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 24-JAN-2024, entry version 191. 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}; 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; 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; 101. DR ELM; O95208; -. DR IntAct; O95208; 56. DR MINT; O95208; -. DR STRING; 9606.ENSP00000320543; -. DR GlyCosmos; O95208; 1 site, 1 glycan. DR GlyGen; O95208; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; O95208; -. DR PhosphoSitePlus; O95208; -. DR BioMuta; EPN2; -. DR EPD; O95208; -. DR jPOST; O95208; -. DR MassIVE; O95208; -. DR MaxQB; O95208; -. DR PaxDb; 9606-ENSP00000320543; -. DR PeptideAtlas; O95208; -. DR ProteomicsDB; 19190; -. DR ProteomicsDB; 2056; -. DR ProteomicsDB; 50717; -. [O95208-1] DR ProteomicsDB; 50718; -. [O95208-2] DR ProteomicsDB; 50719; -. [O95208-3] DR Pumba; O95208; -. DR Antibodypedia; 25881; 402 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 AGR; HGNC:18639; -. 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; YLIKCGS; -. DR OrthoDB; 1532at2759; -. 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 1159 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 199 other cell types or tissues. DR ExpressionAtlas; O95208; baseline and differential. 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 CDD; cd16990; ENTH_Epsin; 1. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR003903; UIM_dom. DR PANTHER; PTHR12276:SF50; EPSIN-2; 1. DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1. DR Pfam; PF01417; ENTH; 1. DR SMART; SM00273; ENTH; 1. DR SMART; SM00726; UIM; 2. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS50330; UIM; 2. DR Genevisible; O95208; HS. 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 //