EP15R_MOUSE - dbPTM
EP15R_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EP15R_MOUSE
UniProt AC Q60902
Protein Name Epidermal growth factor receptor substrate 15-like 1
Gene Name Eps15l1
Organism Mus musculus (Mouse).
Sequence Length 907
Subcellular Localization Cell membrane
Peripheral membrane protein . Nucleus . Membrane, coated pit . Localized to plasma membrane coated pits.
Protein Description Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. 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 (By similarity)..
Protein Sequence MAAPLVPLSQQIPGGNPLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLSSLSLTMPPPKFHDTSSPLMATQSSAETHWAVRVEEKAKFDGIFESLLPVNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPSILPPPLIPPSKRKKTVFAGAVPVLPASPPPKDSLRSTPSHGSVSSLNSTGSLSPKHSVKQPPVAWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSKGIDPPQVLSPDMVPPSERGTPIPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGGFGAMDDPFKNKALLFSNNSQELHPDPFQAEDPFKSDPFKGADPFKGDPFQSDPFSEQQTAATDPFGGDPFKESDPFHSSSSDDFFKKQTKNDPFTSDPFTKNPSLPSKLDPFESSDPFSSSSISSKGSDPFGTLDPFGSSSFSSAEGFADFSQMSKPPPSGPFSSSLGGTGFSDDPFKSKQDTPALPPKKPAPPRPKPPSGQSTPVSQLGSSDFPESPDPFQPLGADSGDPFQNKKGFGDPFSGKDPFAPSSSAKPPKTSSSGFADFTSFGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLELAIALSKADMPA
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------MAAPLVPLS
------CCCCCCCHH
20.14-
9PhosphorylationAAPLVPLSQQIPGGN
CCCCCCHHHCCCCCC
17.6119144319
30PhosphorylationYKQVDPAYTGRVGAS
HCCCCHHHCCCCCHH
18.3419144319
31PhosphorylationKQVDPAYTGRVGASE
CCCCHHHCCCCCHHH
22.1819144319
49PhosphorylationFLKKSGLSDIILGKI
HHHHCCCCHHHHHHH
30.2322942356
74PhosphorylationFLDKQGFYVALRLVA
CCCCCCHHHHHHHHH
7.5216452087
106PhosphorylationPPPKFHDTSSPLMAT
CCCCCCCCCCCCEEC
23.6426239621
107PhosphorylationPPKFHDTSSPLMATQ
CCCCCCCCCCCEECC
35.7023335269
108PhosphorylationPKFHDTSSPLMATQS
CCCCCCCCCCEECCC
24.9326824392
113PhosphorylationTSSPLMATQSSAETH
CCCCCEECCCCCCCE
18.2828833060
115PhosphorylationSPLMATQSSAETHWA
CCCEECCCCCCCEEE
27.4528833060
116PhosphorylationPLMATQSSAETHWAV
CCEECCCCCCCEEEE
21.9528833060
119PhosphorylationATQSSAETHWAVRVE
ECCCCCCCEEEEEHH
23.5728833060
217PhosphorylationPPSKRKKTVFAGAVP
CCHHCCCEEEECCEE
24.7225619855
229PhosphorylationAVPVLPASPPPKDSL
CEEECCCCCCCCCCC
35.6824925903
235PhosphorylationASPPPKDSLRSTPSH
CCCCCCCCCCCCCCC
31.6322942356
238PhosphorylationPPKDSLRSTPSHGSV
CCCCCCCCCCCCCCC
50.3824925903
238 (in isoform 2)Phosphorylation-50.3819144319
239PhosphorylationPKDSLRSTPSHGSVS
CCCCCCCCCCCCCCC
23.5224925903
241PhosphorylationDSLRSTPSHGSVSSL
CCCCCCCCCCCCCCC
40.3424925903
244PhosphorylationRSTPSHGSVSSLNST
CCCCCCCCCCCCCCC
17.2524925903
246PhosphorylationTPSHGSVSSLNSTGS
CCCCCCCCCCCCCCC
30.7024925903
247PhosphorylationPSHGSVSSLNSTGSL
CCCCCCCCCCCCCCC
29.4324925903
250PhosphorylationGSVSSLNSTGSLSPK
CCCCCCCCCCCCCCC
39.1624925903
251PhosphorylationSVSSLNSTGSLSPKH
CCCCCCCCCCCCCCC
29.7124925903
