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-like 1  

UniProtKB / Swiss-Prot ID :  EP15R_HUMAN

Gene Name (Synonyms) : 
EPS15L1, EPS15R  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Peripheral membrane protein (By similarity). Nucleus (By similarity). Membrane, coated pit (By similarity). Note=Localized to plasma membrane coated pits (By similarity). 

Protein Function :  Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. 

Protein Sequence MAAPLIPLSQQIPTGNSLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDK...
Predicted Secondary Structure CCCHHHHHHCCCCCCCHHHHHHHHHCCCCCCCCCCHHHHHHHHHHCCCCHHHHHHHHHHHCCCCCCCCCH...
Protein Variant -
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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
Predicted PTM Sites
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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
2N-acetylalanine.---MAAPLI
---CCCHHH
20.14UniProtKB
Link-
49PhosphoserineKSGLSDIIL
HCCCCHHHH
30.23HPRD
Link-
106PhosphothreonineKFHDTSSPL
CCCCCCCCC
23.64HPRD
Link-
107PhosphoserineFHDTSSPLM
CCCCCCCCC
35.70HPRD
Link-
108PhosphoserineHDTSSPLMV
CCCCCCCCC
24.93HPRD
Link-
108PhosphoserineHDTSSPLMV
CCCCCCCCC
24.93PhosphoELM
Link-
108Phosphoserine.HDTSSPLMV
CCCCCCCCC
24.93UniProtKB
Link-
229PhosphoserineVLPASPPPK
CCCCCCCCC
35.68HPRD
Link-
229PhosphoserineVLPASPPPK
CCCCCCCCC
35.68PhosphoELM
Link-
229PhosphoserineVLPASPPPK
CCCCCCCCC
35.68SysPTM
Link-
229Phosphoserine.VLPASPPPK
CCCCCCCCC
35.68UniProtKB
Link-
238PhosphoserineDSLRSTPSH
CCCCCCCCC
50.38HPRD
Link-
238PhosphoserineDSLRSTPSH
CCCCCCCCC
50.38PhosphoELM
Link-
238PhosphoserineDSLRSTPSH
CCCCCCCCC
50.38SysPTM
Link-
238Phosphoserine.DSLRSTPSH
CCCCCCCCC
50.38UniProtKB
Link-
239PhosphothreonineSLRSTPSHG
CCCCCCCCC
23.52HPRD
Link-
239PhosphothreonineSLRSTPSHG
CCCCCCCCC
23.52PhosphoELM
Link-
241PhosphoserineRSTPSHGSV
CCCCCCCCH
40.34HPRD
Link-
241PhosphoserineRSTPSHGSV
CCCCCCCCH
40.34PhosphoELM
Link-
241Phosphoserine.RSTPSHGSV
CCCCCCCCH
40.34UniProtKB
Link-
244PhosphoserinePSHGSVSSL
CCCCCHHHH
17.25HPRD
Link-
244PhosphoserinePSHGSVSSL
CCCCCHHHH
17.25PhosphoELM
Link-
244Phosphoserine.PSHGSVSSL
CCCCCHHHH
17.25UniProtKB
Link-
247PhosphoserineGSVSSLNST
CCHHHHHHH
29.43HPRD
Link-
251PhosphothreonineSLNSTGSLS
HHHHHHCCC
29.71HPRD
Link-
251PhosphothreonineSLNSTGSLS
HHHHHHCCC
29.71SysPTM
Link-
253PhosphoserineNSTGSLSPK
HHHHCCCCC
26.26HPRD
Link-
253PhosphoserineNSTGSLSPK
HHHHCCCCC
26.26PhosphoELM
Link-
255PhosphoserineTGSLSPKHS
HHCCCCCCC
33.33HPRD
Link-
255PhosphoserineTGSLSPKHS
HHCCCCCCC
33.33PhosphoELM
Link-
255PhosphoserineTGSLSPKHS
HHCCCCCCC
33.33SysPTM
Link-
255Phosphoserine.TGSLSPKHS
HHCCCCCCC
33.33UniProtKB
Link-
366PhosphothreonineSERGTPGPD
HHHCCCCCC
31.15HPRD
Link-
366Phosphothreonine.SERGTPGPD
HHHCCCCCC
31.15UniProtKB
Link-
371PhosphoserinePGPDSSGSL
CCCCCCCCC
39.47HPRD
Link-
371Phosphoserine.PGPDSSGSL
CCCCCCCCC
39.47UniProtKB
Link-
374PhosphoserineDSSGSLGSG
CCCCCCCCH
31.35HPRD
Link-
374Phosphoserine.DSSGSLGSG
CCCCCCCCH
31.35UniProtKB
Link-
377PhosphoserineGSLGSGEFT
CCCCCHHHH
40.20HPRD
Link-
528PhosphothreonineVQLETIIKS
HHHHHHHHH
36.27HPRD
Link-
560Phosphoserine.EAHRSLEQY
HHHHHHHHH
26.79UniProtKB
Link-
577Phosphothreonine.GASLTDLAN
CCCCCHHHH
26.86UniProtKB
Link-
593PhosphoserineAERGSFGAM
CCCCCCCCC
27.08HPRD
Link-
708PhosphoserinePFESSDPFS
CCCCCCCCC
41.95HPRD
Link-
708PhosphoserinePFESSDPFS
CCCCCCCCC
41.95PhosphoELM
Link-
793PhosphoserinePKPPSGKST
CCCCCCCCC
68.34HPRD
Link-
793PhosphoserinePKPPSGKST
CCCCCCCCC
68.34PhosphoELM
Link-
793PhosphoserinePKPPSGKST
CCCCCCCCC
68.34SysPTM
Link-
793Phosphoserine.PKPPSGKST
CCCCCCCCC
68.34UniProtKB
Link-
797Phosphothreonine.SGKSTPVSQ
CCCCCCCCC
31.06UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NUPL_HUMANin vivo
yeast 2-hybrid
HPRD:09445HPRD10613896
EPN1_HUMANin vitroHPRD:09445HPRD9723620
HRBL_HUMANENSP00000248070STRING
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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
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-229; SER-238 AND SER-255, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366; SER-371 ANDSER-374, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"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-255, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-229; SER-238 AND SER-255, 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-244; SER-255; SER-560;THR-577 AND THR-797, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-244 ANDSER-255, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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-108 AND SER-793, ANDMASS SPECTROMETRY.
"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-229, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures