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Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)

 EPS15_HUMAN             Reviewed;         896 AA.
P42566; B2R8J7; D3DPJ2; Q5SRH4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
30-AUG-2017, entry version 191.
RecName: Full=Epidermal growth factor receptor substrate 15;
Short=Protein Eps15;
AltName: Full=Protein AF-1p;
Name=EPS15; Synonyms=AF1P;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-822.
TISSUE=Melanoma;
PubMed=8183552;
Wong W.T., Kraus M.H., Carlomagno F., Zelano A., Druck T., Croce C.M.,
Huebner K., di Fiore P.P.;
"The human eps15 gene, encoding a tyrosine kinase substrate, is
conserved in evolution and maps to 1p31-p32.";
Oncogene 9:1591-1597(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8134107;
Bernard O.A., Mauchauffe M., Mecucci C., van den Berghe H., Berger R.;
"A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related
to AF-4, AF-9 nor ENL.";
Oncogene 9:1039-1045(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kronstein R., Grossklaus S., Schnittler H.-J.;
"Eps15 in human umbilical vein endothelial cells.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH CRK.
PubMed=8662907; DOI=10.1074/jbc.271.24.14468;
Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T.,
Nagashima K., Kurata T.;
"Interaction between the amino-terminal SH3 domain of CRK and its
natural target proteins.";
J. Biol. Chem. 271:14468-14472(1996).
[9]
INTERACTION WITH EPN1.
PubMed=9723620; DOI=10.1038/29555;
Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H.,
Di Fiore P.P., De Camilli P.;
"Epsin is an EH-domain-binding protein implicated in clathrin-mediated
endocytosis.";
Nature 394:793-797(1998).
[10]
INTERACTION WITH HGS AND STAM2.
PubMed=12551915; DOI=10.1074/jbc.M210843200;
Bache K.G., Raiborg C., Mehlum A., Stenmark H.;
"STAM and Hrs are subunits of a multivalent ubiquitin-binding complex
on early endosomes.";
J. Biol. Chem. 278:12513-12521(2003).
[11]
INTERACTION WITH SH3BP4.
PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
Tacchetti C., Di Fiore P.P.;
"TTP specifically regulates the internalization of the transferrin
receptor.";
Cell 123:875-888(2005).
[12]
INTERACTION WITH UBQLN1, AND SUBCELLULAR LOCATION.
PubMed=16159959; DOI=10.1242/jcs.02571;
Regan-Klapisz E., Sorokina I., Voortman J., de Keizer P.,
Roovers R.C., Verheesen P., Urbe S., Fallon L., Fon E.A., Verkleij A.,
Benmerah A., van Bergen en Henegouwen P.M.;
"Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates
via a UIM-UBL interaction.";
J. Cell Sci. 118:4437-4450(2005).
[13]
INTERACTION WITH ERBB2.
PubMed=16314522; DOI=10.1128/MCB.25.24.11005-11018.2005;
Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G.,
Wang S.C., Hung M.C.;
"Endosomal transport of ErbB-2: mechanism for nuclear entry of the
cell surface receptor.";
Mol. Cell. Biol. 25:11005-11018(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[16]
FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION
(ISOFORM 2), AND INTERACTION WITH HSG AND AP2A2.
PubMed=18362181; DOI=10.1083/jcb.200708115;
Roxrud I., Raiborg C., Pedersen N.M., Stang E., Stenmark H.;
"An endosomally localized isoform of Eps15 interacts with Hrs to
mediate degradation of epidermal growth factor receptor.";
J. Cell Biol. 180:1205-1218(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796 AND SER-814, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[18]
INTERACTION WITH UBQLN1 AND UBQLN2.
PubMed=18199683; DOI=10.1091/mbc.E07-08-0775;
N'Diaye E.N., Hanyaloglu A.C., Kajihara K.K., Puthenveedu M.A., Wu P.,
von Zastrow M., Brown E.J.;
"The ubiquitin-like protein PLIC-2 is a negative regulator of G
protein-coupled receptor endocytosis.";
Mol. Biol. Cell 19:1252-1260(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-323; SER-485
AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
FUNCTION.
PubMed=19458185; DOI=10.1091/mbc.E09-03-0256;
Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G.,
Schmid S.L.;
"Endocytic accessory proteins are functionally distinguished by their
differential effects on the maturation of clathrin-coated pits.";
Mol. Biol. Cell 20:3251-3260(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324;
SER-814 AND TYR-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-467; SER-470;
SER-790; SER-796 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
INTERACTION WITH FCHO2.
PubMed=20448150; DOI=10.1126/science.1188462;
Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y.,
Mittal R., McMahon H.T.;
"FCHo proteins are nucleators of clathrin-mediated endocytosis.";
Science 328:1281-1284(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
INTERACTION WITH FCHO2.
PubMed=21762413; DOI=10.1111/j.1365-2443.2011.01536.x;
Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.;
"Characterization of the EFC/F-BAR domain protein, FCHO2.";
Genes Cells 16:868-878(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-485; SER-790;
SER-796 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
FUNCTION, AND INTERACTION WITH DAB2.
PubMed=22648170; DOI=10.1091/mbc.E11-12-1007;
Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
"The clathrin adaptor Dab2 recruits EH domain scaffold proteins to
regulate integrin beta1 endocytosis.";
Mol. Biol. Cell 23:2905-2916(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[31]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-746; THR-777;
SER-790; SER-796 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; THR-777; SER-796
AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
INTERACTION WITH CORO7.
PubMed=24768539; DOI=10.1016/j.molcel.2014.03.035;
Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C.,
Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.;
"K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin
E3 ligase regulates protein trafficking.";
Mol. Cell 54:586-600(2014).
[36]
INTERACTION WITH VACCINIA VIRUS PROTEIN A36.
PubMed=27670116; DOI=10.1038/nmicrobiol.2016.141;
Snetkov X., Weisswange I., Pfanzelter J., Humphries A.C., Way M.;
"NPF motifs in the vaccinia virus protein A36 recruit intersectin-1 to
promote Cdc42:N-WASP-mediated viral release from infected cells.";
Nat. Microbiol. 1:16141-16141(2016).
[37]
STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH CALCIUM IONS.
PubMed=9721102; DOI=10.1126/science.281.5381.1357;
de Beer T., Carter R.E., Lobel-Rice K.E., Sorkin A., Overduin M.;
"Structure and Asn-Pro-Phe binding pocket of the Eps15 homology
domain.";
Science 281:1357-1360(1998).
[38]
STRUCTURE BY NMR OF 217-311 IN COMPLEX WITH CALCIUM IONS.
PubMed=10757979; DOI=10.1021/bi9927383;
Enmon J.L., de Beer T., Overduin M.;
"Solution structure of Eps15's third EH domain reveals coincident Phe-
Trp and Asn-Pro-Phe binding sites.";
Biochemistry 39:4309-4319(2000).
[39]
STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH PEPTIDE LIGAND AND CALCIUM
IONS, AND DOMAIN.
PubMed=11062555; DOI=10.1038/80924;
de Beer T., Hoofnagle A.N., Enmon J.L., Bowers R.C., Yamabhai M.,
Kay B.K., Overduin M.;
"Molecular mechanism of NPF recognition by EH domains.";
Nat. Struct. Biol. 7:1018-1022(2000).
[40]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 719-730 IN COMPLEX WITH
AP2B1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
Mills I.G., Benmerah A., McMahon H.T.;
"Role of the AP2 beta-appendage hub in recruiting partners for
clathrin-coated vesicle assembly.";
PLoS Biol. 4:E262-E262(2006).
[41]
STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH STON2 AND CALCIUM IONS,
MUTAGENESIS OF VAL-154 AND TRP-169, AND SUBCELLULAR LOCATION.
PubMed=18200045; DOI=10.1038/sj.emboj.7601980;
Rumpf J., Simon B., Jung N., Maritzen T., Haucke V., Sattler M.,
Groemping Y.;
"Structure of the Eps15-stonin2 complex provides a molecular
explanation for EH-domain ligand specificity.";
EMBO J. 27:558-569(2008).
[42]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 645-654, AND INTERACTION
WITH SGIP1.
PubMed=26822536; DOI=10.1038/srep19565;
Shimada A., Yamaguchi A., Kohda D.;
"Structural basis for the recognition of two consecutive mutually
interacting DPF motifs by the SGIP1 mu homology domain.";
Sci. Rep. 6:19565-19565(2016).
-!- FUNCTION: Involved in cell growth regulation. May be involved in
the regulation of mitogenic signals and control of cell
proliferation. Involved in the internalization of ligand-inducible
receptors of the receptor tyrosine kinase (RTK) type, in
particular EGFR. Plays a role in the assembly of clathrin-coated
pits (CCPs). Acts as a clathrin adapter required for post-Golgi
trafficking. Seems to be involved in CCPs maturation including
invagination or budding. Involved in endocytosis of integrin beta-
1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1
as DAB2-dependent cargo but not TFR seems to require association
with DAB2. {ECO:0000269|PubMed:16903783,
ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185,
ECO:0000269|PubMed:22648170}.
-!- SUBUNIT: Interacts with SGIP1 (PubMed:26822536). Interacts with
HGS; the interaction bridges the interaction of STAM or STAM2 with
EPS15. Isoform 2 interacts with HGS and AP2A2. Part of a complex
at least composed of EPS15, HGS, and either STAM or STAM2. Binds
AP2A2. Interacts with AP2B1; clathrin competes with EPS15. Binds
STON2 and EPN1. Interacts (via its SH3-binding sites) with CRK.
Interacts with SH3BP4/TTP. Interacts with ERBB2. Interacts with
FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2.
Interacts (via UIM repeats) with CORO7 (when ubiquitinated at
'Lys-472'). Interacts (via UIM domains) with UBQLN1 (via
ubiquitin-like domain) and can interact with both the
ubiquitinated and the non-ubiquitinated forms of UBQLN1. Interacts
with UBQLN2 (By similarity) (PubMed:10757979, PubMed:11062555,
PubMed:12551915, PubMed:16159959, PubMed:16314522,
PubMed:16325581, PubMed:16903783, PubMed:18199683,
PubMed:18200045, PubMed:18362181, PubMed:20448150,
PubMed:21762413, PubMed:22484487, PubMed:22648170,
PubMed:24768539, PubMed:8662907, PubMed:9721102, PubMed:9723620).
Interacts with vaccinia virus protein A36 (PubMed:27670116).
{ECO:0000250|UniProtKB:P42567, ECO:0000269|PubMed:10757979,
ECO:0000269|PubMed:11062555, ECO:0000269|PubMed:12551915,
ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:16314522,
ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:16903783,
ECO:0000269|PubMed:18199683, ECO:0000269|PubMed:18200045,
ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:20448150,
ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22484487,
ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:24768539,
ECO:0000269|PubMed:26822536, ECO:0000269|PubMed:27670116,
ECO:0000269|PubMed:8662907, ECO:0000269|PubMed:9721102,
ECO:0000269|PubMed:9723620}.
-!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus
protein A36 (PubMed:27670116). {ECO:0000269|PubMed:27670116}.