253PhosphorylationSSLNSTGSLSPKHSV
CCCCCCCCCCCCCCC
26.2624925903
255PhosphorylationLNSTGSLSPKHSVKQ
CCCCCCCCCCCCCCC
33.3324925903
255 (in isoform 2)Phosphorylation-33.3319144319
259PhosphorylationGSLSPKHSVKQPPVA
CCCCCCCCCCCCCEE
36.82-
291PhosphorylationTDLDLDGYVSGQEVK
CCCCCCCCCCHHHHH
7.3625195567
293PhosphorylationLDLDGYVSGQEVKEI
CCCCCCCCHHHHHHH
26.6926525534
304PhosphorylationVKEIFMHSGLTQNLL
HHHHHHCCCHHHHHH
24.5820495213
353PhosphorylationIDPPQVLSPDMVPPS
CCCCCCCCCCCCCCH
21.7225521595
360PhosphorylationSPDMVPPSERGTPIP
CCCCCCCHHCCCCCC
33.5826239621
364PhosphorylationVPPSERGTPIPDSSS
CCCHHCCCCCCCCCC
25.0225521595
369PhosphorylationRGTPIPDSSSTLASG
CCCCCCCCCCCCCCC
22.3428833060
370PhosphorylationGTPIPDSSSTLASGE
CCCCCCCCCCCCCCC
34.4228833060
371PhosphorylationTPIPDSSSTLASGEF
CCCCCCCCCCCCCCC
31.2425521595
372PhosphorylationPIPDSSSTLASGEFT
CCCCCCCCCCCCCCC
28.4328833060
375PhosphorylationDSSSTLASGEFTGVK
CCCCCCCCCCCCCCC
41.8026824392
379PhosphorylationTLASGEFTGVKELDD
CCCCCCCCCCCCHHH
36.4428833060
400PhosphorylationQLQREKYSLEQDIRE
HHHHHHHCHHHHHHH
36.1828066266
430PhosphorylationQNDLDRETSSLQELE
HHHHHHHHHHHHHHH
25.2228066266
431PhosphorylationNDLDRETSSLQELEA
HHHHHHHHHHHHHHH
25.0528066266
432PhosphorylationDLDRETSSLQELEAQ
HHHHHHHHHHHHHHH
41.3028066266
462PhosphorylationAKLRDMLSDVRQKCQ
HHHHHHHHHHHHHHH
27.6729514104
480PhosphorylationQTISSLKTQIQSQES
HHHHHHHHHHHHHHH
35.8818779572
484PhosphorylationSLKTQIQSQESDLKS
HHHHHHHHHHHHHHH
37.2318779572
487PhosphorylationTQIQSQESDLKSQED
HHHHHHHHHHHHHHH
40.3818779572
490UbiquitinationQSQESDLKSQEDDLN
HHHHHHHHHHHHHHH
55.9022790023
532UbiquitinationETILRSLKCTQDDIN
HHHHHHCCCCHHHHH
36.1622790023
533GlutathionylationTILRSLKCTQDDINQ
HHHHHCCCCHHHHHH
5.1124333276
544UbiquitinationDINQARSKLSQLQES
HHHHHHHHHHHHHHH
46.7522790023
546PhosphorylationNQARSKLSQLQESHL
HHHHHHHHHHHHHHH
32.3629899451
558PhosphorylationSHLEAHRSLEQYDQV
HHHHHHHCHHHHHCC
26.7922499769
558 (in isoform 4)Phosphorylation-26.7929899451
562PhosphorylationAHRSLEQYDQVPDGV
HHHCHHHHHCCCCCC
10.0422499769
562 (in isoform 4)Phosphorylation-10.0429899451
570PhosphorylationDQVPDGVSGTSLPDL
HCCCCCCCCCCCCCH
41.7122499769
572PhosphorylationVPDGVSGTSLPDLAT
CCCCCCCCCCCCHHH
21.4222499769
573PhosphorylationPDGVSGTSLPDLATL
CCCCCCCCCCCHHHH
41.2422499769
579PhosphorylationTSLPDLATLNEGILL
CCCCCHHHHCCCEEE
37.1023984901
579 (in isoform 4)Phosphorylation-37.1029514104
600UbiquitinationGAMDDPFKNKALLFS
CCCCCCCCCCEEEEC
64.0322790023
602UbiquitinationMDDPFKNKALLFSNN
CCCCCCCCEEEECCC
40.7922790023
607PhosphorylationKNKALLFSNNSQELH
CCCEEEECCCCCCCC
34.7626239621
610PhosphorylationALLFSNNSQELHPDP
EEEECCCCCCCCCCC
29.3126824392
610 (in isoform 2)Phosphorylation-29.3119144319
625UbiquitinationFQAEDPFKSDPFKGA
CCCCCCCCCCCCCCC
60.38-
626PhosphorylationQAEDPFKSDPFKGAD
CCCCCCCCCCCCCCC
51.3925293948
630UbiquitinationPFKSDPFKGADPFKG
CCCCCCCCCCCCCCC
59.5922790023
636UbiquitinationFKGADPFKGDPFQSD
