EPS15_MOUSE - dbPTM
EPS15_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPS15_MOUSE
UniProt AC P42567
Protein Name Epidermal growth factor receptor substrate 15
Gene Name Eps15
Organism Mus musculus (Mouse).
Sequence Length 897
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Membrane, clathrin-coated pit. Recruited to the plasma membrane upon EGFR activation and localizes to coated pits. Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregat
Protein Description 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..
Protein Sequence MAAAAQLSLTQLSSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLVACAQNGLEVSLSSLSLAVPPPRFHDSSSPLLTSGPSVAELPWAVKSEDKAKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFHLINQKLIKGIDPPHSLTPEMIPPSDRSSLQKNITGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTHQESSVRSSPEIAPSDVTDESEAVTVAGNEKVTPRFDDDKHSKEEDPFNVESSSLTDAVADTNLDFFQSDPFVGSDPFKDDPFGKIDPFGGDPFKGSDPFASDCFFKQTSTDPFTTSSTDPFSASSNSSNTSVETWKHNDPFAPGGTVVAAASDSATDPFASVFGNESFGDGFADFSTLSKVNNEDAFNPTISSSTSSVTIAKPMLEETASKSEDVPPALPPKVGTPTRPCPPPPGKRPINKLDSSDPLKLNDPFQPFPGNDSPKEKDPDMFCDPFTSSTTTNKEADPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAAAQLSL
------CCHHHHHHH
13.05-
8PhosphorylationMAAAAQLSLTQLSSG
CCHHHHHHHHHHHCC
19.7930352176
10PhosphorylationAAAQLSLTQLSSGNP
HHHHHHHHHHHCCCC
24.8828066266
13PhosphorylationQLSLTQLSSGNPVYE
HHHHHHHHCCCCHHH
26.7825293948
14PhosphorylationLSLTQLSSGNPVYEK
HHHHHHHCCCCHHHH
51.7025293948
19PhosphorylationLSSGNPVYEKYYRQV
HHCCCCHHHHHHHHH
14.1425293948
106PhosphorylationPPPRFHDSSSPLLTS
CCCCCCCCCCCCCCC
24.9324925903
107PhosphorylationPPRFHDSSSPLLTSG
CCCCCCCCCCCCCCC
41.8724925903
108PhosphorylationPRFHDSSSPLLTSGP
CCCCCCCCCCCCCCC
24.4224925903
112PhosphorylationDSSSPLLTSGPSVAE
CCCCCCCCCCCCHHH
39.0424925903
113PhosphorylationSSSPLLTSGPSVAEL
CCCCCCCCCCCHHHC
48.9924925903
116PhosphorylationPLLTSGPSVAELPWA
CCCCCCCCHHHCCCE
37.1724925903
138PhosphorylationKYDAIFDSLSPVDGF
HHHHHHHCCCCCCCC
21.7223984901
140PhosphorylationDAIFDSLSPVDGFLS
HHHHHCCCCCCCCCC
27.1626745281
221PhosphorylationKRKTWVVSPAEKAKY
CCCCEEECHHHHCCC
14.5825338131
227UbiquitinationVSPAEKAKYDEIFLK
ECHHHHCCCCEEEEE
65.3922790023
242PhosphorylationTDKDMDGYVSGLEVR
CCCCCCCCCCCHHHH
6.2817242355
244PhosphorylationKDMDGYVSGLEVRET
CCCCCCCCCHHHHHH
29.2226525534
321PhosphorylationSSLQKNITGSSPVAD
HHHHHHCCCCCCCCC
40.1724925903
323PhosphorylationLQKNITGSSPVADFS
HHHHCCCCCCCCCHH
23.8724925903
324PhosphorylationQKNITGSSPVADFSA
HHHCCCCCCCCCHHH
25.4124925903
330PhosphorylationSSPVADFSAIKELDT
CCCCCCHHHHHHHHH
29.6328833060
337PhosphorylationSAIKELDTLNNEIVD
HHHHHHHHHCHHHHH
43.9725367039
367PhosphorylationEDTVKQRTSEVQDLQ
HHHHHHHHHHHHHHH
27.0925338131
386UbiquitinationRESINLQKLQAQKQQ
HHHHHHHHHHHHHHH
45.8122790023
434PhosphorylationSSLKAEITSQESQIS
HHHHHHHHCCHHHHH
18.8330635358
