ID EPN1_HUMAN Reviewed; 576 AA. AC Q9Y6I3; Q86ST3; Q9HA18; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 2. DT 12-AUG-2020, entry version 191. DE RecName: Full=Epsin-1; DE AltName: Full=EH domain-binding mitotic phosphoprotein; DE AltName: Full=EPS-15-interacting protein 1; GN Name=EPN1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH RP REPS2. RC TISSUE=Brain; RX PubMed=10557078; DOI=10.1038/sj.onc.1202974; RA Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., RA Kikuchi A.; RT "Epsin binds to the EH domain of POB1 and regulates receptor-mediated RT endocytosis."; RL Oncogene 18:5915-5922(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION AT SER-382, MUTAGENESIS OF SER-382, AND INTERACTION WITH RP REPS2; EPS15 AND AP-2 ALPHA SUBUNIT. RX PubMed=10764745; DOI=10.1074/jbc.m000521200; RA Kariya K., Koyama S., Nakashima S., Oshiro T., Morinaka K., Kikuchi A.; RT "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by RT mitotic phosphorylation."; RL J. Biol. Chem. 275:18399-18406(2000). RN [6] RP INTERACTION WITH RALBP1. RX PubMed=12775724; DOI=10.1074/jbc.m302191200; RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.; RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to RT phosphorylate epsin during the switch off of endocytosis in mitosis."; RL J. Biol. Chem. 278:30597-30604(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP INTERACTION WITH AP2B1, AND MUTAGENESIS OF PHE-404. RX PubMed=16516836; DOI=10.1016/j.devcel.2006.01.016; RA Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., RA Roth R., Heuser J.E., Owen D.J., Traub L.M.; RT "Molecular switches involving the AP-2 beta2 appendage regulate endocytic RT cargo selection and clathrin coat assembly."; RL Dev. Cell 10:329-342(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND THR-460, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [11] RP INTERACTION WITH UBQLN2. RX PubMed=18199683; DOI=10.1091/mbc.e07-08-0775; RA N'Diaye E.N., Hanyaloglu A.C., Kajihara K.K., Puthenveedu M.A., Wu P., RA von Zastrow M., Brown E.J.; RT "The ubiquitin-like protein PLIC-2 is a negative regulator of G protein- RT coupled receptor endocytosis."; RL Mol. Biol. Cell 19:1252-1260(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-454; THR-460 AND RP THR-494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420; SER-435; RP SER-454; THR-460 AND THR-470, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-454; THR-460 AND RP THR-494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-447 AND SER-454, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420; SER-435; RP SER-447; SER-454 AND THR-464, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP STRUCTURE BY NMR OF 1-144. RX PubMed=12836669; DOI=10.1023/a:1011397007366; RA Koshiba S., Kigawa T., Kikuchi A., Yokoyama S.; RT "Solution structure of the epsin N-terminal homology (ENTH) domain of human RT epsin."; RL J. Struct. Funct. Genomics 2:1-8(2002). CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- CC bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and CC facilitates the formation of clathrin-coated invaginations (By CC similarity). Regulates receptor-mediated endocytosis. {ECO:0000250, CC ECO:0000269|PubMed:10557078}. CC -!- SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1 (By CC similarity). Binds ubiquitinated proteins (By similarity). Binds REPS2, CC EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex also CC containing NUMB and TFAP2A during interphase and mitosis. Interacts CC with AP2B1. Interacts with UBQLN2. {ECO:0000250|UniProtKB:O88339, CC ECO:0000250|UniProtKB:Q80VP1, ECO:0000269|PubMed:10557078, CC ECO:0000269|PubMed:10764745, ECO:0000269|PubMed:12775724, CC ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:18199683}. CC -!