CCCCCCCCCCCCCCC
68.72-
646PhosphorylationPFQSDPFSEQQTAAT
CCCCCCCCHHHHCCC
39.6223984901
650PhosphorylationDPFSEQQTAATDPFG
CCCCHHHHCCCCCCC
20.2523984901
653PhosphorylationSEQQTAATDPFGGDP
CHHHHCCCCCCCCCC
41.5623984901
664PhosphorylationGGDPFKESDPFHSSS
CCCCCCCCCCCCCCC
51.6927742792
669PhosphorylationKESDPFHSSSSDDFF
CCCCCCCCCCHHHHH
32.0927742792
670PhosphorylationESDPFHSSSSDDFFK
CCCCCCCCCHHHHHH
25.8727742792
671PhosphorylationSDPFHSSSSDDFFKK
CCCCCCCCHHHHHHH
40.5827742792
672PhosphorylationDPFHSSSSDDFFKKQ
CCCCCCCHHHHHHHH
43.0527742792
677UbiquitinationSSSDDFFKKQTKNDP
CCHHHHHHHHCCCCC
43.92-
678UbiquitinationSSDDFFKKQTKNDPF
CHHHHHHHHCCCCCC
59.03-
681UbiquitinationDFFKKQTKNDPFTSD
HHHHHHCCCCCCCCC
57.78-
687PhosphorylationTKNDPFTSDPFTKNP
CCCCCCCCCCCCCCC
43.6018779572
692UbiquitinationFTSDPFTKNPSLPSK
CCCCCCCCCCCCCCC
68.2122790023
695PhosphorylationDPFTKNPSLPSKLDP
CCCCCCCCCCCCCCC
63.4130352176
699UbiquitinationKNPSLPSKLDPFESS
CCCCCCCCCCCCCCC
55.7722790023
706PhosphorylationKLDPFESSDPFSSSS
CCCCCCCCCCCCCCC
41.9526060331
713PhosphorylationSDPFSSSSISSKGSD
CCCCCCCCCCCCCCC
28.5626060331
715PhosphorylationPFSSSSISSKGSDPF
CCCCCCCCCCCCCCC
28.1326060331
732PhosphorylationLDPFGSSSFSSAEGF
CCCCCCCCCCCCCCC
30.74-
774PhosphorylationPFKSKQDTPALPPKK
CCCCCCCCCCCCCCC
14.1527600695
791PhosphorylationPPRPKPPSGQSTPVS
CCCCCCCCCCCCCHH
58.9729899451
794PhosphorylationPKPPSGQSTPVSQLG
CCCCCCCCCCHHHCC
37.9025521595
795PhosphorylationKPPSGQSTPVSQLGS
CCCCCCCCCHHHCCC
21.5929899451
798PhosphorylationSGQSTPVSQLGSSDF
CCCCCCHHHCCCCCC
22.3825521595
808PhosphorylationGSSDFPESPDPFQPL
CCCCCCCCCCCCCCC
34.5426060331
817 (in isoform 2)Phosphorylation-18.5827149854
827UbiquitinationGDPFQNKKGFGDPFS
CCCCCCCCCCCCCCC
68.0022790023
836UbiquitinationFGDPFSGKDPFAPSS
CCCCCCCCCCCCCCC
62.1122790023
846UbiquitinationFAPSSSAKPPKTSSS
CCCCCCCCCCCCCCC
64.8922790023
849UbiquitinationSSSAKPPKTSSSGFA
CCCCCCCCCCCCCCC
70.3522790023

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

Oops, there are no upstream regulatory protein records of EP15R_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EP15R_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 EP15R_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGFG1_HUMANAGFG1physical
9303539
AGFG2_HUMANAGFG2physical
9303539
NUMB_HUMANNUMBphysical
9303539
NUMBL_HUMANNUMBLphysical
9303539
PRP17_HUMANCDC40physical
9303539
EPN2_HUMANEPN2physical
9303539

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EP15R_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 SER-9; TYR-30; THR-31;SER-238 AND SER-255, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"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-244; SER-250 ANDSER-255, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-353 ANDTHR-364, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND MASSSPECTROMETRY.

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