EP15R_HUMAN
ID EP15R_HUMAN Reviewed; 864 AA.
AC Q9UBC2; A2RRF3; A5PL29; B4DKA3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Epidermal growth factor receptor substrate 15-like 1;
DE AltName: Full=Eps15-related protein;
DE Short=Eps15R;
GN Name=EPS15L1; Synonyms=EPS15R;
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 1).
RC TISSUE=Brain;
RA Nakashima S., Morinaka K., Ikeda M., Kishida S., Koyama S., Kikuchi A.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Thalamus;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] (ISOFORMS 3 AND 4).
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 FUNCTION.
RX PubMed=9407958;
RA Carbone R., Fre S., Iannolo G., Belleudi F., Mancini P., Pelicci P.G.,
RA Torrisi M.R., Di Fiore P.P.;
RT "eps15 and eps15R are essential components of the endocytic pathway.";
RL Cancer Res. 57:5498-5504(1997).
RN [8]
RP INTERACTION WITH 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP INTERACTION WITH UBQLN1.
RX PubMed=16159959; DOI=10.1242/jcs.02571;
RA Regan-Klapisz E., Sorokina I., Voortman J., de Keizer P., Roovers R.C.,
RA Verheesen P., Urbe S., Fallon L., Fon E.A., Verkleij A., Benmerah A.,
RA van Bergen en Henegouwen P.M.;
RT "Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a
RT UIM-UBL interaction.";
RL J. Cell Sci. 118:4437-4450(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP INTERACTION WITH CAV1N3.
RX PubMed=19262564; DOI=10.1038/emboj.2009.46;
RA McMahon K.A., Zajicek H., Li W.P., Peyton M.J., Minna J.D., Hernandez V.J.,
RA Luby-Phelps K., Anderson R.G.;
RT "SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae
RT function.";
RL EMBO J. 28:1001-1015(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-255; SER-560;
RP THR-577 AND THR-797, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP 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 [17]
RP INTERACTION WITH FCHO2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP 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 [20]
RP FUNCTION, AND INTERACTION WITH DAB2.
RX PubMed=22648170; DOI=10.1091/mbc.e11-12-1007;
RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate
RT integrin beta1 endocytosis.";
RL Mol. Biol. Cell 23:2905-2916(2012).
RN [21]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-229; SER-244;
RP SER-253; SER-255; SER-259; THR-366; SER-374; SER-377; SER-593; SER-672;
RP SER-697 AND SER-717, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; THR-366; SER-371;
RP SER-377; SER-593; SER-666; SER-734 AND SER-793, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [24]
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).
CC -!- FUNCTION: Seems to be a constitutive component of clathrin-coated pits
CC that is required for receptor-mediated endocytosis. Involved in
CC endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR);
CC internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to
CC require association with DAB2. {ECO:0000269|PubMed:22648170,
CC ECO:0000269|PubMed:9407958}.
CC -!- SUBUNIT: Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates
CC with the clathrin-associated adapter protein complex 2 (AP-2) (By
CC similarity). Interacts with FCHO1. Interacts with FCHO2. Interacts (via
CC EH domains) with DAB2. Interacts with UBQLN1 (via ubiquitin-like
CC domain). Interacts with CAVIN3 (via leucine-zipper domain)
CC (PubMed:19262564). Interacts with REPS2 (PubMed:10393179).
CC {ECO:0000250|UniProtKB:Q60902, ECO:0000269|PubMed:10393179,
CC ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19262564,
CC ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:22484487,
CC ECO:0000269|PubMed:22648170}.
CC -!- INTERACTION:
CC Q9UBC2; Q969G5: CAVIN3; NbExp=2; IntAct=EBI-2556746, EBI-3893101;
CC Q9UBC2; P63218: GNG5; NbExp=3; IntAct=EBI-2556746, EBI-10220734;
CC Q9UBC2; P0DI81: TRAPPC2; NbExp=3; IntAct=EBI-2556746, EBI-5663373;
CC Q9UBC2-3; A1L1C6: LRRC7; NbExp=3; IntAct=EBI-11958621, EBI-10171988;
CC Q9UBC2-3; O14777: NDC80; NbExp=3; IntAct=EBI-11958621, EBI-715849;
CC Q9UBC2-3; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-11958621, EBI-11961968;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, coated pit
CC {ECO:0000250}. Note=Localized to plasma membrane coated pits.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UBC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBC2-2; Sequence=VSP_042200;
CC Name=3;
CC IsoId=Q9UBC2-3; Sequence=VSP_045429;
CC Name=4;
CC IsoId=Q9UBC2-4; Sequence=VSP_046904, VSP_046905;
CC -!- PTM: Phosphorylated on tyrosine residues by EGFR. {ECO:0000250}.
