EPN1_HUMAN - dbPTM
EPN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN1_HUMAN
UniProt AC Q9Y6I3
Protein Name Epsin-1
Gene Name EPN1
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the p
Protein Description Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis..
Protein Sequence MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDAQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPGGGPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
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
2Phosphorylation------MSTSSLRRQ
------CCHHHHHHH		36.6829514088
3Phosphorylation-----MSTSSLRRQM
-----CCHHHHHHHH		22.4929514088
4Phosphorylation----MSTSSLRRQMK
----CCHHHHHHHHH		21.7729514088
5Phosphorylation---MSTSSLRRQMKN
---CCHHHHHHHHHH		26.4528355574
11UbiquitinationSSLRRQMKNIVHNYS
HHHHHHHHHHHHCCH		34.8721890473
11 (in isoform 1)Ubiquitination-34.8721890473
11 (in isoform 2)Ubiquitination-34.8721890473
11 (in isoform 3)Ubiquitination-34.8721890473
16PhosphorylationQMKNIVHNYSEAEIK
HHHHHHHCCHHHEEE		31.0017016520
17PhosphorylationMKNIVHNYSEAEIKV
HHHHHHCCHHHEEEE		7.9428152594
17 (in isoform 1)Phosphorylation-7.9425159151
18PhosphorylationKNIVHNYSEAEIKVR
HHHHHCCHHHEEEEE		35.3328152594
23UbiquitinationNYSEAEIKVREATSN
CCHHHEEEEEECCCC		27.0921890473
23 (in isoform 1)Phosphorylation-27.0929743597
23 (in isoform 1)Ubiquitination-27.0921890473
23 (in isoform 2)Ubiquitination-27.0921890473
23 (in isoform 3)Ubiquitination-27.0921890473
83PhosphorylationKAMTLMEYLIKTGSE
HHHHHHHHHHHHCCH		10.3624114839
86UbiquitinationTLMEYLIKTGSERVS
HHHHHHHHHCCHHHH		44.2121890473
86 (in isoform 1)Ubiquitination-44.2121890473
86 (in isoform 2)Ubiquitination-44.2121890473
86 (in isoform 3)Ubiquitination-44.2121890473
97UbiquitinationERVSQQCKENMYAVQ
HHHHHHHHHCCCHHE		48.0321890473
97 (in isoform 1)Ubiquitination-48.0321890473
97 (in isoform 2)Ubiquitination-48.0321890473
97 (in isoform 3)Ubiquitination-48.0321890473
101PhosphorylationQQCKENMYAVQTLKD
HHHHHCCCHHEECCC		18.4025159151
105PhosphorylationENMYAVQTLKDFQYV
HCCCHHEECCCCEEE		29.2223403867
107UbiquitinationMYAVQTLKDFQYVDR
CCHHEECCCCEEECC		60.9421890473
107 (in isoform 1)Ubiquitination-60.9421890473
107 (in isoform 2)Ubiquitination-60.9421890473
107 (in isoform 3)Ubiquitination-60.9421890473
111PhosphorylationQTLKDFQYVDRDGKD
EECCCCEEECCCCCC		12.3319060867
111 (in isoform 1)Phosphorylation-12.3328348404
113 (in isoform 1)Phosphorylation-37.7128348404
114 (in isoform 1)Phosphorylation-44.5328348404
115 (in isoform 1)Phosphorylation-65.1228348404
116 (in isoform 1)Phosphorylation-36.0128348404
117UbiquitinationQYVDRDGKDQGVNVR
EEECCCCCCCCCCHH		51.6821890473
117 (in isoform 1)Ubiquitination-51.6821890473
117 (in isoform 2)Ubiquitination-51.6821890473
117 (in isoform 3)Ubiquitination-51.6821890473
122 (in isoform 1)Ubiquitination-33.67-
128UbiquitinationVNVREKAKQLVALLR
CCHHHHHHHHHHHHC		56.0621890473
128 (in isoform 1)Ubiquitination-56.0621890473
128 (in isoform 2)Ubiquitination-56.0621890473
128 (in isoform 3)Ubiquitination-56.0621890473
134 (in isoform 1)Ubiquitination-4.71-
149UbiquitinationEERAHALKTKEKLAQ
HHHHHHHHHHHHHHH		59.3321906983
149 (in isoform 1)Ubiquitination-59.3321890473
149 (in isoform 2)Ubiquitination-59.3321890473
149 (in isoform 3)Ubiquitination-59.3321890473
197 (in isoform 1)Ubiquitination-51.62-
204PhosphorylationEEADQPPSCGPEDDA
HHHCCCCCCCCHHHH		38.0925159151
208 (in isoform 1)Ubiquitination-54.53-
218PhosphorylationAQLQLALSLSREEHD
HHHHHHHHHCHHHHC		20.7725159151
218 (in isoform 1)Ubiquitination-20.77-
220PhosphorylationLQLALSLSREEHDKE
HHHHHHHCHHHHCHH		33.9825159151
221 (in isoform 1)Ubiquitination-59.6321890473
221 (in isoform 3)Ubiquitination-59.6321890473
228 (in isoform 1)Ubiquitination-60.18-
239 (in isoform 1)Malonylation-16.9032601280
239 (in isoform 1)Ubiquitination-16.90-
240SulfoxidationGDDLRLQMAIEESKR
HCHHHHHHHHHHHHH		4.8621406390
246UbiquitinationQMAIEESKRETGGKE
HHHHHHHHHHHCCCC		58.4921906983
246 (in isoform 2)Ubiquitination-58.4921890473
256PhosphorylationTGGKEESSLMDLADV
HCCCCCCCHHHHHHH		30.8725332170
265PhosphorylationMDLADVFTAPAPAPT
HHHHHHHCCCCCCCC		31.4225332170
332 (in isoform 1)Ubiquitination-37.26-
357PhosphorylationPWGSSDGGVPVSGPS
CCCCCCCCCCCCCCC		26.0810764745
382PhosphorylationFSDPWGGSPAKPSTN
CCCCCCCCCCCCCCC		20.1110764745
387PhosphorylationGGSPAKPSTNGTTAA
CCCCCCCCCCCCCCC		33.5226074081
388PhosphorylationGSPAKPSTNGTTAAG
CCCCCCCCCCCCCCC		46.3126074081
391PhosphorylationAKPSTNGTTAAGGFD
CCCCCCCCCCCCCCC		18.4826074081
392PhosphorylationKPSTNGTTAAGGFDT
CCCCCCCCCCCCCCC		18.8626074081
410PhosphorylationEFSDFDRLRTALPTS
CCCCHHHHHHCCCCC		6.5018669648
412PhosphorylationSDFDRLRTALPTSGS
CCHHHHHHCCCCCCC		36.8230278072
416PhosphorylationRLRTALPTSGSSAGE
HHHHCCCCCCCCHHH		46.7130278072
417PhosphorylationLRTALPTSGSSAGEL
HHHCCCCCCCCHHHH		34.4430278072
419PhosphorylationTALPTSGSSAGELEL
HCCCCCCCCHHHHHH		19.4430278072
420PhosphorylationALPTSGSSAGELELL
CCCCCCCCHHHHHHH		43.7630278072
429PhosphorylationGELELLAGEVPARSP
HHHHHHHCCCCCCCC		36.0818669648
435PhosphorylationAGEVPARSPGAFDMS
HCCCCCCCCCCCCCC		29.7729255136
437PhosphorylationEVPARSPGAFDMSGV
CCCCCCCCCCCCCCC		39.8718669648
439PhosphorylationPARSPGAFDMSGVRG
CCCCCCCCCCCCCCH		11.3918669648
441SulfoxidationRSPGAFDMSGVRGSL
CCCCCCCCCCCCHHH		2.8021406390
442PhosphorylationSPGAFDMSGVRGSLA
CCCCCCCCCCCHHHH		35.6630266825
443 (in isoform 3)Ubiquitination-13.4021890473
444 (in isoform 1)Ubiquitination-4.9921890473
447PhosphorylationDMSGVRGSLAEAVGS
CCCCCCHHHHHHHCC		17.5330266825
454PhosphorylationSLAEAVGSPPPAATP
HHHHHHCCCCCCCCC		27.8629255136
460PhosphorylationGSPPPAATPTPTPPT
CCCCCCCCCCCCCCC		29.7829255136
462O-linked_GlycosylationPPPAATPTPTPPTRK
CCCCCCCCCCCCCCC		35.13OGP
462PhosphorylationPPPAATPTPTPPTRK
CCCCCCCCCCCCCCC		35.1330266825
464PhosphorylationPAATPTPTPPTRKTP
CCCCCCCCCCCCCCC		44.3630266825
467PhosphorylationTPTPTPPTRKTPESF
CCCCCCCCCCCCHHH		46.1029255136
468PhosphorylationPTPTPPTRKTPESFL
CCCCCCCCCCCHHHC		46.7710764745
469PhosphorylationTPTPPTRKTPESFLG
CCCCCCCCCCHHHCC		71.5518669648
469UbiquitinationTPTPPTRKTPESFLG
CCCCCCCCCCHHHCC		71.5521890473
469 (in isoform 2)Ubiquitination-71.5521890473
470PhosphorylationPTPPTRKTPESFLGP
CCCCCCCCCHHHCCC		29.0629255136
473PhosphorylationPTRKTPESFLGPNAA
CCCCCCHHHCCCCCE		27.2929255136
486PhosphorylationAALVDLDSLVSRPGP
CEEEEHHHHHCCCCC		37.6624732914
489PhosphorylationVDLDSLVSRPGPTPP
EEHHHHHCCCCCCCC		37.7430278072
494PhosphorylationLVSRPGPTPPGAKAS
HHCCCCCCCCCCCCC		48.2930278072
501PhosphorylationTPPGAKASNPFLPGG
CCCCCCCCCCCCCCC		44.3120068231
503 (in isoform 1)Phosphorylation-29.6527251275
505 (in isoform 1)Phosphorylation-3.9827251275
