GenomeNet

Database: UniProt/SWISS-PROT
Entry: EPN1_HUMAN
LinkDB: EPN1_HUMAN
Original site: EPN1_HUMAN 
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   31-JUL-2019, entry version 183.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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
RT   project: 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
RP   WITH 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.,
RA   Kikuchi A.;
RT   "Regulation of complex formation of POB1/epsin/adaptor protein complex
RT   2 by 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
RP   BY 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling 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
RT   endocytic 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
RT   phosphorylation 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
RT   sequential 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
RT   protein-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
RP   AND THR-494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RP   AND THR-494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
RP   SER-454, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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.,
RA   Ayoub D., 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
RT   human 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.
CC       {ECO:0000250, ECO:0000269|PubMed:10557078}.
CC   -!- SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1 (By
CC       similarity). Binds ubiquitinated proteins (By similarity). Binds
CC       REPS2, EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex
CC       also containing NUMB and TFAP2A during interphase and mitosis.
CC       Interacts with AP2B1. Interacts with UBQLN2.
CC       {ECO:0000250|UniProtKB:O88339, ECO:0000250|UniProtKB:Q80VP1,
CC       ECO:0000269|PubMed:10557078, ECO:0000269|PubMed:10764745,
CC       ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:16516836,
CC       ECO:0000269|PubMed:18199683}.
CC   -!- INTERACTION:
CC       Q15038:DAZAP2; NbExp=3; IntAct=EBI-713198, EBI-724310;
CC       Q96CS7:PLEKHB2; NbExp=3; IntAct=EBI-713198, EBI-373552;
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
CC       clathrin-coated pits are forming. Colocalizes with clathrin and
CC       AP-2 in a punctate pattern on the plasma membrane. Detected in
CC       presynaptic nerve terminals and in Golgi stacks. May shuttle to
CC       the nucleus when associated with ZBTB16/ZNF145 (By similarity).
CC       {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         Note=Ref.1 (AAD38326) sequence differs from that shown due to a
CC         frameshift in position 98. {ECO:0000305};
CC       Name=3;
CC         IsoId=Q9Y6I3-3; Sequence=VSP_041011, VSP_041012;
CC         Note=May be due to a competing donor splice site. No
CC         experimental confirmation available.;
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
CC       interaction 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
CC       the membrane fraction. Depolarization of synaptosomes results in
CC       dephosphorylation. {ECO:0000269|PubMed:10764745}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend
CC       - Issue 42 of January 2004;
CC       URL="https://web.expasy.org/spotlight/back_issues/042";
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. [Q9Y6I3-2]
DR   RefSeq; XP_011525183.1; XM_011526881.1.
DR   RefSeq; XP_016882211.1; XM_017026722.1. [Q9Y6I3-3]
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; 70.
DR   CORUM; Q9Y6I3; -.
DR   ELM; Q9Y6I3; -.
DR   IntAct; Q9Y6I3; 27.
DR   MINT; Q9Y6I3; -.
DR   STRING; 9606.ENSP00000406209; -.
DR   BindingDB; Q9Y6I3; -.
DR   ChEMBL; CHEMBL3259465; -.
DR   MoonDB; Q9Y6I3; Curated.
DR   iPTMnet; Q9Y6I3; -.
DR   PhosphoSitePlus; Q9Y6I3; -.
DR   BioMuta; EPN1; -.
DR   DMDM; 332278179; -.
DR   EPD; Q9Y6I3; -.
DR   jPOST; 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   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   GeneCards; EPN1; -.
DR   HGNC; HGNC:21604; EPN1.
DR   HPA; CAB009729; -.
DR   HPA; HPA061136; -.
DR   MIM; 607262; gene.
DR   neXtProt; NX_Q9Y6I3; -.
DR   OpenTargets; ENSG00000063245; -.
DR   PharmGKB; PA134860916; -.
DR   GeneTree; ENSGT00940000160411; -.
DR   HOGENOM; HOG000008298; -.
DR   InParanoid; Q9Y6I3; -.