-!- INTERACTION:
Q0JRZ9:FCHO2; NbExp=3; IntAct=EBI-396684, EBI-2609756;
Q3UQN2:Fcho2 (xeno); NbExp=3; IntAct=EBI-396684, EBI-6094986;
Q15811:ITSN1; NbExp=2; IntAct=EBI-396684, EBI-602041;
P16333:NCK1; NbExp=2; IntAct=EBI-396684, EBI-389883;
Q9QZS3-1:Numb (xeno); NbExp=3; IntAct=EBI-396684, EBI-9547433;
Q9QZS3-2:Numb (xeno); NbExp=3; IntAct=EBI-396684, EBI-3896014;
Q8WXE9:STON2; NbExp=17; IntAct=EBI-396684, EBI-539742;
Q9UMX0:UBQLN1; NbExp=5; IntAct=EBI-396684, EBI-741480;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit.
Note=Recruited to the plasma membrane upon EGFR activation and
localizes to coated pits. Colocalizes with UBQLN1 in ubiquitin-
rich cytoplasmic aggregates that are not endocytic compartments
and in cytoplasmic juxtanuclear structures called aggresomes.
{ECO:0000269|PubMed:16159959}.
-!- SUBCELLULAR LOCATION: Isoform 2: Early endosome membrane
{ECO:0000269|PubMed:18362181}; Peripheral membrane protein
{ECO:0000269|PubMed:18362181}; Cytoplasmic side
{ECO:0000269|PubMed:18362181}. Note=Colocalizes with HGS on
bilayered clathrin coats on endosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P42566-1; Sequence=Displayed;
Name=2; Synonyms=Eps15b;
IsoId=P42566-2; Sequence=VSP_036168, VSP_036169;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
target proteins. {ECO:0000269|PubMed:11062555}.
-!- DOMAIN: The UIM (ubiquitin-interacting motif) repeats specifically
bind 'Lys-33'-linked ubiquitin. {ECO:0000269|PubMed:11062555,
ECO:0000269|PubMed:24768539}.
-!- PTM: Phosphorylation on Tyr-849 is involved in the internalization
of EGFR. Not required for membrane translocation after EGF
treatment or for targeting to coated pits, but essential for a
subsequent step in EGFR endocytosis (By similarity).
Phosphorylated on serine upon DNA damage, probably by ATM or ATR.
{ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P42567}.
-!- DISEASE: Note=A chromosomal aberration involving EPS15 is found in
acute leukemias. Translocation t(1;11)(p32;q23) with KMT2A/MLL1.
The result is a rogue activator protein.
-!- CAUTION: Studies in clathrin-mediated endocytosis of ITGB1 and TFR
used a siRNA mixture of EPS15 and EPS15L1, and a Dab2 mutant with
impaired binding to EH domain-containing proteins EPS15 and ITSN1
suggesting a partially overlapping role of the EH domain-
containing proteins. {ECO:0000305|PubMed:22648170}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF1pID11.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U07707; AAA52101.1; -; mRNA.
EMBL; Z29064; CAA82305.1; -; mRNA.
EMBL; AK313396; BAG36194.1; -; mRNA.
EMBL; DQ367924; ABD34786.1; -; mRNA.
EMBL; BX647676; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL671986; CAI13030.1; -; Genomic_DNA.
EMBL; AC104170; CAI13030.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX06823.1; -; Genomic_DNA.
CCDS; CCDS557.1; -. [P42566-1]
PIR; S43074; S43074.
RefSeq; NP_001153441.1; NM_001159969.1. [P42566-2]
RefSeq; NP_001972.1; NM_001981.2. [P42566-1]
UniGene; Hs.83722; -.
PDB; 1C07; NMR; -; A=217-311.
PDB; 1EH2; NMR; -; A=121-218.
PDB; 1F8H; NMR; -; A=121-215.
PDB; 1FF1; NMR; -; A=121-215.
PDB; 2IV9; X-ray; 1.90 A; P=723-730.
PDB; 2JXC; NMR; -; A=121-215.
PDB; 4RH5; X-ray; 1.60 A; B=846-854.
PDB; 4RH9; X-ray; 1.60 A; B=846-854.
PDB; 4RHG; X-ray; 1.58 A; B=846-854.
PDB; 4S0G; X-ray; 1.72 A; B=846-854.
