVSAIDADELQLVQYQIEAGNELDFFSLNPNSGVLSLKRSLMDGLGAKVSFHSLRITATDGENFATPLYINITVAASHKLVNLQCEETGVAKMLAEKLLQANKLHNQGEVEDIFFDSHSVNAHIPQFRSTLPTGIQVKENQPVGSSVIFMNSTDLDTGFNGKLVYAVSGGNEDSCFMIDMETGMLKILSPLDRETTDKYTLNITVYDLGIPQKAAWRLLHVVVVDANDNPPEFLQESYFVEVSEDKEVHSEIIQVEATDKDLGPNGHVTYSIVTDTDTFSIDSVTGVVNIARPLDRELQHEHSLKIEARDQAREEPQLFSTVVVKVSLEDVNDNPPTFIPPNYRVKVREDLPEGTVIMWLEAHDPDLGQSGQVRYSLLDHGEGNFDVDKLSGAVRIVQQLDFEKKQVYNLTVRAKDKGKPVSLSSTCYVEVEVVDVNENLHPPVFSSFVEKGTVKEDAPVGSLVMTVSAHDEDARRDGEIRYSIRDGSGVGVFKIGEETGVIETSDRLDRESTSHYWLTVFATDQGVVPLSSFIEIYIEVEDVNDNAPQTSEPVYYPEIMENSPKDVSVVQIEAFDPDSSSNDKLMYKITSGNPQGFFSIHPKTGLITTTSRKLDREQQDEHILEVTVTDNGSPPKSTIARVIVKILDENDNKPQFLQKFYKIRLPEREKPDRERNARREPLYHVIATDKDEGPNAEISYSIEDGNEHGKFFIEPKTGVVSSKRFSAAGEYDILSIKAVDNGRPQKSSTTRLHIEWISKPKPSLEPISFEESFFTFTVMESDPVAHMIGVISVEPPGIPLWFDITGGNYDSHFDVDKGTGTIIVAKPLDAEQKSNYNLTVEATDGTTTILTQVFIKVIDTNDHRPQFSTSKYEVVIPEDTAPETEILQISAVDQDEKNKLIYTLQSSRDPLSLKKFRLDPATGSLYTSEKLDHEAVHQHTLTVMVRDQDVPVKRNFARIVVNVSDTNDHAPWFTASSYKGRVYESAAVGSVVLQVTALDKDKGKNAEVLYSIESGNIGNSFMIDPVLGSIKTAKELDRSNQAEYDLMVKATDKGSPPMSEITSVRIFVTIADNASPKFTSKEYSVELSETVSIGSFVGMVTAHSQSSVVYEIKDGNTGDAFDINPHSGTIITQKALDFETLPIYTLIIQGTNMAGLSTNTTVLVHLQDENDNAPVFMQAEYTGLISESASINSVVLTDRNVPLVIRAADADKDSNALLVYHIVEPSVHTYFAIDSSTGAIHTVLSLDYEETSIFHFTVQVHDMGTPRLFAEYAANVTVHVIDINDCPPVFAKPLYEASLLLPTYKGVKVITVNATDADSSAFSQLIYSITEGNIGEKFSMDYKTGALTVQNTTQLRSRYELTVRASDGRFAGLTSVKINVKESKESHLKFTQDVYSAVVKENSTEAETLAVITAIGNPINEPLFYHILNPDRRFKISRTSGVLSTTGTPFDREQQEAFDVVVEVTEEHKPSAVAHVVVKVIVEDQNDNAPVFVNLPYYAVVKVDTEVGHVIRYVTAVDRDSGRNGEVHYYLKEHHEHFQIGPLGEISLKKQFELDTLNKEYLVTVVAKDGGNPAFSAEVIVPITVMNKAMPVFEKPFYSAEIAESIQVHSPVVHVQANSPEGLKVFYSITDGDPFSQFTINFNTGVINVIAPLDFEAHPAYKLSIRATDSLTGAHAEVFVDIIVDDINDNPPVFAQQSYAVTLSEASVIGTSVVQVRATDSDSEPNRGISYQMFGNHSKSHDHFHVDSSTGLISLLRTLDYEQSRQHTIFVRAVDGGMPTLSSDVIVTVDVTDLNDNPPLFEQQIYEARISEHAPHGHFVTCVKAYDADSSDIDKLQYSILSGNDHKHFVIDSATGIITLSNLHRHALKPFYSLNLSVSDGVFRSSTQVHVTVIGGNLHSPAFLQNEYEVELAENAPLHTLVMEVKTTDGDSGIYGHVTYHIVNDFAKDRFYINERGQIFTLEKLDRETPAEKVISVRLMAKDAGGKVAFCTVNVILTDDNDNAPQFRATKYEVNIGSSAAKGTSVVKVLASDADEGSNADITYAIEADSESVKENLEINKLSGVITTKESLIGLENEFFTFFVRAVDNGSPSKESVVLVYVKILPPEMQLPKFSEPFYTFTVSEDVPIGTEIDLIRAEHSGTVLYSLVKGNTPESNRDESFVIDRQSGRLKLEKSLDHETTKWYQFSILARCTQDDHEMVASVDVSIQVKDANDNSPVFESSPYEAFIVENLPGGSRVIQIRASDADSGTNGQVMYSLDQSQSVEVIESFAINMETGWITTLKELDHEKRDNYQIKVVASDHGEKIQLSSTAIVDVTVTDVNDSPPRFTAEIYKGTVSEDDPQGGVIAILSTTDADSEEINRQVTYFITGGDPLGQFAVETIQNEWKVYVKKPLDREKRDNYLLTITATDGTFSSKAIVEVKVLDANDNSPVCEKTLYSDTIPEDVLPGKLIMQISATDADIRSNAEITYTLLGSGAEKFKLNPDTGELKTSTPLDREEQAVYHLLVRATDGGGRFCQASIVLTLEDVNDNAPEFSADPYAITVFENTEPGTLLTRVQATDADAGLNRKILYSLIDSADGQFSINELSGIIQLEKPLDRELQAVYTLSLKAVDQGLPRRLTATGTVIVSVLDINDNPPVFEYREYGATVSEDILVGTEVLQVYAASRDIEANAEITYSIISGNEHGKFSIDSKTGAVFIIENLDYESSHEYYLTVEATDGGTPSLSDVATVNVNVTDINDNTPVFSQDTYTTVISEDAVLEQSVITVMADDADGPSNSHIHYSIIDGNQGSSFTIDPVRGEVKVTKLLDRETISGYTLTVQASDNGSPPRVNTTTVNIDVSDVNDNAPVFSRGNYSVIIQENKPVGFSVLQLVVTDEDSSHNGPPFFFTIVTGNDEKAFEVNPQGVLLTSSAIKRKEKDHYLLQVKVADNGKPQLSSLTYIDIRVIEESIYPPAILPLEIFITSSGEEYSGGVIGKIHATDQDVYDTLTYSLDPQMDNLFSVSSTGGKLIAHKKLDIGQYLLNVSVTDGKFTTVADITVHIRQVTQEMLNHTIAIRFANLTPEEFVGDYWRNFQRALRNILGVRRNDIQIVSLQSSEPHPHLDVLLFVEKPGSAQISTKQLLHKINSSVTDIEEIIGVRILNVFQKLCAGLDCPWKFCDEKVSVDESVMSTHSTARLSFVTPRHHRAAVCLCKEGRCPPVHHGCEDDPCPEGSECVSDPWEEKHTCVCPSGRFGQCPGSSSMTLTGNSYVKYRLTENENKLEMKLTMRLRTYSTHAVVMYARGTDYSILEIHHGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVALEVNGNYARLVLDQVHTASGTAPGTLKTLNLDNYVFFGGHIRQQGTRHGRSPQVGNGFRGCMDSIYLNGQELPLNSKPRSYAHIEESVDVSPGCFLTATEDCASNPCQNGGVCNPSPAGGYYCKCSALYIGTHCEISVNPCSSKPCLYGGTCVVDNGGFVCQCRGLYTGQRCQLSPYCKDEPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECSGNPCLHGALCENTHGSYHCNCSHEYRGRHCEDAAPNQYVSTPWNIGLAEGIGIVVFVAGIFLLVVVFVLCRKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRNRQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV 4588 Q14542 Equilibrative nucleoside transporter 2 SLC29A2 9606 Yes SL-0178 SL-0182 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. UNIPROT Q14542 UNIPROT B3KPY7 UNIPROT O43530 UNIPROT Q52M84 UNIPROT Q96R00 UNIPROT Q9UPE0 Pfam PF01733 OMIM 602110 DisGeNET 3177 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}. GO:0016323 GO:0016021 GO:0005887 GO:0031965 GO:0005730 GO:0005886 GO:0098793 GO:0005337 GO:0015853 GO:0015854 GO:0035344 GO:0098810 GO:0006139 GO:0015858 GO:0035364 GO:0015862 MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNNWVTLLSQLPLLLFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAELLQSDENGIPSSPQKVALTLDLDLEKEPESEPDEPQKPGKPSVFTVFQKIWLTALCLVLVFTVTLSVFPAITAMVTSSTSPGKWSQFFNPICCFLLFNIMDWLGRSLTSYFLWPDEDSRLLPLLVCLRFLFVPLFMLCHVPQRSRLPILFPQDAYFITFMLLFAVSNGYLVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL 456 Q14643 Inositol 1,4,5-trisphosphate receptor type 1 ITPR1 9606 Yes SL-0198 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}. UNIPROT Q14643 UNIPROT E7EPX7 UNIPROT E9PDE9 UNIPROT Q14660 UNIPROT Q99897 Pfam PF08709 Pfam PF00520 Pfam PF02815 Pfam PF08454 Pfam PF01365 PROSITE PS50919 OMIM 117360 OMIM 147265 OMIM 206700 OMIM 606658 DisGeNET 3708 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}.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. P04626 EBI-465548,EBI-641062 Q9NRI5 EBI-465548,EBI-529989 Q14108 EBI-1564650,EBI-465548 Q96GC9 EBI-2800296,EBI-465548 P38646 EBI-354932,EBI-465548 P31749 EBI-296087,EBI-465548 P30405 EBI-465548,EBI-5544229 Q81T40 EBI-465548,EBI-2816570 Q15149 EBI-297903,EBI-465548 Q9BS26 EBI-465548,EBI-541644 Q9Y3M8 EBI-465548,EBI-465487 GO:0005955 GO:0005623 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0005637 GO:0005730 GO:0048471 GO:0005886 GO:0031088 GO:0031094 GO:0031095 GO:0014069 GO:0016529 GO:0098685 GO:0030667 GO:0030658 GO:0019855 GO:0005509 GO:0015085 GO:0015278 GO:0070679 GO:0098695 GO:0005220 GO:0035091 GO:0006816 GO:0032469 GO:0042045 GO:0070059 GO:0050849 GO:0030168 GO:0009791 GO:0010506 GO:1903779 GO:0050796 GO:0051209 GO:0001666 GO:0007165 GO:0050882 MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA 2758 Q14764 Major vault protein MVP 9606 Yes SL-0178 SL-0185 SL-0198 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). UNIPROT Q14764 UNIPROT Q96BG4 UNIPROT Q9BPW6 UNIPROT Q9BQT1 UNIPROT Q9UBD1 PDB 1Y7X Pfam PF11978 Pfam PF01505 Pfam PF17794 Pfam PF17795 Pfam PF17796 PROSITE PS51224 OMIM 605088 DisGeNET 9961 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}. O15162 EBI-740019,EBI-2816254 Q07065 EBI-2816254,EBI-702400 Self EBI-2816254,EBI-2816254 P13569 EBI-349854,EBI-2816254 Q8NHY2-1 EBI-9698228,EBI-2816254 Q6FHY5 EBI-16439278,EBI-2816254 P60710 EBI-353957,EBI-2816254 Q9QWF0 EBI-639217,EBI-2816254 Q9D6T1 EBI-10990005,EBI-2816254 P51692 EBI-1186119,EBI-2816254 Q6IRU7 EBI-2553851,EBI-2816254 Q08380 EBI-354956,EBI-2816254 Q07797 EBI-8399565,EBI-2816254 Q06180 EBI-8471238,EBI-2816254 P21980 EBI-727668,EBI-2816254 Q5SRY7 EBI-11073522,EBI-2816254 Q3TRR0 EBI-8328917,EBI-2816254 Q9NYZ3 EBI-2511327,EBI-2816254 Q00610 EBI-354967,EBI-2816254 Q9D8B3 EBI-8322817,EBI-2816254 P18031 EBI-968788,EBI-2816254 Q9UMR2-2 EBI-21500353,EBI-2816254 Q9UKK3 EBI-2816254,EBI-2623021 Q9P2K3-3 EBI-2816254,EBI-11087909 Q9HD26-2 EBI-2816254,EBI-11102276 P11142 EBI-2816254,EBI-351896 Q9H0E2 EBI-74615,EBI-2816254 Q53EP0-3 EBI-10242151,EBI-2816254 P52292 EBI-349938,EBI-2816254 P00156 EBI-1224441,EBI-2816254 Q14161 EBI-1046878,EBI-2816254 Q13423 EBI-1391318,EBI-2816254 Q9NUX5 EBI-2816254,EBI-752420 P34913 EBI-2816254,EBI-724704 P00738 EBI-2816254,EBI-1220767 A0A384KY07 EBI-2816254,EBI-2843582 Q81ME0 EBI-2816254,EBI-2813646 Q81ZA2 EBI-2816254,EBI-2811440 Q81TT4 EBI-2810319,EBI-2816254 A0A0F7RF31 EBI-2810739,EBI-2816254 P20339 EBI-399437,EBI-2816254 O60496 EBI-1046024,EBI-2816254 Q14254 EBI-348613,EBI-2816254 Q16778 EBI-1056125,EBI-2816254 Q93079 EBI-352469,EBI-2816254 P57053 EBI-2880265,EBI-2816254 P58876 EBI-4409942,EBI-2816254 Q5QNW6-2 EBI-20847120,EBI-2816254 Q8WUN7 EBI-2816254,EBI-12867288 Q16656-4 EBI-2816254,EBI-11742836 Q86UW9 EBI-2816254,EBI-740376 Q96HA8 EBI-2816254,EBI-741158 Q1K9H5 EBI-6050669,EBI-2816254 P03431 EBI-2547514,EBI-2816254 Q6IQ23 EBI-2125301,EBI-2816254 GO:0005737 GO:0005856 GO:0005829 GO:0070062 GO:0005576 GO:1904813 GO:0016020 GO:0005643 GO:0005634 GO:0048471 GO:0034774 GO:0042802 GO:0019901 GO:0019903 GO:0038127 GO:0051028 GO:0031953 GO:0061099 GO:0023057 GO:0043312 GO:0015031 GO:0023051 MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGIQDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTGTAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTEAIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR 893 Q148F6 Protein rogdi homolog ROGDI 9913 Yes SL-0178 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}. UNIPROT Q148F6 Pfam PF10259 DE Reference Proteome: Yes; GO:0030424 GO:0005623 GO:0030054 GO:0030425 GO:0005635 GO:0005634 GO:0043204 GO:0043291 GO:0008021 GO:0032502 GO:0007035 MATVMAATAAERAVLEEEFRWLLHDEVHAVLRQLQDILKEASLRFTLPGSGTEGPTKQENFILGSCGTDQVKGVLTLQGDALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFRTGAEVLKLMDAVMLQLTRARNRLTTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHTLQPNSTKNFRPAGGAVLHSPGAMFEWGTQRLEVSHVHKVESVIPWLNDALVFFTVSLQLCQQLKDKISVFSSYWSCRPF 287 Q15056 Eukaryotic translation initiation factor 4H EIF4H 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q15056 UNIPROT A8K3R1 UNIPROT D3DXF6 UNIPROT D3DXF8 Pfam PF00076 PROSITE PS50102 OMIM 603431 DisGeNET 7458 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.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}. P60842 EBI-73449,EBI-748492 Q6MZP7 EBI-1389411,EBI-748492 Q9H3H3 EBI-721765,EBI-748492 Q8TBB1 EBI-739832,EBI-748492 Q91W50 EBI-8318466,EBI-748492 Q96FW1 EBI-1058491,EBI-748492 P19320 EBI-6189824,EBI-748492 P10225 EBI-6148417,EBI-748492 P02751 EBI-1220319,EBI-748492 A0A384LA14 EBI-748492,EBI-2845602 A0A1S0QL17 EBI-2814598,EBI-748492 Q14164 EBI-748492,EBI-307369 O60739 EBI-748492,EBI-1043343 P23508 EBI-307531,EBI-748492 P0DTD1 EBI-25475877,EBI-748492 GO:0005829 GO:0016281 GO:0016020 GO:0048471 GO:0005844 GO:0045296 GO:0003723 GO:0008135 GO:0003743 GO:0048589 GO:0006446 GO:0019953 GO:0006413 GO:0016032 MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE 248 Q15256 Receptor-type tyrosine-protein phosphatase R PTPRR 9606 Yes SL-0198 [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. UNIPROT Q15256 UNIPROT B2R5Z7 UNIPROT B7Z3J1 UNIPROT F5GXR7 UNIPROT O00342 UNIPROT Q92682 UNIPROT Q9UE65 PDB 2A8B Pfam PF00102 PROSITE PS00383 PROSITE PS50056 PROSITE PS50055 OMIM 602853 DisGeNET 5801 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}. P02545 EBI-2265659,EBI-351935 P42704 EBI-2265659,EBI-1050853 P19022 EBI-2265659,EBI-2256711 P09619 EBI-641237,EBI-2265659 P28482 EBI-2265659,EBI-959949 O60783 EBI-2265659,EBI-1045956 O75688 EBI-2265659,EBI-1047039 P07237 EBI-2265659,EBI-395883 P10809 EBI-2265659,EBI-352528 P14625 EBI-2265659,EBI-359129 P17987 EBI-2265659,EBI-356553 P23528 EBI-2265659,EBI-352733 P31153 EBI-2265659,EBI-1050743 P40227 EBI-2265659,EBI-356687 P42166 EBI-2265659,EBI-395393 P48643 EBI-2265659,EBI-355710 P49368 EBI-2265659,EBI-356673 P50990 EBI-2265659,EBI-356507 P50991 EBI-2265659,EBI-356876 P56134 EBI-2265659,EBI-712794 P63261 EBI-2265659,EBI-351292 P78371 EBI-2265659,EBI-357407 P82650 EBI-2265659,EBI-1050752 P82673 EBI-2265659,EBI-2513649 P82675 EBI-2265659,EBI-1054287 P82914 EBI-2265659,EBI-2880040 P82930 EBI-2265659,EBI-1048516 Q02978 EBI-2265659,EBI-359174 Q15149 EBI-2265659,EBI-297903 Q16875 EBI-2265659,EBI-764464 Q7L014 EBI-2265659,EBI-2555356 Q8NCE2 EBI-2265659,EBI-5658424 Q92552 EBI-2265659,EBI-2211879 Q92665 EBI-2265659,EBI-720602 Q96EY1 EBI-2265659,EBI-356767 Q96EY7 EBI-2265659,EBI-721110 Q99832 EBI-2265659,EBI-357046 Q9BU76 EBI-2265659,EBI-742459 Q9GZT3 EBI-2265659,EBI-1050793 Q9H3K6 EBI-2265659,EBI-1642537 Q9NVI7 EBI-2265659,EBI-352007 Q9NWB6 EBI-2265659,EBI-2808785 Q9NXV2 EBI-2265659,EBI-1056857 Q9ULV4 EBI-2265659,EBI-351384 Q9Y291 EBI-2265659,EBI-2688704 Q9Y2Q9 EBI-2265659,EBI-5325249 Q9Y2R9 EBI-2265659,EBI-1054973 Q9Y399 EBI-2265659,EBI-2880048 Q9Y3D9 EBI-2265659,EBI-1054270 P19338 EBI-2265659,EBI-346967 P22087 EBI-2265659,EBI-358318 Q13610 EBI-2265659,EBI-1050630 Q5VZ46 EBI-2265659,EBI-20895075 Q6P5R6 EBI-2265659,EBI-2512545 Q9BQ67 EBI-2265659,EBI-351000 Q9NSD9 EBI-2265659,EBI-353803 Q9NUL7 EBI-2265659,EBI-2560229 GO:0030054 GO:0005829 GO:0005615 GO:0016021 GO:0048471 GO:0005886 GO:0019901 GO:0004725 GO:0005001 GO:0038128 GO:0001701 GO:0010633 GO:0070373 GO:0006470 MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQIVNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKKNSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVIIVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYESRLSAETVQ 657 Q15283 Ras GTPase-activating protein 2 RASA2 9606 Yes SL-0198 Cytoplasm. Cytoplasm, perinuclear region. UNIPROT Q15283 UNIPROT A8K7K1 UNIPROT G3V0F9 UNIPROT O00695 UNIPROT Q15284 UNIPROT Q92594 UNIPROT Q99577 UNIPROT Q9UEQ2 Pfam PF00779 Pfam PF00168 Pfam PF00169 Pfam PF00616 PROSITE PS50004 PROSITE PS50003 PROSITE PS00509 PROSITE PS50018 PROSITE PS51113 OMIM 601589 DisGeNET 5922 Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4). GO:0005829 GO:0048471 GO:0005096 GO:0046872 GO:0005543 GO:0000165 GO:0046580 GO:0007165 MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQEEVYRTQVVEKSLSPFFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVAIKKEDLCNHSGKETWFSLQPVDSNSEVQGKVHLELKLNELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQFQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIKVPVNVLRTDSSHQAWYLLQPRDNGNKSSKTDDLGSLRLNICYTEDYVLPSEYYGPLKTLLLKSPDVQPISASAAYILSEICRDKNDAVLPLVRLLLHHDKLVPFATAVAELDLKDTQDANTIFRGNSLATRCLDEMMKIVGGHYLKVTLKPILDEICDSSKSCEIDPIKLKEGDNVENNKENLRYYVDKLFNTIVKSSMSCPTVMCDIFYSLRQMATQRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFHLRPHHPDAQTIRTLTLISKTIQTLGSWGSLSKSKSSFKETFMCEFFKMFQEEGYIIAVKKFLDEISSTETKESSGTSEPVHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTYHKQPGSKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSRCNQNRLSFYHPSVYLNGNWLCCQETGENTLGCKPCTAGVPADIQIDIDEDRETERIYSLFTLSLLKLQKMEEACGTIAVYQGPQKEPDDYSNFVIEDSVTTFKTIQQIKSIIEKLDEPHEKYRKKRSSSAKYGSKENPIVGKAS 850 Q15642 Cdc42-interacting protein 4 TRIP10 9606 Yes SL-0198 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. UNIPROT Q15642 UNIPROT B2R8A6 UNIPROT B7WP22 UNIPROT D6W645 UNIPROT O15184 UNIPROT Q53G22 UNIPROT Q5TZN1 UNIPROT Q6FI24 UNIPROT Q8NFL1 UNIPROT Q8TCY1 UNIPROT Q8TDX3 UNIPROT Q96RJ1 PDB 2CT4 PDB 2EFK PDB 2KE4 Pfam PF00611 Pfam PF00018 PROSITE PS51741 PROSITE PS51860 PROSITE PS50002 OMIM 604504 DisGeNET 9322 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}. Self EBI-739936,EBI-739936 Q96RU3 EBI-1111248,EBI-739936 Q9H4E5 EBI-739936,EBI-6285694 Q969G3 EBI-739936,EBI-455078 Q92558 EBI-739936,EBI-1548747 Q17R89-2 EBI-10238335,EBI-739936 Q1RLN5 EBI-739936,EBI-3959665 Q68EM7 EBI-739936,EBI-1642807 Q9Y3L3 EBI-346869,EBI-739936 A0A384LA14 EBI-2845602,EBI-739936 A0A0F7RIX9 EBI-739936,EBI-2817483 Q17R89-1 EBI-25410514,EBI-739936 Q9Y2W2 EBI-714455,EBI-739936 GO:0005938 GO:0042995 GO:0005737 GO:0005856 GO:0005829 GO:0070062 GO:0005794 GO:0043231 GO:0005764 GO:0005654 GO:0048471 GO:0001891 GO:0042802 GO:0008289 GO:0030036 GO:0007154 GO:0006897 GO:0061024 GO:0051056 GO:0007165 MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN 601 Q15811 Intersectin-1 ITSN1 9606 Yes SL-0178 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}. UNIPROT Q15811 UNIPROT A7Y322 UNIPROT A8CTX8 UNIPROT A8CTY3 UNIPROT A8CTY7 UNIPROT A8D7D0 UNIPROT A8DCP3 UNIPROT B4DTM2 UNIPROT E7ERJ1 UNIPROT E9PE44 UNIPROT E9PG01 UNIPROT E9PHV2 UNIPROT O95216 UNIPROT Q0PW94 UNIPROT Q0PW95 UNIPROT Q0PW97 UNIPROT Q14BD3 UNIPROT Q1ED40 UNIPROT Q20BK3 UNIPROT Q9UET5 UNIPROT Q9UK60 UNIPROT Q9UNK1 UNIPROT Q9UNK2 UNIPROT Q9UQ92 PDB 1KI1 PDB 2KGR PDB 2KHN PDB 3FIA PDB 3QBV PDB 4IIM PDB 5HZI PDB 5HZJ PDB 5HZK PDB 6GBU PDB 6H5T Pfam PF00168 Pfam PF12763 Pfam PF16652 Pfam PF00621 Pfam PF00018 Pfam PF14604 PROSITE PS50004 PROSITE PS00741 PROSITE PS50010 PROSITE PS00018 PROSITE PS50222 PROSITE PS50031 PROSITE PS50003 PROSITE PS50002 OMIM 602442 DisGeNET 6453 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}. P35658 EBI-602041,EBI-1222270 Q12840 EBI-713468,EBI-602041 Q9NRI5 EBI-529989,EBI-602041 Q6NSK7 EBI-602041,EBI-21369851 O43175 EBI-350495,EBI-602041 P63010 EBI-432924,EBI-602041 O43150 EBI-602041,EBI-310968 P22681 EBI-518228,EBI-602041 Q6ZUJ8 EBI-2654168,EBI-602041 Q15427 EBI-348469,EBI-602041 P22674 EBI-2556878,EBI-602041 Q99471 EBI-602041,EBI-357275 Q9Y2W2 EBI-714455,EBI-602041 Q07889 EBI-297487,EBI-602041 Q92734 EBI-357061,EBI-602041 Q9NS91 EBI-2339393,EBI-602041 P15311 EBI-1056902,EBI-602041 O43493 EBI-1752146,EBI-602041 A0A1Q4LW06 EBI-602041,EBI-2815425 O75940 EBI-602041,EBI-1052641 Q8TAQ2 EBI-357418,EBI-602041 Q15599 EBI-602041,EBI-1149760 P22307 EBI-602041,EBI-1050999 O95757 EBI-602041,EBI-358652 P51659 EBI-602041,EBI-358398 Q9UBC2 EBI-602041,EBI-2556746 P42566 EBI-602041,EBI-396684 Q13011 EBI-602041,EBI-711968 P09496 EBI-602041,EBI-1171169 Q969X6 EBI-602041,EBI-2602591 P04040 EBI-602041,EBI-2432181 Q96CW1 EBI-602041,EBI-297683 O94973 EBI-602041,EBI-1642835 O95782 EBI-602041,EBI-353552 Q07889-1 EBI-25408451,EBI-602041 P60953-1 EBI-602041,EBI-3625591 P68104 EBI-352162,EBI-602041 Q13432 EBI-711260,EBI-602041 Q9BYC9 EBI-714361,EBI-602041 Q9Y5X3 EBI-715760,EBI-602041 GO:0097440 GO:0044305 GO:0030054 GO:0005905 GO:0005737 GO:0005829 GO:0043197 GO:0030139 GO:0098978 GO:0030027 GO:0043025 GO:0005635 GO:0005886 GO:0098871 GO:0098833 GO:0055037 GO:0005509 GO:0005085 GO:0019209 GO:0060090 GO:0070064 GO:0007420 GO:0034613 GO:0048013 GO:0006887 GO:0007186 GO:0061024 GO:0043524 GO:0043065 GO:2001288 GO:0060999 GO:0060124 GO:0051897 GO:0015031 GO:1905274 GO:0051056 GO:0007264 GO:0048488 GO:0016032 MAQFPTPFGGSLDIWAITVEERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSALPPVMKQQPVAISSAPAFGMGGIASMPPLTAVAPVPMGSIPVVGMSPTLVSSVPTAAVPPLANGAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASVPPVAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGISVISSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQENVKVVYYRALYPFESRSHDEITIQPGDIVMVKGEWVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENEVPAPVKPVTDSTSAPAPKLALRETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLTVPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPIRKSTSMDSGSSESPASLKRVASPAAKPVVSGEEFIAMYTYESSEQGDLTFQQGDVILVTKKDGDWWTGTVGDKAGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTSKITPTEPPKSTALAAVCQVIGMYDYTAQNDDELAFNKGQIINVLNKEDPDWWKGEVNGQVGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSRQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP 1721 Q16620 BDNF/NT-3 growth factors receptor NTRK2 9606 Yes SL-0198 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}. UNIPROT Q16620 UNIPROT B1ANZ4 UNIPROT B4DFV9 UNIPROT Q16675 UNIPROT Q59GJ1 UNIPROT Q8WXJ5 UNIPROT Q8WXJ6 UNIPROT Q8WXJ7 PDB 1HCF PDB 1WWB PDB 2MFQ PDB 4ASZ PDB 4AT3 PDB 4AT4 PDB 4AT5 PDB 5MO9 Pfam PF07679 Pfam PF13855 Pfam PF01462 Pfam PF07714 Pfam PF16920 PROSITE PS50835 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS00239 OMIM 600456 OMIM 613886 OMIM 617830 DisGeNET 4915 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}.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. P00533 EBI-297353,EBI-3904881 P34130 EBI-3904881,EBI-3907456 P14618-1 EBI-3904881,EBI-4304679 Q10567 EBI-3904881,EBI-1171303 P62487 EBI-347928,EBI-3904881 Q9HAN9 EBI-3904881,EBI-3917542 P08238 EBI-3904881,EBI-352572 GO:0030424 GO:0043679 GO:0030054 GO:0005829 GO:0030425 GO:0043197 GO:0005769 GO:0031901 GO:0000139 GO:0005887 GO:0048471 GO:0005886 GO:0014069 GO:0043235 GO:0043195 GO:0005524 GO:0048403 GO:0060175 GO:0043121 GO:0005030 GO:0042803 GO:0004713 GO:0004714 GO:0007202 GO:0031547 GO:0071230 GO:1990416 GO:1990090 GO:0021954 GO:0021987 GO:0007623 GO:0007631 GO:0014047 GO:0007612 GO:0060291 GO:0042490 GO:0007275 GO:0022011 GO:2000811 GO:0043524 GO:0007399 GO:0030182 GO:0001764 GO:0019227 GO:0048011 GO:0048709 GO:0048935 GO:0050772 GO:0008284 GO:0010628 GO:0033674 GO:0043410 GO:0010976 GO:1903997 GO:0033138 GO:0014068 GO:0001934 GO:0051965 GO:0046777 GO:0043087 GO:0043408 GO:0051896 GO:0046548 GO:0099183 GO:0099551 GO:0007169 GO:0001570 MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG 822 Q17285 Period circadian protein per 34689 No SL-0198 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}. UNIPROT Q17285 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}. GO:0005634 GO:0048471 GO:0048511 SKSSTGTPPSYNQLNYNENLMRFFKSKPVTVGKEESMAVEQSYNDVELQRDPSPDQCCDYSGESGSAGNLSSGSNVQMEIITNGSNTGTGTSSGSFQPPLLTEALLN 107 Q17602 Nuclear pore complex protein 14 npp 6239 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q17602 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}. GO:0031965 GO:0005643 GO:0089720 GO:0008139 GO:0017056 GO:1990001 GO:0051028 GO:1900118 GO:0006606 GO:0006405 MSNEDVAEDVSQVTDFHFHTCRKFRLFSSKSDGYSQNEINIRNRVATSSQLGVTFVTVNSNQLSCFHTKSLLGYKITRENMNVEVTDLPIKTIRLHGVVLINDMGVNSDGTVLGVLHTKNNDVSVDVFDIKKICTSSSIEPFKPLCTTRVGTEQINQGSCLEWNPAFPDTFAASSTDRSILVAKINVQSPANQKLVGIGKFGAVTTAISWSPKGKQLTIGDSLGKIVQLKPELEVVRSQHGPENKPNYGRITGLCWLATTEWLVSLENGTDQDAYLMRCKKDKPTEWIQFHELSYSSSKWPLPPQLFPATQLLVDWNVVIVGNSKTSEISTVGKRDDWQTWVPVEGESIYLPTTSSGKDTVPIGVAVDRSMTDEVLLNPDGSQRHRPSPLVLCLTNDGILTAHHIISTFAAHIPCQMSSQNLAINDLKKLQFDSQKPISAPPSDQTPVTKPSTVFGQKPEAETLKSSLVGSPSSVQTPKPSSSLFNPKSIASNIETSQLTESKPSTPAAPSSQPKIASTPKSEAIPKISDKTLEHKKAELIATKKQVLIERMDKINDSMAGAKDATMKLSFAVGKVKTTIMECADVVRASLGDSKEVMDELKNLILSIERMSDRTQHTVKEMDFEIDEKMELVAGVEDGNQVLEKLRNMSETEKLMRFNKLETAADLLNGKYEECSDLIKKLRMSLSEKESLRKQAILSPLRLSSNLNQLRSGSETELALKVMRNVSKIIMDTREQIQRTELEFVRFQRDVKFQNFKKGKENLNFTQPLEMSSLDGDAPQGKSLTDAESIKVRQALVNQIQKRGIVKTRNVIVESYKKSENSAAMKNDLLDTSNLSNAILKLSMTPRRVMPSSSLFSASPSTPSTKSDAATQADEPPIVKTVVVTVESPAKPIASAPAVSSPLIKLNTTTATTTMTTPKVTVPKEEANKTQDQKPIISTPASSSIFSSGSLFGTKTQTPLVSKEESTLTTGVPSLINSSLSISPQEIEKASSKVETLNKTEEVKDEKSENEVTPDLKSEEPKSLETKVKEEPKPAVQTPVKEEETGSNIQKTPSFSFNSTTTPKSTSSTSSIFGGGLKTQTPSSSNSTNIFGARTTTTATPTPASNTSSIFGGGSKAASSPFGSFGQAGCQPAKTSNPATSTASVTFSFNTGATSASAKPAGFGSFGAGASAKPSSVFGGSVTAPTVPNVDDGMEDDSMANGGGSGGFMSGLGNARTSNTSGGNNPFAPKTSTGTSASSSSWLFGGGGNQQQQQQQKPSFSFNTAGSSAQQASAPATGTSSVFGGAPKFGSQPAFGAKPFGGGANAGLSKNASIFGGATSSTTNNPATGGFAQFASGQKTSSLFGGGATPQTNTSIFGGGANTTPAPTSSVFGGGASANANKPTSFTSWR 1390 Q17902 Egalitarian protein homolog egal 6239 Yes SL-0178 Nucleus envelope {ECO:0000305|PubMed:20005871}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}. UNIPROT Q17902 UNIPROT Q65ZH5 Pfam PF01612 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}. Q22799 EBI-328330,EBI-328324 V6CJ04 EBI-2006416,EBI-328330 GO:0005635 GO:0008408 GO:0003676 MEEAKNMALLFFMDHLMQKNGRRTIHDLSCQFGARGFSEEMRNAVGTTQEGLTEFLQGHPSLFTVEGDQVILNGHNDLNAKNNPLLQSGIRSRNYEKEAVDFFVTKLTKFGPELQIKSLLGHRSQAAPEVRLVSGRHLKEFCEFLQSQVDYFVVEGDRVRLKNMPEPDENAIEMDDEGRPLAGVKAKQAAVEYLKSVLEQNEDQPIPLDQFYQNFCQRFSHTIRQDVATNPKELLQFLKLNRGLFFIRSNKVSLVKNRLNEDGSENGSDEGEETNNNGMFPLDQSALTRIHFVKALKPAQDLISRLWQDINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATTSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKFNKSLNEMRPISFINLQRVYYPQSIMLSDVTPRKMSMCPNWGVRPITEEFQLTIVEEAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPEVLLASPNRPPPQPFISSPYRASTRRDVRNGGSIMQSFSPAPYAAAPRPQMSDACTQTFSTGDIEVLNVFYE 574 Q17DK5 Cryptochrome-1 cry 7159 Yes SL-0198 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}. UNIPROT Q17DK5 Pfam PF00875 Pfam PF03441 PROSITE PS00394 PROSITE PS51645 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}. GO:0005737 GO:0005641 GO:0005634 GO:0048471 GO:0009882 GO:0050660 GO:0045892 GO:0018298 GO:0042752 GO:0048511 MTVNNILWFRHGLRLHDNPSLLEALRNDGTGSESVRLYPIFIFDGESAGTKLVGFNRMKFLLESLADLDRQLREIGGQLYVFKGNAVNVMRRLFEELNIRKLCFEQDCEPIWKARDDAIQNLCRMMDVKCVEKVSHTLWDPQQIIRTNGGIPPLTYQMFLHTVDIIGKPPRPVAAPSFEFVEFGSIPSILAQEVKLQQVRNLSPEDFGIYYEGNPDISHQQWMGGETKALECLGHRLKQEEEAFLGGYFLPTQAKPEFLVPPTSMSAALRFGCLSVRMFYWCVHDLYEKVQANNQYRNPGGQHITGQLIWREYFYTMSVHNPHYAEMEANPICLNIPWYEPKDDSLDRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGALWISWEAGVQHFLKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPIALARRLDPKGEYVRRYLPELKNLPTLYVHEPWKAPLDVQKECGCIVGRDYPAPMIDLAAASRANANTMNSIRQKLMERGGSTPPHCRPSDVEEIRNFFWLPEDVVADC 545 Q17RY0 Cytoplasmic polyadenylation element-binding protein 4 CPEB4 9606 Yes SL-0198 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}. UNIPROT Q17RY0 UNIPROT B7ZLQ7 UNIPROT Q7Z310 UNIPROT Q8N405 UNIPROT Q9C0J0 PDB 2MKI PDB 2MKJ PDB 5DIF Pfam PF16366 Pfam PF16367 PROSITE PS50102 OMIM 610607 DisGeNET 80315 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}. Q6ZNJ1 EBI-2862306,EBI-2848203 Q9H4B6 EBI-1017775,EBI-2848203 Q9H6Z9 EBI-1175354,EBI-2848203 Q8D052 EBI-2844272,EBI-2848203 GO:0030054 GO:0005737 GO:0030425 GO:0043197 GO:0005783 GO:0030426 GO:1990124 GO:0043005 GO:0005634 GO:0048471 GO:0014069 GO:0045202 GO:0046872 GO:0003730 GO:0043022 GO:0003723 GO:0008135 GO:0000900 GO:0071230 GO:0036294 GO:0042149 GO:0035235 GO:2000766 GO:0043524 GO:0002931 MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDTIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN 729 Q18508 Protein mel-28 mel 6239 Yes SL-0178 SL-0179 SL-0182 SL-0185 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}. UNIPROT Q18508 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}. G5EE71 EBI-2002749,EBI-2002730 Q21443 EBI-314110,EBI-2002730 P91001 EBI-313007,EBI-2002730 GO:0000777 GO:0000776 GO:0005635 GO:0005637 GO:0005643 GO:0005654 GO:0003677 GO:0060090 GO:0051301 GO:0051321 GO:0000070 GO:0051028 GO:0051292 GO:0015031 MDNENSSIFKSYQGYECWRGEKQIILKDSIGRQLPYIVNFKKNTCQIFDIEWERVTHSFVFPEGCALIDADYFPTEEGKLGILVGVEDPRQSCGAEHFVLALAVDPDSPAMTITHSLEVPSKITVVKTLFSSADMADETQRTVLKLYHRLMTWQHIVAIGCKETQCYLARLVAVETPSSPVITVHSEKKYLINLMNAYVSGSVLQYTLDDGAYREYPTAAVYISALSLMPRSRTLLVGLSMGGILAASLNPSNQMMLLELRHERLVRKIAPLEPEDDPDKFEYFIATVDCSPRHPIMIQLWRGSFKTLEDVDGEEKYDRPSFSVCLEHKILFGERWLAVNPIVTERDHMMLTRKRGTEDSMHNVSQTFGSTSNRNSVLLAYERKKMVIGTEDPNAEPEYIVEAAIFDIDSWYYKRVPGRVSTDGTVLKQCAFLSTIKSNIRSEDVNDIGILTNEATDVSSFSSMVSDADQLFYPSALSFERVFVAKNTRIDWMKIQNIQDTILNKCAVKLPALIRNPEMISSVVMAAGLVRKNILSGSPNSSAAEINELQLSSDQKVLLNVIVYYGKIEEFCQLASRPDISDTLKRELAEWALHEAVDYKRTISDKMVSLFQGRSLALSPLAEESIAQGIKLFRVVYEYLKACSKALKDDRLRNLAHSVICMRNHTKLTSQFINFAIIPVDPIRQQRMKDLHSKRKNMARKNSSSLPVQSVVRKMNRQAPNAQFWNDIPHDEWYPPTPLDLLECLLNVSISESIKRELVVQYVIDWISTSPEDSEHSEKQLALETIKIMTNQMLNVNLEKIYYILDQGKKALTSSKTSDDMRALGEKVFSMKDDEISYEKLWGKDAPMTVTIGKHDLQRFEQRMKMQMEGGKVRLPVLDPESEILYQMFLFENEKFEAMSSEAISSNKLLSAFLPGMIKKDGRGRQKTAKEQEIEISVKKMFERKVQNDDEDMPEVFASVNDKTERKRKSSQFGEDDESSVSSSQYVPPTAKRIQQWKSAVESVANNSSINSITSPDSHQNAEINMMIATPARYYKRHNEEENVQDGFLSPAGNRPPPVSAHNSILKTAKGGQSASRGRIRFRADVPRGADESIEDNGRKGLALNFAILEDEEEETMTIRKSRSMGKHDEEKDSEKNVVDEMEEVKDQEQENDECIESEKTFENQDDFEVLEDTSAPEAANTENGSETPPMEDTFEVRDDDVMPPTDETYLSHLQTDKTGILEEEGEDEDIWDGVQRSFEVQMDEDCEAVPTIDVADDLESKSEEVNEEEVVESEEVQQDAKEPEKTEKRQEEPEPEVMQPVIPEEPQNESLESSIKLQEELQEEPDIVPTGDEDTADKVQEQAVEEDRPPSRNTRSSSVQKSTSQVEDRDPKELVEEERPPSRNTRSASVQKSSNQEKTSESGEVTEEDRPPSRNTRSASVQKSSSKVKDQKPEELIEEDRPPSRNTRSASAQKTVAANKSVLESEIPSRSASRRTRSTSLRNDTVAEPDETSVAMTTRRRTRATSEVVSKQSSEDDGRSTPKTGRTPTKKAAASTSSSRAGSVTRGKKSIIQKMPSPLEVTMEVQEEEEEEAEEERPASRSTRSASVKNTTVDPSSSALASTKRTTSRKRGNSETIDFNQDDKSAPTTPKRGRPAKKDAGSPKVGSKARGTKPKSIFENQEDEEDRSSSPDIEQPATPTRSSKRTARSRANSESIDDDSKQKTPKKKNAAVNEAGTSKQSRSVTRSRASSIDVQQEVEEPTTPKRGRGRPPKTVLENIEEGEEERKETAATPLLRSARRAKQ 1784 Q19131 Nuclear pore complex protein 5 npp 6239 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q19131 Pfam PF04121 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}. O17982 EBI-325671,EBI-318528 GO:0000777 GO:0031965 GO:0005643 GO:0031080 GO:0017056 GO:0007049 GO:0051301 GO:0034613 GO:0007059 GO:0051382 GO:0006406 GO:0002119 GO:0000973 GO:0006606 GO:0034501 GO:1900037 GO:0010965 GO:0097298 GO:0006355 MTDLFASGDNSSNSFDDSNDEIARKNETAFKYTTIFHTNLSEKLYHELCALAFGEFDIPQGQISPLMWTRLHEIYSEVEMQTRKLPAGSNYSASSQKYANEAVQIASVLSIYTALAHEYDETVEVSLLSKLVVEDVEFRRIYALLLWSEKAISEQQYEKGLGDKVRKLEGIKSSRINSMMALKRPTFGAANAPKDASLDPDAPGTKEDQALEQMAMNVFFQLIRSGETSKAANLAIDLGMGAIGAQLQLHSMLRNPLDIPLEASKQNFGEYKRSRRAKYYQMTQKLIEQSQGSEDDAYWMLISAIRGNIQPMLKAGKSVIEKVWAYANSAVLARILAAEGAMTQETISTLFNVPLTSKSILDELRSEADRTKEVYILLRVIDDMLNDDIEDLYKFANETVGEFVPNDKNCQVNMLALDIFFHLVAVSYASGFEPNDDGNAVIILGFDDLRARSGTSSHKKMAAFYSRFLPEDMKLPEIVETMKAVDSDEEREILAESLKQSDIDFGRCACTLIEQIRKDDKTKVVTLEEQIDHWHWLLIGGEETALAALEECNRLVRKVMLSTPIDESVIRQIIRKALHFEVPKLLSQAVENEATVLSLITDGTLFEQKPGSQLAINKIEHAALEFYGLCSFVDVNNFMITIALKLGLMFKYTPITDDELSMIGGVKRLDNTTAADWEASLRVRARAEQTLREEVLKKRAAEHNTRVGMVQQHLDTVLPMLRGLVNNIGVRPEYFLSPRANGDPMRVHRKEIQEIRNLFLPQFFILLAQAAVRLDDTTNFNDFFTSFNNDLGLDQEWMVFIKAFYAELNLKVE 813 Q19253 Transducer of Cdc42-dependent actin assembly protein 1 homolog toca 6239 Yes SL-0198 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}. UNIPROT Q19253 UNIPROT Q8MQ82 Pfam PF00611 Pfam PF00018 PROSITE PS51741 PROSITE PS51860 PROSITE PS50002 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}. P39055 EBI-6533634,EBI-317945 A0A1C3NSL9 EBI-327553,EBI-6533634 O17578 EBI-6533634,EBI-2412885 Q09442 EBI-2316106,EBI-6533634 G5ED57 EBI-327853,EBI-6533634 Q9XZI6 EBI-6533634,EBI-311866 B7WN72 EBI-2914750,EBI-6533634 Q93343 EBI-6533634,EBI-6533726 Q20877 EBI-315480,EBI-6533634 Q19782 EBI-6533634,EBI-320224 Q20010 EBI-6533634,EBI-327608 G5EFY6 EBI-6533634,EBI-317770 Q94246 EBI-6533634,EBI-6461124 O01900 EBI-315098,EBI-6533634 G5EF97 EBI-6533634,EBI-6533878 Q9U304 EBI-6533634,EBI-329038 G5EC72 EBI-6531450,EBI-6533634 A8WFL0 EBI-6533929,EBI-6533634 A5PEX6 EBI-6532321,EBI-6533634 Q4VNJ8 EBI-2918529,EBI-6533634 Q23571 EBI-6533634,EBI-330837 O17577 EBI-6542250,EBI-6533634 O61701 EBI-6533634,EBI-6537266 Q95QQ9 EBI-6533634,EBI-2317344 Q1XFY2 EBI-2316564,EBI-6533634 G5ECJ4 EBI-6533634,EBI-317668 F5GUF0 EBI-6542338,EBI-6533634 Q95QA6 EBI-6533634,EBI-327642 A8XQ35 EBI-6533634,EBI-6542385 GO:0016324 GO:0016323 GO:0005911 GO:0097708 GO:0048471 GO:0005886 GO:0055037 GO:0048613 GO:0006897 GO:1904703 GO:2000370 GO:1901046 GO:0032956 MNDSCSWDQLWDQQGTLNEYTGKGIDLLERIMAYSKERASIELEYSSKLKALSKKTAMKMKSESELWNSVSYVKGFHDVIAGIVPVATQHELIAENLKSAVIPFTTQKIAEYRVAKKQLESDNSNLGKQLRMVIDEMAKSHKEYVKCYKETEAAMLKYAKAEKNMDISRLELEKTKNNYQQKCGMLEESKQTYAVMTTKANEEQSAHYDRKLPQLLDNYKKLHTNRILDTVEILSKCVEAESCVNQIIASCHNDMRRDIGLIDPSRDANLVVENMKSGHPVPQPFVFEDLGHPQDRSSFMGGGASGPAGSMDGMDATMKKGGTLMSKNGKGVARKQSMHQKFFGGGTADKKTDSGDYGTLPPQQRARKIAGKISDLEKEKDRATQSREGVSKMQAAYRENPKLGNPSDCDAQLAQYGHEIDALSNQIQKFKILLDDVNAQLGAGGLSATSVGGSDTPPSIRSVSSASSGVTSRVNTINDAHRTNGGVGGGRRESFSGSNGGSDTDPTINGNGHGRDELYEECSNPNPVLGEAIAQFAFDGAQDGTIRMEANEKLWLIEKDEGDGWTRVRKENNSADGFVPSSYLKVTWFGKV 592 Q19972 Chromo domain-containing protein cec-4 cec 6239 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792}; Peripheral membrane protein {ECO:0000305|PubMed:26607792}. UNIPROT Q19972 Pfam PF00385 PROSITE PS50013 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}. GO:0000793 GO:0005637 GO:0003682 GO:0035064 GO:0097240 GO:0045595 GO:0010468 MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQSDDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTPKSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDEDDDDEQREEVVTTAPVETKSRWGFGSWKWF 270 Q1ECZ4 Protein CASC3 casc3 7955 Yes SL-0198 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}. UNIPROT Q1ECZ4 UNIPROT Q7T1P0 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003723 GO:0000398 GO:0051028 GO:0000184 GO:0006417 MADRRRRRRRASQDSEEEDESASGSESGRSFSASRKTRGREPEPVESPAERVAAKSDDESECVSEDGVGEAVLSDYDSADLEENGSHTEGGEEEEEAEHFSEEEASRPAAESKPVADAPTEELVEGEERDESVKEVKADEKGNLAGERQSGDGQESTEDPENKGSKGQKLDDDEDRKNPAYIPRKGLFFEHDVRGQATEEERPKGRNRKLWKDEGRWEHDKFREEEQAPKSRDELIAFYGYDIRNGTGPSDGRSYRSRKPRHAGSPSREPRRYREGDKSVRSSWQGPPPGHRNAPQSVTVQSGQPLAPLSAPKPSGRPSTQPPQRSFQGSRAPSAPHRTEGRGPSKPSLDGAPLRGPRSQPVEGERGPRLRGRSSHAVHADRSPSLVVEDICSEEEEEEGEIPTATTTYTAHHYKTEKERVPSPRKQDSGMVMEGGSAAGQVRELSPPQERQVEKKSYSRARRATRTRPSDLSKQASLDDSSSAVQQAPVAAKSESWQEQSEAGTQSGLTGLDQDLARLSLTGQNWAQNPPSYLQAEMRGIRGSMHMAGGPPQYGNMEDMGVGGGRAKRYSSQRQRPVPEPAPMHIGVMEGHYYEPMTFQGPIYTHGESPAALPPQGMLVQPEMHLPHPTHPGLHPHQSGGPLPNPAIYAAPPVSLSPGQPPPQQLLPPPFYPPPGVMTFGNTNYPYPAGGTLPPMYPNPQAQSQVYGGVTYYDTIQQQAQPKRSPPRRSSNPVTVRPPPPEDQSRKAAEEIRS 754 Q1L911 Nurim nrm 7955 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q1L911 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 GO:0031965 MASVTFRDGFLCVSALITFVFVFVTGADFVRFVSFRAINHNLSGAAPLCRDSVPWSVALRDGVVQKAVAVDVLLLVVFSLQHSLLAWTPVKRVCQSVFGVLSRSVYCFTTAAALQILMHYWRPVTSAPCLWSVSSAPWEIWFPLICFIVHFLCWAIICSILLIFDYPELLGIKQVYYECLGLGDPLLLKSERAQRLYSHLRHPVCVELLTVLWLLPSFPLDRLLLAVFLTVYLILAHSLDKQDCAYLRHQLRNKLQLFSTPLEGSEQTNDNNKLE 275 Q1LX29 Telomere repeats-binding bouquet formation protein 1 ccdc79 7955 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q1LX29 UNIPROT A3KQ98 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}. GO:0005623 GO:0000781 GO:0000784 GO:0005637 GO:0003677 GO:0070197 GO:0045141 GO:0007129 MEATKTDLRLLLECLKYQMKWPGSQKQALLTIISICKQNDQYVEFLREIGGISFIYNLSKSSTFSQVKETALFTLASLAELHESCKQALCREEMFRDFVQHLEQEMPLTEKRVAVYMLSVLVANNRCGQTLAKTSRCIEALLRLFRQSFPVPGESYEQLQLWITVSSALCGSVNNPQNEENQNVCMSVFPEIKPWLQEVALPRAELAQPLCSFIGMTVANNPCAQEYFVSVGGLDSLSDTLTRVLSQSTHSASVCKMATIITKTLSACISNNELLGSSLSKLRVIPGLLRLLSSPNLDPQDQLAVVLTTGHLTDACVEQQSQLLSAGGLPIIITLLTETSDEELKKAAIFVLHTCNRITESLGPGMSTIDPNECDREGQWRSAGQILQRIQLLEKKIGKKLWERDPESQPHSMKRSDSHVECDDELWEGSVMRKVKGNHRVYGEFRAIPAGTPITSEILQDQDSLQPDSSEEGLSPVQVNLFKGPNWEKSKKRKHKQKRENERSDNQETRREGVNKRELKRNVKSERVVKRLKMMNLESDDDGYELLQNCSTPTEGNRDTQGPDIFRHPDPVKRNQREPSLSDDNMSLCTELLDKEINKFLKPPSASKSNTLRCAGCVKHMNELNSRSFGAVLSSCRFQCDFHLTLREAEDRFRRSQPLKRTSHTPTHTHINTHRKIREHSTSAQEHKQKSKREKHKLSHQSSDRCYRLTPLRRPRETYSPDVKQWTDHRHLKKSSEDARSKNSSGRHRKRQNWSDKELCYLTKGVKRFGHSWNTILWKYPFHPGRTNVDLAKKFYHMQKAKAQGVDLSVAKAL 814 Q1LYM3 Protein spire homolog 1 spire1 7955 Yes SL-0198 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}. UNIPROT Q1LYM3 UNIPROT Q08BK5 Pfam PF16474 PROSITE PS51377 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}. GO:0032154 GO:0030659 GO:0005856 GO:0005829 GO:0048471 GO:0003779 GO:0045010 GO:0070649 GO:2000781 GO:0015031 GO:0016192 MTDGGMLISPSALQDPGDGARPEDIAMDCTDGEEELCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKHRRKETGVSPPGRIAGPGDVRIRKDGNVKLYQPSNPDKHTPPSSSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETDCPDEGYEATEEEDEGEEENAEVSNVRGYRDIISLCLSHLPSPSDAPNHYQAVCRALYAETKELRTFLEKIKSAKENLRKMEGETEEPVRDLNELQNADWARFWVQVMRDLRHGVKLKKVQERQYNPLAIEYQLTPYEMLMDDIRSKRYKLRKVMVNGDIPPRLKKSAHEIILEFIRSRPPLNPVSARKLKPHAPQPPTLHERILEEIRSERKLRPVSPDMIRRSRLGAGKSISTPQDLFRSSDIPDGPRKLAISTLSLANGTSPARSPVNGVAGGHSLSQRKRLLKAPTLAELDSSDSEEEQSTRKSDSSSSISTSLVEDTSPESVMGKKPPPQFLPISSTPQPDKRIAPQRRHSIEKEAPTNIRHFLPPSRQNSKSLAHALGSGHAEEFCFPVECLTLTVEEVMHIRQVLVKAELEKFQQYKDIYNALKKGKLCFSCRSKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPISSLGPSILPKKEPGASSAPTDKTSSTSSHKKNSLQRSLSRSSKHGDRSSSKDELELPEQFTEDWSTMEVCVDCKKFINDIISNSRRNLSTKRARLHRRTHSVYSSSTSSSNYKPTERTIKEV 761 Q1XG89 Putative ATP-dependent RNA helicase TDRD12 TDRD12 7091 Yes SL-0178 SL-0182 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}. UNIPROT Q1XG89 UNIPROT H9JJS3 Pfam PF04969 Pfam PF00270 Pfam PF00567 PROSITE PS51203 PROSITE PS51192 PROSITE PS51194 PROSITE PS50304 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}. GO:0005694 GO:0005829 GO:0031965 GO:0043186 GO:1990923 GO:0005524 GO:0003676 GO:0003724 GO:0030154 GO:0031047 GO:0051321 GO:0007275 GO:0007283 MASDYYQVEILHYLNPNLIWVEVLNSPNEISFEQLGVYGILPIDASLDVERPGLKLQRSEDWMPATAILMKNIFQNLEQVWFSPTHIDRRSSIFDNNIHKYGELIIKKNGVQLYLSKELVKAGLATEDPCQFHQYMSLGKIKTKLSNTETRAVIKNLEEYYRKSSKPKELWQKSVHQNTSIFHAGERLQALTVKNLERHNNRQNIMLLENKLKDLEQCKGSDEVSLGRGVCRVPSNKSEMVMLTNKRLKNRLELLSKINMKSDATDAVKSTKRNFSGDGQRKNFENDFESDDESVKKVSIANTINTSDGSANVVDKLLDEKQIDNVFNNKKQICYTESTRRNPVKKAACIVYGPPSINIDKLPLKEAPKMTKTVKWTPHVDCDKEASEVSFGDVDSHVKLDVKNLDKFHEIADRIEIEKTIPVDVNIHKDLYDSMINNKNESESKIMETANLKTEMKNLRKSSILQSKLKQFDKFNVSSNSAASESSTKSSMDSSRISDEDDLSSDDEMSEIMETFKLNLATPKKSEAKHTIDHIEVNNTKLNANPFKNLDGSKSVFVDKLTSPVLLVHTKRNNKVQPCSLLRDVPFGTSIHVVLRNMGIKHPTRLQTVSWGTILRGLSTFLISPPRSGKTMGYLPAVCRLVRDFRKESPDSCGPKCIIVCATSKSVSEVERISKMLLGLEDKVFACYSGMDNLSVTTALLNGCDLLICTPKSIVRLLQNDLSVDLRDLTTFVVDDCERISDVYSNEVKYVLYEIKNMLKNRVNKELKVQIVVASRIWCDFLEPIVLKAPDSVVCIGAFQELILYSKISTTVDFLRPENKIANVLQFIDSVQGPKRTVVVCRADNEVKAVESSLRYNNRVVFACDNTMNIHDLYNLNVVWGDFEDPTLGPILVCCDSNLVHLNVTDASYLIHYSLPALFSTFCKRFSVLNDNYPSIFKNESRDLKVKVLMDESNVEQLPKILNFLKRCTENVPKILDEVSEKILNEKDLAKVKDLVPLCDNLLSLGICPDTWNCTERHRIFKECDSPADWIPKNGVVTFQILYFHSAVMYSARLLSNTVDGETTKYPQTYSTLSLKMGMYFSKESSRRLHGIPMVGDVCAVSKKQNFFIRCQVVKIISFYKNGNPNYVVIKLIDEEKFEQSRDIYLYHLPDEFKDMKTYVVQVRLANIQPQDKDITFSCLAKNELEKIVEKNEDLFMRGHVAMSVGSCIFVDTLEACLDLSSLSETVVRHNFKQELLNAHAVPNPKHLSILEEMCEKSGLIVKAVTNEQVVPKPIPVLPAAQWAHLEDDLSSVYLASVEDMDKLFVRLVKFESCMKLLNIEINKYVSENTVPLDGSNVGDIVLAKFPDDSMYERARIDHIYSEDKVKCFFVDQGDWRDVSTNDLATITENFITQLPFQAIECRLIGIRPFGEQWTEFSTNWFSDHCFEDAKGNLKHLYVKHFTKEKADCTGGHKYGVALIDTYTNEDIIVNQLLIDLNLAKENVDEIAYLSEIKCNKTVLNNDATVDEEEGSLSGVSEPESNINVPLDKVFLKAPIRSVPLVDSEYETSDSDTWQINRPEDFKALFMRTRPESSKIIPMITANEVQNNADGETSKDTSTILEEKGQLPEKVKDDELKLSKPKICWSQNKNTVKLKILIAGIEDYKLKIEDRAVAFSANHCDVEYGFKLELYGVVDVNKSRHSNKGQYVLVTMTKLMCRNWLALTKEGDSQKWIVYDVDTIEASSDEEVYRDDTLEVIKNIHNTNNGSDSEDDDFLDDVS 1759 Q1XHX8 Nurim NRM 9598 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q1XHX8 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 GO:0031965 MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLMAAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLRYLRAQLQRKLHLLSRPQDGEAE 262 Q20745 Nuclear migration and anchoring protein unc-84 unc 6239 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q20745 UNIPROT Q9U475 UNIPROT Q9U476 Pfam PF07738 PROSITE PS51469 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}. P34258 EBI-322705,EBI-313630 Q23064 EBI-2902228,EBI-313630 O45904 EBI-313630,EBI-316320 G5EFL5 EBI-313630,EBI-316352 P90740 EBI-313630,EBI-313626 GO:0005737 GO:0005856 GO:0016021 GO:0005635 GO:0005637 GO:0005521 GO:0043495 GO:0040011 GO:0007399 GO:0006998 GO:0007097 GO:0030473 GO:0018991 GO:0009791 GO:0030334 GO:0040025 MAPATEADNNFDTHEWKSEFASTRSGRNSPNIFAKVRRKLLLTPPVRNARSPRLTEEELDALTGDLPYATNYTYAYSKIYDPSLPDHWEVPNLGGTTSGSLSEQEHWSAASLSRQLLYILRFPVYLVLHVITYILEAFYHVIKITSFTIWDYLLYLVKLAKTRYYAYQDHRRRTALIRNRQEPFSTKAARSIRRFFEILVYVVLTPYRMLTRSNNGVEQYQYRSIKDQLENERASRMTTRSQTLERSRKFDGLSKSPARRAAPAFVKTSTITRITAKVFSSSPFGEGTSENITPTVVTTRTVKQRSVTPRFRQTRATREAITRALDTPELEIDTPLSTYGLRSRGLSHLNTPEPTFDIGHAAATSTPLFPQETYNYQYEEATGNKIKTAFTWLGYLILFPFFAARHVWYTFYDYGKSAYMKLTNYQQAPMETIHVRDINEPAPSSSDVHDAVGVSWRIRIADFLSSFVATIVEAHQVVFAMFKGGIVETVSYFGGLFAGLTDKKSSKFSWCQILGLLLALLFAIFLLGFLTSDNTAIRVKEITKDKNASKKSEGSLPAVPIWISAANHVKHYTWMVKEFVVDIAFDTYNYGKSTIGRLGTTPRYAWDLIASGCGAVGNGLKSVLSSSFRFIDFCAGKLFYYGSDGFLSANKSIGTFFNGCYETLYNGCTAIVGHTKSFIYNASNAVYNFFSTIFAGLLNFSTSSQNSILSLLKSFGTGITNIFYNFIYAPIAGVFNFAGDNYMYFFNEVAAVFGKVYNSVVSVLKTVINWILFLIAYPFSLCTRAWIRISQYAPEDVVQVIPIPQAITPTPDVERIVEEPLRKVTDVEDEELVIIPAPAPKPIPVPAPTPAPVIIHQTNVVETVDKDAIIKEVTEKLRAELSAQFQQELSAKFEQNYNTIIEQLKMENTNIQYDKNHLEAIIRQMIYEYDTDKTGKVDYALESSGGAVVSTRCSETYKSYTRLEKFWDIPIYYFHYSPRVVIQRNSKSLFPGECWCFKESRGYIAVELSHFIDVSSISYEHIGSEVAPEGNRSSAPKGVLVWAYKQIDDLNSRVLIGDYTYDLDGPPLQFFLAKHKPDFPVKFVELEVTSNYGAPFTCLYRLRVHGKVVQV 1111 Q20924 Sun domain-containing protein 1 sun 6239 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305|PubMed:14697201}; Single-pass membrane protein {ECO:0000305|PubMed:14697201}. Nucleus envelope {ECO:0000269|PubMed:24297748}. UNIPROT Q20924 Pfam PF07738 PROSITE PS51469 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}. GO:0016021 GO:0005635 GO:0031965 GO:0043495 GO:0051642 GO:0009792 GO:0006998 GO:0008104 GO:0010824 MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYKEITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFHQTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTPEKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVLSPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQEQFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA 473 Q21443 Lamin-1 lmn 6239 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q21443 UNIPROT O62127 Pfam PF00038 Pfam PF00932 PROSITE PS51842 PROSITE PS51841 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}. G5EEH9 EBI-6455549,EBI-314110 Q18508 EBI-314110,EBI-2002730 Self EBI-314110,EBI-314110 G5EDM4 EBI-314110,EBI-313674 Q09284 EBI-314110,EBI-2915600 G5ECZ8 EBI-2915667,EBI-314110 C1P635 EBI-2917046,EBI-314110 Q7JLR4 EBI-2415541,EBI-314110 Q9XTB5 EBI-314110,EBI-2535391 O44548 EBI-2002279,EBI-314110 G5ECR7 EBI-330567,EBI-314110 P34402 EBI-1570073,EBI-314110 Q19749 EBI-320763,EBI-314110 Q9U3C1 EBI-314110,EBI-2004353 Q21295 EBI-314110,EBI-2004307 O01585 EBI-2004403,EBI-314110 P30642 EBI-314110,EBI-311981 P91457 EBI-2004585,EBI-314110 Q86S68 EBI-3902879,EBI-314110 Q95XY1 EBI-331661,EBI-314110 Q65XX1 EBI-2004375,EBI-314110 G5ECG0 EBI-314110,EBI-320612 Q95QC4 EBI-314110,EBI-331795 O02217 EBI-1187455,EBI-314110 Q8WQC0-3 EBI-6459543,EBI-314110 P39745-1 EBI-6455829,EBI-314110 Q9N583 EBI-6460139,EBI-314110 Q09601-1 EBI-314110,EBI-6455756 P12114 EBI-2001946,EBI-314110 Q8MPS6 EBI-314110,EBI-6457529 Q23593 EBI-6460566,EBI-314110 Q09583 EBI-314110,EBI-315406 Q17391 EBI-593075,EBI-314110 P91505 EBI-314110,EBI-326040 Q9XXH8 EBI-314110,EBI-312159 O01527 EBI-314110,EBI-6726969 Q9GYG1 EBI-314846,EBI-314110 O62090 EBI-314110,EBI-2917690 P34288-2 EBI-314110,EBI-11465290 Q8WQC0 EBI-6499941,EBI-314110 Q95ZY7 EBI-11468703,EBI-314110 Q965F9 EBI-314110,EBI-11465387 O44452 EBI-314110,EBI-314097 Q19633 EBI-314110,EBI-320052 Q19969 EBI-314110,EBI-317340 GO:0005638 GO:0005635 GO:0005637 GO:0034399 GO:0042393 GO:0042802 GO:0005198 GO:0008340 GO:0009792 GO:0007281 GO:0030473 GO:0031081 GO:0006997 GO:0008284 GO:0008104 GO:0051983 GO:0007346 MSSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVHHVSFSSGGASAQRGVKRRRVVDVNGEDQDIDYLNRRSKLNKETVGPVGIDEVDEEGKWVRVANNSEEEQSIGGYKLVVKAGNKEASFQFSSRMKLAPHASATVWSADAGAVHHPPEVYVMKKQQWPIGDNPSARLEDSEGDTVSSITVEFSESSDPSDPADRCSIM 566 Q22663 Globin-like protein 26 glb 6239 Yes SL-0178 SL-0180 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}. UNIPROT Q22663 Pfam PF00042 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}. GO:0005737 GO:0016020 GO:0005652 GO:0005886 GO:0020037 GO:0046872 GO:0019825 GO:0005344 MGSSTSTPAPPPKKNKPEGRKADNQILNSYQKSIVRNAWRHMSQKGPSNCGSTITRRMMARKSTIGDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYRRSKGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQLRFGYSRGLHVQGSRETKEDDEE 183 Q22747 Transmembrane protein 201 homolog samp 6239 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q22747 Pfam PF09779 Plays a role in nuclear migration in hypodermal cells. {ECO:0000269|PubMed:25057012}. Q94420 EBI-320790,EBI-324189 Q21021 EBI-2003933,EBI-324189 Q9N5U1 EBI-2005375,EBI-324189 Q9U2Z1 EBI-324189,EBI-2006699 H2L0Q6 EBI-324189,EBI-11466777 O17915 EBI-324189,EBI-324099 GO:0005639 GO:0005635 GO:0031965 GO:0051015 GO:0005521 GO:0009792 GO:0030473 MEVAAAVGVIASVPILYKAIRPRIKTSVECWFCRKSTKVEYQQRNSFTCPSCEQYNGFTEDGDYNRRIPGQAWTTPKRYCEPGKMQSEKPSTFLDRFGGVNMSPKASNGLCSECNLGQEIIMNKVAEFEPIDEDRWNEELEDYRYKLERMYQLCPRCTIQVHGKLEEDKKKYSYLLKVKYKLKHAIGSTLREVMNNQKRSRRFFFAGGSTCEALHFGCLISSIILFLANIDFLQQDAGASLINLPKALQDILPEVYKYSFVINFLIFTTHLIAAFNNKCRVTLPDLLLPILLILAMLTVLTSSDNLSQDVALVRGACASFSTILSMAVTLLPRKKLHKKRPNKIVSSAFSVASTPISQCSSQNSRNASLLDHDHTILRRSPHTPSASPPAMNSSPPLLREITNGPVWSAMRSRENKENMQSYQTKPNNHVESMDWDDSESMAAQSVAQSTRSSHFKPGLLSRNINERMTAQQLTPSVANLNLDTRSVDSPSIFSRQHRQMAQQQNHTPTRSLFGPPRSMVASQYDRSHYMAPEAHTRPGSVFTSVSQQDGHSTVSGAWQCRVIGILFALVFIVLIMQIGLFYVLFTRN 588 Q22799 Dynein light chain 1, cytoplasmic dlc 6239 Yes SL-0178 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}. UNIPROT Q22799 Pfam PF01221 PROSITE PS01239 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}. Q17902 EBI-328330,EBI-328324 Self EBI-328324,EBI-328324 Q23064 EBI-2902228,EBI-328324 Q23064-3 EBI-328324,EBI-2902257 G5ECT7 EBI-328382,EBI-328324 C6KRN1 EBI-328324,EBI-323135 Q9XUM8 EBI-328324,EBI-328132 Q19207 EBI-323336,EBI-328324 Q7K714 EBI-328324,EBI-2005487 Q19816 EBI-328324,EBI-328360 Q18529 EBI-328324,EBI-314884 Q17902-2 EBI-17158122,EBI-328324 O45599 EBI-328324,EBI-319105 P30642 EBI-311981,EBI-328324 Q18194 EBI-2002421,EBI-328324 P46502 EBI-312846,EBI-328324 G5EFV3 EBI-1187461,EBI-328324 O45087 EBI-313406,EBI-328324 G5EBL8 EBI-328324,EBI-2003045 P34766 EBI-311911,EBI-328324 P91249 EBI-313893,EBI-328324 O45335 EBI-324368,EBI-328324 G5EG76 EBI-322231,EBI-328324 Q9XVX4 EBI-328324,EBI-328356 Q93572 EBI-319283,EBI-328324 P48150 EBI-328370,EBI-328324 O45436 EBI-313048,EBI-328324 Q19988 EBI-328365,EBI-328324 Q20805 EBI-328376,EBI-328324 P48154 EBI-321394,EBI-328324 G5EBX2 EBI-316840,EBI-328324 P55853 EBI-313647,EBI-328324 P34574 EBI-319001,EBI-328324 Q22696 EBI-328387,EBI-328324 G5EDQ5 EBI-320979,EBI-328324 Q9U2M6 EBI-328406,EBI-328324 P55954 EBI-328392,EBI-328324 Q9N432 EBI-328399,EBI-328324 H2L0C9 EBI-328416,EBI-328324 G5EBV6 EBI-328338,EBI-328324 Q18192 EBI-319458,EBI-328324 O16474 EBI-328348,EBI-328324 O17641 EBI-328342,EBI-328324 GO:0005737 GO:0005868 GO:0030286 GO:0005874 GO:0005635 GO:0045505 GO:0051959 GO:0003774 GO:0006915 GO:0051301 GO:0051321 GO:0007017 GO:2000582 MVDRKAVIKNADMSDDMQQDAIDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG 89 Q22908 Ras and EF-hand domain-containing protein homolog rsef 6239 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}. UNIPROT Q22908 UNIPROT Q21466 UNIPROT Q22906 Pfam PF00071 PROSITE PS00018 PROSITE PS50222 PROSITE PS51419 Binds GTP and GDP (By similarity). Plays a role in uterine seam cell development (PubMed:25281934). {ECO:0000250|UniProtKB:Q8IZ41, ECO:0000269|PubMed:25281934}. GO:0012505 GO:0048471 GO:0005509 GO:0005525 GO:0003924 GO:0006886 GO:0032482 MSKPEVENLFSLCDSESKGYLTMEDLRKVCPQLDDNDLRFIFTELDQDGSGKIEKLEFLRGFQDTVQHGESHGLNGMQRRASVAVEDPPMFLRDEQMFDSESDSTSSRPAIRVFDEEHYHSESDTNINIDFSVPCQEEVLVLYEQLQSSGVPALLRKFERVVGSFHKELSEKKHENERLQRIYASEREMYNRRMEEMESEVDQQLELTEMKARQEERDRLTKEKEEMRQRMSDEMSEMRNNIERLQKMEKALERENERLNHQKELSDKLKVVNEENNDLRQNLAENHLELAMIKSELAQVRCEFDQKQDELSARRGILFQLEPINSLSSSDQASHATEESESVRKQLQLLFDANRKLHETNESLRDALDSRASVLRQFNLRTPSPGLLSSNRNSVENFQTSTNVFRSVPLHAISTEEQGTIFGTIEEKTSLILDDAHSLQGLDTPGDLMGLNDANGPAERTFRIVMCGDAAVGKSSFVMRVIRRQFTNQLPSTLGVDFHVKTVNVDGRNVALQLWDTAGQERFRSLCKSYFRRADGAILVYDVCAEQSFLRVRDWIETIKESTERSIPIILVGNKVDMRISTPGSVAKTDGASMAAAMGVLFMETSALDGSNIDNAMLALTRELMAVEDVEIRSTGVVLNPAVAKKGGCFSKCRGS 656 Q23064 Nuclear migration protein unc-83 unc 6239 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT Q23064 UNIPROT Q95WB6 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}. Q20745 EBI-2902228,EBI-313630 Q22799 EBI-2902228,EBI-328324 V6CJ04 EBI-2006416,EBI-2902228 GO:0016021 GO:0005635 GO:0005640 GO:0045503 GO:0040011 GO:0007399 GO:0007097 GO:0030473 GO:0018991 GO:0009791 GO:0090435 GO:0030334 GO:0040025 MDVMDSFSEVEMPNDISSEDHLLKVIESSAEEVDIFLENCSSLYNLILDSLHNLTSKTISCECLDEMTSTLEKSAKKILAERPEAENSVLLRLNTICCAMDQLRVQHNSRMMSGADSDTASSARSSTSSSTGEMRLWLHEVERRLEINEKRIRVEPNLQLLLSDQQALQLEIQHEGQLLVNRLNKQIKDDHDSDSSEEEKRKTCVDAIRKRWHTIYLNSLSLVCRIEELINHQQASEDSESDPDLVGPPIKRARIRTVGHLTASDTEESEADEEDRHSQTETVVTEDDNVLPFAENEYESIMDGRVTVDSCTSSSEDQMVEQSTNKKWESVLQDVGYSSGENSIHEALNTCADHLVPETSDMRRKRIECSPVKAFYRTVQLEDMSDLEVTKAINHDVEEEPNLSDSMYVNHDSTFLATQNLPEYDEVMALMDDDDLPMDMSMTESFNTKWREIHGQKKPLRRASRPSREQMNLIAKSSCDASSEDSSEGENQTNLEDDPEMMSVSFNSAQFDTSSPLKRQRSARGLKNASFLYDSLEMDGSFCSTRSEMLPPCKTRSLARRKLRVRRMPRSMSDGEQLGVVSSKPEGMMTPMIRVSPPSTPVRRLLRKLDEQIRNRDSDTAPEHSDAAQAYEWDEYNPPQKDDSISDRHIQTMTDISDQLMNIDDDFAEHFGTSSAIRLIEESKSHLRVVLKALEESDSNIPQLSNFELIARSNLRQVDEALKIQSGNQPSFLETSTLQDLRSEWANLYESIRSPFARIMHQVKKFAATLQEVSSMASLGDVDIRSKEDVAKTLDAVTAIERRLSSERQELRDLLASSSFRDVAKDLSCEFESVSEGYDDAVDKIGKMAHSLSQVKGEWDAWNSRQNDIRNAMVRIESHLKEGQMDNKMIADEMELCQERMNSLETMCNYLTASLGSIQNESNSKNLPDFKAELSIYSNALARLKDRFNDMIRVPTPPTVQFHPPEPLPSLARSMTTQTAEMESETENEPLTIAEAISSSRLIKFTFALSLLAALAAIFYYHVFGKPFGPHVTYVNGPPPV 1041 Q23529 Zygote defective protein 12 zyg 6239 Yes SL-0178 SL-0182 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. UNIPROT Q23529 UNIPROT Q2V4T6 UNIPROT Q7JPD4 Pfam PF05622 PROSITE PS50021 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}. Q9U2Z1 EBI-1570263,EBI-2006699 P91409 EBI-1570263,EBI-326499 G5ED30 EBI-1570263,EBI-11465218 H2KYA1 EBI-1570263,EBI-11466183 Q93198 EBI-1570263,EBI-11468631 GO:0005813 GO:0005737 GO:0016021 GO:0005874 GO:0005635 GO:0031965 GO:0051959 GO:0008017 GO:0043621 GO:0051642 GO:0007059 GO:0031122 GO:0030705 GO:0009792 GO:0051647 GO:0035046 MLDLTNKESESSDNGNSKYEDSIDGREVGTSKPFKEERSLEDLQADLADMAVWMEGLDATKLPLNDPQLLCNGRAFSEVLHNVDKNFFTDGWLETMPENRTTNIMVFRSCTRKLWRKMFDYVNHINRTVVSSRWTDIHERIDGIYESDLPAMVNLGMAVVTLAHIGKNAKRFVDYSKALTSTHKSMMSNVAKMVTTVIDEMPENPCFHEISELHGSQSELNSLSESSGKLNGNGSSERRSNADQILVDAELEIERLRTETENQRKEIERLTKSFETAQHDMSSNSESGDISILEKQNEELRQKRRELEEKNLELDAAVDQFKGIVFELTNENDVLRRSDKERQRLQTVLDAAQSDLDEWKTVANQYQKEAELSKQQDKEIKELLSQNKALKSRLDHHVKSATLEDANKNGIAQLRTQVGGLTALNTELKASLDSKKRCVEQLEIQLIQHKEKVKELEDRKDELIEERNRLENQLIFKEAVTPRSLHESMFEAGNLSFEPFSEKNTLPLEIENKRLTERIQELESLEPLKGELITLKSKNGVLEEEKLFATKQIEELQQQIEDLQENLLKNQEHASGDVVGLKIQLEKAEVEAQQMREAKMRAETNQAQVDEILKKRTAELEVNATALQKAKAVIDELEYNSRPVSEDSMTSVQAFKEMKEENEKLRQKVEKLEIELNTVTQGFEQENRLLTSASHQQVLNRSIDEVMSMRAHAGSEEPQTLLDTQKMSGALPWRSLASETRRELPTAMASILVLGFLVFIAWMFININSALNAPPNA 777 Q23544 Protein adenylyltransferase fic-1 fic 6239 Yes SL-0178 SL-0182 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}. UNIPROT Q23544 PDB 5JJ6 PDB 5JJ7 Pfam PF02661 PROSITE PS51459 PROSITE PS50005 PROSITE PS50293 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}. GO:0005737 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0005524 GO:0016787 GO:0070733 GO:0050829 GO:0018117 MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSSPPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHDEISIDDILEMHRRVLGNADPVEAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSDNILNSGDSKLTPEESEVSEKIEAECRAGN 508 Q24246 Cytoplasmic dynein 1 intermediate chain sw 7227 Yes SL-0178 SL-0182 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. UNIPROT Q24246 UNIPROT O96508 UNIPROT O96510 UNIPROT O96511 UNIPROT O96512 UNIPROT O96513 UNIPROT O96514 UNIPROT O96515 UNIPROT O96516 UNIPROT Q5U0Z1 UNIPROT Q86BQ5 UNIPROT Q9NG49 UNIPROT Q9TZR7 UNIPROT Q9TZR8 UNIPROT Q9TZR9 UNIPROT Q9TZS0 UNIPROT Q9VR78 PDB 2P2T PDB 3FM7 PDB 3L9K Pfam PF11540 PROSITE PS50082 PROSITE PS50294 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}. GO:0005868 GO:0005765 GO:0005874 GO:0043005 GO:0031965 GO:0032991 GO:0034452 GO:0045504 GO:0045503 GO:0003774 GO:0008088 GO:0007349 GO:0051642 GO:0001754 GO:0000226 GO:0007018 GO:2000582 GO:0034501 GO:0007291 GO:0007051 GO:0010970 MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMTSDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDYVMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQPSRDEWSRFNTHLSEIKMNQSDEV 663 Q24568 Netrin-B NetB 7227 Yes SL-0198 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}. UNIPROT Q24568 UNIPROT Q9VY23 Pfam PF00053 Pfam PF00055 Pfam PF01759 PROSITE PS00022 PROSITE PS01248 PROSITE PS50027 PROSITE PS51117 PROSITE PS50189 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}. 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EBI-3406532,EBI-3407775 O61735-2 EBI-3406532,EBI-440389 Q9VBW3 EBI-3406532,EBI-3404264 Q7K4B4 EBI-3406532,EBI-3407113 Q9VZP5 EBI-3406532,EBI-171044 A1ZBB4 EBI-3406532,EBI-170192 Q8MV48 EBI-3406532,EBI-106149 Q9W1G7 EBI-3406532,EBI-180893 Q9VHX9 EBI-3406532,EBI-149978 Q9Y1T2 EBI-3406532,EBI-114593 Q9VG29 EBI-3406532,EBI-3406349 Q95TU2 EBI-3406532,EBI-139966 Q9VPP2 EBI-3406532,EBI-195064 Q9W1D3 EBI-3406532,EBI-3407150 A1ZAK1 EBI-3406532,EBI-148930 Q9VA35 EBI-3406532,EBI-2890306 Q24141 EBI-3406532,EBI-183986 Q9V6U9 EBI-3406532,EBI-177823 Q9VEF7 EBI-3406532,EBI-3406312 Q9VUM0 EBI-3406532,EBI-169029 Q9VNC3 EBI-3406532,EBI-3406471 Q7K0F7 EBI-3406532,EBI-179939 Q9VBR7 EBI-3406532,EBI-3408097 Q961D3 EBI-3406532,EBI-180605 Q7KRY7-2 EBI-3406532,EBI-3404221 Q9VF20 EBI-3406532,EBI-104505 Q8SX64 EBI-3406532,EBI-3406194 Q9VP43 EBI-3406532,EBI-3406500 Q9VS54 EBI-3406532,EBI-86020 Q9VXU8 EBI-3406532,EBI-188191 Q9VZK2 EBI-3406532,EBI-163256 A1Z9I9 EBI-3406532,EBI-171485 Q9V9X8 EBI-3406532,EBI-137454 Q8MSQ4 EBI-3406532,EBI-870203 Q0KHR4 EBI-3406532,EBI-99044 Q9W1S1 EBI-3406532,EBI-3407772 Q9U3W7 EBI-3406532,EBI-9944840 Q9VWJ0 EBI-3406532,EBI-3406496 Q9W4X1 EBI-3406532,EBI-143242 Q9W205 EBI-3406532,EBI-112086 Q9VRC8 EBI-3406532,EBI-128793 Q9VVG4 EBI-3406532,EBI-168923 Q9VT32 EBI-3406532,EBI-146688 O61307 EBI-3406532,EBI-118556 Q9VGW1 EBI-3406532,EBI-139913 Q9W3Y7 EBI-3406532,EBI-115606 Q9VU76 EBI-3406532,EBI-156334 Q9W1A0 EBI-3406532,EBI-161680 Q9VG43 EBI-3406532,EBI-2890546 Q9VS63 EBI-3406532,EBI-3404012 Q9W1U2 EBI-3406532,EBI-91105 Q9W472 EBI-3406532,EBI-3406460 Q9VFG4 EBI-3406532,EBI-3406481 Q8SWW4 EBI-3406532,EBI-98746 Q9W1W0 EBI-3406532,EBI-116547 Q9VHB5 EBI-3406532,EBI-169701 Q9W1A4 EBI-3406532,EBI-91385 Q9VM62 EBI-3406532,EBI-2507813 Q9VRF2 EBI-3406532,EBI-3406415 Q9VLN6 EBI-3406532,EBI-3407882 Q9VGI5 EBI-3406532,EBI-3406455 Q9VN58 EBI-3406532,EBI-3407755 Q7JR75 EBI-3406532,EBI-3406647 O46067 EBI-3406532,EBI-3406881 Q9VAE4 EBI-3406532,EBI-153347 P40301 EBI-3406532,EBI-98978 Q9W0Z5 EBI-3406532,EBI-94769 Q8IPL3 EBI-3406532,EBI-3407968 Q9VAU5 EBI-3406532,EBI-153806 Q7KU30 EBI-3406532,EBI-130703 Q9VCH1 EBI-3406532,EBI-136479 Q9VW47 EBI-3406532,EBI-139710 Q9W278 EBI-3406532,EBI-3406916 Q9V9W5 EBI-3406532,EBI-108326 Q9VUC7 EBI-3406532,EBI-177260 Q9VLI2 EBI-3406532,EBI-109911 Q86B79 EBI-3406532,EBI-90517 Q7Z020 EBI-3406532,EBI-3433727 Q8IM95 EBI-3406532,EBI-3407269 Q9VHD1 EBI-3406532,EBI-148163 Q7JV09 EBI-3406532,EBI-141560 Q9U3V5 EBI-3406532,EBI-3407583 Q9VQ61 EBI-3406532,EBI-129434 Q9VFI3 EBI-3406532,EBI-152984 O77410 EBI-3406532,EBI-111126 Q7KQM6-2 EBI-3406532,EBI-3406403 Q9VL96 EBI-3406532,EBI-157240 Q9VSM6 EBI-3406532,EBI-86489 Q9VP16 EBI-3406532,EBI-111934 Q9W0E3 EBI-3406532,EBI-3407605 Q9VW80 EBI-3406532,EBI-3407048 Q07886 EBI-3406532,EBI-3406559 Q9VJF6 EBI-3406532,EBI-126430 Q9VAW3 EBI-3406532,EBI-171618 Q9V7P1 EBI-3406532,EBI-138088 Q9VHH2 EBI-3406532,EBI-3406245 Q9VY63 EBI-3406532,EBI-3408068 Q9VUE8 EBI-3406532,EBI-2507788 Q9W093 EBI-3406532,EBI-3406537 Q9W0S9 EBI-3406532,EBI-94338 Q9VMQ4 EBI-3406532,EBI-3406282 Q9VAS7 EBI-3406532,EBI-82460 Q9VLM8 EBI-3406532,EBI-3402873 Q9NFV7 EBI-3406532,EBI-3403514 Q7KTX8 EBI-3406532,EBI-110730 Q9VWI5 EBI-3406532,EBI-3407255 Q9VAH7 EBI-3406532,EBI-2509120 Q9XZS9 EBI-3406532,EBI-3403938 Q9VTC1 EBI-3406532,EBI-90688 Q9VPM5 EBI-3406532,EBI-178893 Q9W592 EBI-3406532,EBI-122425 Q27294 EBI-3406532,EBI-2890847 Q5BI50 EBI-3406532,EBI-191142 Q9VNX1 EBI-3406532,EBI-115702 Q0KIF4 EBI-3406532,EBI-146233 Q9V9Z9 EBI-3406532,EBI-243148 A1ZAJ2-1 EBI-3406532,EBI-3406636 A1Z6W6 EBI-3406532,EBI-155731 Q9VDY9 EBI-3406532,EBI-178694 Q7KTW3 EBI-3406532,EBI-2509116 Q9V3X4 EBI-3406532,EBI-3408088 Q9VW64 EBI-3406532,EBI-3407961 Q9VPH6 EBI-3406532,EBI-164999 Q7JVN6 EBI-3406532,EBI-84801 Q9VJ21 EBI-3406532,EBI-160882 A1Z9I3 EBI-3406532,EBI-3406677 Q9V9K7 EBI-3406532,EBI-283668 Q9V9T2 EBI-3406532,EBI-3407405 Q4V5M2 EBI-3406532,EBI-193476 Q9V895-1 EBI-3406532,EBI-3407136 Q9VK72 EBI-3406532,EBI-3407031 Q9W1S3 EBI-3406532,EBI-2509178 I0DHL3 EBI-3406532,EBI-9944848 Q9VAY6 EBI-3406532,EBI-162110 Q9VTG7-2 EBI-3406532,EBI-3407949 P08155-2 EBI-3406532,EBI-3407648 O46040-1 EBI-3406532,EBI-3406861 Q9VY78 EBI-3406532,EBI-3406749 Q9VWQ3 EBI-3406532,EBI-3407660 Q9VL52 EBI-3406532,EBI-2508552 Q9VX34 EBI-3406532,EBI-3407051 Q9VHB4 EBI-3406532,EBI-3406586 Q9VLP5 EBI-3406532,EBI-191609 Q8IPP9 EBI-3406532,EBI-3407937 Q9VIK0 EBI-3406532,EBI-102051 Q9VU11 EBI-3406532,EBI-3407566 Q9VR59 EBI-3406532,EBI-153960 Q9VQ36 EBI-3406532,EBI-164303 A1ZB09 EBI-3406532,EBI-3404157 Q9N6D8 EBI-3406532,EBI-122286 Q9VGU5 EBI-3406532,EBI-88232 Q86BS3 EBI-3406532,EBI-109513 Q9VUK7 EBI-3406532,EBI-164419 A1Z7L8 EBI-3406532,EBI-103891 Q9W213 EBI-3406532,EBI-151958 Q9VKU2 EBI-3406532,EBI-3407461 Q8IN81 EBI-3406532,EBI-196787 Q7KNA0 EBI-3406532,EBI-131459 Q7K2B0 EBI-3406532,EBI-2507846 A1Z8R2 EBI-3406532,EBI-2508444 Q9W3K5 EBI-3406532,EBI-3406992 A1ZAD3 EBI-3406532,EBI-2890523 Q9VU57 EBI-3406532,EBI-3406724 Q9W0S2 EBI-3406532,EBI-3406974 Q9VD46 EBI-3406532,EBI-86484 Q7K3L1 EBI-3406532,EBI-191301 Q8MRN4 EBI-3406532,EBI-1109586 Q9VNH1 EBI-3406532,EBI-1629458 Q9W0S7 EBI-3406532,EBI-131216 Q9VPT4 EBI-3406532,EBI-3406206 Q9W3E2 EBI-3406532,EBI-3407921 Q86B72 EBI-3406532,EBI-3407501 Q9VX14 EBI-3406532,EBI-3407350 Q9NGK5 EBI-3406532,EBI-3407445 A1ZBF7 EBI-3406532,EBI-3407533 Q9VHL1 EBI-3406532,EBI-176306 Q94538 EBI-3406532,EBI-6895101 GO:0044295 GO:0005604 GO:0031012 GO:0043025 GO:0048471 GO:0009887 GO:0007411 GO:0048749 GO:0016358 GO:0070983 GO:0008347 GO:0008045 GO:2000289 GO:0007432 GO:0016200 GO:0008039 GO:0009888 MVRATGTRMGLLLPIILALAIGSSAAGISSNDPCYFEGKPRKCLPSFVNAAYGNPVQASSVCGAQQPERYCELLRDGNAGECRSCEQQRYGPAALTDLNNPSNVTCWRSGAVNVPHDPDSAPPDNVTLTLSLGKKYELTYISLSFCPRSPRPDSLAIFKSSDFGQTWQPFQFYSSQCQKFYGRPDRAKISKFNEQEARCINSQHDTGGAAQRFAFNTLEGRPSANDLDSSLVLQDWVTATDIRVVFHRLELPPQLLKVKNANAFSDEMGGSREEDEDDDADLELDGEQDEYDYNLQDNDSADAGYDEYEEPKKHLELDDDHLHLDYASDGESVVKRQGKHKGSAYEKHYQSKLAATTPPQQPPKVTPPGKVTPPSTAAPSAAASAVTLPISQHYAVSDFAVGGRCKCNGHASECVATVSSGSGTALSDQDDGQDEDTPSAPSLANHFGRSTQMSAKLTMTCACKHNTAGPECERCKPFYFDRPWGRATDNDANECKMCQCNGHARRCRFNLELYKLSGRVSGGVCYNCQHDTTGRYCHYCREGYYRDATKPPNHRKVCKRCDCHPVGSTGKTCNHLSGQCPCKEGVTGLTCNRCARGYQQTRSHVAPCIKVPTNANMIQAESAGGGGGGGTGDYKDGGGSQVEEMKKYCGKCKASPKKLNLNKFCMEDYAILAKVIGHDRASQDISTEKFSIERQNEIYKYEINIQTIFKRNPMSGTTSSLLGRGNMMLLVPRKSIECQCPKIKLNKSYLILGRDSEAAPGYLAIGPSSVVLEWKDEWSLRMKRFQRRARKCS 793 Q24JJ9 Nuclear pore complex protein NUP43 NUP43 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q24JJ9 UNIPROT O65565 UNIPROT Q8LCD6 DE Reference Proteome: Yes; GO:0005635 GO:0031080 GO:0051028 GO:0015031 MEMMQDSFQVHRIPQSKYVDGVRWLPQASALNRFFATASYDADCDSSSIEIQSLDPNPRGNHNTNPLIESLSSWTSPSRVSSLEVAGNGGGGGSFKPMVSAATSSGSLHVLMIDLVEGAAIEEFYAAEGERFHVGRVEGVDWREGGECVTVGEDGRVNVVKIVNGEGLRYRKVFDGNGLVAYRAVKWASPTEFVTGGYGFGLQLWDQRKSGEAVSQLKGNWFQGKTSAIVHSIDIHPSRKHTCIAGGSSGTVFAWDLRWPQQPIVLSGVGASENINNPLSESEVWEVQYDSYTKSNVSSSRILPVMTCSEDGILGIIEQGEEPIELLAEPCAINSFDIDRQNPQDVICSLEWESIAVFSRP 361 Q27J81 Inverted formin-2 INF2 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:20023659}. UNIPROT Q27J81 UNIPROT Q27J83 UNIPROT Q69YL8 UNIPROT Q6P1X7 UNIPROT Q6PK22 UNIPROT Q86TR7 UNIPROT Q9BRM1 UNIPROT Q9H6N1 Pfam PF06367 Pfam PF06371 Pfam PF02181 Pfam PF02205 PROSITE PS51444 PROSITE PS51232 PROSITE PS51082 OMIM 610982 OMIM 613237 OMIM 614455 DisGeNET 64423 Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.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. O14976 EBI-714707,EBI-2557882 Q14108 EBI-1564650,EBI-2557882 P84089 EBI-2551866,EBI-2557882 P35579 EBI-350338,EBI-2557882 Q9NQW6 EBI-2553589,EBI-2557882 Q9D6P8 EBI-11062253,EBI-2557882 P62140 EBI-352350,EBI-2557882 Q9P2B7 EBI-2558932,EBI-2557882 P36873 EBI-356283,EBI-2557882 Q15388 EBI-711636,EBI-2557882 Q9NS69 EBI-1047508,EBI-2557882 P27824 EBI-355947,EBI-2557882 A0A0F7RE19 EBI-2557882,EBI-2809783 A0A384KTM2 EBI-2557882,EBI-2847147 GO:0048471 GO:0003779 GO:0017048 GO:0030036 GO:0090140 MSVKEGAQRKWAALKEKLGPQDSDPTEANLESADPELCIRLLQMPSVVNYSGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLSGRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHVLTLDALDHYKTVCSQQYRFSIVMNELSGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARLRDLEDADLLIQLEAFEEAKAEDEEELLRVSGGVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLLWEALESLVNRAVLLASDAQECTLEEVVERLLSVKGRPRPSPLVKAHKSVQANLDQSQRGSSPQNTTTPKPSVEGQQPAAAAACEPVDHAQSESILKVSQPRALEQQASTPPPPPPPPLLPGSSAEPPPPPPPPPLPSVGAKALPTAPPPPPLPGLGAMAPPAPPLPPPLPGSCEFLPPPPPPLPGLGCPPPPPPLLPGMGWGPPPPPPPLLPCTCSPPVAGGMEEVIVAQVDHGLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPAAKPKEPTMVAPRARKEPKEITFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQYTERLQASISAFRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPVRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAASMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQLEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKSFSEDAVTDSSGSGTLPRARGRASKGTGKRRKKRPSRSQEEVPPDSDDNKTKKLCVIQ 1249 Q27YE2 RING finger protein Z Z 55096 No SL-0382 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}. UNIPROT Q27YE2 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGQNQSRDKQKAIQNQPKDTGNRADIIPDATGMGPEFCKSCWFERRSLVACNNHYLCMNCLTLLLSVSERCPICKLPLPQKLKLTSSPSAPPSPSPPPYSP 101 Q28379 Interferon-induced GTP-binding protein Mx1 MX1 9796 Yes SL-0198 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}. UNIPROT Q28379 Pfam PF01031 Pfam PF00350 Pfam PF02212 PROSITE PS00410 PROSITE PS51718 PROSITE PS51388 Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}. GO:0030424 GO:0005737 GO:0031410 GO:0043197 GO:0044327 GO:0005789 GO:0016020 GO:0015630 GO:0031966 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0098844 GO:0045211 GO:0098793 GO:0045202 GO:0005525 GO:0003924 GO:0008017 GO:0051607 GO:0045087 GO:0061025 GO:0000266 GO:0048285 GO:0098884 GO:0031623 GO:0050803 GO:0016185 MVHSEAKMTRPDSASASKQQLLNGNADIQETNQKRSIEKNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKRLVKEDEWKGKVSYRDIEVEISNALDVEEQVRKAQNVLAGEGVGISQELVTLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKTLIRKYIQRQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEEQVVDVVRNLICHLKKGYMIVKCRGQQDIQDRLSLAEALQREKAFFEENPYFRGLLEEGRASVPCLAERLTTELITHISKSLPLLENQIKESYQNLSDELQKYGTDIPEDETEKTFFLIVKITTFNQNITSFVQGEELVGPNDTRLFNKIRQEFQKWSGVIENNFRKGGEAIRRQIWTFENQYRGRELPGFVNYRTFETIIKQQIQLLEEPAIDMLHRISDLVRDTFTKVSEKNFSEFFNLHRTTKSKLEDIKLEQENEAEKSIRLHFQMEKIVYCQDHVYRGTLQKVRENEMEEEKKKKTINVWGQNTSTESSMAEILEHLNAYQHEAGNRLSTHIPLIIQFFVLQTFGQQLQKSMLQLLQDRDTYDWLLKERNDTCDKRKFLKERLARLAQARRRLAKFPG 660 Q28H54 Choline/ethanolaminephosphotransferase 1 cept1 8364 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q28H54 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0004142 GO:0004307 GO:0046872 GO:0016780 GO:0006646 MSGQRAAKRRTGDLHTEFPTSCGNPYQTACLLSKFIELPTPPLTRHQLKRLEEHRYQSCGKSLLEPIMQGFWEWLVEQVPQWIAPNLITIIGLLINIITTVVLVYYCPTATEKAPTWTYLSCAIGLFIYQSLDAIDGKQARRTNSSTPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIPVLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYILTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEHLVLWIALVLSFIDLIRYSVSICNQIASHLHIEVFRIKTKVARFNHH 416 Q296J9 Nurim homolog nrm 46245 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q296J9 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 MATFAKVMLLLSSVATFGYTFFVVGKLMLFLSTPRSISKAHTWIFNLLDNKSRLETAYGPIVFDTLYLIGFIFQHSFLKSALVKNLWRKLGLAAAERTIYSLTSSICLHYLLKNWLPAQSIVLWQVDVDESAPLWWTFVVTHGLGWAVIFGGSLIMDLPELLGVKQVYYDLKEYGEPVAYKSSELRNLYSHVRHPSFVGLSVILFATNVMSLDRLLLASLLTVYMYVAWSTDDKDVAYQKQQLRNKKHELKAQ 253 Q298S5 Nucleoporin Ndc1 Ndc1 46245 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q298S5 Pfam PF09531 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}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MSHLSTINACKLLLFRRCLQAVLLTVGIQFLLLTIFLLFVNFQLLRPLHWISVTLSLVCSMYTWFASIPLVGAVVLYGMILCQQHLAERLYCPTRFRWLVHYAPRKLLFLAAHLLVGYLTAWLYTGYMHTDYRHLWYKCYDQECISAYHVYLLGMGIFAGCYYFVSVHMRQEVEIEFPIVNHLWGEKLREVLYSSLARSLIKSLLPTLAYTLLFWLFGGVVCHKLSHIFAVDLDERLEGFFGVATNGRLLFYGWLLTSQILSNMHLMRCFYSMFLSEEFPLAITKNRAAFVQEKEVTVVAALGLSNVYVVQCLAAKYLYNLVTAGDAEKRSELFQLTEPGNRPANWRSLCDQCLSLFGNFTDELIDSMQKISVLKGSPSSPPLTPISENASASLMAERVLTRQYNQMHGIRAIVSPRSNAVIDRPVDRIHRVPDWCERTSMQLEQSLQLLINRIPGIVYMFTEPEGAKTAFLLTHSLPLVFVIQALSQICVFSLKEDRYGVVQTDLPDIIRSMSRLKGELDKLSSVASNLRGPGSSFSVLRGAVRRSLFHICVAFGEYLSELIPSGEELHQLQTVINQE 579 Q29KT5 Protein spire spir 46245 Yes SL-0198 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}. UNIPROT Q29KT5 Pfam PF16474 PROSITE PS51377 PROSITE PS51082 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}. GO:0030659 GO:0005856 GO:0048471 GO:0005886 GO:0003779 GO:0045010 GO:0007275 GO:0015031 GO:0016192 MTEHHMDVQADATQSASESKAMAAPKGKFSEAEEGFLSTSPDSANGDAQQAHTHTHIISHTHSKGAAKTQTQTQNGNGTLGMGLGAPMLPGGSRQLLRQAFYQCSCPEQCVTLNNILDSFKAPLSEDQAWALIYQFGSLYYKVAAQAHKSGGDYEADLPSRFELHFHRDGNVHFSGAERLPELVESQEQEASQQEQQQKQPQMDDSATSSVDSNAALDRAFDNNNHEHHHHHHHQHHHPVDSNAALDRAHHTPLVVSHRKIISEMAEIVYTALDYNLPEDEECQMSQELENLFNFMTADETDEDCIDEGIDEGDKRWDDEAEEERNDTKELEHIIETCRNHLQKPALADNHYKAVCRALATETIELRVFLQQVLNNGAEKLIKAAESSPTTQKELAKLGFNDWARFWVQVIDELRRGVRLKKSNFERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRPPLKKASERQLGPPRMCTPTPREQLMESIRQGKELKQITPPEAPPLRQRMLPSANSTLSRSRQRLIKVDFSQLQDDELFFDDSSMSSSHSTAATHQHHQQHQPHHAHLAELHRCSQPKMPPYPFGGYMVPSQARQECQATATQLRPRRTMDTSAPRQTLPQPQAQARPPPPAEPSFTEDEYHRFFDNALESYDLATQCESRRASLRRHTIVGCQSNLEETHSMPPTRPESRQSDDAGSQSQSGASSEAPGIRKSPLMEGDHSQTTDGPPRLDEAHSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELEGLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTPSPSHHAHQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGAGASTSAAPGHAVEALHDQAAMSASYSSAMRPSGVMQHHQKHHYNNAMSRSMEGPRSLPVHSPAYRPLSNSSTLERKSRFSRGFALFSSGSHLAQTQDQKENLRGEQVPVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK 1096 Q29RU0 E3 ubiquitin-protein ligase RNF128 RNF128 9913 Yes SL-0198 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}. UNIPROT Q29RU0 Pfam PF13639 PROSITE PS50089 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}. GO:0005856 GO:0005783 GO:0005794 GO:0016021 GO:0005770 GO:0048471 GO:0046872 GO:0061630 GO:0006511 MGQLPGAGVFCRGGCGFSRLLAWCFLLVLSPQTPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVPGDWGSSVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGRLQLRTQKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHVFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNETSSNASPHEEDNRSETASSGYASVQGADEPPLEEHAHSANENLQLVNHEANSMAVDVVPHVDNPTFEEDESPDQETTVREIKS 431 Q29RU2 Oncoprotein-induced transcript 3 protein OIT3 9913 Yes SL-0178 Nucleus envelope {ECO:0000250}. Note=Can be secreted into blood. {ECO:0000250}. UNIPROT Q29RU2 Pfam PF00100 PROSITE PS00010 PROSITE PS01187 PROSITE PS51034 May be involved in hepatocellular function and development. {ECO:0000250}. GO:0031012 GO:0005635 GO:0032190 GO:0005509 GO:0007339 GO:0035803 GO:2000344 MPQLLLLACLLIIVTRVAPRALDPCSAYISLNEPWRNTEHQFDESRGSPLCDNSVDGEWYRFTGMAGDAMPTFCIPENHCGTHAPVWLNGSHPLEGDGIVQRQACASFNGNCCLWNTTVEVKSCPGGYYVYRLTKPSVCFHVYCGHFYDICDDDCHGSCLGTSECTCAPGTVLGPDRQTCFDENECEQNNGGCSEICVNLKNSYRCECGIGRVLRSDGKTCEDIEGCHNNNGGCSHSCLTSETGYQCECPRGLVLSEDNHTCQVPVFCKSNTIEVSIPRDLVGGLELFLTNTSCRGVSNGTHVNILFSLKTCGTVVDVVNDKIVASNLVTGLPKQTPGSSGDIIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNTPLEIMSRSHGIFPFTLEIFKDHEFEEPYREALPTLKLRDSLYFGIEPLVHVNGLESLVESCFATPTSKIDEIMKYYIIQDGCVSDDSVKQYTSRDHLAKHFQVPVFKFVGKDHKEVFLHCRVLVCGMLDERSRCAQGCHRRVRREASTEGEDASGPRSQMLTGGPISIDWED 547 Q2KHS5 2-acylglycerol O-acyltransferase 2-A mogat2 8355 No SL-0198 Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}. UNIPROT Q2KHS5 Pfam PF03982 Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250|UniProtKB:Q3SYC2}. GO:0005789 GO:0016021 GO:1990578 GO:0003846 GO:0006071 GO:0019432 MKIQFAPHNVPFERRLQTAAVLQWVFSFLALAQTCILLFFVLLFTRFWIISVVYGVWWFLDWDTPSKGGRRGEWLRRHVIWTYMKDYFPITLVKTADLDPQQNYVVGSHPHGVLVAGAFTNFCTEATGFHRLFPGITPYLLMLPLWFRAPFFRDYIMSGGLIPSDKDSASYLLKNKAGGNAVVIAVGGAPESLDARPGAFTLLIKNRKGFVRLAILHGASLVPVFSFGENELFDQVDNPRGSWLRKIQEKLQKMMGVALPLFHARGVFQYSFGLIPYRKPIATIVGKPIRVEENPNPSSEEVDKLHKIYMEELSKLFEEHKTKYNVPADKHLTFV 335 Q2KIA2 Multifunctional methyltransferase subunit TRM112-like protein TRMT112 9913 Yes SL-0198 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}. UNIPROT Q2KIA2 Pfam PF03966 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}. GO:0005654 GO:0048471 GO:0046982 GO:0018364 GO:2000234 GO:0070476 GO:0030488 MRLLTHNLLSSHVRGVGPRGFPLRLQATEVRINPVEFNPDFIVRMIPKVEWAALLEAADHLHLIQVPKEPIQGYEHNEEFLRKMHHVLLEVEVLEGTLQCPESGRVFPISRGIPNMLLSDEETET 125 Q2KIC8 Transmembrane protein 100 TMEM100 9913 Yes SL-0198 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}. UNIPROT Q2KIC8 Pfam PF16311 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}. GO:0005783 GO:0016021 GO:0043204 GO:0048471 GO:0005886 GO:0001525 GO:0060842 GO:0030509 GO:0071773 GO:0003198 GO:0001701 GO:0007219 GO:0045603 GO:2001214 GO:0043491 GO:0050848 GO:0051930 GO:0001570 MTDEPIKEILGTPKSPKPVAMEKNANGEVVVTLVPLVSEIQLAAATGGAELSCYRCVIPFAVVVLITGTVVTAVAYSFNSHGSIISILGLVLLSLGLFLLASSALCWKVRQRSKKAKRRESQTTLVVNQRGWFA 134 Q2M2T9 Telomere repeats-binding bouquet formation protein 2 TERB2 9913 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q2M2T9 Pfam PF15101 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}. GO:0005623 GO:0000784 GO:0005637 GO:0070197 GO:0045141 GO:0007129 MFQGQRGWFCGSVSHDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAEIKNSVALGHFILPPASLQKEIRRKIGSFIWEQDQHFLIEKHDEVTSNELKVFRESSVLATDHKKDLSKSTEKHFIRTPVVEKQMYFPLQHYPVNNMVTGYISIDAMKKFLGELHDFIPGSSGYLAYHVQNEINMSAIKNKLKNKY 221 Q2T9M1 PRKCA-binding protein PICK1 9913 Yes SL-0198 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}. UNIPROT Q2T9M1 Pfam PF06456 Pfam PF00595 PROSITE PS50870 PROSITE PS50106 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}. GO:0030054 GO:0005737 GO:0005856 GO:0043005 GO:0048471 GO:0005886 GO:0014069 GO:0098842 GO:0045202 GO:0008021 GO:0032588 GO:0051015 GO:0071933 GO:0046872 GO:0005543 GO:0019904 GO:0005080 GO:0036294 GO:0042149 GO:0097062 GO:0097061 GO:0021782 GO:0006886 GO:0060292 GO:0034316 GO:0002092 GO:0043113 GO:0034315 MFADLGYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQEHVQDIVLQLQRFVSTMSKYYNDCYSVLRDADVFPIEVDLAHTTLAYGLSQDEFTDGEDEEDEDEEDTAAGEPPRDSRGAAGPLDKGGSWCNS 417 Q2TBA3 Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog Malt1 10090 Yes SL-0198 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}. UNIPROT Q2TBA3 UNIPROT Q2TBA2 UNIPROT Q811E3 UNIPROT Q8BFT0 UNIPROT Q8C7N9 PDB 3V4L Pfam PF13895 Pfam PF18703 PROSITE PS50208 PROSITE PS50835 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}. Q60803 EBI-15909803,EBI-520135 GO:0032449 GO:0005737 GO:0005829 GO:0001650 GO:0005634 GO:0048471 GO:0002096 GO:0032991 GO:0004197 GO:0042802 GO:0019209 GO:0008233 GO:0002020 GO:0043621 GO:0004842 GO:0007250 GO:0042113 GO:0001923 GO:0071222 GO:0045087 GO:0031663 GO:0051168 GO:0043280 GO:0032731 GO:0032743 GO:0051092 GO:0050870 GO:0002726 GO:2000321 GO:0006508 GO:0042981 GO:0050856 GO:0009620 GO:0042098 GO:0050852 MSLWGQPLQASPPLAVRQPPTASSGPSTSPPAGATLNRLPEPLLRRLSESLDRAPEGRGWRQLAELAGSRGRLRLSGLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQALEHTEVLPLLNPPGLKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPYGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFSQWSQLDVCDVAEVTDSFQGSMDGISESRLQICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYTVPYVDIEHEGTYWCHVYNDRDSQDSKKAEVTIGRTDEAVECTEDELNNLGHPDNKEQTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMCNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGRQALEIRSSLSEKRALTDPVQGAPCSAEALVRNLQWAKAHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYVTDFPLDLDIDPKHANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLIAKLDMHRGLGRKTCFQACRMPDEPYHSSTSTSAGAGHFHSSQDSFHDVYHSHLGNADSGMPPDRCHCSRTPHTFISNYPPHHYCQFGRSNVPVETTDEMPFSFSDRLMISEN 832 Q2TLY1 Macoilin-2 maco1b 7955 Yes SL-0178 SL-0182 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}. UNIPROT Q2TLY1 UNIPROT B7ZUY4 Pfam PF09726 May play a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}. GO:0030424 GO:0016021 GO:0031965 GO:0030867 GO:0051015 GO:0008017 GO:0006935 GO:0023041 MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQNGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTENLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPSSSASSSSKGDRKQKYGGGKNSASHRDPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSVVYSADTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPLKK 699 Q2TLY2 Macoilin-1 Maco1a 7955 Yes SL-0178 SL-0182 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}. UNIPROT Q2TLY2 UNIPROT Q1L869 UNIPROT Q2TLY0 Pfam PF09726 May play a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}. GO:0016021 GO:0031965 GO:0030867 GO:0051015 GO:0008017 GO:0006935 GO:0023041 MKRRNADCSKLRRPLKRNRITEGIHSSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPKQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQRQERETEEATSKGMSEADSVLVAQNGTAINKKLPISLPELEYKEKGKDSAKDKKQQQHSIGINNNILQTVDAKLQDIEYMENHLNAKRLNNELGGSAENLFLKEEVGAGGGSAPSKHYKNSSPRSHNSTNGSVPSSSSNRSDKKQKCTGKNLAPHRDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQDLRSQISSLSSAERSMRSELGQLRQENELLQNKLHNAVQAKQKDKQTIVQLEKRLKAEQEARAAVEKQLAEEKKRKKMEEATAARAVALAAASRGECTDSLKSRIRELESECKKLTHDMKLKEEQIRELELKAQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKEQEIKELKQKIAEVMAVMPSITYSAETNNMTPVTPHYSSKFMDTSPSSLDPNASVYQPLKK 664 Q2VRL0 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 PLCZ1 9031 Yes SL-0198 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}. UNIPROT Q2VRL0 Pfam PF00168 Pfam PF09279 Pfam PF00388 Pfam PF00387 PROSITE PS50004 PROSITE PS50007 PROSITE PS50008 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}. GO:0005623 GO:0005829 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0045120 GO:0061827 GO:0004435 GO:0032266 GO:0005546 GO:0010314 GO:0032959 GO:0016042 GO:0007275 GO:0048015 GO:0060470 GO:0051209 MEENRWFLNIIQDGFMNGKIDFDSTVKLLEKLHMPFNLAHVKHVFKKTVDKRKIHTINIEDFRAIYRAIVHRNEFHEIFCAYSENRKNLADTELTAFLKKEQFKTEGAETTALEVILKYEPIDEVRKRRQLSFEGFIRYMSSEDCTIFKKEHRTVYQDMNHPLCDYFISSSHNTYLVSDQLIGPSDLNGYISALLKGCRCLEIDCWDGSNNDPVVYHGHTLTSKITFCSVIHVVDKYAFAASDYPVVLSLENHCSTKQQERIAQYLLNILGDKLLTSPIGDIEVTQLPSPEALKFKILVKNKKCGTIEETMLRKGRDSHGETGEVSEEEITSSDEETDEKTPLYPKSGSSKRKSEGRSSPPPRKKAKVKKMKIAMGLSDLVIYTKSEKFVSFEHSLAHQKCYENNSIGELKAQKFVKHAANQFVSHTSRFITRIYPKGTRAGSSNYNPQEFWNVGCQMVALNFQTSGTPMELQNGKFLDNGGCGYILKPEFLRNRNSTFNPHNVGRYSNPLSLSIRLISGHQLPPSNLSKSNKADPLVQLEIYGVPEDQAKRKSSVIKSNALSPRWDETFSFTVQVPELALIRFCVQDEISLVANDFLGQYTLPLLSLSKGYCTVPLFSKSGGKLEPASLFVYVWYY 637 Q2VWQ2 Protein kinase C-binding protein NELL1 Nell1 10090 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region. {ECO:0000250}. UNIPROT Q2VWQ2 Pfam PF12947 Pfam PF07645 Pfam PF02210 Pfam PF00093 PROSITE PS00010 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 PROSITE PS01187 PROSITE PS50025 PROSITE PS01208 PROSITE PS50184 Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:16537572}. GO:0005737 GO:0005615 GO:0005635 GO:0048471 GO:0005509 GO:0008201 GO:0042802 GO:0005080 GO:0030154 GO:1903363 GO:0033689 GO:0043065 GO:0030501 GO:0045778 GO:0045669 GO:0010468 GO:0045667 MPMDVILVLWFCVCTARTVLGFGMDPDLQMDIITELDLVNTTLGVTQVAGLHNASKAFLFQDVQREIHSAPHVSEKLIQLFRNKSEFTFLATVQQKPSTSGVILSIRELEHSYFELESSGPREEIRYHYIHGGKPRTEALPYRMADGQWHKVALSVSASHLLLHVDCNRIYERVIDPPETNLPPGSNLWLGQRNQKHGFFKGIIQDGKIIFMPNGFITQCPNLNRTCPTCSDFLSLVQGIMDLQELLAKMTAKLNYAETRLGQLENCHCEKTCQVSGLLYRDQDSWVDGDNCRNCTCKSGAVECRRMSCPPLNCSPDSLPVHISGQCCKVCRPKCIYGGKVLAEGQRILTKTCRECRGGVLVKITEACPPLNCSEKDHILPENQCCRVCRGHNFCAEAPKCGENSECKNWNTKATCECKNGYISVQGNSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCIPGYIRVDDFSCTEHDDCGSGQHNCDKNAICTNTVQGHSCTCQPGYVGNGTVCKAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECAEGFVECHNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGLKHNGQVWILREDRCSVCSCKDGKIFCRRTACDCQNPNVDLFCCPECDTRVTSQCLDQSGQKLYRSGDNWTHSCQQCRCLEGEADCWPLACPSLSCEYTAIFEGECCPRCVSDPCLADNIAYDIRKTCLDSSGISRLSGAVWTMAGSPCTTCQCKNGRVCCSVDLVCLENN 810 Q32NG5 Solute carrier family 2, facilitated glucose transporter member 12 slc2a12 8355 No SL-0198 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}. UNIPROT Q32NG5 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-regulated facilitative glucose transporter. {ECO:0000250|UniProtKB:Q6NWF1}. GO:0012505 GO:0016021 GO:0048471 GO:0005886 GO:0022857 GO:0008643 MLAHSTAQDLILQQRSSDDHPQTNPRQTGCGAFIILSSVIAAISGLLVGYELGIISGALLQLQSLLELTCQQQEIVVSALLIGALVASLVGGCLIDLYGRRTTIIFTSILLVFANLLPVVVVSYGSLIAGRIFIGVSISLSAIATCVYIAELSPQDKRGMLVSLNELMIVAGILLAYICNYLFASVNNGWKYMFGLITPLAALQAVAMFFLPRSPRFLIMKGYDDAAGKVLQKLRATTDINEELTAIKSSIKAEYQYKFLDLFCSRDNMRARLLIGLTLSFFVQITGQPNILFYASTVLKSVGFQSTEAASLASTGIGVVKVVSTIPAIFLVDKIGSKTFLCIGSAVMAVSLVSVGLVSLQLDVNYNNICKVHTVQNHSLQDSFVYGPVALAKHNESLFEETGTWLESTKASYHSTSQNGTKLLHVSAPEDSSFGFTVKEPKVKSQSDEIPEYMKWLCLSSLLAFVAAFSIGLGPMAWLVQSEIFPAGIKGRAFAITSSMNWGMNLLISLTFLTLTEMIGLPWMLFGYALMSIASLVFVIMFVPNTKGRPLEEISKELANRSYMCNAVCHRRRSKKKLTPVALIQSPA 588 Q32PE2 Ran guanine nucleotide release factor RANGRF 9913 Yes SL-0198 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}. UNIPROT Q32PE2 Pfam PF04603 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}. GO:0005634 GO:0048471 GO:0005886 GO:0005085 GO:0015031 MEPTRDNPLFGGAFSATLPPGAIDVSDLRPVPDHQEVFCHRVTDQSLIVELLELQAHVQGEEAARYHFEDVGGVQEARAVQVETVQPLVLEKLALRGCCQEAWILSGQQQVAKENQQVAKYVTLHQALLRLPQYQTDLLLTFNQPPPENRSSLGPENLSIPPWSLGDFEQLVTSLTLHDPNIFGPE 186 Q32PZ3 Protein unc-45 homolog A Unc45a 10116 Yes SL-0198 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}. UNIPROT Q32PZ3 Pfam PF13181 Pfam PF11701 PROSITE PS50005 PROSITE PS50293 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}. Q68CZ2 EBI-1220488,EBI-22265203 GO:0005829 GO:0005794 GO:0016607 GO:0048471 GO:0051879 GO:0030154 GO:0061077 GO:0007517 MTVSGPGTPEPRPSDPGASSAEELRKEGNELFKCGDYEGALTAYTQALSLGATPQDQAILHRNRAACHLKLEDYSKAESEASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLKRCVSLEPKNKVFQESLRNIGGQIQEKVRYMSSTDAKVEQMFQILLDPKEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDTGETDLMLAALRTLVGICSEHQSRTVATLSVLGTRRVVSILGVENQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLELLTEIGVSGQGRDNALTLLIKMVPRKSPKDPNNSLTLWVIDQGLKKILEVGGSVPEAAGELTVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIRSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVALLKDLYKGSERDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADVKEEFVEDEAALKALFQLSRSEERSVLFAVGSALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLLAAGVVSAMTCMVKTESPVLTNSCRELLSRVFLALVEEVEDRGTVVAQGGGKALLPLALEGTDVGQTKAAQALAKLTITSNPEMTFPGERIYEVVRPLVSLLHLSCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMCNLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLRRAAAGGLAMLTSMRPSLCSRIPQVTTHWLEILQALLLSPNPELQHRGTVVVLNMMESSKEIASTLMESEVLEILSVLAKGEESPVTRAAAACLEKAVEYRLIQPNQDGE 944 Q32ZD5 RNA-directed RNA polymerase NS5 POLG 44024 No SL-0382 [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}. UNIPROT Q32ZD5 PDB 2V6I PDB 2V6J Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MTKKPGRPGRNRAVNMLKRGASRALGPMIKLKRMLFGLLDGRGPLRMVLAILAFFRFTALKPTAGLLKRWGMMDKVHALSLLKGFKKDLASMTDFVHLPKKKSGVSIIGRMLVFSFTAAVRVTLENGMSLMKIQKADVGKVITIRTDRGENRCIVQAMDVGEDCEDTMKYLCPAIENPSEPDDIDCWCDKADAMVTYGRCSKTRHSRRSRRSTNIAGHADSRLDSRGSVWMDTKKATSYLTKAESWALRNPGYALVAAVLGWSLGTSNAQKVIFTVMILLIAPAYSIRCVGVENRDFIEGVSGGTWVDVVLEHGGCVTIMAPDKPTIDLELTSTIAKSMAVTRTYCVQAQVSELSVETRCPTMGEAHNSKSSDAAYVCKKGFSDRGWGNGCGLFGKGSMETCAKFSCQTKAEGRIIQRENLEYTIHMNVHASQETGHFMNDTIASENKHGAKISITATGPSRTADLGDYGMVTLDCEPRAGLDFDNLYLLTLGRNSWLVNRDWFHDVNLPWIGGAEGHWKNRESLVEFGKTHATKREVLALGSQEGTLQVALAGAMIAKFGSNVATINSGHLKCRLKLDKLKIKGTTYHMCKGSFAFTKTPSDTGHGTVLLELTYSGSDGPCRVPISMSVSLSNIEPVGRMVTVNPIVLSSSPQKTIMIEVEPPFGDSFIIAGTGEPRAHYHWRKSGSSIGAAFATTIKGARRLAVIGDDAWDFGSVGGILNSVGKALHQIFGGMFRTLFGGMSWFTQIMIGALCCWLGINARDRTIAVTFLAVGGVLVFLATSVNADSGCALDLKRKEFKCGNGIFVFNDAEAWSHSYRYHPSTPKKLAGSIVRAIEEGQCGVRSVGRLEHEMWRANAREINAILLENEKNLSVVVLESEYYRKAKNLMPIGDEMPFGWKSWGKKFFEEPQLQNQTFVVDGRVGKECPEEKRSWNNFRIEDFGFGVFTTSVWMEQRTEYTEDCDQKVIGAAVKGELAAHSDLGYWIESRSKNGSWELERAYLLESKSCSWPATHTLWNGGVEESELIIPKSRAGPVSHHNTRKGYHNQIKGPWHLTPLEIRFESCPGTTVVTTEECGNRGPSLRTTTTSGKVISEWCCRSCTMPPLSFRTADGCWYGMEIRPLKEREETMVKSHVSAGRGDGVDNLSLGLLVLTIALQEVMRKRILGRHITWMVIAVFMAMILGGLSYRDLGRYLVLVGAAFAERNSGGDLLHLVLVATFKVKPMALLGFVLGGRWCRRQSLLLSIGAVLVNFALEFQGGYFELVDSLALALLFVKAVVQTDTTSVSLPLLAALAPAGCYTVLGTHRFIMLTLVLVTFLGCKKTASVKKAGTAAVGVVLGMVGMKTIPMLGMLMVTSRARRSWPLHEAMAAVGILCALFGALAETEVDLAGPLAAAGLIVMAYVISGRSNDLSIKKVEDVKWSDEAEVTGESVSYHVSLDVRGDPTLTEDSGPGLEKVLLKVGLMAISGIYPVAIPFALGAWFFLEKRCKRAGALWDIPSPREAKPAKVEDGVYRIFSRKLFGESQIGAGVMVKGTFHTMWHVTRGAVLKAGEGLLEPAWADVRKDLICYGGNWKLEEHWDGNEEVQLIALEPGKKVRHIQTKPGIFKTSEGEIGALDLDCMAGTSGSPIVNKNGEVVGLYGNGVLIKGDRYVSAISQKENVGQEDGAEIEDNWFRKRELTVLDLHPGAGKTRRVLPQLVREAVKKRLRTVILAPTRVVASEMYEALRGEPIRYMTPAVQSERTGNEIVDFMCHSTFTMKLFQGVRVPNYNLYIMDEAHFLDPASVAARGYIETRVSMGDAGAIFMTATPPGTTEAFPPSNSPIIDEETRIPDKAWNSGYEWIIEFDGRTVWFVHSIKQGAEIGTCLQKAGKKVLYLNRKTFESEYPKCKSEKWDFVITTDISEMGANFKADRVIDPRKTIKPILLDGRVSMQGPIAITPASAAQRRGRIGRNPEKLGDIYAYSGNVSSDNEGHVSWTEARMLLDNVHVQGGVVAQLYTPEREKTEAYEGEFKLKTNQRKVFSELIRTGDLPVWLAFQVASANVEYHDRKWCFDGPNEHLLLENNQEIEVWTRQGQRRVLKPRWLDGRITSDHLNLKSFKEFASGKRSALSILDLIAVLPSHLNLRLQEALDTAAILSRSEPGSRSYKAALENSPEMIETFLLCALVCLMTIGLVVVLVRGKGPGKLAFGMVSIGVMTWLLWSAGVDPGKIAAAVILVFLLLVVLIPEPEKQRSVQDNQLAMLMLLIATILGGVAANEMGWLEKTKADLSWVVRGRSSTTTPVVELDMKPATAWTLYALATTLLTPLFQHLIVTKYANISLMAIASQAGTLFSMDSGIPFSSIELSVPLLALGCWTQITPCSLILACVLLSTHYAILLPGMQAQAARDAQRRTAAGIMKNAVVDGIVATDIPPLDGAGPLTEKKLGQLLLFAAAVTGVVITRSPRSWSELGVLGSAVGSTLIEGSAGKFWNATTVTAMCNLFRGSYLAGVPLTYTIIRNSNPSNKRGGGIGETLGEKWKARLNQMNTLEFHRYRRSHIMEVDREPARAALKSGDFTRGAAVSRGSAKLRWMHERGYIRLHDKVVDLGCGRGGWCYYSATVKEVKEVKGYTKGGRGHEEPVLTQSYGWNIVQMKSGVDVFYKEAEPCDVVLCDIGECSSSPAVEADRSTKVLELAERWLERNDGADFCIKVLCPYMPEVVEKLSKLQLRYGGCLVRNPLSRNSTHEMYWVSGYKGNLIGVINSTSALLLRRMEIKFAEPRYEEDVNLSCGTRAVSIAPPKFDYKKIGQRVERLKAEHMSTWHYDCEHPYRTWAYHGSYVVKPSGSASSQVNGVVKLLSKPWDVSSEVTGMSMTDTTPFGQQRVFKEKVDTKAPEPPAGAEMASVIVSEWLWKRLNREKKPRLCTKEEFVRKVRGNAALGPVFEEENQWKDAAEAVQDPGFWNLVDMERKNHLEGKCETCVYNMMGKREKKRGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRGNSGGGVEGLGIQKLGYVMREIGEKGGILYADDTAGWDTRITECDLRNEAHIMEYMENEHRKLARAIFELTYKHKVVKVMRPGKGVPLMDIISREDQRGSGQVVTYALNTFTNLVVQLIRMAEAECVLTPEDLHEMSQSAKLRLLKWLKEEGWERLTRMAVSGDDCVVAAPDARFGAALTFLNAMSKIRKDIKEWTPSKGWKNWEEVPFCSHHFHRLQMKDGRELVVPCRSQDELIGRARVTQGPGDLMSSACLAKAYAQMWQLLYFHRRDLRLMGNAICSAVPVDWVPTGRTTWSIHGKGEWMTSENMLEVWNRVWIEENEHMEDKTPVREWTDIPYLGKREDPWCGSYIGYRPRSTWAENIKVPVNVIRVKIGGNKYQDYLGTQKRYESEKRVEFRGVL 3410 Q32ZE0 RNA-directed RNA polymerase NS5 POLG 64304 No SL-0382 [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}. UNIPROT Q32ZE0 Pfam PF01003 Pfam PF07652 Pfam PF02832 Pfam PF00869 Pfam PF01004 Pfam PF00948 Pfam PF01005 Pfam PF01002 Pfam PF01350 Pfam PF01349 Pfam PF00972 Pfam PF01570 Pfam PF01728 Pfam PF00949 PROSITE PS51527 PROSITE PS51528 PROSITE PS51192 PROSITE PS51194 PROSITE PS50507 PROSITE PS51591 [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}. GO:0005576 GO:0044167 GO:0042025 GO:0044220 GO:0016021 GO:0019028 GO:0019031 GO:0055036 GO:0005524 GO:0003725 GO:0046872 GO:0004482 GO:0004483 GO:0046983 GO:0003724 GO:0003968 GO:0004252 GO:0005198 GO:0075512 GO:0039654 GO:0039520 GO:0039563 GO:0039564 GO:0039502 GO:0039694 GO:0019062 MARKPGRPGGNRVVNMLKRTAANAASPLGLAKRLLGDAFAGRGPLRVILAVVAFFRFTAIKMSPALLKKWGTVEKGAAIAIMKSFKKEIGSMLDVVARRKTKNKGKRSVESSALLVLLTACLALGFKVVTGPEGPIMDVTKKDVGKALEIPFQNFNNTCWVMAMDVGHPCEDTIEYECPSLDIGAEPNDIDCWCDTMPMRVRYGRCTKGSIPKRSRRNAVFPQHTENVLATRQETWMNTDVIMKHLIKVETWALRNPGFALVAITLGWMLGSNRSQKIIFTILLLLVAPAYNMRCIGVENRDFVEGLSGGTWVDVVLEHGGCVTVRVEGKPTLDFELVQTKATGLAAVRAYCYQAKVSDIQISAACPAVQLTENSKATDSNYLCRRGVTNRGWNNGCGLFGKGDIHTCVKFKCEKKAAGFSIGKENLEYEVRASVHNSIGADKFSNELADGEPHTQKMKFSPLSPSAEKSFGDYGTLGMDCEPQSGLDFGQLYLMTIESKSWLVNRDWYHDLHLPYTVGSGSQWNNREALVEFQEPHATKQEVLALGSQEGALHSALAGAIMANRETSSPHALLLTAGHLKCRIKMDKMVIKGITYGQCSGTFKMEKHPADTGHGTVVLDVSYQGDDAPCKIPIVITSNLAEVEPVGRLVSAHPVITAKNVRTMLEVEPPYGDSYIVIGVGDGRLKQHWFKKGSVIGGAFSTTMKGAKRLAVLGDAAWDFGSVGGVFNSLGKAVHQLFGGIFRTLFGGMSWLSRLMIGALCLWIGINARDHSIAVTMLSVGGILIFLSINVSADTGCVVDIERKELKCGSGIFIMNDIEAWRDEYAFHPSGPKALAASVVEAFSQGVCGVRSVNRLEHKMWESIADELNAILEENEREITIVVKDMENPAQKGKMRLRPVEKELKYGWKKWGASFFKRASRKNATFLVDGPSGEECPNSNRAWNSFFIEDFGFGVFKTSVWLGLNEQMTEVCDTKMIGTGVKNDRAVHSDLGYWIESRKNLTWEISRARLIETKACIWPRSHTLWSDGIEETQLIIPKSLGGPRSRHNMRSGYKTQINGPWDQIPLDIKFEECPGTSVTVTPNCGGRGPSARSTTASGKVIADWCCRDCILPPLTFRSGETCWYAMEIRPVSEREETLIRSKVSAGDGNEIDTFSLGLLVAMLVTQEGLRKRWATRHIMVASLTMLAAMVTGHITYRDLLRYVVLLGATFAQINDGGDVMHLALVAVFKVQPGFLLGFLLRRRWTPRESMLLAISACFLHLVFSELSTDITTLAHNFSLALLILRAIIQTDVSSVTLPVLSMMAPSFQLSVLGTFRMAVAVYVIVNLMMSKRNDAVKKAAPSVVAAALGQFGMVNATAALGTLYVLEKHGKRSWPPSEIFSAVGVLCALVGALGNVQSTPLAGPMAACGLLIAAYVVTGKSTDIEIERAGLISWSEDAEVSGSSPRVDVALDENGDFSLIDGQGPSLESVILKTALVAFSGLFPVSIPFCAAAWYLHGKSGRRAGALWDIPAPREVKKGSTENGVYRILANRLFGKTQVGVGVMHEGVFHTMWHVTRGAALKSGEGRLDPYWGDVKKDLISYGGPWKLEGRWDGVSEVQLIAVPPKEKAKNVQTTPGVFKTPHGEIGAIVLDFPAGSSGSPIINKLGEVIGLYGNGLMMGDAYASSIAQAEVEDEPDTPNCLPPDVTHKKKLTVLDLHPGAGKTRKVLPKLLQEALEKRLRTVVLAPTRVVAAEMAEALKGMPIRYQTAAVTSSHSGNEIIDLMCHATFTSRLMQPHRVPNYNLYIMDEAHFTDPASIAARGFIATKVSLGEAAAVFMTATPPGSDNPFPASNAPITDTEAQIPDKAWSTGFDWITEYGGKTVWFVPSVRMGNEIAACLTKAKKKVIQLSRRTFNTEYPKCKQGDWDFVVTTDISEMGANFKATRVIDSRRAIKPSIMQDQEERVVLSGPTPISPASAAQRRGRVGRNPNQLGDEYVFSGLTQANDEGNACWTEARMLLDNIHMQNGLIAQLYGPEQDKCFATDGEFKLREKERATFLEFLKADLPVWLSFKAASSGVQYHDRKWCFDGPDNNLVLEDNVPVEIWTKSGERKKLKPRWSDARTYCDHGALTAFKEFAGGRRSVTTGLLEGVGRLPEHLGQRLKESIDTLYLAFTAEVGSRPHREAMQEMPAALETVLVFFLLMIMTGCTFFLLMRHKGINKMGYGMVVMSAVGGLLWYGNVPAPKIAGILLLTFLLMVVLIPNPEKQRSIQDNQLALVVLGCLMFLGGIAANEMGMLERTKQDLAGVFHKTERKSTEFTLLTPPDLRPATAWSIYAIGTTLITPLIHHMITTHYANFSLMAMANQAGSLFGMQTGAPFSKMDWAVPAIVVGCWQQLTPATLMTALVLLAVHYIYMIPGWQAGAARAAQRRTAAGIMKNPVVDGLVVTDIPTLEEVDPLVEKKLGQYILLAVAIAAAVLRQDLQSWSECATLSAAAAATLWEGSPGKIWNASTACSLVNIFRGHTLAAVPFMFTILRNTGNTGKRGGVEGETLGEKWKHLLNAMDKYEFSRYKVNGIFEVDREPARMALANGLVTSGHAVSRGSAKLRWMVERAAVRPTGRVIDLGCGRGGWSYYCATLKQVQEVRGYTKGGPGHEEPRMVQSYGWNIVTLKSGVDVFHRPAEVGDTILCDIGESSATPEVEEARTLKVLEMVEPWLKNKPEFCIKVLCPYRPKVIERLSALQRTYGGGLVRVPLSRNSTHEMYWTSGTAGNIINAVNLTSKVLLHRMEKKWIGPRYEKDVNLGSGTRAVIVKRKAPDMDKIGNRVKRLKEEHIATWCYDDMNPYRTWNYHGSYEVKPTGSASSMINHVVKMLSKPWDTLNSVTSISMTDTTPFGQQRVFKEKVDTKAPEPPTGVAEVMDIISDWTWRLLSRQKKPRLCTRDEFKAKVNNHAAMGSIFEEEHQWQTAKEAVEDPGFWALVDREREAHLAGRCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWLSRENSYAGVEGLGLQRLGYVLRDISRRPGGKMYADDTAGWDTRITEKDLDNEAKIIDQMEGEHKQLAKAIMELTYRHKVVKVMRPGPGGKTYMDIISREDQRGSGQVVTYALNTFTNMIVQLTRCAEAEGVLIPSMRERKLTPAEHRALLLWLDTEGVKRLKKMAISGDDCVVKGEDERFATALYFLNAMAKVRKDIQEWKPSSGWADWQEVPFCSHHFKELQLKDGRTIVVPCRHQDELVGRARVSPGAAWTVRESAGLAKAYAQMWKLMYFHRRDLRLMANAICSAVPKDWVPTGRTTWSIHGKGEWMTNEDMLEVWNRVWIRENPHVEDKTEVADWKDVPYLGKREDQWCGSLIGSRTRATWAENIWVAVNQVRAKIGKEEYSDHLSSQQRFENWGEVRFSGVL 3429 Q38942 Protein RAE1 RAE1 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:21189294}. UNIPROT Q38942 UNIPROT Q1LYY5 UNIPROT Q9SAJ0 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 DE Reference Proteome: Yes; Q9M0V3 EBI-1632780,EBI-1632807 GO:0080008 GO:0005829 GO:0005635 GO:0005643 GO:0003723 GO:0043130 GO:0051028 GO:0015031 GO:0006405 GO:0000972 MATFGAPATANSNPNKSYEVTPSPADSISSLSFSPRADILVATSWDNQVRCWEISRSGASLASAPKASISHDQPVLCSAWKDDGTTVFSGGCDKQAKMWPLLSGGQPVTVAMHEGPIAAMAWIPGMNLLATGSWDKTLKYWDTRQQNPVHTQQLPDKCYTLSVKHPLMVVGTADRNLIVFNLQNPQTEFKRIQSPLKYQTRCVTAFPDQQGFLVGSIEGRVGVHHLDDSQQSKNFTFKCHRDGNDIYSVNSLNFHPVHGTFATAGSDGAFNFWDKDSKQRLKAMSRCNQPIPCSSFNHDGSIYAYAACYDWSKGAENHNPATAKSSIFLHLPQESEVKAKPRVGATGRK 349 Q39134 Amino acid permease 3 AAP3 3702 Yes SL-0178 SL-0182 Cell membrane {ECO:0000269|PubMed:15361541}. Nucleus membrane {ECO:0000269|PubMed:15361541}. Endomembrane system {ECO:0000269|PubMed:15361541}. Note=Not found in vacuole membrane. UNIPROT Q39134 UNIPROT Q8LE75 Pfam PF01490 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}. Q39222 EBI-16894298,EBI-4463452 Q84N34 EBI-1810738,EBI-4463452 Q8LAA6 EBI-4440607,EBI-4463452 Q9SHI7 EBI-4476710,EBI-4463452 Q9LSP7 EBI-16895382,EBI-4463452 Q9FN48 EBI-7889805,EBI-4463452 Q9FNH6 EBI-4461284,EBI-4463452 P57752 EBI-2008339,EBI-4463452 F4I1Z0 EBI-16882439,EBI-4463452 Q9LPN5 EBI-6392819,EBI-4463452 Q9C7D7 EBI-16893154,EBI-4463452 Q8GW19 EBI-16897007,EBI-4463452 O04265 EBI-16897382,EBI-4463452 O64852 EBI-16882559,EBI-4463452 Q8RY98 EBI-4452570,EBI-4463452 Q94F23 EBI-16891935,EBI-4463452 Q9FJB4 EBI-16890988,EBI-4463452 Q93Z82 EBI-16897870,EBI-4463452 Q9LHA6 EBI-4430467,EBI-4463452 Q1JPM5 EBI-16884610,EBI-4463452 Q8L8T2 EBI-16890309,EBI-4463452 Q9LVU1 EBI-16889489,EBI-4463452 Q8L9S0 EBI-16889232,EBI-4463452 C0LGW2 EBI-16888393,EBI-4463452 Q9SVG8 EBI-16888161,EBI-4463452 Q9LMN8 EBI-2320063,EBI-4463452 Q9AST5 EBI-4448696,EBI-4463452 Q8H129 EBI-16886692,EBI-4463452 Q944J0 EBI-16885927,EBI-4463452 Q9C835 EBI-16885299,EBI-4463452 F4JN35 EBI-4463452,EBI-4426607 Q94F58 EBI-2319707,EBI-4463452 GO:0016021 GO:0031965 GO:0005886 GO:0015171 GO:0015293 GO:0003333 GO:0015802 MVQNHQTVLAVDMPQTGGSKYLDDDGKNKRTGSVWTASAHIITAVIGSGVLSLAWATAQLGWLAGPVVMLLFSAVTYFTSSLLAACYRSGDPISGKRNYTYMDAVRSNLGGVKVTLCGIVQYLNIFGVAIGYTIASAISMMAIKRSNCFHKSGGKDPCHMNSNPYMIAFGLVQILFSQIPDFDQLWWLSILAAVMSFTYSSAGLALGIAQVVVNGKVKGSLTGISIGAVTETQKIWRTFQALGDIAFAYSYSIILIEIQDTVKSPPSEEKTMKKATLVSVSVTTMFYMLCGCMGYAAFGDLSPGNLLTGFGFYNPYWLLDIANAAIVIHLIGAYQVYCQPLFAFIEKQASIQFPDSEFIAKDIKIPIPGFKPLRLNVFRLIWRTVFVIITTVISMLLPFFNDVVGLLGALGFWPLTVYFPVEMYIAQKKIPRWSTRWVCLQVFSLGCLVVSIAAAAGSIAGVLLDLKSYKPFRSEY 476 Q3KP22 Membrane-anchored junction protein MAJIN 9606 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q3KP22 UNIPROT B3KS99 UNIPROT E9PPE5 PDB 6GNX PDB 6GNY PDB 6J08 Pfam PF15077 OMIM 617130 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}. P53350 EBI-21493388,EBI-476768 P26998 EBI-21493388,EBI-1965681 GO:0005623 GO:0005639 GO:0000784 GO:0003677 GO:0070197 GO:0045141 GO:0007129 MSLKPFTYPFPETRFLHAGPNVYKFKIRYGKSIRGEEIENKEVITQELEVPVEKKAVGAVMRKRKHMDEPSSPSRPGLDRAKIGTSSQGPSKKKPPVETRRNRERKTQQGLQETLASDITDVQKQDSEWGHSLPGRIVPPLQHNSPPPKERAATGFFGFLSSLFPFRYFFRKSSHS 176 Q3MHM8 ADP-ribosylation factor-like protein 6-interacting protein 6 ARL6IP6 9913 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q3MHM8 Pfam PF15062 DE Reference Proteome: Yes; GO:0016021 GO:0005637 MSFVESGRRSAPLRRRPGTPVPFARPAYSVFSQGDSWGEGEVEEEEGCDQVARDLRAEFSAGSSSKLRKDPVLQPDGDGSPVLPDKRNGIFSADAGGKALARRWPVQVLSILCSLLFAILLACLLAITYLIVKELHAENLKNEDDVNTGLLGFWSLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKMTGHSFHMGYSMAILNGIVAALTVAWCLM 226 Q3MHW7 Sigma intracellular receptor 2 TMEM97 9913 Yes SL-0178 SL-0182 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}. UNIPROT Q3MHW7 UNIPROT A1L510 PROSITE PS51751 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}. GO:0005783 GO:0016021 GO:0005764 GO:0031965 GO:0005886 GO:0005791 GO:0030867 GO:0042632 MGTLGARRGLEWFLGFYFLSHIPITLLMDLQGVLPRDLYPVELRNLQQWYIEEFKDPLLQTPPAWFKSFLFCELVFQLPFFPIAAYAFFKGGCKWIRTPAIIYSVHTMTTLIPILSTLLLDDFSKASHFRGQGPKTFQERLFLISVYIPYFLIPLILLLFMVRNPYYKSEEKRKKK 176 Q3T005 PDZ and LIM domain protein 4 PDLIM4 9913 Yes SL-0198 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}. UNIPROT Q3T005 Pfam PF15936 Pfam PF00412 Pfam PF00595 PROSITE PS00478 PROSITE PS50023 PROSITE PS50106 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}. GO:0005912 GO:0005737 GO:0005856 GO:0043197 GO:0031905 GO:0031901 GO:0031941 GO:0030027 GO:0005634 GO:0048471 GO:0045211 GO:0034777 GO:0055038 GO:0001725 GO:0030018 GO:0003779 GO:0051393 GO:0046872 GO:0051371 GO:0042803 GO:0019903 GO:0030036 GO:0031532 GO:0098976 GO:0007507 GO:0061061 MPHSVTLRGPSPWGFRLVGGRDFSVPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCRDHLTLSVSRPEGRSWPSTPEDNKAQAHRIHIDSEAQDGSPLTSRRPSATGLGPEDGRPGLGSPYGQSPRLPVPHNGSNSEATLLAQMGALHVSPPHSTDPARGLPRSRDCGVDLGSEVYRMLREPAEPAAAEPKQSGSFRYLQGMLEAGEGGERPGPGGPRNLKPTASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVVAVYPNAKVELV 331 Q3T0A9 Protein shisa-5 SHISA5 9913 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}. UNIPROT Q3T0A9 Pfam PF13908 Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}. GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0042771 MAAPAPAPRILVLLLLLLPAPEGAQSELCMISHGRKVDPWVCPDFCCGNCNDQYCCSDVLKQVMWIEEDCHAPEASILTDDFDSGFDSDPVARFGTVIAIGVTLFVIAVVTVIVCCTCSCCCLYKMCRRPQPVVTTTMATTVTHTPYLQPPSYPGPTYQGYHSVVPQPGMPTAPYPTQPTGPPAYHETMAGGAALPYPASQPPYNPAYMEPPKAVP 216 Q3T0C9 Synaptojanin-2-binding protein SYNJ2BP 9913 Yes SL-0198 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}. UNIPROT Q3T0C9 Pfam PF00595 PROSITE PS50106 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}. GO:0016323 GO:0030054 GO:0016021 GO:0005741 GO:0031594 GO:0043005 GO:0048471 GO:0098839 GO:0098609 GO:0007268 GO:0006897 GO:0045197 GO:0016525 GO:0010596 GO:0001937 GO:0070373 GO:1903671 GO:0043113 GO:0097120 GO:0008593 MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIFVSRIKENGAAALDGRLQEGDKILSVNGQDLKNLLHQDAVDLFRNAGYAVSLRVQHRLQVQNGPIGPQGEGEPSGIPIAMVLVPVFALTMVAAWAFMRYRQRL 145 Q3TB82 Pleckstrin homology domain-containing family F member 1 Plekhf1 10090 Yes SL-0198 Nucleus {ECO:0000269|PubMed:16188880}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16188880}. Lysosome {ECO:0000269|PubMed:16188880}. Note=Translocates to lysosome during apoptosis. UNIPROT Q3TB82 UNIPROT Q99M16 Pfam PF01363 Pfam PF00169 PROSITE PS50003 PROSITE PS50178 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}. GO:0005768 GO:0005764 GO:0005739 GO:0005634 GO:0048471 GO:0046872 GO:0035091 GO:0032266 GO:0070273 GO:0010314 GO:0006915 GO:0007032 GO:0010508 GO:2001244 GO:0072659 GO:0046902 GO:0016050 MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLSKRKYRSQHIIPLEEVTLEPLPETLQAKNRWMIKTAKKSFVVSAASTTERQEWISHIEECVRRQLLATGRQPTTEHAAPWIPDKATDICMRCTQTRFSALTRRHHCRKCGFVVCAECSRERFLLPRLSPKPLRVCSLCYRELAAQKLREEAREGIGGSPPQLSHLGGTVCGASSGDDDDSDEDREGNGDGDWPTQVEFYASGVSWSAFHS 279 Q3U487 E3 ubiquitin-protein ligase HECTD3 Hectd3 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}. UNIPROT Q3U487 UNIPROT B1AUL1 UNIPROT Q3TN76 UNIPROT Q641P3 UNIPROT Q8BQ74 UNIPROT Q8R1L6 Pfam PF03256 Pfam PF00632 PROSITE PS51284 PROSITE PS50237 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}. GO:0048471 GO:0019905 GO:0004842 GO:0043161 MAGPGPGAALESPRQLLGRVRFLAEAARSLRAGLPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAVGAAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLSDCSLDEGWLLVCRPAEGGARLVPIDTPDHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYTEAIQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVNIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPASLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPSLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGVDKETFEFKFGKELTFTTVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE 861 Q3U5C7 Prickle-like protein 1 Prickle1 10090 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}. UNIPROT Q3U5C7 Pfam PF00412 Pfam PF06297 PROSITE PS00478 PROSITE PS50023 PROSITE PS51303 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}. GO:0005829 GO:0031965 GO:0005634 GO:0008134 GO:0008270 GO:0035904 GO:0060976 GO:0090090 GO:2000691 GO:0045892 GO:0001843 GO:0032436 GO:0031398 GO:0006606 MPLEMEPKMSKLVFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHDNEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAVMHAVCEQCGLQMNGGEVAVFASRAGPGVCWHPSCFVCFTCNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCCGCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDIHASDSSDSAFQSARSRDSRRSVRMGRSSRSADQCRQSLLLSPALNYKFPGLSGNADDTLSRKLDDVSLASRQGAGFANEEFWKARVEQEASEDPEEWAEHEDYMTQLLLKFGDKNLFQQQSSEVDPRASEHWIPDNMVTNKPEVKPNHQGLASKKYQSDMYWAQSQDGLGDSAYGSHPGPASSRRLQELDLDHGAAGYTHDQSQWYEDSLECLSDLKPEQSIRDSMDSLALSNITGASVDGESKPRPSLYSLQNFEEIEAEDCEKMSNMGTLNSSMLHRSAESLQSLNSGLCPEKILPEEKPAHLPVLRRSKSQSRPQQVKFSDDVIDNGSYDIEIRQPPMSERTRRRAYHFEERGSRPHHHRHRRSRKSRSDNALNLVTERKYSAKDRLRLYTPDNYEKFIQNKSARELQAYMQNANLYSQYAHATSDYALQNPGMNRFLGLCGEDDDSWCSSSTSSSDSEEEGYFLGQPIPQPRPQRFTYYTDDLSSPASALPTPQFTQRTTKSKKKKGHKGKNCIIS 832 Q3U827 E3 ubiquitin-protein ligase RNF180 Rnf180 10090 Yes SL-0178 Endoplasmic reticulum membrane {ECO:0000269|PubMed:18363970}; Single-pass membrane protein {ECO:0000269|PubMed:18363970}. Nucleus envelope {ECO:0000269|PubMed:18363970}. UNIPROT Q3U827 UNIPROT Q3UW39 UNIPROT Q80ZX1 UNIPROT Q8CCR1 UNIPROT Q9CXV6 PROSITE PS00518 PROSITE PS50089 E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000269|PubMed:18363970}. GO:0016021 GO:0031227 GO:0005635 GO:0046872 GO:0031624 GO:0061630 GO:0030534 GO:0042415 GO:1901360 GO:0032436 GO:0031398 GO:0000209 GO:0050790 GO:0042428 MKRSEESTSTQSPEEQTGTLHCWRCRKCIASSGCFMTPLETQVVEQDRHESVDAQNTCHLWHMNVDALPEWISCLLQKAQWTVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLCKSRTDHQAAQGGRLMRPALKHLPHPGVPSGCDKETLLTGGGSKTRNHWLLSMARNSNGLGRLTEALCLEVRATYFEMKNEKLLFKASDPKCQPFVPQPDTGRCPSRASHRKSHSLDLNISEKLILLPTLYEIHRKPTAYPRLNETGPIDLSGLALPCSNSSCSFQSPPSFDPNMLLHRLSVAPHETQAQRGRECQCGLEASSVYSDHANANSLPFLMDLPSAGRSVLEASDQEEHLSQLDFLRSASFPLGTINHRLNNRERSKLRTLRRQQRRERWLQKQGKYSGVGLLDHMTVSNEMSTDEETEFPEEKDSYMCAVCLDVYFNPYMCYPCHHIFCEPCLRTLAKDNPASTPCPLCRTIISRVFLQTELNNATKTFFTKEYLKIKQSFQKSSSAKWPLPSCRKGFHLFGGFHRRAAPVTRRQFPHGAHRMDYLHFEDDSRGWWFDMDMVIIYIYSVNWVIGFVVFCFLCYFFFPF 592 Q3UFJ6 Transmembrane protein 184A Tmem184a 10090 Yes SL-0198 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}. UNIPROT Q3UFJ6 UNIPROT Q8BII8 UNIPROT Q8K1B0 Pfam PF03619 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}. GO:0030659 GO:0031901 GO:0005768 GO:0016021 GO:0048471 GO:0005886 GO:0030667 GO:0030658 GO:0008201 GO:0018992 GO:0032880 GO:0051046 MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFASLALRYAFPSQVYSEKKNSPVPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPAPSTHPGPASGSGGGKKSRNIEKRMLIPSEDL 425 Q3UJ81 Nuclear envelope phosphatase-regulatory subunit 1 Cnep1r1 10090 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}. UNIPROT Q3UJ81 UNIPROT A7E1Z4 UNIPROT Q8VEG8 UNIPROT Q9D3Q4 Pfam PF09771 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}. GO:0005737 GO:0005829 GO:0016021 GO:0071595 GO:0031965 GO:0006629 GO:0035307 GO:0010867 GO:0034504 MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGLFFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ 125 Q3YBM2 Transmembrane protein 176B TMEM176B 9606 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q3YBM2 UNIPROT B2RDK2 UNIPROT D3DWZ7 UNIPROT E9PAV4 UNIPROT Q5BJI2 UNIPROT Q9BT42 UNIPROT Q9Y609 Pfam PF04103 OMIM 610385 DisGeNET 28959 May play a role in the process of maturation of dendritic cells. Required for the development of cerebellar granule cells (By similarity). {ECO:0000250}. Q9RMZ4 EBI-2821474,EBI-2821479 Q96HP8 EBI-2800645,EBI-2821479 GO:0016021 GO:0031965 GO:0009887 GO:0030154 GO:2001199 MTQNTVIVNGVAMASRPSQPTHVNVHIHQESALTQLLKAGGSLKKFLFHPGDTVPSTARIGYEQLALGVTQILLGVVSCVLGVCLSLGPWTVLSASGCAFWAGSVVIAAGAGAIVHEKHPGKLAGYISSLLTLAGFATAMAAVVLCVNSFIWQTEPFLYIDTVCDRSDPVFPTTGYRWMRRSQENQWQKEECRAYMQMLRKLFTAIRALFLAVCVLKVIVSLVSLGVGLRNLCGQSSQPLNEEGSEKRLLGENSVPPSPSREQTSTAIVL 270 Q3ZBU9 UBX domain-containing protein 4 UBXN4 9913 Yes SL-0178 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}. UNIPROT Q3ZBU9 Pfam PF00789 PROSITE PS50033 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}. GO:0005829 GO:0005789 GO:0005635 GO:0006986 GO:0030433 MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSTQMAASWEDEKVTEASSNSFVAIKIDTRSEACLQFSQIYPVVCVPSSFFIGDSGIPLEVIAGSISADELVTRIHKVRQMHSLKGEASLANGSQSEGSVSTPSASFEHNNTSENCQSRNVELCETPSTSDTKSDSATGGESSGQTTVSQEPSGCSNQRPTEDLTVRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKRKQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEIKRETSTKERSTVARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVLLPAGRPTTSMVHSSSGDFWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSVRAASLETSNLASSSNSEKREPVRKRVLEKRGEDFKKEGKIYRLRTQDDGEDENNTWNGNSTQQM 508 Q3ZC61 MORF4 family-associated protein 1 MRFAP1 9913 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}. UNIPROT Q3ZC61 Pfam PF15155 DE Reference Proteome: Yes; GO:0005634 GO:0048471 MRPLDIVELAEPEEVEVLEPEEDFEQFLLPVINEMREDIAALSREHGRAYLRNRSKLWEMDNMLIQIKTQVEASEESALNHLQNPDDGAEGRGTKRCEKAEEKAKEIAKMAEMLVELVRRIEKSESS 127 Q3ZC98 Nuclear pore complex protein Nup85 NUP85 9913 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q3ZC98 UNIPROT A7E3X3 Pfam PF07575 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}. GO:0000777 GO:0005829 GO:0031965 GO:0031080 GO:0005654 GO:0005819 GO:0017056 GO:0030032 GO:0048246 GO:0006406 GO:0072006 GO:0045893 GO:0006606 MEEFDGEPTVTWIPGVNSQKKQMCFDWGPGEMLVCETSFNKKEKSEMVAGCPFIHIIRKDIDVYSKILRKLFNESHGIFVGLQRIEEELTGKSRKAQLVRVSKNYRSVIRACMEEMHQFAVADKDSAIGRQFSSQVSILSAVELIWNLCEILFIEVAPAGPLLLYLLDWVRLHVCEVDSLSADVLGSENPSKHESFWNLVTTLVLQGRLDEARQMLSKEADSNPTSAGMCRVLGDLMRTMPILSPGNTQTLTELELRWQHWHEECERHLQDGTFASNPHLESLCKVLLGDDAALLEHKELLSNWYHFLVTRLLYSQPTVKPMDLHLYAQSSLDLFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMREFLLLEYASGLFAHHSLWQLGVDYCDHCPELGRVSLELHIERIPLTTEQKALKVLRVCEQRQMTEQVRSICKVLAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKCFVDAASLLLSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELLRCLEDLTSGRPLCGEPDAQQLQDDDIETTKVEILRLALARNLARSIIKEGSLEGS 656 Q4FZC9 Nesprin-3 Syne3 10090 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum. UNIPROT Q4FZC9 UNIPROT Q8BMM1 UNIPROT Q8C117 Pfam PF10541 Pfam PF00435 PROSITE PS51049 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}. GO:0005623 GO:0005737 GO:0016021 GO:0034993 GO:0005635 GO:0031965 GO:0005640 GO:0005791 GO:0051015 GO:0090286 GO:0007010 GO:0090150 GO:0007097 GO:0051647 GO:0008360 MTQQPQEDFERSVEDAQAWMKVIQEQLQVNDNTKGPRAALEARLRETEKICQLESEGMVKVELVLRAAEALLATCQEGQKPEILARLRDIKSQWEETVTYMTHCHSRIEWVWLHWSEYLLAQDEFYRWFQKMVVALEPPVELQLGLKEKQWQLSHAQVLLHNVDNQAVLLDRLLEEAGSLFSRIGDPSVDEDAQKRMKAEYDAVKARAQRRVDLLAQVAQDHEQYREDVNEFQLWLKAVVEKVHSCLGRNCKLATELRLSTLQDIAKDFPRGEESLKRLEEQAVGVIQNTSPLGAEKISGELEEMRGVLEKLRVLWKEEEGRLRGLLQSRGDCEQQIQQLEAELGDFKKSLQRLAQEGLEPTVKTATEDELVAQWRLFSGTRAALASEEPRVDRLQTQLKKLVTFPDLQSLSDSVVATIQEYQSMKGKNTRLHNATRAELWQRFQRPLNDLQLWKALAQRLLDITASLPDLASIHTFLPQIEAALTESSRLKEQLAMLQLKTDLLGSIFGQERAATLLEQVTSSVRDRDLLHNSLLQRKSKLQSLLVQHKDFGVAFDPLNRKLLDLQARIQAEKGLPRDLPGKQVQLLRLQGLQEEGLDLGTQIEAVRPLAHGNSKHQQKVDQISCDQQALQRSLEDLVDRCQQNVREHCTFSHRLSELQLWITMATQTLESHQGDVRLWDAESQEAGLETLLSEIPEKEVQVSLLQALGQLVMKKSSPEGATMVQEELRKLMESWQALRLLEENMLSLMRNQQLQRTEVDTGKKQVFTNNIPKAGFLINPQDPIPRRQHGANPLEGHDLPEDHPQLLRDFEQWLQAENSKLRRIITMRVATAKDLRTREVKLQELEARIPEGQHLFENLLRLRPARDPSNELEDLRYRWMLYKSKLKDSGHLLTESSPGELTAFQKSRRQKRWSPCSLLQKACRVALPLQLLLLLFLLLLFLLPAGEEERSCALANNFARSFALMLRYNGPPPT 975 Q4HY71 ATP-dependent RNA helicase DBP5 DBP5 229533 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q4HY71 UNIPROT A0A0E0RW04 UNIPROT V6RQB4 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0003723 GO:0003724 GO:0051028 GO:0015031 MADLASRITKPDEVAAETPAETPAETAPAASGELGQADGNIEDLGGSGLQEPEWDVEVSLSELQNNEATPFHSATTWQDLGLREDLLKGLLSLNFLKPSKVQGKSLPLMLSDPPRNMLAQSQSGTGKTAAFVTAILSRVDFSKPDQPQALALAPSRELARQIEGVINAIGRFVENKKVAAAIPGVLPRGEPVRASVIVGTPGTVMDIIRRRQLDISQLRVLVLDEADNMLDQQGLGDQCLKVKNMLPKEIQVLLFSATFPENVMKYAGKFAPNAHSLKLQRSELTVKGISQMFIDCPDDNMKYDILCKLYGLMTIGQSVIFVKTRDSASEIERRMVADGHKVSALHAAFDGAERDNLLTKFRQGENKVLITTNVLARGIDVSSVSMVINYDIPMKGRGDTEPDAETYLHRIGRTGRFGRVGVSISFVYDKKSFDALSKIAEMYGIDLVKLDTEDWDEAEERVKEVIKKNRAQASYAPSATEPKAAAGA 488 Q4PCB8 Protein transport protein SEC13 SEC13 237631 Yes SL-0178 SL-0185 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}. UNIPROT Q4PCB8 UNIPROT A0A0D1E5R0 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0030127 GO:0005829 GO:0005789 GO:0000139 GO:0031080 GO:0005198 GO:0090114 GO:0051028 GO:1904263 GO:0015031 MTTVTSSSAGLSLSAERPKNIETQHEDMVHDAQLDFYGKRLATCSSDRTVKVFDIVNGTPSTTAETLHGHQGPVWQVAWAHPTFGDILASCSYDGKVVIWKDNGAGASIGASAPYGSQSAYGAPTSSAGGWTKIKEHTLHTASVNSISWAPHELGSILACASSDGNVSVLTFNNDGTWAVDLVAAHPVGCNAVSWAPAVVPGSLISAQSVGANAGAASNGEAKLVKRFASAGCDNTVKIWEFSQEANRFVEVEALQGHSDWVRDVAFAPNVGLPRSYLATASQDRTVLIWTQDSPTAAWSKTALNPISASAAAGAGSNKFPDTVWRVSWSVSGNVLAVSCGDGKITLWKENLKGAWECVSEMDS 364 Q4PT37 Nuclear envelope-associated protein 3 NEAP3 3702 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:27630107}; Single-pass membrane protein {ECO:0000255}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27630107}. UNIPROT Q4PT37 UNIPROT O80530 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 GO:0005654 GO:0043621 MPTSVSLREDDPLLKDLSEKKQSFRRNVVSLATELKEARTRLAEQERSCSKEAMSRQEAETRVKRMEDEMHELAKELNEKVEQIRASDVATEKFVKELADIKSQLAATHATAEASALSAESAHSHCRVLSKQLHERTGSLKEHEDQVTRLGEQLENLRKELRVRESSQKQLRDELLKVEGDIMRAVSVVKTKENSEVRNMLNEDTPKNSERINKLLTAKDDEIARLRDELKIISAHWRFKTKELEDQVENQRRIDQELKKKVLKLEFCLRETRIQTRKLQKMGERNDVAIQELKEQLAAKKQHEADHSSNQNLWDKSGFKIVVSMSMLILVAFSRR 336 Q4R599 Translin-associated protein X TSNAX 9541 Yes SL-0198 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}. UNIPROT Q4R599 Pfam PF01997 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}. GO:0005794 GO:0005634 GO:0048471 GO:0046872 GO:0043565 GO:0030154 GO:0007275 GO:0007283 MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSAPDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTDDNGKENKTPSSDTQDEQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVSKKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVSSVKTEMIDQEEGIS 290 Q4R707 Protein spire homolog 1 SPIRE1 9541 Yes SL-0198 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}. Note=Punctate spots in perinuclear region and cytoplasm, co-localised with Rab11. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion. {ECO:0000250|UniProtKB:Q52KF3}. UNIPROT Q4R707 Pfam PF16474 PROSITE PS51377 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}. GO:0005623 GO:0005938 GO:0032154 GO:0030659 GO:0005856 GO:0005829 GO:0048471 GO:0003779 GO:0030036 GO:0045010 GO:0036089 GO:0051295 GO:0070649 GO:0046907 GO:0040038 GO:2000781 GO:0015031 GO:0016192 MANTVEADGSNDEGYEAAEEGPEDEEDEKREISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLAKVKSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLDVTTPESTKNLMESSMVNGGLTSQTKENGLSSAEQVPAQRKKLLKAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSPPGPSEYCPSERTISEI 584 Q4R834 NAD-dependent protein deacetylase sirtuin-2 SIRT2 9541 Yes SL-0198 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}. UNIPROT Q4R834 Pfam PF02146 PROSITE PS50305 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}. GO:0005814 GO:0005813 GO:0005694 GO:0005737 GO:0005829 GO:0097386 GO:0030426 GO:0044224 GO:0043219 GO:0072687 GO:0005874 GO:0030496 GO:0072686 GO:0043209 GO:0005720 GO:0005634 GO:0033010 GO:0033270 GO:0043204 GO:0048471 GO:0005886 GO:0043220 GO:0005819 GO:0003682 GO:0004407 GO:0070403 GO:0046970 GO:0034979 GO:0033558 GO:0016740 GO:0042903 GO:0008270 GO:0007049 GO:0051301 GO:0044242 GO:0061433 GO:0071872 GO:0035729 GO:0071456 GO:0071219 GO:0034599 GO:0048012 GO:0070932 GO:0070933 GO:0022011 GO:0010507 GO:0008285 GO:1900425 GO:0045599 GO:0070446 GO:0010801 GO:0042177 GO:2000378 GO:0000122 GO:0061428 GO:0034983 GO:0014065 GO:0051987 GO:0051781 GO:0043388 GO:1900119 GO:0045836 GO:1900195 GO:0032436 GO:2000777 GO:0045944 GO:0043161 GO:0006476 GO:0043491 GO:0051726 GO:0031641 GO:0090042 MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMILGLGGGMDFDSKKAYRDVAWLGDCDQGCLALAELLGWKKELEDLVRREHASIDAQSGAEAPNPSTSASPRKSPPPAQDEARTTEREKPQ 389 Q4R914 Calcium-binding and coiled-coil domain-containing protein 2 CALCOCO2 9541 Yes SL-0198 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}. UNIPROT Q4R914 Pfam PF17751 Pfam PF18112 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:1901098 GO:0098792 MEKTIEDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCRYTFTQNFIPRQKDWIGIFRVGWKTVREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETEQLEHLKKENGHLFLSLTEQRKDQKKLEQTVEEMKQNETTAMKKQQELMDENFDLSRRLSEKKMIYNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGAGQNPGLVYGNPYSGIQESSSPSQLSIKKCPICKADDICDHTLEQQQMQALCLNCPICDKIFPATEKQIFEDHVFCHSL 398 Q4VBT2 Nucleolar complex protein 4 homolog noc4l 7955 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}. UNIPROT Q4VBT2 Pfam PF03914 DE Reference Proteome: Yes; GO:0016021 GO:0030692 GO:0031965 GO:0005730 GO:0032040 GO:0042254 MAPSGDSNVKEHNNQVSYKKAINTKTDLILQNKKHANDIFDVIEYLQSEKEKEIIFATNACSKIFCELIERGDLFVGELPKEEDLAQGDRSAEEKYHIFMRHRYNSCVELMLENVSHESFQVKETSLCAVMKFVATEGKHPLQNLDWSEHYNFPRELIQALVEHLLSEKEDMSLLISRFQEFMEKDDVRYYVMSSVRYSTATVMERNKKAVIPVFQNNVFNLLTTINIPNQASEMTNFLVQQQSKHDDWKAAKLKEHKRAFEQMWLLFLRYKLPGSMYKKILVILHESILPQMSDPKLMMDFLSAAYDIGGAISLSALNGLFVPIHEHNLDYPDFYKKLYNLLDPSIFHVKYRARFFHLANIFLSSTHLPVYLVAAFVKRLARLSLTAPPTALLILLPFICNLIRRHPSCRVLIHRPSAADEPCDDPYVMEEEDPAQCHALESSLWEIKTLQNHHHPDVSKAATMINEPLSAQEEDISELLELTTFELMERELKGEKKTVPLEFDMATDLLKSSREVLGVHFTLE 525 Q4VKV5 Matrix protein M 1560034 Yes SL-0415 SL-0418 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}. UNIPROT Q4VKV5 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}. GO:0044200 GO:0055036 GO:0039660 GO:0039702 MLRWFSFGSNEGSEVAGNGWSVKPIGNMSIKKDDPVGFPQGYQCLLKVIIQLEKKDPTKSDVSELIAGWVKRYSGPHLLERLIKALIILTVPKLSRENIDNHVKLGGLFEGQVTFHFSSRDLIPTKYLSYATSIRTTVKGIYSYLSIEAELNPSSHQGTSVAKLLRASDVAKYYDNTLQSIFSQFEIKNVTITDDQIIFN 200 Q4WNB5 UDP-N-acetylglucosamine transferase subunit alg14 alg14 330879 Yes SL-0178 SL-0182 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}. UNIPROT Q4WNB5 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPLSTLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVKRSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD 228 Q54B27 Exocyst complex component 6 exoc6 44689 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. UNIPROT Q54B27 Pfam PF04091 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0090543 GO:0016020 GO:0048471 GO:0017137 GO:0070177 GO:0006887 GO:0006893 GO:0015031 GO:0006904 MSNKKQKEEINTAGGSVILKTMVRDKDKEQKEEKREKKEKKRLEKKEAENVKKEKKKEKKELKKIGKAGRSGSITSDSSTHSGAQEFDSYGNDSNGGGGGLSASIDSNGLSSSGQPMQTRHLEKEVGEKQGIYSLSSQDRSSSLPHSSQDDQAKPLITESEIFSSESFLIAVSDTDHLGPAIKSVFENNKEKEVIKILNAYIAQKDLDIEKICGENHEGFINSVTAFLGLKGENLDLKQDVINLNYELQEIGRKYVTKAEELFAYKQIKDNIKRTKEVLNNCQYAILLGMKVDEYVQQKKYYQAIKNMDQLHNVYLKKLSDFQFARNMDYNIPVLKEKIKKLVKDEFNQWMVEIKEKSAVIGKLGMIQTSKKLLKEREINPLKIKTTFGENEQIWDKILDIPPIINSSSIGSLALYPTLNSPVTAPIYSPNSGKTPSSFGFNKQINEKDLKEDINQFSPFDESDIQFHPLYQCLFIHASIGQLEEFQAYYTLNRLLQFQLVIQPKESGQVWELFLQQILGYFMVESKVIDSTEPFLSKTTINDSWNSALVKVTSVLQELFTHCVDTQPLIAFKKFVLIFTNTMSFYSYHVQPLYYFLDTMKEKYCQFSIKEAVERFTIILERDSHCSLIIESLEEYKSLILANKLDILERQQLRQLQNSLNNNQFQFGDKNLNNNNNNDDDDDYFDEDENEDDKISKRLPKSFLFSKMVPQFYTLIKKFISEFYEFSDQLTENENFIIRSTDTLIKKINEVLYSYLTQSQAVPQVIQLVINLQHLISGCSFFKDYLNSLILGEDYQKNQSIVNETNKVILNSQNLLYTTKSHGEKLIIKLCEQKIEDLMSSAANIEWFPQNAIDDRPRDYIIDVCTFLEVTLPFISPLSQNLKEEFITKAFKNISESLFSLIYDDQLKKLNLQGVKSFDADLKYIETYVKEKANEKERTTTTSRNMVGYFVELRQLTNFLLSDNPEDFVDPKIKAKHYNLITNIPQLLNILNKYKEESKGFTTSKEIKDRNKKIADAIKKIKDSL 1025 Q54BP6 Exocyst complex component 3 exoc3 44689 Yes SL-0198 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}. UNIPROT Q54BP6 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0000149 GO:0051601 GO:0006887 GO:0015031 METVSLVPLEGLDDLSAQSAAIKKIEQNFSNIDSLASVTNHKISLIQQKKTIEAQIKNEVHSELEKSKKGLETLYKSYNRINRMDESFSDTVELCSETSNLIGHYQLIKKVNTVRVNLINILKEVDRLLTIPEKAAEIEQLLSDDLNLLEIHSKLRELERLHQKALKQFESNFEELEAIKEMFSSVPELSHRFENKIWNIVSNSIDIAQIKPAVLVKVAQIIEREKLHEQKQKEKKSQNSLISSEGIHDDDDDDDDTEVNLNNSNKQQNNENENSSSNNNNNYDINNEDEGYDRNRSNYGDRFLEVLIQSISGKFEPMFLNSHNDLVQTLKDVNKMVDELFIVMDIVQECYPPSYDLFNFYVDQYHTKFYSLFGSFSNLMESSHVNNNYQVVVTKNIPSAHILMLVEWVVKNYSRDLSRLGIQDISPPLLDSLDPLIKIYKMHIKQLMREWCDNIINNDNQNKPEVVDGQYCSLAPIQLFESVASQLDIAAATKCQKLVVGVMEEVVSALMYFQVQSITLLQERNHEIKLENVIAYVNNNSKCYDHTQTIVDKVSNILDSEHMGYLDFDPVLEGFLNVSKVATQAISSVIFRDLDECIHKFYTVEWYQEDLMQPIINTFEDYVTNDIQKYILENYLKRLALLLLDTLIEQLLAQLIGGKNKFNENTYKILSNDCDKLLDFFKKYLRLSVVTAKVQILEDFKQMITSSIDMVPVYFRSVINFHKDINERVVELVLYQRTDISKSEITEVLGQIKTIVETVHTDPTNPPTGIFSRMNIYQRGWFS 783 Q54C85 Importin-13 homolog A ipo13A 44689 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q54C85 Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}. GO:0005737 GO:0005635 GO:0008536 GO:0006606 MYNNNGFHEETNIDESQFTVEKVETVLKSLYFPQNNDYSALPQIQQWLIQFQKSFSSWSIAPLLLMSNIKEIQYFGASTIENKIKNNWLSLSQDMKKEFLDNLLLFLKTQITKCSTVVITRLCLAVSVIACHSTTDLWANPILDVLQLSFQDINNLDCFNPNLVNLTLELLTIFPEELTNADYITQEKRNKVGLQFNKHNSKVFEILCKIMSLPQNQQTLIFMKSSLKCFKSWILFDCSPREYLIDSDLILKCFEAVSNNPKLVEDFLMVLDEMFTFMGGKIFRSYTSAFSLVLSRILMIFPSFYILALQEENQIFNQIFLLFSHIAENHIKTLLKNPELSNNFFKALIQMALKGDFETCELLSPVITEIAALHELHSTSSTTEATTTTIATTTTPTTTSDCDISGWYQYLGEMVEVFRLKSMYPLDKDISDLYEEDAEKFFAFRVIAGDSVLEVYNILEGKILQQLLNSLWSDIQSFPTTKCWQSIEATIYLLSCLSESITEDTEFVPQLFSILGQLPIQSTPLIKSTMTLAGNYSNLIDKSTIFLEKIVKDFFPAFENPDLKSVASQSFLSISKNSKCASILSNSITQLISLCAPILSNNNKILDDPSNFNILEALLYIISTLPSDSQVLNYSTQLLYPFILFIKNYYTNQLQQQQQQQQQQQTELRLLLSSINLLTKFCKIYDDEQVNEYGTTQQENNNNNNNNNNNNNNNNNNNNNNNNNNIKPVFEIINNIIPIYGELLSLNTLESSIIEAISIFYKKAIMINNNHQNITNIPEINRQLTLAFLKHKPLSLVLSTLSISIVNLPKEQHLDFLADSLSSISSKMIQIWSEKSNQNNKKNNKKINNNIDIDNDNENNNNNNQIQFENNELNEFKNLKISIYPDITKEYFTMITQYIRYNAVSIPQGVISHLFSIILVNITKIHDKVTARACFSFMALIITKSKEMKSQIKWEPLLNEINGWLSIHGELFIKQILYSAGGGIPRSVVQFISEVIASLVSSYPDVFRISALKCLSVDGFPSSNITKEQKEKFLNSLMLYRSKKLPLKIVTDFSLVSLGIATNQ 1064 Q54DN3 Exportin-7 xpo7 44689 Yes SL-0178 SL-0185 Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. UNIPROT Q54DN3 Mediates the nuclear export of proteins (cargos) with broad substrate specificity. {ECO:0000250}. GO:0005737 GO:0005643 GO:0005634 GO:0005049 GO:0051028 GO:0006611 MSIQSEQDFFKFEELCKDFYLKPEETIKIDDILHQYFLNPNFLIEYKQILSFTKNSYVVAQVIRGLIKCVTSFWTSLTPNQKNDMSKSIEHHCIGLRILKDIISEFNEYIGEHLTVLQHRNISISLRDNILLDIFCISLESLNYALANSMDEKFKSIKELALDLSYSCLSFDFIKTTSIDSSEEILTVQIPSQWKSTFDENNPLELFFKIYKQYHSTKSLECILQIVSIRRSFFTTEDERVKFLASIVQYTTEILKSNIGFNEPNNHLVFSRVIERLKTNYHLNNLVTVVGYNDWISNLSTFTIDTLKNPQFSPNSIYFLLTLWAKLVSSIIYVKGDPSKTYLEKYSPIIMESFINSKIDNSYSDEEDEHLMDYEKMVEILEGIPHLGRITYQATCRQIILLFDSISSKFLNETNPTQLEVYERQCAWLVYIIGCLILGRTSINSSEEHDKIDGELSVRVFILIGYNDKKLSAESNTQYQYRTSRISLELSFIYFMQNFRRIYIGENSISSSKIYQRISELSGPTDHTSVLFSIVQKIGFNFKYWAENDEIIKKSLDMFWESVNGHSTSKMLIDNKITKDILKTHSSQVFPFLEKNSNPRNRTSLYKTIGKLLFTDENMGFFDEFIAPFDDTIKHLLNISTPEQFRTEEIKRKVIGLLRDLRGIITSANSKRSYLLFFEWIHLNFSEVLIKIINVWVDSPEVTTSLLKFISEFVFNRQSRLIFDSSSANGFIIFRDTSKILVSYASLILKANISKQDLYKFKIKGIQTSMLLFTRCLVGGYCNFGVFELYGDPSFTSAIDYIFQLCLSVSLDELMSFPKASKAYVTMLEALCLGHTLSIIQLNQQYFIHIMKSLHRCLDSQDVTMSSSSCTSIEKIITVCYYHLKKKNSQCLQAIHQNFFSNSNILYEIIDKIISIIIYEDNFNQFMFSKLLLTCIIFHQDTFTTLKQKYIHSFNSQCPEKVEKAFVQLMENTLDNLETKNKDKFTSNVSIFRKEMKLISSSTGRYL 1007 Q54DS8 Protein SEC13 homolog sec13 44689 Yes SL-0178 SL-0185 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}. UNIPROT Q54DS8 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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. GO:0030127 GO:0005829 GO:0005789 GO:0000139 GO:0005765 GO:0005643 GO:0031080 GO:0005198 GO:0090114 GO:0006888 GO:0051028 GO:1904263 GO:0015031 MATQNVDSGHEDMVHDAQFDYYGKFLATCSSDKMIKIFDVGGENPQHLVDLRGHEGPVWQVAWAHPKFGKILASASYDRKVIVWKEVGNNSWSIIHQYAGHELSVNSISWAPHEFGLSLACASSDGSVTIHNYNNNVWEAPQKIQVSQIGVNSVSWSPAAIPTSLVNSANTIIPAPIKRIVTGSCDNLIKIFKNVEDKWILDKQLEDHKDWVRDVAWAPNIGLPYSKIASCSQDRSVIVWTQDENGVWSGKPLPKFDDIVWRVSWSVIGNILAVSCGDNQVTLWKEGVDSEWKLISHVENN 301 Q54ED3 DnaJ homolog subfamily A member 1 homolog dnaja1 44689 Yes SL-0198 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}. UNIPROT Q54ED3 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. GO:0005829 GO:0005783 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0031072 GO:0046872 GO:0051082 GO:0006457 GO:0009408 MVKEKEYYERLGVKPDCTEDELKKAYRKMAVKYHPDKNQGPGKDAAEAKFKDISEAYEVLSDPEKRKMYDSYGSEGMKESGFHASSAEDLFSHFFGAGGGGGGFSFGGGGGDDFGGFSFGNMGGMGGMGGMGGGHKKRRKGEDIEHEMNRSLEELYNGKLVKISISRDEVCKTCKGSGSNKPGVTTTCPTCNGSRYVFQKKQVGPGMIQQVQTACHTCHGTGEKIKEEDKCKECKGKRVIQGKKIVQFQVEKGTRDGERIMLQGQGSEYPGVPPGDVIITIREKPNVNFKRNGDNLIYTKRLKLLDSIAGSQFIINTLDQRKLWVNHEKGDIIKQGDMRYIENEGMPIKGTSRKGKLIIAFDIEYPSNLTNDDIEKLSKILPKAATPSVSKSDCKSVGLSKVNFNTNEQSSHGGAGGAYQQHGGAYGHQKQQQQGFNPADFGAQFGGGGPQQAQQCQQQ 459 Q54EQ8 Nuclear pore complex protein Nup96 nup98 44689 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q54EQ8 Pfam PF04096 Pfam PF13634 Pfam PF12110 PROSITE PS51434 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}. GO:0031965 GO:0005643 GO:0044614 GO:0008139 GO:0003723 GO:0017056 GO:0051028 GO:0051292 GO:0000973 GO:0006606 GO:0006405 GO:0034398 MFGGQFGSFGAKPAATASPFGAPSAAPTTSLFGSTAPSSGFGGFGSTAQTTQPTTGGFGGFGGFGGATTTQQPAASPFGGGGTGGSGLFGSSAQTTTQQPGASPFGGGFGTTTTTTTQQPGASPFGGTGGGLFGSSAQTTTQQQGASPFGGFGGATTTQPSLLSGATGGFGGFGGSTTSGTQLGGGGGATSGAFGGSSSPFGGSGGATTSSPFGGGGGSFGATTQKQYGTPIPYQQTTIEGNTFVSISAMPQYNDRSFEELRFEDITHRKDIVYKTGGGSGGGNSLFGSTPTTQPSSPFGAQTTTQTTGGLFGGQTTTSPFGGQTSATPGSSLFGSTQPTQQQTSGGLFGSVQPTQQQAGGGLFGSMPSTGGSSLFGSTQPTQQQTGGAQPTQSLFGGQTQTTTSPFGSQTSTPFGQPQQTNTGSGLFGAQQTQQTNTGGGLFGAQPTQQTSGGGLFGTQPTSGTGLFGTSPTAGGTGLFGTTQPTSQGTGLFGTTQPTTQGTGLFGTSPTSGTGLFGSTPTSGTGLFGSTPTSGTGLFGSAQPPQNQQSQTSLFGNTGTGATNTGTGLFGSAQPSSNPGGGLFGSAQPSTTTGGLFGSNQPTAQPTTSLFGNTTGSVGGLGATPNITSGLFGSNPAQTGGLFGSTQPTTQTSLFGNTGSTGGLGAQNGGGLFGNLSQPTATAGQGLSGGLFGNLSQPTATAGQGLSSGGLFGNTLLGQPSTQGLSSALPTLGLGLMGGQPQQTQQLPQGSLMLQQTQQPLQQQPLQQQQQPLQQSTIQLNNQINSASPYFPISSPAPFATFVKDLTSTSKVVSPPSYTQRSLSHHGYIPKSTTKLVPRRGPNNVDLGFSVIQNQNGLFPIDKFITKHSKSLNINTTNETEDTLRSLNTKSSSLFNNNNNNNNNNNNRNVNTNVNDYQNNGLPSSSLYNSNINQLSNNNNNNNNIYNNNNNNNINNNNNNNNISTQFNLRNNQSSSDNLNNDKSLSSSSSNKSQQQQQKEQKEEQPPKPIKEKEFINPNAPKLTRDGYQCVPSIKELSKKTDKELSSVQGFTISRDGCGSIYFPGSTNLVALDLDDIVDIEPREVSVYKDEETKPEIGYGLNRDAVVTLENCWPKNKNGEVVKEDGTILDKYENALKKVSAKSDCGFVSYSRSNGTWVFTVKHFSKYSAPDFDEDDQQMQQQTQQKQQQTQPSKVTFQQPSTKLTKPKFTANLDNFDSDSETSSGDENQDEMVPQKKTPFIKRVSNRESGLFDTPSVVPMSEKIETTPSKIARVSEPTSQSSRMSNNALKFSTFNPQQQQLQSSRFKSTGLSILSNPVKNLIQSDVNNEQSMFSNTTTTSTTRIQPLPSQQHLVQPIPTTISLNKNYFSKVRIDPQVYDRIVPKEESITNQYRMKNERLNHSTQDVSLFMRRSFRVGWAPGGKLISITKSSFKNLLIKKLPTDTKEDKKESIIKFLKNHHSHSSLVPENLKSIGWFSISNVQEQIESQLTLNVPSSQSVYYNRIWSLISNLWGNVLKGNGSKYINTNYSEDTIRKLNLNQWLKDVIAPLLRDEMDSLRKKTNSNYLEQIFSYLSAKQIKEASDLANENKDFRLATMMSQIWSSSESGKELILKQLTTYHSNGSDEFINEKRLEILHLIAGSVNKIYKNLNDWIRCFAVSFWFKYSLEYSIEDSVENFERSFNAHRSVYPLPPYLIKSTSTNSKQIEEQQHYYDICFLLLKLFAVNRGSSHFDKFKNIFYPENIGQDLLDYHLSWNLYTVLKSIPSLNKQPDLVNASNLHSSFALQLERLGLWQWSIYVLLHTPDQSNHVREEAVKSLIARAAPVITSEDRVFLTTKLHIPEIWIDEAKAWYSGYDCNNDIYDQIDALFKSYQYTKIHDIIFSNIGPNYIIQKRYHSLKDLLIRLEPHSSFISTWRYGGSIFLEFADICIQYKEILSQLSNTAEEIQRTKYYVNLKDITTRIVNILSDISKITQSSEIKNTSASYKQSLSFMSEALITKASLLRDLPESIVKLVSTNNLVSTLNSLPLTQDYRSKNLESLTDQIQDTLLNSIYQ 2053 Q54EV7 Exportin-1 xpo1 44689 Yes SL-0198 Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. UNIPROT Q54EV7 Pfam PF08767 Pfam PF18777 Pfam PF18784 Pfam PF18787 Pfam PF03810 Pfam PF08389 PROSITE PS50166 Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES). GO:0005737 GO:0005634 GO:0048471 GO:0005049 GO:0008536 GO:0006611 GO:0046825 GO:0000055 GO:0000056 MENILNFNEPLDINLLDQIVSVLYNPLSNKNDIKAAQMVLGKFQEHPDAWSKVDTILETSKIVQTKFIALVIMDSLIKYRWKSLPREQCEGIKNYIVSLIIRLSSDPQTSSREKLLVNKLNLVFVQILKQEWTTNWSTFIPEIISSSKTNESLCENNMVILRLLSEEIFNFSEEQMTQTKIQTLKITFEKEFSLINDLCFYILENATRASLIKATLETLQRFLNWVPLHYIIEVNGGIAEPSKLVKLLLHKYFPEPLFRNSTLKCLTEIGNLNLGNQQYDAVFIAIIDKFMNQIKFIKPDPSKIPQDYEDGDQGERSFIHTVSLFLTGFFKSHLKIMENSLNIPYLTLAHEILVNISNIDELELFKICLEYWNFLSSNLYSDIATFTTTLLSTPPRLQLYKSVLSKVRVVLIDHMAKPEEVIVVEDENGNIVRETTKDTDSLTLYESMRETLIFLTHLDSENTQHIMLEKLQTLISGREFTFQRLNTLCWAIGSISGAQNKEQEKRFLVTVIKDLLELCQNKKGKDNKAVIASDIMYIVGQYPRFLKDHWKFLKTVVNKLFEFMHESHPGVQDMACDTFLKISKQCKRKFVVLQVEESQPFINELLNQLSTTIAHLEQSQIHTFYEAVGYMIASSSDAAFREKLVNKFMELPNHSWLQIMGAASVKVESLLTVEVARDILNLIKTNNRAAMSLENCYITQISKIYLDLLNVYRTYSDHISRNPNIYRETLGQAMRSVKKETLKLLETFIEKSSDKQVIYSNFLQPLLEAVLGDYRTNIPETRDPEVLSLMTAIITSLKQLVHPEVPKILEAVFETTLSMITKNFEDYPYHRINFFNLIRAINSNAFTVFHNLHPQQFKLLIDCVVWAFKHTERNISETGLHILKELIENVSKNSDVANVFFKTYLVSLLNDILYILTDSFHKSGFALECDILRMMFQVVENGVVKIPLFDPQQANFPSNSEYVKEIVVTFLSASPNVSRPQIQAFVTRLFNLANINNNDFKSATRDFLITLKEWKSHENADLYSDEKNIEKALALKKQSMIPGMVRPNDVNLEMNDL 1057 Q54HI5 Lamin-like protein lmnB 44689 Yes SL-0178 SL-0179 SL-0182 Nucleus envelope {ECO:0000269|PubMed:19466752}. Nucleus inner membrane {ECO:0000269|PubMed:22090348}. UNIPROT Q54HI5 PROSITE PS51842 PROSITE PS51841 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}. GO:0005882 GO:0005635 GO:0005637 GO:0030527 GO:0007098 GO:0051642 GO:0010847 MDMSKKKSKRASPIESSQEEIAISTSKTATTEKPKKTKTTTKKKASQPSQEVVMETESEVEITTTTTSTSTTNNNNITTTSTSSQQSNGTLSSSSSPTIQSIPTTPISKYIPSLSQIGTPLSPNRAAQRLREKDELSLIHNRLKSALKKLESAETELEKKNQEYEELDQKHTATIKQLKQRSDQVEKQLIEEQNQNSDLTSNRNILENELKSKESVWKKEKDEILLKFQESINKLNQENSLAQSQLKSEIVSKEYEIDGLKSEINRLKDDLQYRIREGEEKSRKLLENEYNRFKGKEEEYNQLIVSKDEEIKKYKFELKEKEKSSNAMNKKENELNNLIQAHERQIEDMRDSINREWELKAAQMMEEHHARTIHLQQAVDSFNEEKERIKSQMETLNGQIEDINIKNNEYEDRIKEMNVLLSQKDNSIGELGVEIEESKKKMRKQMADLKSKDGQIALLQIEINTKDNKCNTLQTETNRLKSELYSITNQIDPEIPLDPEINSLKELVKGFEKTVDDRKRKRSKLQHEFNAAANQDQNGMTIEEQSSTSTTTTTSATGSSSSTSHLDNIDSSKLPTGPEQSELFNPDTVSFSLVDSNQEFIKLSVHGDMDNGLSISKWRLIVVKPDGSKSGFSFPDGIQPFKGIKSVTVWTGRPRPQGTPTENEFYWARTELWTSPVEGTIVKLVSPSEETTTVTLPADGIYQKPSSAGKSNCLIM 716 Q54MI3 SUN domain-containing protein 2 sun2 44689 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. UNIPROT Q54MI3 Pfam PF07738 PROSITE PS51469 DE Reference Proteome: Yes; GO:0005737 GO:0016021 GO:0016020 GO:0031965 GO:0005634 GO:0005773 GO:0031154 GO:0000281 MIINKKYILFILLLLFITSCTIVFSQQQQQQTEQSEQTEQAINNDVNNSINDIFENDSSKQLRQPQQQHTIVDDGNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNPIDNKDILGLKKLALLKQFEEQKSKSENDINNDIVILNLENDNPNQIIETTTTTLNNSNDNKNNIIDDNQDEKLNENIKEDKNEIKNEIKNENQEKDKGIIDVEKDENQPNIEEKGKEKQNLLEKGIENENQNENQIQIEKEKEIEIEIEKEKEKENKELIEESKTEKDNQQKENKENTNEINVTVVEEPEQPQPQQQNQQEQQEQQQQEHKEEQQQQEQQQQEQQTQQEQQTHQQQQEHQETQKNSSEETKTQSPIQVNTTDVNNEIELKNEGDNNSQLNDSSIPITSPLTNDNDTLKTTKEDSNNNNKNEVINNQTPLIDEKNHQHNYEGNNRNGDDVSIISNIPKTNKAPETQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHVVLTPNDLPDKFNYASSECGANVLQTNKEAWEVSSILASSRDRYLLNECNKSQWFVVELCEEIGVQIIELANFEFFSSMFKDFIVLGSNRYPAQSWHYLGQFTAENSRKQQYFVLKEKAWYKYLKVKILSHYGDQLYCPISSFKVYGSTMVDDLKNQVDINISELEKFQRDLSSIPYPMEIGSDTSYSTTTSTTSSSSTSSSYPSSKTKSSNSEYPSWERIQSFSEKLRKNVEQQLIQPPSVLNTNDNNNNNNNNNNNNNNNNNNNNNNNNNEEQFIYYETNGNGGPPSTSTSTSSSSSQNHQARTPQSVFKTLADKIKAIEFNQSIGNKFMEKLERYYSEEIKNLKFDVSEFLNDIIKLGNSLDEKLKDHRKYDDNKFKETSKEIKILKEKIEKLEEQKSADRNFYLVVTLVSLLIGLLLKPLFTSSSSSSNKSYPNSMPNSPTYLNSGSNNYNNNGIINSSGGSGGGGGNLQNSSFIGINGQLNFSDDNISAFLNSSCSNFGLNNNNNNNNGINNNNNNSNSNSNNNSINNGSININSNNSLQQRIHHNKYIHQRRNSSPLVGVQLESFFSPNAIPPTIPIVPQDDNNINYNYNNNNNTNNINNNYNYNNNNNNNNNNNNNNNNNNNNNSDNYNNNNNSNNNVNSPSSPTPSSIILSPKFITSIPKNINYYNNGGSGSHLKNRFSRQASESVLSQNHYQINHQNHSLNGVTTNINNNNSNSNGNSNGNSNNMTNGLPPVSMPSSSSHDNLLLHRGNNQSKKYKRRSHL 1278 Q54NA0 Nuclear pore complex protein nup85 nup85 44689 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}. UNIPROT Q54NA0 Pfam PF07575 Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}. GO:0031965 GO:0031080 GO:0017056 GO:0006406 GO:0045893 GO:0006606 MFSLNPQSNGNSNNLFGNVTLGNFSNNSNNLFGGSSTTSTNTNNSNNLFGGSSTTNSNNLFGSGGSSTTNNNNFNSNFNNNNIKNENKIKNGKKFYNFRWSPTGEILLYNTLNNFDNHNFDQKNGGSDTIRYEMNTTLSTIKKFYNDLYTNFETMQRIAGLSNQVIPDDRVREISHHSRTYLSVILAAINQMSKSQKTGSYIDDEDSCMNCDPLDNDLIKIQTPRVLEYFKQYPNKTLIFFCGSIDSIYPYLCSKLSMETKSKCILIARESNVPNSKRLDLIRTISNQGELKILNKDEYSNRYQIANENYGELDDVLTLEIDDTYLAYEREIDNLICMSTMWRVANLFYFSVSSSSNSVSPTQLLDCIELERKELLNSIEQQGTQDPMDSEYYNQIARLLVCGCIDQVIQQLNILSRAPRSASQIKSTSRKSPINLLIDILSSIPLKKKSINGGGGAPLYPNEHLIQWNKWHQETQKILSQYIESGSSSTNQVDENLLPIVKILLGDQQTIMSTCNSFLQLVVSNILFVEYTTSTTQLRQLFTQCYQTIQAPTTVDKIFLSFATKDLDITLKKIFKHSPAWLAVHLSDLLYHHPYVMRKLPNSESQLTNIREYLLSDFGQSLASDSSLLSIGCNYLKYVKNGGLEMIDQFISRQPIHFEKNAIKMLDKWATSVETKNSIYKMLSLQDFKRKRYAASLNWLMLANDNSHITLLSNYLLENQLNSEFLNDLQSLLEKNDEIDCNINNNNNNNNNNNSNNRISGNNNNNMIIDENKFEITNNSELIFLIRYRELISLWKERSFKEYSSSLCLMFKDRVIPKRFWLRLLIDCVPLLESLKNLYFTYQDTLLLQSCLEEIIQSHLFDQYSFNISNQDIQILRSALARNLAKSIIS 890 Q54RV6 Trafficking protein particle complex subunit 2 trappc2 44689 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. UNIPROT Q54RV6 Pfam PF04628 May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. GO:0005783 GO:0005794 GO:0048471 GO:0006888 MSTFTFLIIGKNDNPLYEIEFPITVQKKETYVLQYIAHGSLDIVEEHVWKSNNMYLKIIDKFNKVQISSFVTAGHIKFLLLHEKKDEDAIKNFFVEVHDLYLKILLNPFYEYNKPITSTAFDAKVRKIGTKYF 133 Q54TL0 Kinesin-related protein 7 kif7 44689 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:9693369}; Single-pass membrane protein {ECO:0000269|PubMed:9693369}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9693369}. UNIPROT Q54TL0 UNIPROT Q94463 Pfam PF00225 PROSITE PS00411 PROSITE PS50067 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}. GO:0016021 GO:0005871 GO:0005874 GO:0031965 GO:0048471 GO:0005524 GO:0008574 GO:0016887 GO:0008017 GO:0003777 GO:0030705 GO:0007018 MESPVVEGNSGEVATPTLPQPPTPVSSNIRVVCRVRPLTELEKGRNEHSIVHFFDSKSISIRANGPQFTFDRIFGYQETQSQIFEDVAEPIVNDFLDGYHGTIIAYGQTASGKTFTMVGDPDSHGIIPRVIESIFVGISKMREKDTSLSLAFCLKISALELYNEKLYDLYDASKSNLNIREHKQNGIYVEGISEIVITSIEEAYNFLNISNNNRAIASTKMSAASSRSHSVLMIELSQQNLSMESSKISKLFLVDLAGSERAHKTGAEGDRMQEAKNINLSLSALGKVINALTCGANYVPYRDSKLTRVLQDSLGGNSKTSLIINCSPSNNNEHETITTLQFGTRAKTIKNQPKINKKITYHELELFIIKLAKDLEKSRKECEEITRSKNLEINNLLIQLENNQKMVVESNQKLELLNSQISSNHSFDNTFKEIENTCENSKIIFDDLNDHINNNNNVDENNNTNNNDNNNNDNNNNNQYQEESNQYQQENNQKDGDQNNSSFDSIKVEDLRDLDDEPDIEDIILNSTLGNISDDDDDDDDHHSNNNNVDDNNNGEINNDSDGYLNRSLKDIKIPEISDLNDHNINNNNNNNNNINNDNNSNSGGLRVSTSYITSSPNLSPSKSMDVNNSPPLFSYFKTKDFPPSSDENDKFFNDLIAKGENEQQQQQQQHNDDDEDIKSTTSNATTTTITTIDMNASHPSGIDDPIEFTIIKSDKTITSTIERETIQPSSLSNSTSLLDIETVESSTLPAPPPVTTTTTLTTVTTTKLTKTTNIPSNTNDINSIDDFGFSKIEEEGSSSNRKPNDTAILSFGDDDDEENEDNENEDVIVDSDEDTHSGKNNLLNTFKNDHHRGDFGATPTKSIFNKNGNITIKEFETPQQQQQQQQQQQQQQQQQQQQQQPLILQTTSTNPTIISIKSNKEPSPSSSTTTSIKKKNFNKRRSWIIFTIILTITLVSSSLLCLYLPEYKERLVQRRGYLNKLGIYSDYPTNEKISLAQHNQISLAKELYGGNSKQYYDEMSSFNTAYNHLIEMNHLETAVSKIFGSAIDLRFSGDDVINSIECKRAIHKLKTNNYVNGDLDQQQQQHNYITKIDQLSEQSKEQNQLIENFKLDLKNKTSEIEKLEKEIKQKDNKIKEKEEKIELIESRVLNEEKGGEKVLEDQIISLRNDKNTLSTQILNLEGDKKSLGVLVIKLNSDKTEIQNEVKELKRKVQELEDAPIALIPNPFVKWVKSFYVEKKSWFVENIYKIWNWFK 1255 Q54VZ8 Exocyst complex component 8 exoc8 44689 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. UNIPROT Q54VZ8 Pfam PF16528 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0042995 GO:0000145 GO:0048471 GO:0006887 GO:0006893 GO:0008104 GO:0015031 MKKGVTYPLKIDTNLSTVSSSVNYNDIECVDIKSNGHYIVKFMYREWVGPLNLMTTQKTSIKISIDLKEQTVTCTHTDKKKTVYRWGEFPNKKETEQNKKEDNPVQYETFLSSNFNSEKYVNDLFTHKTDQQATVHLQYLENRKLGCIDHLKKDVYKNHLIFIGASKEIANSEVDMLDFRNLISDYGNVMSSLQNISISWDHYKVKKSGKIDFEPLSPATEPIQWLTTAPNELSVSIEQREFEVAVGLVEKINKIYESNPKVEIVMQTHPLKDQIENKVKILTDKLMNELRSPLLKANQIKDTISLLVRLSQNDKAKSIFLESRSHSINQAIKKIVFSGDLNRFIGELARVIFNSINSTCNDFTNSFPSYMNSGLVSWIIEELVLISDIFNRQVFILDNFYSISQAIRIIESHCEMMDQTGLSIGFYWNLLLQPHVEQLIVNYEIKIRDSMLHQLMDEKWNGVSNWDYEVKSQLNSLPSSLKNSGTPNSGGSGISNNNSNNNNNYQSPIINNNFNSGGGNKKIGLTFQQMHQDNLNNMEDIDQGRLKLTSSTIFLNTIIQKFAIDICQIITIDLIPVISQSLGSIFKDYMSYLKNEIQKEYLSDTQCLAIISDSVYIVDDLVSRIATRFEDATGEKLNNLTQLSSLLYSYFESIRDQYSTRKALELVDNSMNWEEQEYQVEEELDPFPKNFIVLSEALDRLAESIQTNVNVESVLPIASRIISEIVNIISNRFESTSNLVFGYGGLQHFILEMKYLATFAGKYPVEDSTFELINTMIRNHKEIYLNNTSDPKPLKTEEYFTSIIDNLVYQKAVYN 815 Q54WT9 Importin-13 homolog B ipo13B 44689 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q54WT9 Pfam PF03810 Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}. GO:0005737 GO:0005635 GO:0008536 GO:0006606 MNTNAMDQYENCPSYGSFDVKSFSDSPIPFTNNNNNNNNNNNNNSICVMPSNYNNKNNNNNNNEKLEPEATLDVLTHALHTLYKSNDSNQRKLAEKWLILFQKQPIAWEFCPRLLLETNIFELQYFGASTLESKLKNEWNECNVEMKSKILNTIVSIIQNSTKLPICCVTRVSVTLTIAVMYTFPEIWRNAIFDIIHLSIKQDINTLSLHDPSQNHFNTDRLLMVLEFLSILPDELKKQDLALCKYSEIQKELKLIIDKIYKFLLSVLFLPINENFEFIKISYKALSAWLKYMLPSNGTMLQSCFEISFTVGQQKVSNNSNGNGNGNNNNNNNRNSIGYPLIDSLALVLEGSSLSIEGQSNGSCYIEAFRYAIEQSLTIFPTFYNEATVMNQDDSKAKPIFNVFVQFISSNNSQLFTTDLIHRCLNLLISFIEIGSRETISLLFYLIDDFKTHTMLVQQDQNILKFFFLKLLNRFLDVSMYPNGKDYCPIENGTNPLSTSQNAQFNGVLCETNIETLLDDDIEQFRSCSSDCLMNIQENDIIPKSTFLKFLIEKLNAFINEKCPHWEQYESILYYIYAFSGGSQDGQLEYVPILLNIIPLIPIKSIPLVRTSIKLIGRYSSFLKTNTDYLAKVVSDLLPALSHAELIGSAASSLLSICVSDKCSTMLWPHFNQILDQIEPILLGPQKSNPSIVLVYKSLLHILHKAPIHELSPLFTRLISPVIPNITDHIPRVKSKDHYNQLLVQLSILYSVNEIIEYDEFATMGANGEFTSPSKHPLYPFFQTTIPIQGQLLKHYKSEFEIIDCITTFYRYMMLYFREIANDFVDEILQQATQSFNQYPIASLLQIISSIIIPKLQPLTITNIKNSISLISNTFINTLKSVILATNNNNKNNDNTNNNDDNNNKNDNNNNNNNNDNDKSNFILDFTITPDITKDYLILITKILKTSPQCIEPNIISTICIYIIYNLTDLTKDKPTTGNCCLFLTNCLSLNNGKLQISDPNGNKVLEQIKNEMNALFESDPKHSYVLVYNILMNICWTPTSIQVTQHFSDVLLSFAIGYPNLLKLHATNILNDPNFIKDKQINPHDKQSFLTNILKSNSTQVDYRSSVRTFSFICNDKE 1119 Q54Z22 Nuclear pore complex protein nup43 nup43 44689 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}. UNIPROT Q54Z22 PROSITE PS50294 Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}. GO:0031965 GO:0031080 GO:0051028 GO:0015031 MSSVSVHYSTHKINKVRFLNRNFHNDTSLFVTGTNHPVLSKNKISVWGLESRQNSDEIEELASVPIDGIVTELKVIEINNKPMIIGSTSKGSIFMYSIFNLPNKFEYIGYDGLLDKKYENYNNINNINDTYDTCNLLKERIWFNSSSNNNNVNSNNINNNNYNNNNNNYNNNNNNNNNNNNNNNNNNNNGSCINSFDISYDQHSLVTVGNDGVMNLLSIENLIPIYTNRYIDGLSVNVVKSITSNQIITSGELGRYIKFWDIRSNSSQPVKTIKTQCPRIFSLAIHKDEQHIIAAGSSDGQVNLFDIRNDYSIDQNKTHNSNVWELSFSKSNPNQLYSCSEDGFIYQYSYNKDNLGGGGMMTLPNQINNTFDIYSKEVSLLQLPTSIGSIDSFDINSNINRLICCSTSSQCLIVKSL 417 Q557F4 Probable importin subunit alpha-A DDB_G0273595 44689 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q557F4 UNIPROT Q869V5 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. GO:0005829 GO:0005643 GO:0005654 GO:0061608 GO:0008139 GO:0006607 MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMENKIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQTQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIGLIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLEYPDSIVFTPALRAVGNIVTGESSQTQIVIDNNGVELITRLLAVQKKSIRKESCWALSNITAGEPSQIDVVVSNPKTVTTLISLLSHSEHDIKREACWALSNSTNNSSTKSIQTLVRHNILKHFIDLLNSQDLVILKIVLEGLINIIKEGEKTKTKTGVNPYVNLISEMQGESIIYDLQEHQSKDVYKKAFELIEFFESSDYSDSENSEPNINQNGQYEFSSNYNSNSINI 550 Q558Z2 Sun domain-containing protein 1 sun1 44689 Yes SL-0178 SL-0182 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}. UNIPROT Q558Z2 Pfam PF07738 PROSITE PS51469 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}. GO:0016021 GO:0005635 GO:0005637 GO:0005640 GO:0005654 GO:0003682 GO:0003677 GO:0042802 GO:0043495 GO:0051301 GO:0034508 GO:0007098 GO:0051642 GO:0000070 GO:0006998 GO:0006997 MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINIRNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDENPKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQIDNNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYFPSFSTTKTNSPFNSTNNNIQFSNLITKEQLYPIIDEYFKKNEILKSYNKLFEKIENDIKYLSEREQYKDIINEIKEELKLVKLSNMDEDRVNQLISKMINHYNNNENNKQELKELLSKSIEELTKLKSDSKEQLIQISTESMNQLGQLKSESINQLGQVKSESIDKFQSTLKSLSKEEQSKIEREFNHQFNQLNKDADQLLSQHSLKIEKLREEINENQQSSLLKLTQEYKQLEERLKEFSSKLQQSISSSSMDQFESWKLVFIKDIEERINKESSKLTNQYIQLTQQFTKIQSFIKDNPSIDSLTNTIESLEGIKLLIEDILEVYSADKIAKVDYALGLAGASIEYNALHYRVSETYPPIKGSGSGSGSGGANGNSLGLYYYNLATNWIFPQPKPNPPETILDPMVNTGSCWGFYTGNGTIVIRLAKKIAITEVTMEHISSNISHHIDSAPKEFQVFGLINSSDIGQSLGVFTYDTTINRHLQTFKVNKIQSTTTTTTNQDQNDDDNIQEFSHVALRILSNHGYRYTCIYRFRVHGYQIPHPEQEQIQIIQEEQSFKQEEINQQQIEQIEQIEQIEKQQQSDEL 905 Q55AP1 Metabotropic glutamate receptor-like protein A grlA 44689 Yes SL-0198 Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17950724}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17950724}. UNIPROT Q55AP1 Pfam PF00003 Pfam PF02608 PROSITE PS50259 May play an important role in the terminal differentiation. {ECO:0000269|PubMed:17950724}. GO:0005938 GO:0005789 GO:0016021 GO:0005635 GO:0048471 GO:0005886 GO:0004930 GO:0030587 GO:0030435 MNKLKFLIILFITFLFNLKYINSLKQCKISVLLSGDWSDMGYNYQMNNARIKAESALNLEMSLCYKNLEVSIDLAKQAIEDSIKKGANFIVISSSVHTSIGYEYARLHRDKDIYWLIRGRGRPVPDDLPKVAVINFNTHLLHYTLGLVSGYLTTSGTVGFISPGPQILALANSNSFYLGALASRKNVTFLNAYTGSWYNPEVAYKASQMLISNGADFIGMSQDDMSVQKALMDSGKMALGITGFSNRLIWGSDIALSYITDWSDVFIKYAGHILNDTWPEYTDYYTTLAEGGSLLFDTFSYRVPSEVQKLVSLEIEKLKNSSYQPFRCNPMYSQINLNFDSNGCANDMEFKNTKLLLKGTDISKTINLGLYTIPIEFVDYSNSMKLGLTIVSGFCILFCIISMVLVIMFRHAKIIKSASPIFCLLILFGCIIIFSGCIIFSLSPTDGICGARVWLLSIGYTIFLGSLLVKNWRIWLLFDNPKLKKRSITNWKLYPFVAGILAADVLILALWQGLGDIRSESRIGIDSLTKYQYANVCSSNDQGSVALYILLVFHGIKLLAACFISFKIKAVDIEEFNESKPIASSIYIITFCLFIVIPLMVSPQSVASQVITIVVCAIVTTLISISLLFGSKFYMMATQGLALNQTFATNTKSSSFSLSLEKQKSKSNGLEFEDSDESEEKLPQIKNYSNSEIPNLQHNHSRLAHFSSDSCTSAEQDSKLDLENQNDENEIENNQNNQNNIVEDCQKVEKLEKDENLEKDENLEKDENLEKDNENQSIIQKKRLSKNFNQSEIDPDDV 798 Q55BX5 Nuclear pore complex protein nup54 nup54 44689 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}. UNIPROT Q55BX5 Pfam PF13634 Pfam PF13874 Probable component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}. GO:0044613 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0036228 MSLFGNTTTGGGGLFGNTTTPTQTTGGGLFGNTTTGGGLFGNTATPTTGGGGLFGNTATPTLTTGGGGGLFGNTTAPTTGGGGLFGNTPTQTTGGGLFGNTATGGGGLFGNTQQQQQQQQQQQQQQQQQQQQQPSTSLFSQSSLGSQSSLGSQSSLGSQSSLGSQSSLGSFGQTQQPQTSSLFGNLQQQQQLQQPQRSIIEQKLYDFMQSISPNSLNCRFLYWFYNYQANGQLVDPNSIPKPPNVTVDQWAYALSNNPDPSILIPVAAKSFDDLINRRMKQEETIIALDQNTQEALKRMRDLENHLNFHIHTQLEMMRKKQIELIQRYIEVWSNLEIYQSKGKTFTTSEERIMKKIYELFEEINQPNSIKSKVEEISNQLKLGSMEKEKIKYEISPEAVEPLYNLLKNMTISIERITNELEIAVKDAQILKNELYQLKKC 440 Q55CQ7 Transportin tnpo 44689 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q55CQ7 Pfam PF03810 PROSITE PS50166 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}. GO:0005737 GO:0005829 GO:0005635 GO:0005634 GO:0061608 GO:0008139 GO:0008536 GO:0006606 MSEWVPNQDGLKQLVYVLNLSNSTSREVHDQIREELDKFHSVPDYNNYLTLIFKSNELQPHIRSVAGLVLKTNIKQYFEKMPREVQNYIKREILPVLSDPDASVRHTVGNIITNLIKKSCFSEWPELLPALNLALDSNSQDLIEGSLYTLSLLCEDSTKKLDSDDSGRALNQLIPKLIMFFKCNNADFRKKALVSISYFIISMPGALLINMEAFLKGIFSMSEDPSEAVRTNVCKTLVTLVETKIEFLLPYIKDVIQYMLHATKDKSEEVALEACEFWTAISQAEGCRDLLRDYLPVLVPILLNGMVYTEQDYEYLDQGDDSMTPDRPQDIKPFIASTKSHGSGSSGGGQDTGFVNPDNNNNSNNNNSSNNNSSNNNNNNNNEDDEEYNDDDDDDDDDGFEDEAWTIRKSSAFAIDVLSGIFPDAEYLSVTLPLIEQRMNEQNPWPVRESAILALGAIADGSKNGLAPHLSKVIPYLINTLNDPKPLVRSITCWTLSRYSYWIAQADGRDYLHPLVVNLLNRIVDNNKKVQEAACSAFATLEEEADLLLIPYLQMILVTFVNAFGKYQAKNLLILYDAISTLAKVVGNELNKPELINILVPPLLQKFNALDDSNKNLLPLLGCLNQVCSSIGAGLQNLISLFFNRSIKLIEGSLQAHYKYNNQDQKGSSSSSDQDFIVAALDLLQGLSEGIGTSIESLIPNSNLPHLLLQCMNLRGSDVLQSSFALLGDMSKFCLIHFKQYIPDYLNILTNNLYPEYLSVCNNASWAIGEIAIRMPDEVKPFVVAIRDRLISNINKVNLNRGVLENTAVTIGRLGIVSPADISPFVDKFIQCWCMAIRRKTDDIEKDSAFRGMWLIINNNPNGALRHLVYICDAVASWDKMQPDLYEAYFKLLHMYKTSMGGVWAQFYNQFPEQLREILNEKFKLNQDISQ 931 Q55DA6 Probable 18S rRNA (guanine-N(7))-methyltransferase DDB_G0269722 44689 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. UNIPROT Q55DA6 Pfam PF08241 Pfam PF12589 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}. GO:0005730 GO:0005654 GO:0048471 GO:0016435 GO:0070476 MSRPEHIAPPEIFYDDVESKKYSSNSRIIEIQTKMAERAYELLAIPETAEGLMLLDIGCGSGISGDVITDAGHYWIGCDISQHMLDVAIDREVEGDVMLRDIGQGFPFRAGSFDAAISISAIQWLCNAEKSHHNPRKRLHTFFQSLFNVLTRGGKAILQFYPENSAQIEMITASALRCGFSGGLLIDFPNSSKAKKYFLVLFTGNNNIMPSAKGVEGEEYEQQEEEDSNEVKYSNRKRDRRRVTKSKGSAQHKTKEWIMNKKDRQRKQGREIKNDSKFSGRKRGPKF 287 Q55FW7 Nucleoporin GLE1 gle1 44689 Yes SL-0178 SL-0185 Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. UNIPROT Q55FW7 Pfam PF07817 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}. GO:0005737 GO:0031012 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0006446 GO:0006449 MNKTSSNNISNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNRILSPFKRNNSKENGNGSVTITLEPLVSPFKLIKSNFKDDVHTNNINNNNNKIKRFLDEDNEFEITIPIRRSGNSINFNIGIVPSSNKKQQQQQQQQQKQKQKKKKTLSPLKKAPGIYSLKDLTIDSDSDSDSYSDNDDNEEYNIKLKSPIKNKIVNNNNNQQQQQKQKEKEEKEEKEKVEKDKKEKDKKKLILNSFQSELIINRVEREREIKINRIVEEKNKEIDDKWVEIKEYNQNQMIKERKEFHSQQIRLNNLIKKQHKKDIKEFSIKLKQAKQKHQSELSESLSLLNQLNKLEQQEIDRHNEELLKYELAIKEEKRKQQQLIERYEQKKREEKQRQLQQEQKEKQEKLEKEEKEKEQQEQQKQLLIKLAKEKEEKEKFEKEQQQQKEKELQKEKELLQQKEKEKEKEKLQQQQQQQQQQQQQQQQQLQQQQQQQNQQNNNLGYIKKDGIIFSLNENSKNFNDFKERSKEFDMIIKFINEKKSMLSREMVEFERQNSKLINIAINQISASQEQVNEKTNKLIKSIQDSQQSDYLKKSTILSIVKKSLSQVESQITFHNASSFPLALVLVRVGEKYPELIDCLLASLNEKCCYTVPYYVSPKENESQSSISKRMGYAFSNDIVGDNDKPIETEDEFHKRICGYLSLYCALILKSEQPHKSSSSSSSSSSSTMMFGFGTQIGNNNNNKLINKNLNIESSLRWLKDLVSLRPRRITSYLFVTFFTHLGNLLSKNQKSSLEFKIIVGKIVEENFFNQMNKPGTEGSFSRLKNLIEEYYKTGTFQQHEGVDF 837 Q567X9 Inositol 1,4,5-trisphosphate receptor-interacting protein itprip 7955 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT Q567X9 Pfam PF03281 Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}. GO:0016021 GO:0005640 GO:0005886 MQGAIARVCMVVVAAILNHPLLFPNENTTVPEQDEDLLARMKEHQEKLEAEQKRLEQEISQNETSVIGDQDGYGWYFWSALCLVIFFTIEVCRQDLISAEIPDPAEDEDGDCSTGYHSAKSIALDRGTLNNFCKTRFFPYTNESGRVREFIEGFADDLLEALRSICDLKADLEVEDFAGIGSMFESWRVSKPPTCDLIVPFSPPQPLRFQFELWCDPSTEIPLDLQGCGRIQLIKPGGNGTDCLCGSIDLGDDMLCLLHNRNECEVLEDDALPELLCARDTTYLSKGQIMRWFQISVSKAWGKISHKYDFELAFRNLDFPGALKIKFPSGKTVVLNLTPAVQFENTDAYLISHFPSDTSNSSDTHWQLSLSVYEKNLLKHLAKSLPTNSCHIHCLQIVAFLHKKQTTLTGRSAFCNYHIKTALLHLLLSKRPAMWQPQNLDSRLRDLLSFLQQSLEEKKLYHALVGNPRIPVEILVPKIIRTAEPINLYRPLVLQRHVYAKMEEHFEEMVRNTSVLVQEYTPHFSNGHVRHEFSSAEQI 539 Q568Z6 IST1 homolog Ist1 10116 Yes SL-0178 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}. UNIPROT Q568Z6 Pfam PF03398 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}. GO:0005813 GO:0000785 GO:0031410 GO:0005829 GO:0005793 GO:0070062 GO:0090543 GO:0030496 GO:0005635 GO:0042802 GO:0090541 GO:0019904 GO:0044877 GO:0009838 GO:0051301 GO:0061640 GO:0045184 GO:0048672 GO:0045862 GO:0008104 GO:0015031 GO:0046745 GO:0019076 MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPVGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGAPDGTMPMPMPMPMPMPSPSPNAPFAYPLPKGPSDFSGLPVGTYQAFPNIHPPQIPATPPSYESVDDINADKNVSSAQIVGPKPEAPAKPPSRPVDNYNTFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT 366 Q59WU8 Nuclear fusion protein KAR5 KAR5 237561 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q59WU8 UNIPROT A0A1D8PPH8 UNIPROT A0A1D8PPH9 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0031301 GO:0031965 GO:0000742 GO:0048288 MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEKNEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSIFNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMKVVDID 485 Q5A5N6 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 237561 Yes SL-0178 SL-0182 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}. UNIPROT Q5A5N6 UNIPROT A0A1D8PIT0 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWIYTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILFLYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI 219 Q5AJD0 ATP-dependent RNA helicase DBP5 DBP5 237561 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5AJD0 UNIPROT A0A1D8PJB3 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0003723 GO:0003724 GO:0016973 MSSEKVKRVEADATDLLASLSIDKSGEKLEEIKKGSTPDPSDLLGGLSLKEGDSKKPEEKKEVVEEPENKEINDDKKDEDKKDESKDEVKDGDGAKEETKEEVKEESKEEPKEPKEPKEPATNLIKSSYEVKVKLADIQADPNSPLYSVKSFEELGLSPELLKGLYAMKFNKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFSLTMLSRVDPTIKMPQCLCLSPTRELARQTLEVITTMGKFTNITTQLVVPNAIPRGSSVNAQVLVGTPGIAIDLIRRRQLNLSKMKVFVLDEADNMLEAQGLGDQAIRVKKALPRGVQLVLFSATFPTEVREYAERLVPDANSLELKQEELNVDGIKQLYMDCRSEQHKFEVLCELYGLLTIGSSIIFVEKKETADVLYGKMKKEGHTVSVLHGGLDNTDRDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDMPTDKYGKPDPSTYLHRIGRTGRFGRVGVSISFIHDRRSYDILMAIKAYFGNVEMTRVPTDDWDEVEKIVKKVIKS 540 Q5EE04 Nucleoprotein TPR tpr 8355 No SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5EE04 UNIPROT P79992 Pfam PF07926 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}. GO:0005737 GO:0005868 GO:0019898 GO:0000776 GO:0072686 GO:0042405 GO:0031965 GO:0034399 GO:0005643 GO:0044615 GO:0003682 GO:0031072 GO:0051019 GO:0003729 GO:0042803 GO:0017056 GO:0051301 GO:0034605 GO:0007094 GO:0031990 GO:0046832 GO:0000122 GO:0045947 GO:0031453 GO:0090316 GO:0090267 GO:0046827 GO:0042307 GO:0006606 GO:0010965 GO:1901673 GO:0070849 GO:0006405 GO:0006404 QEQHSQLEAAKTQVEKDMGEKISNLERELENANDLLCSTKRKGVMLSEEELTAMSPTAAAVAKVVKPGMKLTELYNAYVETQDKLLMEKQENKRITKYLDEIVKEVEAKSPILKRQREEYERMQKTVASLSAKLEQAMREIQRMQDETDKANKCSSVLERENQRLELQIKDLSQQIRVLLMELEEARGNFVQRDDVSSANISSSSEVITQHLVTYRNIEELQQQNQRLLVALRELGEAKEREEQESTSSRVSELEKELENALSELQQLREARSHQMTLVESIVRQRDMYRILLSQTTGVVLPAQDETALTSTPRKSPGVSLDGSTSTPAAVVVSDSTEAAEARAALKQLQEVFENYRKEKAENDRMLNEQHDKLQEQVTELRSQNTKISTQLEFASKRYEMLQDNVEGYRREITALQEKTQKLSATTQKQEQIINTLTHDLRAANEKLAVAEVRAENLKREKELLKMSEVRLTQERESLVAEQRGQNLLLTNLQTIQVTLERSETEIKQRYNNQIEKLEQELAQTKKKLEHEIEQRHLLGKNQDVQVLELKKQYEMELNLHNNTKELLKNSHKEISVLKQQLNSFELQLASRSSQQAANRDKDVNIEDVEEIKTKLRQSEELVNDLKERLKTATSNVEQYRSVVLNLEESLNKEKQVTEEVRKTIEVRLKESSEYQSQLEKKMMESEKEKQELRDEKHKTVEQMEQQVTQLRQSLSSLQAEVQQALQRATTSASNEQKAKQDCQEQARIAAEAQNKYERELMLHAADVEALQAAKKQLTSASAIRHKCEETAQKAGSQLLESRASWEERERMLKEEVSQIQSRCKDLEKQNGLLHEQIESLSKKMVTSVQEGALNMSFGEEGKSQEQVMEILRFVRREKEIAEARFEVAQVECLRYRQRIEHMERELHELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVLIESNKILREENEKQEQELQQLQAKIRKLESNILPLQESNAELSEKSGMLQAEKKLLEEDVRRWRARTQHLLSQQKDTDAEEYKKLLSEREVNTKRIQQLTEETGKLKTEVARTNASLNTCQSQLQSVKDDLTKIKAEKEKLQKELDAKILDIQEKIKTITQVKKIGRRYKTQYEELKVTHDKMVAEASSAKADQLQEQASQKEVQELKDSLQRSEAKVTTMQTTVDNMQKTLDDKDNEIKEHQEQISRMQAELSHLHKDLQDKTAQEEQMRQQINEKEEKTKKTLLVVRQKLAQNNGAKEQLTRENEDLKQKNANLEQQKEELEVRMSALRSQYDGRISRLERELREQQERHHEQRDEPQETTRIPQQRQITLQPTTAAGERGSANTSEPPTANIKPTPSKVTTAAVPVNKSTPRASIRPMVTPAAVSTPTSTPTATVMPTTQVDQQEVQSEGQMEHVPVFGSASGSVRSTSPNVQSSLPQPILTLQQQTQTTAFVQPTQQSHATIESPTQETPVEIVQSSPVERPTTSSTFGTYSATPSSSIPKRPREEEEDSTIETPEQIADDTDQQRTKKRKEEDIEEKTETEAVINTEDALHILTQCSNMEFPLEEEIVESPIQTSQVIESQAPEQLQNVQSTQDSLQDTPPKKTHNLVIVISDEENEDEQEGYEEEEQEDEEEDEDDAGIGEGDDSNEETGSADGNEDYEGDDAEEADGTDPDTETEDSMTAGEGNQRAADSQNIGDSGVVTAESTFSQETREQPSSASDRQGPRPPQSPRRQAHPPRLTILAPPQELGPPPAQRIPVARRQSVGRGLQLTPGVGGMQHFFDEEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQASSSHSDLGQLASQGGLGMYDTPLFLAHEEESGGRSVPTTPLQVAAPVSVFAENPAADTSDHASQSVPMVTTSTGNVPTSVDSGAADEGDEVFVEAESEGIGAESTLEMDTQQEEPVQPSEADLPSTSQDPPSSSIADTSSSKPKPRRVWLQPQPGGRPFKRSRGGSDFRGRGGINRSNI 1997 Q5F334 Leucine-rich repeat-containing protein 59 LRRC59 9031 Yes SL-0178 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}. UNIPROT Q5F334 Pfam PF13855 Required for nuclear import of FGF1. {ECO:0000250}. GO:0005789 GO:0016021 GO:0005635 MARGGGKSGSLKDKLDGNELDLSLCGLSEVPVRELAALPKATVLDLSCNSLVSLPSDFCSLTHLVKLDLSKNRLQQLPVDFGRLVSLQHLDLLNNRLVTLPVSFAQLKLSLHHSPVEILSRLLGTPSSLLVFHSFHSWENQNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQAAVRVLQHMKVIQSEQDRERQRKLQAEREMEKKREAEQRAREAQERELRKREKAEEKERRRREYDAQRAAKQEMEKKTKKETVQTRKLASSSRPPQPARHKHSWSRSVLRALLLVLLCILCTLAVCKLTELQHQPLCVSVNTLYEDVVAAVQNHKTLQNMLQQNSQQ 339 Q5F410 Transmembrane protein 18 TMEM18 9031 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q5F410 Pfam PF14770 DE Reference Proteome: Yes; GO:0016021 GO:0031965 GO:0003677 MRSVAVAMEQPLHGPPGLSTILARTDWAEPWLLGLAGFHVLCFLLTCFSFQHYRVQIGHFLCMVCLVYCAEYINELAAMNWRLFSKYQYFDSRGMFISLVFSAPLLVNTIIIVVNWVYRTLNVMTELKTLQQRIKAEKDKKK 142 Q5FVB0 Ataxin-10 atxn10 8364 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5FVB0 Pfam PF09759 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}. GO:0048471 MAAPVERLAGVCAELEQWLGEESGQRNDWAEGEGIVWRLSELFREAQYRELAEPRIFRLILQILSRVSCEIKVATLPAGAFTDTHCQLPAECFRCLRNACVQCASNQDSVRNVGLIEESVRLIQIFGAPHVLQEPALVAFRCGLQFLGNTAAGNRDSQNAVWACAFPDLFLSCLVHDDEKVVTYSSMVLFTCINREKVSTLQDPSKLDVALSVVTAYSKYPDAEWMYLIVMDHFLLCPDLVKAVYLSQSSPERVTLLELILGKISQKEPLSAEESEALQAIAAFLSDCFQTQCKTILKLTSPSACDEEEPIVVTRLLDILCEVTSKNEHLSCLQTCPGLLEAAVDILRLTHLAGKQSMNVFTAAHTMSMGQDLTHAAVGFKAHLIRLIGNLCYQNKENQEKVYQLDGIALILDNCSIDDNNPFLNQWAVFAIRNLTENNDKNQELIASMERQGLADSSLLKSMGLQAEERDGKLLLKSVKKSPAL 485 Q5FVP8 Diacylglycerol O-acyltransferase 2 Dgat2 10116 Yes SL-0198 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}. UNIPROT Q5FVP8 UNIPROT Q8K4Y4 Pfam PF03982 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}. GO:0005623 GO:0005783 GO:0005789 GO:0030176 GO:0016021 GO:0043231 GO:0005811 GO:0016020 GO:0005739 GO:1990578 GO:0048471 GO:0003846 GO:0004144 GO:0042803 GO:0050252 GO:0071400 GO:0035356 GO:0042632 GO:0046339 GO:0060613 GO:0055089 GO:0006071 GO:0019915 GO:0035336 GO:0034383 GO:0046322 GO:0045722 GO:0010867 GO:0090181 GO:0050746 GO:0097006 GO:0019432 MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKHLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAALYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIVIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHTMYMEALVKLFDNHKTKFGLPETEVLEVN 388 Q5FW14 Charged multivesicular body protein 7 chmp7 8364 Yes SL-0178 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}. UNIPROT Q5FW14 Pfam PF03357 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}. GO:0000815 GO:0005635 GO:0010458 GO:0045324 GO:0031468 GO:0015031 MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIVIQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRALPLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERLQSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLALKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWETDQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ 468 Q5FW52 Muscular LMNA-interacting protein Mlip 10090 Yes SL-0178 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}. UNIPROT Q5FW52 UNIPROT Q9D6X9 Pfam PF15274 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}. GO:0005635 GO:0031981 GO:0005634 GO:0016605 GO:0042383 GO:0005521 GO:0003714 GO:0010614 GO:1903243 GO:0000122 MEFGKHEPGSSLKRNKNLEEGVTFEYSDHMTFSSESKQERVQRILDYPSEVSGRNSQQKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGGPGNIATRPKSLAISSSLASDVVRPKVRGADLKTSSHPEIPHGIAPQQKHGLALDEPARTESNSKASVLDLPVEHSSDSPSRPPQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTASESQLTKPGVIRPVPVKSKLLLRKDEEVYEPNPFSKYLEDNSGLFSEQ 269 Q5HZ92 Ceramide-1-phosphate transfer protein cptp 8355 No SL-0178 SL-0182 SL-0183 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}. UNIPROT Q5HZ92 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0120009 GO:0010507 GO:0050713 GO:1900226 MSSTEEKFSLKEVLVSFKACLIDDDKDVILEHYVNGWKGLVRFMSSLGTIFSFVSKDAVSKIQIMESYLAGPNGERYRTLQSMVEYELSSDLVDLTKRSDHTDSGCRTLLRLHRALRWLQLFLEKLRVSNEDSKTSTLCTEAYNDSLANFHPWIVRKAATVSFIALPYRNTFFEIMNVGTTEEVVAMLGESMPYVTKVYDFTQEVYSQHNLLELP 215 Q5I034 Protein CUSTOS Custos 10116 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. UNIPROT Q5I034 Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. GO:0005635 GO:0007275 GO:0030178 GO:0060061 GO:0016055 MVAPSGAMSDSESSSSDSSDAEELARCREAATPAWGLEQRPREAERPAAGTADTQAPAPQPSRRREVNQHDEDGNELQTTPEFRAYVAKKLGALLDSSIAIAEVWKKTQQARLQQEAKEQQEAKEQQAAKEEQAAKKEEDGFRLFFTSVPGGHEKEASPRPCRKRQPPSSSEDSDEELQRCREAAVSASDILQESAIHCPAKVEKEAEKKKLKKKAKKKADADLAAATGLEQVKEAGSVNGDPVLSGTKKKKKKKAKKAREASLCPPAECAAAEPKN 277 Q5I0I8 Nucleolar complex protein 4 homolog Noc4l 10116 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}. UNIPROT Q5I0I8 Pfam PF03914 DE Reference Proteome: Yes; GO:0016021 GO:0030692 GO:0031965 GO:0005730 GO:0005654 GO:0032040 GO:0042254 MERQPASTGSRQELGRLLEAVLSNRGRANAVFDILAVLQSEDPEEIKEGVRTCSRLFGTLLEREELFVGSLPCEDMALAGSQGATYKYKVWMRHRYHSCCNRLEELLTHPSFQVKELALETLMKFVQLEGAKPLEKPQWESHYLFPRTLFRAVVGGLLTPEDDHSLLISQFCEYLEYDDIRYHAMQVATSILARATSRQPEVSLTFWNNAFTLLSAVNLPLQEHELTNFYVKHAQTSSKWKVVHLKEQRKAFQEMWLGFLKHKLPLSLYKKVLVAMHDSILPHLAQPTLMIDFLTSACDVGGAISLLALNGLFILIHKHNLEYPDFYQRLYGLLDPSIFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPLICNLLRRHPACRVMVHRPQGPELDADPYDPTEKDPARSRALESCLWELQTLQQHYHPEVSRAASVINQALSVPEVSIAPLLELTAYEIFEQDLKKMMPESVPLEFIPAKGLLGRQDDLCTQFFCLS 516 Q5JTH9 RRP12-like protein RRP12 9606 Yes SL-0178 SL-0182 Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. UNIPROT Q5JTH9 UNIPROT B4DK00 UNIPROT E9PCK7 UNIPROT Q5JTH8 UNIPROT Q69YK4 UNIPROT Q96E87 UNIPROT Q9BUH3 UNIPROT Q9Y4C7 Pfam PF08161 OMIM 617723 DisGeNET 23223 DE Reference Proteome: Yes; A0A142I5B9 EBI-20625235,EBI-310743 Q7KZN9 EBI-3248549,EBI-310743 P62491 EBI-745098,EBI-310743 P51151 EBI-4401353,EBI-310743 Q9NWT8 EBI-448665,EBI-310743 P03372 EBI-78473,EBI-310743 F5H1C8 EBI-21259559,EBI-310743 Q96DB2 EBI-301713,EBI-310743 Q92731 EBI-78505,EBI-310743 P01100 EBI-310743,EBI-852851 Q9JMK2 EBI-771709,EBI-310743 P62960 EBI-529779,EBI-310743 Q99661 EBI-1642317,EBI-310743 Q6ZWV7 EBI-2554199,EBI-310743 P41218 EBI-2829677,EBI-310743 P27635 EBI-352398,EBI-310743 Q00839 EBI-351126,EBI-310743 F8VQC7 EBI-11104531,EBI-310743 Q16666-2 EBI-6273540,EBI-310743 F8VQC1 EBI-11054761,EBI-310743 O00567 EBI-396034,EBI-310743 Q9QZD9 EBI-7466616,EBI-310743 P06748 EBI-78579,EBI-310743 P22087 EBI-358318,EBI-310743 P68431 EBI-79722,EBI-310743 P62753 EBI-356625,EBI-310743 P27824 EBI-355947,EBI-310743 Q15075 EBI-298113,EBI-310743 Q08379 EBI-618309,EBI-310743 O43493 EBI-1752146,EBI-310743 Q96GD4 EBI-624291,EBI-310743 O15155 EBI-749204,EBI-310743 Q14684 EBI-372051,EBI-310743 P55075-2 EBI-21635150,EBI-310743 O43159 EBI-2008793,EBI-310743 Q86VZ2 EBI-996170,EBI-310743 P01127 EBI-1554925,EBI-310743 Q7L5N1 EBI-486838,EBI-310743 Q86VP6 EBI-456077,EBI-310743 Q13616 EBI-359390,EBI-310743 Q92905 EBI-594661,EBI-310743 Q13618 EBI-456129,EBI-310743 Q9NY93 EBI-372376,EBI-310743 P56180-2 EBI-11960323,EBI-310743 Q96KR7 EBI-717068,EBI-310743 P62263 EBI-352783,EBI-310743 Q02539 EBI-932603,EBI-310743 Q9BYG3 EBI-2561019,EBI-310743 P18124 EBI-350806,EBI-310743 Q8IVT5 EBI-486984,EBI-310743 P22492 EBI-1056618,EBI-310743 P11487 EBI-11478259,EBI-310743 Q6AW86 EBI-4395769,EBI-310743 Q96HE9 EBI-3957108,EBI-310743 Q9NY72 EBI-17247926,EBI-310743 P19438-2 EBI-21717938,EBI-310743 Q13895 EBI-358049,EBI-310743 Q2NL82 EBI-358058,EBI-310743 Q15020 EBI-308619,EBI-310743 Q5T3I0-3 EBI-21605187,EBI-310743 Q8N0W7 EBI-21682158,EBI-310743 P10412 EBI-358163,EBI-310743 O14836-2 EBI-12023110,EBI-310743 Q8WYQ3 EBI-16721660,EBI-310743 P15880 EBI-443446,EBI-310743 Q99558 EBI-310743,EBI-358011 Q96CW1 EBI-297683,EBI-310743 GO:0005829 GO:0016021 GO:0043231 GO:0031965 GO:0005730 GO:0005886 GO:0003723 MGRSGKLPSGVSAKLKRWKKGHSSDSNPAICRHRQAARSRFFSRPSGRSDLTVDAVKLHNELQSGSLRLGKSEAPETPMEEEAELVLTEKSSGTFLSGLSDCTNVTFSKVQRFWESNSAAHKEICAVLAAVTEVIRSQGGKETETEYFAALMTTMEAVESPESLAAVAYLLNLVLKRVPSPVLIKKFSDTSKAFMDIMSAQASSGSTSVLRWVLSCLATLLRKQDLEAWGYPVTLQVYHGLLSFTVHPKPKIRKAAQHGVCSVLKGSEFMFEKAPAHHPAAISTAKFCIQEIEKSGGSKEATTTLHMLTLLKDLLPCFPEGLVKSCSETLLRVMTLSHVLVTACAMQAFHSLFHARPGLSTLSAELNAQIITALYDYVPSENDLQPLLAWLKVMEKAHINLVRLQWDLGLGHLPRFFGTAVTCLLSPHSQVLTAATQSLKEILKECVAPHMADIGSVTSSASGPAQSVAKMFRAVEEGLTYKFHAAWSSVLQLLCVFFEACGRQAHPVMRKCLQSLCDLRLSPHFPHTAALDQAVGAAVTSMGPEVVLQAVPLEIDGSEETLDFPRSWLLPVIRDHVQETRLGFFTTYFLPLANTLKSKAMDLAQAGSTVESKIYDTLQWQMWTLLPGFCTRPTDVAISFKGLARTLGMAISERPDLRVTVCQALRTLITKGCQAEADRAEVSRFAKNFLPILFNLYGQPVAAGDTPAPRRAVLETIRTYLTITDTQLVNSLLEKASEKVLDPASSDFTRLSVLDLVVALAPCADEAAISKLYSTIRPYLESKAHGVQKKAYRVLEEVCASPQGPGALFVQSHLEDLKKTLLDSLRSTSSPAKRPRLKCLLHIVRKLSAEHKEFITALIPEVILCTKEVSVGARKNAFALLVEMGHAFLRFGSNQEEALQCYLVLIYPGLVGAVTMVSCSILALTHLLFEFKGLMGTSTVEQLLENVCLLLASRTRDVVKSALGFIKVAVTVMDVAHLAKHVQLVMEAIGKLSDDMRRHFRMKLRNLFTKFIRKFGFELVKRLLPEEYHRVLVNIRKAEARAKRHRALSQAAVEEEEEEEEEEEPAQGKGDSIEEILADSEDEEDNEEEERSRGKEQRKLARQRSRAWLKEGGGDEPLNFLDPKVAQRVLATQPGPGRGRKKDHGFKVSADGRLIIREEADGNKMEEEEGAKGEDEEMADPMEDVIIRNKKHQKLKHQKEAEEEELEIPPQYQAGGSGIHRPVAKKAMPGAEYKAKKAKGDVKKKGRPDPYAYIPLNRSKLNRRKKMKLQGQFKGLVKAARRGSQVGHKNRRKDRRP 1297 Q5JVF3 PCI domain-containing protein 2 PCID2 9606 Yes SL-0178 SL-0185 Cytoplasm {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. UNIPROT Q5JVF3 UNIPROT A6NK09 UNIPROT Q3ZCX1 UNIPROT Q5TC57 UNIPROT Q5TC58 UNIPROT Q9H7K1 UNIPROT Q9HBZ7 UNIPROT Q9NUK6 UNIPROT Q9NVY1 UNIPROT Q9NW44 UNIPROT Q9NWH3 PDB 3T5X Pfam PF01399 PROSITE PS50250 OMIM 613713 DisGeNET 55795 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}. P49336 EBI-394377,EBI-1051701 Q9NWT8 EBI-448665,EBI-1051701 P03372 EBI-78473,EBI-1051701 Q9UKT9 EBI-1051701,EBI-747204 Q8XA11 EBI-10038919,EBI-1051701 P62753 EBI-356625,EBI-1051701 Q14684 EBI-372051,EBI-1051701 P60896 EBI-1051701,EBI-79819 Q99AU3 EBI-6150155,EBI-1051701 C3W5S7 EBI-6152135,EBI-1051701 P03496 EBI-2547442,EBI-1051701 Q9WPI5 EBI-6149678,EBI-1051701 Q13618 EBI-456129,EBI-1051701 Q9HC98 EBI-1051701,EBI-740364 Q13418 EBI-1051701,EBI-747644 Q9HAW0 EBI-1051701,EBI-1055224 Q53F19 EBI-6657994,EBI-1051701 Q96PV6 EBI-1051701,EBI-739546 C5E524 EBI-12561527,EBI-1051701 Q194T2 EBI-11515076,EBI-1051701 GO:0005737 GO:0044615 GO:0005634 GO:0070390 GO:0003690 GO:0003723 GO:0043066 GO:2000117 GO:0071033 GO:0016973 GO:0045579 GO:0090267 GO:0045893 GO:0000973 GO:0043488 GO:0048536 GO:0006368 MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEAFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC 399 Q5M7B7 Optineurin optn 8355 No SL-0198 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}. UNIPROT Q5M7B7 Pfam PF16516 Pfam PF11577 PROSITE PS51801 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}. GO:0005776 GO:0005794 GO:0048471 GO:0055037 GO:0070530 GO:0046872 GO:0006914 GO:0016192 MENELLNHPHNNNMVNGHQDAPYDALSMKNDAEMLEQIKQLLMENNNLKETMKQMNQEMKERLEELLKRHNQHLLDLNSANEVLRKELQSLKEKIATSNQGSAVCSTSEEASENKQLKNQLTRLQAEKADLLGLISELQLKLGSFSEDSFVEIGFSERESGEIVNEEKANKILSDHNISYRTNSIKEEGGGTEPEEVAISRLLRSLREETQKVERLEKELFSANKRLAELEKQTSEFCDKGVQTEQESEQSQSEVIISSEVDILKEKVKSLNKELQETNDKLNEAKQFKNSLQEKCILLDKRLQENQVDLEEKQSLRYSIKKLELQVESQESEIKLEQNKTEAEKNQLGILQVSYDKLNSEYQELRIREIEKVSKVEFNELLEKLDVCEKALAKKQFEIDEMREMDTKHEEDKETIELLRAQVDVYCADFHAERSARENIHQEKEQLATRLAYMIQEYEKLKEEMMGKQSIEQLQRRHGATSLLDASEGPYLVARGAANMEQPSITVYTCPKCNLTVPDMDTLQIHVMDCIT 532 Q5M844 Nesprin-4 Syne4 10116 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Localization at the nucleus outer membrane location requires the presence of SUN1. {ECO:0000250}. UNIPROT Q5M844 Pfam PF10541 PROSITE PS51049 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. Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity). {ECO:0000250}. GO:0031309 GO:0034993 GO:0045198 MAQFPLLGHGFPPEPVNHPLGGPRGLDVAGPTICPAPEEEPSRPEQVQASLDAPEHFMDEPKSTESATSPSKLPLASSHEHQDGGKPCEALQAELQGAAERVDALLVFGEGLAERSEPRAWTSLEQVLRALGTHRDTIFQRLWQLQAQLISYSLVLEKANLLDQDLEVEGDSDGPAAGGVWGPWAPSIFPTPAELEWDPAGDVGGLGPSGQKISRIPGAPCELCGYRGSQSSGQGFEDLLSLGLGHRKHLAAHHRRRLQKPQDKKRQGPPSLPDAMLEVDRGVPAPASRRPLTFLLLLLFLLLVGATLLLPLSGVPCCSHTRLARTPYLVLSYVNGLPPI 340 Q5N941 Probable ion channel POLLUX P0039A07 39947 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q5N941 UNIPROT Q0JHD3 UNIPROT Q5N940 Pfam PF06241 Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}. GO:0016021 GO:0031965 GO:0006811 MAESDGGEASPSGGGGGEGSPDPRRPPARPQLTKSRTISGSAASAFDRWGTSNSSSSILVRRSSTAPLPPGAAPRGLLTVAVDEPSYAAPNGGAAMLDRDWCYPSFLGPHASRPRPPRSQQQTPTTTAAAAADSRSPTPAAPPQTASVSQREEEKSLASVVKRPMLLDERRSLSPPPPQQRAPRFDLSPYLVLMLVVTVISFSLAIWQWMKATVLQEKIRSCCSVSTVDCKTTTEAFKINGQHGSDFINSADWNLASCSRMLVFAIPVFLVKYIDQLRRRNTDSIRLRSTEEEVPLKKRIAYKVDVFFSGHPYAKLLALLLATIILIASGGIALYVVSGSGFLEALWLSWTFVADSGNHADQVGLGPRIVSVSISSGGMLVFATMLGLVSDAISEKVDSWRKGKSEVIEVNHILILGWSDKLGSLLKQLAIANKSIGGGVVVVLAERDKEEMEMDIGKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGMRFGDVLISFPDAVPCGVKIASKAGKILMNPDNDYVLQEGDEVLVIAEDDDTYVPASLPQVRKGFLPNIPTPPKYPEKILFCGWRRDIHDMIMVLEAFLAPGSELWMFNEVPEKERERKLTDGGMDIYGLTNIKLVHKEGNAVIRRHLESLPLETFDSILILADESVEDSIVHSDSRSLATLLLIRDIQSKRLPSKELKSPLRYNGFCHSSWIREMQHASDKSIIISEILDSRTRNLVSVSKISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIRSAEFYLYEQEELSFFDIMVRARERDEVVIGYRLANDDQAIINPEQKSEIRKWSLDDVFVVISKAGNATYFVKTTVMRSNPVVYSSTF 965 Q5NCP0 E3 ubiquitin-protein ligase RNF43 Rnf43 10090 Yes SL-0178 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}. UNIPROT Q5NCP0 UNIPROT B2KGH3 UNIPROT Q6DI76 UNIPROT Q8BME0 UNIPROT Q8C191 UNIPROT Q8K0X4 Pfam PF13639 Pfam PF18212 PROSITE PS50089 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}. GO:0005789 GO:0005887 GO:0005635 GO:0005109 GO:0046872 GO:0061630 GO:0004842 GO:0007275 GO:0030178 GO:0016567 GO:0072089 GO:0006511 GO:0038018 GO:0016055 MSGGHQLQLAVLWPWLLMATLHAGFGHTGRVLAAAVESERSAEQKAVIRVIPLKMDPTGKLNLTLEGVFAGVAEVTPAEGKLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGANAVLFDITEDRSAAEQLQQPLGLTKPVVLIWGSDAAKLMEFVYKNRKAYVWIELKEPPAGANYDVWILLTVVGTVFVIILASVLRIRCRPHHSRPDPLQQRTARAISQLATRRYQAGCRRARAEWPDSGSSCSSTPVCAICLEEFSEGQELRVISCLHEFHRTCVDPWLYQHRTCPLCMFNIVEGDSFSQAPAASPSYQEPGRRLHLIRQHPGHAHYHLPSAYLLGPSRTSVARTPRPRPFLPSQEPSMGSRHQRLPRTSHLRAPEEQQHLAVSPHPYAQGWGLNRLRCTSQHPAACPVALRRARPHESSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVVNCTDVSLQGIHGSSSTFRSSLSSDFDPLVYCSPEGDLQGKGIQPSVTSRPRSLDSVVPRGETQVSSHIHYHRHRHHHYKRQFQWHGRKPGPETGIPQSMPAASHTQLEPSLPDQQLITPNPTASSMLPNPQRPRALTEPAPGLAEASSPSPSPKPNPSGLLNLQKSSLTVRHPHRKRRGGPSEPLPTSLPPDLTVHTACPVFPHYSPRLAYPWPPEVHPLMFRPPGPDRRLLHEVPGPCYSSSQPVWLYLNPCQPLGPCLPGEGHSKWTFDSPEGRRCPYSHCQVLPAQPGSEEELEELCEQAV 784 Q5NE24 Protein NODULATION SIGNALING PATHWAY 2 NSP2 3880 Yes SL-0178 SL-0182 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. UNIPROT Q5NE24 UNIPROT G7J334 Pfam PF03514 PROSITE PS50985 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}. GO:0005783 GO:0031965 GO:0009877 MDLMDMDAINDLHFSGHSSLTNTPTSDEDYGCTWNHWSPIVNWDTFTGAPDDFHHLMDTIIEDRTTVLEQLSPSITTTTTTTTTTDEEEEEMETTTTTTTTAIKTHEVGDDSKGLKLVHLLMAGAEALTGSTKNRDLARVILIRLKELVSQHANGSNMERLAAHFTEALHGLLEGAGGAHNNHHHHNNNKHYLTTNGPHDNQNDTLAAFQLLQDMSPYVKFGHFTANQAIIEAVAHERRVHVIDYDIMEGVQWASLIQSLASNNNGPHLRITALSRTGTGRRSIATVQETGRRLTSFAASLGQPFSFHHCRLDSDETFRPSALKLVRGEALVFNCMLNLPHLSYRAPESVASFLNGAKTLNPKLVTLVEEEVGSVIGGFVERFMDSLHHYSAVFDSLEAGFPMQNRARTLVERVFFGPRIAGSLGRIYRTGGEEERRSWGEWLGEVGFRGVPVSFANHCQAKLLLGLFNDGYRVEEVGVGSNKLVLDWKSRRLLSASLWTCSSSDSDL 508 Q5R601 Vesicle-associated membrane protein-associated protein A VAPA 9601 Yes SL-0178 SL-0182 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}. UNIPROT Q5R601 Pfam PF00635 PROSITE PS50202 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}. GO:0005923 GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0005886 GO:0033149 GO:0008219 GO:0031175 GO:0070972 MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFIGFFLGKFIL 249 Q5R7K7 Sentrin-specific protease 2 SENP2 9601 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5R7K7 UNIPROT Q5RDS3 Pfam PF02902 PROSITE PS50600 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}. GO:0005737 GO:0031965 GO:0005643 GO:0070140 GO:0045444 GO:0051028 GO:0016926 GO:0015031 GO:0016055 MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVTSACNGTRNVAPSGEVFSNPSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGYNRRPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHRTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYHSSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTEKMVGIRFENESRRGYQLEPDLSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNIDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL 589 Q5R812 Charged multivesicular body protein 7 CHMP7 9601 Yes SL-0178 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}. UNIPROT Q5R812 Pfam PF03357 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}. GO:0000815 GO:0005635 GO:0010458 GO:0045324 GO:0031468 GO:0015031 MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEAFQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKAEEVYRLYQSSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVGVYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPDNPRDRHFTNSVPNPRISDAGLEAELEKLSLSEGGLVPSGKSPKRQLEPTLKPL 453 Q5R8I2 RNA transcription, translation and transport factor protein RTRAF 9601 Yes SL-0198 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}. UNIPROT Q5R8I2 Pfam PF10036 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}. GO:0005813 GO:0005737 GO:0005829 GO:0072686 GO:0005654 GO:0005634 GO:0048471 GO:0072669 GO:0042802 GO:0003723 GO:0000993 GO:0006469 GO:0045944 GO:0006388 MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILVQERLTQDAVAKANQTKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR 244 Q5R923 Optineurin OPTN 9601 Yes SL-0198 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}. UNIPROT Q5R923 Pfam PF16516 Pfam PF11577 PROSITE PS51801 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}. GO:0005776 GO:0005794 GO:0048471 GO:0055037 GO:0005802 GO:0070530 GO:0046872 GO:0006914 GO:0034620 GO:0090161 GO:0016192 MSHQPLSCLTEKEDSPTESTGNGPPYLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTSRALSKYRSRSAEGAKNYLEHEELTVSQLLLCLREGNQKVERLEIALKEAKERVSDFEKKASNRSEIETQTEGSTEKENDEEKGLETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKSKLTVLQMTHNKLLREHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMTVLRAQMEVYCSDFHAERAAREKIHEQKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSGADQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII 527 Q5R9S8 Transmembrane protein 43 TMEM43 9601 Yes SL-0178 SL-0179 SL-0182 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}. UNIPROT Q5R9S8 Pfam PF07787 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}. GO:0005783 GO:0005794 GO:0016021 GO:0005637 GO:0071763 MAANYSSTSTRREHVKVKTGSQPGFLERLSETWGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSVAPENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDEQVKKETRYSYNTEWRSEIINSKNFDREIGHKNPSAMAVESFTATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLRVSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMFMGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPIIVARTRVPAKKLE 400 Q5RA57 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma AGPAT3 9601 Yes SL-0178 Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NRZ7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRZ7}. UNIPROT Q5RA57 Pfam PF16076 Pfam PF01553 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}. GO:0005789 GO:0016021 GO:0005635 GO:0003841 GO:0016024 MGLLAFLKTQFVLHPLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE 376 Q5RBN6 Protein NDRG2 NDRG2 9601 Yes SL-0198 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}. UNIPROT Q5RBN6 UNIPROT Q5R695 UNIPROT Q5R6V9 Pfam PF03096 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}. GO:0030426 GO:0048471 GO:0030154 GO:0007399 GO:0016055 MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC 371 Q5RBP6 Chitinase-3-like protein 1 CHI3L1 9601 Yes SL-0198 Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q5RBP6 Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006954 GO:0072606 GO:0030324 GO:0045766 GO:0070374 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 MGVKAAQTGIWASQGQSIRVVGFQAQTAHRAICLLGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDAIDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSNIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGQRDKQHFTTLIKEMRAEFIKEAQPGKKQLLLSAAVSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLEAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKERQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT 410 Q5RBY5 Nucleoporin NDC1 NDC1 9601 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5RBY5 Pfam PF09531 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}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MATAVSGPCAGRSRDILWRVLGWRIVASIIWSVLLLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYLLLLSVVIIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGANSFGSPAAQTCLNEYHLFFLLAGALMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKAWISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGAFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLNSNPPPIIKYLALQDLMLFSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLVLYQEAAATNGRVSSSYPVEPKKLNSPEETTFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPEVVSPFGTPFGSSVMNRMAGIFDVNTCFGSPQSPQLIRRGPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMHIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKTAIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE 674 Q5RCJ3 Cullin-7 CUL7 9601 Yes SL-0198 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}. UNIPROT Q5RCJ3 Pfam PF03256 Pfam PF11515 Pfam PF00888 PROSITE PS50069 PROSITE PS51284 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}. GO:1990393 GO:0005813 GO:0031467 GO:0005737 GO:0005794 GO:0048471 GO:0031625 GO:0001837 GO:0007030 GO:0000226 GO:0000281 GO:0001890 GO:0050775 GO:0016567 GO:0007088 GO:0006511 MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESTGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGEGQCGEEGKAGEELGRLRDSQDTVAGASDLIRTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEEWSGERGQLELEFSMAMGTLISELVQAIRWDQASDRPRSSARSPGSIFQPQLADVSPGLPATQAQPSFRRSRHFRPRSEFASGNTYALYVRDTLQPGMRVRMLDEYEEISAGDEGEFRQSNNGVPPVQVLWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDSEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNPAYPSLLEAQEDVLLEAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRELITNILGGCIQMVLGQIEDHRRTHRPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDRNPKTYWESNGSAGSRYITLHMRQGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLETLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDNEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCRRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGHGASGKEHKSEKEEEAGAAAAVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHCWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLALSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEEGRNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTVQIRSRGVPYASCTATQSFSTFR 1729 Q5RDB1 MOB-like protein phocein MOB4 9601 Yes SL-0198 Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. UNIPROT Q5RDB1 UNIPROT Q5R8K8 Pfam PF03637 May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}. GO:0005737 GO:0005794 GO:0032580 GO:0048471 GO:0019900 GO:0046872 MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA 225 Q5RE06 Ataxin-10 ATXN10 9601 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5RE06 Pfam PF09759 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}. GO:0048471 MAAPRLPPARALSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQLITECFRCLRNACIECSVNQNSIRNLDAIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLNNQERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTELLGYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP 476 Q5RED8 Ubiquitin carboxyl-terminal hydrolase CYLD CYLD 9601 Yes SL-0198 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}. UNIPROT Q5RED8 Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 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}. GO:0005813 GO:0036064 GO:0097542 GO:0005829 GO:0005874 GO:0048471 GO:0005886 GO:0005819 GO:0061578 GO:0004843 GO:0008270 GO:0045087 GO:0090090 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:0016579 GO:0070536 GO:1990108 GO:1902017 GO:0050727 GO:0010803 GO:0006511 GO:0016055 MSSGLWSQDKVTSPYWEERVFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNRIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKVGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSPPLQPPPVNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 956 Q5RHB5 Lymphoid-restricted membrane protein lrmp 7955 Yes SL-0178 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. UNIPROT Q5RHB5 UNIPROT J9WMP5 Pfam PF14658 Pfam PF14662 Pfam PF05781 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}.