DR   KO; K12471; -.
DR   OMA; GMMQASP; -.
DR   OrthoDB; 1263849at2759; -.
DR   TreeFam; TF313361; -.
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   EvolutionaryTrace; Q9Y6I3; -.
DR   GeneWiki; EPN1; -.
DR   GenomeRNAi; 29924; -.
DR   PRO; PR:Q9Y6I3; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000063245; Expressed in 206 organ(s), highest expression level in body of stomach.
DR   ExpressionAtlas; Q9Y6I3; baseline and differential.
DR   Genevisible; Q9Y6I3; HS.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; TAS:ProtInc.
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;
KW   Complete proteome; Cytoplasm; Endocytosis; Lipid-binding; Membrane;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1    576       Epsin-1.
FT                                /FTId=PRO_0000074513.
FT   DOMAIN       12    144       ENTH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00243}.
FT   DOMAIN      183    202       UIM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00213}.
FT   DOMAIN      208    227       UIM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00213}.
FT   DOMAIN      233    252       UIM 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00213}.
FT   REPEAT      274    276       1.
FT   REPEAT      294    296       2.
FT   REPEAT      306    308       3.
FT   REPEAT      319    321       4.
FT   REPEAT      332    334       5.
FT   REPEAT      349    351       6.
FT   REPEAT      367    369       7.
FT   REPEAT      377    379       8.
FT   REPEAT      502    504       1.
FT   REPEAT      518    520       2.
FT   REPEAT      572    574       3.
FT   REGION      274    379       8 X 3 AA repeats of [ED]-P-W.
FT   REGION      502    574       3 X 3 AA repeats of N-P-F.
FT   MOTIF       402    411       [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif.
FT   COMPBIAS    267    573       Ala/Gly/Pro-rich.
FT   BINDING       8      8       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   BINDING      11     11       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   BINDING      25     25       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   BINDING      30     30       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   BINDING      63     63       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   BINDING      73     73       Phosphatidylinositol lipid headgroup.
FT                                {ECO:0000250}.
FT   MOD_RES     382    382       Phosphoserine; by CDK1.
FT                                {ECO:0000269|PubMed:10764745}.
FT   MOD_RES     419    419       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     420    420       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     435    435       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     447    447       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     454    454       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     460    460       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     464    464       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     470    470       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     473    473       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q80VP1}.
FT   MOD_RES     494    494       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     534    534       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q80VP1}.
FT   VAR_SEQ       1      1       M -> MGDQSWLWNQAAPGVRSPVFACSVEKGNVPLVLSEH
FT                                LAHSRDPGSGAVRFLISPEPWASAILGTSGLLASPVLPAAL
FT                                DAVTCQHLPQPSSGSRPISPRIGALCPLLLQPGTM (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:10557078}.
FT                                /FTId=VSP_041010.
FT   VAR_SEQ     202    226       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:10557078,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_041011.
FT   VAR_SEQ     393    393       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_041012.
FT   MUTAGEN     382    382       S->A: Abolishes phosphorylation by CDK1.
FT                                {ECO:0000269|PubMed:10764745}.
FT   MUTAGEN     382    382       S->D: Abolishes phosphorylation by CDK1
FT                                and reduces REPS2 binding.
FT                                {ECO:0000269|PubMed:10764745}.
FT   MUTAGEN     404    404       F->A: Reduces interaction with AP2B1.
FT                                {ECO:0000269|PubMed:16516836}.
FT   HELIX        20     27       {ECO:0000244|PDB:1INZ}.
FT   HELIX        39     47       {ECO:0000244|PDB:1INZ}.
FT   HELIX        51     62       {ECO:0000244|PDB:1INZ}.
FT   HELIX        63     65       {ECO:0000244|PDB:1INZ}.
FT   HELIX        72     86       {ECO:0000244|PDB:1INZ}.
FT   HELIX        90     98       {ECO:0000244|PDB:1INZ}.
FT   HELIX       100    108       {ECO:0000244|PDB:1INZ}.
FT   HELIX       121    134       {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
//
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