435PhosphorylationSLKAEITSQESQISS
HHHHHHHCCHHHHHH
37.3030635358
438PhosphorylationAEITSQESQISSYEE
HHHHCCHHHHHHHHH
25.7730635358
441PhosphorylationTSQESQISSYEEELL
HCCHHHHHHHHHHHH
21.1630635358
442PhosphorylationSQESQISSYEEELLK
CCHHHHHHHHHHHHH
37.8930635358
443PhosphorylationQESQISSYEEELLKA
CHHHHHHHHHHHHHH
22.1430635358
449UbiquitinationSYEEELLKAREELSR
HHHHHHHHHHHHHHH
59.0122790023
467PhosphorylationETAQLEESVESGKAQ
HHHHHHHHHHHCHHH
23.08-
470PhosphorylationQLEESVESGKAQLEP
HHHHHHHHCHHHHHH
43.36-
472UbiquitinationEESVESGKAQLEPLQ
HHHHHHCHHHHHHHH
42.0922790023
485PhosphorylationLQQHLQESQQEISSM
HHHHHHHHHHHHHHH
24.97-
561PhosphorylationHQESSVRSSPEIAPS
CCCCCCCCCCCCCCC
48.3525521595
562PhosphorylationQESSVRSSPEIAPSD
CCCCCCCCCCCCCCC
18.9125521595
568PhosphorylationSSPEIAPSDVTDESE
CCCCCCCCCCCCCCC
35.3725619855
571PhosphorylationEIAPSDVTDESEAVT
CCCCCCCCCCCCCEE
38.7525619855
574PhosphorylationPSDVTDESEAVTVAG
CCCCCCCCCCEEECC
33.4025619855
578PhosphorylationTDESEAVTVAGNEKV
CCCCCCEEECCCCEE
16.2225619855
586PhosphorylationVAGNEKVTPRFDDDK
ECCCCEECCCCCCCC
21.5825619855
595PhosphorylationRFDDDKHSKEEDPFN
CCCCCCCCCCCCCCC
47.7223375375
605PhosphorylationEDPFNVESSSLTDAV
CCCCCCCCCHHHHHH
22.4223737553
606PhosphorylationDPFNVESSSLTDAVA
CCCCCCCCHHHHHHH
18.8323737553
607PhosphorylationPFNVESSSLTDAVAD
CCCCCCCHHHHHHHC
44.5623737553
609PhosphorylationNVESSSLTDAVADTN
CCCCCHHHHHHHCCC
24.7023737553
615PhosphorylationLTDAVADTNLDFFQS
HHHHHHCCCCCHHHC
28.1326643407
622PhosphorylationTNLDFFQSDPFVGSD
CCCCHHHCCCCCCCC
41.9426643407
638UbiquitinationFKDDPFGKIDPFGGD
CCCCCCCCCCCCCCC
44.2922790023
648UbiquitinationPFGGDPFKGSDPFAS
CCCCCCCCCCCCCCC
63.99-
655PhosphorylationKGSDPFASDCFFKQT
CCCCCCCCCCCEEEC
34.9828066266
662PhosphorylationSDCFFKQTSTDPFTT
CCCCEEECCCCCCCC
33.9025338131
664PhosphorylationCFFKQTSTDPFTTSS
CCEEECCCCCCCCCC
51.5925338131
670PhosphorylationSTDPFTTSSTDPFSA
CCCCCCCCCCCCCCC
28.3425338131
681PhosphorylationPFSASSNSSNTSVET
CCCCCCCCCCCCEEE
27.2425338131
700PhosphorylationDPFAPGGTVVAAASD
CCCCCCCEEEEEECC
20.0926643407
706PhosphorylationGTVVAAASDSATDPF
CEEEEEECCCCCCCC
27.6326643407
708PhosphorylationVVAAASDSATDPFAS
EEEEECCCCCCCCHH
30.4926643407
710PhosphorylationAAASDSATDPFASVF
EEECCCCCCCCHHHH
48.4326643407
715PhosphorylationSATDPFASVFGNESF
CCCCCCHHHHCCCCC
20.5426643407
721PhosphorylationASVFGNESFGDGFAD
HHHHCCCCCCCCCCC
38.2326643407
730PhosphorylationGDGFADFSTLSKVNN
CCCCCCHHHHHCCCC
29.0526643407
731PhosphorylationDGFADFSTLSKVNNE
CCCCCHHHHHCCCCH
34.7426643407
733PhosphorylationFADFSTLSKVNNEDA
CCCHHHHHCCCCHHH
34.3526643407
744PhosphorylationNEDAFNPTISSSTSS
CHHHCCCCCCCCCCC
34.3025293948
746PhosphorylationDAFNPTISSSTSSVT
HHCCCCCCCCCCCEE
22.2525293948
747PhosphorylationAFNPTISSSTSSVTI
HCCCCCCCCCCCEEE
33.5125293948
748PhosphorylationFNPTISSSTSSVTIA
CCCCCCCCCCCEEEE
26.0525293948
749PhosphorylationNPTISSSTSSVTIAK