- INTERACTION: CC Q9Y6I3; Q15038: DAZAP2; NbExp=3; IntAct=EBI-713198, EBI-724310; CC Q9Y6I3; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-713198, EBI-373552; CC Q9Y6I3-3; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12026538, EBI-724310; CC Q9Y6I3-3; Q99732: LITAF; NbExp=3; IntAct=EBI-12026538, EBI-725647; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus CC {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. CC Note=Associated with the cytoplasmic membrane at sites where clathrin- CC coated pits are forming. Colocalizes with clathrin and AP-2 in a CC punctate pattern on the plasma membrane. Detected in presynaptic nerve CC terminals and in Golgi stacks. May shuttle to the nucleus when CC associated with ZBTB16/ZNF145 (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y6I3-2; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y6I3-1; Sequence=VSP_041010, VSP_041011; CC Name=3; CC IsoId=Q9Y6I3-3; Sequence=VSP_041011, VSP_041012; CC -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding. CC -!- DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin CC binding. CC -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction CC with the AP-2 complex subunit AP2B1. {ECO:0000250}. CC -!- PTM: Phosphorylated on serine and/or threonine residues in mitotic CC cells. Phosphorylation reduces interaction with REPS2, AP-2 and the CC membrane fraction. Depolarization of synaptosomes results in CC dephosphorylation. {ECO:0000269|PubMed:10764745}. CC -!- PTM: Ubiquitinated. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: [Isoform 2]: CC Sequence=AAD38326.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend - Issue 42 CC of January 2004; CC URL="https://web.expasy.org/spotlight/back_issues/042"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF073727; AAD38326.1; ALT_FRAME; mRNA. DR EMBL; AK022454; BAB14041.1; -; mRNA. DR EMBL; AC008735; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC044651; AAH44651.1; -; mRNA. DR CCDS; CCDS46198.1; -. [Q9Y6I3-1] DR CCDS; CCDS46199.1; -. [Q9Y6I3-2] DR CCDS; CCDS46200.1; -. [Q9Y6I3-3] DR RefSeq; NP_001123543.1; NM_001130071.1. [Q9Y6I3-1] DR RefSeq; NP_001123544.1; NM_001130072.1. [Q9Y6I3-2] DR RefSeq; NP_037465.2; NM_013333.3. [Q9Y6I3-3] DR RefSeq; XP_005258886.1; XM_005258829.2. DR RefSeq; XP_011525183.1; XM_011526881.1. DR RefSeq; XP_016882211.1; XM_017026722.1. DR PDB; 1INZ; NMR; -; A=1-144. DR PDB; 1KYD; X-ray; 2.00 A; P=366-370. DR PDBsum; 1INZ; -. DR PDBsum; 1KYD; -. DR SMR; Q9Y6I3; -. DR BioGRID; 118965; 72. DR CORUM; Q9Y6I3; -. DR ELM; Q9Y6I3; -. DR IntAct; Q9Y6I3; 38. DR MINT; Q9Y6I3; -. DR STRING; 9606.ENSP00000406209; -. DR BindingDB; Q9Y6I3; -. DR ChEMBL; CHEMBL3259465; -. DR DrugBank; DB03316; 1,4-Dioxane. DR DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate. DR MoonDB; Q9Y6I3; Curated. DR GlyGen; Q9Y6I3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y6I3; -. DR MetOSite; Q9Y6I3; -. DR PhosphoSitePlus; Q9Y6I3; -. DR BioMuta; EPN1; -. DR DMDM; 332278179; -. DR EPD; Q9Y6I3; -. DR jPOST; Q9Y6I3; -. DR MassIVE; Q9Y6I3; -. DR MaxQB; Q9Y6I3; -. DR PeptideAtlas; Q9Y6I3; -. DR PRIDE; Q9Y6I3; -. DR ProteomicsDB; 86689; -. [Q9Y6I3-2] DR ProteomicsDB; 86690; -. [Q9Y6I3-1] DR ProteomicsDB; 86691; -. [Q9Y6I3-3] DR Antibodypedia; 4051; 208 antibodies. DR DNASU; 29924; -. DR Ensembl; ENST00000085079; ENSP00000085079; ENSG00000063245. [Q9Y6I3-3] DR Ensembl; ENST00000270460; ENSP00000270460; ENSG00000063245. [Q9Y6I3-2] DR Ensembl; ENST00000411543; ENSP00000406209; ENSG00000063245. [Q9Y6I3-1] DR GeneID; 29924; -. DR KEGG; hsa:29924; -. DR UCSC; uc002qlv.4; human. [Q9Y6I3-2] DR CTD; 29924; -. DR DisGeNET; 29924; -. DR EuPathDB; HostDB:ENSG00000063245.14; -. DR GeneCards; EPN1; -. DR HGNC; HGNC:21604; EPN1. DR HPA; ENSG00000063245; Low tissue specificity. DR MIM; 607262; gene. DR neXtProt; NX_Q9Y6I3; -. DR OpenTargets; ENSG00000063245; -. DR PharmGKB; PA134860916; -. DR eggNOG; KOG2056; Eukaryota. DR GeneTree; ENSGT00940000160411; -. DR HOGENOM; CLU_012678_4_2_1; -. DR InParanoid; Q9Y6I3; -. DR KO; K12471; -. DR OMA; SNYGTPR; -. DR OrthoDB; 1263849at2759; -. DR TreeFam; TF313361; -. DR PathwayCommons; Q9Y6I3; -. DR Reactome; R-HSA-182971; EGFR downregulation. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; Q9Y6I3; -. DR SIGNOR; Q9Y6I3; -. DR BioGRID-ORCS; 29924; 18 hits in 875 CRISPR screens. DR ChiTaRS; EPN1; human. DR EvolutionaryTrace; Q9Y6I3; -. DR GeneWiki; EPN1; -. DR GenomeRNAi; 29924; -. DR Pharos; Q9Y6I3; Tbio. DR PRO; PR:Q9Y6I3; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9Y6I3; protein. DR Bgee; ENSG00000063245; Expressed in body of stomach and 218 other tissues. DR ExpressionAtlas; Q9Y6I3; baseline and differential. DR Genevisible; Q9Y6I3; HS. DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IGI:BHF-UCL. DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR003903; UIM_dom. DR Pfam; PF01417; ENTH; 1. DR SMART; SM00273; ENTH; 1. DR SMART; SM00726; UIM; 3. DR SUPFAM; SSF48464; SSF48464; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS50330; UIM; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Coated pit; Cytoplasm; KW Endocytosis; Lipid-binding; Membrane; Methylation; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..576 FT /note="Epsin-1" FT /id="PRO_0000074513" FT DOMAIN 12..144 FT /note="ENTH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243" FT DOMAIN 183..202 FT /note="UIM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 208..227 FT /note="UIM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 233..252 FT /note="UIM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT REPEAT 274..276 FT /note="1" FT REPEAT 294..296 FT /note="2" FT REPEAT 306..308 FT /note="3" FT REPEAT 319..321 FT /note="4" FT REPEAT 332..334 FT /note="5" FT REPEAT 349..351 FT /note="6" FT REPEAT 367..369 FT /note="7" FT REPEAT 377..379 FT /note="8" FT REPEAT 502..504 FT /note="1" FT REPEAT 518..520 FT /note="2" FT REPEAT 572..574 FT /note="3" FT REGION 274..379 FT /note="8 X 3 AA repeats of [ED]-P-W" FT REGION 502..574 FT /note="3 X 3 AA repeats of N-P-F" FT MOTIF 402..411 FT /note="[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif" FT COMPBIAS 267..573 FT /note="Ala/Gly/Pro-rich" FT BINDING 8 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT BINDING 11 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT BINDING 25 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT BINDING 30 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT BINDING 63 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT BINDING 73 FT /note="Phosphatidylinositol lipid headgroup" FT /evidence="ECO:0000250" FT MOD_RES 382 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:10764745" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT MOD_RES 460 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231" FT MOD_RES 464 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 470 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:19690332" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80VP1" FT MOD_RES 494 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231" FT MOD_RES 534 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q80VP1" FT VAR_SEQ 1 FT /note="M -> MGDQSWLWNQAAPGVRSPVFACSVEKGNVPLVLSEHLAHSRDPGSGA FT VRFLISPEPWASAILGTSGLLASPVLPAALDAVTCQHLPQPSSGSRPISPRIGALCPLL FT LQPGTM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10557078" FT /id="VSP_041010" FT VAR_SEQ 202..226 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10557078, FT ECO:0000303|PubMed:15489334" FT /id="VSP_041011" FT VAR_SEQ 393 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041012" FT MUTAGEN 382 FT /note="S->A: Abolishes phosphorylation by CDK1." FT /evidence="ECO:0000269|PubMed:10764745" FT MUTAGEN 382 FT /note="S->D: Abolishes phosphorylation by CDK1 and reduces FT REPS2 binding." FT /evidence="ECO:0000269|PubMed:10764745" FT MUTAGEN 404 FT /note="F->A: Reduces interaction with AP2B1." FT /evidence="ECO:0000269|PubMed:16516836" FT HELIX 20..27 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 39..47 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 51..62 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 63..65 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 72..86 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 90..98 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 100..108 FT /evidence="ECO:0000244|PDB:1INZ" FT HELIX 121..134 FT /evidence="ECO:0000244|PDB:1INZ" SQ SEQUENCE 576 AA; 60293 MW; 68DD433F3168E975 CRC64; MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD QPPSCGPEDD AQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP WGSSDGGVPV SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE PDEFSDFDRL RTALPTSGSS AGELELLAGE VPARSPGAFD MSGVRGSLAE AVGSPPPAAT PTPTPPTRKT PESFLGPNAA LVDLDSLVSR PGPTPPGAKA SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP VPGAPPTYIS PLGGGPGLPP MMPPGPPAPN TNPFLL //