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}. GO:0005813 GO:0000785 GO:0005789 GO:0016021 GO:0072686 GO:0097431 GO:0031965 GO:0007052 GO:0051028 GO:0051984 GO:0007344 GO:0035046 MDVGVTPRRHNPVDSICRKLQTIQRRDQEINSPFQIPKFQTNSYDSPHSGLRFNLEAILKKHTVRPDDSDSASSAGMLTPTASPGPGSSCNTPRAPITPVNATYSITSTLGTLGTIGDRRTSGTYSRPFRRNCSTPSAQTGDNYFNFTPRYSTQSQGPDTDVRTSKIPTPGLFSYNLNFSSDISNMDSELAYPALVVKRLSLGEGSLFTSEPKKESMAEVSLICEEDLLDTIFQACDTQCRGKVYVSHIVDFLRHTTCRSSEDSGLEELCNMLDPERKDISIDLDTYHAIMKEWIEDCRNQGKDLKNDTQQESSKLRDSLSAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSGSLQTELALAQNPLEGLEHLSTSVCFASSLDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTENSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWDEEYVLSESPPLQELGPDQQMLEELCCDEEVLQALKQEEEEPTETVSDKEKITAKSEGEGEATYDSGVENEEPQRDFTLSHMCLPDKKSERESNEAPFVGEGGEQRPCMSLKEEDRLPECTGPEDAHEQAAPLPHTHCECAGDQPLTYDNLEVTSVKDHILSTEPSSLMTCELVSPSTGHPEVGNSITGRTEQLVGTNGEPEEERLTTGADMSDLQRLGEGQLSKVSAKSDKSLLLPVAEEEEAMPEAVEVTSAGVNSPDKHKTGSKKTVVTSDSNSTGSADSLKDPSEKVKDMTFDPAASEDNIPTVPATQSPKKDPLASRNKLKKEMSSMEVIEEQKAQEDGEPTVVTEKEGDTSVSSENASDSTKDDKNSLSPSDKEIEAEFHRLSLGFKCDMFTLEKRLRLEERSRDLAEENVRKEVISCKALLQALIPRCEEDNQSMEIIHRVQKNLEILVQSMTRVSSRSEMLGAIHQETRVGKTVEVMIQHVENLRRMYTKEHAELLELRENLTPNERSFGSHSERDDFRNKKQTTSNIFKTTSRRISIATIPRSIGGQTHFDMPKDMAETEVERLSRRSPWNMAAKRPPLKRFVSSGTWADIDEPTLMNSPTPSPTDNAPPSLMEGRPAVSRGARGIWIWVALFVVLAVLLALLASLMLQPAVDAAPVGTGDSWMTIQQLLWPYTGLRHNGQPPV 1447 Q5RI56 Optineurin optn 7955 Yes SL-0198 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}. UNIPROT Q5RI56 UNIPROT Q6P3H5 UNIPROT Q7SXF4 Pfam PF16516 Pfam PF11577 PROSITE PS51801 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}. GO:0005776 GO:0005737 GO:0005794 GO:0005634 GO:0048471 GO:0055037 GO:0070530 GO:0046872 GO:0006914 GO:0007409 GO:0043122 GO:0051648 GO:0016192 MNGDISHPRGSGPGNLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKRESCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQRRHVPRGANPQGPTAPNNLPGGRGEWQQQNIPDHACPKCGEVLPDLDSLQIHIMDCII 517 Q5RJR8 Leucine-rich repeat-containing protein 59, N-terminally processed Lrrc59 10116 Yes SL-0178 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}. UNIPROT Q5RJR8 UNIPROT Q63742 Pfam PF13855 PROSITE PS51450 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}. P11362 EBI-1028277,EBI-22243518 GO:0005789 GO:0016021 GO:0042645 GO:0005635 MTKTGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATVLDLSCNKLSTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNRLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQQAKEAKERELRKREKAEEKERRRKEYDAQKASKREQEKKPKKETNQAPKSKSGSRPRKPPPRKHNRSWAVLKGLLLLLLLCVAGGLVVCRVTGLQQQPLCTSVNAIYDNAVQGLRHHEILQWVLQTDSQQ 307 Q5SNT2 Transmembrane protein 201 TMEM201 9606 Yes SL-0178 SL-0179 SL-0182 [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}. UNIPROT Q5SNT2 UNIPROT B9EH90 UNIPROT Q5SNT3 Pfam PF10476 Pfam PF09779 DisGeNET 199953 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}. P57078 EBI-4422308,EBI-10986145 P61021 EBI-8320093,EBI-10986145 Q8N3V7 EBI-352936,EBI-10986145 GO:0005737 GO:0005639 GO:0005635 GO:0031965 GO:0000922 GO:0051015 GO:0005521 GO:0051642 GO:0010761 GO:0006998 GO:0030473 GO:0090435 MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTMVNCWFCNQDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYLEHLNHVVSSAPSLRDPSQPQQWVSSQVLLCKRCNHHQTTKIKQLAAFAPREEGRYDEEVEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFKRREADQTHAQNFSSAVKSPVQVILLRALAFLACAFLLTTALYGASGHFAPGTTVPLALPPGGNGSATPDNGTTPGAEGWRQLLGLLPEHMAEKLCEAWAFGQSHQTGVVALGLLTCLLAMLLAGRIRLRRIDAFCTCLWALLLGLHLAEQHLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRFFPGDSAGLFPTSPSLAIPHPSVGGSPASLFIPSPPSFLPLANQQLFRSPRRTSPSSLPGRLSRALSLGTIPSLTRADSGYLFSGSRPPSQVSRSGEFPVSDYFSLLSGSCPSSPLPSPAPSVAGSVASSSGSLRHRRPLISPARLNLKGQKLLLFPSPPGEAPTTPSSSDEHSPHNGSLFTMEPPHVPRKPPLQDVKHALDLRSKLERGSACSNRSIKKEDDSSQSSTCVVDTTTRGCSEEAATWRGRFGPSLVRGLLAVSLAANALFTSVFLYQSLR 666 Q5SQN1 Synaptosomal-associated protein 47 SNAP47 9606 Yes SL-0198 Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}. UNIPROT Q5SQN1 UNIPROT B6EDE0 UNIPROT Q5HYB5 UNIPROT Q5TBZ3 UNIPROT Q8N558 UNIPROT Q8TB31 UNIPROT Q8TCW8 UNIPROT Q8WV46 UNIPROT Q96CQ3 UNIPROT Q96FE1 UNIPROT Q96I66 UNIPROT Q96NU3 UNIPROT Q9BT10 UNIPROT Q9BVB2 PROSITE PS50192 DisGeNET 116841 Plays a role in intracellular membrane fusion. {ECO:0000250}. Q92844 EBI-356349,EBI-10244848 O95183 EBI-10191195,EBI-10244848 P51809 EBI-10244848,EBI-1052205 Q9BV40 EBI-10244848,EBI-727028 O75379 EBI-10244848,EBI-744953 Q15836 EBI-10244848,EBI-722343 Q9Y6D6 EBI-1044254,EBI-10244848 Q92845-3 EBI-11294297,EBI-10244848 Q9UPN3-2 EBI-4295250,EBI-10244848 Q13190 EBI-10244848,EBI-714206 Q86Y82 EBI-10244848,EBI-2691717 P32851 EBI-539720,EBI-10244848 P43360 EBI-10244848,EBI-1045155 Q08379 EBI-10244848,EBI-618309 Q12846 EBI-10244848,EBI-744942 Q6P597 EBI-10244848,EBI-1643885 Q8IYX8-2 EBI-10244848,EBI-10181988 Q8IZU0 EBI-10175124,EBI-10244848 Q969F0 EBI-743099,EBI-10244848 Q96R06 EBI-10244848,EBI-413317 Q9UJV3-2 EBI-10172526,EBI-10244848 Q96GX1 EBI-11349465,EBI-10244848 Q86X19 EBI-11343485,EBI-10244848 P28574 EBI-1183003,EBI-10244848 Q15388 EBI-711636,EBI-10244848 Q8IWR1 EBI-10262539,EBI-10244848 P55056 EBI-10244848,EBI-18302142 P61266 EBI-9071709,EBI-10244848 Q16623 EBI-712466,EBI-10244848 Q9Y624 EBI-742600,EBI-10244848 Q96K19-5 EBI-12055631,EBI-10244848 Q9NR31 EBI-3920694,EBI-10244848 Q9HCJ2 EBI-3925442,EBI-10244848 Q9H400 EBI-2830566,EBI-10244848 P41181 EBI-12701138,EBI-10244848 O14880 EBI-724754,EBI-10244848 P15151 EBI-3919694,EBI-10244848 Q8N6L0 EBI-749265,EBI-10244848 Q8N137 EBI-947360,EBI-10244848 Q9UJY5 EBI-10244848,EBI-447141 Q9NTX5 EBI-10244848,EBI-2807146 O75396 EBI-1058865,EBI-10244848 Q9P2W9 EBI-725334,EBI-10244848 O15400-2 EBI-11042829,EBI-10244848 GO:0030425 GO:0098978 GO:0098686 GO:0043025 GO:0048471 GO:0005886 GO:0014069 GO:0031201 GO:0030672 GO:0005484 GO:0019905 GO:0098967 GO:0006887 GO:0060291 GO:0031629 GO:0016082 GO:0006906 MRAARRGLHCAGAERPRRRGRLWDSSGVPQRQKRPGPWRTQTQEQMSRDVCIHTWPCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTGEILVSFPLSSIVEIKKEASHFIFSSITILEKGHAKHWFSSLRPSRNVVFSIIEHFWRELLLSQPGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTELESPAWWPFSSKLWKTPPETKPREDVSMTSCEPFGKEGILIKIPAVISHRTESHVKPGRLTVLVSGLEIHDSSSLLMHRFEREDVDDIKVHSPYEISIRQRFIGKPDMAYRLISAKMPEVIPILEVQFSKKMELLEDALVLRSARTSSPAEKSCSVWHAASGLMGRTLHREPPAGDQEGTALHLQTSLPALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT 464 Q5T0L3 Spermatogenesis-associated protein 46 SPATA46 9606 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q4FZF2}. Note=Located throughout the subacrosomal area. {ECO:0000250|UniProtKB:Q4FZF2}. UNIPROT Q5T0L3 UNIPROT Q6X961 UNIPROT Q8NEC3 Pfam PF17734 OMIM 617257 DisGeNET 284680 Plays a role in spermiogenesis and fertilization. {ECO:0000250|UniProtKB:Q4FZF2}. Q93062 EBI-750105,EBI-740322 Q9H0I2 EBI-750105,EBI-744099 Q15834 EBI-750105,EBI-739674 Q13077 EBI-359224,EBI-750105 O43711 EBI-750105,EBI-3939165 O76011 EBI-1047093,EBI-750105 A8MQ03 EBI-3867333,EBI-750105 P50747 EBI-750105,EBI-3915568 Q9Y343-2 EBI-750105,EBI-11075770 Q99685 EBI-750105,EBI-721306 Q14C86-2 EBI-750105,EBI-21529077 P48729-2 EBI-750105,EBI-2040168 O15151 EBI-750105,EBI-398437 A2RUC4 EBI-750105,EBI-21511702 GO:0031965 GO:0030154 GO:0007342 GO:0007283 MENFSLLSISGPPISSSALSAFPDIMFSRATSLPDIAKTAVPTEASSPAQALPPQYQSIIVRQGIQNTALSPDCSLGDTQHGEKLRRNCTIYRPWFSPYSYFVCADKESQLEAYDFPEVQQDEGKWDNCLSEDMAENICSSSSSPENTCPREATKKSRHGLDSITSQDILMASRWHPAQQNGYKCVACCRMYPTLDFLKSHIKRGFREGFSCKVYYRKLKALWSKEQKARLGDRLSSGSCQAFNSPAEHLRQIGGEAYLCL 261 Q5TZ18 Neuron navigator 3 nav3 7955 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000250}. UNIPROT Q5TZ18 Pfam PF00004 Pfam PF00307 PROSITE PS50021 May be involved in neuron regeneration. {ECO:0000250}. GO:0030175 GO:0005794 GO:0030027 GO:0005640 GO:0003779 GO:0005524 GO:0072576 GO:0007399 GO:0022008 GO:0031016 MAHGLAPRSSELRVTESPMLSCQLSFKTEIHDRRTNLVPAPAATLARSSREAEESKICKIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLSAEEVCNGNLKSILGLFFILSRYKQQQQHQQQYLQSLVELQQHVTHQTTGAAQLSQHKTQDMQSSLTARYTSPPGHSGIAAPQKKNTRLPGPSRVPAAGSGSNSSKGSSNLNRRSQSFNSIDKSKPLQYASGNDRGSMNGSGSVPSSTSGQQLASAIPSPTAGKTWRSKSMNMKHSATSSMLATKPPSPTSSPTPPSSSDRLRPPITDASKSAPGNQRSMLEKFRILNPRATSRTSPSVAEMALQEEDDLSEFGDEGTFSPTPPCGISKQQGKPSASAFAPPSKSNNCKNHNNKSLPQPKDKEDKNKTKNKASTPPKEEPVIVETSKKGSKIASLIPKGSKTSAASVKKESAIPASSSIPKPGLKAPTATSKPAGTQSCVPATTGGEKTKLNKGSQSIYMQRSLGGLENRKTSMVLSTSTSALSASTTSGLGGGCALGGNGAVQLPQQQQHNHPNTATVAPFMYRTYSENDCTTVVPPEPCLSPTKELVYGKTAKQCLEEISGEDPETRRMRTVKNIADLRQNLEETMSSLRGTQITHSTLETTFDTTVTTEVNGRGLPALSSRSSPMSWRLGQGSSPRLQAGDAPSYTPPRSSAGSTTVRYGEPSRLLYTAPLRRAAASGARGAEPGEKGGISEVGPEVDVTGYGSDGDILAKNVHADDISGYHTDGGIYSRNVDLYSRNVGRPAEMTPAREVVQKGVKEMQGEDSWDDSSSVSSGLSDTLDNISTDDLNPAPYSGISSRKSKAAQSNKETHRHIEQDASSWAGAEDLKKVDEEMEPGMDPSCKWKTSSPSSSCQGEDISQKTGLPMSQTGSWRRGMSAQVGITPPRTKGTSTSLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSGSATLGKVPKSACIGKSTGISNGRKTSLDGAQHQDDAVLLGCGGSEVPLQYRSLPRPAKSSSGGSSVVSRSGHRSSSSSIDSNVSGKSAGGSGVAVGTPTSTKRRDTGKVGSGRSSPVTINQTDKEKVAGSDQEGTGLPTSPKSSPTSTQSGLRQPGSKYPDIASPTFRRLFGSKASSKPSSPGTPDSGKCPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQSGGSSPLYGKTPDLGTDSPASSPASGLSLPSNARPWPPNLSSSSAGSKDTLSCHSMTSLHTSSESIDLPLPHHHGPKVTRTGSVKSTLSEGMPLDRNTLPKKGLRQTSHEEGKEWLRSHSTGGLQDTGSPLSPPGTTCANAGKYHYSNLLSPTSMSQYNIPSTSMSRSNSIPAQDSFELYGEGHPLGGSATSLEERPRGMSRSGSFRDSTDEVHGSSLSLVSSTSSLYSAQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELRETIEALKTQNTDAQTAIQVALNGPDHVHRDLRIRRQHSSESMSSINSAASHSSLGSAKDAEDKKKKKKSWLRSSFKQAFSKKKTNKPQSSHDEIEEMTDSSLPSSPKLLHISRQASSPQPLLSSPSTTELCECTEAEAEIILQLKNELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIELLKAENDRLKSSGNTTPAATPAKTARPPSETSSTSSSSSRQSLGLSLNNLNITDTIMSDILLDDGYEGNLRKEGRSVRIVVTINSDSNKTKAMQKKQYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRVDPLTSLGMNSDSIVCYRMGDVVRSHASEVPELLPCGYLVGDNNVITVTLKGVKEGSIDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFILSKTGREVTDTNLATFNVDQKSSKDLRQYLSSLAEQCNTEECEIELPTVVILDNLHHIGSLSDIFNGFLNCKYHKCPYVIGTMNQGVSSSPNLELHHNFRWVLCANHTEPVKGFLGRFLRRKLIETEIDKNMRSNDLIKIIDWIPKIWQHLNSFLEAHSSSDVTIGPRLFLSCPMDADGSRVWFTDLWNYSLVPYLLEAVREGLQHEGQSLLQLRPEDVGYDGYSSSKDGAASKQVSQSDTEGDPLMNMLMRLQEAANYSSAQSCDSDSASHHEDLLDSSLESAL 2269 Q5U249 Protein ELYS ahctf1 8355 No SL-0178 SL-0185 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}. UNIPROT Q5U249 Pfam PF13934 Pfam PF16687 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}. Q6P5F9 EBI-2550236,EBI-11609120 GO:0005737 GO:0005643 GO:0005654 GO:0003677 GO:0051028 GO:0015031 MQNLEAQVTGSLVAFPDVTQKALKEDEINLDSVLRGKFSTGRTSLAWLACGPQLEITNSVTGERISAYHFSGLTERPPVVVAVKEFTWQKKTGLLVGLVEAEGSVLCLYDIGISKVVKAVVLPGSVTAVEPIINHGGASASTQHLHQSLRWFFGVTAVVTDVGHVLLIDLCLDEVSSNQDELDASDLEVMSVIPTKIPKLREAATRERRHLCLQLAAPTGTTVSCLSYISRTNQLAVGYSDGYFSLWNMKTLRRDYHVQIEGGRVPVCAVAFQEPENDPRNCCYLWAVQSSESGGDVSLHLLQLAFSDRKCLASGQIMYELLEYCEERYSLDLSGSTLSLRGQSNNTKLLGCQTIEKFRVHGEREDGVHEVTSPDTSVSVFSWQVNTYGQGKPSVYLGVFDINRWYQAQMPDSLRSGQFLRNCSYFAFWSLEAVVNITTQDIIFDILVHERSLSRGIPPSYPPPEQFYYPSTYNFDATCLLNSGLIHFACTGFQKETLHFLKKSGSSLNEAIPDGYNRCLAAGLLAPKFTDVQASSLSQEEQLQAILAAAVETSSLGLLTSCIKRWTAEEQPRSAANLRFVLEWTWKKVTLTKQEFDRLCFRLFDGSCNFIDPHTLQSLQQCHLYFSNLTAVLNCFIAQAKEVTQQGAVDLTNKQSVTRLLTLYASVVLWFCRSGMLPDSSDETVQLTRPFYNYQVIQQYYSDQRKKLERLARGKWDTSSLMIDGLINQFGDRIQQLWSRDDNGTGKYPPANLHALLDVYLLENADEMSKHAITIYFLLDIMYSFPDKPDSSIESFPTAFFVPGSLIKLIQGFWLLDHNDYQNSVDCILNPASSRVMSWQHSQIIENLLCHGDSRQALRYLQVMKPVATTSKEVKLHMTVLLANRSILEAWNLQRLHSSRLNVEELLKHMYEMCQEMGLIEELLKLTFTDFEQGYLHKFLQTTGVQNQELLLVHHLQRANYISALQLNQSLKTNHLNDCDRRLRERSGARNAILDQYGKILPRVQRTLASERAKPYSLPSLVWREVARPKPLSTTAKQAAPGSIITKANFICNVLSKIKEVSTANEKREEYSPYQSMVSEEPTAPPLQDIDVPDAFFGTPINKSRRVSRLLDSVVHPVLMEPTPLTSSDTDNNQTPHKSPLLKTSSPLHSSLRRIAHMRSFAKASEFSLLETPLVVRKAKALAANTASSGYTSITPQSILRSSVRTTPLVSPSVSPGRSLTPPLRPKETKISFMELSFTRHAKAAHSSEGNLLAISPVLRSSPDAVWSVKGKVASFTQNTPVKKLDEIDASSSGIQEESQDEMEVSKEISNISVRSEQASLEYHDAPTPEDLENDEISGTTNSQPQVNEVHHQMEDGQLTEKPAELALTEMQEEFIDSEEREIEYISAPLNGPNALECMTAVPDIYLEDASQCILETPEGSSVSVTGEQECVSSAKDSESVISIHDSDDAHSNLSENDQDSEEIEENNLRVPTTVTRCEEFDLIETKDLEVELEEADSEKTNYKDIYPDATVQLGFTVESIEQRYTCELADRRETPSETDEIEGEHFETENNFSLVLEGDVTEEEILEPSSSKTDLELTRPPIAHQKLISENRENIENCETTEKIPANMSPLVDSDHESKTLETLPSEADLSVAEKVLKGTEEKDVPPEVHSEVVLESKLVGNAMMSLDSSESQEVIISQYDNVISIEKLEMTQEKMYGEKTEQINEGQVSPNRDQSTLVKPLTPRRSIRKSSKPADSSTDIIGNITLPTTPKRGLKKAKENVDTLKNSISVVPEEELTLGTRRITRKATLTALDNPEPLQIKEPPSGEDLQVQPSTPTRGRRGKVITSDDLKEPPSGEDLQVQPSTPTRGRRGRVITSDDLREPPPGEDLQVQPSTPTRGRRGRVITSDDIKESPSVEDLQVQPSTPTRGRRGKVITSDDIKEPPSVEDLQVQPSTPTRGRKGKVITSDDIKEPLSGEDLQVQPSTPTRGRKGKVITSDDIKEPLSEEVLQEQPSTPTRGRRGRVITSDGKGYECVEEKNALPLTPTRITRSKNILEPEKGISQIEPEKGISQIEPDKGLSQIEDTGETEHEVVTPRRGRRGKRVVNELVKHFERNSSQPNIKADTSPPVSPKKVSLRWTRTRSENQRINATEEQASKIQEDLSDTPRKRYKKSSNKMGFEETTDTVTEGAIVEDVQESLIISHLGKNPNTSIVRSARKTALPPVTEDHSEQPLLPPESHSKVHSSLAIADEENKTNTRTRSGNKSSVDVSAITFEFSTPKARTKKTAKGSAVPTELIPSTQYVFSPPSTRTRRATRANVSEAVIEPQLQFQESCEIAETEVPEVPASKPRGRPPKHKAKAVTRVLKKPSWSTPPVEIKLISPPESPAVSETNTKTDSTEAKGAEKISVRRTRRRIIAKPVTRRKMR 2408 Q5U2W6 Prostate tumor-overexpressed gene 1 protein homolog Ptov1 10116 Yes SL-0198 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}. UNIPROT Q5U2W6 Pfam PF11232 May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation (By similarity). {ECO:0000250}. GO:0044798 GO:0005654 GO:0048471 GO:0005886 GO:0045944 MVRPRRAPHRSGAGGPLGGRGRPPRPLVVRAVRSRSWPAGPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGGLAVNEHRLSNKLLAWSGVLEWQEKRRPFSDSAAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNSQLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNAIRQVITTRKQAVGPGGVHSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTDQWPRRLFMQLIPQQLLTTLVPLFRNSRLVQFHFTKDMETLKSLCRIMDNGFAGCVHFSYKASCEVRVLMLLYSSEKKIFIGLIPHDQSNFVNGIRRVIANQQQVLQRSLEQEQQQRGMGG 416 Q5U349 Ubiquitin carboxyl-terminal hydrolase 2 Usp2 10116 Yes SL-0198 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}. UNIPROT Q5U349 UNIPROT Q9QXL3 UNIPROT Q9QXL4 UNIPROT Q9R083 UNIPROT Q9R084 Pfam PF00443 PROSITE PS00972 PROSITE PS00973 PROSITE PS50235 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}. GO:0005938 GO:0005813 GO:0005737 GO:0016020 GO:0005634 GO:0048471 GO:0030332 GO:0042802 GO:0046872 GO:0004843 GO:0031625 GO:0007049 GO:0048512 GO:0032922 GO:0043153 GO:0045475 GO:0007517 GO:0051926 GO:0048642 GO:0000122 GO:0045931 GO:0048643 GO:0016579 GO:0050821 GO:0006511 MSQLSSTLKRYTESSRYTDAPYAKSGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPLLRSDITGGSKRSESQTRGNERPSGSGLNGGSGFPYGVTSNSLSYLPMNARDQGVTLGQKKSNSQSDLARDFSSLRTSDSYRTSDGYRASDGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPSRVPEVLSPTYRPSGRYTLWEKNKGQASGPSRSTSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVAARPKPSPESLDHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM 618 Q5U395 CTD nuclear envelope phosphatase 1A ctdnep1a 7955 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q5U395 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0004721 GO:0004722 GO:0006998 GO:0010867 GO:0006470 MLKTRQCLLGIRTFLGVTSRIWSFFLYILRKHLRTIIQYQTVRYDILPLSPISRNRLNAVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGILKRRYYRQHCTLDLGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTSDVRSVLSRNLHQHRLW 245 Q5U651 Ras-interacting protein 1 RASIP1 9606 Yes SL-0198 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. UNIPROT Q5U651 UNIPROT Q6U676 PDB 5KHO PDB 5KHQ Pfam PF01843 Pfam PF00788 PROSITE PS51126 PROSITE PS50200 OMIM 609623 DisGeNET 54922 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}. Q5NI89 EBI-2796250,EBI-2797123 P60953 EBI-81752,EBI-2797123 Q9H0H5 EBI-717233,EBI-2797123 O95229 EBI-1001132,EBI-2797123 O43684 EBI-1050987,EBI-2797123 Q7TSY8 EBI-2552468,EBI-2797123 Q9H4P4 EBI-2130266,EBI-2797123 Q9DC28 EBI-6392453,EBI-2797123 Q9JLB0 EBI-771456,EBI-2797123 Q14103 EBI-299674,EBI-2797123 Q9NVK5 EBI-1104764,EBI-2797123 Q9BRV8 EBI-1773646,EBI-2797123 Q99PU7 EBI-1791471,EBI-2797123 O95817 EBI-747185,EBI-2797123 Q6NYC8 EBI-2557469,EBI-2797123 Q8N6T3 EBI-716933,EBI-2797123 A0A384KVT4 EBI-2797123,EBI-2842443 P23528 EBI-352733,EBI-2797123 GO:0005911 GO:0005795 GO:0048471 GO:0032991 GO:0051020 GO:0042803 GO:0001525 GO:0048754 GO:0010507 GO:1905709 GO:0035024 GO:2000299 GO:0033625 GO:0043087 GO:0007165 GO:0001570 MLSGERKEGGSPRFGKLHLPVGLWINSPRKQLAKLGRRWPSAASVKSSSSDTGSRSSEPLPPPPPHVELRRVGAVKAAGGASGSRAKRISQLFRGSGTGTTGSSGAGGPGTPGGAQRWASEKKLPELAAGVAPEPPLATRATAPPGVLKIFGAGLASGANYKSVLATARSTARELVAEALERYGLAGSPGGGPGESSCVDAFALCDALGRPAAAGVGSGEWRAEHLRVLGDSERPLLVQELWRARPGWARRFELRGREEARRLEQEAFGAADSEGTGAPSWRPQKNRSRAASGGAALASPGPGTGSGAPAGSGGKERSENLSLRRSVSELSLQGRRRRQQERRQQALSMAPGAADAQIGTADPGDFDQLTQCLIQAPSNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGNSSGRGGSPAPYVDTFLNAPDILPRHCTVRAGPEHPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDPRTGGSGPARPPWLPARPGATPPGPGWAFSCRLCGRGLQERGEALAAYLDGREPVLRFRPREEEALLGEIVRAAAAGSGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPENHPEGVPEVPLTPEAVSVELRPLMLWMANTTELLSFVQEKVLEMEKEADQEDPQLCNDLELCDEAMALLDEVIMCTFQQSVYYLTKTLYSTLPALLDSNPFTAGAELPGPGAELGAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSMAVNLLCVPRTSLLKASWSSLRTDHPTLTPAQLHHLLSHYQLGPGRGPPAAWDPPPAEREAVDTGDIFESFSSHPPLILPLGSSRLRLTGPVTDDALHRELRRLRRLLWDLEQQELPANYRHGPPVATSP 963 Q5VWP3 Muscular LMNA-interacting protein MLIP 9606 Yes SL-0178 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}. UNIPROT Q5VWP3 UNIPROT B7Z2N0 UNIPROT D6RE05 UNIPROT Q96H08 UNIPROT Q96NF7 Pfam PF15274 OMIM 614106 DisGeNET 90523 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}.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}. GO:0005635 GO:0031981 GO:0005634 GO:0016605 GO:0042383 GO:0005521 GO:0003714 GO:0010614 GO:1903243 GO:0000122 GO:0045944 MELEKREKRSLLNKNLEEKLTVSAGGSEAKPLIFTFVPTVRRLPTHTQLADTSKFLVKIPEESSDKSPETVNRSKSNDYLTLNAGSQQERDQAKLTCPSEVSGTILQEREFEANKLQGMQQSDLFKAEYVLIVDSEGEDEAASRKVEQGPPGGIGTAAVRPKSLAISSSLVSDVVRPKTQGTDLKTSSHPEMLHGMAPQQKHGQQYKTKSSYKAFAAIPTNTLLLEQKALDEPAKTESVSKDNTLEPPVELYFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRSPKTLLGSDTVKTPTTLPRAAGRETKYANLSSPSSTVSESQLTKPGVIRPVPVKSRILLKKEEEVYEPNPFSKYLEDNSDLFSEQDVTVPPKPVSLHPLYQTKLYPPAKSLLHPQTLSHADCLAPGPFSHLSFSLSDEQENSHTLLSHNACNKLSHPMVAIPEHEALDSKEQ 458 Q5W5U4 Probable ATP-dependent RNA helicase DDX4 DDX4 9913 Yes SL-0198 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}. UNIPROT Q5W5U4 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0033391 GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0071546 GO:0071547 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0030154 GO:0043046 GO:0007276 GO:0031047 GO:0007141 GO:0007140 GO:0007275 GO:0010529 GO:1990511 GO:0034587 GO:0007283 MGDEDWEAEIIKPHISSYVPVFEKDRYSSGANGDTFNRTPASSSEMGDGSSRRDHFMRSGFASGRSLGNRDPGESNKRENTSTVGGFGVGKSFGNRGFSNNKFEEGDSSGFWRESSIDCEDNQTRNRGFSKRGGYQDGNDSEALGSSRRGGRGSFRGCRGGFGRGSPNSDYEQDEGTQRSGGIFGSRRSALSGAGNGDTFQSRSGGGSGRGGYKGLNEEVITGSGKNSWKSEAEGGESGDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDPPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIIQGGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDVIGKEKIGLRQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDSQLAQPLVKVLSDAQQDVPAWLEEIAFSTYGPGFSGNARGNVFASVDTRKNYPGKSSLNTAGFSSTQAPNPVDDESWD 729 Q5XGC9 Serum response factor-binding protein 1 srfbp1 8364 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}. UNIPROT Q5XGC9 UNIPROT Q28EI0 Pfam PF09073 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}. GO:0030686 GO:0005634 GO:0048471 GO:0030490 MEPVLNLNNEVVKLRKDVKKVKVLIIRKLTRHIAKLKSKKGTEELILKNQRRAQRLLEEIHSVKELKPDDVTKTALRKEISFEKVCKKPNSTAEERALARLATHPLLKQKITAIKEAIKAFKDARKTAAEGEREREKDEPEQVTKIKETKKPVQAKLNKNTEEIKSAKEHVKEEKCKNLLEDSDKGTEKALELPYVQENLPEQTAENKEQPKAQDVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPVVESPAVERPPVESPPKKKACLEQELGCELSDIEDSDKEKEYFDDSTEERFYKHSSSFEDSDSGSDNDFFIGKIRRTKKKKSDKDGSKQKEEKVPPTKEKAQTSEVQKEIPTAKSMKLKSVFCKSLSQTKPKPSFTKRETNFRQERNKRPVMPQASPLAKKPLQSKATSVRQPGRKLEAQPLHPSWEASRKRKEQQAQITKFQGKKIVFDD 535 Q5XGN1 Nucleoporin NUP42 nup42 8355 No SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5XGN1 UNIPROT Q4QQY9 PROSITE PS50103 Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}. GO:0031965 GO:0005643 GO:0046872 GO:0051028 GO:0015031 MAICNFFLQGRCRYGEKCWNEHPRGGGGGGGNRYQSQNRYQEQSRYQEQSRYPEQSRYPEQNRYQEPAGNAKGTWGASSQRYVQPSNFSKSTTWINRDSEKPSAGSFSGFGSRNVKSTAATGLPSTQNRFAALSSQDNSRDGQTDKGNILDDIMKDMEIWESSGQWMFSVYSMLKEKKNISGFTDFSPEELRLEYSVCQAEGNPLKYINAVQQLGSKWKQRILELKNPNPSIKTALLNELNSPSPDVTPGYSGQQNSAFGALSFPTSNTAPTAVTFSFKADTTTAAKPAVPNALAGSDFSAFGNKPTSAPSFGSGVAAAAASFSFAPSTISGFGSTASNSGFGAASNAAGFQGAANIAAAPAFGVASSTAPASGFGGGFGTTVNTGAKTSSVRDLFSAGTAVPVQTTLLFGQATGSLNTTASSTSLAGQPFKASTSATAVSGSFTSDNTSNPLFTPRNELSVEDLAQFEAKQFTLGKTPIKPPSADLLKVT 491 Q5XIS2 Ceramide-1-phosphate transfer protein Cptp 10116 Yes SL-0178 SL-0182 SL-0183 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}. UNIPROT Q5XIS2 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0016020 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0008289 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0050713 GO:1900226 MDGPERDFNLKVVLISFKKCLTDKGEVLLDHYTASWKGLVRFLNSLGAVFSFISKDVVSKLQIMEHLRSGPQSEHYISLQSMVAYEVSNKLVDRDSRSRPRHPNSGCRTVLRLHRALHWLQLFLEGLRTSSEDARTSTLCSEAYNATLAAYHSWIVRQAVNVAFHALPPRKVFLEAMNMGSSEQAVEMLGEALPFIEQVYDISQKLYAEHSLLDLP 216 Q5XTS1 Calcium-independent phospholipase A2-gamma PNPLA8 9986 Yes SL-0198 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}. UNIPROT Q5XTS1 Pfam PF01734 PROSITE PS51635 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}. GO:0005789 GO:0000139 GO:0016021 GO:0048471 GO:0004622 GO:0016042 MSINLTIDICIYLLSNARNLCGKHRSKQLHLVCSPNHCWKIRHVSLQRGLHPHKVRCKWTKSETHSCSKHYYSPSNHGLHIGILKLSTSAPKGLTKVSIRMSRIKSTLNSVSKAVFGSQNEMISRLAQFKPSSRILRKVSDSGWLKQESIKQAIRSLKKYSDKSTEKSPVPEGRNHIIDKEDDIGKQSLFHYTGNITTKFGESFYFLSNHINSYFKRAEKMSQDKENSHFQEKSELEGKKVEEGKSSSLDPGILTSQADKPDPKSSAGTMDKATSPSGTPESLPISTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKYDSKSQAEEQEEPAKSEPAGSKDKTVEEKKHLSLQREKIIARVSIDNRTRALVQALRRTADPKLCITRVEELTFHLLEFPEGKGVAVKERLIPCLLRLRQMKDETLQAAVREILALIGYVDPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHLPLDECEELYRKLGSDIFSQNVIVGTVKMSWSHAFYDSQTWEKILKERMGSALMIETARNPMCPKVAAVSTIVNRGSTPKAFVFRNYGHFPGSQSHYLGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDAPLECIVSLGTGRYESDVRNNTTYTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGSKYIERNEHKMKKVAKILSQEKTTLQKINDWIKLKTDMYEGLPFFSKL 786 Q5XVI1 Protein SINE1 SINE1 3702 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}. UNIPROT Q5XVI1 UNIPROT Q1KS90 UNIPROT Q9SLJ5 Plays a role in nucleus positioning in guard cells. {ECO:0000269|PubMed:24891605}. GO:0005737 GO:0016021 GO:0005635 GO:0031965 GO:0005634 GO:0032797 GO:0003779 GO:0000387 MGLNLNPILRQELANLDKDTESRKSAMKALKSYVKDLDSKAIPGFLAQVFETKETNSLSGEYTISLYEILARVHGPNIVPQIDTIMSTIVKTLASSAGSFPLQQACSKVIPAIARYGIDPTTTEDKKRVIIHSLCKPLTDSLLASQESLTSGAALCLKALVDSDNWRFASDEMVNRVCQNVVVALDSNSNQTHLQMGLVMSLAKHNPLIVEAYARLLIHTGLRILGFGVSEGNSQKRLSAVQMLNFLMKCLDPRSIYSEVELIIKEMERCQSDQMAYVRGAAYEAMMTSKRIAAELESKMEKGCRSVTGSNFSRRNCSSIVPDYSLSPESQTLGSFSGYDSPVESSPISHTSCNSEFDRRSVNRKLWRRDENGGVVDISLKDGLFSRVTKGSTTVSDSPLVPYDTCENGDEFEGFLMESLRNTTPSPQRQRSRRINAEDFNIFSTPRKLISSLQYPDDVDLDHSDIQSPILRGEREKTIGSRKNPKLRKQFPTMVETMSSTITVSEDTAQTQMITGKKKKKKMSYAKLVIAISFVVVALFATVILMVNQDDDVGYYTVPT 560 Q5Y5T1 Palmitoyltransferase ZDHHC20 Zdhhc20 10090 Yes SL-0198 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}. UNIPROT Q5Y5T1 UNIPROT Q3TDL1 UNIPROT Q8VCL6 UNIPROT Q9D3Q8 Pfam PF01529 PROSITE PS50216 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}. GO:0005783 GO:0005794 GO:0030173 GO:0043231 GO:0048471 GO:0005886 GO:0016409 GO:0019706 GO:0008270 GO:0018230 GO:0018345 GO:0006612 MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVSTISRTGEKGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQDILRRAARDLPIYTTSASKAIRYCEKCQLIKPDRAHHCSACDRCVLKMDHHCPWVNNCVGFTNYKFFMLFLLYSLLYCLFVAATVLEYFIKFWTLCRRKSTENCPKNEPTVLNFPSAKFHVLFLFFVSAMFFVSVLSLFSYHCWLVGKNRTTIESFRAPMFSYGIDGNGFSLGCSKNWRQVFGDEKKYWLVPIFSSLGDGCSFPARLVGMDPEQASVANQSDYVRSIGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGVTKSGTNNHVTVEIEN 380 Q5ZI22 Nucleoporin NUP42 NUP42 9031 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. UNIPROT Q5ZI22 PROSITE PS50103 Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}. GO:0031965 GO:0005643 GO:0005634 GO:0046872 GO:0005049 GO:0051028 GO:0015031 MTICQFFLQGRCRFGDRCWNEHPRGGGGRPHSAGPVRGAGGGWGAASQRYANVIQPPIFKHSTWGGSGDGGGFSGASDFGSPGNKSAVFSQNRFSALSSAHPADGFSDEEQRLLDCVAKDMATWESSGQWMFSCYSPEAGKPNVSGFREFSAEEVRLEYYNCSANNNTENYINSVNQLVQERRNRLQELKALNASGKESLLSQLKNAVTQPLPSLGFGGQQASSFGFPSFPVSSSSGAASFSFKANPSVPPGNAAAVGSSAAASNPPTFGVTSSPSVPNPVGSGNSSAPSAASFSFKTSGTTSGCGTSGLSGFGSSAAANSSSTAPLPVSATPSAATGTSQSGASSASAAQTAGASGHNVTSAPSAVPNGIASDKLYTPRSELTAEELEQFEAKRFTLGKIPLKPPPIDLLYL 413 Q5ZJY9 Nuclear envelope integral membrane protein 2 NEMP2 9031 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. UNIPROT Q5ZJY9 Pfam PF10225 DE Reference Proteome: Yes; GO:0016021 GO:0005635 GO:0005637 MGPRRLPWARPGPALGLLLLALAGAVPAAGGSCSLLEEGNTIQKLHEDCFCYVQNRTMHLQYIWSTVQVKINSTRTFRFVPTPEKSNCRNSETVFEFAACAVQILWRPETSTETFLKIKQYGEDFCFRIQPFKEELYTVSMTREMLDGKLLFLFAAGIFLFHFANSLSRSTNFFYLSGIILGVLALLVFVLLALKRFIPRRSTFWILLSGCWMSSLYLIYCFKENMQWLWSEHRIYVLGYFVAVGTLSFATCYQHGPLTSELSITLFTWTLQLTAFVFIYCGVNIPQVAYAIIAVKPSPKGLGYPPAAAWHIGRKMKNHFQSKKVVVRCLTEEEYREQGETETVRALEELRSFCKNPDFSSWLAVSKLQSPHRFAGFVLGSPHVSPAETKAHDEEYGIGSSFLEEQLFETRTESEQDETTSYIHEGDDENEDEIHEPISFPYATELL 447 Q5ZKD9 Kelch-like protein 20 KLHL20 9031 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. UNIPROT Q5ZKD9 Pfam PF07707 Pfam PF00651 Pfam PF01344 PROSITE PS50097 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}. GO:0031463 GO:0005737 GO:0005829 GO:0048471 GO:0016605 GO:0005802 GO:0019964 GO:0004842 GO:0006895 GO:0043066 GO:0043161 GO:1990390 GO:0015031 GO:0016567 MDGKPMRRCTSTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTSLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSTKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGYLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW 610 Q5ZM35 Twinfilin-2 TWF2 9031 Yes SL-0198 Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}. UNIPROT Q5ZM35 Pfam PF00241 PROSITE PS51263 Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}. GO:0005884 GO:0005623 GO:0005737 GO:0030016 GO:0048471 GO:0051015 GO:0003785 GO:0030042 GO:0051016 GO:0010976 GO:0010591 GO:0042989 MTHQTGIHATTELRDFFAKARNGSVRLIKVIIEEEQLVLGAHKELARRWDVDYDAFVLPLLDEQQPCYVLYRLDSQNAQGYEWLFISWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDEMFGTVKEDVSLSGYQKHVSSCSAPAPLTAAEQELQQIRINEVKTEISVESKHQTLQGLAFPLQLDAQQAIQTLKQKKINYIQLKLDLERETIDLVHTSPTDISDLPKRIPQDSARYHFFLYKHSHEGDYLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDTVEQEFCLEIAKKIEIDDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPVGKRGQKRLIKGPGENGEDS 349 Q5ZSQ2 Adenosine monophosphate-protein hydrolase SidD sidD 272624 Yes SL-0382 Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:21680813}. UNIPROT Q5ZSQ2 PDB 4IIK PDB 4IIP 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}. GO:0044220 GO:0046872 GO:0044603 GO:0017137 GO:0009405 GO:0018117 GO:0044602 GO:0043087 MVYYEIIKDIVFTYNLQFTHLIHNDRISEVNLGGVTMRSIITQICNGVLHGQSYQSGSNDLDKGNSEIFASSLFVHLNEQGKEIIKHKDSDDKIVIGYTKDGMAFQIVVDGFYGCERQAVFSFIDNYVLPLIDNFSLDLTRYPDSKKVTESLIHTIYSLRSKHAPLAEFTMSLCVTYQKDEQLFCAGFGIGDTGIAIKRNEGTIEQLVCHTEVDGFKDAFDNYSSANIDLVIERNSVFNTKVMPGDELVGYTYVPPMLEMTEKEFEVETVDGKKINKRIVRHLNLDPGNFDDKDPLFSQLLQVVKSKQKQLVEQAKETGQIQRFGDDFTVGRLVIPDQLLINQLRIHALSIGVSDGLLSYIKNENENKGFLGIYGFFTGADKNIEKATLYKNLIAKYQNNHFISLIILSALVSDSKTPLMTQYLVGYLDFPSKALLANKITELLLKELENPDMREILGSRLATDVIEELETKIIRYIHNPAGSDIHSTLNLWTADKIKAATNSSLTI 507 Q60819 Soluble interleukin-15 receptor subunit alpha Il15ra 10090 Yes SL-0178 SL-0182 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}. UNIPROT Q60819 UNIPROT A2AP35 UNIPROT A2AP36 UNIPROT A2AP37 UNIPROT Q80Z90 UNIPROT Q80Z91 UNIPROT Q80Z92 UNIPROT Q8R5E4 PDB 2PSM Pfam PF00084 PROSITE PS50923 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}. GO:0009986 GO:0031410 GO:0005615 GO:0016021 GO:0031965 GO:0005886 GO:0042010 GO:0019901 GO:0035723 GO:0010977 GO:0032825 GO:0050766 GO:0007259 MASPQLRGYGVQAIPVLLLLLLLLLLPLRVTPGTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVINKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTSAGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTKVAISTSVLLVGAGVVMAFLAWYIKSRQPSQPCRVEVETMETVPMTVRASSKEDEDTGA 263 Q61382 TNF receptor-associated factor 4 Traf4 10090 Yes SL-0198 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}. UNIPROT Q61382 UNIPROT Q8BHD9 Pfam PF00097 Pfam PF02176 PROSITE PS50144 PROSITE PS00518 PROSITE PS50089 PROSITE PS50145 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}. GO:0005923 GO:0005737 GO:0005856 GO:0005634 GO:0048471 GO:0005886 GO:0042802 GO:0019901 GO:0031996 GO:0005164 GO:0031625 GO:0050699 GO:0008270 GO:0007250 GO:0006915 GO:0046330 GO:0045860 GO:0070534 GO:0042981 GO:0043122 GO:0007585 GO:0030323 GO:0033209 MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLAIRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVCPQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLKDSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRRLQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAKPQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS 470 Q62825 Exocyst complex component 3 Exoc3 10116 Yes SL-0198 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}. UNIPROT Q62825 UNIPROT Q4QQU2 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. P07949 EBI-2480756,EBI-15885246 GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0042734 GO:0000149 GO:0051601 GO:0006887 GO:0015031 MCKDSACFSTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFAVLDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLVIAKNLLVQCFPPHYDIFKNLLSMYHQALSIRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVNALEPLLSPNVVSELLDTYMSTLTSNIIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQLYKEEHLRNRQHPHCYVQYMVAIINNCQTFKESIISLKRKYLKPETEESLCQSQPSMDGILDAIAKEGCSSLLEEVFLDLEQHLNELMTKKWMLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKMVREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQTIMETLEQGPMQASPNYVPIFQEIVVPSLNVAKLLK 755 Q62910 Synaptojanin-1 Synj1 10116 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}. UNIPROT Q62910 UNIPROT O89092 UNIPROT Q62911 UNIPROT Q810Z8 Pfam PF08952 Pfam PF03372 Pfam PF02383 PROSITE PS50102 PROSITE PS50275 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}. Q5S007 EBI-5323863,EBI-1149123 GO:0005623 GO:0030132 GO:0005737 GO:0098978 GO:0030117 GO:0043005 GO:0098688 GO:0048471 GO:0098794 GO:0098793 GO:0032991 GO:0098685 GO:0097060 GO:0043195 GO:0012506 GO:1990175 GO:0052658 GO:0034595 GO:0004438 GO:0004439 GO:0043812 GO:0008022 GO:0044877 GO:0003723 GO:0017124 GO:0007420 GO:0046855 GO:0007612 GO:0006836 GO:0046856 GO:0046488 GO:1904980 GO:0014015 GO:0048260 GO:0098884 GO:0099149 GO:0034097 GO:0032526 GO:0048488 GO:0016082 GO:0048489 GO:0016191 MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYAKVLDAYGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHASDIHMVSFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFDGSAVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKNMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKSSAQENTFFDDALIDELLQQFAHFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITITLKSPDWIKTLEEEMSLEKISVTLPSSTSSTLLGEDAEVSADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTAPEYSAPSLPIRPSRAPSRTPGPLSSQGAPVDTQPAAQKESSQTIEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARKEFGGVGAPPSPGVTRREMEAPKSPGTARKDNIGRNQPSPQAGLAGPGPSGYGAARPTIPARAGVISAPQSQARVSAGRLTPESQSKPLETSKGPAVLPEPLKPQAAFPPQPSLPTPAQKLQDPLVPIAAPMPPSIPQSNLETPPLPPPRSRSSQSLPSDSSPQLQQEQPTGQQVKINGACGVKQEPTLKSDPFEDLSLSVLAVSKAQPSAQISPVLTPDPKMLIQLPSASQSKVNSLSSVSCMLTMPPVPEQSKSQESVGSSANPFPSLPTRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPVSNSPFPPLMPLSHDMSKPSSSLDGFEDNFDLQSQSTVKTSNPKGWVTFDEDEDFPTKGKSRSVYPDSLGNTAASFDDDWSKGTNVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLSSKASPTLDFTER 1574 Q63190 Emerin Emd 10116 Yes SL-0178 SL-0179 SL-0182 SL-0183 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}. UNIPROT Q63190 Pfam PF03020 PROSITE PS50954 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}. GO:0005737 GO:0016021 GO:0005874 GO:0005635 GO:0005637 GO:0031965 GO:0005640 GO:0005654 GO:0005634 GO:0005819 GO:0003779 GO:0048487 GO:0071363 GO:0090090 GO:0048147 GO:0031468 GO:0046827 GO:0060828 GO:0035914 MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDSAYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATFLLFVYYSIQAQEGNPFWMDP 260 Q63481 Ras-related protein Rab-7L1 Rab29 10116 Yes SL-0198 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}. UNIPROT Q63481 Pfam PF00071 PROSITE PS51419 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}. Q5S007 EBI-6513837,EBI-5323863 GO:0005801 GO:0005737 GO:0005856 GO:0005829 GO:0005769 GO:0012505 GO:0005794 GO:0097708 GO:0042470 GO:0005739 GO:0048471 GO:0005886 GO:0055037 GO:0020003 GO:0005802 GO:0031982 GO:0070840 GO:0019003 GO:0005525 GO:0003924 GO:0019894 GO:0017137 GO:0060271 GO:0007030 GO:0006886 GO:0032438 GO:0007005 GO:0010977 GO:0090316 GO:0001921 GO:0050862 GO:1903441 GO:0072657 GO:0032482 GO:1901214 GO:1905279 GO:0009617 GO:0042147 GO:0007416 GO:0042110 GO:1901998 GO:0039694 MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDSEMVRLQLWDIAGQERFTSMTRLYYRDASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPSGEPVPCLLLANKSDLSPWAVSRDQIDRFSKENGFTGWTETSVKENKNINEAMRVLVEKMMNNSREDIMSSSTQGNYINLQTKPSPGWTCC 204 Q63850 Nuclear pore glycoprotein p62 Nup62 10090 Yes SL-0178 SL-0185 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}. UNIPROT Q63850 UNIPROT Q99JN7 Pfam PF05064 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}. GO:0005642 GO:0005623 GO:0005813 GO:0005737 GO:0090543 GO:0072686 GO:0005635 GO:0031965 GO:0005643 GO:0044613 GO:0005654 GO:0032991 GO:1990904 GO:0000922 GO:0030544 GO:0051879 GO:0019894 GO:0005543 GO:0044877 GO:0051425 GO:0030159 GO:0042169 GO:0017056 GO:0046966 GO:0043130 GO:0007569 GO:0008219 GO:0016477 GO:0007166 GO:0098534 GO:0007098 GO:0000278 GO:0007100 GO:0007080 GO:0051028 GO:0043066 GO:0008285 GO:0042059 GO:0043407 GO:0043069 GO:0046580 GO:0046601 GO:0043123 GO:1903438 GO:0045840 GO:1904781 GO:0045893 GO:0006606 GO:0060236 GO:0042306 GO:0006405 GO:0007283 GO:0006351 MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLSLPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPASSTAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD 526 Q640M6 Glycerophosphodiester phosphodiesterase domain-containing protein 5 Gdpd5 10090 Yes SL-0198 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}. UNIPROT Q640M6 UNIPROT Q8R0T5 UNIPROT Q8R3N5 Pfam PF03009 PROSITE PS51704 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}. GO:0030424 GO:0005789 GO:0030426 GO:0016021 GO:0016020 GO:0043025 GO:0097038 GO:0047389 GO:0008889 GO:0004435 GO:0021895 GO:0006629 GO:0045746 GO:0031175 GO:0045787 GO:0045666 GO:0048505 GO:0021522 MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLVCTFSLTLTWLYFWWGVHNDYDEFNWYLYNRMGYWSDWSVPILVTSAAAFTYIAGLLVLALCHIAVGQQLNLHWIHKMGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHIGALVAITALSWIVAGQFARAERSSSQLTILCTFFAVVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDELSVCSDSSYDTYANANSTATPVGPRNAGSRAKTVTEQSGH 607 Q640Z6 Nuclear pore complex protein Nup153 nup153 8355 No SL-0178 SL-0182 SL-0185 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. UNIPROT Q640Z6 Pfam PF08604 Pfam PF00641 PROSITE PS01358 PROSITE PS50199 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}. GO:0031965 GO:0005643 GO:0003677 GO:0046872 GO:0051028 GO:0051292 GO:0015031 MAAAGGGGPGGPGTGGKIRSRRYHLSSGRTPYSKSRQQQQGIISRVTDTVKSIVPGWLQKYFNKQEEEHDRVHSASEVIVNDTEARENNAEHHIYVVDDDDDEEGNSPTDGRVTPEPIINVDEEVPSTSQSAINNTDALTRPSLHRASLNFNIFDSPALNCQPSTSSAFPIGTSGFSLIKEIKDSTSQHDDDNISTTSGFSSRASDKDLAVSKNVSVPPLWSPEVDRSQSLSHNSSMTSKKPTFNLSAFGSLSPSLGNASILNRQLGDSPFYPGKTTYQGAAAVRSSRVRATPYQAPLRRQVKAKPAAHSQQCGVTSSAARRILQSLEKMSSPLADAKRIPSNSSLSHTPEKNVMDIPENPSKRKKVESPFPPVQRLVTPKSISVSANRSLYIKPSLTPSAVSNTNSRRIQPDKHNESRKNNLQTTSQSHSFSYPKFSTPASNGLSSGTGGGKMMREKGSHYSTKPANEELDGPVLPEIPLPLSTAALPSFQFSTLSGSATSPISVTKPANSTTCRLTSSSPSFTFSSPIVKSTESNAQSPGSSVDFTFSVPAAKASSATSDESKVSAVSRAAKTHAAVSSAKNTDDEQLGFCKPAKTLKEGSVLDMLRSPGFSSSPSLLTSASSLNRSTPTLSKTVGNTFSPANVSLGVGSKQAFGLWQCSACFHENMSSDSNCISCSALKPRPTETSKKLPASPPSSNTKSTVPLSSTPGLGDIFKKPAGMWDCDTCLVQNKAEVTKCVACETPKPGTGMKATLLIPSTTKSTNPATNTLAFASCSASIPNEEMFKKPMGSWECTVCHMQNKTEDNTCVGCKAEKPGTVKSVPTAAPSGLLGLLDQFKKPTGSWDCDVCLIQNKPEANKCIACESAKPGTKAELKGTFDTVKNSVSVAPLSSGQLGLLDQFKKSAGSWDCDVCLVENKPEATKCVACETSKPGTKAELKGFGTSTFSSGTAAPTFKFGVQSSDSTAELKSGASTSGFAKSIGNFKFGLASASTTTEETGKKSFTFGSSTTNEVSAGFKFGIAGSAQTKPDTLSQSTTSGFTFGSVSNTVSLAPTATSSGSTGLQVAAVIADSNLATTATLKSAEEKKAEAPTITPFSFGKTDQNKETASTSFVFGKKDEKTDSAPTGSSFAFGLKKDGEESKQFLFGKPEPTKVDGSAASAGFAFGVTNPTEKKDIEQPGKSVFAFGAQTSITDAGASKQPFSFLTNVSSTAASSSTCGVSSSVFGSVTQSSTPATPSNVFGSAISANAPAPSSGVFGNLTPSNAPAASSTLFGNVAPSSTPSGSSGLFGTAAASSTPATSTSLFGSAAKLSAPASSGGVFNSAAPAAPASTASSVFGSVASSTNTSANSANIFGSSGGAATAPGAFVFGQPASTASTVFGNSSESKSTFVFSGQENKPVTSASTSVTPFLFGAVSASTTPAAPGFNFGRTITSNTTGTSSSPFIFGAGASGSASSSITAQANPVPAFGQSSNPSTAPAFGSSTSVPVFPAGNSQQVPAFGSSSAQPPVFGQQATQPSFGSPAAPSAGSGFPFGNNANFNFNSTNSSGGVFTFNANSGSTTQPPPPGYMFNAAAPGFNMGTNGRTTPASTISTRKIKTARRRK 1605 Q641G3 Cell division cycle and apoptosis regulator protein 1 ccar1 8355 No SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IX12}. UNIPROT Q641G3 Pfam PF14443 Pfam PF14444 Pfam PF02037 PROSITE PS50800 Transcriptional coactivator for nuclear receptors which may play an important role in regulating cell growth and apoptosis. {ECO:0000250|UniProtKB:Q8IX12}. Q6P5F9 EBI-2550236,EBI-11609103 GO:0048471 GO:0007049 GO:0006355 GO:0006417 MAQFGGQKNPPPWATQFTATAVSQPGPLAVQQSSLLGASPTIYTQQSALAAAGLASPSPANYQLSQTAALQQQAAAAAAAAAAALQQQYTQPQQTIYSVQQQLQPPPQAILTQPAVALPTSLALSTPQQAAQITVSYPTPRSNQQQTQPQKQRVFTGVVTKLHETFGFVDEDVFFQLTAVKGKSPQAGDRVLVEATYNPNMPFKWNAQRIQTLPNQNPASAQSLIKNPAAVMQPVAQPTAYAVQTQPPPQAQTLLQAQISAATLTPLLQTQTSPLLQQPQQKAGLLQTPVRIVSQPQPVRRIEPPSRFSVRNDRGDSILSRKDDRNRERERERRRSRDRSPQRKRSRERSPRRERERSPRRPRRVVPRYTVQISKFCLDCPGCDTMELRRRYQNLYIPSDFFDAQFTWVDAFPISRPFQLGNYSNFYIMHKEVDPLEKNTAIVDPPDADHTYSAKVMLLASPSLEELYHKSCALAEDPIEVREGFQHPARLIKFLVGMKGKDEAMAIGGHWSPSLDGPNPDKDPSVLIRTAVRCCKALTGIELSLCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWENLCHGYKQQLVDKLQGDRKEADGEQEEEDKEDGDAKEISTPTHWSKLDPKIMKVNDLRKELESRTLSSKGLKSQLIARLTKQLRIEEQKEEQKELEKCEKEEEEEEERKSEDDKEEEERKRQEELERQRREKRYMLPDEPAIIVHPNWSAKNGKFDCSIMSLSVLLDYRIEDNKEHSFEVSLFAELFNEMLQRDFGVRIYRELLALPEKEEKKDKEKKCKKEDKRERKEDKDDDDEPKPKRRKSSDDKIKLEEKEERKRDDRRKEDYREEDDPDYENQDDYEPIAAEEDDGDYDDREDDDDDSSSKDKREDKRDGNRYSKERQSKDKEKDKKQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLFTKILLKESLLYRKLTDTATEDGSHEETDPLHNDILGNCSLLPSKAVRTGLSTVEDKGGLIVYKGAMVDVGSLLQKLEKSEKTRTELEHRLQTLESKTEEDEKTISQLEASNRNLSEELKQTKDDVGHLKDSLKAAEDTRSLYEDQLTNTIKNLSAAMGEIQVVLNKNPSTTEDQKSKENGSS 1157 Q641M3 Transmembrane protein 18 tmem18 7955 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q641M3 Pfam PF14770 DE Reference Proteome: Yes; GO:0016021 GO:0031965 GO:0003677 MTASNTKNASAIPIDKFSNVRITSIWTFLQSVDWSEPWLMALLAFHVFCFAFTLLSCKYYRIQICHFLLMVAMVYSAEYLNELAAMNWRSFSKFQYFDSKGMFISLVYSVPLLLNTVIIVAVWVWRTFSTMTELKILQLKRKAARENHKKTQ 152 Q64GA5 Cytosolic phospholipase A2 gamma Pla2g4c 10090 Yes SL-0178 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}. UNIPROT Q64GA5 UNIPROT Q08EC7 UNIPROT Q3UWS1 UNIPROT Q7TN01 Pfam PF01735 PROSITE PS51210 Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. {ECO:0000250|UniProtKB:Q9UP65}. GO:0005938 GO:0005737 GO:0005635 GO:0005654 GO:0005819 GO:0005509 GO:0047498 GO:0005544 GO:0047499 GO:0004623 GO:0102567 GO:0102568 GO:0046475 MELSSGVCPATRLQEAEKAAVHKRSPKVLEALRKLNIQADQAPVIAVLGSGGGLRAHIACLGVLSELKELGLLDAVTYLAGVSGSTWALSSLYTKNGNMEGIEEELKHRYEKNEWDFHESLEKAIQASKRENYSLTDFWAYLIVSRQIRELQDSNLSSLKKQVEEGVLPYPIFAAIDEDLLADWRERKTQNSWFEFTPHHAGYPALGAYVPITEFGSRFENGKLVKSEPERDLTFLRGLWGSAFADIKEIKNYILNYFRNPFGKLKFIEGPVTYSEAPRMNVDAMLLDLVMAYFTDMNDPSIKDKLCALQQALGTETDEFGIEMAEIIQNWNETSAEKKEQFLDHLLDRFKKTQEDTTTYSLMNWNTGLVWDRCVFVNETRKCVSKWQWGTVYNFLYKHGKIADETMCSRELLHLVDAGFAINTPYPLVLPPVRETHLILSFDFSAGDPLETIRATADYCQRHEIPFPEVSEDQLKEWAKAPASCYVLRGETGPVVMHFTLFNKDNCGDDIETWRKKYGTVKLSDSYTPDLVRDLLRVSKENVKKNKINILSEMRKVAGNPGNIPRVNKEACLGDRVKDPQGSQTVEFKKSHNISKD 597 Q66669 Nuclear egress protein 2 NEC2 82831 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q66669 Pfam PF04541 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}. GO:0044201 GO:0016021 MNGSKRLVAQLCQVVRSFICQPGTAVDLWQCAAGPHVFAKGSTQPICIVKLVHGQIYNLEFVYKYWCHILQSEKFPYSPVFIISNNGLAITLKCFLCEPMDLHSQFGRCLSMDTDVYLPKNTSVVLSQDDFTKFKTNLVFSKDLNVFNSMVVCRTYLTDFRQALQFLVVKAKNPKRVTAILGTIAQTLGLTPDTRSGEGGKNSERGEDDMVRRPIRAHRAGDSGGSPGTLPAEPQGAPTPPGGGLGLSSGLGLVRRWTRCAFQRYFTVLAVGAVAAATFLAGAKLTG 287 Q66672 Nuclear egress protein 1 NEC1 82831 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q66672 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MDRERPRKTREPASPGSVLSKRSKLSRKSLALRSLNKFHPYKAPSSVRSLKKAHTLVSNGDFFNGISLNCEFGKDFLREMDTPICTSKVICLPLDVHEIAPGRCLVLSPLGHACNMGFYCEKCTQSGQNSYSQFQGRGGNAKMAAQNSKDDLHSVTLTFYNQVSKVVQNKNFYLSLLSHSLTTIKKSFVQPSLLYSYTVLRALCDDVFPIFKDTENGLCMFALFKTDDLHVSETCLRHLVDNLIHYRVTLDCVKHTYMLKFSPIRAEANGMTIQEVEICEAITGLDFTDEIKQEIISGQELVSEL 305 Q66GR8 Protein NETWORKED 3A NET3A 3702 Yes SL-0178 SL-0182 Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22840520}. Nucleus membrane {ECO:0000269|PubMed:22840520}. UNIPROT Q66GR8 UNIPROT Q67ZU6 UNIPROT Q9LR76 Pfam PF07765 PROSITE PS51774 Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex. {ECO:0000305|PubMed:22840520}. GO:0005856 GO:0031965 GO:0005886 GO:0005774 GO:0051015 MVMDSSKWWWIGNHNTTNFSPWLHSTLSELDEKTKEMLRVIDEDADSFAARAEMYYKKRPELIAMVEEFYRSHRSLAERYDLLRPSSVHKHGSDSESHEKSSTCDESSWSEACETHEEYAESEIDNGESKWVDESEIDGIVEEIEPSEVVYSEGNGNSEMMKIEIERLREENKVYSEMVREKDEEKREAIRQMSVAIQMLKEENSELKKRVTNTVVARRNKEGGDSQRKQQMWKPFEFKKIKLEGLWGKGFGNWALPNTDSTSKELMTL 269 Q66H19 Serum response factor-binding protein 1 Srfbp1 10116 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}. UNIPROT Q66H19 Pfam PF09073 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}. GO:0030686 GO:0005634 GO:0048471 GO:0030490 MAADPSPPSAMAQPRPLNLNNEVVKMRKEVKRIRVLVIRKLVRSVSRLKSKKGSEDALLKNQRRAQRLLQEIHAMKELKPDVITKSALNDDINFEKTCKKPDSTATERAIARLAVHPLLKRKVDALKAAIQAFKDARQNAPEAESSKSASKESQCEDIPRSQAEASESQHPERTVVGEQKGKDKDPTTAKKAGSGSKEKLAKGKQGPKAVATPHSPGKPSEKGAGINSERQGAPTPGNHSQGKASTRTTEDSVCEPDDNSISKEEVSEEEKEYFDDSTEERFYKQSSASEDSDSGDDFFIGKVRRTRKKECAVPSSAKEQKPLPKVSSKTNTLETHWDIRNDKHKLIPEARKLESVFFHSLSGPKSSRRDPREQAPKNKAPDIPENEPPIQNKFTKSARRGFESAKQPSYAPLHPSWEASRRRKEQQSKIAVFQGKKITFDD 442 Q66IJ0 Nucleoporin NUP35 nup35 8364 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. UNIPROT Q66IJ0 Pfam PF05172 PROSITE PS51472 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}. GO:0031965 GO:0044613 GO:0044615 GO:0005543 GO:0003697 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0006355 MAAFSMEPMGAEPMALGSPTSPKPSAGAQFLPGFLLGDIPTPVTPQQRPSIGVMEMRSPLLSGGSPPQPVVPTHKDKSGAPPVRSIYDDIASPGLGSTPLNPRKTASFSVLHTPLSGVIPSSPECKNISGSRKRPASSVFSPATIGHSRKTTLSPAQMDPFYTQGDALTSDDQLDDTWVTVFGFPQASASYILLQFAQYGNIIKHVMSNNGNWMHIQYQSKLQARKALSKDGRIFGESIMIGVKPCIDKSVMEATEKVSTPTVSSVFTPPVKNIGTPTQSVGTPRAASMRPLAATYKTPASADYQVVADKQAPRKDESIVSKAMEYMFGW 330 Q66KV4 Barrier-to-autointegration factor B banf1 8355 No SL-0178 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}. UNIPROT Q66KV4 Pfam PF02961 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}. GO:0005694 GO:0005635 GO:0003677 MSSTSQKHRDFVAEPMGEKSVQCLAGIGDTLGRRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDACSANAKQSRDCYGCLKEWCDAFL 90 Q66T02 Pleckstrin homology domain-containing family G member 5 Plekhg5 10090 Yes SL-0198 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}. UNIPROT Q66T02 UNIPROT A2A8B6 UNIPROT A2A8B7 UNIPROT Q66T00 UNIPROT Q6P3B1 UNIPROT Q6ZQ62 UNIPROT Q8R571 Pfam PF00621 PROSITE PS50010 PROSITE PS50003 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}. P35294 EBI-6552478,EBI-9079953 GO:0005911 GO:0005737 GO:0030139 GO:0030027 GO:0048471 GO:0005886 GO:0098793 GO:0005089 GO:0035767 GO:0043542 GO:0099575 MGTGPGVSGRRAAARPSSELPSPDSQLLWVGGHAHSSDSQVCHHADCQQLHHRGPLNLCETCDSKFHSTLHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAADLEEEEEGCTDGKGDRKSAGLKISKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAKPGDEGKVEQGVKDSKSLSLPALRPSGAGPPVSERVDPQSRRESSLDILAPGRRRKNMSEFLGEAGIPGHEPPAPSSCSLPVGSSGGTSSGINESWKNRAASRFSGFFSSSPSTSAFSREVDKMEQLESKLHAYSLFGLPRMPRRLRFDHDSWEEEEEDDEEDEESSGLRLEDSWRELTDGHEKLTRRQCHQQEAVWELLHTEVSYIRKLRVITNLFLCCLLNLQESGLLCEVEAERLFSNIPEIAKLHRGLWGSVMVPVLEKARRTRALLQPSDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYVTWAEKHQQCQRLKLSDMLAKPHQRLTKYPLLLKSVLRKTDDPRTKEAIVTMISSVERFIHHVNTCMRQRQERQRLAGVVSRIDAYEVVEGSNDEVDKLLKEFLHLDLTAPMPGTSPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTKVIRPPLLVDKIVCRELRDPGSFLLIYLNEFHSAVGAYTFQASSQALCRSWVDTIYNAQNQLQQLRAQLSAQEHPGSQHLQSLEEEEDEQEEEGEESGTSAASSPTILRKSSNSLDSEHCTSDGSTETLAMVVVEPGATLSSPEFEGGPVSSQSDESSLSNTASSVTPTSELLPLGPVDGRSCSMDSAYGTLSPTSLQDFVAPHPVVEPAPVPQTPSPQPSPRLRRRTPVQLLPRPPRLLKSKSEASLLQLLSGTPAARGVPPAPSRSLSELCLISVAPGVRTQRPLQEGGPGWNGPGMCDPCHGPQLSESENRPSHMTGGPADSARRRCREMPSGTMSRVQSEPPSGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV 1073 Q684P5 Rap1 GTPase-activating protein 2 RAP1GAP2 9606 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:15632203}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15632203}. UNIPROT Q684P5 UNIPROT B2RTY5 UNIPROT Q684P4 UNIPROT Q6AI00 UNIPROT Q6ZVF0 UNIPROT Q9UPW2 Pfam PF02145 PROSITE PS50085 OMIM 618714 DisGeNET 23108 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}. P62258 EBI-356498,EBI-3452992 Q9H4A3 EBI-3452992,EBI-457907 Q6FHY5 EBI-16439278,EBI-3452992 Q6P5F9 EBI-2550236,EBI-3452992 GO:0005813 GO:0005829 GO:0043005 GO:0031965 GO:0048471 GO:0005886 GO:0005096 GO:0010977 GO:0008361 GO:0051056 MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQKNKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRHFLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVLYPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVESVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYKVSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGPEEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPIKRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSSTSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDKLSHASSGAGH 730 Q68749 RNA-directed RNA polymerase POLG 356413 No SL-0382 [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. UNIPROT Q68749 Pfam PF07652 Pfam PF01543 Pfam PF01542 Pfam PF01539 Pfam PF01560 Pfam PF01538 Pfam PF01006 Pfam PF01001 Pfam PF01506 Pfam PF08300 Pfam PF08301 Pfam PF12941 Pfam PF02907 Pfam PF00998 PROSITE PS51693 PROSITE PS51192 PROSITE PS51194 PROSITE PS51822 PROSITE PS50507 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}. GO:0005576 GO:0044167 GO:0044186 GO:0044191 GO:0042025 GO:0044220 GO:0020002 GO:0016021 GO:0044385 GO:0019031 GO:0019013 GO:0055036 GO:0005524 GO:0004197 GO:0005216 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0017124 GO:0005198 GO:0008270 GO:0075512 GO:0039654 GO:0039520 GO:0039645 GO:0039707 GO:0051259 GO:0039545 GO:0039563 GO:0039547 GO:0039502 GO:0019087 GO:0039694 GO:0019062 MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRAARKTSERSQPRGRRQPIPKDRRSTGKSWGRPGYPWPLYRNEGLGWAGWLLSPRGSRPSWGPSDPRHKSRNLGKVIDTLTCGFADLMGYIPVVGAPVGGVARALAHGVRVLEDGINYATGNLPGCSFSIFLLALLSCISVPVSAVEVRNTSSSYMATNDCSNSSIVWQLEGAVLHTPGCVPCEKTGNKSRCWVPVTPNIAINQPGALTKGLRAHIDVIVMSATLCSALYVGDVCGALMIAAQVVVVSPQHHHFVQECNCSIYPGKITGHRMAWDMMMNWSPTTTMLLAYLVRIPEVVLDIITGGHWGVMFGLAYFSMQGAWAKVVVILLLTAGVEASTYTTGAVVGRSTHLFTSMFSLGSQQRVQLIHTNGSWHINRTALNCNDSLETGFLAALFYTSSFNSSGCPERLAACRSIESFRIGWGSLEYEESVTNDADMRPYCWHYPPRPCGIVPARTVCGPVYCFTPSPVVVGTTDRAGAPTYNWGENETDVFLLNSTRPPKGAWFGCTWMNGTGFTKTCGAPPCRIRKDFNASEDLLCPTDCFRKHPGATYIKCGAGPWLTPRCLVDYPYRLWHYPCTVNYTIYKVRMFVGGIEHRLQAACNFTRGDRCNLEDRDRSQLSPLLHSTTEWAILPCSYTDLPALSTGLLHLHQNIVDVQYLYGLSPAITKYVVKWEWVVLLFLLLADARVCACLWMLLLLGQAEAALEKLVILHAASAASSNGLLYFILFFVAAWCIKGRAVPMVTYTLLGCWSFVLLLMALPHQAYALDAAEQGQIGMALLIAITAFTITPAYKILLSRCLWWTCYMLVLAEALIQDWIPPLQARGGRDGVIWAMTMFYPGVVFDITKWLLAILGPGYLFRAAVMRTPYFVRANALLRMCALVKQLAGGKYVQVALITLGKWTGTYIYDHLSPMSDWAADGLRDLAVAVEPIVFSPMERKVIVWGAETTACGDIIHGLPVSARLGQEVLLGPADGYTSKGWRLLAPITAYAQQTRGLLSAIVVSMTGRDKTDQAGEIQVLSTVTQSFLGTSISGVLWTVFHGAGNKTLAGSRGPVTQMYSSAEGDLVGWPSPPGTRSLEPCTCGAVDLYLVTRNADVIPARRRGDRRGALLSPRPLSSLKGSSGGPVLCPRGHAVGIFRAAVCSRGVAKSIDFIPVESLDVVTRSPNFTDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAYGINPNIRTGVRTVTTGDAITYSTYGKFLADGGCSGGAYDVIICDECHSVDSTTILGIGTVLDQAETAGVRLTVLATATPPGSVTTPHPNIEEVALGHEGEIPFYGKAIPLSAIKGGRHLIFCHSKKKCDELAVALRGMGLNAVAYYRGLDVSIIPTQGDVVVVATDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFTITTQTVPQDSVSRSQRRGRTGRGRLGIYRYVSSGERASGMFDTVVLCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGEGFPYLVAYQATVCARAKAPPPSWDVMWKCLIRLKPTLVGPTPLLYRLGSVTNEVTLTHPVTKYIATCMQADLEIMTSTWVLAGGVLAAVAAYCLATGCVSIIGRIHVNQKTIIAPDKEVLYEAFDEMEECASRTALIEEGHRIAEMLKSKIQGLMQQASKQAQGVQPAVQATWPKLEQFWAKHMWNFISGIQYLAGLSTLPGNPAVASMMSFSAALTSPLSTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVGAAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPSVEDVVNLLPAILSPGALVVGVICAAILRRHVGQGEGAVQWMNRLIAFASRGNHVAPTHYVAESDASQRVTQLLGSLTITSLLRRLHQWITEDCPVPCSGSWLRDVWDWVCSILIDFKNWLSAKLFPRLPGIPFISCQKGYRGTWAGTGIMTTRCPCGANITGNVRLGTMRISGPKTCLNTWQGTFPINCYTEGSCVPKPAPNFKTAIWRVAASEYAEVTQHDSHAYVTGLTADNLKVPCQLPCPEFFSWVDGVQIHRFAPTPKAFMRDEVSFSVGLNSYVVGSQLPCEPEPDTEVLASMLTDPSHITAEAAARRLARGSPPSAASSSASQLSAPSLRATCTTHAKCPDIDMVDANLFCWCTMGGNMTRIESESKVLMVDSFDPVVDKEDEREPSIPSEYLLPKSRFPPALPPWARPDYNPPLLETWKRPDYQPPVVAGCALPPPGTTPVPPPRRRRAVVLDQSNVGEALKELAIKSFGCPPPSGDPGHSTGGGTTGETSKSPPDEPDDSEAGSVSSMPPLEGEPGDPDLEPEQVEHPAPPQEGGAAPGSDSGSWSTCSDVDDSVVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYHNKVYCTTSRSASQRAKKVTFDRVQLLDSHYESVLKDVKQAATKVSAKLLSIEEACALTPPHSARSKYGFGAKEVRSLSRRAVDHIKSVWEDLLEDHCSPIDTTIMAKNEVFCVDPTKGGKKPARLIVYPDLGVRVCEKMALYDITQKLPVAVMGQSYGFQYSPAQRVDFLLQAWKEKKTPMGFSYDTRCFDSTVTERDIRTEESIYLSCSLPEEARTAIHSLTERLYVGGPMTNSKGQSCGYRRCRASGVLTTSMGNTLTCYVKAKAACNAAGIVAPTMLVCGDDLVVISESQGVEEDERNLRVFTEAMTRYSAPPGDPPKAEYDLELITSCSSNVSVALDPRGRRRYYLTRDPTTPLARAAWETARHSPVNSWLGNIIQYAPTVWVRMVLMTHFFSVLMAQDTLDQDLNFEMYGAVYSVSPLDLPAIIERLHGLEAFSLHSYSPHELTRVAAALRKLGAPPLRAWKSRARAVRASLISRGGSAATCGRYLFNWAVRTKLKLTPLPAARLLDLSSWFTVSAGGGDIYHSVSRARPRLLLLGLLLLCVGVGIFLLPAR 3037 Q68772 Non-structural protein 12 rep 38143 Yes SL-0382 [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}. UNIPROT Q68772 UNIPROT P89132 UNIPROT Q87077 Pfam PF16749 Pfam PF05411 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF01443 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 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}. GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0008270 GO:0006351 GO:0019082 GO:0039694 MFCECPRSNLVVMCSGAFCCVLCGHRRRPRPASESDRAKYGPIVQYVEARVAHVYSGLEGRYCALEMIPITYGNKFPYCKPLPVSFVIKTLAGVQGDLTRLEETPLPGGYGVIPCWGPHLAAVGYLSPAHVGRDWFEGATHAIVHIGSYGGHERPTTIPFNTTGGDVYQLGTCTIVETIDHVEWHAGVKPGTAICPLDRIDFAQKVITAFPEGFLANKAWLGDKRGTLKVEADPETAALSFEHGRCWLKLFPDPACELTTASTFGYQLNCGVQGKYIARRLQTNGLKLVQNQEGKFIAYTFHRGSWLGHIGHADESVPPDCQIIARFDVLPYNEWSPLPLLKLPGKTYFGGNASSVSWPEWKYDEQLLYADSLTAGFCWLQLFPPLSRKSEAQRAILAQQVNNYGVTGTYLEYRLRQYGIVLAECDYGEHYIYAAASDSSIRHISPVPIHDRHHVFVTRLTARFGAFDEGFDLGFGTRYGRRRGGGKKSGQSSGVRAPGRTTPDLAGDWGKAVDDQEKTASKVTTDKAMSTSEPAVVQVGCETKPVADAAAVPASVNSTGCALLPVQADPCCTAGVAAKESEPKAVAAPSIPITFGAPAGETLPVAASPLVVKKDKRCISVKLTAKKALPKETFIPPPDGGCGVHAFAAIQYHINTGHWPEQKPVVNWAYEAWTTNEDIGHMICSTETPAALEPCLHARYVVRLDSDHWVVDHYPNRPMCFVEACAHGWCSSLLSEPTGEEGEHLVDCSALYDCLGKFRNGTEFADTVLGLSKTAHCCNKRVPTPRKQAIMSLLNRPNCVPCIAPPSQVRTVDPSQPAAPLPPVPRPRKRKAAAQQVSKVPSEQDPSLAHDPPEKPDSVRPPKLGYLDRAWNNMLARTHKLHNLQQRVFGLYPQLLSMLLPSGARPSTPRLLGCYFSMAVAMFFLFLGSPLFILCAVLAGVIAPSARYPKILCCCLVVVYICTLFADAISSVCDNDDADCRAFLSDLGDRYSTNQPVYITPGPATFFLAVSRNFFVVSVALFPLHLLLLMVDVLLVIGVLCMDGYCFRCFSRCVRKAPEEVSLLTIPQSRVSRRFLLDICDFYSAPPVDIIRLATGLNGCFRGDYSPIGSSTSVITADKIDVKKVSCRTVCSFPSCPSEAVKVLHVLSVRGQMCAHNEQKVEKVDALPCKNPLFPYDLSSKKIVPVDSGTYEILSSIGCDMSHLVIGDGDFFKVMGVPRPSPFTVMRLRACRVVGGGRIFRTALAAAWVLFFVCAGYWVQMSTPCGIGTNDPFCKSSFGVPTYVNQGVCHGQYCASSKGVSRATSILTVRNPAVAPYIVLAACLVYLASVYVPGIIEVSLLVLNALLPAGPAISALRTLVMIIAAPHLSMKYIAFFCCTTAFVDFTSVVVVLTALLVGWILARYTGIGGFVTPYDIHDVVKSQRDGVAVANAPPNTYLGAVRRAALTGKPAFFVANNTGIVLEGLLREKTRASNSVSVYGVTCGSGGLFSDGNNTVCLTATHVCGNNKAVVDYQGTRYEAVFTTKGDYASAVVPIPGAFPPLKFAPQSYTGRAYWYANTGVETGFVGTTGCLVFSGPGDSGSPIITPDGLIVGVHTGSDSKGSGAYTTPNGLTVSGPLSLKEMGAHYEGPIVDVPTRLPRNVHNDTKSVPQPLARLLESSINLEGGLGTIQLIIVAVVLWKYAVDPLSIPFVVAFFLLNEILPKCLIRCFYNYSLFCLAAFSPLASRIFFIRLLTAALNRNPTALICHACFAGIAVLNDFIILGDIRLALRFTSFYVVGVNHDAIAIAVIGALVCVAACCLELFGLPQMASVIGCHGSFDPTFLSRYVHEGIRQGVSSGFGTESLSTALACALSEDELNFLAQAVDHKAIVSAIHVHKTLQDYILSKNAKILRASLASVHANHNASKALASLDKFLQGTSTQLKPGDPVILLGSTSAELVSVFSGDSEYIAEPIRSHPVAGTICTLCVVQAKCEGGLVTQVNGKFSPAKYLAVAGKVLADHPDYKLENDGRFPRTREDRVKDSVQVDTVDIGSHTFKKMWNKTTGDVWYDIIMPESAANPLAVHDLDSAVAAIGMSKEIPEKDMNRLRAIISKLQGLVSSEALNLLTAAGCTSADRSGLVITLDYAKIITHHARTRAFSSIDFKVVSPDEAMRTARLSPSPQPIIASFSDDKFLLLRRHPPSLLDVLTKGLDATCREPLHSPGDQGIDGYLWDFEAPHSKEAIWLSNQIISACAARRGDAPGCYPYKLHPVRGDPYRVGNVLKNTRFGDVTYTAVSDSDSPWLKVASINSGGCPVVTDRVLGSTIPVGSEIYLPTLPESVLDYLDSRPDCPTYYTQHGCEAAALQDLKKFNLSTQGFILPEVLNIVRNYLLGTIGYRPAIYKPSTVPSNDSHAGINGLSFSTKTLQALPDIDELCEKAIAEVWQTVTPVTLKKQFCSKAKTRTILGTNAMASLALRALLSGVTQGFQLAGKNSPICLGKSKFDPCTFEVKGRCLETDLASCDRSTPAIVRHFATKLLFEMACAERALPLYVVNCCHDLIVTQTSAATKRGGLSSGDPVTSIANTIYSLVLYVQHMVLTLLENGHPLSLKFLSGKLNFQDLYKLQAFIVYSDDLILLNESDDLPNFERWVPHLELALGFKVDPKKTVITSNPGFLGCEYRHGWLVPQKQRVLAALAYHVNAKDVHTYYINATAILNDASALSAFEPDWFDDLVIGLADCARKDGYSFPGPAAFREFFSRVSGYQFEGKEVQVCSICCSTARTTSLCGMALCDFCAHRHYHPGCHVLSSFCKHVIGSNTCKMCSIPILKDRTKFAELLASDQYRSVCTVEVTVVDGYTDAAPGRYSYQKKQYMLRKERRGCPLDLPDGKYSMKLLPNSCSGICVPKAQENATLSNFVVGPPGSGKTTFISNLLDDDAVVYCPTHVSLIAYSKSLPAARFSVPRGQDPAEYGTPALSGPTLQLLSAGYVPGAKHYLDEACYANPFDVFKLLSKTPITAIGDPAQLTPVGFDTPLYVFELMKKNALHAIYRFGQNICNAIQPCYSTKLVSQRQGDTEVIFQTKFAPRGKVLTPYHRDRVGAAVTIDSSQGSTYDVVTLYLPTKGSLTLARGLVGITRARERLYVYDPHHQLAKYFNLQPSSTTIRPHAVVIDGKARVMLSDKCYAAPEDFPGMLCTARPATAADRKILEETCLKLDFLESGSLSPLPRVCYNLGFYYSPDITKLLPIPSELAKHWPVATNRNNPEWPNRLVVSATRLSPLSHPAVCAGYYVGDSLFVGTPNVTSYWLTKFLDGRAVPMEDSVYSTGRFEMDIRDYLDSAERDFAAKHPHAFIGDTKGTTVGGCHHITSQYLPHVLPADSVVKVGVSKPGVAHKALCTVTDIYLPMLGSYTSPPTQSKVYKVNVDHKACKLMVWRDQTMYFQEGFDYHTLVDALRFVRLSSDGVYRVAPELTPMIGNRRLDLGAKPLRPVDLAITPWDDPKCEFLVTHASPFDMSDEFLLVNAFDFIKEDLLGKSVTPVYFYKRLSEPLHFDQNLPPHVGAILSKAPRFISLAKVFNFCFTPTACHCKVSVKTATGDHMCKCSLSSDEFLSRFNPTVGTP 3595 Q69ZQ1 Myogenesis-regulating glycosidase Myorg 10090 Yes SL-0178 SL-0182 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}. UNIPROT Q69ZQ1 UNIPROT A2ANN6 UNIPROT B2RU42 Pfam PF01055 Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2 (PubMed:19706595). {ECO:0000269|PubMed:19706595}. GO:0005789 GO:0016021 GO:0031965 GO:0004553 GO:0005975 GO:0043568 GO:0051897 GO:0048741 MSQNLQETSQAYPRHRPGSHAGPKSLKVTPRATMYTFLPDNFSPAKPKPTKELRPLLCSAVLGLLLVLAAVVAWCYYSASLRKAERLRAELLDLNRGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSRAADGRPLHFFIQTVRPKDTVMCYRVRWEEAVPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVNDSVPFHLGWNSTERSMRLQARYHDTSYKPPAGRTAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPASEAFRDPIWSTWALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLSDPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMIGGNAVPERTAGRQDGPGPERELYVRWLEVAAFMPAMQFSIPPWQYDAEVVAIAHKFAALRASLVAPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEVAYFTWAS 716 Q6AX31 Nucleoporin NDC1 ndc1 8355 No SL-0178 SL-0182 SL-0185 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. UNIPROT Q6AX31 Pfam PF09531 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}. GO:0016021 GO:0031965 GO:0005643 GO:0051028 GO:0015031 MTMLGERLVLRWRVAASFAWSVILMPVCCALFIVLSRIQILHPIQWLTDSISDLTSSYTIFCLLLICAILGLQCTFLMEYYTVVPSIPCSRLALIGNLLLPHRILHSLAHVAMGVLASWCYAVLSKGKYQLLVVSCTLQSEDEADKPSHCLNESHLFQLLCGAFFGYSYSLQYFVHNMNYLSFPSIQQYKYLQFRRFLPLIIKQSVFQSLYFIRSYAILYFCLGNIPRTWIQTALNLHMDRQQPSLDTLRGFLNLSLFYQIWLSGTFLLATWYMVWILFRIYTTEARIFPVQTSFAEEAEKCLPFILNSNTLPLVKYLAMQDLVLLSQYSPSRRQEVFSLSQPGGHPHNWTSISKECLNLMSSLTSRLIAHQEAAANNGRMRVPSSPKQIRKSSSSSGTSLIEDSAEQTQNLSTIPRIGIPSLLKTASLKSSLDIGSPFATPGVKQMSESLDPNTPCHGSVQSPQVTRRGAKLWTSDSDVQKNGSEVSPVMHRPVCNGAKQGILHTWFQHKLVQIKNVLSKRGLIMYLFSKHPEASSQDVFADAQIHIWALEALSHLVAASFSEDRMGVVQTSLSSVLAILLTLQEAVEKHFKLPHASSKPARNPGSLLDSSCKTLRFSLRAALKTAIYRITTTFGEHLHAVPVSSEHKKKLQQFLDFKE 660 Q6AZL2 PCNA-associated factor pclaf 8364 Yes SL-0198 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}. UNIPROT Q6AZL2 Pfam PF15715 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}. GO:0005634 GO:0048471 GO:0003682 GO:0006974 GO:0007098 GO:0006260 GO:0051726 GO:0009411 GO:0019985 MVRTKADSAGSSASSGSYRKAVAARAPRKTFGSSSSGSNHVTSPTGKKSESKYAGGNPVCVRPTPTWQKGIGEFFGSPSTSQPEKENRIPSDDEEAGGSGAGKAPRKSRPLPPDPSEEAADSDDE 125 Q6AZZ1 E3 ubiquitin-protein ligase TRIM68 TRIM68 9606 Yes SL-0198 Cytoplasm, perinuclear region. Nucleus. Note=Colocalized with AR in nucleus. UNIPROT Q6AZZ1 UNIPROT A6NI19 UNIPROT A8K551 UNIPROT B3KPM5 UNIPROT B4DVK4 UNIPROT Q8WZ70 UNIPROT Q96LE5 UNIPROT Q96PF7 UNIPROT Q9H9C2 UNIPROT Q9NW18 Pfam PF13765 Pfam PF00622 Pfam PF00643 PROSITE PS50188 PROSITE PS50119 PROSITE PS00518 PROSITE PS50089 OMIM 613184 DisGeNET 55128 Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000269|PubMed:18451177}. Self EBI-2130449,EBI-2130449 Q5VVX9 EBI-2130449,EBI-2130181 O76076 EBI-2850068,EBI-2130449 P29279 EBI-2835375,EBI-2130449 Q8IV31 EBI-7238458,EBI-2130449 O95081 EBI-2847286,EBI-2130449 Q99954 EBI-12067698,EBI-2130449 Q9BWP8-4 EBI-21848899,EBI-2130449 P49765-2 EBI-21717775,EBI-2130449 P51888 EBI-2827057,EBI-2130449 Q9H7T9 EBI-2130449,EBI-10693257 Q9H239 EBI-2130449,EBI-20858485 Q96BZ8 EBI-726510,EBI-2130449 Q7RTY5 EBI-2130449,EBI-21891692 Q5TGY3 EBI-948813,EBI-2130449 P34130 EBI-2130449,EBI-3907456 O95561 EBI-10191951,EBI-2130449 O14494-2 EBI-2130449,EBI-21891618 Q9NQ48 EBI-2824799,EBI-2130449 P15884-3 EBI-13636688,EBI-2130449 Q9NRI5-2 EBI-11988027,EBI-2130449 Q96N21 EBI-11139477,EBI-2130449 P62487 EBI-347928,EBI-2130449 Q9BRJ7 EBI-2949792,EBI-2130449 Q04864-2 EBI-10829018,EBI-2130449 Q3SY46 EBI-10241252,EBI-2130449 Q0VD86 EBI-6509505,EBI-2130449 B2RXF5 EBI-12287587,EBI-2130449 Q52LG2 EBI-11953846,EBI-2130449 Q8TBB1 EBI-739832,EBI-2130449 B9A064 EBI-6677229,EBI-2130449 Q8N0V5 EBI-21492685,EBI-2130449 P01148 EBI-21753351,EBI-2130449 P13284 EBI-2868897,EBI-2130449 O75791 EBI-740418,EBI-2130449 C9JJ79 EBI-12117156,EBI-2130449 Q13227 EBI-713355,EBI-2130449 Q9Y215-2 EBI-21671462,EBI-2130449 GO:0005737 GO:0005829 GO:0005794 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0050681 GO:0035035 GO:0004842 GO:0008270 GO:0060333 GO:0051865 GO:0060765 MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVEKVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAWKLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQVLWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSEDRKRVHYGDTNQKLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCKQNVDRKEVVYLSPHYGFWVIRLRKGNEYRAGTDEYPILSLPVPPRRVGIFVDYEAHDISFYNVTDCGSHIFTFPRYPFPGRLLPYFSPCYSIGTNNTAPLAICSLDGED 485 Q6B9X6 Alpha-protein kinase vwkA vwkA 44689 Yes SL-0198 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). UNIPROT Q6B9X6 UNIPROT Q55FF0 Pfam PF02816 PROSITE PS51158 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}. GO:0031164 GO:0000331 GO:0005737 GO:0005829 GO:0048471 GO:0005524 GO:0005516 GO:0004672 GO:0004674 GO:0070177 GO:0033298 GO:0006971 GO:0000281 GO:0031038 GO:0018209 GO:0018107 GO:0006468 GO:0031156 GO:0031288 MESKYVLSTEKESKTKPSGRVNVSDMDSISNSLSKTSLGTRKVPTSLKTDASRSGLSSGGSKTHISDESALRMVYGSTPRDEKTTTTKDSITLAKEKEKKIEKRNEEIKLTFKAIRASECVDLLFIVDCTGSMDPYIEQIKSDIVKLQEALKLKHSFLDIEFGFIRYTDFDVASNRCSTFQFSRSTVEFVRFVSEIRAGGGADGPEDVFGGMDLIKSMKWRPNSTRVVIHIADAPCHGTEYHSMADSYPGGDPNGIKLDDLLTDIISLNINYYFGHINLKETGQMIDFFDKKTKEISRNKKSINSFDSKETSKMNERIFISIEESISVSRSVLTEQYLGHNIDGSTGKQRSEREFEINTNMDIDFGELPYIQMLQTKFKMPSDIVTCLSSSYEMKLNEITISIKIAPNPFSHGACRLAYLGIDEHGKKVVLKQSKYIGGRENSKKRYFESMECQTVAAKFALEFNKQLSLTSSEHQITFTVAKVLQMKHSEKPMYFGIETFINGEYQKYNSNCGWLKDDAMSEILQTFSHWTYQESKNKAIVVDIQGVKTSKGYLLTDPAIHSTDTLRFGSCNLGKPGIIKFFQSHKCNQHCKKLGLTIPSFTSSSSTSSSSRSTSSSSSISYSY 625 Q6BMD0 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 284592 Yes SL-0178 SL-0182 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}. UNIPROT Q6BMD0 Pfam PF08660 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}. GO:0005789 GO:0016021 GO:0031965 GO:0006488 MDFESQLCIKVVLLLLPFFIIGIRLLWVLPAVNSPAMGSEKEKGLSQIPSELRGSNIMIFLGSGGHTGEMMRILANVDLNNFNRTWVTSSGDSTSILKCKKYEDERLTSGQNKSDYLVLHRARTVGESIISSVFSTVRSLISTIKHLYELPQFPSILLLNGPGTSVPLAYIIFLLKFLGLCKTRIIYIESLARVKQLSVSGLLILPITDRFIVQWKQLAVKYKRAEYYGILI 232 Q6BNJ4 Nuclear fusion protein KAR5 KAR5 284592 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q6BNJ4 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MDCVNISWFLITLFAAIATSTMHDGENNNVGKMLQEPTYLQSEMIESIMSRHLESFSLTESDFEDIIFMKPRSKCVKDALKDIIPECMRLGVDSIEPGLQKKAAIQLSICEFENSKVTYPSSCYNMINDNDFDSCIFDIERAPQYWTTFSGYYREITKICYEESLPFEKEQIISLYSNITKLYSKMFQDLNDSYKDSTHIQQMMKNEFKELQRMMKVILDQNEKTSEEVKEKYEEFSEQYSSMLSTSLEISKKFSLGTENLVEDMANNIKYLDFELSRISIAIEDLDFETKLTDMKNSVLDDVRNLSDESISLLDSILTNLESLDILSQDAQNITNGISQSLKKNEVLSNNMNNALIETDTQLHEHNEVIRFEFEETISYLSQFSDQAIDNAIRDTSEEITKHVATFIDSINLRLEETTTKLEEVIYNIDDLSDKVGNASSYLIEGLNLLTSNGIMDALLLTYNNVASGLESGFGMLTTLKSDIFKIVRFITACILFAILFIWSMNRLFSQNRTKHTTLSSISPIGILNFRRIFRFLTNLALWLSVMGGTLLAVIVTNFLIQLKVYISKLSTND 574 Q6C619 Nuclear protein localization protein 4 NPL4 284591 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT Q6C619 Pfam PF05021 Pfam PF05020 PROSITE PS50249 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}. GO:0005789 GO:0031965 GO:0005634 GO:0048471 GO:0043130 GO:0031625 GO:0051028 GO:0015031 GO:0006511 MILRFRSKKGTLRAEAQPTDLFDVAFKKLTEDLPDIDPATITLATSPTGKQEPASRLLGKTVQKLGLNHGDMLFVSYTDSAPRAAVEAVTAETAPQMTAAHIRDATKQLPVDDYLEKQDGKIKRQLSALQQRKFGSRGMGEDTLPVDPWDEEYLKEQKIKHMSYHAYVKKLNSQANKKNGGGYIAPLNVSDFGVSKSCTGAHAPWPEGICSRCQPSAITLQSQPFRMVDHVEFAESGMINSFIEPWRQSGTQRIGWMYGHYEPYELVPLGIKAVVEAIYEPAQSGEYDGITITEITQADGQPQPPHIATAEACGLVPLGVIFTDLVDAGNGDGSVICKRHADSYFLSSLEVAFAGAMQARFPNKSRWSPTSEFSSKFVTAVISGNPKGEIDVSCYQVSEQCEAMARADLIEPSINPSVLLVKEATKTRYVPDVFYKKNNEYGRTVLQGANPQLPVDYMLVTLTHGFPQDPRPLFSSGLSSFPVENRELIGVTQSPQALGKALDSGSAGGAVSNFHLLSYIQSMGVLSAEEFQLLAKVATEKKDEDVSRLVASEGWNNLLLIIQ 563 Q6C994 Nuclear fusion protein KAR5 KAR5 284591 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q6C994 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0031301 GO:0031965 GO:0000742 GO:0048288 MSLSYSFNTTIFTENRDLVAALQPQTNCARTALTLIVSDCGKLSSFNEDQQLRVSLAVGLAVCEFKAAQVTYPDACNNIEDWMSTSACTQQLVSSPQWWTTYHGCYNSVKQICHMHEASRECDRALKTHSQIVDMQEKLHTKMDQYWELVETMSDHRDAVLDYWNDTFDFMSETLAHMKETSVSLNAVYRDNFAQAQEHFQMLSENLQEARVQMENLGWAAQDAVVSLSKSTLAEQSLVSERLKNDASSLHKLLVLAHQDTTESFETQLQQSLTILVESSDNVLLNHVQQVSSRLSALMSDLEESQKKNMDMQHQLQQKVRTINDDIEGFTDTVKQGLEASHSLLNLVKSKIQLVNGVVSIFSRPVRSAFQLASFIIMIRAAFIGGIYTSIGLVMGSMLGVLVMQQV 407 Q6CF02 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 284591 Yes SL-0178 SL-0182 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}. UNIPROT Q6CF02 Pfam PF08660 Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 MVTTILIAASAILVLLLLRLLFVLPASNRFGFLYRPKHSNPKLMVMMGSGGHTGEMLRMLKTLKLQSYAKRVYVSSSGDVDSLEKVKVLESTTKTDIKTMVLENIPRARKVGQSYPSSVITSAVSFAVAVKLVHKHKPHVIVCNGPATCVMLCYAAFLLRFMALIDTRIIYVESLARVNRLSLSGLILLPFCDRFLVQWPQLAEKYPRAEYHGILV 216 Q6CIJ3 Nuclear fusion protein KAR5 KAR5 284590 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q6CIJ3 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITAVRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDMYSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDEVNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDELMQTQEETIHLIFQYNKLVHESVIPLLTDDLLPVVRGVSNSIVENLDNMNVELTSHLENVSQTIEVKFKALEKETDRSLLKAKEVESNLRNLNNLVSTSLKGLQTIVRLLTFLLKRQVVLVGILQIFLRKYISMNLYLYAIAVVVTALAGSKVGSWGSLLMKSFVTR 487 Q6CJG3 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 284590 Yes SL-0178 SL-0182 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}. UNIPROT Q6CJG3 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 MLLTTAWCLLIWSVTLLLVRICLVIPIFHSSREAGPLTKDKDNVGGRMKNLVLFIFLGSGGHTGEMLRLIEHYQGMLLESAVTIHVGYSDDDSIIKFKNKIHQISVSNTLRAKVIYHRFDKARDVGSSLAGSIKSIIKTAIRSMVLTYRIKSSMRGHPNLTLLNGPGTCCIITFWLKLYHIFLWQPSKIVYVESLARTNRLSLTGMILYPLADEFVVQWADLLPIYPKAKYYGVLV 236 Q6CKY2 Nuclear rim protein 1 NUR1 284590 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q6CKY2 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 MAFWRNRHESPAISQERSPSPDRFQNSEDIREDNNNYNEDEKLGWFASFMGMFSLPYDWYLSINEDIAVIDWDSKSNSVAWPLGNVLTFLFFSVRLLQDNVIAPNINKLTHSDDAFDFSKSKNLQKYDYFQQYGGSASSSENLYYKMLRQLHRLFYLLTVLLLITNISVTYRYLFAHFQTYSIFYWKTVPKSKNVTKKSLHDLNHTYVEDAKRDSLWGMIKYLLFNGSHDDETNRAHYYELRKWTPSRFLTSFFVSFSPIAFCFLWMTDVTFKTLIPIIIHQYVLWFIVIDRYEQKLKDEQILSMSSVAELNSKVIQPKMNVLKQDAMVDATPYNDGIVYFYPAYTTTRSHVFATHTLSGKLSKEKYNPRTDSFEDANSQRTENYVRFSYHHPKSINGAYVRESYPSRQHSPRLSPSRYSHLQSGNTPSAPSTPLLIPSQQPHFDHSMLANASRNHNISERRNSHSPIKQHFANRLLNYPDETNDSIPDVSDDRFRMDDRFRRGRQGYFNRSPDINSGTLHYDDGDDDDNRISKSPFRNSSSSPFR 546 Q6CLY1 Nuclear protein localization protein 4 NPL4 284590 Yes SL-0178 SL-0182 SL-0198 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}. UNIPROT Q6CLY1 Pfam PF05021 Pfam PF11543 Pfam PF05020 PROSITE PS50249 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}. GO:0036266 GO:0000837 GO:0000839 GO:0031965 GO:0048471 GO:0030894 GO:1990112 GO:0034098 GO:0071629 GO:0006274 GO:0071712 GO:0072671 GO:0051228 GO:0051028 GO:0051974 GO:0070651 GO:1900182 GO:0072665 GO:0030970 GO:1990116 GO:0030433 MLLRLRSKLGIHRVSCEGNDNFGSVIEKWANQLRLNVDPDSVSVSTQPGVSKLMTEIAHQGVESLGLRHGDMVTVEFKVLDTEEKNVSEKEMTNMTVSASTTSVPISSSHNKGSIRGKVKESALDIELEGETGLIPRSRSSLCRHGEKGMCEYCSPLPPWDKGYQDEHSIKHISFHAYLKQLDEVTNKKSSGSSYIPPLSEPNYEINLNCAGGHEPWPKGICSKCQPSAITLQQQSFRMVDHVEFQESELINQFIDSWRTTGMQRFGYLYGYYKRYDNVPLGIKAVVEAIWEPPQHDEQDGLTMDMDQVVKEVEDTDKLAREMGLERIGMIFTDLTDTGLGDGSVYCKRHKDSFFLSSLEVIMAAKHQLRHPNVSKFSETGLFSSRFVTCCISGNLNQEIDIATYQVSIEAEGLVEADLISGSTHPSQAYINETNDKRYVPEIFYTRKNEYNLTVKQNAKPAFPVDYLLVSLTHGFPKETDDDSTTTANTTTVFKTVAGFPWTNRQAMGQSQDYTELKRYVYKACTGNDLAELQAKLSNFHFLLYLHSIEVLNQQEWSLLIRTVTAPTLHEATEPLLNLINSPGWQTFVMILEQSM 596 Q6CS73 Monopolar spindle protein 2 MPS2 284590 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT Q6CS73 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MTKQISKSTQYKPSKSTLVSAKLFSMNRTESTRLLDRAWSVLESGSDGYVYAKDIPEIISFIDRELPSKLTTQSNDKVIESWVNNDPMKTLSKEQFLEAFSMLVGTSFDTAVQIAMQSDILTPTRRGASLFGSYRRSSNDLEQVLPAEQIKALKRELQEWKDKYTFLEHEFQFFLSQEKKNPEVIDNTKHEFIISELNRKLREQDEAIEDLKSQLDYGLVPELKDKTNWIKALQRKAYNYLLPKILICLLLLLLYYCLAAKILFTKSSSTDDVPSFIRQQSWWERNKILSRIQWYFKDRIENNVVRNSSEVIQNYNSVFGIH 322 Q6CV05 Spindle pole body component KRE28 KRE28 284590 Yes SL-0178 SL-0182 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}. UNIPROT Q6CV05 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MTHYHSEYYSEVEKFEYQVTHVTEQILQEQDRLRGSTLHEYNQTILQLVSDYEMFNSNGQCDPSEINLPLEKLESWTNSLKQIHLELESIDNFLRYAIPSDQTILNLSKFNESKYETLQAEVSELRDINVVQLQKEIESLQQQITTKSDENLLISEKIKESCLEASQDIDQCWKLLEQLEAYENANPSTEVITTTDPAFSTYNQWKWNQLAESELKHINQQLITLRATKEKLDKVFSKRSELETSPKSIETFTSYQLLSQLWRSKFIRQLLPDIANLEVYPQSGKLKFEVGIMQVIMQIESGIIKSVSLFSYELSYDRIETIKEDILGRIEHQKSLFKVLVVITDYIVNSL 351 Q6DF48 Calcium-binding and coiled-coil domain-containing protein 2 calcoco2 8364 Yes SL-0198 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}. UNIPROT Q6DF48 Pfam PF17751 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:0003676 GO:1901098 GO:0098792 MASDAPPTSMLQPEERNYSQVVFSRVEQSYVPGIDIICYFTYTSGFHPAKKDWVGIFKVSWKTTREYYTWVSADCEEQGLEKRVTFKAYYLPKESDDYYQFCYVDQKGEVRGVSIPFQLCRKIQDEGEEDILLVTTEEEAQGMKEKQRVLEEKVAALEKDKCTLQDECTQLALEQKNKAALIESLQAQQLECAKKNEELDQQNQELERQLEEEKCKNGSLHLKVVSAEEERERVQNDIRSLQLEQNQLKEENMELHKHTNDMEFSLKKYSEEAKNQEEEVQELKDKLWDAEAKHHLLQVQLQDIQMEKKKDKYSIELLTKEAEKVADLRQNLEKKDKTMETMEKQLAQLQRENATVLRQMEDLSYTLELRKAEISDMQQQRVRDGAEIEHLNRLLTEQSSSTPRNQGLFFQNPYESESLISFANEPQPGEAPGGSSVRHVQMQCPECGSEFENFQVFQDHIFCHDLESTE 470 Q6DFQ5 Sigma intracellular receptor 2 tmem97 8364 Yes SL-0178 SL-0182 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}. UNIPROT Q6DFQ5 PROSITE PS51751 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}. GO:0005783 GO:0016021 GO:0005764 GO:0031965 GO:0005886 GO:0005791 GO:0030867 GO:0042632 MAVCARLLEWIFFFYFFSHIPITLLVDLQAVLPPSLYPQELLDLMKWYTVAFKDHLMANPPPWFKSFVYCEAILQLPFFPVAAYAFFKGGCKWIRIPAIVYSAHVATTVIAIIGHILFGEFPKSDVIAPLTQKDRLTLVSIYAPYLLVPVLLLLTMLFSPRYRQEEKRKRK 171 Q6DFT4 Trafficking regulator of GLUT4 1 trarg1 8364 Yes SL-0198 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}. UNIPROT Q6DFT4 Pfam PF04505 Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. {ECO:0000250|UniProtKB:Q8C838}. GO:0030659 GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0032869 GO:0099638 GO:0044381 GO:0072659 MAINTDTQYEKALGGSGNPLPADSHETEKLLTNASENKEENGMKKSFSVTMSSEKSMGDLEQNGHNLPYKSVSAGQLESAPLSPSRVSLARASSTATTAQEQGRPTDYLVLAIFSCFCPVWPVNIVALVFSIMSRNSLQQGDLDGARRLGRLARLLSVVSILLGLVIIVLCILSLTIFH 179 Q6DGE9 Protein unc-45 homolog B unc45b 7955 Yes SL-0198 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}. UNIPROT Q6DGE9 UNIPROT Q8UVX6 Pfam PF11701 PROSITE PS50293 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}. GO:0031672 GO:0005737 GO:0048471 GO:0030018 GO:0051879 GO:0048738 GO:0061077 GO:0002088 GO:0048747 GO:0030239 GO:0060538 GO:0007519 MTMGEIGDSVQLKEEGNKHFQAGEIDQAIDCYTKAIKTCKKEDKKALAVIYRNRSACFLKKENYSNAASDATKAIDVDAADIKALYRRCQAFEKLGKLDMAFKDVQRCATIEPKNKTFLETLRRLGAEIQQKLKTTFSTDSRVQNMFDILFSDEPDKEKREKAANNLIVLAREDAGAERIFQNNGVPLLMQLIDTGKPEMILAAIRTLSGMCTGHRARATAIIHSVGISKLCSIMAVDNEEIALATANLFQCVNDSLSGGDKRNYGKEEALVLDSSKDLKDILLALLEMIASKNVSGHGRDQALNLLTKNVPRQNKKSTDNSKCLFTIDHGLKKILKVCGQVPDLPDQLPMTENTQLIASVLLSKLYDDLRCDPERDQFRDICDDYIKSKFDPNDMDKNIHAINTLSGILQGPFDLGNVLAGRQGVMEMMVALCGSEREVDQLVAVEALIHASTKTSKASFFISNGVSLLKEMYKKTKNEKIKIRALVGLCKLGSAGGDDYSMRQFAEGSTEKLAKQCRKWLCNPTLDVRTRKWAIEGLAYLTNDADVKDDFAEDEPAMRAMFELTKSNDKTILYAVACTLVNCTNSYDKKEIIPEMVQLAKFSKQHVPEQHPKDKKDFIVRRVKRLLKAGVTSALAVMVKADNSILTDQTKEMLARVFLALTEDVKDRGIIVAQGGGKALIPLALEGTDKGKIKASHALAKIAAVSNPEIAFPGERIYEVVRPLVSLLGTDRDGMENFEALRGLTNLAGLNDKLRVKILKEKALPEIENYMFEDHEQIRQAATECMCNLVCCKEVQDRYLEDGNDKLKLLVLLCGEDEEKLQRAAAGALAMLTAAQKKLAVKMTKVTEQWLEILQRLCIHDNPEIQHRGLVTVFNMLDADDQLAKKLVESDMLEILTYVAKLEDNPKKQNAIDAARACLSKAMDNGLIKPFSN 934 Q6DRB1 Nucleoporin GLE1 gle1 7955 Yes SL-0178 SL-0185 Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. UNIPROT Q6DRB1 UNIPROT Q502U5 Pfam PF07817 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}. GO:0005737 GO:0005576 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0060287 GO:0006406 GO:0048666 GO:0016973 GO:0060296 GO:0006446 GO:0006449 GO:0014044 GO:0014037 GO:0014010 MPSENLRWETLEALKNSPKGKLKYSPDWVEKGEDVLAGCVEVPSLSPLSGQILKRMSPRMLLKNCSRSSSVRDTSPGLSEEAAVCRSAPISPRLKRSSCSLPAVSIQTEEEEEKEEEEKAEVVVEAPAVSPEASVSTPPAVSVLSPRATQISGCIRMCEQKHKAKAKMELSLRQEQQERLVATVANHESEQLKRFEEFMELKQRQEHQSIRDTNEKEAQESLGRQEKLREEHRHRMKILNLRLREMEQQRLREVELERQRQVEGRERHRAINAIQEEVLQLNRLLQPQQSTHAEVEHAPYITRGNQLCSQLSEVVPAAADDQFPSVEDLSVAERALQEMRSLVRSLQEAVSQAAERKKKKEQEEEEEKRRQEQLKAQQEEQKKSAALSAKEKAKKEGLQTGADDSTLKWYNSLQDLANQCAQAFDDLNKAKDTQTKKLKMELQKAATTPVSQIANSSGAPLKEAFEKIDKLLSRRPVTSAGKTVSTSQHPQGLEFASYRLAEKFVKQGEEEVASNHSAAFPIGAVASGIWELHPKIGDLILAHLHKKCPYAVPHYPPMESGTSVEDYQKILGYRVDEGKVEGQDSFLKRMSGMIRLYAAIIQMRWPYSSKQGLHLHGMNHGWRWMAQILNMEPLADITATILFDFLEVCGNALMKQYRVQFWKLILIINEEYFPRYLCFASILHFTCIHWLQNIE 695 Q6DVA0 LEM domain-containing protein 2 Lemd2 10090 Yes SL-0178 SL-0179 SL-0182 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. UNIPROT Q6DVA0 UNIPROT Q8C4H8 UNIPROT Q8R0N2 Pfam PF03020 Pfam PF09402 PROSITE PS50954 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}. GO:0000785 GO:0005783 GO:0005639 GO:0031965 GO:0060914 GO:0030514 GO:0043409 GO:0051898 GO:0022008 GO:0006998 GO:0071168 GO:0035914 MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPLRARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPDRHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANVTSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER 511 Q6FL09 Nuclear rim protein 1 NUR1 284593 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q6FL09 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 MFSWLIPDIPELFLTISVWFRLQGWEDNTKLGFIIGNTLTTIFYILRLAQDTLLAGVSRKLIRDYELFDLSKSETLLSDPAFSSYHDVLFNKHHSTANASSYNKRVRKVTSTVYWSTYFLLLLSCYTCYRLFNTYKVYRIYYLKDLNLDKHPSLKKIEPDYEVDEKLLKTSLKSKLLSRFIRLLQLQDEVETELPKVTEHYTLNKWDPSKLIISLSTSFSPTIIICLMYTNVTFLTVIPIIIHQGIFYFMIWNRYEERFKDDALLMRENYLQYDTKYVKPLKQIMYQDVMTDTATISDGGFTKFFPVSKSTLFKHHEMSGDVIIERYNKKSREFENVTDIIKPHHHINNTVKILPPTIRKDHKTNRYDHRQQSILKDRKFNIDSNEPQIINALTTAIPSRSFFNNNPSGSNDDNCSGIKVRSSPTRETFFPATPLRKK 438 Q6FQU6 Protein transport protein SEC13-2 SEC132 284593 Yes SL-0178 SL-0185 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}. UNIPROT Q6FQU6 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0030127 GO:0005789 GO:0000139 GO:0005643 GO:0005198 GO:0090114 GO:0051028 GO:1904263 GO:0015031 MVKIENAHEGVIHHAALNYYGTRLATCSSDKTVKIFEINDVNNSSSLLETLVGHEGPVWYADWCHPSLGENLLATCGYDGKVLIWKESGHGGKMQIIGKHAVHSASVNCVKWAPHEYGLILLCGSADGKISVVELKDGQIASTKILDNAHKFGVNSISWAPLMKTDSSDDGDETTAVKQFISGGNDNLVKIWKFDDDQETYVVADTLEGHKDAVTAVDWSPTTLLQSYVASVSNDKQCLVWTQDHSSKKNDWKKISVNEGKFEQKLGSVSWSLSGNLLAVSDDDKNVTIWKESGDGKWEEVVN 303 Q6FS52 Monopolar spindle protein 2 MPS2 284593 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT Q6FS52 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MSEVDVPELLFERVWLQVDRDRDGFIYAKQMPSFITQCEQVIKDTVNTNKTDFHMTRFKNRLKLPLLPKLHMDLIDAFAKETPYYKIYKESFSDMLNKLTGNNFSTVINKIFEDCDGFPASFISALEVKADVKSSPRSKADSLGSPIKVDLLRNLKPQEEPETPRRINRKYKSLELQLESMKRELEDKEKTIMNNERNLTELRSTISKLKEKYDLLSEEYEQRHIHGGNNGTAIKHDVVIGELKSRLQEQNRLIRILQEQIQFDPQLKRETRVHDNKSKNNTFNGAIAYVIPFLLFIFVIRSLITKEDIGDATMALPWWERNNLASRLAWYFRDVFSNDSAKFLESDAYDKVFGIH 356 Q6FSC7 Spindle pole body component KRE28 KRE28 284593 Yes SL-0178 SL-0182 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}. UNIPROT Q6FSC7 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MEAQLHELQEEITRSSDLVLTEQDKRLQGTLREIDQSIRKLIETSDYLKLSGDADSLIDIKQLEVKSRELDSLMDLLRKLYWREESLDLFLKYTINSDAEQVPVFSDTDPKYQSLQDEVSHLRDDVMTVKNQEIDQITGEILQVAHEITEKQDQVNMLYLETTNELDKCWELLDEWQRLQDDQRITKNEDNSNRKDTELNAMEECYEEWKTLEELAVLNDNLQKQIDELEKVDNKAINSTQLAEESIVNTVQLNDLIDMWKRRIIASIHEDISEIVLYPYSRKLQLRVANRYTIIIQLDKHQTHDGKSTIHDIDLFTEQDSRIIPMRELRKQVLQECKGHSNILQALKNIINRVINNDN 359 Q6FU40 Nuclear fusion protein KAR5 KAR5 284593 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q6FU40 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0000742 GO:0048288 MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVGLSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVSETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKKTIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKLPTLEQQYLGNFAQALSNIDKQVLSASLQWQYDYDVVFANLYAALDLLNSNLNSSVKKIEQIEHVIDTIIVDTSFLNDQLANLILIPSTILRAFSFIGVKRVIIAIIVLYFKSTLLCLVHYGQSFRIAALLMSATAGIFCSKLLMSYIYN 469 Q6FV75 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 284593 Yes SL-0178 SL-0182 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}. UNIPROT Q6FV75 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVLLNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHLTLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGILV 242 Q6GLC9 Synaptic functional regulator FMR1 fmr1 8364 Yes SL-0198 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}. UNIPROT Q6GLC9 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. GO:0030424 GO:0043679 GO:0030054 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0030425 GO:1902737 GO:0043197 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0035770 GO:0045202 GO:0003682 GO:0070840 GO:0002151 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0045182 GO:0030371 GO:0006974 GO:0072711 GO:0034644 GO:0007215 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0060999 GO:0051491 GO:2000637 GO:0033129 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVSYDSENYQLVILSVNEVTIKRANMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENDKNISPEEGMVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRPDKEKGYQSEDLSGTGRGSRPYNNRGRSRRGTGYASDIRYGDPDYRKTTYPEYPRSQAFWIKGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGPRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEGSRLRTGKDRVQKKEKSEVVDGPQVVVNGIP 590 Q6GNM0 Nurim nrm 8355 No SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q6GNM0 DE Reference Proteome: No; GO:0016021 GO:0005635 GO:0005637 MSANVQVSGQLSSGPSLPACIVLSAVSLLCFVAGFGTGAEFVRFLSFGAIFRNISGGLDGEIPLTWSEAIRNTQFQCCIGIDIGLLFLFVLQHSLMAWTAVKKNVLHVFGVLQRSIYILCTALSLQVLMRFWQPCPHGPYLWNVSSDPWSAWLPLLCALVHTISWLLIFSVLLIFDYAELMGIKQVYYFCLGMGDPLSHKSPRVARLYAHLRHPIYLELLLILWAVPCLPPDRLILAIFFTLYLSLVHRLDVQDYAYLRSQLEKKFLLFSREEASAVGGQIRKNN 285 Q6INS1 F-box/LRR-repeat protein 5 fbxl5 8355 No SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q6INS1 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSNNNDLLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSHTVYNVHSDNKLSEMLVLFEKGMKNVKNEYKQLNYVQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDEMKDIKKKVIAQHCSQKDTTELLRGLSLWNKAEELQKVLKYSVDEKAERNSKTQKSSSSISSLPPEVMLNIFTYLNPQDLCRCSQVNTEWAQLAKTGSLWRHLYPVLWARGDWYSGSHAYLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEEEDSSISMAQREKELLNSLVHYILPYVGHSVKTLVLAYSSATSSKVIRQMLEYCPNLEHLDLTQTDISDSAFNGWHFGACQTLHHIDLSGCDKITDLTLEKLSVALGIPSAHKKRLLKCYRNNRTLKDIRNQMRCSSLAQITGESTIYSDAFWANSDRSQDYTSPPIWILDSGNPGDIEDAADWKFRTTDGLCVLEMAPSVTCFSNGCCSRARPGRWTNVGWQEHCKAATVSYCGHTLCGNTLRTIHTLPEASALCNIGTRTLHSDITDCFPGSAKSDQQAARALQFLSLSGCHQITDHGLRALTIGGGLPKLEHLNLSGCLNVTGSGLQDLVATCPSLNDEHFYYCDNISGPHGATASGCQNLQCGFRMCCRSGE 678 Q6NRD3 E3 ubiquitin-protein ligase SH3RF1 sh3rf1 8355 No SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. UNIPROT Q6NRD3 UNIPROT Q3L1I1 Pfam PF14604 Pfam PF00097 PROSITE PS50002 PROSITE PS00518 PROSITE PS50089 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}. GO:0005794 GO:0030027 GO:0048471 GO:0005078 GO:0046872 GO:0061630 GO:0006915 GO:0001764 GO:0046330 GO:0051865 GO:0043370 GO:2000564 MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRKELRCPECRTLVECGVDELPSNILLVRLLDGIRQRPRKAGDGGSAGNSTNALRAQGSVTTNGGLNDAQNTQSGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIVLRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAAKQLIELDKPSGADTGEGSSGTSHSGNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSMEISPPVLISSSNPTAAARISELTGLSCSAPSQDMNPPLLPPPPMATPVITSASSGAAAVAQRNIIGPVEQVPHLRTSARPSVFIAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRALTTATPAKVAMATATTSNVVNLVTPTPPGAPCQKLPVSGVEFAKTSSTNGVSPAGVPGCHIQTSPQSKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAAVTPIQAQTPAASALPQQAAASQQVPPPLSAPAAYINAAMNISRPSVPAASAASSALPTAAFEAESSWKSSSGLSGCSFSENVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPHSPTQEVEQTNSEAAAALEGAVGPDIVPVIVNGRAAPCTVDCDSVSASTPAQDNRKPASLDNNIPIAPPPRQPCSSLGSVLNDSRPCERYRVMVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI 826 Q6NRG5 NADPH-dependent diflavin oxidoreductase 1 ndor1 8355 No SL-0198 Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. UNIPROT Q6NRG5 Pfam PF00667 Pfam PF00258 Pfam PF00175 PROSITE PS51384 PROSITE PS50902 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}. GO:0005829 GO:0048471 GO:0050660 GO:0010181 GO:0050661 GO:0003958 GO:0008219 GO:0036245 GO:0016226 MPQQNLLILYGSQTGTAEDLAGRLSREAKRHHFNCRTEALDEYRVANLINEHLVIFVCATTGQGDPPDNMKNFWRFIFRRNLPHNALCQMDYAVLGLGDSSYPKFNFIAKKLHKRLNQLGACPLLPAALGDDQHELGPDAVVDPWLKDLWSKVLSMFPLRPGLEIISEDVLLPPKYSLRLLEEKVGQSELSGDAYERDFISNNTTPPSEIHPFLAPVLSNERVSAHDHFQDVRLIEFNITGSAIQFYPGDVVMVQPRNSLLHVEQFCSLLHLDPLNKVVVEPSDPESPVPMHLAALCSVQQLVERYLDICSIPRRSFFQLFCHFSPDEMEREKLKEFSCAAGQEELYSYCNRPRRTILEVLVDFPHTTRCIPATFLLELIPQIRPRAFSIASSMEALPNTIQILMAVVQYKTKLIEPRRGLCSTWLASLPPHGTERVPIWVKKGSMKFPCDPDTPVVMVGPGTGVAPFRAAIQERVANGRPGNCLFFGCRGKSKDFYFEKEWEDLGNRGYLTLFTAFSRDQEDKIYVQHRIKENSKLLWDLIGTKQGYVYIAGNAKLMPNEVTDALKWVLQLEGGMSAPDAEQYLASMEKSCRFQSETWS 600 Q6NRQ2 Nucleolar complex protein 4 homolog A noc4l 8355 No SL-0178 SL-0182 Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}. UNIPROT Q6NRQ2 Pfam PF03914 DE Reference Proteome: No; GO:0016021 GO:0031965 GO:0005730 GO:0042254 MAARKTKHACRIQDKRSDAERQDLDTKLAAVLESRGNANAVFDILEHLESKKEEVVQAAIRTASKLFEVMLEKRELYIGDLPAENGTLPDTYSAEDKYKMWMRHRYNSCAACILDLLQHSSFSNQELALCTLMKFIQLEGKFPLENSEWKDSYRFPRELLKFVIDNLLQEEADCTLLITRFQEYLEYDDVRYYTMTVTNDCVSRVQQKNKLVLPPVFQTNVFCLLSSINIPVEESALGNFLVTKNVNNEDWKPSKLKDHKRVFERVWMIFLKHQLSVSLYKKVLLILHESILPHMSKPTLMIDFLTAAYDVGGAISLLALNGLFILIHQHNLEYPDFYKKLYSLLEPSIFHVKYRARFFHLANMFLSSTHLPVYLVAAFAKRLARLALTAPPQVLLMIIPFICNLIRRHPACRVLIHRPSAGDLATDPYIMEEQDPAKSQALESSLWELEVLQQHYHGDVVRAANVISRPLSAQESDISGLLEISSCELYDKEMKKKKFKSVPLEYEPVRGLLGLKSDITAQHFTF 526 Q6NVE8 WD repeat-containing protein 44 Wdr44 10090 Yes SL-0198 Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}. UNIPROT Q6NVE8 UNIPROT Q3UT13 UNIPROT Q8BTS1 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}. GO:0005829 GO:0010008 GO:0005794 GO:0005874 GO:0048471 GO:0017137 GO:0030334 MASESDTEEFYDAPEDVHLGTGYPVGSPGKVGLLSFKEAENTANQAGNESPVQELRQDVSKKIIESIIEESQKVLQLEDDSLDSKGKGLSDEATAGPSVAGTEFSNIPGLLAIEHELQQDSEKAESQNVAEESELETQKCFPSDETCEKSEKTVDETDNLTEVSSGEQLDASGLEAETLNKEALEVKEGDVLDPASLDTLSTTDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPPPPSRPAPPPRKKKSELEFEALKTPDLDVPKENITSDSLLTTNMASENTVRDSLPSLDLASATSGDKIVTAQENGKAPDVQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDATQSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEGRVSPSPSQESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLDSTSTGIVKTDNTEVLLSADFTGAIKVFINKRKTVS 915 Q6NWF1 Solute carrier family 2, facilitated glucose transporter member 12 slc2a12 7955 Yes SL-0198 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}. UNIPROT Q6NWF1 UNIPROT Q6PHV4 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-regulated facilitative glucose transporter. {ECO:0000269|PubMed:25326603}. GO:0012505 GO:0005887 GO:0048471 GO:0005351 GO:0046323 GO:0044381 GO:0060047 GO:0007507 GO:0003179 MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSCPEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAAEVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHATLLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHGNEAATLASTGFGVVKVGGTIPAIFLVDKVGPKALLCVGVVVMMLSTATLGAITMQSRTHVSSLCRGPGNTANFTLFETGDETDIQTNTPLGLYQPQNKLKTNTFLTSINDTREHWILNHTYNHRTALMETAELSKKDSAKIALQSLHEVSPSLKWISLVSLLVYVAGFSISLGPMVHVVLSAIFPTGIRGKAVSVISAFNWATNLLISMTFLTLTERIGLPTVIFSYSAMSFLLVVFVIVFVPETKGRSLEQISKELAMKNHLRGTLLCHRRKHKATAQPSQEEKALATV 610 Q6NWG1 Leucine-rich repeat-containing protein 59 lrrc59 7955 Yes SL-0178 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}. UNIPROT Q6NWG1 Pfam PF13855 PROSITE PS51450 Required for nuclear import of FGF1. {ECO:0000250}. GO:0005789 GO:0016021 GO:0005635 MNKGKIENIKDKIDGNELDLSLSNLTEVPVKELAAFPKATFLDLSCNNLITLTPEFCSLTHLIKIDLNKNQLVCLPEEIGQLVNLQHLDLYNNKLKMLPIGFSQLKSLKWLDLKDNPLEPTLAKAAGDCLDEKQCRQCASRVLQHMKVLQEEAEKELERRLLKEREQEKKKEAKQREKEAREKEAQKKKKAEEKERKRKEYQAQVAAVAAQEQQKKKKEEKKKKAAQNQGKKAAPESVPKAKRSICSLFFSLLLKLVLLLVIGVSSVVAVCQLTELRKEAFCIPLNVHFEETVRWAQGLDVVQQVIQKMSDLRT 314 Q6NX12 Nuclear pore complex protein Nup93 nup93 8364 Yes SL-0178 SL-0182 SL-0185 Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}. UNIPROT Q6NX12 Pfam PF04097 Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. {ECO:0000250}. GO:0031965 GO:0034399 GO:0005643 GO:0017056 GO:0051292 GO:0016973 GO:0006606 MDGEGFGELLQQAEQLAAETEGVTELPHVERNLQEIQQAGERLRSKTMTRTSQESANVKASVLLGSRGLDISHISQRLESLSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFVMAEEYHRESMLVEWEQVKQRVLHTLLASGEDALDFTQESETSYISESGAPGRSSLDNVEMAYARQIYMYNEKVVSGHLQPSLVELCTEAAERLDDKNVSDLWVMVKQMTDVPLIPASDSLKSRCSVQMQMAFLRQALHFLEQSYKNYTLMSVFANLQQAQLGGVPGTYNLVRSFLNIRLPAPIPGLQDGEVEGYPVWALIYYCMRCGDLMAAQQVVNRAQHQLGDFKNCFQEYVHSKDRRLSPTTENKLRLHYRRAVRASTDPYKRVVYCIIGRCDVTDNHSEVADKTEDYLWLKLSQVCFEDEANSSPQDRLTLPQFQKQLFEDYGESHFAVNQQPYLYFQVLFLTAQFEAAIAFLFRLERTRCHAVHVALALFELKLLLKSTGQSAQLLSLEPGDPQGVRHLNFIRLLMLYTRKFEPTDPREALQYFYFLRNEKDSQGESMFLRCVSELVIESREFDMLLGKLEKDGSRKPGAIDKFTRDTKTIINKVASVAENKGLFEEAAKLYDLAKNPDKVLELTNKLLSPVVSQISAPQSNRERLKNMALAIAERYKSQGVSAEKSINSTFYLLLDLITFFDEYHAGHVDLAFDVIERLKLVPLSQDSVEERVAAFRNFSDEIRHNLSEILLATMNILFTQYKRLKGSGPNTLGRPQRAQEDKDSVLRSQARALITFAGMIPYRMSGDTNARLVQMEVLMN 820 Q6NX28 Leucine-rich repeat-containing protein 59 lrrc59 8364 Yes SL-0178 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}. UNIPROT Q6NX28 Pfam PF13855 Required for nuclear import of FGF1. {ECO:0000250}. GO:0005789 GO:0016021 GO:0005635 MARANGRSQNLRDKLDGNELDLSLSDLSEVPVRDLVAIPKATALDLSCNKLTSLPDDFCNLSYIVRLDLSKNQIAQLPSEFGRLVNLQHLDLLQNRIVALPVSFAQLKSLKWLDLKDNPLKPALAKVAGDCLDEKQCKECAQGVLQYMKSVQSDHERELQRKLQLDKDRKQRLEAQQRVKEEQDRELRKRMKQQQKERKRRDYNAMQEAQKALNNNKKKAEEEPSENHKPVPTPKEKKLARRQSRLRKIACILLFGLMVALLGVVACRFTDLKTFEVCRSVNAVYKETLSALHSNPVLERFLQDPSSQ 308 Q6P0E8 Inactive phospholipid phosphatase 7 plpp7 7955 Yes SL-0178 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}. UNIPROT Q6P0E8 Pfam PF01569 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}. GO:0005789 GO:0016021 GO:0005635 MPANQTRSRARERNNVLNRPEFMSLNQPIKSGGGGGGGESRGTARRPSQRQQQNQQQQGDNPQPENNKDKKELPEEDCMQLNPSFKGIAMNSLLAIDICMSKRLGVCAHPSSSWGSVRSMVKLLALTGHGIPWVFGTIVCLMRSNTLAGQEVLVNLLLALLLDVMTVSGMQKLVKRKGPWEMPPGFFDYLAMDIYSFPAAHASRAVMVSKFLLAHLVLAVPLRILLVLWAILVGISRVLLGRHHLTDVGCGFALGFLHYSLVEMVWLSSNTCQTLISIGTFNWSPLY 287 Q6P0U9 Nucleoporin NUP42 nup42 7955 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q6P0U9 PROSITE PS50103 Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}. GO:0031965 GO:0005643 GO:0005634 GO:0046872 GO:0005049 GO:0051028 GO:0015031 MPVCNFFLQGRCRYGDTCWNEHPTGGRGGDYRGNQQPSNRGGFGNRVWINPSQRGGGGSSSAGGSNEWGRGAASARDVQSSEFSFSQNRFSALETQRAGAEDTHTTLDTIQKEMEVWQTSGQWPFSCYSAVNRQISGFIELCPEELRLEYYTSRASGDIQPYINSVQQLANQWRSRVQELRNMSSSTQISVIAELKSSSPPASAPGFGSPGPGFGSATSGFGNTSLSSPPAGFGGAGFGSGPQSSSTFSFAQSKTDFGASNTQQASGFGSSAFAQPSSGFGNPAPSAASFSFAAADSESKPSAGGFGSASGFSFKTATAGQGSGFGSGFGSSSGFGSSSGFGSSSGFGSAFGSAAPAQSSSFGSTGGAADTQSGHGLFTANSELTPEELKEFMAKRFTLGQIPLRPPPADLLMI 414 Q6P2B1 Transportin-3 Tnpo3 10090 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:Q9Y5L0}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y5L0}. Note=Localizes to the nuclear envelope and annulate lamellae, which consists in stacks of endoplasmic reticulum membranes containing a high density of nuclear pores. {ECO:0000250|UniProtKB:Q9Y5L0}. UNIPROT Q6P2B1 UNIPROT Q7TSL6 UNIPROT Q8BKX4 UNIPROT Q8BP42 Pfam PF08389 Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation. The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively. Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus. {ECO:0000250|UniProtKB:Q9Y5L0}. GO:0005642 GO:0005737 GO:0043231 GO:0005635 GO:0042802 GO:0008536 GO:0006606 MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHSIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVHLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIAHSLDSFMLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANSSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMSQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR 923 Q6P4S8 Integrator complex subunit 1 Ints1 10090 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. UNIPROT Q6P4S8 UNIPROT Q0KK58 UNIPROT Q80UQ7 UNIPROT Q91Z01 UNIPROT Q9CTF7 Pfam PF12432 Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q8N201}. GO:0016021 GO:0032039 GO:0031965 GO:0005634 GO:0001832 GO:0001833 GO:0043066 GO:0043154 GO:0016180 GO:0034474 MNRAKPTTVRRPSAAAKPSGHPPPGDFIALGSKGQASESKTTSTLLKPAPSGLPSERKRDASASLSGTSALTGLTKRPKLSSTPPLSALGRLAEAAVAEKRAISPSIKEPSVVPIEVLPTVLLDEIEAAELEGNDDRIEGVLCGAVKQLKVTRAKPDSTLYLSLMYLAKIKPNIFATEGVIEALCSLLRRDASVNFKAKGNSLVSVLACNLLMAAYEEDENWPEIFVKVYIEDSLGERIWVDSPHCRTFVDNIQTAFNTKMPPKSVLLQGEGARSGGELGAGSSPHPSLTEEEDSQTELLIAEEKLSPEQEGQLMPRPRYDELTESVEEYVLDMLRDQLNRRQPIDNVSRNLLRLLTATCGYKEVRLLAVQRLEMWLQNPKLTRPAQDLLMSVCMNCNSHGSEDMDVISHLIKIRLKPKVLLNHYMLCIRELLNAHKDNLGTTIKFVIFNELSNARNPNNMQILYTVLQHSSELAPKFLAMVFQDLLTNKDDYLRASRALLREIIKQTKHEINFQAFCLGLMQERKEPQYLEMEFKERFVVHITDVLAVSMMLGITAQVKEAGVAWDKGEKRNLEVLRTFQNQIAAIQRDAVWWLHTVVPSVSKLAPKDYVHCLHKVLFTEQPETYYKWDNWPPESDRNFFLRLCSEVPILEDTLMRVLVIGLSRELPLGPADAMELADHLVKRAAAVQADDVEVLKVERIQLIDAVLNLCTYHHPENIQLPPGYQPPNLAISTLYWKAWPLLLVVAAFNPENIGLAAWEEYPTLKMLMEMVMTNNYSYPPCTLTDEETRTEMINRELQISQREKQEILAFEGHLAAASTKQTITESSSLLLSQLTSLDPQGPPRRPPPHILDQVKALNQSLRLGHLLCRSRNPDFLLHIIQRQASSQSMPWLADLVQSSEGSLDVLPVQCLCEFLLHDAADSTASGEEDDEGESREQKAKKRQRQQKQRQLLGRLQDLLLGPKADEQTTCEVLDYFLRRLGSSQVASRVLAMKGLSLVLSEGGLRDKEEKEPPMEEDIGETDALQGYQWLLRDLPRLPLFDSVRTTTALALQQAIHMETDPQTISAYLIYLSQHTPVEEQGPHSDLALDVARLVVERSTIMAHLFSKPSCSTASDAVLSALLSVFSRYVRRMRKSKEGEEVYSWSESQDQVFLRWSSGETATMHILVVHAMVILLTLGPPRSGDSEFSELLDIWFPEKKPLPTAFLVDTSEEALLLPDWLKLRMIRSEVPRLVDAALQDLEPQQLLLFVQSFGIPVSSMSKLLQYLDQAVAQDPQTLEQNIMDKNYMAHLVEVQHERGASGGQTFHSLLTASLPPRRDSTEAPKPESSPEPPPGQGRTRAGTQVPVLGPEDDLAGIFLQIFPLSPDPRWQSSSPRPLALALQQALGQELARVRQGNPEVPGITVRLLQAMTTLLSSPHGGTLALAMHHSHFLSCPLMRQLYQYQRAVPQDTGFSSLFLKVLMQILQWLDSPAVEDGPLQAQLKLFATRYSARHRISDVRSGLLHLADALSFHGDLEVANSTARAVIATLRSGEKCPVEPELISKVLRGLIEVRSPHLEELLTALFSATTETSCPSPASGPIVVVSSLLLQEKEELLGPSKQEVEGASTEAMRLGPASGLLVDWLETLDPEVVCSCPDLQWKLLFSRRKGKGHISAQVLSFRPYLLALLTHQASWSTLHCCIRVLLGKSREQRLDPSASLDFLWACIHVPRIWQGRDQRTPQKRREELVLHVQGPELLSLVELILSEAETRSQDGDSAARTLIQTRLPLLLSCCRSNDESIGKVTEHLTSCIQQWGDSVLGQRCRDLLLQLYLQRPEVRVPVPEVLLQSEGATSSSICKLDGLVHRFITLLADTSDSRSSESRVADANMACRKLAVAHPVLLLRHLPMIAALLHGRTHLNFQEFRQQNHLAFFLHVLGILELLQPRVFQSEHQGALWDCLRSFIRLLLNYRKSSRHLAPFISKFVQFIHKYVGCSAPAAVAFLQKHAEPLHDLSFDNSDLVMLKSLLAGLSLPSRDGRTDQGLDEEGEDERSAGSLPLVSVSLSTPLTVADVAPHMKRLSRGRAVEDVLETLSDIDEMSRRRPEVLGFFSTNLQRLMSSAEESCRNLAFSLALRSIQNNPSIAADFLPTFMYCLGSRDFEVVQTALRNLPEYTLLCQEHAAVLLHRAFLVGVYGQIDTSAQISEALKILHMEAVM 2195 Q6P5Z2 Serine/threonine-protein kinase N3 PKN3 9606 Yes SL-0198 Nucleus {ECO:0000269|PubMed:10441506}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10441506}. Note=Nuclear and perinuclear Golgi region. UNIPROT Q6P5Z2 UNIPROT Q9UM03 Pfam PF02185 Pfam PF00069 Pfam PF00433 PROSITE PS51285 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 PROSITE PS51860 OMIM 610714 DisGeNET 29941 Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}. O96018 EBI-6115839,EBI-1384335 Q8IVD9 EBI-744342,EBI-1384335 P17918 EBI-1173716,EBI-1384335 Q96BD8 EBI-741854,EBI-1384335 Q9UKF6 EBI-1044699,EBI-1384335 O95235 EBI-2551319,EBI-1384335 Q8VC57 EBI-2551470,EBI-1384335 Q62376 EBI-6665659,EBI-1384335 Q96L14 EBI-743488,EBI-1384335 Q8BQ46 EBI-645898,EBI-1384335 Q9UBN7 EBI-301697,EBI-1384335 Q00839 EBI-351126,EBI-1384335 Q91YI4 EBI-994161,EBI-1384335 D3Z482 EBI-11073196,EBI-1384335 Q9EQU5 EBI-1543689,EBI-1384335 P58771 EBI-298478,EBI-1384335 Q9Z2X1 EBI-4283704,EBI-1384335 P62714 EBI-1044367,EBI-1384335 P67775 EBI-712311,EBI-1384335 Q13033 EBI-1053857,EBI-1384335 P23258 EBI-302589,EBI-1384335 Q9D8B3 EBI-8322817,EBI-1384335 P19788 EBI-11032993,EBI-1384335 Q14103 EBI-299674,EBI-1384335 Q13352 EBI-712105,EBI-1384335 Q9P2B7 EBI-2558932,EBI-1384335 Q9BQE3 EBI-1103245,EBI-1384335 P62937 EBI-437708,EBI-1384335 P55795 EBI-352823,EBI-1384335 Q14134 EBI-702370,EBI-1384335 O60232 EBI-741415,EBI-1384335 Q86WV1-2 EBI-11995314,EBI-1384335 A8K8V0-2 EBI-21612038,EBI-1384335 P33151 EBI-2903122,EBI-1384335 P43115 EBI-15009894,EBI-1384335 Q9UNA1-1 EBI-25412129,EBI-1384335 Q5JR59-3 EBI-11522433,EBI-1384335 Q9UBB9 EBI-1105213,EBI-1384335 Q8N1B4 EBI-2799833,EBI-1384335 Q08379 EBI-618309,EBI-1384335 Q8ND90 EBI-302345,EBI-1384335 Q71U36 EBI-302552,EBI-1384335 Q15323 EBI-1384335,EBI-948001 O95619 EBI-1384335,EBI-399269 Q6NZI2 EBI-2559016,EBI-1384335 O43482 EBI-1384335,EBI-536879 O15516 EBI-1384335,EBI-1794265 O00327 EBI-1384335,EBI-1794206 O00233 EBI-1384335,EBI-750973 Q5R372 EBI-1384335,EBI-2810417 O43815 EBI-1384335,EBI-1046642 Q8TBA6 EBI-1384335,EBI-11278147 Q8TD31 EBI-1384335,EBI-949834 Q7Z4H7 EBI-1384335,EBI-2558196 Q6NSJ2 EBI-1384335,EBI-6148204 Q5VIR6 EBI-1384335,EBI-2850511 Q5T0U0 EBI-1384335,EBI-2836961 Q567U6 EBI-1384335,EBI-1104769 Q53HC9 EBI-1384335,EBI-1055422 Q4V328 EBI-1384335,EBI-717919 Q15276 EBI-1384335,EBI-447043 Q14161 EBI-1384335,EBI-1046878 P61244 EBI-1384335,EBI-751711 P0C1Z6 EBI-1384335,EBI-1245626 Q9BZD4 EBI-1384335,EBI-724102 Q96P16 EBI-1384335,EBI-1053506 Q96JG6 EBI-1384335,EBI-11044388 Q96EK4 EBI-1384335,EBI-1790529 Q96BD5 EBI-1384335,EBI-745085 Q86Y13 EBI-1384335,EBI-948630 Q9Y3A3 EBI-1384335,EBI-713935 Q9Y2X7 EBI-1384335,EBI-466061 Q9UKL0 EBI-1384335,EBI-926563 Q9UJ41 EBI-1384335,EBI-913954 Q9UID3 EBI-1384335,EBI-2932923 Q9NP66 EBI-1384335,EBI-740641 Q9NNX1 EBI-1384335,EBI-2557363 Q9HCH0 EBI-1384335,EBI-3437824 O15460-2 EBI-10182841,EBI-1384335 Q96F46 EBI-5591258,EBI-1384335 P52799 EBI-7532268,EBI-1384335 Q9Y5G3-2 EBI-21584477,EBI-1384335 Q8TDQ0 EBI-11472922,EBI-1384335 Q9Y279 EBI-903131,EBI-1384335 Q9H8J5 EBI-2830042,EBI-1384335 Q15768 EBI-3908475,EBI-1384335 P04201 EBI-21274133,EBI-1384335 P61586 EBI-446668,EBI-1384335 Q8N831 EBI-12023322,EBI-1384335 Q6ZN54-2 EBI-12346463,EBI-1384335 P37173 EBI-296151,EBI-1384335 GO:0005794 GO:0005634 GO:0048471 GO:0005524 GO:0004698 GO:0017049 GO:0004672 GO:0004674 GO:0010631 GO:0035556 GO:0018105 GO:0006468 GO:0007165 MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILLPGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLRMKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLLEQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQRGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLSLSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRTPTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFRCLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTEFVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEKRLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFDFVSERFLEP 889 Q6P752 Torsin-1A-interacting protein 2 Tor1aip2 10116 Yes SL-0178 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q6P752 Pfam PF05609 Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity). {ECO:0000250}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0001671 GO:0051117 GO:0007029 GO:0032781 GO:0090435 MSQTLKSQDTNMSDSGYRDPVEDSQNVLGNDPSVNSQAQDPIVTPSNTVEAQTLHPTSDLKEDHHEIGAKGQEHADTGDRAESSEEPALEKPPLDKAELERSPSSQDTEQRHHPYSEHVGGDTLVLDPNYSQSDLGGRADAHLESSSAAPTEGAGEGGEAGAHLESSCAALPVGADEGGRANAHLESSSAAPTEGAGEGGEADVHLESSSAVPPEEAHLESSSAAPSEGAGEGGEADAHLESSSAAPSEGAGEGGETAQNLLAVDSTDAQSPCHSSAGPGSQDSLRRRLPVTEAERHEEETQLVTEKEEVAQETLRKTEKKSLWTYGSMFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFSQLREKFPGQSAFLWQRGRKFLQKHLNASNPSEPATVIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSYGFENGHKAAVVHHFESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPRETEEKVRDLLWAKFTDSGTPSSFSHMDSDKLSGLWSRISHLVLPVQPVKNIEERGCLL 578 Q6P9B9 Integrator complex subunit 5 INTS5 9606 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:23904267}. UNIPROT Q6P9B9 UNIPROT Q8N6W5 UNIPROT Q9C0G5 Pfam PF14838 Pfam PF14837 OMIM 611349 Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}. P03372 EBI-78473,EBI-7600112 Q76MZ3 EBI-400413,EBI-7600112 E9Q512 EBI-11157440,EBI-7600112 Q96SY0 EBI-4409724,EBI-7600112 Q8IX90 EBI-1773976,EBI-7600112 P80315 EBI-772370,EBI-7600112 Q8BH65 EBI-11109879,EBI-7600112 Q9D1D4 EBI-6999360,EBI-7600112 Q9CY25 EBI-2553800,EBI-7600112 Q9D8B3 EBI-8322817,EBI-7600112 P67775 EBI-712311,EBI-7600112 P46013 EBI-876367,EBI-7600112 P01889 EBI-1046513,EBI-7600112 P60410 EBI-7600112,EBI-10171774 P30153 EBI-302388,EBI-7600112 A5YKK6 EBI-1222758,EBI-7600112 P32970 EBI-18539709,EBI-7600112 P35613-2 EBI-11037868,EBI-7600112 Q9UQV4 EBI-3924202,EBI-7600112 P49146 EBI-6655721,EBI-7600112 Q8WWB7-2 EBI-21518323,EBI-7600112 Q9UN75-2 EBI-21510478,EBI-7600112 O43493-2 EBI-21537762,EBI-7600112 Q8WVE6 EBI-10264837,EBI-7600112 Q9NS69 EBI-1047508,EBI-7600112 P08173 EBI-6655217,EBI-7600112 P40259-2 EBI-21668936,EBI-7600112 P01375 EBI-359977,EBI-7600112 P10909-2 EBI-16399180,EBI-7600112 GO:0005737 GO:0005829 GO:0016021 GO:0032039 GO:0016020 GO:0031965 GO:0005654 GO:0005634 GO:0034472 GO:0016180 GO:0042795 MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGVFDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYSGQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIISRVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDSLAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASGAGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNHVGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLARVHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALSPSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVSASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWGAPILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRGLLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKFIFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT 1019 Q6PBQ2 Charged multivesicular body protein 7 chmp7 7955 Yes SL-0178 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}. UNIPROT Q6PBQ2 UNIPROT Q6NYA6 Pfam PF03357 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}. GO:0000815 GO:0005635 GO:0010458 GO:0045324 GO:0031468 GO:0015031 MSVSVEKRSAWFPPDWDDDERMSFLFSAFKENRDVDCTDWDGKIDFWSPLIIEHCRRCGSVCVNLQDLNENFRRKGSVPLGLSTVIQSMIRSGKVQKESDFAANVDSGWLSWGVGLLLVRPLKWTLSALLGSGRVPLEESFVVIELVKEKAAELLAAYRGSALSARSLLSFQELRSLSSHICPDESTLCMALLQLQREKHVTVSLHEGEKLVKFSQAGQGRVSPVSEVDLGIYQLQCSEKLLEERVEALGHEAEKCKQQAKSLLKEGKKSQALRCLRGSKRVEKKADRLFAQLETVKGILDRIANSQTDRLVMQAYQAGVAALRISLKGVTVERAENLVDQIQELCDTQDEVNQTLASGAPDAGEDSEDLEEELKSLMEKSVPENDLFPAVPTHPITPPRKTDLPDAAFVQFLPSVPNPGMNITDEELDRELRRLTVSDKGLPRESVSPQRRLEPAQ 457 Q6PBT6 GTP cyclohydrolase 1 feedback regulatory protein gchfr 7955 Yes SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT Q6PBT6 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}. GO:0005737 GO:0005829 GO:0031965 GO:0005634 GO:0044549 GO:0009890 GO:0043105 MPYILISTQIRLETGPTMVGDEYSDPSIMNYLGARKITVLGNNFSEYHVDEPPRLVLDKLDKIGYRVVSMTGVGQTLVWCLHKESSNTL 89 Q6PEE2 CBP80/20-dependent translation initiation factor Ctif 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q6PEE2 UNIPROT Q6A069 Pfam PF02854 Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD) (By similarity). {ECO:0000250}. GO:0005829 GO:0048471 GO:0003723 GO:0008494 GO:0000184 GO:0006446 MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLTDKTEGDGESQRTQSHISQWTADCREQLDGSCSFSRGRAPPQQNGNKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGISLNDIEKVLPTWQGYHPMPHEAEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSGPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGSHRNAKETVTVENPKLEDGPGDTGHSGLEPPCSPDTLTPAASERPTPQLPGGPEAEIKHKDTVLPERLRERPKITLLQSSKDRLRRRLKEKDRDEVAVETSSPQPSKMDRLMEILNIMRNNSSDVDAKLTSFMEEAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA 600 Q6PFJ7 Sphingomyelin phosphodiesterase 4 smpd4 7955 Yes SL-0178 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}. UNIPROT Q6PFJ7 Pfam PF14724 Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000250}. GO:0005789 GO:0000139 GO:0016021 GO:0005635 GO:0046872 GO:0004767 GO:0050290 GO:0046513 GO:0046475 GO:0006685 MAASALQQPSYLLANLKADWTNKPLHQRCHELCKIIDDYPAKELHAIFPWLVECVFGSLDGILTGWNLRFLQARSAEYSIAMEFLDPSGPMMKLVYKLQAEEYKYEFPISYLPGPIKSSIHAGVLPDCPLFHNKIQFPMSGLLFLNPFEYYMFNFASSLIAPKNYPQGQHGSSSDSAYFVLVDTYLKYFLPTEGNVPPSPFSDTRGTVASPAPRSTNVPYVGYGGHSTSLLKRHITHQSSVNADPAAQEIWRSETLLQVFVEMWLHHYSLEMYQKLQSPQVKEPFMPSEEHVLVVRLLVKHLHTFSSSLKPESISSSPSAHSHSSPLEELKRVVVQRFVQQKLYVFLQHCFGHWPLDASFRAVLETWLSYIQPWRYTGDKNNTQTDGPNRTVPDKWASFVQENLLLYTKLFQGFLNRAMRTDLVNAKNALMVFRVAKVFAQPSLSEMIQKGEQLFLEPEHAILQRHNRVFLTPSHGGSFLSARQPMGTDNVFKVKSHVYSLEGQDCQYNLMFGPDQRKNVLKLIQIIAQARQTAKRISDHSTEMAANNSFLSWFGVGSPDHNSTFTGGEMDEMGGEGVKKTHEFLDKALDYLCQIFRLNAGQLSQLISNVASVDNNGASKQLPDCIPSENGLVLTDLGRLQIINGLRRFEIEYQGDPELQPIRSYENAFLVRLLFQISSFINERLGEHMEVLCSRQDFLGSVGRHYLSSSSAVVEQRRKSPVTRQMRDRPQRARLSLRALASYRTLLTLLLLYMLFALLSFGLFSSTGLILIISFLYELLSNFFHEKLKTH 791 Q6PFP6 NADPH-dependent diflavin oxidoreductase 1 ndor1 7955 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. UNIPROT Q6PFP6 UNIPROT Q5RL12 Pfam PF00667 Pfam PF00258 Pfam PF00175 PROSITE PS51384 PROSITE PS50902 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}. GO:0005829 GO:0048471 GO:0050660 GO:0010181 GO:0050661 GO:0003958 GO:0016491 GO:0016709 GO:0008219 GO:0036245 GO:0016226 MSGHTVLVLYGSQTGTAQDTAERIGRQAQRRRLRVKVEALDTYNVVNLISESLVVFVCATTGQGDPPDNMKKFWRFLFRKSLPADSLSRLDCAVLGLGDSSYPKFNFVAKKLHKRLLQLGANMLLPVGLADDQHDLGPDGVIDPWLLSFWQKTLSLYPPPAGLAPLREEDKLPPRYIFHFLSEVPNKLTEHLQTVDNKSSPTPLRPFPAPLVFNQRVTHTAHFQDVRHIEFDITGSNIEFSAGDTVMMRPCNTSEDVEQLCQLLKLDPESYFTLTPTDSSTEVPARLPQPCSIRFLLEHFLDISAVPRRSFFELLATFATDELEQEKLLEFSSAAGQDTLHSYCNRPRRTALEVLTDFPHTTAELSIGRLLDLFPEIQPRSFSIASSLLEHPNRIQILLAVVKYKTMLVKPRKGLCSSWLASLDPSKGDVYVPLWVKKGSLKFPQDPESPVIMVGPGTGVAPFRSAIQERVAQGKMANVLFFGCRSESKDFYCGSEWQEKVQAGQMILVTAFSRDQEDKVYVQHRVKEQGKLLWDLIAKKNAFFYIAGNAKQMPTSVCDALKAVFQKEGGMSENQAQEMLDGMEKNGRFQSETWS 595 Q6RKD8 Leucine-rich repeat transmembrane protein FLRT1 Flrt1 10090 Yes SL-0198 Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, neuron projection {ECO:0000269|PubMed:20421966}. Cell junction {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along neurites and at contacts between neurite termini and other cells (PubMed:20421966). Proteolytic cleavage gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}. UNIPROT Q6RKD8 UNIPROT Q14DT7 UNIPROT Q6RKD9 Pfam PF13855 Pfam PF01462 PROSITE PS50853 PROSITE PS51450 Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases (PubMed:16872596, PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length (PubMed:20421966). May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000305|PubMed:22405201}. GO:0005911 GO:0031410 GO:0030659 GO:0005789 GO:0005615 GO:0005925 GO:0005887 GO:0044306 GO:0032809 GO:0048471 GO:0005104 GO:0007155 GO:0016358 GO:0008543 GO:1990138 GO:0051965 MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKVQVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNHLSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLPSAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAAVVNVRGLMCQGPEKVRGMAIKDITSEMDECFEAGSQGGAANAAAKTTVSNHASATTPQGSLFTLKAKRPGLRLPDSNIDYPMATGDGAKTLVIQVKPLTADSIRITWKAMLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMVTMETGNTYVADETPVCAKAETADSYGPTTTLNQEQNAGPMAGLPLAGIIGGAVALVFLFLVLGAICWYVHRAGELLTRERVYNRGSRRKDDYMESGTKKDNSILEIRGPGLQMLPINPYRSKEEYVVHTIFPSNGSSLCKGAHTIGYGTTRGYREAGIPDVDYSYT 646 Q6SW81 Nuclear egress protein 2 NEC2 295027 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6SW81 UNIPROT D2K3L8 PDB 5D5N Pfam PF04541 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}. GO:0044201 GO:0016021 GO:0046765 MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCAVSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYENLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAGPRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHHRHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD 398 Q6TEL0 Myotubularin-related protein 8 mtmr8 7955 Yes SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}. UNIPROT Q6TEL0 UNIPROT Q7SZD1 Pfam PF06602 PROSITE PS51339 PROSITE PS00383 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}. GO:0005635 GO:0004708 GO:0052629 GO:0004438 GO:0004725 GO:0001568 GO:0014065 GO:0046856 GO:0010506 MEHIITPKVENVKLLNRYTEKKSALGTLYLTATHLIYVEQTSNTRKETWVLHHHILSVEKLLLTASGCPLLIRCKTFQHLHLLFQKERDCQDVYQSLLRLFQPVKEEELYAFLYNPHQNEEERRRGWELISVVNDFNRMGLSNDYWEISHINKNFEMCSTYPSILGLPKSASVATVTGSAKFRSRGRLPVLSYYHKDTKAAICRCSQPLSGLNSRCVEDEQMLQAISQANPNSPFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFQGIENIHVMRSSLQKLLEVCSMKSPSMSDYLTGLENSGWLRHIKSVMDAGVFLAKAVCEERASVLVHCSDGWDRTAQVCSLACLLLDPYYRTIKGLMVLIEKEWISFGHKFSHRCGHLDSDPKEASPVFTQFLECVWQLSQQFPCVFEFNEHYLIEIHDQVYACQYGNFIGNCQKERLDMRLHEKTFSLWPHLLENQHQYRNPLYRRSLESTVLRPSTLPLHFKFWCGMYNHYDRGMHPKQSVLDTLLTLTQRQVEGERTMTELQRQLAVADGVLPDPAGPINTHADQNNQSEKMPAPPVVQSNGSCAPLINGNVKEVGPGAENSNQEDREEPAANEHDLSSKDKPVFVETEHSKEEVQESS 632 Q6TVP7 Protein ORFV073 V073 647330 Yes SL-0382 Host nucleus {ECO:0000269|PubMed:28787456}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:28787456}. Virion {ECO:0000269|PubMed:28787456}. UNIPROT Q6TVP7 Plays a role in the inhibition of the host NF-kappa-B pathway early during infection. Prevents the host RELA subunit from reaching the nucleus and activate transcription. {ECO:0000269|PubMed:28787456}. GO:0042025 GO:0044220 GO:0019012 GO:0039644 MARRARFSPRLHIPAARAALGPHLHFPRRRLVLRHCGVRAFVGDAIVSKKEMTNPLCAQAIVFGNGFVETYVRSLDPRLLGAYHALSRPVCERPLFAVRGWRRLFPIVARRLDAVERRTRRVLRSMCRTYTTCMSADRAAAVSHPVMRRRWFGHRATKTRRARLRRRCRNRSSKRRAERRKRFCNYCP 188 Q6UDH4 Envelope glycoprotein M gM 670426 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6UDH4 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 MGNYYYGGQESRLERISWRMWMVEAACYIVLVLLTLVSSFASLSSTTGFPCFVGTVGESSFGGDLMGHGMTPARRDGVKIFFMSSPSTLFVVFSAVFVWLVVAVYLLLGGVRVKMCNFDSSYGASELSSAVATMTSLVTLSITAWAWQVFVLMLSYRQLTLAAVAFVGIFIAGLVFMLSFASGGKSPENYATFNSQLKTVCKDVHAVITAFKAVVLNLFCVVFGVWHLMLVMLGAVIMVLNFGVSIPKATTGALVVFIVLGLVYLMMIELVVSRYVHVLLGPHLGMIIALGIAGTSALSYAETLDEIMYASWKPVAAGILGAFSVIVLALAVLRAVRSYKFHKAAQSKFLQQVASVAQTVKNRARRERNGPRVHKRYYDAVPVDAYEDDPYRQSPRRSRHGEAEDVIYENMKY 413 Q6UDI5 Protein UL20 UL20 670426 Yes SL-0415 SL-0418 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}. UNIPROT Q6UDI5 Pfam PF04544 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}. GO:0044175 GO:0044178 GO:0044200 GO:0020002 GO:0016021 GO:0019012 GO:0019058 MADASAPDKKNAPTNALKPDLIKIAVERVLAAIDTENNEDLILAAAREPREVVAARAPDLFTSAAYSWSEEDELGTRMRASSFFPVASMFAKIICCLFLLWAKSCTGHGAMVTGLTACTGAYAIASLLCSFVVYYNVRTDNMPFGTYTKLFQIAACIGCGCYALGLTMEKLFGDSEMYFALFPDAKNSPLVGATAKGSALILPQGCSVAPYVPLAVSVAYCAAVVYDIADTIFPLLWVRTTLNEFAVF 248 Q6UDJ7 Nuclear egress protein 2 NEC2 670426 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6UDJ7 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}. GO:0044201 GO:0016021 MRSDKYSQLVSVVNAGLGACGTSATLVYIRNNARVAPTGDIITLPARLDGPPIPAEYILEAMTSLLSIRTAWLRIQNTGQAVIVAGCSTQNFHHGDVTWEPPASTVTLTTAKSLWVSASAVREMKVIQRIRTAPLAAMMFMCFYRGGKNEVTVRFAFYKSDSEPNLLKISKCVYEAIDAEATRNLPKPRGFDTPPCAVLAQRMRPLGAAEGGDRETSAQTHSPAAQAQHVMQHATATKSWGALGRTLKHKKNLGWILFTCALSLAAAFVTAYIK 274 Q6UDK0 Nuclear egress protein 1 NEC1 670426 Yes SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6UDK0 Pfam PF02718 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}. GO:0044201 GO:0016020 GO:0046872 GO:0046765 MSDVALKRNSSFFRAKARLTLLKRRDGGVISRSLEHRRSSRRRSSVSAPTRRVSGTLAKLGADDRRQFFDAFFRMTAVSPEETVSLLRSMTVPVIQQENISLPYDINAKFAPGDCISLSEMGYTLEMGGCCSLCSYGWSTTTPPELPALELAFMHHLSSVVEFKELVTSLRVCAGNSIVGNGAYENEGLLRMIKHLLEQSTLFYAYYTVKGGVSHDFRVLISEDGGGDGGSPAYAMYFVFKPGSPLHLGAKLIRQLIFNCPGYKWHADVHEGAFLLVVTRDRCSAIPEPRRVKLDPEDVYRRYCDVLVTEEKVHDYSRLYSTFSTYCPPASRREQTAAPATAKQV 345 Q6UW56 All-trans retinoic acid-induced differentiation factor ATRAID 9606 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:21723284}. Cell membrane {ECO:0000269|PubMed:17524364}; Single-pass membrane protein {ECO:0000269|PubMed:17524364}. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region (PubMed:21723284). UNIPROT Q6UW56 UNIPROT A8C1S2 UNIPROT A8K779 UNIPROT Q96FF6 UNIPROT Q96RT2 UNIPROT Q9Y2R7 UNIPROT Q9Y5L7 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 DisGeNET 51374 Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. {ECO:0000269|PubMed:21723284}. A0A0F7RH87 EBI-2811343,EBI-723802 Q93052 EBI-718388,EBI-723802 Q16236 EBI-2007911,EBI-723802 Q14145 EBI-751001,EBI-723802 GO:0016021 GO:0005765 GO:0005635 GO:0048471 GO:0005886 GO:0030154 GO:1903363 GO:0033689 GO:0030501 GO:0045669 GO:0010468 MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS 229 Q6UY62 RING finger protein Z Z 2169992 No SL-0382 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}. UNIPROT Q6UY62 Pfam PF03854 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}. GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0003723 GO:0008270 GO:0046761 GO:0039702 MGNSKSKSKLSANQYEQQTVNSTKQVAILKRQAEPSLYGRHNCRCCWFANTNLIKCSDHYICLKCLNIMLGKSSFCDICGEELPTSIVVPIEPSAPPPED 100 Q6ZMK1 Cysteine and histidine-rich protein 1 CYHR1 9606 Yes SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250}. UNIPROT Q6ZMK1 UNIPROT B3KSX0 UNIPROT D3DWM3 UNIPROT Q9BSF6 UNIPROT Q9BSU6 PROSITE PS50145 OMIM 616635 DE Reference Proteome: Yes; O00629 EBI-3908824,EBI-396343 P30838 EBI-3908824,EBI-3905126 P45984 EBI-713568,EBI-3908824 P61086 EBI-473850,EBI-3908824 GO:0005654 GO:0048471 GO:0008270 MAPKPGAEWSTALSHLVLGVVSLHAAVSTAEASRGAAAGFLLQVLAATTTLAPGLSTHEDCLAGAWVATVIGLPLLAFDFHWCTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCCRNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGSELMEILDGMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTLSFQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHFVFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLFQIQK 362 Q6ZMQ8 Serine/threonine-protein kinase LMTK1 AATK 9606 Yes SL-0198 Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10837911}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10837911}. Note=Predominantly perinuclear. UNIPROT Q6ZMQ8 UNIPROT O75136 UNIPROT Q6ZN31 UNIPROT Q86X28 Pfam PF07714 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 605276 DisGeNET 9625 May be involved in neuronal differentiation. {ECO:0000269|PubMed:10837911}. P04626 EBI-2008380,EBI-641062 P31689 EBI-2008380,EBI-347834 Q15078 EBI-746189,EBI-2008380 P51571 EBI-2008380,EBI-1054539 Q9UJS0 EBI-2008380,EBI-1222503 P62136 EBI-2008380,EBI-357253 P36873 EBI-2008380,EBI-356283 Q15293 EBI-2008380,EBI-948278 Q9NVI7 EBI-2008380,EBI-352007 P04792 EBI-2008380,EBI-352682 P68032 EBI-2008380,EBI-352273 O75746 EBI-2008380,EBI-1047585 Q9H936 EBI-2008380,EBI-1050588 Q96EY1 EBI-2008380,EBI-356767 P13674 EBI-2008380,EBI-1237386 O60762 EBI-2008380,EBI-719526 Q02978 EBI-2008380,EBI-359174 P53007 EBI-2008380,EBI-359163 Q96N21 EBI-11139477,EBI-2008380 GO:0016021 GO:0048471 GO:0005524 GO:0004674 GO:0004713 MSSSFFNPSFAFSSHFDPDGAPLSELSWPSSLAVVAVSFSGLFAVIVLMLACLCCKKGGIGFKEFENAEGDEYAADLAQGSPATAAQNGPDVYVLPLTEVSLPMAKQPGRSVQLLKSTDVGRHSLLYLKEIGRGWFGKVFLGEVNSGISSAQVVVKELQASASVQEQMQFLEEVQPYRALKHSNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLRSCRVAESMAPDPRTLQRMACEVACGVLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLAHCKYREDYFVTADQLWVPLRWIAPELVDEVHSNLLVVDQTKSGNVWSLGVTIWELFELGTQPYPQHSDQQVLAYTVREQQLKLPKPQLQLTLSDRWYEVMQFCWLQPEQRPTAEEVHLLLSYLCAKGATEAEEEFERRWRSLRPGGGGVGPGPGAAGPMLGGVVELAAASSFPLLEQFAGDGFHADGDDVLTVTETSRGLNFEYKWEAGRGAEAFPATLSPGRTARLQELCAPDGAPPGVVPVLSAHSPSLGSEYFIRLEEAAPAAGHDPDCAGCAPSPPATADQDDDSDGSTAASLAMEPLLGHGPPVDVPWGRGDHYPRRSLARDPLCPSRSPSPSAGPLSLAEGGAEDADWGVAAFCPAFFEDPLGTSPLGSSGAPPLPLTGEDELEEVGARRAAQRGHWRSNVSANNNSGSRCPESWDPVSAGGHAEGCPSPKQTPRASPEPGYPGEPLLGLQAASAQEPGCCPGLPHLCSAQGLAPAPCLVTPSWTETASSGGDHPQAEPKLATEAEGTTGPRLPLPSVPSPSQEGAPLPSEEASAPDAPDALPDSPTPATGGEVSAIKLASALNGSSSSPEVEAPSSEDEDTAEATSGIFTDTSSDGLQARRPDVVPAFRSLQKQVGTPDSLDSLDIPSSASDGGYEVFSPSATGPSGGQPRALDSGYDTENYESPEFVLKEAQEGCEPQAFAELASEGEGPGPETRLSTSLSGLNEKNPYRDSAYFSDLEAEAEATSGPEKKCGGDRAPGPELGLPSTGQPSEQVCLRPGVSGEAQGSGPGEVLPPLLQLEGSSPEPSTCPSGLVPEPPEPQGPAKVRPGPSPSCSQFFLLTPVPLRSEGNSSEFQGPPGLLSGPAPQKRMGGPGTPRAPLRLALPGLPAALEGRPEEEEEDSEDSDESDEELRCYSVQEPSEDSEEEAPAVPVVVAESQSARNLRSLLKMPSLLSETFCEDLERKKKAVSFFDDVTVYLFDQESPTRELGEPFPGAKESPPTFLRGSPGSPSAPNRPQQADGSPNGSTAEEGGGFAWDDDFPLMTAKAAFAMALDPAAPAPAAPTPTPAPFSRFTVSPAPTSRFSITHVSDSDAESKRGPEAGAGGESKEA 1374 Q6ZPJ0 Testis-expressed protein 2 Tex2 10090 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi- pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus- vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833, ECO:0000250|UniProtKB:Q8IWB9}. UNIPROT Q6ZPJ0 UNIPROT B1ATR1 PROSITE PS51847 During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000250|UniProtKB:Q8IWB9}. GO:0005783 GO:0016021 GO:0008289 GO:0006869 MTSLNGRHAEKTIDMPKPSAPKVHVQRSVSRDTIAIHFSASGEEEEEEEEEFRGYLEEGLDDQSIVTGLEAKEDLYLESQGGHDPAGPVSTAPADGLSVSESPAILPVSENTVKLLESPAPALQVLSPVPLALSPGSSSSGPLASSPSVSSLSEQKTSSSSPLSSPSKSPVLSSSASSSALSSAKPFMSLVKSLSTEVEPKESPHPPRHRHLMKTLVKSLSTDTSRQESDTVSYKPPDSKLNLHLFKQFTQPRNTGGDSKTAPSSPLTSPSDTRSFFKVPEMEAKIEDTKRRLSEVIYEPFQLLSKIIGEESGSHRPKALSASASELSSLSGLNGHLESNNYSIKEEEGDSEGEGYGSDSNTSRSDHLKPTEDASKEVEPKGSQASSLKDLGLKTSSLVLEKCSLSALVSKEDEEFCELYTEDFELETEGEGRLDKTLDLPLKPEVLASDGVALESEDEEDSATEHQELPVKTLGFFIMCVYAYLILPLPYYMSGLFLGVGLGFMTAVCMIWFFTPPSAHKHHKSLKALRHQSTRSLDIKEPEILKGWMNEIYNYDPETYHATLTHSVFVRLEGGTLRLSKPNKNISRRASYNETKPEVTYISQKIYDLSDSKIYLVPKSLARKRIWNKKYPICIELGRQDDFMSKAQSDKEATEEKPPPEKELPSEDLKKPPQPQEGTKSSQRDPILYLFGRTGREKEEWFRRFILASRLKSELRKPAGVSGSKSGLLPAHSRHSSPSGHLSHSRSSSKGSVEEMMSQPKQKELVGSVRQKMLLDYSVYMGRCVPQDNRSPHRSPVQSAESSPTASKKLPEAPPSEEEEQEAWVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLGKEPLVEALKVGEIGKEGCRPRAYCLADSDEESSSAGSSEEDDPPEPTAGDKQPLPGAEGYVGGHRTSKIMRFVDKITKSKYFQKATETEFIKKKIEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRIWYGFRKPPYVELKARPKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIPIMHSAMDPRSTSCLLKEPPVETSDQL 1128 Q6ZQH8 Nucleoporin NUP188 homolog Nup188 10090 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000305}. UNIPROT Q6ZQH8 UNIPROT Q4VA15 UNIPROT Q80UL4 UNIPROT Q8C7A1 UNIPROT Q8R3F1 Pfam PF10487 May function as a component of the nuclear pore complex (NPC). P52948 EBI-2554037,EBI-295727 P62826 EBI-2554037,EBI-286642 Q5SRE5 EBI-2554037,EBI-1049404 P78406 EBI-2554037,EBI-724495 O15294 EBI-2554037,EBI-539828 Q8WYU3 EBI-2554037,EBI-2555238 B4DYZ6 EBI-2554037,EBI-2562666 Q99567 EBI-2554037,EBI-726178 O14980 EBI-2554037,EBI-355867 P14618 EBI-2554037,EBI-353408 Q8N1F7 EBI-2554037,EBI-1042703 Q92878 EBI-2554037,EBI-495494 P62847 EBI-2554037,EBI-354515 Q9BRJ2 EBI-2554037,EBI-2514313 E9PJN9 EBI-2554037,EBI-10969856 Q567V2-2 EBI-2554037,EBI-10969860 P35658-4 EBI-2554037,EBI-10966398 Q5T0N5-3 EBI-2554037,EBI-4403262 O95373 EBI-2554037,EBI-286735 Q9BXS6-2 EBI-2554037,EBI-10969852 Q9HCN8 EBI-2554037,EBI-2339921 Q9H5Q4 EBI-2554037,EBI-1043912 GO:0044611 GO:0017056 GO:0051028 GO:0006606 GO:0006405 MAAAAGGPCVRSSRELWTILLGRSALRELNQIEAELNKYWQRLLEGLSYYKPPSPSSAERVKANKDVASPLKELGLRVSKFLGLDEEQSVQLLQCYLQEDYRGTRDSLKTVLQDERQSQALTLKIADYYYEERTCILRCVLHLLTYFQDERHPYRAEYADCVDKLEKELVLKYRQQFEELYRTEAPTWETHGNLMTERQVSRWLVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFKEQGFGSRQTSRHLVGGTMDPFVDRIGYFSALILVEGMDIESLHKYALDDRRELHQFAQDGLICQDMDRAMLTLGDIPHHAPVLLAWALLRHTLSPEETSSVVRKIGGTAIQLNVFQYLTRLLRSLASGGNDCTTSTACMCVYGLLSFALTSLELHTLGNQQDVIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELHKHKPHDVLSHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQHCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVNVIASCVNCLTVLAARNPAKVWTDLRHTGFLPFVAHPVSNMTQMISAEGMNAGGYGSLLMNSEQPQGEYGVTIAFLRLVTTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHKWRYNSHGVRELIGCLILELIHAILNLCQETELHSSHTPSLPSLCICSLAYTEAGQTVISIMGIGVDTIDMVMAAQPRSDGPEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALTQHGAHGNNLIAVLAKYIYHRHDPALPRLAIQLLKRLATVAPMSVYACLGSDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSNGSKEFSLGVWSCLHVVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSVLETCALIMKIICLEIYYVVKGSLDQSLKDTLKKFSSEKRFAYWSGYVKSLAVYMADTEGSSCTSLLEYQMLVSAWRILLIIAASHADVMHLTDMAVRRQLFLDVLDGTKALLLVAASVNCLRLGSMMCTLLLILLRQWKRELGAVEKILGPLTEILEGVLQADQQLMEKTKAKVFSAFITVLQMKELRVGDIPQYSQLVLNVCETLQEEVIALFDQTRHSLASDSAAEDKDSMETDDCPRPRHKDQRDGVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEAALHLLLTLARTQQGATAVAGAGITQSICLPLLSVYQLSSNGTGQTPSTSRKSLDAPSWPGVYRLSMSLMERLLKTLRYNFLTEALDFVGVHQERTLQCLNAVKTVQSLACLEEADHTVGFILQLSHFRKEWHFHLPQLMRDVQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVTPRAQRPSTTTTTTTTTTALATPAGCSSKQPTADTEASEQRALHTVQYGLLKILSRTLAALRHFTPDVCQILLDQSLDLAEYNFLFALSFTTPTFDSEVAPSFGTLLATVNVALNMLGELDKKKESLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAVRYLRDPAVHPRDKQRMKQELSSELSTLLSSLSRYFRRGAPSSPAAGVLPSPQGKATSLSKASPESQEPLIQLVQAFVRHVQR 1759 Q6ZRP7 Sulfhydryl oxidase 2 QSOX2 9606 Yes SL-0178 SL-0182 Membrane {ECO:0000269|PubMed:14633699}; Single- pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single- pass membrane protein {ECO:0000305}. Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane. UNIPROT Q6ZRP7 UNIPROT A2CEE0 UNIPROT A6NLB0 UNIPROT Q5TB37 UNIPROT Q7Z7B6 UNIPROT Q86VV7 UNIPROT Q8N3G2 Pfam PF04777 Pfam PF18371 Pfam PF18108 Pfam PF00085 PROSITE PS51324 PROSITE PS51352 OMIM 612860 DisGeNET 169714 Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. {ECO:0000269|PubMed:14633699}. P05161 EBI-746466,EBI-11127401 Q99614 EBI-11127401,EBI-742074 Q5VYS8 EBI-11127401,EBI-2810086 Q9C0F1 EBI-11127401,EBI-744115 Q8IZH2-2 EBI-11127401,EBI-10965083 Q86YS7 EBI-11127401,EBI-1051086 Q12824 EBI-11127401,EBI-358419 Q9UBD5-2 EBI-11127401,EBI-10962124 Q6ZNJ1-3 EBI-11127401,EBI-11028033 F8VY35 EBI-11127401,EBI-10968005 Q9P2X3 EBI-11127401,EBI-2857352 Q9Y6K0 EBI-11127401,EBI-1237183 Q8TB52 EBI-11127401,EBI-2556210 P0DTD1 EBI-25475871,EBI-11127401 Q8IWL3 EBI-1805738,EBI-11127401 Q20MH8 EBI-12576433,EBI-11127401 P20036 EBI-2802853,EBI-11127401 Q9NRD5 EBI-79165,EBI-11127401 GO:0005623 GO:0005615 GO:0005794 GO:0030173 GO:0031965 GO:0005654 GO:0005886 GO:0016971 GO:0003756 GO:0045454 GO:0006457 MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKGPDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNNKMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQHYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPGAHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV 698 Q6ZWR6 Nesprin-1 Syne1 10090 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres (By similarity). {ECO:0000250}. UNIPROT Q6ZWR6 UNIPROT Q8K3T7 UNIPROT Q9ERT7 UNIPROT Q9ERT8 Pfam PF00307 Pfam PF10541 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS51049 Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus- centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenenis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786}. Q9D415 EBI-400152,EBI-10760754 P83510 EBI-7280013,EBI-10760754 Q62108 EBI-300895,EBI-10760754 GO:0005623 GO:0005737 GO:0043197 GO:0044327 GO:0005794 GO:0016021 GO:0034993 GO:0030496 GO:0005635 GO:0031965 GO:0005640 GO:0005730 GO:0005654 GO:0000932 GO:0048471 GO:0045211 GO:0030017 GO:0005819 GO:0003779 GO:0051015 GO:0019899 GO:0042802 GO:0005521 GO:0042803 GO:0005102 GO:0051642 GO:0090286 GO:0007030 GO:0042692 GO:2001054 GO:0061886 GO:0090292 GO:0007097 GO:0002053 GO:0048260 GO:1902017 GO:0048814 GO:1903353 GO:0099149 GO:0007283 MATSRASSRSHRDITNVMQRLQDEQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKIKLVNINATDIADGRPSIVLGLMWTIILYFQIEELTSNLPQLQSLSSSASSVDSMVSTETASPPSKRKVAAKIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPEDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDGQEDDVVFVGFTNNIALLLGFQRDDRLILKETKVWIEQFERDFTRAQMTESSLQDKYQAFKHFRVQYEMKRKQVEHIIQPLQRDGKLTLDQALVKQCWERVSSRLFDWHIQLDKSLPAPLGTIGAWLYRAEVALREEITIQQVHEETANTIQRKLEQHKDLLQNTDAHKRAFHEIYQTRSVNGIPMPPDQLEDMAERFHFVSSTSELHLMKMEFLELKYRLLSLLVLAESKLKSWIIKYGRRESVELLLQSYISFIENSKFFEQYEVTYQILKQTADIYVKAEGSVEEAENVMKFMSEATAQWRNLSVEVRSVRSMLEEVISNWDRYGDTVASLQAWLEDAEKMLSQSEHAKKDFFRNLPHWIQQHTAMNDAGNFLIETCDEIVSRDLKQQLLLLNGRWRELFMEVKQYARADEMDRMKKEYIDVTTTLFGFATEAHRKLSEPLEVSFINVKLLIQDLEDLEKRVPVMDAQYKMIAKKAHLFAKESPQEEANEMLTTMSKLKEQLSKVKECCSPLLYEAQQLTVPLEELETQITSFYDSLGKINEILSVLEQEAQSSTLFKQKHQELLASQENCKKSLTLIEKGSQSVQKLVTSSQARKPWDHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAQEGLEEKGDPEELLRRHTEFFSQLDQRVLNAFLKACDELTDILPEQEQQGLQEAVRKLHKQWKDLQGEAPYHLLHLKIAVEKDRFSAAVEECRAELEQETKLAPQEGSEKIIKEHRVFFSDKGPHHLCEKRLQLIEELCGKLPVQDPVRDTCGACHTALKELKASIDNTYTMLVDDPDKWKDYTSRFSEFSSWVSAKKACLKKIKDEPIDTGNHDEVKHMVDEIRNDITKKGESLSWLKSRLKYLIDISSENEAQKRGDELAELSSSFKALVALLSEVEKLLSNFGECVQYKEIVKSSLEGLISGPQESKEEAEMILDSKNLLEAQQLLLHHQQKTKMISAKKRDLQEQMEQAQQGGQAGPGQEELRKLESTLTGLEQSRERQERRIQVSLRKWERFETNKETVVRYLFQTGSSHERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKEAAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTMEMVKSKWDHFGSNFETLSIWILEKENELSSLEASASAADVQISQIKVTIQEIESKIDSIVGLEEEAQSFAQFVTTGESARIKAKLTQIRRYWEELQEHARGLEGTILGHLSQQQKFEENLRKIRQSVSEFAERLADPIKICSSAAETYKVLQEHMDLCQAVESLSSTVTMFSASAQKAVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALFSVASKEDVAVMKLQLEQLDERWGDLPQIISKRMHFLQSVLAEHKQFDELLFSFSVWIKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAQDLHPLQSKVDDCFQLFEEASQVVERRKLALAQLAEFLQSHACMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESSAISLDGTLTKAQCHLKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMDRERLKVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRRQIHENQGQCCGLIDLVREYQSLKSTVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSKQKELDSFTSKGKHLLSELKKIHSGDFSLVKTDMESTLDKWLDVSERIEENMDMLRVSLSIWDDVLSRKDEIEGWSNSSLPKLAENISNLNNSLRAEELLKELESEVKIKALKLEDLHSKINNLKELTKNPETPTELQFIEADLRQKLEHAKEITEEARGTLKDFTAQRTQVERFVKDITAWLINVEESLTRCAQTETCEGLKKAKDIRKELQSQQNSITSTQEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQARIQDSLEKHFSGSMKEFQEWFLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQSKLDVVTQEGQTLYAHLPKQIVSSIQEQITKANEEFQAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTENLGESKHHISEKKNEVRKVEMFLGELLAARESLDKLSQRGQLLSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKDVQDRLACAESTLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLEMLKKAWAEAMNSAVHAQSTLESVIDQWNDYLEKKSQLEQWMESVDQRLEHPLQLQPGLKEKFSLLDHFQSIVSEAEDHTGALQQLAAKSRELYQKTQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKDHLMYLDAVQEFADWLHSAKEELHRWSDTSGDPSATQKKLLKIKELIDSREIGAGRLSRVESLAPAVKQNTAASGCELLNSEMQALRADWRQWEDCLFQTQSSLESLVSEMALSEQEFFGQVTQLEQALEQFCTLLKTWAQQLTLLEGKNSDEEILECWHKGREILDALQKAEPMTEDLKSQLNELCRFSRDLSPYSEKVSGLIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKITTAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLNTMLFKGELLSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKESALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNRLYDLPAKRREQQKLQSVLEEIQCYEPQLHRLKEKARQLWEGQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEHNRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLKLEALLSVRQEKEIQMKMVVTRGEYVLQSTSLEGSAAVQQQLQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALGKAKLLNEEVLSHSSLLETIEVKRAAMTEHYVTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSVHEGDTNAHETMLRDLQELQVRCAEGQALLNSVLHTREDVIPSGLPQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEKINFRSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEEVGTRAQGILDETHISSRMGCQATQLTSRYQALLLQVLEQIKFFEEELQCLEETESSLSSYSDWYGSTHKNFKNVATKIDKVDESMMGKKLKTLEVLLKDMEKGHSLLKSAREKGERAMKFLAEHEAEALRKEIHTYMEQLKNLTSTVRKECMSLEKGLHLAKEFSDKYKVLAQWMAEYQEILCTPEEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQSLKDKIQKLQSDFQDLCSRAKERVFSLEAKVKDHEDYNTELQEVEKWLLQMSGRLVAPDLLEMSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHLQAKQKQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDTLQQCQAWISAVQPDLKPSPQPPLSRAEAVKQVKHFRALQEQARTYLDLLCSMCDLSNSSVKNTAKDIQQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDADQQLQNMKRRHTELEINIAQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKNQESPEHKEITHLNDQWQDLCLQSDKLCAQREQDLQRTSSYHDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYAIDDLKDCKQKLIEQLGLDDRELVREQTSHLEQRWFQLQDLVKRKIQVSVTNLEELNVIQSRFQELMEWAEEQQPNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLKSLMKDADRVMADLGLNERKVIQKALSEAQKHVSCLSDLVGQRRKYLNKALSEKTQFLMAVFQATSQIQQHERKIVFREYICLLPDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLVSRKHFKEDFDKACHWLKQADIVTFPEINLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLSEKLSALPQQFNVIVALAKDKFYKTQEAILARKEYTSLIELTTQSLGDLEDQFLKMRKMPSDLIVEESVSLQQSCSALLGEVVALGEAVNELNQKKESFRSTGQPWQPEKMLQLATLYHRLKRQAEQRVSFLEDTTSVYKEHAQMCRQLESQLEVVKREQAKVNEETLPAEEKLKVYHSLAGSLQDSGILLKRVATHLEDLSPHLDPTAYEKAKSQVQSWQEELKQMTSDVGELVTECESRMVQSIDFQTEMSRSLDWLRRVKAELSGPVCLDLSLQDIQEEIRKIQIHQEEVLSSLRIMSALSHKEQEKFTKAKELISADLEHTLAELQELDGDVQEALRTRQATLTEIYSRCQRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTEGQFHSNMEELRGLVARLDPLIKATGKEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVIELMNDAEKKLSEFAVLKTSSIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQEKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLLESHDTYLMDLESQQLTLGVLQQRALSMLQDRAFPGTEEEVPILRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYLGNPTIEIDTQLEELKRLLAEATSHQESIEKIAEEQKNKYLGLYTVLPSEISLQLAEVALDLKIHDQIQEKVQEIEEGKAMSQEFSCKIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELHQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKAKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQHLANVYCTGKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLCHRQHLLSEMESLKPKMQAVQLCQSALRIPEDVVASLPLCHAALRLQEEASQLQHTAIQQCNIMQAKKHSLIFPPKEAVVQYEQYKQEMKHLQQLIEEAHREIEDKPVATSNIQELQAQISLHEELAQKIKGYQEQIDSLNSKCKMLTMKAKHATMLLTVTEVEGLAEGTEDLDRELHPTPSAHPSVVMMTAGRCHTLLSPVTEESGEEGTNSEISSPPACRSPSPVANTEAAVNQDIAYYQALSAEGLQTDAARIPPSAAVSQELYEPGLEPSATAKLGDLQRSWETLKNVISEKQRTLYEVLERQQKYQDSLQSISTKMEAMEMKLGESLEPSRSPESQMAEHQALMDEVQMLQDEINGLQVSLAEELVAESQESDPAEQLALQSTLTVLAERMSTIRMKAAGKRQLLEEKLSDQLEEQRQEQALQRYRCEADELDHWLLNTKATLDVALGTSQEPMDMDAQLVDCQNMLVEIEQKVVALSQLSVHNENLLLEGKAHTKEEAEQLAVKLRLLKGSLGELQRALHDRQLDMQGVTQEKEENDVDFTDTQSPGVQEWLAQARTTRTHQRQSSLQQQKEFEQELAEQKSLLRSVASRGEEILTQHSTAEGSGGLGEKPDVLSQELGIAEDQMRVKWESLHQEFSAKQKLLQNILEQEQEQVLYSSPNRLLSGVLPFRGEAQTQDKTSVTSLLDGLSQAFGEASSQSGGTDRQSIHLEQKLYDGVSATSTWLNDVEERLFVATAPLPEETEACLFNQEALAKDIKEMSEEMDKNKNLFSQAFPEDSDNRDVIEDTLGCLLGRLSLLDSVVDQRCHQMKERLQQILRFQNDLKVLFTSLADSKYIILQKLANVFEQPIVEQMQAIQQAEEGLRDLEGGISELKRWADKLQVEQSAVQELSKLQDMYDELLMTVSSRRSSLHQNLALKSQYDKALQDLVDLLDTGQEKMTGDQKIIVCSKEEIQQLLGKHKEYFQGLESHMILTEILFRKIVGFAAVKETQFHTDCMAQASAVLKQAHKRGVELEYILEMWSHLDENRQELSRQLEVIENSIPSVGLVEESEDRLVERTNLYQHLKSSLNEYQPKLYQALDDGKRLLMSVSCSELESQLNQLGEHWLSNTNKVSKELHRLETILKHWTRYQSEAAALNHWLQCAKDRLAFWTQQSVTVPQELEMVRDHLSAFLEFSKEVDAKSALKSSVTSTGNQLLRLKKVDTAALRAELSRMDSQWTDLLTGIPVVQEKLHQLQMDKLPSRHAISEVMSWISLMESVILKDEEDIRNAIGYKAIHEYLQKYKGFKIDLNCKQLTADFVNQSVLQISSQDVESKRSDKTDFAEQLGAMNKSWQLLQGRVGEKIQMLEGLLESWSEYENSVQSLKAWFANQERKLKEQHLLGDRNSVENALKDCQELEDLIKAKEKEVEKIEQNGLALIQNKREEVSGSVMSTLQELRQTWISLDRTVEQLKIQLTSALGQWSNHKAACDEINGHLMEARYSLSRFRLLTGSSEAVQVQVDNLQNLHDELEKQEGGLQKFGSITNQLLKECHPPVAETLSSTLQEVNMRWNNLLEEIAEQLHSSKALLQLWQRYKDYSKQCASAIQRQEEQTSVLLKAATNKDIADDEVTKWIQDCNDLLKGLETVKDSLFILRELGEQLGQQVDVSAAAAIQCEQLCFSQRLGALEQALCKQQAVLQAGVVDYETFAKSLEALEVWMVEAEGILQGQDPTHSSDLSTIQERMEELKGQMLKFSSLAPDLDRLNELGYRLPLNDKEIKRMQNLNRHWSLTSSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEHKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIVDGQNLLEQGQVDDREEFSLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLAEVSHLPLSGLGNIPVPLQQVRMLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELTDIQEKWKAASMHLEEQKKKLAFLLKDWEKCERGIANSLEKLRMFKKRLSQPLPDHHEELHAEQMRCKELENAVGRWTDDLTELMLVRDALAVYLSAEDISMLKERVELLQRQWEELCHQVSLRRQQVSERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAVAQENKIQLQEMGERLAKASHESKASEIQYKLSRVKDRWQHLLDLMAARVKKLKETLVAVQQLDKNMGSLRTWLAHMESELAKPIVYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSACSLRQMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKLIRLPVRLPDDHDLSDRELDLEDSTALSDLRWQDPSADGMPSPQPSSNPSLSLPQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESASRTLPSEDEEGEEDKEFYLRGAVGLSGDPSSLESQMRQLDKALDDSRFQIQQTANILRSKTPTGPDLDTSYKGYMKLLGECSGSIDSVRRLEHKLAEEESFPGFVNLNSTETQTAGVIDRWELLQAQAMSKELRMKQNLQKWQQFNSDLNNIWAWLGETEEELDRLQHLALSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDLQDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEMSHALLLMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVIGNRLKLLLKEVSHHIKDLEKLLDMSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKSPRGKCSLSQPGPSVSSPKSRSTRDGSDSSRSDPRPERVGRAFLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPPL 8799 Q709R6 LEM domain-containing protein Bocksbeutel bocks 7227 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:24700158}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Note=Detected in the nucleus envelope and cytoplasm. In the cytoplasm, it appears to localize to discrete foci. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}. [Isoform A]: Nucleus, nucleoplasm {ECO:0000269|PubMed:15035436}. Cytoplasm {ECO:0000269|PubMed:15035436}. Note=Predominantly expressed in the nucleoplasm with very low expression levels in the cytoplasm. {ECO:0000269|PubMed:15035436}. [Isoform B]: Nucleus inner membrane {ECO:0000269|PubMed:15035436}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:15035436}. Note=Appears to be predominantly expressed in the nucleus envelope but expression is not uniform. Outside of the nucleus it is located to discrete foci which may be the endoplasmic reticulum. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}. UNIPROT Q709R6 UNIPROT Q8SZZ5 UNIPROT Q9VHA7 Pfam PF03020 PROSITE PS50954 Inner nuclear membrane protein (PubMed:15035436, PubMed:24700158). May have a role in maintaining the structural integrity of the nuclear lamina (PubMed:24700158). During pupal development, plays essential and redundant functions with the other LEM domain proteins; MAN1 and Ote (PubMed:24700158). Also has a redundant but important role with Ote in larval development (PubMed:24700158). {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:24700158}. Q7JR34 EBI-182405,EBI-93986 Q06559 EBI-114639,EBI-93986 Q9VVQ1 EBI-93986,EBI-173837 Q9VLU0 EBI-105147,EBI-93986 O01666 EBI-159423,EBI-93986 Q9VC86 EBI-174235,EBI-93986 O76454 EBI-87224,EBI-93986 GO:0005737 GO:0005783 GO:0016021 GO:0005635 GO:0005637 GO:0005654 GO:0007049 GO:0051301 MSDLSYLDTLGNKELLAKCLEHGLPGVPVTDSTRSVIIRRLKAKITGVPLNKSKSASKKAIPRRETVHGSQVTTPTSEPVRRTPGKSAGRTSSNNNKISEQSRRTIAYGLDNTSISGRSVQTTTTVSDMSSQSEDDDSYMVDSPVPNYSKDQQPRRYVSLAKSGVLTTSYTREVDQPLYEQEDIPRSYTYERPHVPAATLHALPTYEPRIEPSTYRPTDLGFSRPLLTQTNLNSTSYEESSTYNPKLSPISPRNTFSGSARPFGGPAPAPAPIRQRQSVPVSGSNLARGRLLQPTTAVNTLYPQLNEFYDQPNDAGEPMETESESEVEEVPINSHFQKNRFSPLARKPLVRHHDQVSPMAQFRALAVSLDQKYNLKFYLILVVSVMLATMVYVVLTPNA 399 Q70IA6 MOB kinase activator 2 MOB2 9606 Yes SL-0198 Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15067004}. UNIPROT Q70IA6 UNIPROT B4DKP3 UNIPROT Q96M67 Pfam PF03637 OMIM 611969 DisGeNET 81532 Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000269|PubMed:15067004}. P35610 EBI-6621955,EBI-2558739 Q7KZN9 EBI-3248549,EBI-2558739 P06493 EBI-444308,EBI-2558739 Q96H96 EBI-20304109,EBI-2558739 Q9Y2H1 EBI-991501,EBI-2558739 Q9H8S9 EBI-748229,EBI-2558739 Q7L9L4 EBI-2558745,EBI-2558739 P05549-1 EBI-2558739,EBI-9678982 Q91VJ4 EBI-2527046,EBI-2558739 Q15208 EBI-458376,EBI-2558739 O95562 EBI-4402330,EBI-2558739 P10644 EBI-476431,EBI-2558739 Q8K0Q5 EBI-8586076,EBI-2558739 Q9NRY4 EBI-766200,EBI-2558739 Q3KRB8 EBI-25411786,EBI-2558739 A0A024R136 EBI-25411891,EBI-2558739 A6NKK0 EBI-23725364,EBI-2558739 Q6NZ36-4 EBI-12013806,EBI-2558739 Q86VR2 EBI-10192441,EBI-2558739 Q5JXC2 EBI-2801965,EBI-2558739 Q9GZT6 EBI-713148,EBI-2558739 Q70Z53 EBI-710176,EBI-2558739 Q9NT62 EBI-988094,EBI-2558739 Q96ST8 EBI-2799206,EBI-2558739 Q96HA8 EBI-2558739,EBI-741158 GO:0005829 GO:0044306 GO:0005730 GO:0005654 GO:0048471 GO:0046872 GO:0030036 GO:0010976 GO:0001934 MDWLMGKSKAKPNGKKPAAEERKAYLEPEHTKARITDFQFKELVVLPREIDLNEWLASNTTTFFHHINLQYSTISEFCTGETCQTMAVCNTQYYWYDERGKKVKCTAPQYVDFVMSSVQKLVTDEDVFPTKYGREFPSSFESLVRKICRHLFHVLAHIYWAHFKETLALELHGHLNTLYVHFILFAREFNLLDPKETAIMDDLTEVLCSGAGGVHSGGSGDGAGSGGPGAQNHVKER 237 Q70KF4 Cardiomyopathy-associated protein 5 Cmya5 10090 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes. In skeletal muscles, localizes along myofiber periphery, at costameres. Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. In the mdx mouse model for Duchenne muscular dystrophy, exhibits a discontinuous localization at the myofiber periphery with extensive regions devoid of CMYA5. This highly irregular pattern is associated with an increased cytoplasmic localization, particularly in discrete foci within myofibers. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}. UNIPROT Q70KF4 UNIPROT Q70X91 UNIPROT Q9CV01 UNIPROT Q9CV02 UNIPROT Q9ER93 UNIPROT Q9ER96 Pfam PF00041 PROSITE PS50188 PROSITE PS50853 May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration. Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle. {ECO:0000269|PubMed:17499862, ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:28740084}. Self EBI-782290,EBI-782290 Q91WZ8 EBI-782290,EBI-643186 GO:0043034 GO:0031430 GO:0005634 GO:0048471 GO:0016529 GO:0042802 GO:0070885 GO:0032515 GO:0014733 MESGDSGLAAQGFLGWGADEEVAQELETEEESEGEGEETAAESEEEPDARLSDEDEEGKTKQECIVSDPSFSMVAVQREDSGITWETNSSRSSTPWASGESQTSGICSLEGSALTSPPGSVSFIMDEVKRTRKRTQKSKRGSPSLRRKGSKKRNSLESQDVLTNQEDGPSISESPVLNIENEKSSIGTYDKTRRKKTASNTPPITGAIYKEHKPLVLKPVYIGTVQYKIKMFNSVKEELIPLQFYGTLPKGYVIKEIHYRRGKDSSISLEPDLSNGGSNIVPQRKLAQSPEEDKVRELAPPWRGALSKGSRTSLFSHEEQKKTYADSNLNVPSSTEHAFPSSARNDTADQEENLSLPQMMPQQPADESKTHRMEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFEPDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPIVHREEEHAPEPIVHREEEHAPEPESIVHREEEHAPESIVHREEEHAPEPVPIVHREEEHAPEPESIVHREEEHAPEPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPESIVRKGEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPMVLREEHAPEPIVRREEEHAPEPIVHREEEHAPEPMVHRKAQQLERGVETSTPITDITEPEDSSLEEEIIELDYPESPLASKETSPSPLSPEVEHRKEPILPTQMTFTPERITLSEEEREENESVSTDSAFVSEYSVLQDLNHTPEKLEVEAVSVSDVKSSNEPAVFSEDDEERESYSPAMTSVSEQSLSPSTTEKTSAIQSPLFSTVSPVLSGDEASENVCHSPESESAAEYSVPAHAQELLLKTGDHKLPLKSQRVSEPIIQAEDEKEDIGLLPPAALSQAVLSEDESLGSGSFASDSKLPFKPSVSQNATRESPQKTIDDMPQFKPRGLSDPATLLEEEKEAIGVGLSSSNEVSAVECALPPQTTELLSESHAPPPWAISSEQVVQSEEGSRDQQRGSFSSTPELGHTSLLLKGASSPTGLSEQGQEEDNIGPLSPDSAFASEFSFSPYPTQELEKRELGRDSPLCLTSPSEQTVLSEEDTEEADLFSPDSASQVSIPPYRIAETEQNKVEPDELLPTRSAPDYPYFSEADEEEAGSSVVTLVPEHSEPSQEREESSPCRPVFEDLSLPPSADKTGQAETMSDVPTISTSVSEYLILARQAKTQASLEPEAEDLVPPPTSGWEKRDAKSSLPAVTIAASSSALSSVVKEETTSVLPTSQPSVSPESTCVLKPEQEPTAPLTLTSADEQMALPRVGREKAVLDSQEATAHKSQDQTPEPRLPNVPGSGMKYSVLSDLGDEPKADVKLNLAPTVTSELEQRMLSKNEPEVAKPHSPPEETSISGPKVLSAVKTEVKQESKITRELPAASSGRERGAEHSPPVPPALPALTEETGKDTEASSSATTVPVTKLDSNSTKLGRDEVLTDPSLASPVEHPGLKGIGKSELGSGLPLPSMSASEVLRPEPKLPVNSGVEVEREDNEPPPLQVSPTSKPTVPNDKHEEITRSPDSENLVSDDLAPTLLAFRHEMNRQAEETSSPVPGSFLSGEQELIKLPPEPEKHKQLSEVPTAGSELIDSRDRDRSLGIEPVKPIGTEPGPSILEKGPAELQRRGKEQEENRKLPVPASAPLETASFDLPIEQKEPKRTLHEGQAVEVPDESSSSADKPELGVKQLAEKKENLEQPKPFVTTERASVTGSKVKESLISPKDNIWMLEKPDGLVNQHEDRKPGTGQLESSESTDLMSEKLGAASLDTDHTSETRNQETSKAPVSGEKLSQEPRRVQSKAVDDSEEGRKLASGNVEVLTQSKSVPAVKAKATPQPPETPEVTQKPSEKSLVTEQGLPAEKGKKGISSFKSWMSSLLFGSSIPDSKVSDNEDLETRPGPSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPKGVSVKSSISQDLKEKLTFLSNEDVLKQPKSNSENYGQKELPGFSEGMGESLATSVGDKHPGIHPCSPMGEKVGMEEAQNMAPLHITESQRRQKPEVSPPSMWNISARKEEPSSDHKETWLSSSDVVDRMPQKPKSAQSAFTRMNSEEPASMILPVESKGSLSDLGEDRLRQEMPKPTSLEHCEEEVERPTEEKDGWETRSFSLAGKRGLAEKQEIMAPLELRENEAVGELQRMPESRPFKLEESKAAERLEQRISPTEKLMEKPSKTLALDRREKEVQEWVFSEGEKQEYPPAAMPVPGASAVSLDKAQPHLLAKPTPVVEKPEHIVTEVYPEIRERKAAETQPHPQEEGKTLVEKTKVSRVESPHGEETDGHSLTQEGNLELEKSGESRVDLKEERRRFVMPELPLGASVAAEDGSVQPRPLSKDAARASDMTDETKHLGTPPTQPSAVEPQTLVLGTSVEHAVKKQETWSDRPTVHTFQTSKDDTEEMLKQSVLISKHHLEAVEDVHRNEPPSSAASNYAQFMLSASEISADGVPPMGGTAQEPEGTSVKDEEFSVTSKPAGLSEDQKSAFSIISEGCEILNIHAPAFIPSVDQEESEQMQDKLQYLEEKASFKSISVHDEKKAAASHKTQKSKLEVPDRKITSLKENKTKETHKTKEEIATDSGMGDFTPIQPTVSGEEDYFEKYTLIDYNLSPGSGKQKSTVEESSEEATKTLTSFPESSAEQALDHEYNLVKLDESFYGPEKDDSKLSHAEMQKSLAIQKPDDRNAPKGISRDVDSRSPGMPLFDVEEGVLSKRQIFPTTPKAVNPELLEEPPALSFFYKDLYEGACGEKNEGETASEGDSVDSETSFPRRHSDTDDGPGMYFEKYILKDDILHDESVTQEDQGQGLEEKPVGEEDSQQLRVAEREIRRKPETSFWEKNLEEQHKVVGREGEPTGHMETLDEAAMQQKAPITEQVRAVTQKMSYAVPFQDTRCVLESEPSSQGNEAGNASPDVNLNVPVQVSFPEEESAAGATYAPEVLQERLVPSVSREERLHNTPVQDEYDFVGSLNQEAASQAILPEEPGSESSPKEVLSQGSESFEHIREQELTSEGEPRMSASQEVWDRTEDQSARESVTAKTQKEPKKTQAESYCYTCKSLVSEMDKALDIHKDHEVSALDTAISAVKVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQMVHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAMESTASLENMPAAFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPSSATSTTIAVYWSVNKEDVVDSFQVYCVEEPQDDQEINELVEEYRLTVKESCCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIHVEDCTVCWNTATVRWRPANPEATETYTLEYCRQHSPEGEGLRSFSGIKGHQLKVNLPPNDNYFFYVRATNASGTSEQSEAALISTRGTRFLLLRETAHPALQISANGTVISFSERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPGRCTLHLGLEPPDSVRHK 3739 Q719N1 Spastin SPAST 9823 Yes SL-0198 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}. UNIPROT Q719N1 UNIPROT F1S3Z2 Pfam PF00004 Pfam PF17862 Pfam PF09336 PROSITE PS00674 ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP- Rule:MF_03021}. GO:1904115 GO:0005813 GO:0005783 GO:0005768 GO:0016021 GO:0005874 GO:0030496 GO:0031965 GO:0005634 GO:0048471 GO:0005819 GO:0043014 GO:0005524 GO:0016887 GO:0048487 GO:0016853 GO:0008017 GO:0008568 GO:0008089 GO:0019896 GO:0007409 GO:0032506 GO:0031122 GO:0006888 GO:0010458 GO:0090148 GO:0008152 GO:0001578 GO:0051013 GO:0000281 GO:0051228 GO:0031468 GO:0031117 GO:0034214 GO:0051260 MNSPGGRGKKKGSGGPSSPVPPRPPPPCLASSRPAPRPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSRAAPAPASASPPAPVPGGEVERVRAFHKQAFEYISVALRIDEDEKVGQKEQAVEWYKKGIEELEKGIAVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPVLQFSKSQMDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHPSNSLPRSKAIMKTGSTGLSGHHRAPSCSGLSIVSGMRQGPGPTTATHKSTPKTNRTNKPSTPTTAPRKKKDLKNFRNVDSNLANFIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLRERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARLTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV 616 Q71F54 E3 ubiquitin-protein ligase SH3RF1 Sh3rf1 10116 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:16571722}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}. UNIPROT Q71F54 Pfam PF00018 Pfam PF14604 Pfam PF00097 PROSITE PS50002 PROSITE PS00518 PROSITE PS50089 Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway (PubMed:12514131). Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:12514131}. Q920M9 EBI-957514,EBI-957526 GO:0005829 GO:0005794 GO:0030027 GO:0048471 GO:0005078 GO:0046872 GO:0061630 GO:0006915 GO:0043066 GO:0043154 GO:2001237 GO:0001764 GO:0046330 GO:0051865 GO:0043370 GO:2000564 MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRPWKPGPGGGGSTTCTNVLRAQGSTVVNCGSKDLQSPQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAAQSSSASKHSDTKKNTRKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPTDVPYQAALGTMNPPLPPPPLLATTVLASTPSGATAAAVAAAAAAVAAGVGPRPAVGSTEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQASRGVTMVSPSTAGGPAQKPQGNGVAGNPSVVPTAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAACIGPASVGLPHHSLASQPLPPMVGPAAHIAAVNINRTSVPLACAAGASSLASPNMTTAALETEPSGRTVTILPGLPTSPESAASACGNSSAVKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGSGEVPLQGAVGPELPLGGVHGRVGSCPTDGDGPVAAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI 894 Q750Y9 UDP-N-acetylglucosamine transferase subunit ALG14 ALG14 284811 Yes SL-0178 SL-0182 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}. UNIPROT Q750Y9 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVGYTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVVLFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV 224 Q751U7 Spindle pole body component KRE28 KRE28 284811 Yes SL-0178 SL-0182 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}. UNIPROT Q751U7 Pfam PF17097 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}. GO:0000777 GO:0005737 GO:0031965 GO:0005816 MSTKDTSGQSGYANDIRKLGEQTAHVSEQVLVQQERQRLGALEELHQSIIQIAEENSFVTPIKKDAANVHIDPRGIAVSVQQFKQLAEVLKVTHLEQETLDNFLRYTISDNDQLLDIKSVADSRYARLAEEVCQLEQEELRHLENEIISLNGNITEQTTKVIDANEKVKEECLEVSNGIERCWGLLNELETLRSTTDEGNVELGPLEETYQKWKSVDHFLQQKLHLKEQLRVLEDTRKSLSEVTKSSGNRAPDLDASEKFVTYRLLDSMWKKQFVDTTKIRDLELYPRTGKIQFQVADTIYVLAISGDQISNIQLFNDKLPAADLENNTQDLNKRFLGTSDVRRVVDFITHQQAVPQAQVH 361 Q753I3 CTP-dependent diacylglycerol kinase 1 DGK1 284811 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q753I3 CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. Involved in pre-tRNA splicing (By similarity). {ECO:0000250}. GO:0000139 GO:0030176 GO:0031965 GO:0004143 GO:0006654 GO:0016192 MANEEELQTAESAFVTGARRYSNDYSESESSSKHSGCSTPVEGTPAEAATTIGARASGGSTTWQRLRQLLMERGSDVHLPVTEIHLKSQEWFGDFITKHEVPRKVFHSSIGFFTLALYVRDVDYRNVRLPLIVGFVHVLLLDVIRLHWPAFNTLYCQVTGLLMRKKEVHTYNGVLWYLLGLIFAFSFFSKDVALVSLFLLSWCDTAASTVGRLYGHLTPRISRNKSLAGSLAAFVVGVISCAVFYGYFVPAYSHVNHPGEIMWNPETSRLSLVQLSLLGGFVASLSEGIDLFNWDDNFTIPVLSAIFMHTIIAFSQR 317 Q755A9 Monopolar spindle protein 2 MPS2 284811 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. UNIPROT Q755A9 Pfam PF17060 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}. GO:0005737 GO:0016021 GO:0031965 GO:0005816 GO:0071988 GO:0030474 MWREEAREQLRRGRCCFAAASVVSTAKHNKSLGNCTHGSGVMTEAEGILNNVWDAVDSKQQGFIYAKDMPDLVGRFGQFLAQSLTSRANDEAIAAFASEKPFYKLDKEQFKSTFQTLVGTSLQTAVELAGHGEPRPRLFGAIRRASATGDEQAREELERKSAELSRVRDELDEWKSKYQFLEREFLFYQTHHENSVDSTQHEFIISEMKRTIEEQTRMIGQLRRQVQGGTQVLARAGKRASPVDVFMYVSRQGLLLLMRMPKAAFLLLLLGYFVWYTVMGGAVQGPDPSVALPEPPKQPWWEQNNIISALYWYLTDTFEPSQRINDTVNDNYNSLFGL 338 Q759K4 Nuclear rim protein 1 NUR1 284811 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q759K4 Pfam PF10332 Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 GO:0043007 GO:0007096 MPKHHTFATKLEDLVLTSMSFRMSKHQAHPIEPEDVIREESEDFYSDEEEYKETWSRWALQLLSSSPYDLYLIVNENFESINWDLKAKTLARPLGGTMTFLFFTVRLLQDNVIKPNYHKINRTTDGFDFSRSATLREYDYFSKYQHGASWSSANWRVNSLSILDTLLKCLYILLLVSNSVLTYKFLFGYFLKYSLFHSAQPPASNNLTKKSLHDLAYRSATDVSRGSLWTLIRYTFFQRGRVQEEKPTDEFYYEIKKWCPSSFLTALFASFPPISVWFMAFSDITFVSLLPVILTQYLFWYVIFDCYEDRIKDELAIFKGMAAEYNNKVMKPKLSAQTQDAMVDATMYGQEFVQFYPSYSTARSGVFITHSLCGDVIKEKYNQRTKAFEDIPTGSHSQNIIRYSRNERLYHSVFPQNPLKKINGAAMSVNPMSFNRSPTYGGRYGTPPSRSHGSGQTYSSTSAPTSPMLKNRRAIPTDHSTGGNISGGNYVEYTSNDVHGEPPRRHSTSPLKRDITSSAGREDNHLAFGVNSPNIRSRTVDVKKNLHTHTTVVCPKSDLDTSQLSSKQSSISPFKLSRRGSIESRPPFR 589 Q759Y0 Nuclear fusion protein KAR5 KAR5 284811 Yes SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q759Y0 Pfam PF04163 Required for nuclear membrane fusion during karyogamy. {ECO:0000250}. GO:0005789 GO:0031301 GO:0031965 GO:0000742 GO:0048288 MLEILLFLCVIIQRSHINAEITHVVSHLAETALRQDTNFQLLSQDIIAKKFPILDSSCVRRALSDFLPQCLQYGFETVPSDVRTQAAVKLSICELQASGVDNMPPECVGAVHFGACLRAMERTPQWWTTYSGNYQHLPSTCFENALPYEKEQLLSLFLNITDVYSNFQDDLVVDLEKYRANFEATVEASLRLMKASLMEGTHEIVNQLKDDLNYVNSKLADMGETITEHTDNVRTVFNDISDELNDYDMAGQIAHLKEDTMSLWQKINSDMGTYHDVQMSSLYNINAVFDTFYNRATESVQQVRTSVIESQLETLDLIADFNSLVRKSILPVLADELQPQLQEMSVSISRSLVGLSASYNEHLQAWSNRVNETLSEMESHLNNTMSQVEHMNDSIETLENKVFVLVSLGNALTTYVKWIYTFSRALISGYGIVTLIMSMLVVRYSIKLNSSWIKVLGRSTFILVAVVLGARTGSMLSY 478 Q75JT4 Metabotropic glutamate receptor-like protein J grlJ 44689 Yes SL-0178 Cell membrane {ECO:0000269|PubMed:17501984}. Membrane {ECO:0000269|PubMed:17501984}; Multi-pass membrane protein {ECO:0000269|PubMed:17501984}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17501984}. Golgi apparatus membrane {ECO:0000269|PubMed:17501984}. Nucleus envelope {ECO:0000269|PubMed:17501984}. Note=May also localize to internal membranes. UNIPROT Q75JT4 UNIPROT Q559S6 Pfam PF00003 Pfam PF02608 PROSITE PS50259 May act during the development and be a negative regulator. {ECO:0000269|PubMed:17501984}. GO:0005789 GO:0000139 GO:0016021 GO:0005635 GO:0031090 GO:0005886 GO:0004930 GO:1902610 GO:0031153 GO:0030587 GO:0030435 MKILLYIAIILSFFSLITISSECKIAVLLSGSPNDLGYNYLMNEARVKAESELKLDFSIYYENLEESMEEAEKAFQDALHKGANLIVVGSFVHVGLGLKYAALTKDQDIYWIIRGNKRPNPDLPHVVILNFNSFELHYLLGYFSGLMTKTGIVGFVAPGPDVNTISTDNSFYLGAKYARPNITFLNVYVQSWYNPNVSYSAAKMLIKNGADLIGMSQDDMSCQKAMMDSGLIGIGATGYPTHLLFGGNVGVSYITNWTNLYVKYAQHVLNDDWPDYSSYFTNLSREDSIFIDDYSYKVPIDIQNLVNDEIQRLKNTSYIPYRSDPYLAQLGIPFDSKGLLVEDQFRANKKLLKGDSISKVIDFGQYSIPIEFIDYPNSLKYGVTIVSGVCIFICLVCMTLVVVFKKARVIKSSSPAFLLLILLGCCIIFAACILFAQSPTNQTCSARIWLLSLGYTLFLGNLLVKNWRIWLLFDNPKLKKRAITNWKLYPWVFAILAIDVMILAIWQGLGNINAESRIGYDSLTQYQYKNVCSSDDQGSIALYLLLVFHGLVLLVACFISFKIKVVDIEEFNESKPITTSVYIITFCLFIVIPLMVSPQSLTSQTTIICVCAIVTTLISMLLLFGSKFYKMATQGLAINETFATSTKSSSKSSKSSYGKDNPNPNAINFGEDDTSDETSEEKHKSPKQKSVNFSNKSNSHLAVFTSDEETSKTSKLSIDFENSSKDISIDQLQQQKQQPINTNGDLENKSNDKIDDDNDNSSVLSKRISNQQNGETEIDSNNV 783 Q75LD5 Probable ion channel CASTOR OSJNBa0032G11 39947 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q75LD5 UNIPROT Q10AR8 Pfam PF06241 Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}. GO:0016021 GO:0031965 GO:0006811 MPLDPDSSPAPPHRDWFFPPAPPFLPSSRARTPRAPFPSTSRSSNPYSFPDRRPPPTPRSRSRSPLPPPEQQKQQQPPPTTPPPAPRRRDPRYAGVRRGDVRTLTAEKAAAAAAVPTAAQVHGSKSAASATTLRWSGMVSVAAIVLCFSSLVRSNSSLHDQVHHLKAQLAEATTKLQSCITESSMDMSSILSYQSNNSTSQNRGLKNFSLLLSLSTLYAPLLILKYMDLFLKLRSSQDSEEEVPINKRLAYRVDIFLSLQPYAKPLVLLVATLLLIGLGGLALYGVNDDSLLDCLWLSWTFVADSGNHANAEGFGPKLVSVSISIGGMLVFAMMLGLVTDSISEKFDSLRKGRSEVIEQSHTLVLGWSDKLGSLLNQIAIANESLGGGTIVVMAEKDKEEMEADIAKMEFDLKGTAIICRSGSPLILADLKKVSVSKARAIVVLAEEGNADQSDARALRTVLSLTGVKEGLRGHIVVELSDLDNEVLVKLVGGDLVETVVAHDVIGRLMIQCARQPGLAQIWEDILGFENCEFYIKRWPQLDGMQFEDVLISFPDAIPCGIKVASYGGKIILNPDDFYVLQEGDEVLVIAEDDDTYAPAPLPKVMRGYLPKDFVVPKSPERILFCGWRRDMEDMIMVLDAFLAPGSELWMFNDVPEMDRERKLIDGGLDFSRLENITLVHREGNAVIRRHLESLPLESFDSILILADESVEDSAIQADSRSLATLLLIRDIQAKRLPFREAMVSHVTRGSFCEGSWIGEMQQASDKSVIISEILDPRTKNLLSVSKISDYVLSNELVSMALAMVAEDRQINDVLEELFAEQGNEMQIRPADLYLREDEELNFFEVMLRGRQRKEIVIGYRLVDAERAIINPPDKVSRRRWSAKDVFVVITEKE 893 Q769K2 N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D Napepld 10116 Yes SL-0178 Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}. UNIPROT Q769K2 Pfam PF12706 Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of these bioactive fatty acid ethanolamides (FAEs), including anandamide (N-arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (PubMed:14634025, PubMed:16527816). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (By similarity). {ECO:0000250|UniProtKB:Q8BH82, ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816}. GO:0005737 GO:0005829 GO:0005769 GO:0031901 GO:0005794 GO:0000139 GO:0043227 GO:0005635 GO:0005654 GO:0042802 GO:0102200 GO:0070290 GO:0004620 GO:0008270 GO:0007568 GO:0048874 GO:0070291 GO:0070292 GO:1903999 GO:0009395 GO:0006644 GO:0090336 GO:0050729 GO:0035900 GO:0001659 MDENENSQSPAPSHQYPKETLRKRQNSVQNSGGSESSRLSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNVSIPNVLRWLIMEKDHSSVPGSKEELDKELPVLKPYFISDPEEAGVREAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDVQAKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLKSEDFFILKHGESRYLNTDDKAFEET 396 Q76L40 RNA-directed RNA polymerase RNA1 649895 Yes SL-0382 [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}. UNIPROT Q76L40 Pfam PF00548 Pfam PF00680 Pfam PF00910 PROSITE PS51874 PROSITE PS50507 PROSITE PS51218 [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}. GO:0044165 GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003723 GO:0003724 GO:0003968 GO:0018144 GO:0006351 GO:0039694 MDSETIDMCVKFLKISFGLQSLKNLVKELFGGSELEKLAYVHAAFFHANEMAIHWNADLPWEEVMSSKRIKERFGYVKSHFLRNVVYNADASGQMIRYNTTTCEQWFCCNFNLASYSASYNSLVPEEGGSMPINEEAEIKIGQSLLTCAQSVTKAIYAKLSTLTTRSIQGFLECLRDAICGAFSSWLPCIRGAFAWFGNIIEVLKHWAGAAHEKLHNFLEGIEECLYMGLGLVASTCIVALIEKFLVTMSVISGPCGRPTLFLTSAMAIISSTYLLSKAVEKSSAFTMLLGFVTQSCQTVLGSLFGKSAKGSEEAQGQFGPSAMLESLATLVSSWSSSSVTEIGRTFGAISQIKNGIIALKDMALFVFSKLCEMASKVLGFESQILADLSIILGENVADWLDECDCMLAYLLEFNSNARDIFDRLSQLIEKGKAIRMGILRTTHRGPSQVLSLVTKALDKLTELHNSVIMSGANSTRKTPFMLFFTGKSGVGKTSVVQRMAANWLQQEQLGSNEVYSRNGLDPFWSGYKRQAVVTYDDFGAVPGSVSNEAEIINVVSSNPHSVMMADLKEKGMYFDSRLIIASSNFLAANPESGVHDSEAYERRRHVVVQVSLKEDMAYDPGNPCANQRYTLLESKAPFAEKAVFESYEELWSHVYNAFKAHEEKEKLFLSSLPIPERSEKEALQALIGICVMTTSYAPKAVIQYGIDHLVGYHYLISSAEHVYFWHEKGEVEIVPMHLMKLDKMDKATMASTSLKSALMCQDMAKNFPTLNPLAVLYAKNIVIRGWVDANLQASKKCEDSYMREQIESLPKWQRAYLHVLSGHIASNETRGWFLNCLEVTKSNSRSSYIWEYKSWPMPLKLALGSFLAILAGSAIFCSLQSLWSISGNASFVAGAASIFTIGSATAQSAPPNKDGSEYTYRNKKIKIRNWEGQGPCFGDSALWIAENCMATLVVMKDRVQVCMAPGRSFLGVNHFLRMIPNGVMVKLETGMTETYFVWEKSKLKLFENSEIALYTSSNLPKAPDSLVDRFHFDLETLPKTFPAQFFTYKFDKDMQQYVPELGELLCKKAERALCVVSGEYRRVISHHLTYRNPTVAGDCGGLVLAIIEGKCKLVGLHVASDGEEGAASPVPWDPDFKVAQGQSDFLLSYDEWAVPKVLGPGCKAVGIISPEHTVGSGGKTSFLETPIEWQLNRPCGKIPSILVKGDVRLAGTENADYDPFAVGMTKYAKEAGPFEPNGLDRVCESIAETWHDASDGFEFGPVDLEAALNGIENMEYFDALVLSTSEGYPYRLDRKPGEKGKARYVEGEPGNLEITDERILADIHWFEEISKTQVPDLYCIECVKDERLPVRKVIKEPKSRLFTVLPMSYNLAIRKKFLNFVRFIMKRRDVLPCQVGINPYSRQWGKVADRLLEKGNSILCCDYSRFDGFLPKCIMVKIAEMFSNIVGETGAEREQTKNLMLACCSRYAICGRVLYRVENGIPSGFPLTVIVNSILNEILIKYAYWKCFETESLIRDHFDTYVAMVVYGDDNLISVSEAISSKFNGNFLVNFMCNLGIKVTDGVDKTKVGIEFRTIEDCDFLKRKFKENADGTWSGVMAEEHLWPQLHFVKAKKVEMSEAYISNCNNILRELWLGSPEKAAAFRREVISKLKWVEPQRLLTISQVALFHNEQMNGEHPFVEACHQLENLELMAPLEPGMLPIKTQEIMPGLFVASEKNFTGNFDDYFTISITTNRKFEDGKGFQIIFPYGAGRGGLPSKAFMEQNVIRKGCAIQKAFKQGLEKGNKMLFISQSSVIPAYVFAIMLYRSVDRLPRALSNKALTSALGICKKLSYLPKDFPDLF 1842 Q76P29 Importin subunit alpha-B DDB_G0272318 44689 Yes SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q76P29 UNIPROT Q55A47 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. GO:0005829 GO:0005643 GO:0005654 GO:0061608 GO:0008139 GO:0006607 MQRSKQETRKSQYKKSIDSDESRRKREEASLSIRKNKREESLLKKRTQAVPGSTPVKVDSLINQRLEQLPSLVAEINSENPDLILKSTTAFRKLLSIEKSPPIEEVIKTGIVPRLVKFLYMQDFPQLQFEAAWALTNIASGTPEQTRVVIENGAIQVFVLLLSSPHDDVREQAVWALGNIAGDSHYCRDLVLSHNALPPLLSLLQNPAAIKVSMVRNATWTLSNFCRGKPQPPFEIVRASLPVLAKLIYYQDEEVLIDACWALSYLSDGSNERIQEVIDAKVCRKMVELLGHPTIAVQTPALRTIGNIVTGDDNQTQIVLSVQALSHLLNLLQSPKRAIRKEACWTISNITAGDKNQIQQVIDANIIPSLVYLLANAEFEIQKEAAWAISNATSCGTPQQIHFLVSQGCVKPLCDLLKVSDPRIINVALEGIENILVAGKKEAQVTGVNPYKKIIEDADGLGKIYDLQHHMNKDTFEKVSRIISTYLEDEQEDEGDLMPEGSSFSFSNQTNSNFNL 516 Q77MS4 Protein UL20 homolog MDV032 10389 Yes SL-0415 SL-0418 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}. UNIPROT Q77MS4 Pfam PF04544 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}. GO:0044175 GO:0044178 GO:0044200 GO:0020002 GO:0016021 GO:0019012 GO:0019058 MSKHGFGYYATEANEYTIPLDDIDDGRSDTDAKTLGSVLTQLSEEVDWDDAVDYATMSSYLGDYVFTIPNSYDIHPKFTRYVVLFGLSTFVLRPSCCLIFLFYAIYAQDNRFLILGTTITAFFYGTLMLEMYYMYANIKYDLMPLSKFQQVLIGALSMLGPIIFVAISYNMIFKDVTFMKKILAFDTNLKTSGFVIYLVMIASLAYSITSISDAIGFLLPRLWTRAVLKSCVPF 234 Q7JRE4 Inner nuclear membrane protein Man1 MAN1 7227 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:16439308}; Multi-pass membrane protein {ECO:0000269|PubMed:16439308}. Cytoplasm {ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308}. Note=During anaphase and metaphase, detected in the nuclear envelope and spindle poles. {ECO:0000269|PubMed:16439308}. UNIPROT Q7JRE4 UNIPROT Q961B2 Pfam PF03020 PROSITE PS50954 Inner nuclear membrane protein (PubMed:16439308). Acts as a negative regulator of the BMP (Dpp) signaling cascade during crossvein development in pupal wings and possibly during synaptic transmission at the neuromuscular junction (NMJ) (PubMed:18723885, PubMed:20036230). Appears to be required for pupal development and consequently transition to the adult stage (PubMed:18723885, PubMed:20036230). During pupal development, plays essential and redundant functions with the other LEM domain proteins; bocks and Ote (PubMed:24700158). {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:20036230, ECO:0000269|PubMed:24700158}. P18431-3 EBI-242176,EBI-3415366 GO:0005737 GO:0012505 GO:0016021 GO:0005637 GO:0005654 GO:0000922 GO:0003676 GO:0001525 GO:0030514 GO:0006997 GO:1902531 MSTESLNSLSDKELHRKLIQSGFPSTPVTETTRAVLIEKLRKHTRADKLKKRSNKYVLYSKEQQESPPFPQYHQYHAPQPPQNYANGLDNNNDLDQTGGSSAYNRSLDESDSSPLQLSASKMYAPPPVVASNYDGDCSPHSLGLNGKYLQPCSMPYAIDTSNNYGKPSGKAKLSDGGVVNRLLSFRDTTIQRKFNYPTGQASRIPLRKERLTRFALSDLKSFIRNPDIRPYVIPRVLISLFLIFLTIITVLYVGKRFEQSPIDKAALKYTLCNPNDMQMISEKVNCIEKDSLRGALDMSEELFRHLNERARLHHCKDANLSPALEIGEFVREMVSNPKTHRGNLHSNLMAAKYLITENPQWSIQVVDSTKHLGQTSHFELSEPNLPLKCIVLKKVTRFFTVIGALLLIVAGFLIVYVAVVIYRVKQKEALLAVDQFQKDIINELIYLSSQSESPEVVINQLQEKFLPAKKRSKLLSSWNKALKQLEKNDSRVLFGMVNRDGKAMRTIAWNRNVDKKDVGLVKKWQSPAFDNSNKIANPPTPCLKIRHMFDSSEVDQANLKQSIVESIIEKVGTRCKICDVQLDVQSCCVYIRCASEEDAGTIHKEINGWWFDKRLISIKFLRLERYLSRFPKPSAEPLYFHTNEAANTHS 650 Q7JXF5 Nuclear pore glycoprotein p62 Nup62 7227 Yes SL-0178 SL-0185 Nucleus {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:26341556}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:7641726}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin (PubMed:20144760). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760}. UNIPROT Q7JXF5 Pfam PF05064 Essential component of the nuclear pore complex (By similarity). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein- protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity). Binds to transcriptionally active genes (PubMed:20144760). Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154 (PubMed:26341556). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}. P17886 EBI-127204,EBI-108202 Q9W053 EBI-127204,EBI-87615 Q7KW14 EBI-127204,EBI-101492 Q9VF74 EBI-127204,EBI-208005 Q9GYU8 EBI-127204,EBI-161961 Q9VSF3 EBI-127204,EBI-96764 Q9V6B9 EBI-127204,EBI-179307 Q9VVB4 EBI-127204,EBI-94400 Q9VDS5 EBI-127204,EBI-176038 Q9VBM3 EBI-127204,EBI-83994 Q9VDK2 EBI-127204,EBI-87444 Q9VG59 EBI-127204,EBI-194851 Q9VBJ9 EBI-127204,EBI-147550 Q9VBH0 EBI-127204,EBI-171538 Q8T414 EBI-127204,EBI-95177 Q9W4H1 EBI-127204,EBI-107424 Q9VP67 EBI-127204,EBI-113469 Q9VIY1 EBI-127204,EBI-151825 Q9VYT1 EBI-127204,EBI-103162 GO:0000785 GO:0005737 GO:0005815 GO:0005635 GO:0044613 GO:0000922 GO:0031490 GO:0005543 GO:0017056 GO:0097240 GO:0051028 GO:0030717 GO:0006606 GO:0097298 GO:0006405 MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLGSGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAASTTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQINAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQLKQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF 394 Q7K0D8 Nuclear pore complex protein Nup50 Nup50 7227 Yes SL-0178 SL-0182 SL-0185 Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:20144760}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O08587}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Associates with chromatin (PubMed:20144760). UNIPROT Q7K0D8 Pfam PF08911 Pfam PF00638 Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta- cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation (PubMed:20144760). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000250|UniProtKB:Q9UKX7, ECO:0000269|PubMed:20144760}. Q4V5M2 EBI-193476,EBI-194571 Q9VWE4 EBI-194571,EBI-122539 Q9VD47 EBI-194571,EBI-144988 Q9VSK1 EBI-194571,EBI-148683 P40798 EBI-194571,EBI-88209 P52295 EBI-145898,EBI-194571 Q9W0Y8 EBI-194571,EBI-105939 Q9VJ53 EBI-194571,EBI-122209 GO:0000785 GO:0031965 GO:0005643 GO:0005654 GO:0005704 GO:0031490 GO:0035080 GO:0051028 GO:0045944 GO:0006606 MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKPAASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPTTSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEESARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTASFTAPVPSSSSIFSLTAKPTGEAKSDDTPKSSIFSFGAKDTTTKKDEPNFSAPKTNGFSFGLKSNNDDKPSTSLFAGFGKAPGGAGDGAKGFSFTNSATPFSLGNIHPPAAAAAPAEEEKEEDTPPKVEFKQVVEDDAIYSKRCKVFIKKDKDFGDRGVGTLYLKPVKDSEKIQLLVRADTNLGNILVNLILSKGIPCQRMGKNNVLMVCVPTPEDSKATSLLLRVKTGDEADDLLEKIKEHIK 564 Q7K2X8 Nucleoporin seh1 Nup44A 7227 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:21521741}. Lysosome {ECO:0000269|PubMed:25512509}. Note=Enriched on the nuclear envelope of nurse cells, oocytes and syncytial embryos (PubMed:21521741). In egg chambers detected in lysosomes and autolysosomes of both fed and starved females (PubMed:25512509). {ECO:0000269|PubMed:21521741, ECO:0000269|PubMed:25512509}. UNIPROT Q7K2X8 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 Probable component of the nuclear pore complex (NPC) (By similarity). Involved in maintaining the localization of another nucleoporin Mtor to the nuclear envelope of early meiotic female germline cells (PubMed:21521741). It is not involved in recruiting the nucleoporins Mtor, Nup107, Nup153 and FG-containing nucleoporins to the NPC (PubMed:21521741). {ECO:0000250|UniProtKB:Q96EE3, ECO:0000269|PubMed:21521741}. An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823, PubMed:23723238). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823, PubMed:23723238, PubMed:25512509). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation growth under nutrient replete conditions and growth during female oocyte development (PubMed:21521741, PubMed:25512509, PubMed:23723238, PubMed:27166823). This component is required for activating TORC1 specifically in germline cells to promote cell growth and maintain the oocyte fate, probably influences the organization and/or function of microtubules within ovarian cysts, and promotes accumulation of another GATOR2 complex member mio in germline and somatic tissues (PubMed:27166823, PubMed:23723238, PubMed:25512509, PubMed:21521741). GATOR1 and GATOR2 act at different stages of oogenesis to regulate TORC1 in order to control meiotic entry and promote oocyte growth and development (PubMed:25512509). After exactly four mitotic cyst divisions, the GATOR1 complex members (Iml1, Nprl2 and Nprl3) down-regulate TORC1 to slow cellular metabolism and promote the mitotic/meiotic transition (PubMed:25512509). At later stages of oogenesis, the mio and Nup44A components of the GATOR2 complex inhibit GATOR1 and thus activate TORC1 to promote meiotic progression, and drive oocyte growth and development (PubMed:21521741, PubMed:25512509). In addition to its role in the regulation of the TORC1 complex, functions independently of TORC1 to prevent the inappropriate accumulation of autolysosomes in germline tissues (PubMed:27166823). {ECO:0000269|PubMed:21521741, ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25512509, ECO:0000269|PubMed:27166823}. Q9VH77 EBI-118041,EBI-116084 GO:0044754 GO:0061700 GO:0005764 GO:0005635 GO:0031080 GO:0032991 GO:0035859 GO:0005198 GO:0051301 GO:0034629 GO:0034198 GO:0007293 GO:0051321 GO:0010507 GO:0048477 GO:0010508 GO:0045793 GO:0032008 GO:1904263 GO:0015031 GO:0051445 GO:0007346 MFDVEPIIADHKDVIHDVVFDYYGRRMATCSSDQTVKIWDEDGQGKWNVTSSWKAHSGSIWRVSWAHPEFGQVVATCSFDRTASVWEEVIGEKVSSTNTPTRRWVRRTTLVDSRTSVTDVEFAPKYLGLLLATASADGIIRIYEAPDIMNLSQWPVQHEISNKLPLSCLSWNTSTYMVTQLLAAGSDEAATPTGKVFLFAYSENSRKCVKIDTVNDITDPVTDVAFAPNAGRTFHMLAVASKDLYIVNLRGVTDATDISKLDIQTIKFSEHNCPVWRVCWNMLATMLISTGDDGCVRLWRMNYNRQWRCAAVLKAEGSGPTYEPAPPTPTLATTASATAKFYKKGTIGNQVPWH 354 Q7L576 Cytoplasmic FMR1-interacting protein 1 CYFIP1 9606 Yes SL-0198 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}. UNIPROT Q7L576 UNIPROT A8K6D9 UNIPROT Q14467 UNIPROT Q5IED0 UNIPROT Q6ZSX1 UNIPROT Q9BSD9 UNIPROT Q9BVC7 PDB 3P8C PDB 4N78 Pfam PF07159 Pfam PF05994 OMIM 606322 DisGeNET 23191 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. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). May act as an invasion suppressor in cancers. {ECO:0000250|UniProtKB:Q7TMB8, ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}. Q5S2C4 EBI-1048143,EBI-1547830 Q9Y2A7 EBI-389845,EBI-1048143 Q38919 EBI-1048143,EBI-1548187 P06730 EBI-73440,EBI-1048143 P63073 EBI-2000006,EBI-1048143 Q5S007 EBI-5323863,EBI-1048143 Q13557-8 EBI-11534483,EBI-1048143 P03372 EBI-78473,EBI-1048143 Q9NYB9 EBI-743598,EBI-1048143 Q8WUW1 EBI-2837444,EBI-1048143 Q9P2E7 EBI-9202518,EBI-1048143 Q13200 EBI-357648,EBI-1048143 Q8K2C9 EBI-8329978,EBI-1048143 Q15773 EBI-1048143,EBI-1051875 Q9UIM3 EBI-719882,EBI-1048143 P62873 EBI-357130,EBI-1048143 P47872 EBI-3914358,EBI-1048143 Q15029 EBI-357897,EBI-1048143 Q9Z1B5 EBI-2552918,EBI-1048143 Q921T2 EBI-2552485,EBI-1048143 P50221 EBI-2864512,EBI-1048143 Q5JST6 EBI-2349927,EBI-1048143 Q8IZP0 EBI-375446,EBI-1048143 Q86X19 EBI-11343485,EBI-1048143 Q8VC57 EBI-2551470,EBI-1048143 Q99PT9 EBI-11092400,EBI-1048143 Q9D902 EBI-309435,EBI-1048143 Q8CAF4 EBI-11096298,EBI-1048143 P12004 EBI-358311,EBI-1048143 Q96QS3 EBI-11107474,EBI-1048143 Q9UHB6 EBI-351479,EBI-1048143 Q9UQB8 EBI-525456,EBI-1048143 P11142 EBI-351896,EBI-1048143 O43493 EBI-1752146,EBI-1048143 P15311 EBI-1056902,EBI-1048143 Q9NYB9-2 EBI-11096309,EBI-1048143 Q6NT52 EBI-21804273,EBI-1048143 Q9UPY6 EBI-3907133,EBI-1048143 Q8NB15-2 EBI-12179871,EBI-1048143 P36873-2 EBI-1048143,EBI-3964623 Q8HWS3 EBI-1048143,EBI-746118 Q5NFJ2 EBI-2801973,EBI-1048143 P61981 EBI-1048143,EBI-359832 Q8IWW6-4 EBI-11959591,EBI-1048143 Q70UQ0-4 EBI-12190633,EBI-1048143 Q9H251-9 EBI-11943338,EBI-1048143 Q96EV8-2 EBI-16749183,EBI-1048143 Q9H251 EBI-7968158,EBI-1048143 Q9BSM1 EBI-749901,EBI-1048143 O43639 EBI-713635,EBI-1048143 Q3ZCQ8-2 EBI-16400236,EBI-1048143 Q5HYW2 EBI-2859639,EBI-1048143 Q9ULV8 EBI-2341018,EBI-1048143 Q400G9 EBI-21768765,EBI-1048143 Q04917 EBI-306940,EBI-1048143 Q96L34 EBI-302319,EBI-1048143 P63104 EBI-347088,EBI-1048143 GO:0044295 GO:0090724 GO:0005829 GO:0044294 GO:0043197 GO:0060076 GO:0070062 GO:0005576 GO:0032433 GO:0005925 GO:0030027 GO:0005845 GO:0043005 GO:0043025 GO:0048471 GO:0090725 GO:0001726 GO:0031209 GO:0034774 GO:0035580 GO:0045202 GO:0043195 GO:1904724 GO:0051015 GO:0048365 GO:0000340 GO:0045182 GO:0048675 GO:0007411 GO:0000902 GO:0030031 GO:0032869 GO:0050890 GO:0097484 GO:0038096 GO:0030032 GO:0099563 GO:1903422 GO:0043312 GO:2000601 GO:0045773 GO:1900006 GO:0051388 GO:1900029 GO:0016601 GO:0008360 GO:1905274 GO:0006417 GO:0099578 GO:0051602 GO:0031529 GO:0048010 MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCTSSGSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDSAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTRFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSIVELDGLLEINRMTHKLLSRYLTLDGFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAILFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEGERLDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGEGTPVEHVRCFQPPIHQSLASS 1253 Q7L5N1 COP9 signalosome complex subunit 6 COPS6 9606 Yes SL-0198 Nucleus {ECO:0000269|PubMed:9535219}. Cytoplasm {ECO:0000269|PubMed:9535219}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9520381}. Note=(Microbial infection) The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. {ECO:0000269|PubMed:9520381}. UNIPROT Q7L5N1 UNIPROT A4D2A3 UNIPROT O15387 PDB 4D10 PDB 4D18 PDB 4QFT PDB 4R14 PDB 4WSN PDB 6R6H PDB 6R7F PDB 6R7H PDB 6R7I Pfam PF01398 Pfam PF13012 PROSITE PS50249 OMIM 614729 DisGeNET 10980 Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}. O75569 EBI-486838,EBI-713955 P04406 EBI-486838,EBI-354056 P11802 EBI-486838,EBI-295644 P49454 EBI-486838,EBI-968343 P50402 EBI-486838,EBI-489887 Q3TLR7 EBI-2553626,EBI-486838 Q5JTH9 EBI-486838,EBI-310743 Q99816 EBI-346882,EBI-486838 Q5S007 EBI-5323863,EBI-486838 Q9NRI5 EBI-486838,EBI-529989 P06241 EBI-486838,EBI-515315 Q92905 EBI-594661,EBI-486838 Q3U1J4 EBI-2552275,EBI-486838 P24386 EBI-2515129,EBI-486838 Q9C0D3 EBI-486838,EBI-1811414 Q6TFL4 EBI-486838,EBI-2510117 Q96SW2 EBI-486838,EBI-2510250 Q9UNS2 EBI-486838,EBI-350590 Q96Q07 EBI-486838,EBI-2510245 Q15048 EBI-486838,EBI-2510124 Q96EF6 EBI-486838,EBI-2510157 Q13618 EBI-486838,EBI-456129 Q96M94 EBI-486838,EBI-2510129 Q8WXC6 EBI-486838,EBI-2510257 P15374 EBI-486838,EBI-954554 Q13616 EBI-486838,EBI-359390 Q9UBW8 EBI-486838,EBI-712982 Q99627 EBI-486838,EBI-2510102 Q8NEZ5 EBI-486838,EBI-2510137 Q9P2J3 EBI-486838,EBI-2510152 Q13619 EBI-486838,EBI-456106 Q9H078 EBI-486838,EBI-2107221 Q9H4M3 EBI-486838,EBI-2322644 Q9Y3I1 EBI-486838,EBI-1161222 Q13620 EBI-486838,EBI-456067 Q13617 EBI-486838,EBI-456179 Q15369 EBI-486838,EBI-301231 Q53GT1 EBI-486838,EBI-1996072 Q9UK73 EBI-486838,EBI-310482 B4DN30 EBI-486838,EBI-2510114 Q8TBC3 EBI-486838,EBI-724292 Q9H496 EBI-486838,EBI-2510146 Q8TEB1 EBI-486838,EBI-2213388 Q13309 EBI-486838,EBI-456291 Q9P2K6 EBI-486838,EBI-739890 Q13216 EBI-486838,EBI-295260 Q9NZJ0 EBI-486838,EBI-1176075 Q86XK2 EBI-486838,EBI-1047804 Q92466 EBI-486838,EBI-1176171 Q9BW61 EBI-486838,EBI-2510241 Q9BT78 EBI-486838,EBI-742413 Q647K1 EBI-486838,EBI-2510264 Q9BX70 EBI-486838,EBI-710091 Q9P2G9 EBI-486838,EBI-949008 Q9Y597 EBI-486838,EBI-373299 Q9H9Q2 EBI-486838,EBI-2510162 P61201 EBI-486838,EBI-1050386 Q9Y2M5 EBI-486838,EBI-714379 Q96L50 EBI-486838,EBI-2510106 Q13098 EBI-486838,EBI-725197 Q9Y4B6 EBI-486838,EBI-1996353 Q9H0C5 EBI-486838,EBI-935503 P61024 EBI-486838,EBI-456371 Q5XUX1 EBI-486838,EBI-2322729 Q15843 EBI-486838,EBI-716247 Q9P2N7 EBI-486838,EBI-1996321 Q93034 EBI-486838,EBI-1057139 Q9BQ90 EBI-1055396,EBI-486838 P61081 EBI-1041660,EBI-486838 O94844 EBI-486838,EBI-6426999 Q8WV16 EBI-486838,EBI-2559135 Q13620-1 EBI-486838,EBI-10983971 Q13618-2 EBI-486838,EBI-21546135 Q13098-5 EBI-486838,EBI-21591293 P61201-2 EBI-486838,EBI-21591286 O43583 EBI-716083,EBI-486838 Q7L5Y6 EBI-6425391,EBI-486838 A1L190 EBI-10283466,EBI-486838 Q6UXH8-3 EBI-486838,EBI-12013534 Q8N6Y0 EBI-739895,EBI-486838 Q02556 EBI-2866563,EBI-486838 Q9UBL3 EBI-540797,EBI-486838 P12520 EBI-6164519,EBI-486838 Q5VW00 EBI-486838,EBI-3951747 O15061 EBI-486838,EBI-7843148 Q96ME1 EBI-486838,EBI-6425558 Q12951 EBI-486838,EBI-11318190 Q9H469 EBI-486838,EBI-6144096 Q8N1E6 EBI-486838,EBI-6425532 P10599 EBI-486838,EBI-594644 Q9H4B7 EBI-486838,EBI-2949748 P68366 EBI-486838,EBI-351772 Q01085 EBI-486838,EBI-2820828 O60506 EBI-486838,EBI-1024357 P09234 EBI-486838,EBI-766589 P08621 EBI-486838,EBI-1049228 P05141 EBI-486838,EBI-355133 P31040 EBI-486838,EBI-1057265 P60866 EBI-486838,EBI-353105 P15880 EBI-486838,EBI-443446 P62244 EBI-486838,EBI-347895 P62263 EBI-486838,EBI-352783 P05386 EBI-486838,EBI-354582 P62917 EBI-486838,EBI-438527 Q02878 EBI-486838,EBI-359655 P36578 EBI-486838,EBI-348313 P62899 EBI-486838,EBI-1053664 P83731 EBI-486838,EBI-353146 P62829 EBI-486838,EBI-353303 Q07020 EBI-486838,EBI-352694 P61313 EBI-486838,EBI-443462 Q06830 EBI-486838,EBI-353193 P13647 EBI-486838,EBI-702187 Q14568 EBI-486838,EBI-2826582 O14979 EBI-486838,EBI-299727 Q99729 EBI-486838,EBI-1044873 P13639 EBI-486838,EBI-352560 P53675 EBI-486838,EBI-358826 Q07021 EBI-486838,EBI-347528 P60709 EBI-486838,EBI-353944 P07437 EBI-486838,EBI-350864 Q9BQE3 EBI-486838,EBI-1103245 Q92804 EBI-486838,EBI-2255091 P62316 EBI-486838,EBI-297993 P62701 EBI-486838,EBI-354303 P05387 EBI-486838,EBI-352813 P62424 EBI-486838,EBI-354172 P62913 EBI-486838,EBI-354380 Q13610 EBI-486838,EBI-1050630 P11940 EBI-486838,EBI-81531 P06748 EBI-486838,EBI-78579 P19838 EBI-486838,EBI-300010 P19338 EBI-486838,EBI-346967 O95678 EBI-486838,EBI-2949715 P38646 EBI-486838,EBI-354932 P48741 EBI-486838,EBI-877656 P11021 EBI-486838,EBI-354921 P52597 EBI-486838,EBI-352986 Q14103 EBI-486838,EBI-299674 Q05639 EBI-486838,EBI-354943 P17844 EBI-486838,EBI-351962 O00571 EBI-486838,EBI-353779 P61962 EBI-486838,EBI-359808 P68371 EBI-486838,EBI-351356 Q9Y3Z3 EBI-486838,EBI-1054601 P63173 EBI-486838,EBI-359141 P36639 EBI-486838,EBI-1048967 P34931 EBI-486838,EBI-354912 Q9BUJ2 EBI-486838,EBI-1018153 P31942 EBI-486838,EBI-711437 P31943 EBI-486838,EBI-351590 P22626 EBI-486838,EBI-299649 P62280 EBI-486838,EBI-1047710 P61626 EBI-486838,EBI-355360 Q01546 EBI-486838,EBI-2952745 Q2M2I5 EBI-486838,EBI-2952736 P12268 EBI-486838,EBI-353389 P07900 EBI-486838,EBI-296047 P35637 EBI-486838,EBI-400434 P35527 EBI-486838,EBI-356382 P14625 EBI-486838,EBI-359129 Q01844 EBI-486838,EBI-739737 P06493 EBI-486838,EBI-444308 Q9UQE7 EBI-486838,EBI-80718 Q71RC2 EBI-486838,EBI-2878091 Q92734 EBI-486838,EBI-357061 Q6P5R6 EBI-486838,EBI-2512545 P11142 EBI-486838,EBI-351896 Q9BRP1 EBI-486838,EBI-2372173 Q9H3F6 EBI-486838,EBI-2505886 P35908 EBI-486838,EBI-1247312 P04264 EBI-486838,EBI-298429 P13645 EBI-486838,EBI-465144 P78406 EBI-486838,EBI-724495 Q8N1G4 EBI-486838,EBI-2509921 Q96MP8 EBI-486838,EBI-12537276 Q6PI47 EBI-486838,EBI-20587542 Q9NXK8 EBI-486838,EBI-719790 Q53G59 EBI-486838,EBI-740929 P22830 EBI-486838,EBI-1390356 O95219 EBI-486838,EBI-724909 Q96T23 EBI-486838,EBI-926768 P49642 EBI-486838,EBI-726050 O60237 EBI-486838,EBI-2558026 Q8NDI1 EBI-486838,EBI-2689720 Q9UGM3 EBI-486838,EBI-1044970 Q6P3S6 EBI-486838,EBI-2506081 Q96NC0 EBI-486838,EBI-2682299 P13521 EBI-486838,EBI-947132 Q92834 EBI-486838,EBI-6558417 Q9H4K1 EBI-486838,EBI-740128 Q05BQ5 EBI-486838,EBI-5666902 Q8WXI2 EBI-486838,EBI-1045119 P01042 EBI-486838,EBI-6378713 Q9NXE8 EBI-486838,EBI-746052 Q6IMN6 EBI-486838,EBI-6918449 Q9GZY4 EBI-486838,EBI-6570735 Q9BYV9 EBI-486838,EBI-1642333 O75110 EBI-486838,EBI-2878108 Q9Y2J4 EBI-486838,EBI-746752 Q10570 EBI-486838,EBI-347859 Q15370 EBI-486838,EBI-301238 P63208 EBI-486838,EBI-307486 Q92673 EBI-486838,EBI-1171329 Q00526 EBI-486838,EBI-1245761 P78396 EBI-486838,EBI-375065 Q9NXF7 EBI-486838,EBI-2559096 Q3SXM0 EBI-486838,EBI-20854462 Q8WVD3 EBI-486838,EBI-749039 Q16531 EBI-486838,EBI-350322 O94889 EBI-486838,EBI-2510096 O94952 EBI-486838,EBI-311435 Q5T6F0 EBI-486838,EBI-2559113 Q92624 EBI-486838,EBI-743771 P24941 EBI-486838,EBI-375096 P20248 EBI-486838,EBI-457097 Q7Z7A1 EBI-486838,EBI-2563266 Q96GG9 EBI-740086,EBI-486838 Q8N5D0 EBI-486838,EBI-311222 Q5TAQ9 EBI-486838,EBI-740686 Q5QP82 EBI-486838,EBI-723230 Q96JK2 EBI-486838,EBI-3253159 Q8TEL6 EBI-486838,EBI-2559060 Q58WW2 EBI-486838,EBI-2559044 Q9C0C7 EBI-486838,EBI-2512975 Q53HC5 EBI-486838,EBI-724915 P57775 EBI-486838,EBI-2372268 Q9Y297 EBI-486838,EBI-307461 Q9UKB1 EBI-486838,EBI-355189 Q9UK99 EBI-486838,EBI-2509901 P09466 EBI-486838,EBI-465167 Q9H3D4 EBI-2337775,EBI-486838 P23508 EBI-486838,EBI-307531 P17858 EBI-486838,EBI-487243 Q92561 EBI-486838,EBI-716478 P07602 EBI-486838,EBI-716699 P60484 EBI-486838,EBI-696162 Q9BXR0 EBI-486838,EBI-716832 P51159 EBI-486838,EBI-716881 P11166 EBI-486838,EBI-717153 Q16637 EBI-486838,EBI-395421 Q13190 EBI-486838,EBI-714206 P49888 EBI-486838,EBI-712512 P13385 EBI-486838,EBI-717375 O60315 EBI-486838,EBI-717614 Q9Y4P8 EBI-486838,EBI-719396 P62861 EBI-486838,EBI-358093 Q8IYL3 EBI-486838,EBI-715898 P60903 EBI-486838,EBI-717048 P05154 EBI-486838,EBI-722597 P11230 EBI-486838,EBI-724218 Q15911-2 EBI-486838,EBI-10237226 Q92529 EBI-486838,EBI-79084 Q13515 EBI-486838,EBI-10229433 Q8NBE8 EBI-486838,EBI-2512246 P28482 EBI-959949,EBI-486838 A0A1J9WN09 EBI-486838,EBI-2814859 O95704 EBI-286427,EBI-486838 Q6JEL2 EBI-6426253,EBI-486838 Q9UKA1 EBI-2692340,EBI-486838 Q96RU7 EBI-486838,EBI-492476 Q96HD1 EBI-486838,EBI-713009 O43261 EBI-486838,EBI-710057 Q3KQU3 EBI-486838,EBI-713229 Q9GZN7 EBI-486838,EBI-713255 Q16363 EBI-486838,EBI-711505 Q15102 EBI-486838,EBI-711522 Q6P1K2 EBI-486838,EBI-713832 O00231 EBI-486838,EBI-357816 P40937 EBI-486838,EBI-712376 P15927 EBI-621404,EBI-486838 P21673 EBI-486838,EBI-711613 P50453 EBI-486838,EBI-711626 P40425 EBI-486838,EBI-348489 P62308 EBI-486838,EBI-624585 P04183 EBI-486838,EBI-712550 P17028 EBI-486838,EBI-707773 Q96SN7 EBI-714817,EBI-486838 Q9Y6N8 EBI-486838,EBI-714872 P42773 EBI-486838,EBI-711290 Q14061 EBI-486838,EBI-711311 P20674 EBI-486838,EBI-715032 Q53FE4 EBI-486838,EBI-715110 O14717 EBI-486838,EBI-711937 P05305 EBI-486838,EBI-715181 Q09472 EBI-486838,EBI-447295 P84090 EBI-486838,EBI-711389 Q9NY59 EBI-486838,EBI-715400 P30519 EBI-486838,EBI-712096 Q9BWC9 EBI-486838,EBI-711501 P06858 EBI-486838,EBI-715909 Q13113 EBI-486838,EBI-716063 Q8IYB7 EBI-486838,EBI-716104 Q8N2I9 EBI-486838,EBI-716112 P51948 EBI-486838,EBI-716139 Q99417 EBI-486838,EBI-716185 P08670 EBI-486838,EBI-353844 GO:0008180 GO:0005829 GO:0005654 GO:0048471 GO:0000715 GO:0043687 GO:0000338 GO:0006283 GO:0016032 MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF 327 Q7SXN4 Cytoplasmic polyadenylation element-binding protein 4 cpeb4 7955 Yes SL-0198 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}. UNIPROT Q7SXN4 Pfam PF16366 Pfam PF16367 PROSITE PS50102 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. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. {ECO:0000250|UniProtKB:Q17RY0}. GO:0030054 GO:0005737 GO:0030425 GO:0043197 GO:0005783 GO:0030426 GO:1990124 GO:0043005 GO:0005634 GO:0048471 GO:0014069 GO:0045202 GO:0003730 GO:0043022 GO:0008135 GO:0000900 GO:0071230 GO:0036294 GO:0042149 GO:0035235 GO:2000766 GO:0043524 GO:0002931 MQDDILESEMSKAPQLQQESQEGQDKQTLSPPGHQEPPGIISELDNALPEENQLEKGTMENANGKETLRLESPVLSGFDYQETTGIGTLAQSSSSSSSSLTGFSSWSTAMPPNPSTLIEEVGFFNQAATTNNAPPPLLFQSFSHHTSTGFGGNFSHQIGPLSQHHPSPHPHFQHPHNQHRRSSASPHPPPFSHRSAAFNQLPHLGNNLSKPPSPWGSYQSPSSTPSSTSWSPGGGYGGWGSSQGREYRRGGVNPLNSISPLKKSFPNNQTQTQKYPRNNSGFNTKPWVEDTINRNESIFPFQERSRSFDGFSMHSLENSLIDIMRAEQDSLKGHSSLFPMEDERSYGEDERSDQSLSGLGSPHSFPHQNGERIERYSRKVFVGGLPPDIDEDEITASFRRFGHLFVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACMEEDGKLYLCVSSPTIKDKPVQIRPWNLNDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN 635 Q7SZC5 Nucleoporin NDC1 ndc1 7955 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q7SZC5 Pfam PF09531 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}. GO:0016021 GO:0031965 GO:0070762 GO:0017056 GO:0051028 GO:0006999 GO:0015031 MFSMKQNCWFIRKVVIWRAVASIAWSVLLLPITTAVFVLLSRFSLFHPIQWISDCTNLLTASSTIFSLMVLCAVVLITGFFNLEFYTLVPSIPCSRVALLGTVLHPLQCVHSLVYSSMGMLVMWCASVIISGRYSTLGTPCMQNESGDVLTCLNEYHLFLLLAGAFMGYSHSFLGVVKNMYYVSFQPIQQYKYPQFKGCLPMLLKCSVIQSLYSTRNFAALYFFFGYVPRAWISSTLNLPIDSSLQPLDSLTGLLDFSLLYHLSISGTFLYFTWYLTVLIFRIYATEAYSFPVQSTFSEDAERCLPKVVGEKSTLVMKFLALQDLALLSQHSPSRRQEVFSLSQPGGHPHNWNAISGECLCLLRDLTQRLVAHQDAVASNGRVKSQSASSDTRSASSSSSVLSGMEDVPETPRPTVPLRTPGSVFKSSVGGMHSSLTAPFTPDVDSPFCSPAIRRLVGQQDPQSPWFGTVQSPHIMRRGPKLWSASTESQSNGSPPASPAIAPSPPAANKKPSFLAQWLQNRKEQVKSFLAKRVLIVYLFNKLPEASSQALFADSQAHIWALQGLSHLVAASFSEDQFGVVQTTLPSILSSLVVLLEAVDRHFKLPHASSKPARTVCSMGDSTYKTLRFALRAALKTAIYKITTTFGEHLNAVNISTEHRKRLQQFLEFKE 671 Q7TPN9 Proline-rich protein 14 Prr14 10090 Yes SL-0178 SL-0180 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}. UNIPROT Q7TPN9 UNIPROT Q922N8 Pfam PF15386 Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (By similarity). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (By similarity). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157) (By similarity). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1, ECO:0000269|PubMed:25906157}. GO:0005694 GO:0005652 GO:0005654 GO:0007517 MDLPGNSSPFTQPSLCRQPLSRASWEARSPKRPRLQPLGTPSSLEKASRRVLAVVLEDVMTTNRVPLTHKEDTPSPLTHNHHQDPVCTQSPALPSQQVKWSMQARPPDPLHLCREPLTRARQSSPALRMRSRAASGPEESPSKKTDQVPQPTLVVVLEDIASGRQPAEGFDEDQPNLIVPAQSTFRSLKGPGKHCHRRGLDLEARPTLTLSLHPRAEPVTKAGQPMPTPSDLEPPFQLSTLPADPPESPVPDPALETPVIPTSSSLLRPRLSPWGLAPLFRSVRSKLESFADIFFTPNKTPQPPPPSPPMKLELKIAISEAEQSRATEKITSVSPRPPIRQWRTQCNSLAPVSKSSLGRSYSCPDLGPPDPGSWPPVPSQPSQSRPRRHTVGCGEMARTPPPPRPCLRKEVFPLGGVGVSPSLTTSCSANAPASFFCEPAEPRLGSTKGKELRASKDKVFSDPETKTMGKVSRFRIRRTPVRLQPNLTPMGLPRPIRLNKKEFTLEEIYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRAVEFRDSSLPRSRRPSRGVRTAASRTLTPNLAPSQDVGSLLQERLRELDALLLEEETDKEHPCHL 612 Q7Z2G1 Histone H2B type W-T H2BW1 9606 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:15475252}. Chromosome {ECO:0000269|PubMed:15475252}. UNIPROT Q7Z2G1 UNIPROT B1AK72 UNIPROT Q147W3 Pfam PF00125 OMIM 300507 DisGeNET 158983 Atypical histone H2B. Nucleosomes containing it are structurally and dynamically indistinguishable from those containing conventional H2B. However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes. May be important for telomere function. {ECO:0000269|PubMed:16449661}. Q6NXS1 EBI-18200422,EBI-10251630 GO:0031965 GO:0000786 GO:0003677 GO:0046982 GO:0006334 MLRTEVPRLPRSTTAIVWSCHLMATASAMAGPSSETTSEEQLITQEPKEANSTTSQKQSKQRKRGRHGPRRCHSNCRGDSFATYFRRVLKQVHQGLSLSREAVSVMDSLVHDILDRIATEAGRLARSTKRQTITAWETRMAVRLLLPGQMGKLAESEGTKAVLRTSLYAIQQQRK 175 Q7Z3Z2 Protein RD3 RD3 9606 Yes SL-0198 Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q8BRE0}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8BRE0}. Endosome {ECO:0000250|UniProtKB:Q8BRE0}. Nucleus {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29030614}. Note=Colocalizes with GUCY2E and GUCY2F in rods and cones photoreceptors. Colocalizes with GUK1 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer (By similarity). Strong dot-like perinuclear staining in the epithelial cells (PubMed:29030614). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:29030614}. UNIPROT Q7Z3Z2 UNIPROT A8K595 PDB 6DRF Pfam PF14473 OMIM 180040 OMIM 610612 DisGeNET 343035 Plays a critical role in the regulation of enzymes involved in nucleotide cycle in photoreceptors (PubMed:29515371, PubMed:21928830, PubMed:21078983, PubMed:27471269, PubMed:30559291). Inhibits the basal catalytic activity and the GCAP-stimulated activity of GUCY2D and GUCY2F, two retinal guanylyl cyclases involved in the production of cGMP in photoreceptors (PubMed:21928830, PubMed:27471269, PubMed:29515371, PubMed:30559291). Involved in the transport of GUCY2D and GUCY2F to their target sites in the photoreceptor outer segment (PubMed:21078983). Up-regulates the activity of GUK1, a kinase that plays also an essential role for recycling GMP and indirectly, cGMP (PubMed:29515371). Plays an important role for the survival of rods and cones in the retina (By similarity). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:21928830, ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:29515371, ECO:0000269|PubMed:30559291}.Leber congenital amaurosis 12 (LCA12) [MIM:610612]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:17186464}. Note=The disease is caused by mutations affecting the gene represented in this entry. A2ABF9 EBI-10257497,EBI-10174566 Q14232 EBI-491065,EBI-10257497 Q8NFP9 EBI-10257497,EBI-723014 Q7L592-2 EBI-10257497,EBI-21502380 P50851-2 EBI-10257497,EBI-4403233 P19086 EBI-10257497,EBI-9071731 Q96HA8 EBI-10257497,EBI-741158 Q9NPB3 EBI-10257497,EBI-12011224 Q96KQ7 EBI-744366,EBI-10257497 GO:0120199 GO:0005737 GO:0005768 GO:0005634 GO:0048471 GO:0001917 GO:0001750 GO:0120200 GO:0031283 GO:0015031 GO:0050896 GO:0060041 GO:0007601 MSLISWLRWNEAPSRLSTRSPAEMVLETLMMELTGQMREAERQQRERSNAVRKVCTGVDYSWLASTPRSTYDLSPIERLQLEDVCVKIHPSYCGPAILRFRQLLAEQEPEVQEVSQLFRSVLQEVLERMKQEEEAHKLTRQWSLRPRGSLATFKTRARISPFASDIRTISEDVERDTPPPLRSWSMPEFRAPKAD 195 Q7Z6J2 General receptor for phosphoinositides 1-associated scaffold protein GRASP 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=Localized at postsynaptic membranes. {ECO:0000250}. UNIPROT Q7Z6J2 UNIPROT Q6PIF8 UNIPROT Q7Z741 PDB 2PNT Pfam PF00595 PROSITE PS50106 OMIM 612027 DisGeNET 160622 Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}. Q5NHN0 EBI-2801077,EBI-2806496 GO:0030054 GO:0098978 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0098685 GO:0030306 GO:0042802 GO:0030165 GO:0008104 GO:0099152 GO:0007165 MTLRRLRKLQQKEEAAATPDPAARTPDSEVAPAAPVPTPGPPAAAATPGPPADELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNLSQSPEQQRKVLTLEKEDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAVPGRPRGGARRARGDADDAVYHTCFFGDSEPPALPPPPPPARAFGPGPAETPAVGPGPGPRAALSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGPGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL 395 Q80U58 Pumilio homolog 2 Pum2 10090 Yes SL-0198 Cytoplasm {ECO:0000305|PubMed:19861488}. Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm, perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity). Colocalizes with NANOS3 in the stress granules (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72, ECO:0000269|PubMed:19861488}. UNIPROT Q80U58 UNIPROT Q80UZ9 UNIPROT Q91YW4 UNIPROT Q925A0 UNIPROT Q9ERC7 PDB 3GVO PDB 3GVT Pfam PF00806 PROSITE PS50302 PROSITE PS50303 Sequence-specific RNA-binding protein that acts as a post- transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'- UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q8TB72}. P35637 EBI-400434,EBI-998056 GO:0005737 GO:0010494 GO:0005829 GO:0031965 GO:0048471 GO:0035198 GO:0003730 GO:0003729 GO:0003723 GO:2000637 GO:1900246 GO:0010608 GO:0035196 GO:0051983 GO:0043488 GO:0006417 GO:0034063 MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTSALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAASNTANQQAASQAQPGQQQVLRPGAGQRPITPSQGQQGQQAESLAAAANPTLAFGQSLAAGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSTAAQAAAAAAAAGGTANSLTGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASLGFGSGSSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML 1066 Q80UM3 N-alpha-acetyltransferase 15, NatA auxiliary subunit Naa15 10090 Yes SL-0198 Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton- bound polysomes, but not in the membrane-bound polysomes. {ECO:0000250}. UNIPROT Q80UM3 UNIPROT Q811Z9 UNIPROT Q9JID5 Pfam PF12569 Pfam PF13181 PROSITE PS50005 PROSITE PS50293 Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:10842358, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564, ECO:0000269|PubMed:15452080}. Q9GZZ1 EBI-2554211,EBI-1052523 Q9BXJ9 EBI-2554211,EBI-1042540 Q9NX55 EBI-2554211,EBI-1048743 P41227 EBI-2554211,EBI-747693 GO:0005737 GO:0005829 GO:0031415 GO:0005634 GO:0048471 GO:0005667 GO:0008080 GO:0043022 GO:0001525 GO:0030154 GO:0017196 GO:0006474 GO:0043066 GO:0045893 GO:0050821 MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPGNWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDRFLRMNFSKGCPPVFNTLRSLYRDKEKVAIVEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYVLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSGHPWLHECMIRLFHSVCESKDLPETVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDSSSQKRAIELATTLDGSLTNRNLQTCMEVLEALCDGSLGDCKEAAEAYRASCHKLFPYALAFMPPGYEEDMKITVNGDSSAETEELANEI 865 Q80VJ8 Protein KASH5 Ccdc155 10090 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22826121}. Chromosome, telomere {ECO:0000269|PubMed:22826121}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000269|PubMed:24586178, ECO:0000269|PubMed:26842404}. UNIPROT Q80VJ8 UNIPROT E9QNS3 UNIPROT E9QQ69 Pfam PF14658 Pfam PF14662 As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homologue pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}. GO:0005623 GO:0000781 GO:0016021 GO:0000800 GO:0034993 GO:0090619 GO:0005640 GO:0070840 GO:0042802 GO:0007015 GO:0090220 GO:0000724 GO:0090172 GO:0048477 GO:0007283 GO:0051225 GO:0051653 GO:0007129 GO:0034397 MHSILRSSLSSREALRMRQLKGLRKERPGRHPLGVRLRAIWTSFLFPNPPHSGGKLRASTAAVEEHQEWSMDLPEGQAGGPTAQMYLWEQPEEASSRPLLSLEEQILNSTFEACDPHKTGTVTVAHLLAYLEAVTGQGPQDVRLQTLARSLDPYGEGAGATVELDTFLVVMRDWIAACQLQGGLERAEETAYEGALASPHLPSVCPEAEESANLESFGGEDPRPEGPATAELLSNLEDLELSNRRLAGENAKLQRSVETAEEGSARLGEEITALRKQLRSTQQALQVAKALDEELEDLKTLAKSLEEQNRSLMAQARHTEKEQQHLAAEVETLQEENEKLLAERDGVKRRSEELATEKDALKRQLCECERLICQREAVLSERTRHAESLARTLEEYRTTTQELRQEISNLEEQLSQSQEGPEELLEGAEAGRVGWIMALPPSLDLEIQAIRQEQDVASAGLSSPLYGVWQWEEVEPEPEPEPEPEPEPEPQEVEFPSEDPARQQTDLQREPVRALEGSRAPCLRLSRSQEEEEEEEESWVLADPSSPLGTYHHKLAPGSSRESCHIVPEMHQALMPVVRDLVPVERSRTQHCLHPQHSPGIRISQHPLVPTPVLGLLLLLLLSILLFSQSPPPTWPHLQLYYLQPPPV 648 Q80WJ1 Gametogenetin Ggn 10090 Yes SL-0198 [Isoform 1]: Cytoplasm, perinuclear region. Note=Localizes along the nuclear membrane. [Isoform 2]: Cytoplasmic vesicle. [Isoform 3]: Nucleus, nucleolus. UNIPROT Q80WJ1 UNIPROT Q5EBP4 UNIPROT Q80WI9 UNIPROT Q80WJ0 Pfam PF15685 May be involved in spermatogenesis. {ECO:0000269|PubMed:12574169}. GO:0005737 GO:0031410 GO:0016021 GO:0005635 GO:0005730 GO:0048471 GO:0042802 GO:0031625 GO:0030154 GO:0006302 GO:0007566 GO:0007276 GO:0008104 GO:0065003 GO:0007283 MGNVQSEPSAGGGSRKEQASDRASDSRRTPLVEPEVTPSSPAMRLARGLGVWFPGSSGPPGLLIPPEPQASSSPLPLTLELPSPVTPPPEEAAAVSTPPPPPVGTLLPAPSKWRKPTGTSVPRIRGLLEASHRGQGDPPSLRPLPPLPRQLTEKDPVLRAPAPPPTPLEPRKQLPPAPSTCDPQPLSRRITLASSATSPTESQVRHSSEGQAAGGAHGGVPPQAGEGEMARSATSESGLSLLCKVTFKSGPHLSPTSASGPLAAKASPGAGGGGLFASSGAISYAEVLKQGPQPPGATRPLGEVPPGATRPLGEVPRAAQETEGGDGDGEGCSGPPSVPAPLARALPPPPYTTFPGSKPKFDWVSPPDGTERHFRFNGAVGGIGAPRRRTTTLSGPWGSPPPRSGQTHPSSGPRRPTPALLAPPMFIFPAPNNGEPVRPVPPSPQQIPPLPPPPPTPPATPPPAPPPTPQPPALPRTPILVARPPTPGPGHLESALAPTPPSTLSPTAAADQVPAATPATVTSQVPATATAELSPPMPQPKTRTRRNKGPRAARGVIREEGTSGDGPREPNTAPVTDSSSGGGGGGSNGTSTAGASNKGTARHWPPFEVLNSCPCKCYCRHQRRHRRLPRNVSAWLSTPTNHLSEPPWVATVKLAGSLVAGLEHYDLQATHST 673 Q80Y24 Prickle-like protein 2 Prickle2 10090 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}. UNIPROT Q80Y24 UNIPROT A6H652 Pfam PF00412 Pfam PF06297 PROSITE PS00478 PROSITE PS50023 PROSITE PS51303 DE Reference Proteome: Yes; GO:0016327 GO:0005737 GO:0016328 GO:0031965 GO:0008270 GO:0045197 GO:0031175 MVTVMPLEMEKTISKLMFDFQRSSTSDDDSGCALEEYAWVPPGLKPEQVHQYYSCLPEEKVPYVNSAGEKLRIKQLLHQLPPHDNEVRYCNSLDEEEKRELKLFSNQRKRENLGRGNVRPFPVTMTGAICEQCGGQIKGGDIAVFASRAGHGICWHPPCFVCTVCNELLVDLIYFYQDGKIYCGRHHAECLKPRCAACDEIIFADECTEAEGRHWHMRHFCCFECETVLGGQRYIMKEGRPYCCHCFESLYAEYCDTCAQHIGIDQGQMTYDGQHWHATETCFCCAHCKKSLLGRPFLPKQGQIFCSRACSAGEDPNGSDSSDSAFQNARAKESRRSAKIGKNKGKTEEAMLNQHSQLQVSSNRLSADVDPLSVQMDLLSLSSQTPSLNRDPIWRSREEPFHYGNKMEQNQSQSPLQLLSQCNIRTSYSPGGQGAGAQPDMWAKHFSNPKRSSSMALKGHGGSFIQECREDYYPGRLMSQESYSDMSSQSFNETRGSIPVPKYEEEEEEEEGGISTQQCRPRRPLSSLKYTEDMTPTEQTPRGSMESLALSNATGLSAEGGAKRQEHLSRFSMPDLSKDSGMNVSEKLSNMGTLNSSMQFRSAESVRSLLSAQQYQEMEGNLHQLSNPLGYRDLQSHGRMHQSFDFDGGIASSKLPGQEGVHIQPMSERTRRRTTSRDDNRRFRPHRSRRSRRSRSDNALHLASEREVIARLKERPPLRAREDYDQFMRQRSFQESLGQGSRRDLYSQCPRTVSDLALQNAFGERWGPYFTEYDWCSTCSSSSESDNEGYFLGEPIPQPARLRYVTSDELLHKYSSYGVPKSSTLGGRGQLHSRKRQKSKNCIIS 845 Q810M5 Palmitoyltransferase ZDHHC19 Zdhhc19 10090 Yes SL-0198 Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WVZ1}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8WVZ1}. UNIPROT Q810M5 Pfam PF01529 PROSITE PS50216 Palmitoyltransferase that mediates palmitoylation of STAT3 and RRAS. Palmitoylation of STAT3 induces the homodimerization and transcriptional activation of STAT3, thereby, promoting inflammation and cancer. Palmitoylation of RRAS is linked to cell viability. May be involved in S-stearoylation of STAT3. {ECO:0000250|UniProtKB:Q8WVZ1}. GO:0005783 GO:0005794 GO:0000139 GO:0016021 GO:0048471 GO:0019706 GO:0018230 GO:0045944 GO:0006612 MPFLKDAVTLVKEPQQLPSIPLSWFPSSVFAAFNVTLLLFLSGLFFGFPCRWLVQNGEWAFPAITGPLFILTFFSLVSLNFSDPGILHRGSTKEDPMTVHVVRVNQRAFRLEWCPKCLFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRLFMLLVLSLCLYSGALLVTCLTFLFRTRHLPFSLDKGMAILVAVPAAGFLIPLFLLLLIQALSVSRAESSYESKCRYHPEYNPFDQGFAKNWYLAMFAPLGPNYMSEVVCLQRPVGTAWIQEKTKPSPPRRPKHCRPGPPGPQHQPRRVPGKGPPGSGEAAALQEMRRLPASVEKSPGGPRQPTAEPAAGDP 347 Q83017 Non-structural protein 12 rep 300016 No SL-0382 [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}. UNIPROT Q83017 UNIPROT Q83018 UNIPROT Q83024 UNIPROT Q83025 UNIPROT Q86716 Pfam PF16749 Pfam PF12581 Pfam PF05410 Pfam PF05411 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF01443 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 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}. GO:0033644 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0070008 GO:0008270 GO:0006351 GO:0019082 GO:0039694 MQSGFDRCLCTPNARVFWEHGQVYCTRCLAARPLLPLSQQNPRLGALGLFYRPATPLTWEAPITYPTKECRPGGLCWLSGIYPIARMTSGNHNFQARLNFVASVVYRDGKLTSKHLEEEFEVYSRGCRWYPITGPVPGIALYANAVHVSDEPFPGCTHVLSNLPLPQQPLRKGLCPFSDARAEVWRYKGNTIFVSEQGYLWTTGSNDSVPEPWGEARRLCEKIIASLPADHLVKIEFSNYPFDYSFTGGDGAGYVLFPCKKNDTKFSKCWEKVFEDHSSWKVACEEADLADRMGYRTPAGVAGPYLARRLQYRGLRAVVKPEQNDYVVWALGVPESYIRHISRAGEPVENFFVRVGEFSIVSNCVATPYPKFRFQTRKYYGYSPPGDGACGLHCISAIINDIFGDALCTKLTNCSRDSSEWLSDQDMYQLVMTARLPATLGHCPSATYKLDCVNQHWTVTKRKGDRALGGLSPECVRGVCGGECKFVPTYPREINLELAAKSPISALAFSLGVEPYCDCWNFTNSVLVNDSLAVETARAGEAYRSAMGIPKDDWVLLAELMTENCLTRREVLDKLQRGLRLHATSKPGSPASVSPASSIDFSAAGLLLDGTESDKEAVVAVNNDCYTVLGFDKNSATKSEQELATGLFSELVEPMETSTSKHESRKILEAASRALKSAKPKRKRNKKKKTSSPTPTPPETPTREVPGAIEVVSGDEEAGACESATIVPDKAQARPPPRPKRQALKKAEQGFILKDIIWNPTESGVKCLTIVEDVRAFLKSITPPGGALGTRARITAHIVEQFHVIRESTPELVLAHAEHQAKNMHELLLSEKAKLILGIGEDTLKKLVSSQRSLPRSIGFGAWLSDQQKTADSCGEREFVEVPLKSGAEPTPSKRDLGVSLGDQLSQDGAPRLSSSTACEIKERVPPIKDSGGGLGQKFMAWLNHQVFLLSSHLLAMWSVVLGSRQKLNWADYVYTLFCLCCVLLCFHFPAIGFIPLAGCVFGSPWRVRLSVFSVWLCVAVVVFQEVLPEPGSVCSSASAECAAALERYSGNGVHRPVNHIGVGLVGTVAGFVARVVGGPRHYWFYFLRLMVVLDLGLVFLAVALRGRCKKCFCKCVRVAPHEVHLRVFPLTKVARPTLEAVCDMYSAPRVDPILVATGIKGCWQGKVSPHQVTDKPVSYSNLEEKKISNKTVVPPPTDPQQAVKCLKVLQCGGSIQDVGVPEVKKVSKVPYKAPFFPNVSIDPECYIVVDPVTYSAAMRGGYGVSHLIVGTGDFAEVNGLRFVSGGHVADFVCLGLYVMLNFLISAWLSSPVSCGRGTNDPWCKNPFSYPVVGQGVMCNSHLCISEDGLTSPMVLSYSLIDWALMIAVIATVAIFIAKVSLLVDVICVFLCLLMYVFPPLSVIAFAFPFALCKVHLHPVTLVWVQFFLLAVNFWAGVAVAVILISSWFLARATSSTGLVTPYDVHLVTSTPRGASSLASAPEGTYLAAVRRSALTGRCCMFVPTNFGSVLEGSLRTRGCAKNVVSVFGSASGSGGVFTIHGNPVVVTATHLLSDGKARVSCVGFSQCLTFKSVGDYAFARVAEWKGDAPKVELSDRRGRAYCSPQVEWSLVLLGPNTAFCFTKCGDSGSPVVDEDGNLIGVHTGSNKRGSGMITTHNGKTLGMSNVKLSEMCQHYGGSGVPVSTVRLPKHLIVDVEAVASDLVAVVESLPTPEGALSSVQLLCVFFFLWRLIHVPFVPVIAVAFFFLNEILPVVLARLMFSFALSLFSVFTGFSVQVLLLRLVIAALNRSAVSFGSFLLGQLFHCCLMPSHLETLGPVPGYFYPSTTEVASKEIFVTLLAIHVLALLLSLFKRPMLADVLVGNGSFDAAFFLKYFAEGNLRDGVSDSCNMTPEGLTAALAITLSDDDLEFLQRHSEFKCFVSASNMRNGAKEFIESAYARALRAQLAATDKIKASKSILAKLESFAGGVVTKVEPGDVVVVLGKKIVGDLVEITINDVKHVIRVIETRVMAGTQFSVGTICGDLENACEDPSGLVKTSKKQRRRQKRTGLGTEVVGTVEIDGVSYNKVWHKATGDVTYEGFLVSENSRLRTLGTSAIGRFQEFIRKHGSKVKTSVEKYPVGKNKHIEFAVTTYNLDGEEFDVPDHEPLEWTITIGDSDLEAERLTVDQALRHMGHDSLLTPKEKEKLARIIESLNGLQQSSALNCLTTSGLERCSRGGVTVSKDAVKIVKYHSRTFSIGDVNLKVMSFDEYRRTMGKPGHLLVAKLTDGVVVMRKHEPSLVDVILTGEDAEFFPRTHGPGNTGIHRFVWDFESPPVDLELELSEQIITACSMRRGDAPALDLPYKLHPVRGDPYRHRGVLFNTRFGDITYLIPEKTKEPLHAAACYNKGVPVSDSETLVATTLPHGFELYVPTLPPSVLEYLDSRPDTPRMLTKHGCASAAEKDLQKFDLSRQGFVLPGVLYMVRRYLSRLIGVRRRLFMPSTYPAKNSMAGINGGRFPLTWLQSHPDIDALCKRACEEHWQTVTPCTLKKQYCSKSKTRTILGTNNFVALGLRSALSGVTQGFMRKGIGTPICLGKNKFTPLPVRIGGRCLEADLASCDRSTPAIIRWFTTNLLFELAGAEEWIPSYVLNCCHDVVSTMSGCFDKRGGLSSGDPVTSISNTVYSLIIYAQHMVLSAFRCGHKIGGLFLQDSLEMEQLFELQPLLVYSDDVVFYNESDELPNYHFFVDHLDLMLGFKTDRSKTVITSEPKLPGCRISGGRVLVPQRDRIVAALAYQMKASCVGEYFASAAAILMDACACCDHDESWYFDLVCGIAECAGSPWFRFPGPSFFLDMWNRLSAEEKKKCRTCAHCGAPATLVSSCGLNLCDYHGHGHPHCPVVLPCGHAVGSGVCEQCSSSAMNLNTELDILLMCVPYHPPKVELLSVNDKVSSLPPGAYQARGGVVSVRRDILGNVVDLPDGDYQVMKVAQTCADISMVSVNSNILRSQFVTGAPGTGKTTYLLSVVRDDDVIYTPTHRTMLDVVKALKVCRFDPPKDTPLEFPVPGRTGPTVRLIGAGFVPGRVSYLDEAAYCNPLDVLKVLSKTPLVCVGDLNQLPPVGFNGPCFAFSLMPGRQLIEVFRFGPAVVNSIKKFYKEELVPRGPDTGVKFLKQYQPYGQVLTPYHRDRVDGAITIDSSQGCTYDVVTVYLPTPKSLNSARALVALTRARHYVFIYDPYDQLQQYLQVFEHEPADAWAFWCGDQPKMIVGGVVKQLAGHSRTTDLKLQQLMGLEGTASPLPQVGHNLGFYYSPDLIQFAKIPPELCKHWPVVTAQNRTEWPDRLVCGMNKMDKNSRAVFCAGYYVGPSIFLGVPGVVSYYLTKYLKGESVPLPDSIMSTGRIRLNVREYLDENEIEFAKKCPQPFIGEVKGSNVGGCHHVTSRFLPPVLVPGSVVKVGVSCPGKAAKGLCTVTDVYLPELDSYLHPPSKSMDYKLLVDFQPVKLMVWKDATAYFHEGIRPMEAMSRFLKVPEGEGVFFDLDEFVTNAKVSKLPCKYSVSAHQFLTEVVLSMTPTSEAPPDYELLFARAYCVPGLDVGTLNAYIYKRGPSTYTTSNFARLVKDTAVPVGCKGSGYMFPK 3616 Q84K11 Serine/threonine-protein phosphatase 5 PP5 4081 Yes SL-0178 SL-0182 [Isoform 1]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. [Isoform 2]: Cytoplasm. Nucleus, nucleoplasm. Nucleus speckle. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with phytochromes into speckles. {ECO:0000250}. UNIPROT Q84K11 UNIPROT Q8H1H4 Pfam PF00149 Pfam PF08321 Pfam PF00515 PROSITE PS50005 PROSITE PS50293 Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses (By similarity). Can use para-nitrophenylphosphate (pNPP) and phosphorylated casein as substrate at pH 7.5 and 5.0. {ECO:0000250, ECO:0000269|PubMed:12972652}. GO:0005829 GO:0030176 GO:0031965 GO:0016607 GO:0005634 GO:0009506 GO:0046872 GO:0004722 GO:0046906 GO:0010019 GO:1902325 GO:0010017 GO:0046686 MPGMEAENSNASRAEELKQLANEAFKGHKYSQAIDLYTQAIELNGENAVYYANRAFAHTKLEEYGSAIQDGTRAIEIDPRYSKGYYRRGAAYLAMGKFKDALKDFQQVKKLCPNDPDATKKLKECEKAVMKLKFEEAISVPESQRRSVADSIDYRSVGSGPGSSYVPTKTTAVSAAAALMGVLVVYMGTKAATMVAAAASAALLVVLITFLWGRCSDGFFTKSRTLELEVEPQYAGARIEGDVVTLDFVKKMLDDFKNQKNLHKRYAYQIVLQTREMLRALPSLVDIVVPEGKHFTVCGDVHGQFYDLLNIFELNGLPSEDNPYLFNGDFVDRGSFSLEVILTLFAFKCMCPSAIHLARGNHESKSMNKIYGFEGEVRSKLSEIFVELFAEVFCCLPLAHVINEKVFVVHGGLFSVDGVKLSDIRAIDRFCEPPEEGLMCELLWSDPQPQPGRGPSKRGVGLSFGGDVTKRFLQENNLDLVVRSHEVKDEGYEIEHDGKLITVFSAPNYCDQMGNKGAFIRFEAPDMKPNIVTFSAVPHPDVKPMAYANNFLRMFS 556 Q85041 Envelope glycoprotein M gM 33703 No SL-0415 SL-0418 SL-0419 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}. UNIPROT Q85041 UNIPROT Q5PP86 UNIPROT Q85042 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 GO:0019068 MCGPRNAEAVSWRSWLIEVCGFALAALTLVLTLIFASLPEMGFPCFYATVADYDTLNDTSGGVWTRQPLVAPALFLETPTVTSFFGFTATVLLAHALYAVAGAVVLRREAGRLAFQPSVVLYAASTVAAPGTLMLGALCAWTLQAVVLLMAHKQAGLAAAAYITHFVFLALFGACHACKGTGDVRAALAASPPLRRVAVHARAVVTNVVLGAVGLGAAVVGLMLGVLLANSFHISLWKTAEAALAVFTLLALALMVFVEVVVSGYVQVLPTPAFCVLVASAAFGVSAHRYFAKFSEALGETHGVVIGTRAVLAVLSLIALAMIVVRLVRACIAHRARGSRFYANVDKARTTARRYLQKRLHGRGNDEYLLAPGSGDDEFDDGDEVVYENLGFE 393 Q86CZ2 Hybrid signal transduction histidine kinase K dhkK 44689 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. UNIPROT Q86CZ2 UNIPROT Q54Y10 UNIPROT Q95PH2 Pfam PF02518 Pfam PF00512 Pfam PF00072 PROSITE PS50109 PROSITE PS50110 Involved in a signal transduction pathway that regulates morphogenesis and controls entry into the culmination stage. May act via the regA pathway, being activated by a morphogenesis-stimulated ligand, reducing phosphodiesterase regA levels and allowing cAMP level to rise to promote the culmination stage. This protein probably undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. GO:0016021 GO:0005635 GO:0031965 GO:0005524 GO:0000155 GO:0019933 GO:0031154 MIELNNHSKINKNENNTNTRNNSSNNNNNNNNINKTNTNKYFEYNQNSIIYSSIPNSFLSHHPNSVGSQCLSLNSFLPPKPPILLSIFNSDTIGNNNNNNYSSSSSRNNSSGCSSSNNNNNNNNNNNNNNNNNNNNNNNNCNIEQYKNNQKQPKQQQQQKDQTIATQHRISLSSSSSSSSLSSSSSSSSVKQSFQIVKRLFGSLSEYMFPQKDEILYETDPYYLYQDDTQSNDSNEFYDDTDIGSDIDEANLNNTYNIQNCNKTLYNKQQQQAHFVNMNKNVNSNNGTGNSNQSNNVNKNQQNNNNNNNNNSHNNNNGNQNSSSSSSNSGASGSGGNGNNNNNNNNNNNNNNNNNNNSNSNSNNNSKSNNNNKKEGKDGATMNGSHPLIPFRKKPAQVPSPCFRMNSPNSDNDQYLDQLALENSSKKSLVVYNTDNLDQWKHSHLNENFDILQNDLIDIQQQQQQQQQQDNTLQYSSPINKRQEQEQQHIPFQFTTEQQQQLQQQQQQQQQNKTKQHPILLQRQQQQKQKQQQQQQIQQEQIGNNNSNNNNNINNNNNINNNYNNVNDLMNKFEIDQKQHDSQQNLVEEKRTPSFHEHNIIFNSFNFICSIVLDGSNIKSTEKYKAKLIIGFCFTILSFIPSWIIFFWLSGINKPAVMAIIAMPMSISSLVILKRTGSIHYPCHILCFTLCFALTINSYYTGGHQSTIRLLMSTVPIISALVLGRKASIQWSLMVLSIYLLFFVANLYGHEYVQGIPSIIIRSHMNFIIDVTIIIMTLIFTLCYQYFIDEAHRETKLKNAQLTIAKDAAIEAYQARQEFLATMSHEIRTPLNGLIGMATLLRDSHNLPPEEKTMAKAVKSCGDILLRLVNDILDLSKLEANQMGLEHIPFRMRELTQQICHVLSGQANEKNIHLSCEVSDKIPSILLGDSGRILQILMNLTGNALKFTQSGYVKIIIDLIEEESELVSLKKGEYNISFRVKDTGIGVPVESHQKIFEAFVQADPSDSRKYGGSGLGLYLCAKLVRLMKGEIGVYNNPDCDGSTFWFILPLEEGTDQSMQQMNNGARHKAFPQDCVKVLIAEDNIINQRVAVKFLEKIGIKAEVAGNGNEVLEILERQHYDLIFMDFQMPILDGLRCSKTIREFEQNHKWNRICPSIFICGLTANTMSTDKKRCFDHGMNHFISKPFQLEQLRSAIEMAIEHKQRNLMNLNIRN 1213 Q86D96 Guanine nucleotide-binding protein subunit alpha-1 GA1 5722 No SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Endomembrane system; Lipid-anchor. Note=Predominantly perinuclear. UNIPROT Q86D96 Pfam PF00503 PROSITE PS51882 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250}. GO:0012505 GO:0016020 GO:0048471 GO:0031683 GO:0005525 GO:0003924 GO:0007186 MGCSASKPSEPSNAKLPSAPVPKKVEQVPEPKPEPQPQPEPQPQPEPPKPAEPAPAPAPAPEPQKPAEPAPKVVAVEDDTNEAYGLLLCGAGESGKTTFTRQLKLRYLNGFNEKDCRDFLRTIRGNLVETMQLLLVWLEHNNIEIEDSELSSMAQDIIDVDPQDCEFNEELVEKLKALWENEQIKKAFEHKDETAVPDHMPYFFAKIDELAGEDYIPSNEDVLRARIRSIGIEAITFDLQGARIRIFDVGGQKSERSKWANVMNQVEGVIFCVSFAEFDKPMFEDQNVLRINDSLEIFGNITHQEKFSNSPIFLVCNKFDVFTEKIKNTDAFVKIFPEFSGDSHNPEACADYLIQRFLDKAAPLSEDRPIIQYKIVALNGDQVVETADAICKFISDKYYQDA 402 Q86HW7 Nuclear transport factor 2 nutf2 44689 Yes SL-0178 SL-0179 SL-0182 SL-0183 SL-0185 Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}. UNIPROT Q86HW7 UNIPROT Q551K9 Pfam PF02136 PROSITE PS50177 Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}. O76329 EBI-922673,EBI-922768 GO:0005829 GO:0005635 GO:0005637 GO:0005640 GO:0044613 GO:0005654 GO:0008536 GO:0017056 GO:0051028 GO:0006913 GO:0006606 MQSVDPQVVGVGKQFVEHYYGIFDSNRAGLTQIYQQQTTLTWEGKFLSGADAIVKHIVELPFQQTNRKINSIDCQQTYQPGIMITVTGTLIIDGEAKNQLKFVQVFNLASNNGSFLLINDFFRLVLD 127 Q86UE4 Protein LYRIC MTDH 9606 Yes SL-0178 SL-0182 SL-0198 Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain (By similarity). TNF-alpha causes translocation from the cytoplasm to the nucleus. {ECO:0000250}. UNIPROT Q86UE4 UNIPROT Q05DH2 UNIPROT Q52QU9 UNIPROT Q6PK07 UNIPROT Q8TCX3 PDB 4QMG Pfam PF15686 OMIM 610323 DisGeNET 92140 Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}. A0A142I5B9 EBI-20625235,EBI-1046588 P02545 EBI-351935,EBI-1046588 P08473 EBI-353759,EBI-1046588 Q04206 EBI-1046588,EBI-73886 Q92793 EBI-1046588,EBI-81215 Q5S007 EBI-5323863,EBI-1046588 Q9HBL7 EBI-714824,EBI-1046588 Q9NWT6 EBI-745632,EBI-1046588 P14316 EBI-2866589,EBI-1046588 Q99558 EBI-358011,EBI-1046588 Q9UKV8 EBI-528269,EBI-1046588 Q7KZF4 EBI-1046588,EBI-1044112 O95166 EBI-712001,EBI-1046588 P03372 EBI-78473,EBI-1046588 Q8N6M0 EBI-2510892,EBI-1046588 Q6ZWV7 EBI-2554199,EBI-1046588 Q96Q45 EBI-2602465,EBI-1046588 Q9P0N5 EBI-721260,EBI-1046588 Q9NPD3 EBI-371823,EBI-1046588 P11279 EBI-2805407,EBI-1046588 P27824 EBI-355947,EBI-1046588 Q9Y466 EBI-11792373,EBI-1046588 Q9C0D3 EBI-1046588,EBI-1811414 O75324 EBI-21894129,EBI-1046588 P68400 EBI-347804,EBI-1046588 P0DOE9 EBI-6138585,EBI-1046588 Q13618 EBI-456129,EBI-1046588 O60739 EBI-1046588,EBI-1043343 Q9NX58 EBI-1046588,EBI-713507 P28562 EBI-975493,EBI-1046588 Q8NEH6 EBI-1046588,EBI-743811 P0DTD1 EBI-25475891,EBI-1046588 Q5JR59-3 EBI-11522433,EBI-1046588 Q8IXJ6-2 EBI-5240785,EBI-1046588 GO:0016324 GO:0005923 GO:0005737 GO:0005783 GO:0005789 GO:0001650 GO:0016021 GO:0046581 GO:0016604 GO:0031965 GO:0005634 GO:0048471 GO:0003725 GO:0051059 GO:0003723 GO:0001085 GO:0003713 GO:0003712 GO:0070830 GO:0031663 GO:0043066 GO:0000122 GO:0045766 GO:0010508 GO:0043123 GO:0051092 GO:0051897 GO:0006357 MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET 582 Q86UE8 Serine/threonine-protein kinase tousled-like 2 TLK2 9606 Yes SL-0198 Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2. UNIPROT Q86UE8 UNIPROT D3DU07 UNIPROT Q9UKI7 UNIPROT Q9Y4F7 PDB 5O0Y Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 608439 OMIM 618050 DisGeNET 11011 Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:9427565}.Mental retardation, autosomal dominant 57 (MRD57) [MIM:618050]: A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD57 is characterized by delayed psychomotor development apparent in infancy or early childhood, and a variety of behavioral abnormalities. Affected individuals may have severe gastro- intestinal problems, and facial dysmorphism. MRD57 inheritance is autosomal dominant. {ECO:0000269|PubMed:27479843, ECO:0000269|PubMed:29861108}. Note=The disease is caused by mutations affecting the gene represented in this entry. Self EBI-1047967,EBI-1047967 Q0D2I5 EBI-742894,EBI-1047967 Q53SF7 EBI-2835780,EBI-1047967 Q15306 EBI-751345,EBI-1047967 Q92985 EBI-968267,EBI-1047967 Q15418 EBI-963034,EBI-1047967 Q9NVP2 EBI-1047967,EBI-1055650 Q8NHQ1 EBI-739624,EBI-1047967 P26367 EBI-747278,EBI-1047967 Q02548 EBI-296331,EBI-1047967 Q96NE9-2 EBI-13213391,EBI-1047967 Q9NPF5 EBI-399105,EBI-1047967 Q7KZS0 EBI-10180829,EBI-1047967 Q96IK5 EBI-2548508,EBI-1047967 Q96FJ2 EBI-742371,EBI-1047967 P63167 EBI-349105,EBI-1047967 Q9BWV3 EBI-11898670,EBI-1047967 Q8IY63 EBI-1057112,EBI-1047967 Q9UN30 EBI-6911404,EBI-1047967 GO:0005882 GO:0005634 GO:0048471 GO:0005524 GO:0004674 GO:0007049 GO:0006974 GO:0071480 GO:0006325 GO:0007059 GO:0035556 GO:0010507 GO:0032435 GO:0018105 GO:0006468 GO:0001672 MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPRGHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLDTEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN 772 Q86VE9 Serine incorporator 5 SERINC5 9606 Yes SL-0198 Cell membrane {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (PubMed:26416733, PubMed:26416734). Localizes to the cell membrane, where it is efficiently incorporated into budding virions and impairs subsequent virion entry into target cells (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}. UNIPROT Q86VE9 UNIPROT B4DMH7 UNIPROT Q495A4 UNIPROT Q495A6 Pfam PF03348 OMIM 614551 DisGeNET 256987 Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}. GO:0005813 GO:0005829 GO:0070062 GO:0005794 GO:0016021 GO:0043231 GO:0016020 GO:0043209 GO:0048471 GO:0005886 GO:0051607 GO:0009597 GO:0045087 GO:0006564 GO:0042552 GO:0006658 GO:0008654 GO:1904219 GO:1904222 GO:0006665 GO:0016032 MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFHLLP 423 Q86VF5 2-acylglycerol O-acyltransferase 3 MOGAT3 9606 Yes SL-0198 Endoplasmic reticulum membrane {ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}. UNIPROT Q86VF5 UNIPROT Q496A6 UNIPROT Q496A7 UNIPROT Q496A8 UNIPROT Q9UDW7 Pfam PF03982 OMIM 610184 DisGeNET 346606 Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. {ECO:0000269|PubMed:12618427, ECO:0000269|PubMed:27184406}. GO:0005789 GO:0016021 GO:1990578 GO:0003846 GO:0004144 GO:0006071 GO:0019432 MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYLVWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMCTGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQPQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRLKAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI 341 Q86Y07 Serine/threonine-protein kinase VRK2 VRK2 9606 Yes SL-0178 [Isoform 1]: Cytoplasm. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8BN21}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16704422}. Nucleus {ECO:0000269|PubMed:16704422}. UNIPROT Q86Y07 UNIPROT B4DKL0 UNIPROT D6W5D4 UNIPROT D6W5D6 UNIPROT Q49AK9 UNIPROT Q53EU9 UNIPROT Q53S39 UNIPROT Q53S77 UNIPROT Q53TU1 UNIPROT Q86Y08 UNIPROT Q86Y09 UNIPROT Q86Y10 UNIPROT Q86Y11 UNIPROT Q86Y12 UNIPROT Q8IXI5 UNIPROT Q99987 PDB 2V62 PDB 5UU1 PDB 6NCG Pfam PF00069 PROSITE PS50011 PROSITE PS00108 OMIM 602169 DisGeNET 7444 Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen- activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant. Isoform 2 phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity. P02545 EBI-351935,EBI-1207615 P10415 EBI-77694,EBI-1207615 P62826 EBI-286642,EBI-1207615 O43318 EBI-1207615,EBI-358684 Q9HBL7 EBI-714824,EBI-1207615 P03372 EBI-78473,EBI-1207615 P60953 EBI-81752,EBI-1207615 Q8IVT5 EBI-486984,EBI-1207615 Q02750 EBI-492564,EBI-1207615 Q6ZWV7 EBI-2554199,EBI-1207615 Q6NUS6 EBI-11278332,EBI-1207615 Q5HYA8 EBI-11334880,EBI-1207615 Q96GX1 EBI-11349465,EBI-1207615 Q9P0N5 EBI-721260,EBI-1207615 Q86UK5 EBI-7260649,EBI-1207615 Q86X19 EBI-11343485,EBI-1207615 F8VQC7 EBI-11104531,EBI-1207615 Q13418 EBI-747644,EBI-1207615 Q86WU2 EBI-11156684,EBI-1207615 P46013 EBI-876367,EBI-1207615 P11279 EBI-2805407,EBI-1207615 P27824 EBI-355947,EBI-1207615 Q07817-1 EBI-287195,EBI-1207615 Q07812 EBI-516580,EBI-1207615 P03182 EBI-1207615,EBI-1207659 Q0VAB0 EBI-18271435,EBI-1207615 P36382 EBI-750433,EBI-1207615 Q8N4V1 EBI-6163737,EBI-1207615 Q6PEY1 EBI-17198826,EBI-1207615 Q6UW68 EBI-6269551,EBI-1207615 Q9NUH8 EBI-8638294,EBI-1207615 Q13520 EBI-13059134,EBI-1207615 P38432 EBI-1207615,EBI-945751 GO:0005737 GO:0005783 GO:0005789 GO:0016021 GO:0031966 GO:0005635 GO:0005634 GO:0032991 GO:0005524 GO:0019904 GO:0019901 GO:0004674 GO:0034599 GO:0018105 GO:0046777 GO:0006468 GO:2000659 GO:0043408 GO:0016032 GO:0016055 MPPKRNEKYKLPIPFPEGKVLDDMEGNQWVLGKKIGSGGFGLIYLAFPTNKPEKDARHVVKVEYQENGPLFSELKFYQRVAKKDCIKKWIERKQLDYLGIPLFYGSGLTEFKGRSYRFMVMERLGIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGNHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLKWAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILNPHGIPLGPLDFSTKGQSINVHTPNSQKVDSQKAATKQVNKAHNRLIEKKVHSERSAESCATWKVQKEEKLIGLMNNEAAQESTRRRQKYQESQEPLNEVNSFPQKISYTQFPNSFYEPHQDFTSPDIFKKSRSPSWYKYTSTVSTGITDLESSTGLWPTISQFTLSEETNADVYYYRIIIPVLLMLVFLALFFL 508 Q86YW0 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 PLCZ1 9606 Yes SL-0198 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}. UNIPROT Q86YW0 UNIPROT Q08AQ7 UNIPROT Q96J70 Pfam PF00168 Pfam PF09279 Pfam PF00388 Pfam PF00387 PROSITE PS50004 PROSITE PS50222 PROSITE PS50007 PROSITE PS50008 OMIM 608075 OMIM 617214 DisGeNET 89869 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:Q8K4D7, ECO:0000269|PubMed:12416999, ECO:0000269|PubMed:14697805, ECO:0000269|PubMed:15579586, ECO:0000269|PubMed:26721930, ECO:0000305}.Spermatogenic failure 17 (SPGF17) [MIM:617214]: An autosomal recessive infertility disorder due to failure of oocyte activation and fertilization by sperm that otherwise exhibits normal morphology. {ECO:0000269|PubMed:26721930}. Note=The disease is caused by mutations affecting the gene represented in this entry. P06748 EBI-78579,EBI-20834348 P68032 EBI-352273,EBI-20834348 P14314 EBI-716953,EBI-20834348 GO:0005623 GO:0005829 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0045120 GO:0061827 GO:0005509 GO:0004435 GO:0032266 GO:0005546 GO:0010314 GO:0007343 GO:0043647 GO:0032959 GO:0016042 GO:0007275 GO:0048015 GO:0007204 GO:0060470 GO:0051209 MEMRWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKQIFKDNDRLKQGRITIEEFRAIYRIITHREEIIEIFNTYSENRKILLASNLAQFLTQEQYAAEMSKAIAFEIIQKYEPIEEVRKAHQMSLEGFTRYMDSRECLLFKNECRKVYQDMTHPLNDYFISSSHNTYLVSDQLLGPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTSDYPVVLSLENHCSTAQQEVMADNLQATFGESLLSDMLDDFPDTLPSPEALKFKILVKNKKIGTLKETHERKGSDKRGDNQDKETGVKKLPGVMLFKKKKTRKLKIALALSDLVIYTKAEKFKSFQHSRLYQQFNENNSIGETQARKLSKLRVHEFIFHTRKFITRIYPKATRADSSNFNPQEFWNIGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPHFLRESKSYFNPSNIKEGMPITLTIRLISGIQLPLTHSSSNKGDSLVIIEVFGVPNDQMKQQTRVIKKNAFSPRWNETFTFIIHVPELALIRFVVEGQGLIAGNEFLGQYTLPLLCMNKGYRRIPLFSRMGESLEPASLFVYVWYVR 608 Q8AIH4 Protein Nef NEF 388910 Yes SL-0382 Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}. UNIPROT Q8AIH4 Pfam PF00469 Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28 and probably other immunity surface molecules. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike (By similarity). {ECO:0000250}. GO:0005576 GO:0044220 GO:0020002 GO:0016020 GO:0019012 GO:0005525 GO:0017124 GO:0030683 GO:0009405 MGNIFGRWPGARKAIEDLHNTSSEPVGQASQDLQNKGGLTTNTLGTSADVLEYSADHTEEEVGFPVRPAVPMRPMTEKLAIDLSWFLKEKGGLDGLFFSPKRAAILDTWMYNTQGVFPDWQNYTPGPGIRYPLCRGWLFKLVPVDPPEDDEKNILLHPACSHGTTDPDGETLIWRFDSSLARRHIARERYPEYFK 195 Q8AWW4 E3 ubiquitin-protein ligase RNF128 rnf128 8355 No SL-0198 Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q8AWW4 Pfam PF02225 Pfam PF13639 PROSITE PS50089 E3 ubiquitin-protein ligase that catalyzes polyubiquitin chains (By similarity). Converts epidermis into cement gland and neural tissue in whole embryos. {ECO:0000250, ECO:0000269|PubMed:12435366}. GO:0012505 GO:0016021 GO:0048471 GO:0046872 GO:0016740 GO:0016567 MGALKMRCQCFPLPYLSLLALLLLNLSLTRAETLWTANVNYSYVYDNKTYGEEGEIGVFGQDSPIERAAGLVVLPKSEKLYTACKDNVNFSVPSGWTGPWIALIQRGGGCTFTEKINRAAERGARAVVVYNNGIDNEVFEMSHPGTKDTVAIMIGNLKGNEIVDLIKGGMQVTMVIEVGRKHGSWINHYSIFFVSVSFFIVTAATVGYFIFYSARRWRLTRAQNKKQKRLKAEAKKAIGKLQLRTIKQGDKVLGPDGDSCAVCIEPYKPSDVVRILTCNHFFHKNCIDPWLLEHRTCPMCKCDILKSLGIAEDEEEGTSVAIPSVSSELQRSTVQITEEENHSETASSGYASVRGGDEQVDEGQHIYENTELVHEASATSIEVLPHMDNPGFESEDVHVHEMKS 404 Q8B912 Non-structural protein 12 rep 300563 Yes SL-0382 [Nsp1]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-beta papain-like cysteine proteinase]: Host cytoplasm {ECO:0000250}. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}. UNIPROT Q8B912 UNIPROT Q8B911 Pfam PF16749 Pfam PF14757 Pfam PF14756 Pfam PF05410 Pfam PF05411 Pfam PF05412 Pfam PF05579 Pfam PF00680 Pfam PF01443 PROSITE PS51538 PROSITE PS51493 PROSITE PS51539 PROSITE PS51540 PROSITE PS51652 PROSITE PS51657 PROSITE PS50507 The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. Nsp1-alpha inhibits IFN-beta production. Counteracts the action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-alpha is suppressed. This leads to the blockage of NF-kappaB nuclear translocation and thus interference of NF-kappaB activation. Also seems to inhibit IRF3-dependent pathways (By similarity). {ECO:0000250}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. Deubiquitinates host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation (By similarity). {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}. GO:0033644 GO:0042025 GO:0044220 GO:0016021 GO:0005524 GO:0004197 GO:0003678 GO:0003723 GO:0003724 GO:0003968 GO:0004252 GO:0036459 GO:0008270 GO:0039648 GO:0039579 GO:0039644 GO:0039563 GO:0039502 GO:0006351 GO:0019082 GO:0039694 MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVPELGVLGLFYRPEEPLRWTLPRAFPTVECSPTGACWLSAIFPIARMTSGNLNFQQRMVRVAGEIYRAGQLTPTVLKTIQVYERGCRWYPIVGPVPGVGVYANSLHVSDKPFPGATHVLTNLPLPQRPKPEDFCPFECAMADVYDIGRGAVMYVAGGKVSWAPRGGDEVKFEPVPKELKLVANRLHTSFPPHHVVDMSKFTFMTPGSGVSMRVEYQYGCLPADTVPEGNCWWRLFDLLPPEVQNKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTDTHGPIVIQYFSVKESWIRHLKPVEEPSLPGFEDLLRIRVEPNTSPLAGKNEKIFRFGSHKWYGAGKRARKARSGATTMVAHRASSAHETRQATKHEGAGANKAEHLKLYSPPAEGNCGWHCISAIVNRMVNSNFETTLPERVRPPDDWATDEDLVNTIQILRLPAALDRNGACGGAKYVLKLEGEHWTVSVNPGMSPSLLPLECVQGCCEHKGGLGSPDAVEVSGFDPACLDRLLQVMHLPSSTIPAALAELSDDSNRPVSPAAATWTVSQSYARHRGGNHHDQVCLGKIISLCQVIEDCCCHQNKTNRATPEEVAAKIDQYLRGATSLEECLAKLERVSPPGAADTSFDWNVVLPGVEAAHQTTEQLHVNPCRTLVPPVTQEPLGKDSVPLTAFSLSNCYYPAQGNEVRHRERLNSVLSKLEEVVLEEYGLMSTGLGPRPVLPSGLDELKDQMEEDLLKLANTQATSEMMAWAAEQVDLKAWVKSYPRWTPPPPPPRVQPRKTKSVKSLPEDKPVPAPRRKVRSGCGSPVLMGDNVPNGSEDLTVGGPLNFPTPSEPMTPMSEPVLTPALQRVPKLMTPLDGSAPVPAPRRTVSRPMTPLSEPIFLSAPRHKFQQVEEANPATTTLTHQNEPLDLSASSQTEYEASPLASSQNMSILEAGGQEAEEVLSEISDILNDTSPAPVSSSSSLSSVKITRPKYSAQAIIDSGGPCSGHLQKEKEACLSIMREACDASKLSDPATQEWLSRMWDRVDMLTWRNTSAYQAFRTLNGRFEFLPKMILETPPPHPCGFVMLPHTPAPSVSAESDLTIGSVATEDVPRILGKIGDTGELLNQGPSAPFKGGPVCDQPAKNSRMSPRESDESIIAPPADTGGAGSFTDLPSSDSVDANGGGPLRTVKTKAGRLLDQLSCQVFSLVSHLPVFFSHLFKSDSGYSPGDWGFAAFTLFCLFLCYSYPFFGFAPLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGTACEFDSPECRNVLHSFELLKPWDPVRSLVVGPVGLGLAILGRLLGGARYVWHFLLRFGIVADCILAGAYVLSQGRCKKCWGSCVRTAPNEIAFNVFPFTRATRSSLIDLCDRFCAPKGMDPIFLATVWRGCWTGRSPIEQPSEKPIAFAQLDEKRITARTVVAQPYDPNQAVKCLRVLQAGGAMVAEAVPKVVKVSAIPFRAPFFPAGVKVDPECRIVVDPDTFTTALRSGYSTTNLVLGMGDFAQLNGLKIRQISKPSGGGSHLVAALHVACSMALHMLAGVYVTAVGSCGTGTNDPWCTNPFAAPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGLQEIALVVLIFVSMGGMAHRLSCKADMLCILLAIASYVWVPLTWLLCVFPCWLRWFSLHPLTILWLVFFLISVNIPSGILAVVLLVSLWLLGRYTNIAGLVTPYDIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTQKPSLNTVNVVGSSMGSGGVFTIDGKIKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKAQFCEDGWTGRAYWLTSSGVEPGVIGNGFAFCFTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVTPIKLSELSEFFAGPKVPLGDVKIGSHIIKDTCEVPSDLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVGFFILNEILPAVLVRSVFSFGMFVLSWLTPWSAQVLMIRLLTAALNRNRLSLGFYSLGAVTSFVADLAVTQGHPLQVVMNLSTYAFLPRMMVVTSPVPVIACGVVHLLAIILYLFKYRCLHYVLVGDGVFSSAFFLRYFAEGKLREGVSQSCGMSHESLTGALAMRLTDEDLDFLTKWTDFKCFVSASNMRNAAGQFIEAAYAKALRIELAQLVQVDKVRGTLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSKMTVARVVDPTPAPPPVPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEAVGIFVMDGKKYQKFWDKNSGDVFYEEVHNSTDEWECLRAGDPADFDPETGVQCGHITIEDRVYNVFTSPSGRKFLVPANPENRRAQWEAAKLSVEQALGMMNVDGELTAKELEKLKGIIDKLQGLTKEQCLNCLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPVARPVDGGVVLLRSAVPSLIDVLISGADASPKLLARHGPGNTGIDGTLWDFEAEATKEEVALSAQIIQACDIRRGDAPEIGLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPSGFELYVPTIPASVLDYLDSRPDCPKQLTEHGCEDAALRDLSKYDLVTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFPTKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAALSGVTQGFMKKAFNSPIALGKNKFKELQTPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSVSNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPSMPNYHWWVEHLNLMLGFQTDPKKTAITDSPTFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCARKDGYSFPGPPFFLSMWEKLRSNHEGKKSRMCGYCMAPAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCGECEPPLGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVDLPDGDYASTALLPTCKEINMVAVAPNVLRSRFIIGPPGAGKTHWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPAPSRTGPWVRILAGGWCPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLVSMVNTTRVTYVEKPVRYGQVLTPYHRDREDGAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQLQSMFDLPAKGTPVNLAVHRDEQLIVLDRNNKEITVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGFYFSPDLTQFAKLPAELAPHWPVVTTQNNERWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVRGEAQVLPETVFSTGRIEVDCREYLDDREREVAESLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGEAAKAFCTLTDVYLPDLEAYLHPETQSKCWKVMLDFKEVRLMVWKGKTAYFQLEGRHFTWYQLASYTSYIRVPVNSTVYLDPCMGPALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGEDWEDYNGAFRARQKGKIYKATATSMKFHFPPGPVIEPTLGLN 3961 Q8BFW9 Solute carrier family 2, facilitated glucose transporter member 12 Slc2a12 10090 Yes SL-0198 Cell membrane {ECO:0000269|PubMed:23041416}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}. UNIPROT Q8BFW9 UNIPROT Q14B60 UNIPROT Q3UPR6 UNIPROT Q8BZB7 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-independent facilitative glucose transporter. {ECO:0000269|PubMed:23041416}. GO:0012505 GO:0005887 GO:0016020 GO:0048471 GO:0005351 GO:0046323 GO:1904659 MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTCHEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKVLRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVVSTIPATLLVDHIGSKTFLCIGSSVMSASLLTMGIVNLNINMNFTNICRSHSLLNQSLEEFVFYATGNLSISNSSLREHFKRITPYSKGSFMPMGNGMEPKGEMTFTSSLPNAGLSRTEHQGVTDTAVVPAAYKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGVNLLISLTFLTVTDLIGLSWVCFIYTIMSLASLAFVVLFIPETKGCSLEQISVELAKANYVKNNICFMSHHQEELVPTQLQKRKPQEQLPECNHLCGRGQSQRPSPDT 622 Q8BIA4 F-box/WD repeat-containing protein 8 Fbxw8 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DL28}. Golgi apparatus {ECO:0000250|UniProtKB:P0DL28}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}. UNIPROT Q8BIA4 UNIPROT Q8BI62 UNIPROT Q8BI75 UNIPROT Q8BI76 UNIPROT Q8CID8 UNIPROT Q921Z1 Pfam PF12937 PROSITE PS50181 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 Substrate-recognition component of a Cul7-RING ubiquitin- protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7- RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). {ECO:0000250|UniProtKB:Q8N3Y1}. GO:1990393 GO:0031467 GO:0005829 GO:0005794 GO:0070545 GO:0048471 GO:0030687 GO:0019005 GO:0004842 GO:0008283 GO:0007030 GO:0060716 GO:0000460 GO:0000470 GO:0050775 GO:1901485 GO:0016567 GO:0060712 GO:0006511 MDDHNLEEFRRHWQEELAQSQALRRRRRLEAGERRSPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRGGDRKDTSSRSRSPPDRDATEPEPLVDQLIRDLNELDDVPFFDVRLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAKEHTLRANWKNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNIWDLRTGRFPIFRFEHDARIQALALSQEKPIVATASAFDVVMLYPNEEGHWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKADDSARTLHYVYGQPATCLDVSASQVAFGVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRIHDLRSDKIALSLSAHQLGVSAVQMDDWKVVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYLSFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFAVDQLAFQSPLPVCRLPRDIMAGYSYDLALSFPHDSI 598 Q8BJS4 SUN domain-containing protein 2 Sun2 10090 Yes SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}. Endosome membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes. {ECO:0000269|PubMed:24586178}. UNIPROT Q8BJS4 UNIPROT Q3TBU0 UNIPROT Q3U160 UNIPROT Q6B4H2 PDB 5ED8 PDB 5ED9 Pfam PF07738 Pfam PF18580 PROSITE PS51469 As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. {ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752, ECO:0000269|PubMed:24586178, ECO:0000305}. Q3U1F9 EBI-8468834,EBI-646914 P39428 EBI-646914,EBI-520123 GO:0005623 GO:0000794 GO:0010008 GO:0005639 GO:0034993 GO:0000784 GO:0005635 GO:0005637 GO:0031965 GO:0042802 GO:0005521 GO:0043495 GO:0051642 GO:0090286 GO:0051321 GO:0006998 GO:0090292 GO:0031022 GO:0021817 GO:0030335 MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESYIGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQHSSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGLTYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGMVDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH 731 Q8BLR9 Hypoxia-inducible factor 1-alpha inhibitor Hif1an 10090 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}. UNIPROT Q8BLR9 UNIPROT A1L3B7 UNIPROT Q3U3G4 Pfam PF13621 PROSITE PS51184 Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000250|UniProtKB:Q9NWT6, ECO:0000269|PubMed:17636018}. GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0016706 GO:0071532 GO:0031406 GO:0048037 GO:0102113 GO:0005506 GO:0051059 GO:0005112 GO:0036140 GO:0036139 GO:0042803 GO:0008270 GO:0045746 GO:0061428 GO:0055114 GO:0042265 GO:0042264 GO:0036138 GO:0045663 MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN 349 Q8BPY9 Fidgetin-like protein 1 Fignl1 10090 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000269|PubMed:22110678}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage- induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}. UNIPROT Q8BPY9 UNIPROT Q3UF48 UNIPROT Q8C2I6 UNIPROT Q9ERZ5 Pfam PF00004 Pfam PF09336 PROSITE PS00674 Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:17352653). May play a role in the control of male meiosis dynamic (PubMed:22110678). {ECO:0000250|UniProtKB:Q6PIW4, ECO:0000269|PubMed:17352653, ECO:0000269|PubMed:22110678}. GO:0005737 GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0046034 GO:0071479 GO:0031122 GO:0007140 GO:0043066 GO:2001243 GO:0001649 GO:0033687 GO:0051726 GO:0010569 METSSSMSVETTRSVQVDEWQKNYCVVTSSICTPKQKADAYRALLLHIQYAYANSEISQVFATNLFKRYTEKYSAIIDSDNVVTGLNNYAESIFALAGSRQADSNKWQSGLSIDNVFKMSCVQEMMQAGKKFEESLLEPADASVVLCKEPTAFEVPQLSVCGGSEDADILSSSGHDTDKTQAIPGSSLRCSPFQSARLPKETNTTKTCLTSSTSLGESATAAFHMTPLFGNTEKDTQSFPKTSTGLNMFLSNLSCVPSGCENPQERKAFNDSDIIDILSNPTLNKAPSKTEDRGRREDNSLPTFKTAKEQLWVDQKKKGHQSQHTSKSSNGVMKKSLGAGRSRGIFGKFVPPVSNKQDGSEQHAKKHKSSRAGSAEPAHLTDDCLKNVEPRMVELIMNEIMDHGPPVHWDDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVGNLMSKEQCCLSDEETDLVVQQSDGFSGADMTQLCREASLGPIRSLHAADIATISPDQVRPIAYIDFENAFKTVRPTVSPKDLELYENWNETFGCGK 683 Q8BX43 Tumor necrosis factor receptor superfamily member 19L Relt 10090 Yes SL-0198 Cell membrane {ECO:0000250|UniProtKB:Q969Z4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q969Z4}. UNIPROT Q8BX43 UNIPROT Q497Z8 UNIPROT Q8BTV0 Pfam PF12606 Pfam PF00020 May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation (PubMed:30506946). {ECO:0000250|UniProtKB:Q969Z4, ECO:0000269|PubMed:30506946}. GO:0016021 GO:0005654 GO:0048471 GO:0005886 GO:0097186 GO:0006915 MSLQGLMMKRTLLCWPLSCLFVLLPWPLATPTPITPWLCPPGKEPDPDPGQGTLCRTCPPGTFSASWNSYPCQPHYRCSLQKRLEAQAGTATHDTMCGDCQHGWFGPQGVPHVPCQPCSKAPPSTGGCDESGRRGRRGVEVAAGTSSNGEPRQPGNGTRAGGPEETAAQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAQKEVGPSPGGGGSGINPAYRTEDANEDTIGVLVRLITEKKENAAALEELLKEYHSKQLVQTSHRPVPRLLPASPSIPHICPHHHHLHTVQGLASLSGPCCSRCSQKWPEVLLSPEAAAATTPAPTLLPTASRAPKASAKPGRQGEITILSVGRFRVARIPEQRTSSLLSEVKTITEAGPSEGDLPDSPQPGLPPEQRALLGSGGSHTKWLKPPAENKAEENRYVVRLSESNLVI 436 Q8BXR9 Oxysterol-binding protein-related protein 6 Osbpl6 10090 Yes SL-0178 Nucleus envelope {ECO:0000269|PubMed:14593528}. Cytoplasm, cytosol {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14593528}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000269|PubMed:30028970}. UNIPROT Q8BXR9 UNIPROT Q8BYW2 Pfam PF01237 Pfam PF15409 PROSITE PS01013 PROSITE PS50003 Regulates cellular transport and efflux of cholesterol (By similarity). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (PubMed:30028970). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (PubMed:30028970). Weakly binds 25-hydroxycholesterol (By similarity). {ECO:0000250|UniProtKB:Q9BZF3, ECO:0000269|PubMed:30028970}. Q9EPK7 EBI-6908541,EBI-17170664 GO:0005829 GO:0031901 GO:0005789 GO:0043231 GO:0016020 GO:0031965 GO:0097038 GO:0005886 GO:0015485 GO:0008289 GO:0032934 GO:0015248 GO:0032374 MSSDEKGISPAHKTSTPTHRSASSSTSSQRESRQSIHVLERTASSSTEPSVSRQLLEPEPIPLSKEADSWEIIEGLKIGQTNVQKPDRHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYHLKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPATSTAESSPAANVSVVDGKMQPNSFPWQSPLPCSNSLPATCTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSVSKDTKIQLQEGPPAKGQFNTTRRRQRLAAAVATTVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQEEFCLIAQKVHSLLKSAFNSIAIEKEKLKQVVSEQDHNKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESTICDHVVSVNIIPSPDEPGEQIHVSLPLSQQVANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVADNISRQILNGELTGGAFRNGRRTCLPAPCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKASETDDPYERMVLVAAFAVSGYCSTYFRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIRWKNKFWGKSMEILPVGTLNVTLPKYGDYYVWNKVTTCIHNILSGRRWIEHYGEVTLRNTKSSVCICKLTFVKVNYWNSNVNEVQGVVIDQEGKVVHRLFGKWHEGLYCGVAPSAKCIWRPGSLPTNYELYYGFTRFAVELNELDPVLKDLLPPTDARFRPDQRFLEEGNLEAAAAEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW 959 Q8C0T9 Adenylate cyclase type 10 Adcy10 10090 Yes SL-0198 Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000269|PubMed:12475901}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane- associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}. UNIPROT Q8C0T9 UNIPROT B2RRJ9 UNIPROT Q3V0F8 Pfam PF00211 PROSITE PS50125 Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP- responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (PubMed:14976244, PubMed:16054031). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244, ECO:0000269|PubMed:16054031}. GO:0045177 GO:0016324 GO:0030424 GO:0045178 GO:0005737 GO:0005829 GO:0030425 GO:0005576 GO:0030426 GO:0016020 GO:0015630 GO:0005739 GO:0031514 GO:0043025 GO:0005634 GO:0048471 GO:0004016 GO:0005524 GO:0051117 GO:0071890 GO:0000287 GO:0030145 GO:0006171 GO:0071241 GO:0003351 GO:0035556 GO:0043065 GO:0007283 MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYISAIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEAEEGLDIRVKIGLAAGHITMLVFGDETRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFTKCMGFMDYYPSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVHITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNRYEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQILMANVLGLDTCKHYKERQTNLQNRVKTLLDEKFHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILAQTVREERIIFIIDEAQFVDGTSWAFIEKLIRSMPIFIVMSLAPFSEVPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIPRELDSYLVEGSCGIPYYCEELLKNLDHHRVLLFQQAETEQKTNVTWNNMFKHSVRPTDDMQLFTSISEGQKEVCYLVSGVRLNNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFNCFRSSKDLQLALKQNVPTFEVHYRSLALKLKEGLTYGEEEELREMEGEVVECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEESAHRCNHCRNVDFIPYHHFIVDIRLNTLDMDTVKRMVTSQGFKIDEEEAIFSKSELPRKYKFPENLSITEIREKILHFFDNVILKMKSSPNDIIPLESCQCKELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTNEDSWSQTFEYATFYSLKAEVCFNMGQMVLAKKMLRKALKLLNRMFPCNLLTLTFQMHVEKNRLSHFMNQHTQEGSVPGKKLAQLYLQASCFSLLWRIYSLNFFFHYKYYGHLAAMMEMNTSLETQNDFQIIKAYLDFSLYHHLAGYQGVWFKYEILVMEQLLNLPLKGEAIEIMAYTADTLGHIKFLMGHLDLAIELGSRAHRMWSLLRNPNKYQMVLCRLSKPLFLKSRYKHLVQVLGWLWDLSVTEEDIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFNKFSDRAKHLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVEILKALETLVAQNTTGPVFYPRLYHLMAYVCILMGDGHSCDFFLNTALELSETHGNLLEKCWLSMSKEWWYSASELTGDQWLQTVLSLPSWDKIVSGKGGQRKRSWSWFCPPNFSMVSWSQPQCA 1614 Q8C0V1 Telomere repeats-binding bouquet formation protein 1 Terb1 10090 Yes SL-0178 SL-0179 SL-0182 Chromosome, telomere {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres during meiotic prophase (PubMed:24413433). In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane (PubMed:26548954). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}. UNIPROT Q8C0V1 UNIPROT A1L2Z9 UNIPROT E9QPF2 UNIPROT Q14CI1 UNIPROT Q8C0N5 PDB 1X58 PROSITE PS50176 Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis (PubMed:24885367, PubMed:24413433, PubMed:26548954). Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN- TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA (PubMed:26548954). In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment' (PubMed:26548954). Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex (PubMed:24885367, PubMed:24413433). Also recruits cohesin to telomeres to develop structural rigidity (PubMed:24413433). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954, ECO:0000305|PubMed:24885367}. GO:0005623 GO:0000781 GO:0000784 GO:0005637 GO:0003677 GO:0070197 GO:0045141 GO:0007129 MESEKPKKTQEMKTDLKLLLECLKYHMGNPLSQKEVLITIHSVCKQNSDAGIYFREIGGLMFIINLAKSSEQSLVKEAALYTLGSIAEENVYCQQSLCTSELFQDLTGLLTNDDSNTNLKRMSVYVLLVLVSNNRNGQTLVREVGCIEVLSQMFRTVLSNYELNLSDNSVFQSYLLWSSVCSTLCVCVNNPQNDENQMLCCSLFPCVNEWLMNCMRPEVIRPICSFIGLTLANNTHAQNCFVSSGGLDVLCQVLVQLESDSHNTLSSAKLAVIVTKTMDACITDNSAAFTVVLSKYHIVSTLLALLLHESLDSREKFSIILAIGHCTEDCEKNQYELLKNNGLPLMIQALTEFKNEDLSKAATYVLHNCKKITGKLSLSLGQNSFGENEIELKDISEKETLREHWKAAKEILCRIKQFEKGGKEEKQQNRSGHYKDNTPSMKVNIQTNLKRLCADSTGGTRAEDKDINQSRELRSYKPSEIMSKACANENQLTTRKKNTNPVHPFCKEKGQSKIVHETTPSCAQNLDKEKTFDQKDSVSQSSDQVLKHLPHTVKNRKQVPETDPFTLCLDIIDREVGIQATDSCSRMLKYTCSGCIVARKLLNSRNFSKFLHSCAYQCVHHKVIMEAEDKYKNELRKTFICAKKILLTPCRRRQLCKESTASEELKIVHQKPDSKKLPGLEAQALNTSIPEAMERRSPVPGQSGLHKKRRIRKDFTKEEVNYLFHGVKTMGNHWNSILWSFPFQKGRRAVDLAHKYHRLIKGPSCAAL 768 Q8C6M1 Ubiquitin carboxyl-terminal hydrolase 20 Usp20 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. UNIPROT Q8C6M1 UNIPROT Q69ZT5 UNIPROT Q8CJ72 Pfam PF06337 Pfam PF00443 Pfam PF02148 PROSITE PS51283 PROSITE PS00972 PROSITE PS00973 PROSITE PS50235 PROSITE PS50271 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. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. Q9UHL9 EBI-12517048,EBI-372530 GO:0005813 GO:0005737 GO:0048471 GO:0004197 GO:0001664 GO:0004843 GO:0036459 GO:0008270 GO:0006897 GO:0016579 GO:0071108 GO:0070536 GO:0008277 GO:0006511 MGDARDLCPHLDCIGEVTKEDLLLKSKGTCQSCGVAGPNLWACLQVTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRVWCYACEREVFLEQRLAVHLASSSARLSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPMVAAVAALTDARDSDSSDTDERRDGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSKAEMELLISDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMASLDEQSREAQPPSPRSTSPCQTPEPDNEAHIRSSSRPCSPVHHHHEGHSKLSSSPPRASPVRMGPSYVLKKAQVPSTGGRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYSSQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRPFLAKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQSVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEIDTFIKLNKAFQAEESPAVIYCISMHWFREWEAFVKGKDSEPPGPIDNSRIAQVKGSGHIQLKQGADCGQISEETWTYLSSLYGGGPEIAIRQSVAQLPDPESLHGEQKIEAETRAL 916 Q8CEC0 Nuclear pore complex protein Nup88 Nup88 10090 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}. UNIPROT Q8CEC0 UNIPROT Q80Z13 UNIPROT Q8K090 Pfam PF10168 Component of nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}. P62826 EBI-2553822,EBI-286642 Q8WYU3 EBI-2553822,EBI-2555238 Q99567 EBI-2553822,EBI-726178 B4DYZ6 EBI-2553822,EBI-2562666 O14980 EBI-2553822,EBI-355867 Q9EPK7 EBI-6908541,EBI-2553822 GO:0005643 GO:0005654 GO:0017056 GO:0000278 GO:0006406 GO:0006611 GO:0006606 GO:0000055 GO:0000056 MAAAVGPLGDGELWQSWLPNHVVFLRLREGVRNQSPAEAEKPAASTSPSCPSLPPHLPTRNLVFGLGGELFLWDAEGSAFLVVRLRGPSGGGVEPPLSQYQRLLCINPPLFEIHQVLLSPTQHHVALIGSKGLMALELPQRWGKDSEFEGGKATVNCSTIPIAERFFTSSTSLTLKHAAWYPSEMLDPHIVLLTSDNVIRIYSLREPQTPTKVIVLSEAEEESLILNKGRAYTASLGETAVAFDFGPLVTVSKNIFEQKDRDVVAYPLYILYENGETFLTYVSLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAILCLPCVPNILVIATESGMLYHCVVLEGEEEDDQTLEKSWDPRADFIPSLYVFECVELELALKLASGEDDPFASDFSCPIKLHRDPKCPSRYHCSHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELTAEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPTMICITSTYECLIRPLLSTVHPASPPLLCTQEDAEVAESPLRILAETPDSFEKHIKRILQRSAANPAFLKNCSARSSEKDLAPPPEECLQLISRATQVFREQYILKQDLAKEEIQRRVKLLCDQKRKQLEDLNYCREERVSHLFRKSLREMAERLADKYEEAKEKQEDIMNRMKKVLHSFHAQLPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQRKMEKVLSPQKPTITLSAYQRKCIQSILKEEGEHIREMVKQINDIRNHVTF 753 Q8CFE4 SCY1-like protein 2 Scyl2 10090 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Endosome membrane {ECO:0000250}. Note=Plasma membrane-associated in clathrin- coated vesicles. Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes (By similarity). {ECO:0000250}. UNIPROT Q8CFE4 UNIPROT Q3UT57 UNIPROT Q3UWU9 UNIPROT Q8K0M4 Pfam PF00069 PROSITE PS50011 Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. May be a serine/threonine-protein kinase. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system (By similarity). {ECO:0000250}. GO:0030136 GO:0010008 GO:0005794 GO:0048471 GO:0005524 GO:0004672 GO:0005102 GO:0008333 GO:0090090 GO:2000370 GO:0002092 GO:2000286 MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSSISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNVTPENVILNKSGAWKIMGFDFCVSSSNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGAVMYAVFNQGRPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTSIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYIKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFSSFIAVIKEMLSRLESEHRTKLEQLHVMQEQQRSLDIGNQMSTSEETKVAHSGSQQIDKVFNNIGADLLSGSESENREDGMQGKQKRGSLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPIAPIKQTKDLTDTLMENMSSLTSLSVSTPKISASSTFTPVPSTGLGMMFSTPIDNTKRNLTNGLNANMGFQTSGFSMPVNPNQNFFSGTGTAGVTTMSLGAPPTMSNFSPLTIPPASVKQPQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFAPPQGSPVMGSAAMGTQGNVMGQAAFGMQGNPFFNPQNFAQPPPTTMTSSSSASNDLKDLFG 930 Q8CGZ0 Calcium homeostasis endoplasmic reticulum protein Cherp 10090 Yes SL-0198 Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region. Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}. UNIPROT Q8CGZ0 UNIPROT Q8K291 UNIPROT Q8VCD2 Pfam PF04818 Pfam PF01585 Pfam PF01805 PROSITE PS51391 PROSITE PS50174 PROSITE PS50128 Involved in calcium homeostasis, growth and proliferation. {ECO:0000250|UniProtKB:Q8IWX8}. Q13131 EBI-1181405,EBI-2366446 Q15637 EBI-2366446,EBI-744603 GO:0005623 GO:0005737 GO:0048471 GO:0033017 GO:0044325 GO:0003723 GO:0006874 GO:0008285 GO:0070886 GO:0051209 GO:0006396 MEMPMPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQAPELEPTSAMPPLPQPPLAPTASLTPAQGTPSMDELIQQSQWSLQQQEQHLLALRQEQVTTAVAHAVEQQMQKLLEETQLDMSEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQSLKTQHEEFVSSLAQQQQQQQQQQQQQPQPQPQPQIQLPQMEADVKATPPPPAPPPASAPAPTIPPTTQPDDNKPPIQMPGSSEYDTSAGVQDPAAAGPRGPGPHEQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDPNWNNQFEGPWNNQHEPPPWGGAQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPADMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSSSRSSKSSRSSSRSHSRSRSRSSSRSRSRSRSRSRSSRSRSRSRSRSRSKSYSPGRRRRSRSRSPTPPSAAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDEFSTFGTRKEEKED 936 Q8CHK4 Histone acetyltransferase KAT5 Kat5 10090 Yes SL-0198 Nucleus {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000269|PubMed:12036595}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region. {ECO:0000250|UniProtKB:Q92993}. UNIPROT Q8CHK4 UNIPROT A1L394 UNIPROT Q8CGZ3 UNIPROT Q8CGZ4 UNIPROT Q8VIH0 Pfam PF01853 Pfam PF11717 Pfam PF17772 PROSITE PS51726 Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (By similarity). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (By similarity). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (By similarity). NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Also acetylates non-histone proteins, such as ATM, NR1D2, RAN, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:22539723). Directly acetylates and activates ATM. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (By similarity). Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. Acetylates RAN at 'Lys-134' (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:22539723). {ECO:0000250|UniProtKB:Q92993, ECO:0000269|PubMed:22539723}. P54254 EBI-1169948,EBI-1169713 P54253 EBI-930964,EBI-1169948 O88495 EBI-1169948,EBI-21227860 P0C0S6 EBI-642131,EBI-1169948 P35583 EBI-2893341,EBI-1169948 P28574 EBI-1183003,EBI-1169948 Q9JI44 EBI-2942577,EBI-1169948 P06151 EBI-1169948,EBI-444940 P51859 EBI-1169948,EBI-2943087 Q80YV3 EBI-1169948,EBI-2942477 Q8CHI8 EBI-1169948,EBI-2942504 Q8WTY4 EBI-1169948,EBI-2943068 Q8R3B7 EBI-1169948,EBI-2942609 P60762 EBI-1169948,EBI-2943018 P63268 EBI-1169948,EBI-2693783 P60710 EBI-1169948,EBI-353957 Q9Z2N8 EBI-1169948,EBI-2942759 P63260 EBI-1169948,EBI-351301 Q8VEK6 EBI-1169948,EBI-2942903 Q15906 EBI-1169948,EBI-399189 Q8C9X6 EBI-1169948,EBI-2942636 Q8C0I4 EBI-1169948,EBI-2942663 P01108 EBI-1169948,EBI-1183114 GO:0005829 GO:0000123 GO:0035267 GO:0000790 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0032777 GO:0032991 GO:0000812 GO:0005667 GO:0003682 GO:0010485 GO:0004402 GO:0042393 GO:0046872 GO:0061733 GO:0043274 GO:0044877 GO:0070491 GO:0003713 GO:0008134 GO:0071392 GO:0006978 GO:0006302 GO:0016573 GO:0032703 GO:0000122 GO:0045892 GO:0018394 GO:0010508 GO:1901985 GO:0045944 GO:0045893 GO:0043161 GO:0040008 GO:0006357 GO:0010212 MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW 513 Q8GTY0 Elongation factor 1-alpha 4 A4 3702 Yes SL-0198 Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}. UNIPROT Q8GTY0 UNIPROT P13905 UNIPROT Q0WSD5 UNIPROT Q39093 UNIPROT Q9C5L4 Pfam PF00009 Pfam PF03144 Pfam PF03143 PROSITE PS00301 PROSITE PS51722 This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. GO:0005737 GO:0005739 GO:0005634 GO:0048471 GO:0005886 GO:0009506 GO:0005773 GO:0005525 GO:0003924 GO:0003746 GO:0006412 GO:0006414 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK 449 Q8GWR1 Aladin AAAS 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q8GWR1 UNIPROT Q9LER8 Pfam PF00400 DE Reference Proteome: Yes; Q8GWK2 EBI-25521547,EBI-4425567 Q9LXJ0 EBI-2430270,EBI-4425567 Q9SJH7 EBI-4429038,EBI-4425567 GO:0005783 GO:0005635 GO:0005643 GO:0051028 GO:0006913 GO:0015031 MASFPHPGSVTVCEINRDLITAQNLSDERAQETYGKVLGMVFSPVSFDSTPSSLQENEGQENGDKASGESKGLVATLQMKVADSLKQILQPTDVTLLSEIDLQGVSWHQGKHIIAFISGANQVTIRDYEDKDEKEPCILTSDSQRNVKALEWRPNGGKSLSIACRGGICIWAASYPGNMALVRSGGSALRGSLSRGSGTRWILVDFLRCQNDEQISALSWSPCGRYLASASYDSSSFTIWDVSQGAGTPIRRGLGGISMLKWSPTGDYFFAARFDGTFCLWETNTWTSEPWSLSSGSGSVTGAIWDPEGRFILISFSKSSTLGSVHFSSKPPSLDAHLLPVELPEIASLTGCEGIEKIAWDASGERLAVSYKGGDENYKGLIAIYDTRRTPIVSASLVGFIRGPGENPKALSFSFHDKFKQGPLLSVCWSTGFCCTYPLIFRSHVLP 447 Q8GXA4 WPP domain-interacting protein 1 WIP1 3702 Yes SL-0178 SL-0182 Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips. UNIPROT Q8GXA4 UNIPROT O65589 Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715, PubMed:18591351). As component of the SUN- WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:25759303}. Self EBI-1779367,EBI-1779367 Q8L7E5 EBI-1796628,EBI-1779367 Q9LE82 EBI-1779367,EBI-1779351 Q9M651 EBI-1779367,EBI-1779567 Q9FH18 EBI-1779466,EBI-1779367 Q9FMH6 EBI-1779597,EBI-1779367 Q9C500 EBI-1779367,EBI-1779618 Q94AV5 EBI-1779487,EBI-1779367 Q84MC7 EBI-1779367,EBI-2349513 Q8GYN0 EBI-4450073,EBI-1779367 Q8GYS8 EBI-4450061,EBI-1779367 Q8L603 EBI-4446515,EBI-1779367 Q8RXL7 EBI-4427323,EBI-1779367 Q8RY98 EBI-1779367,EBI-4452570 Q8S8K0 EBI-4453700,EBI-1779367 Q8VYV9 EBI-4463541,EBI-1779367 Q8VZ48 EBI-4455850,EBI-1779367 Q8VZ95 EBI-2010972,EBI-1779367 Q93V66 EBI-4453472,EBI-1779367 Q93V85 EBI-4438153,EBI-1779367 Q93ZQ3 EBI-1779367,EBI-4450641 Q946Y7 EBI-4438441,EBI-1779367 Q94A32 EBI-1779367,EBI-4438745 Q94A99 EBI-4451043,EBI-1779367 Q94AP3 EBI-4449665,EBI-1779367 Q94CK3 EBI-1779367,EBI-4450097 Q9LVZ7 EBI-4443708,EBI-1779367 Q9FH92 EBI-1779367,EBI-4443876 Q9FK55 EBI-1779367,EBI-4426223 Q9FKK1 EBI-1779367,EBI-4453688 Q9FL61 EBI-1779367,EBI-4432515 Q9FVX3 EBI-1779367,EBI-4436871 Q9FZ54 EBI-1779367,EBI-4430708 Q9FZ98 EBI-4425682,EBI-1779367 Q9LDU6 EBI-1779367,EBI-4439540 Q9LJD9 EBI-1779367,EBI-4440036 Q9LPF1 EBI-4466346,EBI-1779367 Q9LQ32 EBI-4436710,EBI-1779367 Q9LSF6 EBI-4434839,EBI-1779367 Q9M2J9 EBI-4434027,EBI-1779367 Q9M9S6 EBI-4434173,EBI-1779367 Q9SA23 EBI-4436558,EBI-1779367 Q9SCL4 EBI-1779367,EBI-4463558 Q9SCZ8 EBI-4458901,EBI-1779367 Q9SEL6 EBI-1162795,EBI-1779367 Q9SHG7 EBI-4436589,EBI-1779367 Q9SIH4 EBI-4451446,EBI-1779367 O80594 EBI-4428472,EBI-1779367 O80895 EBI-4456509,EBI-1779367 O81062 EBI-1779367,EBI-4440921 O82245 EBI-1779367,EBI-4455652 P47192 EBI-1779367,EBI-4433747 P59229 EBI-4432491,EBI-1779367 P82874 EBI-1779367,EBI-2352074 Q41975 EBI-1779367,EBI-4449798 Q42342 EBI-2295493,EBI-1779367 Q5XEV3 EBI-1779367,EBI-4431808 Q5XF13 EBI-1779367,EBI-4431954 Q6NLF5 EBI-4431243,EBI-1779367 Q6NQG3 EBI-1779367,EBI-4429694 Q84MC9 EBI-4427374,EBI-1779367 Q8GWH4 EBI-4426287,EBI-1779367 Q8GX70 EBI-4430355,EBI-1779367 Q9SRE4 EBI-4434931,EBI-1779367 Q9STW3 EBI-4429423,EBI-1779367 Q9SY29 EBI-1779367,EBI-4454735 Q9XI60 EBI-4424450,EBI-1779367 Q9ZQ38 EBI-1779367,EBI-4454302 Q9ZSR7 EBI-4449636,EBI-1779367 Q9ZUJ2 EBI-4424518,EBI-1779367 Q9ZVX8 EBI-1779367,EBI-4425116 GO:0009504 GO:0016021 GO:0005635 GO:0031965 GO:0046982 GO:0006997 MDLESESSALESVDDNVLIQQSASNVCDDGRSLDNGSCSDESVKLLSTSNSVELGKPMSFDSPGDGGGAYSPVLKGQGLRKWRRIRRDLVKDTSANMENSKALKRGLSGVAHSHGKQMQFQSPEVEQESQGSVGSVNMLKSSGDGFDILGSSGYDSRFVAGVGFSAGMDLEIDDDRSSKSSTVARAPKVIRYEKPMISSGQGGNIRVENSKKHRGESVDFEKENSYSSLESDSRKQSGRMMDYNGENGETSMRKDDAGGEGGESINTDNRYSDEMDPLTEAINGFLALQDALEKEVQQFQEIGNEPMPQHHEQVSEANSPHPEIVTLVNNVEQLENMLEETRSMLEVKESHIRDLESTTNQSKHSWGGTEIVVEDIFRQKIEAEIEYLIYSRSIDNLNSQMKLIDEQESLAEEQTHETLNKLGRVQTKAANFTNRAQDLQNDCIEITGTIKKRACKITSYVLIQLVLLSTVVLLLLSQLLPEPDTVVPT 489 Q8GYF7 Nuclear pore complex protein NUP54 NUP54 3702 Yes SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q8GYF7 UNIPROT O48698 Pfam PF13874 DE Reference Proteome: Yes; Q8W4D8 EBI-2015534,EBI-4474560 GO:0005635 GO:0044613 GO:0005730 GO:0017056 GO:0051028 GO:0006607 GO:0006999 GO:0036228 MFGTPSSSPSFGTPSSTPAFGTSSPAFGTPSATPAFGTPSNPSFSSGGFGSSLFSSPFSSQQPQQQQQQQQQQQPSSLFQQQPSSNFGFQSPFNNTAQQQQQTPFPNAQLTTQMAPVAPIPYSLADRDVQAIIEAYKEDPTNPKYAFQHLLFSVTEPQYRVKPAAVSDIMWAEAMSKLEGMDSTERERLWPQLVQGFKDLSQRLKLQDEVLVSDRDRIKTTQSNVKMLQRHLQASTFPSIERLRQKEQSLQRRMLRVMRIIEGLEGKGFRLPLTKGEAELSEKLTAITRQVKGPGAELSRRVQSLQTISRAQANSIAAGSSLYLPGSTKIDEQSLIDMQEVLQQETEAIGRLGNVLKRDMRDMEIMVAEDTEMALDS 377 Q8I4N3 Nucleoporin ndc-1 npp 6239 Yes SL-0178 SL-0182 SL-0185 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}. UNIPROT Q8I4N3 Pfam PF09531 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}. P91001 EBI-2001892,EBI-313007 GO:0016021 GO:0031965 GO:0005643 GO:0070762 GO:0017056 GO:0051028 GO:0006999 GO:0015031 MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRLAGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTFALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANISEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTVHSPTPEQTRTLPNVIETDDSLLKFFALHDLRTIAWNDEKRRVDVFSLSQPGKHPRNWKAVSLPCVRMLDELCSRMTVSAARLVGYSWDDHDIENEDVPRDALLMPRKMREMAYRGTGQSRQQKSMAPIRSHNTQTVGLLSKISNFLGFGVTEKLVISRFDAHMNAYAAEALYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTFLRIVDASLKSSLQRVVTTFGSHLSSLNLPEEHSRTIRMICLTDEL 588 Q8IQV9 Nuclear pore complex protein Nup205 Nup205 7227 Yes SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q92621}. UNIPROT Q8IQV9 UNIPROT B6IDH1 UNIPROT Q3YMV0 UNIPROT Q8MSV6 UNIPROT Q9VWB8 Pfam PF11894 Plays a role in the nuclear pore complex (NPC) assembly and maintenance, but with limited role in NPC permeability. Required for specific nuclear import pathways such as Mad import. {ECO:0000269|PubMed:20547758}. O97159 EBI-112333,EBI-499630 Q960X8 EBI-499630,EBI-90175 GO:0044611 GO:0017056 GO:0042332 GO:0051028 GO:0006999 GO:0006606 MDGECLANEQMCVGRQITNATHASTAVIEDMWTPYKHLYNTFQTAVSNRSGFTSDLEQCLKKYKHNFSNLLRNPPRSEKSRNLLRNALNEGVPMQGHSRKTKMSQDLADEAVILSDMFDLDEGFAVELLCTAQRQQKHHPGLSRGLVAVLLYYDGRKAISCTLRDMFQVVSGVSWNTELPKEITGLVTNYAESLVDGSGILGRLLQLLEEMDVDKECAMLTTNRAFGSKKHQNQVLGLYEDIQQALAMALFNWSAQRGLPRHIAIRLMHQLANRKNHDAGGNMDDVTLIMLMALLYAYDTSMLLVTEEPNEHTTRLPIFSDREFAECFLEELYAQSSWQAPRLNAIIAYSFGLTLASLRHAPLQLQATAISIINRDEMLIDEALGAQVFVFFHSLLLEKDLVYSTQFFYRRVHLLITDFIDFMNSKVSELRGRADESSHTIISFLNEGLEPPPNLDSNFELLMLCVAKMHGDPRVTIRLCNEYWGPGDPNGSTAFKNTSRSVSLFKFISLASDLLPQTLFKAYLKMISGLTRTDFSARCAFNMLRVPQMATGGKYAVSWDHFFTTLGNYYTSMRNDFNTNIGMSGETIYRTRSTPKAITQREAEHLVAVMGIIQAVAEHDEVSRIMICDHPNWQTPQVLLGLVACATPLFLKAEILHTLAALAKSKETARVIWFHLEASQIIPTVPVSRSYAQCSLLEEMEQIESRSEQYNLTRGILQLLYTLMTTNLPKSLGAGQRTPAYEGYLKSMINSVLLKFYNRAYKVPSEKWQVGAQCLKLLYYLLATYRPSAMDFLETVDEPPYPGFHVMMQLQLKSEMLQLLLCIVEEVRERLDNYNRFQGKKLLEECSLYALLILEAALAKQNAFFEAHSAANCPILLSGLNRMLLDLNPRSRKPDHVLNIIKYVTYNSWLPRHALAAIKILASVTQLPNVSTQILSMYGQGSNEKLEIRQGFVECLEMEVCVGKHDDDLLDQLALNNHVPYLGFGDDLDNEREMSGEREYSTIESQLELQAGDGALESKPASIELQLKEAIIKLFEMNLSQQLPNFVYFLLGVDVLREFMANGRQHLAIEMQSSCVNSVVLLLEKYMDKQRHSDKYCEHTARIVERIYHLFHGLCANRRTAETILRYFRLTCSDFLLRHLRSLPFRQHREDHVLHAMGHLLNCVSIDVKLAAKHGQMTRFNQMCDILLIGNGMERSSHGLSMELGHSLISQPSSSFLAMDVLPAGGSISAVAHGAGSASLGAPNTGVKSLKPSLLQETSQGLHVTRLLDILVLEAGTLSQPQLEFFDGHLITQLLRDCEASAEAGANSRANLINVRKLYYILTDELYMVQSIIASGQRKAISTEIMLLLNHAVNINRVRTQRCATLAFMAAWGQLVQVLFSNMPDAVLPATQRRQHIIDIVEKVLIKVQPIQPIIEISVQVSETVLLLLANLRYCCYQAEDQSPEDLAAEDSLSNGNGNAIGNDSQVNALCLGQRAIGTGSDGGSGGGRDIGSGGNSSNLRFILKNLVQWIMISEVKSQKLRINLYSSLLNCLRIAKRLRTDEHLEYQETLISRQESARTYNKEQRRDDRLRLKAMAAEVIGTFGEKLIDTICHDAVTGHDVCRMLALACLDMISELQAVSTLCDFVASRGYLKHILESLDQSSTALCGILQPVPDHLRPLYVYESRMAFLTRMANSNVGARLLLTEQALGVLSNMKVYDQQPDLKSSELNRNEPQTFLPSIDDRFRSILLPALSLCDAIVNSLGPRNNSAAVQVLNFLFAHIDMVEAMLRSATPYMDLGHLQQVAVISNLFARASTHELTALEDSVQLDLRNRLGRVQQLMIVVFGRFCVSEPTIRRMLQQDEEQQTNPTDDSKRLRVKYFLDIAANVSLYCRNVVTSHSKDSMTSKYLLTTVINDVTLLTGKMSSKKLTTIMHTILNQLKGSIGYYLSQKSIADNLLQQRASLPNISFGPNGKQSYIELSQRYNEKRSELRQAVFIAEQNLYLLWIHLDFYLRNTIDYANENRNAINESNMDDDNDMSVLNASQEEIVQLKQLLISTFNETFCTQLINASEDYSIKCKGFNGSLLRRIKALVQFAPITANDVNSSFDS 2090 Q8IVL0 Neuron navigator 3 NAV3 9606 Yes SL-0178 SL-0182 SL-0183 Nucleus outer membrane {ECO:0000250}. UNIPROT Q8IVL0 UNIPROT Q8NFW7 UNIPROT Q9Y2E7 Pfam PF00004 Pfam PF00307 PROSITE PS50021 OMIM 611629 DisGeNET 89795 May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:16166283}.Note=A chromosomal aberration disrupting NAV3 has been found in patients with Sezary syndrome (PubMed:16166283). Translocation t(12;18)(q21;q21.2) (PubMed:16166283). {ECO:0000269|PubMed:16166283}. P25054 EBI-727707,EBI-2795733 P01106 EBI-447544,EBI-2795733 P84101 EBI-720132,EBI-2795733 GO:0005640 GO:0005524 GO:0008017 GO:0030336 GO:0032703 GO:0007026 GO:0007399 GO:0022008 GO:1905929 GO:0031116 MPVLGVASKLRQPAVGSKPVHTALPIPNLGTTGSQHCSSRPLELTETESSMLSCQLALKSTCEFGEKKPLQGKAKEKEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYKQQQHHQQQYYQSLVELQQRVTHASPPSEASQAKTQQDMQSSLAARYATQSNHSGIATSQKKPTRLPGPSRVPAAGSSSKVQGASNLNRRSQSFNSIDKNKPPNYANGNEKDSSKGPQSSSGVNGNVQPPSTAGQPPASAIPSPSASKPWRSKSMNVKHSATSTMLTVKQSSTATSPTPSSDRLKPPVSEGVKTAPSGQKSMLEKFKLVNARTALRPPQPPSSGPSDGGKDDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKLAPPKAGSKNLSNKKSLLQPKEKEEKNRDKNKVCTEKPVKEEKDQVTEMAPKKTSKIASLIPKGSKTTAAKKESLIPSSSGIPKPGSKVPTVKQTISPGSTASKESEKFRTTKGSPSQSLSKPITMEKASASSCPAPLEGREAGQASPSGSCTMTVAQSSGQSTGNGAVQLPQQQQHSHPNTATVAPFIYRAHSENEGTALPSADSCTSPTKMDLSYSKTAKQCLEEISGEDPETRRMRTVKNIADLRQNLEETMSSLRGTQISHSTLETTFDSTVTTEVNGRTIPNLTSRPTPMTWRLGQACPRLQAGDAPSLGAGYPRSGTSRFIHTDPSRFMYTTPLRRAAVSRLGNMSQIDMSEKASSDLDMSSEVDVGGYMSDGDILGKSLRTDDINSGYMTDGGLNLYTRSLNRIPDTATSRDIIQRGVHDVTVDADSWDDSSSVSSGLSDTLDNISTDDLNTTSSVSSYSNITVPSRKNTQLRTDSEKRSTTDETWDSPEELKKPEEDFDSHGDAGGKWKTVSSGLPEDPEKAGQKASLSVSQTGSWRRGMSAQGGAPSRQKAGTSALKTPGKTDDAKASEKGKAPLKGSSLQRSPSDAGKSSGDEGKKPPSGIGRSTATSSFGFKKPSGVGSSAMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTTLQYRSLPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDSESVSLSGSPKSSPTSASACGAQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGVKSSSVMPSPSTTLARQGSLESPSSGTGSMGSAGGLSGSSSPLFNKPSDLTTDVISLSHSLASSPASVHSFTSGGLVWAANMSSSSAGSKDTPSYQSMTSLHTSSESIDLPLSHHGSLSGLTTGTHEVQSLLMRTGSVRSTLSESMQLDRNTLPKKGLRYTPSSRQANQEEGKEWLRSHSTGGLQDTGNQSPLVSPSAMSSSAAGKYHFSNLVSPTNLSQFNLPGPSMMRSNSIPAQDSSFDLYDDSQLCGSATSLEERPRAISHSGSFRDSMEEVHGSSLSLVSSTSSLYSTAEEKAHSEQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAIQGALNGPDHPPKDLRIRRQHSSESVSSINSATSHSSIGSGNDADSKKKKKKNWVNSRGSELRSSFKQAFGKKKSTKPPSSHSDIEELTDSSLPASPKLPHNAGDCGSASMKPSQSASASPLVWPPKKRQNGPVIYKHRSRICECTEAEAEIILQLKSELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIEILKAENDRLKAETGNTAKPTRPPSESSSSTSSSSSRQSLGLSLNNLNITEAVSSDILLDDAGDATGHKDGRSVKIIVSISKGYGRAKDQKSQAYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRIDTSTSLGLSSDCIASYCIGDLIRSHNLEVPELLPCGYLVGDNNIITVNLKGVEENSLDSFVFDTLIPKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGVELPVVIILDNLHHVGSLSDIFNGFLNCKYNKCPYIIGTMNQGVSSSPNLELHHNFRWVLCANHTEPVKGFLGRYLRRKLIEIEIERNIRNNDLVKIIDWIPKTWHHLNSFLETHSSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYILEAVREGLQMYGKRTPWEDPSKWVLDTYPWSSATLPQESPALLQLRPEDVGYESCTSTKEATTSKHIPQTDTEGDPLMNMLMKLQEAANYSSTQSCDSESTSHHEDILDSSLESTL 2385 Q8IWQ3 Serine/threonine-protein kinase BRSK2 BRSK2 9606 Yes SL-0198 Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin. UNIPROT Q8IWQ3 UNIPROT B3KVE9 UNIPROT E9PLM7 UNIPROT O60843 UNIPROT O95099 UNIPROT Q5J5B4 UNIPROT Q6ZMQ4 UNIPROT Q8TB60 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 609236 DisGeNET 9024 Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr- 174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}. Q8WVZ9 EBI-473695,EBI-3232062 Q99PL5 EBI-8361659,EBI-3232062 GO:0005813 GO:0005737 GO:0150034 GO:0005783 GO:0005634 GO:0048471 GO:0005524 GO:0051117 GO:0060590 GO:0000287 GO:0019901 GO:0004674 GO:0048156 GO:0050321 GO:0031532 GO:0007409 GO:0051301 GO:0036503 GO:0030010 GO:0006887 GO:0000086 GO:0035556 GO:0070059 GO:0090176 GO:0030182 GO:0018105 GO:0006468 GO:0043462 GO:0050770 GO:0061178 GO:0010975 GO:1904152 GO:2000807 MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP 736 Q8IX03 Protein KIBRA WWC1 9606 Yes SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Cell projection, ruffle membrane. Note=Colocalizes with PRKCZ in the perinuclear region. UNIPROT Q8IX03 UNIPROT B4DK05 UNIPROT O94946 UNIPROT Q6MZX4 UNIPROT Q6Y2F8 UNIPROT Q7Z4G8 UNIPROT Q8WVM4 UNIPROT Q9BT29 PDB 2Z0U PDB 6FB4 PDB 6FD0 PDB 6FJC PDB 6FJD Pfam PF00397 PROSITE PS50004 PROSITE PS01159 PROSITE PS50020 OMIM 610533 OMIM 615602 DisGeNET 23286 Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance. {ECO:0000269|PubMed:15081397, ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:23778582}. O95831 EBI-715828,EBI-356440 Q2I360 EBI-715828,EBI-912397 P61981 EBI-359832,EBI-715828 Q9UKE5 EBI-715828,EBI-1051794 Q99459 EBI-374880,EBI-715828 Q4VCS5 EBI-2511319,EBI-715828 P29991 EBI-8826689,EBI-715828 Q04917 EBI-306940,EBI-715828 Q8IW50 EBI-715828,EBI-718694 Q05513 EBI-295351,EBI-715828 Q15678 EBI-715828,EBI-1237156 P62258 EBI-715828,EBI-356498 Q9Y2J2 EBI-715828,EBI-310986 P63167 EBI-715828,EBI-349105 O43491 EBI-715828,EBI-1052044 Q96FJ2 EBI-715828,EBI-742371 Q9Y297 EBI-715828,EBI-307461 P27348 EBI-715828,EBI-359854 Q9UKB1 EBI-715828,EBI-355189 P31946 EBI-715828,EBI-359815 Q9NVI7 EBI-715828,EBI-352007 Q6P5F9 EBI-2550236,EBI-715828 Q6P1J9 EBI-930143,EBI-715828 Q5UIP0 EBI-711331,EBI-715828 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0032991 GO:0032587 GO:0019900 GO:0060090 GO:0003713 GO:0016477 GO:0030010 GO:0035329 GO:0035331 GO:0046621 GO:0000122 GO:0043410 GO:0007221 GO:0035330 GO:0032386 MPRPELPLPEGWEEARDFDGKVYYIDHTNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQIEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEILKAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDKKMSDAQGSYKLDEAQAVLRETKAIKKAITCGEKEKQDLIKSLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPLPKQYLDVSSQTDISGSFGINSNNQLAEKVRLRLRYEEAKRRIANLKIQLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARKRLEKDLQAARDTQSKALTERLKLNSKRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLVASSLDSSTSASFTDLYYDPFEQLDSELQSKVEFLLLEGATGFRPSGCITTIHEDEVAKTQKAEGGGRLQALRSLSGTPKSMTSLSPRSSLSSPSPPCSPLMADPLLAGDAFLNSLEFEDPELSATLCELSLGNSAQERYRLEEPGTEGKQLGQAVNTAQGCGLKVACVSAAVSDESVAGDSGVYEASVQRLGASEAAAFDSDESEAVGATRIQIALKYDEKNKQFAILIIQLSNLSALLQQQDQKVNIRVAVLPCSESTTCLFRTRPLDASDTLVFNEVFWVSMSYPALHQKTLRVDVCTTDRSHLEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQSRELKPVGVMAPASGPASTDAVSALLEQTAVELEKRQEGRSSTQTLEDSWRYEETSENEAVAEEEEEEVEEEEGEEDVFTEKASPDMDGYPALKVDKETNTETPAPSPTVVRPKDRRVGTPSQGPFLRGSTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSVRMKRPSSVKSLRSERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEQLEQAKSHGEKELPQWLREDERFRLLLRMLEKRQMDRAEHKGELQTDKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV 1113 Q8IXB3 Trafficking regulator of GLUT4 1 TRARG1 9606 Yes SL-0198 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}. UNIPROT Q8IXB3 UNIPROT A6NMK4 Pfam PF04505 OMIM 612211 DisGeNET 286753 Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}. Q9NWS8 EBI-21815621,EBI-4401316 Q92973-2 EBI-21815621,EBI-11022821 Q7L1Q6-2 EBI-21815621,EBI-21557060 Q4LE60 EBI-21815621,EBI-21502602 P54707-2 EBI-21815621,EBI-21500340 O95470 EBI-21815621,EBI-1046170 GO:0030659 GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0032869 GO:0099638 GO:0044381 GO:0072659 GO:0099500 MAHPVQSEFPSAQEPGSAAFLDLPEMEILLTKAENKDDKTLNLSKTLSGPLDLEQNSQGLPFKAISEGHLEAPLPRSPSRASSRRASSIATTSYAQDQEAPRDYLILAVVACFCPVWPLNLIPLIISIMSRSSMQQGNVDGARRLGRLARLLSITLIIMGIVIIMVAVTVNFTVQKK 177 Q8IZ41 Ras and EF-hand domain-containing protein RASEF 9606 Yes SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:17448446}. UNIPROT Q8IZ41 UNIPROT A6NC29 UNIPROT Q96N04 PDB 2P5S PDB 2PMY Pfam PF13499 Pfam PF00071 PROSITE PS00018 PROSITE PS50222 PROSITE PS51419 OMIM 611344 DisGeNET 158158 Binds predominantly GDP, and also GTP. {ECO:0000269|PubMed:17448446}. P13569 EBI-349854,EBI-21855855 P31150 EBI-946999,EBI-21855855 Q9UNT1-2 EBI-12256104,EBI-21855855 GO:0005829 GO:0048471 GO:0005509 GO:0019003 GO:0005525 GO:0003924 GO:0042802 MEADGDGEELARLRSVFAACDANRSGRLEREEFRALCTELRVRPADAEAVFQRLDADRDGAITFQEFARGFLGSLRGGRRRDWGPLDPAPAVSEAGPETHDSEEDEGDEDAAAALATSCGPASPGRAWQDFQARLGDEAKFIPREEQVSTLYQNINLVEPRLIQPYEHVIKNFIREIRLQSTEMENLAIAVKRAQDKAAMQLSELEEEMDQRIQAAEHKTRKDEKRKAEEALSDLRRQYETEVGDLQVTIKKLRKLEEQSKRVSQKEDVAALKKQIYDLSMENQKVKKDLLEAQTNIAFLQSELDALKSDYADQSLNTERDLEIIRAYTEDRNSLERQIEILQTANRKLHDSNDGLRSALENSYSKFNRSLHINNISPGNTISRSSPKFIGHSPQPLGYDRSSRSSYVDEDCDSLALCDPLQRTNCEVDSLPESCFDSGLSTLRDPNEYDSEVEYKHQRGFQRSHGVQESFGGDASDTDVPDIRDEETFGLEDVASVLDWKPQGSVSEGSIVSSSRKPISALSPQTDLVDDNAKSFSSQKAYKIVLAGDAAVGKSSFLMRLCKNEFRENISATLGVDFQMKTLIVDGERTVLQLWDTAGQERFRSIAKSYFRKADGVLLLYDVTCEKSFLNIREWVDMIEDAAHETVPIMLVGNKADIRDTAATEGQKCVPGHFGEKLAMTYGALFCETSAKDGSNIVEAVLHLAREVKKRTDKDDSRSITNLTGTNSKKSPQMKNCCNG 740 Q8IZQ1 WD repeat and FYVE domain-containing protein 3 WDFY3 9606 Yes SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Cytoplasm, cytosol {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Nucleus, PML body {ECO:0000269|PubMed:20168092}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:15292400}; Cytoplasmic side {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q6VNB8}. Cell projection, axon {ECO:0000250|UniProtKB:Q6VNB8}. Note=Relocalization from the nucleus to the cytosol is stimulated by cellular stress, such as starvation or proteasomal inhibition. In the cytosol of starved cells, colocalizes with autophagic structures (PubMed:15292400, PubMed:20168092, PubMed:20971078, PubMed:20417604). This redistribution is dependent on p62/SQSTM1 (PubMed:20168092). When nuclear export is blocked by treatment with leptomycin B, accumulates in nuclear bodies, that completely or partially colocalize with promyelocytic leukemia (PML) bodies (PubMed:20168092). Localizes throughout neurons, including within axons. In neurons, enriched in the light membrane fraction along with the synaptosomal membrane protein synaptophysin and the membrane- bound form of LC3/MAP1LC3A/MAP1LC3B, called LC3-II, a classic marker for autophagic vesicles (By similarity). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. UNIPROT Q8IZQ1 UNIPROT Q4W5K5 UNIPROT Q6P0Q5 UNIPROT Q8N1T2 UNIPROT Q8NAV6 UNIPROT Q96BS7 UNIPROT Q96D33 UNIPROT Q96N85 UNIPROT Q9Y2J7 PDB 3WIM Pfam PF02138 Pfam PF01363 Pfam PF14844 PROSITE PS50197 PROSITE PS51783 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 PROSITE PS50178 OMIM 617485 OMIM 617520 DisGeNET 23001 Required for selective macroautophagy (aggrephagy). Acts as an adapter protein by linking specific proteins destined for degradation to the core autophagic machinery members, such as the ATG5- ATG12-ATG16L E3-like ligase, SQSTM1 and LC3 (PubMed:20417604). Along with p62/SQSTM1, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with SQSTM1, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Important for normal brain development. Essential for the formation of axonal tracts throughout the brain and spinal cord, including the formation of the major forebrain commissures. Involved in the ability of neural cells to respond to guidance cues. Required for cortical neurons to respond to the trophic effects of netrin-1/NTN1 (By similarity). Regulates Wnt signaling through the removal of DVL3 aggregates, likely in an autophagy-dependent manner. This process may be important for the determination of brain size during embryonic development (PubMed:27008544). May regulate osteoclastogenesis by acting on the TNFSF11/RANKL - TRAF6 pathway (By similarity). After cytokinetic abscission, involved in midbody remnant degradation (PubMed:24128730). In vitro strongly binds to phosphatidylinositol 3-phosphate (PtdIns3P) (PubMed:15292400). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:27008544}.Microcephaly 18, primary, autosomal dominant (MCPH18) [MIM:617520]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH18 affected individuals manifest microcephaly with mild to moderate intellectual disability. {ECO:0000269|PubMed:27008544}. Note=The disease is caused by mutations affecting the gene represented in this entry. Q9GZQ8 EBI-373144,EBI-1569256 Q63HR2 EBI-949753,EBI-1569256 Q92569 EBI-1569256,EBI-79893 Q5R372-2 EBI-1569256,EBI-10692254 P62993 EBI-1569256,EBI-401755 P40763 EBI-1569256,EBI-518675 O95166 EBI-712001,EBI-1569256 Q9H1Y0 EBI-1569256,EBI-1047414 P42858 EBI-466029,EBI-1569256 P37840 EBI-985879,EBI-1569256 P54253 EBI-930964,EBI-1569256 Q13501 EBI-1569256,EBI-307104 P01106 EBI-447544,EBI-1569256 O00418 EBI-6255306,EBI-1569256 Q93079 EBI-352469,EBI-1569256 GO:0005776 GO:0030424 GO:0005737 GO:0005829 GO:0097635 GO:0019898 GO:0016234 GO:0005635 GO:0031965 GO:0005730 GO:0005654 GO:0043204 GO:0005886 GO:0016605 GO:0005545 GO:0003831 GO:0046872 GO:0035973 GO:0007275 MNMVKRIMGRPRQEECSPQDNALGLMHLRRLFTELCHPPRHMTQKEQEEKLYMMLPVFNRVFGNAPPNTMTEKFSDLLQFTTQVSRLMVTEIRRRASNKSTEAASRAIVQFLEINQSEEASRGWMLLTTINLLASSGQKTVDCMTTMSVPSTLVKCLYLFFDLPHVPEAVGGAQNELPLAERRGLLQKVFVQILVKLCSFVSPAEELAQKDDLQLLFSAITSWCPPYNLPWRKSAGEVLMTISRHGLSVNVVKYIHEKECLSTCVQNMQQSDDLSPLEIVEMFAGLSCFLKDSSDVSQTLLDDFRIWQGYNFLCDLLLRLEQAKEAESKDALKDLVNLITSLTTYGVSELKPAGITTGAPFLLPGFAVPQPAGKGHSVRNVQAFAVLQNAFLKAKTSFLAQIILDAITNIYMADNANYFILESQHTLSQFAEKISKLPEVQNKYFEMLEFVVFSLNYIPCKELISVSILLKSSSSYHCSIIAMKTLLKFTRHDYIFKDVFREVGLLEVMVNLLHKYAALLKDPTQALNEQGDSRNNSSVEDQKHLALLVMETLTVLLQGSNTNAGIFREFGGARCAHNIVKYPQCRQHALMTIQQLVLSPNGDDDMGTLLGLMHSAPPTELQLKTDILRALLSVLRESHRSRTVFRKVGGFVYITSLLVAMERSLSCPPKNGWEKVNQNQVFELLHTVFCTLTAAMRYEPANSHFFKTEIQYEKLADAVRFLGCFSDLRKISAMNVFPSNTQPFQRLLEEDVISIESVSPTLRHCSKLFIYLYKVATDSFDSRAEQIPPCLTSESSLPSPWGTPALSRKRHAYHSVSTPPVYPPKNVADLKLHVTTSSLQSSDAVIIHPGAMLAMLDLLASVGSVTQPEHALDLQLAVANILQSLVHTERNQQVMCEAGLHARLLQRCSAALADEDHSLHPPLQRMFERLASQALEPMVLREFLRLASPLNCGAWDKKLLKQYRVHKPSSLSYEPEMRSSMITSLEGLGTDNVFSLHEDNHYRISKSLVKSAEGSTVPLTRVKCLVSMTTPHDIRLHGSSVTPAFVEFDTSLEGFGCLFLPSLAPHNAPTNNTVTTGLIDGAVVSGIGSGERFFPPPSGLSYSSWFCIEHFSSPPNNHPVRLLTVVRRANSSEQHYVCLAIVLSAKDRSLIVSTKEELLQNYVDDFSEESSFYEILPCCARFRCGELIIEGQWHHLVLVMSKGMLKNSTAALYIDGQLVNTVKLHYVHSTPGGSGSANPPVVSTVYAYIGTPPAQRQIASLVWRLGPTHFLEEVLPSSNVTTIYELGPNYVGSFQAVCMPCKDAKSEGVVPSPVSLVPEEKVSFGLYALSVSSLTVARIRKVYNKLDSKAIAKQLGISSHENATPVKLIHNSAGHLNGSARTIGAALIGYLGVRTFVPKPVATTLQYVGGAAAILGLVAMASDVEGLYAAVKALVCVVKSNPLASKEMERIKGYQLLAMLLKKKRSLLNSHILHLTFSLVGTVDSGHETSIIPNSTAFQDLLCDFEVWLHAPYELHLSLFEHFIELLTESSEASKNAKLMREFQLIPKLLLTLRDMSLSQPTIAAISNVLSFLLQGFPSSNDLLRFGQFISSTLPTFAVCEKFVVMEINNEEKLDTGTEEEFGGLVSANLILLRNRLLDILLKLIYTSKEKTSINLQACEELVKTLGFDWIMMFMEEHLHSTTVTAAMRILVVLLSNQSILIKFKEGLSGGGWLEQTDSVLTNKIGTVLGFNVGRSAGGRSTVREINRDACHFPGFPVLQSFLPKHTNVPALYFLLMALFLQQPVSELPENLQVSVPVISCRSKQGCQFDLDSIWTFIFGVPASSGTVVSSIHNVCTEAVFLLLGMLRSMLTSPWQSEEEGSWLREYPVTLMQFFRYLYHNVPDLASMWMSPDFLCALAATVFPFNIRPYSEMVTDLDDEVGSPAEEFKAFAADTGMNRSQSEYCNVGTKTYLTNHPAKKFVFDFMRVLIIDNLCLTPASKQTPLIDLLLEASPERSTRTQQKEFQTYILDSVMDHLLAADVLLGEDASLPITSGGSYQVLVNNVFYFTQRVVDKLWQGMFNKESKLLIDFIIQLIAQSKRRSQGLSLDAVYHCLNRTILYQFSRAHKTVPQQVALLDSLRVLTVNRNLILGPGNHDQEFISCLAHCLINLHVGSNVDGFGLEAEARMTTWHIMIPSDIEPDGSYSQDISEGRQLLIKAVNRVWTELIHSKKQVLEELFKVTLPVNERGHVDIATARPLIEEAALKCWQNHLAHEKKCISRGEALAPTTQSKLSRVSSGFGLSKLTGSRRNRKESGLNKHSLSTQEISQWMFTHIAVVRDLVDTQYKEYQERQQNALKYVTEEWCQIECELLRERGLWGPPIGSHLDKWMLEMTEGPCRMRKKMVRNDMFYNHYPYVPETEQETNVASEIPSKQPETPDDIPQKKPARYRRAVSYDSKEYYMRLASGNPAIVQDAIVESSEGEAAQQEPEHGEDTIAKVKGLVKPPLKRSRSAPDGGDEENQEQLQDQIAEGSSIEEEEKTDNATLLRLLEEGEKIQHMYRCARVQGLDTSEGLLLFGKEHFYVIDGFTMTATREIRDIETLPPNMHEPIIPRGARQGPSQLKRTCSIFAYEDIKEVHKRRYLLQPIAVEVFSGDGRNYLLAFQKGIRNKVYQRFLAVVPSLTDSSESVSGQRPNTSVEQGSGLLSTLVGEKSVTQRWERGEISNFQYLMHLNTLAGRSYNDLMQYPVFPWILADYDSEEVDLTNPKTFRNLAKPMGAQTDERLAQYKKRYKDWEDPNGETPAYHYGTHYSSAMIVASYLVRMEPFTQIFLRLQGGHFDLADRMFHSVREAWYSASKHNMADVKELIPEFFYLPEFLFNSNNFDLGCKQNGTKLGDVILPPWAKGDPREFIRVHREALECDYVSAHLHEWIDLIFGYKQQGPAAVEAVNVFHHLFYEGQVDIYNINDPLKETATIGFINNFGQIPKQLFKKPHPPKRVRSRLNGDNAGISVLPGSTSDKIFFHHLDNLRPSLTPVKELKEPVGQIVCTDKGILAVEQNKVLIPPTWNKTFAWGYADLSCRLGTYESDKAMTVYECLSEWGQILCAICPNPKLVITGGTSTVVCVWEMGTSKEKAKTVTLKQALLGHTDTVTCATASLAYHIIVSGSRDRTCIIWDLNKLSFLTQLRGHRAPVSALCINELTGDIVSCAGTYIHVWSINGNPIVSVNTFTGRSQQIICCCMSEMNEWDTQNVIVTGHSDGVVRFWRMEFLQVPETPAPEPAEVLEMQEDCPEAQIGQEAQDEDSSDSEADEQSISQDPKDTPSQPSSTSHRPRAASCRATAAWCTDSGSDDSRRWSDQLSLDEKDGFIFVNYSEGQTRAHLQGPLSHPHPNPIEVRNYSRLKPGYRWERQLVFRSKLTMHTAFDRKDNAHPAEVTALGISKDHSRILVGDSRGRVFSWSVSDQPGRSAADHWVKDEGGDSCSGCSVRFSLTERRHHCRNCGQLFCQKCSRFQSEIKRLKISSPVRVCQNCYYNLQHERGSEDGPRNC 3526 Q8K2T1 NmrA-like family domain-containing protein 1 Nmral1 10090 Yes SL-0198 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}. UNIPROT Q8K2T1 UNIPROT Q8BVF0 UNIPROT Q9CZP2 Pfam PF05368 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}. Q3UHD9 EBI-771911,EBI-9989325 P52927 EBI-912574,EBI-9989325 GO:0005654 GO:0005634 GO:0048471 GO:0042802 MADRKLVVVFGATGAQGGSVARALLEDGTFRIRVVTRNPEQRAAKELKQQGAEVVRGDQDDAASMELALAGAHATFIVTNYWETCSQDREVQQPHQWDQVFKQGKLLADLAKRLGLHYVVYSGLENIRKLTAGKLAAGHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLLSYFLPQKAADGKSFLLDLPMGDVPMDGMSVSDLGPVVLSLLKKPEEYVGQNIGLSTCRHTAEEYAALLSKHTGKAVHHAKTTPEDYEKLGFQGAQDLANMFRFYTLKPDRNIHLTLRLNPKAQTLDQWLEQHKGDFAQL 309 Q8K3Z9 Nuclear envelope pore membrane protein POM 121 Pom121 10090 Yes SL-0178 SL-0182 SL-0185 Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}. UNIPROT Q8K3Z9 UNIPROT Q7TSH5 Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL) (By similarity). {ECO:0000250}. GO:0005789 GO:0016021 GO:0031965 GO:0005643 GO:0005654 GO:0008139 GO:0017056 GO:0051028 GO:0006999 GO:0006606 GO:0006405 MSPAAAAADGGERRRPPLGGREGRSRARGYGGPAGAAALGLALLGLALYLVPAAAALAWLAVGASAAWWGLSREPRGPRALSSFVRDARRHPRPALTASPPPAKSPVNGSLCEPRSPLGGPDPAELLLMGSYLGKPGPPEPALRQDPRERPGRRPPARSPPPASAVQRVHHVYPALPTPLLRPSRRPPHRDCGPLSSRFVITPRRRYPIQQAQYSLLGALPTVCWNGGHKKAVLSPRNSRMVCSPVTVRIAPPDSKLFRSSMSEQILDTTLSSPSSNAPDPCAKETVLNALKEKKKRTVAEEDQLHLDGQENKRRRHDSGGSGHSAFEPLVANGVPAAFVPKPGSLKRSLASQSSDDHLNKRSRTSSVSSLASACTGGIPSSSRNAITSSYSSTRGISQLWKRSGPTSSPFSSPASSRSQTPERPAKKTREEEPCQQSSSSPPLVTDKESPGEKVTDTTTGKQQSSWTSPPTPGSSGQRKRKIQLLPSRRGDQLTLPPPPELGYSITAEDLDMERKASLQWFNKVLEDKPDDASASATDGPPSTSPPFTFTLPAVGPAASPASLPAPSSNPLLESLKKMQESPAPSSSEPAEAATVAAPSPPKTPSLLAPLVSPLAGPLASTSSDSKPAATFLGLASASSITPLTDSKSSGVSQAEQSVSTPASTASSPTPKPSMLFGMLSPPASSSSLATPAPACASPMFKPIFPATPKSESDSPLPSSSSAATTASSSTAPPTAASTTPTFKPIFDKMEPFTAMPLSTPFSLKQTTATATTTATSAPLFTGLGTATSTVASGTAASASKPVFGFGVTTAASTASSTMTSTSQSVLFGGAPPVTTSSSAPALASIFQFGKPLAPAASAAGTSFSQPLASSTQTAASNSGFSGFGSTLTTSTSAPATTSQPTLTFSNTVTPTFNIPFSSSAKPALPTYPGANSQPTFGATDGATKPALAPSFGSSFTFGNSVASAPSAAPAPATFGSAAQPAFGGLKAAASTFGAPASTQPAFGSTTSVFSFGSATTSGFGAAATAATTTQTTNSGSSSSLFGSSAPSPFTFGGSAAPAGSGGFGLSATPGTSSTSGTFSFGSGQSGTPGTTTSFGSLSQNTLGAPSQGSPFAFSVGSTPESKPVFGGTSTPTFGQSAPAPGVGTTGSSLSFGASSTPAQGFVGVGPFGSAAPSFSIGAGSKTPGARQRLQARRQHTRKK 1200 Q8K4D7 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 Plcz1 10090 Yes SL-0198 Nucleus {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. UNIPROT Q8K4D7 UNIPROT Q3KPE5 Pfam PF00168 Pfam PF09279 Pfam PF00388 Pfam PF00387 PROSITE PS50004 PROSITE PS50222 PROSITE PS50007 PROSITE PS50008 The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:17933795, ECO:0000269|PubMed:18028898, ECO:0000269|PubMed:18322275, ECO:0000305}. GO:0005623 GO:0005737 GO:0005829 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0045120 GO:0061827 GO:0005509 GO:0004435 GO:0032266 GO:0005546 GO:0010314 GO:0004629 GO:0006816 GO:0007343 GO:0032959 GO:0016042 GO:0007275 GO:0048015 GO:0007204 GO:0060470 GO:0051209 MESQLHELAEARWFLSKVQDDFRGGKINVEITHKLLEKLDFPCHFAHVKHIFKENDRQNQGRITIEEFRAIYRCIVHREEITEIFNTYTENRKILSENSLIEFLTQEQYEMEIDHSDSVEIINKYEPIEEVKGERQMSIEGFARYMFSSECLLFKENCKTVYQDMNHPLSDYFISSSHNTYLISDQILGPSDIWGYVSALVKGCRCLEIDCWDGSQNEPIVYHGYTFTSKLLFKTVVQAINKYAFVTSDYPVVLSLENHCSPGQQEVMASILQSTFGDFLLSDMLEEFPDTLPSPEALKFKILVKNRKVGTLSETHERIGTDKSGQVLEWKEVIYEDGDEDSGMDPETWDVFLSRIKEEREADPSTLSGIAGVKKRKRKMKIAMALSDLVIYTKAEKFRNFQYSRVYQQFNETNSIGESRARKLSKLRVHEFIFHTAAFITRVYPKMMRADSSNFNPQEFWNVGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPDILRDTTLGFNPNEPEYDDHPVTLTIRIISGIQLPVSSSSNTPDIVVIIEVYGVPNDHVKQQTRVVKNNAFSPKWNETFTFLIQVPELALIRFVVETQQGLLSGNELLGQYTLPVLCMNKGYRRVPLFSKSGANLEPSSLFIYVWYFRE 647