CC -!- CAUTION: Studies in clathrin-mediated endocytosis used a siRNA mixture
CC of EPS15 and EPS15L1. {ECO:0000305|PubMed:22648170}.
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DR EMBL; AF110265; AAF21930.1; -; mRNA.
DR EMBL; AB015346; BAA88118.1; -; mRNA.
DR EMBL; AK024166; BAG51266.1; -; mRNA.
DR EMBL; AK296473; BAG59115.1; -; mRNA.
DR EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84542.1; -; Genomic_DNA.
DR EMBL; BC131590; AAI31591.1; -; mRNA.
DR EMBL; BC142716; AAI42717.1; -; mRNA.
DR CCDS; CCDS32944.1; -. [Q9UBC2-1]
DR CCDS; CCDS58653.1; -. [Q9UBC2-3]
DR CCDS; CCDS58654.1; -. [Q9UBC2-2]
DR CCDS; CCDS59363.1; -. [Q9UBC2-4]
DR RefSeq; NP_001245303.1; NM_001258374.1. [Q9UBC2-2]
DR RefSeq; NP_001245304.1; NM_001258375.1. [Q9UBC2-3]
DR RefSeq; NP_001245305.1; NM_001258376.1. [Q9UBC2-4]
DR RefSeq; NP_067058.1; NM_021235.2. [Q9UBC2-1]
DR AlphaFoldDB; Q9UBC2; -.
DR SMR; Q9UBC2; -.
DR BioGRID; 121840; 113.
DR ELM; Q9UBC2; -.
DR IntAct; Q9UBC2; 45.
DR MINT; Q9UBC2; -.
DR STRING; 9606.ENSP00000393313; -.
DR MoonDB; Q9UBC2; Curated.
DR iPTMnet; Q9UBC2; -.
DR MetOSite; Q9UBC2; -.
DR PhosphoSitePlus; Q9UBC2; -.
DR BioMuta; EPS15L1; -.
DR DMDM; 61223942; -.
DR EPD; Q9UBC2; -.
DR jPOST; Q9UBC2; -.
DR MassIVE; Q9UBC2; -.
DR MaxQB; Q9UBC2; -.
DR PaxDb; Q9UBC2; -.
DR PeptideAtlas; Q9UBC2; -.
DR PRIDE; Q9UBC2; -.
DR ProteomicsDB; 466; -.
DR ProteomicsDB; 83933; -. [Q9UBC2-1]
DR ProteomicsDB; 83934; -. [Q9UBC2-2]
DR Antibodypedia; 14142; 213 antibodies from 31 providers.
DR DNASU; 58513; -.
DR Ensembl; ENST00000248070.10; ENSP00000248070.5; ENSG00000127527.14. [Q9UBC2-1]
DR Ensembl; ENST00000455140.7; ENSP00000393313.1; ENSG00000127527.14. [Q9UBC2-2]
DR Ensembl; ENST00000535753.6; ENSP00000440103.1; ENSG00000127527.14. [Q9UBC2-3]
DR Ensembl; ENST00000597937.5; ENSP00000472267.1; ENSG00000127527.14. [Q9UBC2-4]
DR Ensembl; ENST00000602022.5; ENSP00000471981.1; ENSG00000127527.14. [Q9UBC2-3]
DR GeneID; 58513; -.
DR KEGG; hsa:58513; -.
DR MANE-Select; ENST00000455140.7; ENSP00000393313.1; NM_001258374.3; NP_001245303.1. [Q9UBC2-2]
DR UCSC; uc002ndx.5; human. [Q9UBC2-1]
DR CTD; 58513; -.
DR DisGeNET; 58513; -.
DR GeneCards; EPS15L1; -.
DR HGNC; HGNC:24634; EPS15L1.
DR HPA; ENSG00000127527; Low tissue specificity.
DR MalaCards; EPS15L1; -.
DR neXtProt; NX_Q9UBC2; -.
DR OpenTargets; ENSG00000127527; -.
DR Orphanet; 2440; Isolated split hand-split foot malformation.
DR PharmGKB; PA134906266; -.
DR VEuPathDB; HostDB:ENSG00000127527; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00940000155438; -.
DR HOGENOM; CLU_007270_1_1_1; -.
DR InParanoid; Q9UBC2; -.
DR OMA; AMYLVRQ; -.
DR OrthoDB; 597979at2759; -.
DR PhylomeDB; Q9UBC2; -.
DR TreeFam; TF324293; -.
DR PathwayCommons; Q9UBC2; -.
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; Q9UBC2; -.
DR BioGRID-ORCS; 58513; 28 hits in 1082 CRISPR screens.
DR ChiTaRS; EPS15L1; human.
