Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Epidermal growth factor receptor substrate 15  

UniProtKB / Swiss-Prot ID :  EPS15_HUMAN

Gene Name (Synonyms) : 
EPS15, AF1P  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the plasma membrane upon EGFR activation and localizes to coated pits. Isoform 2: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Colo 

Protein 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 (By similarity). 

Protein Sequence MAAAAQLSLTQLSSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNK...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
822I -> M (in dbSNP:rs17567). VAR_016142
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
107PhosphoserineFHDTSSPLL
35.70HPRD
Link-
107PhosphoserineFHDTSSPLL
35.70Phosphositeplus
Link-
108PhosphoserineHDTSSPLLI
22.97HPRD
Link-
108PhosphoserineHDTSSPLLI
22.97Phosphositeplus
Link-
108Phosphoserine.HDTSSPLLI
22.97UniProtKB
Link-
116PhosphoserineISGTSAAEL
29.07HPRD
Link-
140PhosphoserineFDSLSPVNG
30.65HPRD
Link-
140PhosphoserineFDSLSPVNG
30.65PhosphoELM
Link-
140PhosphoserineFDSLSPVNG
30.65Phosphositeplus
Link-
140PhosphoserineFDSLSPVNG
30.65SysPTM
Link-
140Phosphoserine.FDSLSPVNG
30.65UniProtKB
Link-
323PhosphoserineNIIGSSPVA
22.51HPRD
Link-
323PhosphoserineNIIGSSPVA
22.51PhosphoELM
Link-
323PhosphoserineNIIGSSPVA
22.51Phosphositeplus
Link-
323PhosphoserineNIIGSSPVA
22.51SysPTM
Link-
323Phosphoserine.NIIGSSPVA
22.51UniProtKB
Link-
324PhosphoserineIIGSSPVAD
20.41HPRD
Link-
324PhosphoserineIIGSSPVAD
20.41PhosphoELM
Link-
324PhosphoserineIIGSSPVAD
20.41Phosphositeplus
Link-
324PhosphoserineIIGSSPVAD
20.41SysPTM
Link-
324Phosphoserine.IIGSSPVAD
20.41UniProtKB
Link-
413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEQLKEVRK
54.58Phosphositeplus
Link-
443PhosphotyrosineQISTYEEEL
17.98Phosphositeplus
Link-
467PhosphoserineELEESVESG
23.08HPRD
Link-
467PhosphoserineELEESVESG
23.08Phosphositeplus
Link-
470PhosphoserineESVESGKAQ
43.36HPRD
Link-
470PhosphoserineESVESGKAQ
43.36Phosphositeplus
Link-
485PhosphoserineHLQDSQQEI
22.32HPRD
Link-
485PhosphoserineHLQDSQQEI
22.32PhosphoELM
Link-
485PhosphoserineHLQDSQQEI
22.32Phosphositeplus
Link-
485PhosphoserineHLQDSQQEI
22.32SysPTM
Link-
485Phosphoserine.HLQDSQQEI
22.32UniProtKB
Link-
495Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SMQMKLMEM
27.99Phosphositeplus
Link-
562PhosphoserineSPARSSPEL
52.96HPRD
Link-
562PhosphoserineSPARSSPEL
52.96PhosphoELM
Link-
562PhosphoserineSPARSSPEL
52.96Phosphositeplus
Link-
563PhosphoserinePARSSPELL
19.48PhosphoELM
Link-
563PhosphoserinePARSSPELL
19.48Phosphositeplus
Link-
595PhosphoserineNNRHSKEED
38.23HPRD
Link-
595PhosphoserineNNRHSKEED
38.23PhosphoELM
Link-
638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DPFGKIDPF
44.29Phosphositeplus
Link-
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVITKNVFE
39.73Phosphositeplus
Link-
763Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETSVKSEDE
48.14Phosphositeplus
Link-
777PhosphothreoninePKIGTPTRP
25.59HPRD
Link-
777PhosphothreoninePKIGTPTRP
25.59PhosphoELM
Link-
777PhosphothreoninePKIGTPTRP
25.59Phosphositeplus
Link-
777PhosphothreoninePKIGTPTRP
25.59SysPTM
Link-
777Phosphothreonine.PKIGTPTRP
25.59UniProtKB
Link-
788Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPPGKRSIN
49.06Phosphositeplus
Link-
790PhosphoserinePGKRSINKL
33.72HPRD
Link-
790PhosphoserinePGKRSINKL
33.72Phosphositeplus
Link-
793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RSINKLDSP
52.59Phosphositeplus
Link-
796PhosphoserineNKLDSPDPF
41.46HPRD
Link-
796PhosphoserineNKLDSPDPF
41.46PhosphoELM
Link-
796PhosphoserineNKLDSPDPF
41.46Phosphositeplus
Link-
796PhosphoserineNKLDSPDPF
41.46SysPTM
Link-
796Phosphoserine.NKLDSPDPF
41.46UniProtKB
Link-
801Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PDPFKLNDP
52.33Phosphositeplus
Link-
814PhosphoserinePGNDSPKEK
41.70HPRD
Link-
814PhosphoserinePGNDSPKEK
41.70PhosphoELM
Link-
814PhosphoserinePGNDSPKEK
41.70Phosphositeplus
Link-
814PhosphoserinePGNDSPKEK
41.70SysPTM
Link-
814Phosphoserine.PGNDSPKEK
41.70UniProtKB
Link-
816Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NDSPKEKDP
79.80Phosphositeplus
Link-
818Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SPKEKDPEI
82.05Phosphositeplus
Link-
849PhosphotyrosineNFSAYPSEE
13.19PhosphoELM
Link-
849PhosphotyrosineNFSAYPSEE
13.19Phosphositeplus
Link-
849Phosphotyrosine (EGFR)NFSAYPSEE
13.19HPRD
Link-
849Phosphotyrosine; by EGFR.NFSAYPSEE
13.19UniProtKB
Link-
860Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IEWAKRESE
58.74Phosphositeplus
Link-
890Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IALSKSEIS
53.62Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
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.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; THR-777; SER-796AND SER-814, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-814, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-323; SER-485AND SER-814, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324;SER-814 AND TYR-849, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures