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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   03-AUG-2022, entry version 200.
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   FUNCTION, AND INTERACTION WITH EPS15 AND REPS2.
RX   PubMed=10393179; DOI=10.1093/emboj/18.13.3629;
RA   Nakashima S., Morinaka K., Koyama S., Ikeda M., Kishida M., Okawa K.,
RA   Iwamatsu A., Kishida S., Kikuchi A.;
RT   "Small G protein Ral and its downstream molecules regulate endocytosis of
RT   EGF and insulin receptors.";
RL   EMBO J. 18:3629-3642(1999).
RN   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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 (PubMed:10557078,
CC       PubMed:10393179). {ECO:0000250|UniProtKB:O88339,
CC       ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:10557078}.
CC   -!- SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1 (By
CC       similarity). Binds ubiquitinated proteins (By similarity). Binds AP2A1
CC       and AP2A2. Interacts with RALBP1 in a complex also containing NUMB and
CC       TFAP2A during interphase and mitosis. Interacts with AP2B1. Interacts
CC       with UBQLN2. Interacts with REPS2; the interaction is direct
CC       (PubMed:10557078, PubMed:10764745, PubMed:10393179). Interacts with
CC       EPS15; the interaction is direct (PubMed:10764745, PubMed:10393179).
CC       {ECO:0000250|UniProtKB:O88339, ECO:0000250|UniProtKB:Q80VP1,
CC       ECO:0000269|PubMed:10393179, 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; P42566: EPS15; NbExp=2; IntAct=EBI-713198, EBI-396684;
CC       Q9Y6I3; Q15884: FAM189A2; NbExp=5; IntAct=EBI-713198, EBI-8636612;
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";
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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   AlphaFoldDB; Q9Y6I3; -.
DR   BMRB; Q9Y6I3; -.
DR   SMR; Q9Y6I3; -.
DR   BioGRID; 118965; 99.
DR   CORUM; Q9Y6I3; -.
DR   ELM; Q9Y6I3; -.
DR   IntAct; Q9Y6I3; 42.
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; 2 sites, 2 O-linked glycans (2 sites).
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; 221 antibodies from 30 providers.
DR   DNASU; 29924; -.
DR   Ensembl; ENST00000085079.11; ENSP00000085079.6; ENSG00000063245.15. [Q9Y6I3-3]
DR   Ensembl; ENST00000270460.11; ENSP00000270460.6; ENSG00000063245.15. [Q9Y6I3-2]
DR   Ensembl; ENST00000411543.6; ENSP00000406209.1; ENSG00000063245.15. [Q9Y6I3-1]
DR   GeneID; 29924; -.
DR   KEGG; hsa:29924; -.
DR   MANE-Select; ENST00000270460.11; ENSP00000270460.6; NM_001130072.2; NP_001123544.1.
DR   UCSC; uc002qlv.4; human. [Q9Y6I3-2]
DR   CTD; 29924; -.
DR   DisGeNET; 29924; -.
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   VEuPathDB; HostDB:ENSG00000063245; -.
DR   eggNOG; KOG2056; Eukaryota.
DR   GeneTree; ENSGT00940000160411; -.
DR   HOGENOM; CLU_012678_4_2_1; -.
DR   InParanoid; Q9Y6I3; -.
DR   OMA; CEKADEM; -.
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; 30 hits in 1085 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 apex of heart and 183 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: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:1903671; P:negative regulation of sprouting angiogenesis; IGI:BHF-UCL.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   DisProt; DP02930; -.
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   Pfam; PF02809; UIM; 3.
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          149..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..379
FT                   /note="8 X 3 AA repeats of [ED]-P-W"
FT   REGION          448..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        293..322
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..470
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..576
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
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:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         460
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         464
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|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:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|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:0007829|PDB:1INZ"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           51..62
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           90..98
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           100..108
FT                   /evidence="ECO:0007829|PDB:1INZ"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|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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