DR GeneWiki; EPS15L1; -.
DR GenomeRNAi; 58513; -.
DR Pharos; Q9UBC2; Tbio.
DR PRO; PR:Q9UBC2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UBC2; protein.
DR Bgee; ENSG00000127527; Expressed in gastrocnemius and 172 other tissues.
DR ExpressionAtlas; Q9UBC2; baseline and differential.
DR Genevisible; Q9UBC2; HS.
DR GO; GO:0030132; C:clathrin coat of coated pit; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR CDD; cd00052; EH; 3.
DR CDD; cd00176; SPEC; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR Pfam; PF12763; EF-hand_4; 3.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 3.
DR SUPFAM; SSF47473; SSF47473; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50031; EH; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane; Coated pit;
KW Coiled coil; Endocytosis; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..864
FT /note="Epidermal growth factor receptor substrate 15-like
FT 1"
FT /id="PRO_0000146118"
FT DOMAIN 15..104
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 48..83
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..215
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 159..194
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 274..309
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 275..365
FT /note="EH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 310..343
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 618..620
FT /note="1"
FT REPEAT 640..642
FT /note="2"
FT REPEAT 645..647
FT /note="3"
FT REPEAT 650..652
FT /note="4"
FT REPEAT 656..658
FT /note="5"
FT REPEAT 661..663
FT /note="6"
FT REPEAT 667..669
FT /note="7"
FT REPEAT 685..687
FT /note="8"
FT REPEAT 690..692
FT /note="9"
FT REPEAT 709..711
FT /note="10"
FT REPEAT 728..730
FT /note="11"
FT REPEAT 754..756
FT /note="12"
FT REPEAT 806..808
FT /note="13"
FT REPEAT 812..814
FT /note="14"
FT REPEAT 833..835
FT /note="15"
FT REGION 15..368
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000250"
FT REGION 221..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..835
FT /note="15 X 3 AA repeats of D-P-F"
FT COILED 386..553
FT /evidence="ECO:0000255"
FT COMPBIAS 235..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 74
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60902"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60902"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60902"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 564
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60902"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 797
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 598..601
FT /note="DDPF -> VKVE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046904"
FT VAR_SEQ 602..864
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046905"
FT VAR_SEQ 750..864
FT /note="PPPSGPFTSSLGGAGFSDDPFKSKQDTPALPPKKPAPPRPKPPSGKSTPVSQ
FT LGSADFPEAPDPFQPLGADSGDPFQSKKGFGDPFSGKDPFVPSSAAKPSKASASGFADF
FT TSVS -> VKVHL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045429"
FT VAR_SEQ 863..864
FT /note="VS -> FGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLELAIALSKADMP
FT AA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042200"
FT CONFLICT 680
FT /note="K -> E (in Ref. 3; BAG59115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 864 AA; 94255 MW; F4126069F6E00387 CRC64;
MAAPLIPLSQ QIPTGNSLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA
DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSNLNLSMPP PKFHDTSSPL MVTPPSAEAH
WAVRVEEKAK FDGIFESLLP INGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD
RDEFAVAMHL VYRALEKEPV PSALPPSLIP PSKRKKTVFP GAVPVLPASP PPKDSLRSTP
SHGSVSSLNS TGSLSPKHSL KQTQPTVNWV VPVADKMRFD EIFLKTDLDL DGYVSGQEVK
EIFMHSGLTQ NLLAHIWALA DTRQTGKLSK DQFALAMYFI QQKVSKGIDP PQVLSPDMVP
PSERGTPGPD SSGSLGSGEF TGVKELDDIS QEIAQLQREK YSLEQDIREK EEAIRQKTSE
VQELQNDLDR ETSSLQELEA QKQDAQDRLD EMDQQKAKLR DMLSDVRQKC QDETQMISSL
KTQIQSQESD LKSQEDDLNR AKSELNRLQQ EETQLEQSIQ AGRVQLETII KSLKSTQDEI
NQARSKLSQL HESRQEAHRS LEQYDQVLDG AHGASLTDLA NLSEGVSLAE RGSFGAMDDP
FKNKALLFSN NTQELHPDPF QTEDPFKSDP FKGADPFKGD PFQNDPFAEQ QTTSTDPFGG
DPFKESDPFR GSATDDFFKK QTKNDPFTSD PFTKNPSLPS KLDPFESSDP FSSSSVSSKG
SDPFGTLDPF GSGSFNSAEG FADFSQMSKP PPSGPFTSSL GGAGFSDDPF KSKQDTPALP
PKKPAPPRPK PPSGKSTPVS QLGSADFPEA PDPFQPLGAD SGDPFQSKKG FGDPFSGKDP
FVPSSAAKPS KASASGFADF TSVS