PDB; 5AWT; X-ray; 2.70 A; B=640-649.
PDB; 5AWU; X-ray; 2.70 A; B=645-654.
PDB; 5JP2; X-ray; 2.40 A; E/F=615-637.
PDBsum; 1C07; -.
PDBsum; 1EH2; -.
PDBsum; 1F8H; -.
PDBsum; 1FF1; -.
PDBsum; 2IV9; -.
PDBsum; 2JXC; -.
PDBsum; 4RH5; -.
PDBsum; 4RH9; -.
PDBsum; 4RHG; -.
PDBsum; 4S0G; -.
PDBsum; 5AWT; -.
PDBsum; 5AWU; -.
PDBsum; 5JP2; -.
ProteinModelPortal; P42566; -.
SMR; P42566; -.
BioGrid; 108374; 160.
DIP; DIP-33064N; -.
ELM; P42566; -.
IntAct; P42566; 73.
MINT; MINT-107223; -.
STRING; 9606.ENSP00000360798; -.
iPTMnet; P42566; -.
PhosphoSitePlus; P42566; -.
BioMuta; EPS15; -.
DMDM; 67476728; -.
OGP; P42566; -.
EPD; P42566; -.
MaxQB; P42566; -.
PaxDb; P42566; -.
PeptideAtlas; P42566; -.
PRIDE; P42566; -.
Ensembl; ENST00000371733; ENSP00000360798; ENSG00000085832. [P42566-1]
GeneID; 2060; -.
KEGG; hsa:2060; -.
UCSC; uc001csq.2; human. [P42566-1]
CTD; 2060; -.
DisGeNET; 2060; -.
GeneCards; EPS15; -.
HGNC; HGNC:3419; EPS15.
HPA; CAB010164; -.
HPA; HPA008451; -.
MIM; 600051; gene.
neXtProt; NX_P42566; -.
OpenTargets; ENSG00000085832; -.
PharmGKB; PA27838; -.
eggNOG; KOG0998; Eukaryota.
eggNOG; ENOG410XTDR; LUCA.
GeneTree; ENSGT00760000118985; -.
HOGENOM; HOG000004804; -.
HOVERGEN; HBG005591; -.
InParanoid; P42566; -.
KO; K12472; -.
OMA; YYRQVDT; -.
OrthoDB; EOG091G01RG; -.
PhylomeDB; P42566; -.
TreeFam; TF324293; -.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
SignaLink; P42566; -.
SIGNOR; P42566; -.
ChiTaRS; EPS15; human.
EvolutionaryTrace; P42566; -.
GeneWiki; EPS15; -.
GenomeRNAi; 2060; -.
PRO; PR:P42566; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000085832; -.
CleanEx; HS_EPS15; -.
ExpressionAtlas; P42566; baseline and differential.
Genevisible; P42566; HS.
GO; GO:0016235; C:aggresome; IDA:UniProtKB.
GO; GO:0030122; C:AP-2 adaptor complex; IEA:Ensembl.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
GO; GO:0032456; P:endocytic recycling; IC:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:ProtInc.
GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IMP:CACAO.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0016050; P:vesicle organization; TAS:UniProtKB.
GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000261; EH_dom.
InterPro; IPR003903; UIM_dom.
Pfam; PF12763; EF-hand_4; 3.
SMART; SM00054; EFh; 3.
SMART; SM00027; EH; 3.
SMART; SM00726; UIM; 3.
SUPFAM; SSF47473; SSF47473; 3.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 4.
PROSITE; PS50031; EH; 3.
PROSITE; PS50330; UIM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calcium;
Cell membrane; Chromosomal rearrangement; Coated pit;
Complete proteome; Cytoplasm; Endocytosis; Endosome;
Host-virus interaction; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Protein transport; Proto-oncogene; Reference proteome;
Repeat; SH3-binding; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 896 Epidermal growth factor receptor
substrate 15.
/FTId=PRO_0000146116.
