EPN2_HUMAN
ID EPN2_HUMAN Reviewed; 641 AA.
AC O95208; A8MTV8; B3KRX8; E9PBC2; O95207; Q52LD0; Q9H7Z2; Q9UPT7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Epsin-2;
DE AltName: Full=EPS-15-interacting protein 2;
GN Name=EPN2; Synonyms=KIAA1065;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP AP-2 AND CLATHRIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT
RP ALA-401.
RC TISSUE=Brain;
RX PubMed=10567358; DOI=10.1074/jbc.274.48.33959;
RA Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E.,
RA Di Fiore P.P., De Camilli P.;
RT "The epsins define a family of proteins that interact with components of
RT the clathrin coat and contain a new protein module.";
RL J. Biol. Chem. 274:33959-33965(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-401.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 3), AND VARIANT ALA-401.
RC TISSUE=Embryo, Fetal brain, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-401.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-401.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 (ISOFORM 3), AND
RP IDENTIFICATION 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., 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 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-195 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-156 (ISOFORM 3),
RP AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-192 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-153 (ISOFORM 3), 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).
CC -!- FUNCTION: Plays a role in the formation of clathrin-coated
CC invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.
CC -!- SUBUNIT: Binds EPS15 (By similarity). Interacts with ITSN1 (By
CC similarity). Binds AP-2 and clathrin. Interacts with UBQLN2.
CC {ECO:0000250|UniProtKB:Q8CHU3, ECO:0000250|UniProtKB:Q9Z1Z3,
CC ECO:0000269|PubMed:10567358, ECO:0000269|PubMed:18199683}.
CC -!- INTERACTION:
CC O95208-2; Q8N5I2: ARRDC1; NbExp=3; IntAct=EBI-12135243, EBI-2339564;
CC O95208-2; Q8TBH0: ARRDC2; NbExp=3; IntAct=EBI-12135243, EBI-12191751;
CC O95208-2; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-12135243, EBI-2875665;
CC O95208-2; P54253: ATXN1; NbExp=3; IntAct=EBI-12135243, EBI-930964;
CC O95208-2; Q9H305: CDIP1; NbExp=3; IntAct=EBI-12135243, EBI-2876678;
CC O95208-2; Q15038: DAZAP2; NbExp=5; IntAct=EBI-12135243, EBI-724310;
CC O95208-2; P60228: EIF3E; NbExp=3; IntAct=EBI-12135243, EBI-347740;
CC O95208-2; Q9BWQ8: FAIM2; NbExp=3; IntAct=EBI-12135243, EBI-9056723;
CC O95208-2; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-12135243, EBI-11978259;
CC O95208-2; Q8IYD8: FANCM; NbExp=3; IntAct=EBI-12135243, EBI-3957237;
CC O95208-2; Q99732: LITAF; NbExp=5; IntAct=EBI-12135243, EBI-725647;
CC O95208-2; O15344: MID1; NbExp=3; IntAct=EBI-12135243, EBI-2340316;
CC O95208-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-12135243, EBI-10172526;
CC O95208-2; Q16655: MLANA; NbExp=3; IntAct=EBI-12135243, EBI-2509726;
CC O95208-2; Q86T03: PIP4P1; NbExp=3; IntAct=EBI-12135243, EBI-6164623;
CC O95208-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-12135243, EBI-373552;
CC O95208-2; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-12135243, EBI-13318883;
CC O95208-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-12135243, EBI-1383852;
CC O95208-2; O76064: RNF8; NbExp=3; IntAct=EBI-12135243, EBI-373337;
CC O95208-2; Q15797: SMAD1; NbExp=3; IntAct=EBI-12135243, EBI-1567153;
CC O95208-2; Q8N0X7: SPART; NbExp=3; IntAct=EBI-12135243, EBI-2643803;
CC O95208-2; P52888: THOP1; NbExp=3; IntAct=EBI-12135243, EBI-372399;
CC O95208-2; P36406: TRIM23; NbExp=3; IntAct=EBI-12135243, EBI-740098;
CC O95208-2; Q12899: TRIM26; NbExp=3; IntAct=EBI-12135243, EBI-2341136;
CC O95208-2; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-12135243, EBI-6929619;
CC O95208-2; P40222: TXLNA; NbExp=3; IntAct=EBI-12135243, EBI-359793;
CC O95208-2; P62987: UBA52; NbExp=3; IntAct=EBI-12135243, EBI-357304;
CC O95208-2; P0CG48: UBC; NbExp=3; IntAct=EBI-12135243, EBI-3390054;
CC O95208-2; Q96G27: WBP1; NbExp=3; IntAct=EBI-12135243, EBI-3867685;
CC O95208-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-12135243, EBI-10316321;
CC O95208-2; Q969T9: WBP2; NbExp=3; IntAct=EBI-12135243, EBI-727055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10567358}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:10567358}. Note=In punctate structures throughout
CC the cell, associated with clathrin-coated vesicles, and particularly
CC concentrated in the region of the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=2b;
CC IsoId=O95208-1; Sequence=Displayed;
CC Name=2; Synonyms=2a;
CC IsoId=O95208-2; Sequence=VSP_009155;
CC Name=3;
CC IsoId=O95208-3; Sequence=VSP_009154, VSP_009155;
CC Name=4;
CC IsoId=O95208-5; Sequence=VSP_047003;
CC -!- TISSUE SPECIFICITY: Highest expression is found in brain. Detected at
CC lower levels in lung and liver. {ECO:0000269|PubMed:10567358}.