CCCCCCCCCCEEEEH
27.2825293948
750PhosphorylationPTISSSTSSVTIAKP
CCCCCCCCCEEEEHH
25.4329472430
751PhosphorylationTISSSTSSVTIAKPM
CCCCCCCCEEEEHHH
24.3025293948
753PhosphorylationSSSTSSVTIAKPMLE
CCCCCCEEEEHHHHH
19.7125293948
762PhosphorylationAKPMLEETASKSEDV
EHHHHHHHHCCCCCC
27.1925293948
764PhosphorylationPMLEETASKSEDVPP
HHHHHHHCCCCCCCC
44.1030352176
766PhosphorylationLEETASKSEDVPPAL
HHHHHCCCCCCCCCC
36.2125338131
779PhosphorylationALPPKVGTPTRPCPP
CCCCCCCCCCCCCCC
25.1926824392
781PhosphorylationPPKVGTPTRPCPPPP
CCCCCCCCCCCCCCC
47.2628725479
795UbiquitinationPGKRPINKLDSSDPL
CCCCCCCCCCCCCCC
55.1622790023
798PhosphorylationRPINKLDSSDPLKLN
CCCCCCCCCCCCCCC
47.2626824392
799PhosphorylationPINKLDSSDPLKLND
CCCCCCCCCCCCCCC
42.8022942356
803UbiquitinationLDSSDPLKLNDPFQP
CCCCCCCCCCCCCCC
51.1122790023
816PhosphorylationQPFPGNDSPKEKDPD
CCCCCCCCCCCCCCC
41.7024925903
818UbiquitinationFPGNDSPKEKDPDMF
CCCCCCCCCCCCCCC
79.8022790023
820UbiquitinationGNDSPKEKDPDMFCD
CCCCCCCCCCCCCCC
79.3422790023
830PhosphorylationDMFCDPFTSSTTTNK
CCCCCCCCCCCCCCC
27.4423984901
831PhosphorylationMFCDPFTSSTTTNKE
CCCCCCCCCCCCCCC
26.5123984901
832PhosphorylationFCDPFTSSTTTNKEA
CCCCCCCCCCCCCCC
27.0723984901
833PhosphorylationCDPFTSSTTTNKEAD
CCCCCCCCCCCCCCC
37.0923984901
842PhosphorylationTNKEADPSNFANFSA
CCCCCCCCCCCCCCC
45.1623984901
848PhosphorylationPSNFANFSAYPSEED
CCCCCCCCCCCCHHH
27.0523984901
850PhosphorylationNFANFSAYPSEEDMI
CCCCCCCCCCHHHHH
13.1918515860
852PhosphorylationANFSAYPSEEDMIEW
CCCCCCCCHHHHHHH
40.7327180971
864PhosphorylationIEWAKRESEREEEQR
HHHHHHHHHHHHHHH
46.0920469934

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
850YPhosphorylationKinaseEGFRP00533
PSP
850YPhosphorylationKinaseEGFRQ01279
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPS15_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EPS15_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYN1_HUMANDNM1physical
11483962
EPS15_MOUSEEps15physical
9182572
AGFG1_HUMANAGFG1physical
9303539
NUMB_HUMANNUMBphysical
9303539
NUMBL_HUMANNUMBLphysical
9303539
PRP17_HUMANCDC40physical
9303539
EPN2_HUMANEPN2physical
9303539
AGFG2_HUMANAGFG2physical
9303539
PRKN_HUMANPARK2physical
16862145
PRKN_MOUSEPark2physical
20064468
ITSN1_MOUSEItsn1physical
10064583

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPS15_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-779 AND SER-816, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-324; SER-561;SER-562 AND THR-781, AND MASS SPECTROMETRY.
"Tyrosine phosphorylation of Eps15 is required for ligand-regulated,but not constitutive, endocytosis.";
Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.;
J. Cell Biol. 150:905-912(2000).
Cited for: PHOSPHORYLATION AT TYR-850 BY EGFR, AND MUTAGENESIS OF TYR-850.

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