DOMAIN 15 104 EH 1. {ECO:0000255|PROSITE-
ProRule:PRU00077}.
DOMAIN 128 216 EH 2. {ECO:0000255|PROSITE-
ProRule:PRU00077}.
DOMAIN 160 195 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 223 258 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 224 314 EH 3. {ECO:0000255|PROSITE-
ProRule:PRU00077}.
REPEAT 599 601 1.
REPEAT 623 625 2.
REPEAT 629 631 3.
REPEAT 634 636 4.
REPEAT 640 642 5.
REPEAT 645 647 6.
REPEAT 651 653 7.
REPEAT 664 666 8.
REPEAT 672 674 9.
REPEAT 692 694 10.
REPEAT 709 711 11.
REPEAT 737 739 12.
REPEAT 798 800 13.
REPEAT 804 806 14.
REPEAT 825 827 15.
DOMAIN 851 870 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 877 896 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
CA_BIND 173 184 1.
CA_BIND 236 247 2.
REGION 2 330 Interaction with DAB2. {ECO:0000250}.
REGION 599 827 15 X 3 AA repeats of D-P-F.
MOTIF 768 774 SH3-binding.
COMPBIAS 768 850 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000250|UniProtKB:P42567}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000250|UniProtKB:P42567}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 777 777 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 779 779 Phosphothreonine.
{ECO:0000250|UniProtKB:P42567}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 796 796 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 814 814 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 849 849 Phosphotyrosine; by EGFR.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 314 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_036168.
VAR_SEQ 315 346 SLQKNIIGSSPVADFSAIKELDTLNNEIVDLQ -> MYLKS
DSGLGGWITIPAVADVLKYSCIVCWSS (in isoform
2). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_036169.
VARIANT 822 822 I -> M (in dbSNP:rs17567).
{ECO:0000269|PubMed:8183552}.
/FTId=VAR_016142.
MUTAGEN 154 154 V->E: Loss of interaction with STON2 NPF
motifs. {ECO:0000269|PubMed:18200045}.
MUTAGEN 169 169 W->A: Loss of interaction with STON2 NPF
motifs. {ECO:0000269|PubMed:18200045}.
CONFLICT 446 446 Missing (in Ref. 5; BX647676).
{ECO:0000305}.
HELIX 126 136 {ECO:0000244|PDB:1EH2}.
STRAND 142 144 {ECO:0000244|PDB:1EH2}.
STRAND 145 147 {ECO:0000244|PDB:2JXC}.
HELIX 148 156 {ECO:0000244|PDB:1EH2}.
TURN 157 159 {ECO:0000244|PDB:1EH2}.
HELIX 162 172 {ECO:0000244|PDB:1EH2}.
STRAND 177 179 {ECO:0000244|PDB:1EH2}.
HELIX 182 197 {ECO:0000244|PDB:1EH2}.
TURN 207 209 {ECO:0000244|PDB:1EH2}.
HELIX 212 214 {ECO:0000244|PDB:1F8H}.
HELIX 223 235 {ECO:0000244|PDB:1C07}.
STRAND 240 243 {ECO:0000244|PDB:1C07}.
HELIX 245 253 {ECO:0000244|PDB:1C07}.
TURN 254 256 {ECO:0000244|PDB:1C07}.
HELIX 259 269 {ECO:0000244|PDB:1C07}.
STRAND 274 278 {ECO:0000244|PDB:1C07}.
TURN 279 281 {ECO:0000244|PDB:1C07}.
HELIX 282 293 {ECO:0000244|PDB:1C07}.
TURN 305 307 {ECO:0000244|PDB:1C07}.
TURN 624 627 {ECO:0000244|PDB:5JP2}.
TURN 630 633 {ECO:0000244|PDB:5JP2}.
HELIX 723 726 {ECO:0000244|PDB:2IV9}.
SEQUENCE 896 AA; 98656 MW; A1B9FE15B47ABAFF CRC64;
MAAAAQLSLT QLSSGNPVYE KYYRQVDTGN TGRVLASDAA AFLKKSGLPD LILGKIWDLA
DTDGKGILNK QEFFVALRLV ACAQNGLEVS LSSLNLAVPP PRFHDTSSPL LISGTSAAEL
PWAVKPEDKA KYDAIFDSLS PVNGFLSGDK VKPVLLNSKL PVDILGRVWE LSDIDHDGML
DRDEFAVAMF LVYCALEKEP VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD
GFVSGLEVRE IFLKTGLPST LLAHIWSLCD TKDCGKLSKD QFALAFHLIS QKLIKGIDPP
HVLTPEMIPP SDRASLQKNI IGSSPVADFS AIKELDTLNN EIVDLQREKN NVEQDLKEKE
DTIKQRTSEV QDLQDEVQRE NTNLQKLQAQ KQQVQELLDE LDEQKAQLEE QLKEVRKKCA
EEAQLISSLK AELTSQESQI STYEEELAKA REELSRLQQE TAELEESVES GKAQLEPLQQ
HLQDSQQEIS SMQMKLMEMK DLENHNSQLN WCSSPHSILV NGATDYCSLS TSSSETANLN
EHVEGQSNLE SEPIHQESPA RSSPELLPSG VTDENEVTTA VTEKVCSELD NNRHSKEEDP
FNVDSSSLTG PVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS DPFASDCFFR
QSTDPFATSS TDPFSAANNS SITSVETLKH NDPFAPGGTV VAASDSATDP FASVFGNESF
GGGFADFSTL SKVNNEDPFR SATSSSVSNV VITKNVFEET SVKSEDEPPA LPPKIGTPTR
PCPLPPGKRS INKLDSPDPF KLNDPFQPFP GNDSPKEKDP EIFCDPFTSA TTTTNKEADP
SNFANFSAYP SEEDMIEWAK RESEREEEQR LARLNQQEQE DLELAIALSK SEISEA


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EIAAB13299 Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,Eps8l1,EPS8-like protein 1,Eps8r1,EPS8-related protein 1,Mouse
EIAAB13298 DRC3,Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,EPS8L1,EPS8-like protein 1,EPS8R1,EPS8-related protein 1,
CSB-EL007748MO Mouse Epidermal growth factor receptor substrate 15(EPS15) ELISA kit 96T
CSB-EL007748HU Human Epidermal growth factor receptor substrate 15(EPS15) ELISA kit 96T
EPS8 EPS15 Gene epidermal growth factor receptor pathway substrate 15
CSB-EL007748HU Human Epidermal growth factor receptor substrate 15(EPS15) ELISA kit SpeciesHuman 96T
CSB-EL007748MO Mouse Epidermal growth factor receptor substrate 15(EPS15) ELISA kit SpeciesMouse 96T
EPS15_MOUSE ELISA Kit FOR Epidermal growth factor receptor substrate 15; organism: Mouse; gene name: Eps15 96T
CSB-EL007748HU Human epidermal growth factor receptor pathway substrate 15 (EPS15) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007748MO Mouse epidermal growth factor receptor pathway substrate 15 (EPS15) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007752MO Mouse Epidermal growth factor receptor kinase substrate 8-like protein 1(EPS8L1) ELISA kit 96T
CSB-EL007754MO Mouse Epidermal growth factor receptor kinase substrate 8-like protein 3(EPS8L3) ELISA kit 96T
CSB-EL007754HU Human Epidermal growth factor receptor kinase substrate 8-like protein 3(EPS8L3) ELISA kit 96T
CSB-EL007753HU Human Epidermal growth factor receptor kinase substrate 8-like protein 2(EPS8L2) ELISA kit 96T
CSB-EL007752HU Human Epidermal growth factor receptor kinase substrate 8-like protein 1(EPS8L1) ELISA kit 96T


 

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