CC -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding.
CC -!- DOMAIN: The DPW repeat domain is involved in AP-2 and clathrin binding.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83017.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG52540.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF062084; AAC78608.1; -; mRNA.
DR EMBL; AF062085; AAC78609.1; -; mRNA.
DR EMBL; AB028988; BAA83017.2; ALT_INIT; mRNA.
DR EMBL; AK001996; BAG51000.1; -; mRNA.
DR EMBL; AK024115; BAB14831.1; -; mRNA.
DR EMBL; AK092366; BAG52540.1; ALT_SEQ; mRNA.
DR EMBL; AC106017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471212; EAW50876.1; -; Genomic_DNA.
DR EMBL; BC093972; AAH93972.1; -; mRNA.
DR EMBL; BC093974; AAH93974.1; -; mRNA.
DR CCDS; CCDS11203.1; -. [O95208-1]
DR CCDS; CCDS11204.1; -. [O95208-2]
DR CCDS; CCDS42277.1; -. [O95208-5]
DR RefSeq; NP_001096134.1; NM_001102664.1. [O95208-5]
DR RefSeq; NP_055779.2; NM_014964.4. [O95208-1]
DR RefSeq; NP_683723.2; NM_148921.3. [O95208-2]
DR AlphaFoldDB; O95208; -.
DR SMR; O95208; -.
DR BioGRID; 116569; 84.
DR ELM; O95208; -.
DR IntAct; O95208; 49.
DR MINT; O95208; -.
DR STRING; 9606.ENSP00000320543; -.
DR GlyGen; O95208; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95208; -.
DR PhosphoSitePlus; O95208; -.
DR BioMuta; EPN2; -.
DR EPD; O95208; -.
DR jPOST; O95208; -.
DR MassIVE; O95208; -.
DR MaxQB; O95208; -.
DR PaxDb; O95208; -.
DR PeptideAtlas; O95208; -.
DR PRIDE; O95208; -.
DR ProteomicsDB; 19190; -.
DR ProteomicsDB; 2056; -.
DR ProteomicsDB; 50717; -. [O95208-1]
DR ProteomicsDB; 50718; -. [O95208-2]
DR ProteomicsDB; 50719; -. [O95208-3]
DR Antibodypedia; 25881; 348 antibodies from 27 providers.
DR DNASU; 22905; -.
DR Ensembl; ENST00000314728.10; ENSP00000320543.5; ENSG00000072134.16. [O95208-1]
DR Ensembl; ENST00000347697.6; ENSP00000261495.3; ENSG00000072134.16. [O95208-2]
DR Ensembl; ENST00000395618.7; ENSP00000378980.3; ENSG00000072134.16. [O95208-5]
DR Ensembl; ENST00000395620.6; ENSP00000378982.2; ENSG00000072134.16. [O95208-2]
DR GeneID; 22905; -.
DR KEGG; hsa:22905; -.
DR MANE-Select; ENST00000314728.10; ENSP00000320543.5; NM_014964.5; NP_055779.2.
DR UCSC; uc002gvd.5; human. [O95208-1]
DR CTD; 22905; -.
DR DisGeNET; 22905; -.
DR GeneCards; EPN2; -.
DR HGNC; HGNC:18639; EPN2.
DR HPA; ENSG00000072134; Low tissue specificity.
DR MIM; 607263; gene.
DR neXtProt; NX_O95208; -.
DR OpenTargets; ENSG00000072134; -.
DR PharmGKB; PA38615; -.
DR VEuPathDB; HostDB:ENSG00000072134; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000157239; -.
DR InParanoid; O95208; -.
DR OMA; EKQSHML; -.
DR OrthoDB; 1263849at2759; -.
DR PhylomeDB; O95208; -.
DR TreeFam; TF313361; -.
DR PathwayCommons; O95208; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O95208; -.
DR BioGRID-ORCS; 22905; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; EPN2; human.
DR GeneWiki; EPN2; -.
DR GenomeRNAi; 22905; -.
DR Pharos; O95208; Tbio.
DR PRO; PR:O95208; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O95208; protein.
DR Bgee; ENSG00000072134; Expressed in colonic epithelium and 198 other tissues.
DR ExpressionAtlas; O95208; baseline and differential.
DR Genevisible; O95208; HS.
DR GO; GO:0030128; C:clathrin coat of endocytic vesicle; IEA:InterPro.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
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; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:BHF-UCL.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027319; Epsin-2_metazoa.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276:SF50; PTHR12276:SF50; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Lipid-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..641
FT /note="Epsin-2"
FT /id="PRO_0000074516"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 275..294
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 300..319
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 352..354
FT /note="1"
FT REPEAT 364..366
FT /note="2"
FT REPEAT 377..379
FT /note="3"
FT REPEAT 391..393
FT /note="4"
FT REPEAT 409..411
FT /note="5"
FT REPEAT 427..429
FT /note="6"
FT REPEAT 537..539
FT /note="1"
FT REPEAT 552..554
FT /note="2"
FT REPEAT 637..639
FT /note="3"
FT REGION 163..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..639
FT /note="6 X 3 AA repeats of [DE]-P-W"
FT REGION 470..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..639
FT /note="3 X 3 AA repeats of N-P-F"
FT COMPBIAS 163..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..510
FT /note="Polar 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 170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHU3"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHU3"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 508
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..285
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047003"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009154"
FT VAR_SEQ 200..256
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10567358,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_009155"
FT VARIANT 401
FT /note="V -> A (in dbSNP:rs6587220)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:10567358, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_053080"
FT VARIANT 531
FT /note="P -> T (in dbSNP:rs1062727)"
FT /id="VAR_047923"
FT VARIANT 532
FT /note="P -> T (in dbSNP:rs1062727)"
FT /id="VAR_053081"
FT CONFLICT 256
FT /note="A -> AS (in Ref. 1; AAC78609)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="T -> N (in Ref. 1; AAC78608/AAC78609)"
FT /evidence="ECO:0000305"
FT MOD_RES O95208-2:192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES O95208-2:195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES O95208-3:153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES O95208-3:156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 641 AA; 68482 MW; 0BE24CBD824F357A CRC64;
MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VAFSEIMSMV
WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG
INVREKSKQL VALLKDEERL KAERAQALKT KERMAQVATG MGSNQITFGR GSSQPNLSTS
HSEQEYGKAG GSPASYHGSP EASLCPQHRT GAPLGQSEEL QPLSQRHPFL PHLGLASRPN
GDWSQPCLTC DRAARATSPR VSSELEQARP QTSGEEELQL QLALAMSREV AEQEERLRRG
DDLRLQMALE ESRRDTVKIP KKKEHGSLPQ QTTLLDLMDA LPSSGPAAQK AEPWGPSAST
NQTNPWGGPA APASTSDPWP SFGTKPAASI DPWGVPTGAT VQSVPKNSDP WAASQQPASS
AGKRASDAWG AVSTTKPVSV SGSFELFSNL NGTIKDDFSE FDNLRTSKKT AESVTSLPSQ
NNGTTSPDPF ESQPLTVASS KPSSARKTPE SFLGPNAALV NLDSLVTRPA PPAQSLNPFL
APGAPATSAP VNPFQVNQPQ PLTLNQLRGS PVLGTSTSFG PGPGVESMAV ASMTSAAPQP
ALGATGSSLT PLGPAMMNMV GSVGIPPSAA QATGTTNPFL L