506 (in isoform 1)Phosphorylation-39.5027251275
512PhosphorylationLPGGGPATGPSVTNP
CCCCCCCCCCCCCCC		53.4020068231
515PhosphorylationGGPATGPSVTNPFQP
CCCCCCCCCCCCCCC		42.8120068231
517PhosphorylationPATGPSVTNPFQPAP
CCCCCCCCCCCCCCC		41.3220068231
521 (in isoform 1)Phosphorylation-34.2124719451
527PhosphorylationFQPAPPATLTLNQLR
CCCCCCCEEEECEEE		26.5020068231
528 (in isoform 1)Phosphorylation-5.7924719451
529PhosphorylationPAPPATLTLNQLRLS
CCCCCEEEECEEECC		21.2220068231
534MethylationTLTLNQLRLSPVPPV
EEEECEEECCCCCCC		24.29-
536PhosphorylationTLNQLRLSPVPPVPG
EECEEECCCCCCCCC		19.8820068231
540 (in isoform 1)Phosphorylation-45.2124719451
546 (in isoform 1)Phosphorylation-36.9824719451
547PhosphorylationPVPGAPPTYISPLGG
CCCCCCCCEECCCCC		32.2127251275
548PhosphorylationVPGAPPTYISPLGGG
CCCCCCCEECCCCCC		12.7420068231
548 (in isoform 1)Phosphorylation-12.7424719451
550PhosphorylationGAPPTYISPLGGGPG
CCCCCEECCCCCCCC		12.0327251275
550 (in isoform 1)Phosphorylation-12.0327251275
555 (in isoform 1)Ubiquitination-16.00-
556 (in isoform 1)Phosphorylation-44.4124719451
571PhosphorylationPGPPAPNTNPFLL--
CCCCCCCCCCCCC--		43.1220068231
580 (in isoform 1)Phosphorylation-24719451
587 (in isoform 1)Phosphorylation-27251275
622 (in isoform 1)Phosphorylation-27251275
634 (in isoform 1)Phosphorylation-27251275
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
357SPhosphorylationKinaseCDK1P06493
PhosphoELM
382SPhosphorylationKinaseCDK1P06493
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN1_HUMAN !!
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 EPN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3A_HUMANGTF3Aphysical
12775724
CE126_HUMANKIAA1377physical
16169070
MED31_HUMANMED31physical
16169070
DPYL1_HUMANCRMP1physical
16169070
CLH1_HUMANCLTCphysical
10692452
EPS15_HUMANEPS15physical
9723620
EP15R_HUMANEPS15L1physical
9723620
AP2A2_HUMANAP2A2physical
9723620
REPS2_HUMANREPS2physical
10557078
AP1M2_HUMANAP1M2physical
16574660
SCNNA_HUMANSCNN1Aphysical
16574660
SCNNB_HUMANSCNN1Bphysical
16574660
SCNNG_HUMANSCNN1Gphysical
16574660
DLL1_HUMANDLL1physical
22658936
EPS15_HUMANEPS15physical
16429130
EGFR_HUMANEGFRphysical
19054389
EPN3_HUMANEPN3physical
21115825
REPS2_HUMANREPS2physical
15809337
EPS15_HUMANEPS15physical
15809337
AP1B1_HUMANAP1B1physical
12538641
REPS2_HUMANREPS2physical
10764745
AP2A1_HUMANAP2A1physical
10764745
SMAD5_HUMANSMAD5physical
22939629
VGFR2_HUMANKDRphysical
23187125
BCAR1_HUMANBCAR1physical
22863883
VGFR3_HUMANFLT4physical
25314967
PKHB2_HUMANPLEKHB2physical
25416956
UBC_HUMANUBCphysical
16497222
DVL2_HUMANDVL2physical
25871009
LRP6_HUMANLRP6physical
25871009
FZD7_HUMANFZD7physical
25871009
FZD8_HUMANFZD8physical
25871009
IRS2_HUMANIRS2physical
25879670
ERBB3_HUMANERBB3physical
26975582
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-419; SER-420; SER-435;SER-454; THR-460 AND THR-470, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, 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-435; SER-454; THR-460;THR-464 AND THR-494, AND MASS SPECTROMETRY.
"Regulation of complex formation of POB1/epsin/adaptor protein complex2 by mitotic phosphorylation.";
Kariya K., Koyama S., Nakashima S., Oshiro T., Morinaka K.,Kikuchi A.;
J. Biol. Chem. 275:18399-18406(2000).
Cited for: PHOSPHORYLATION AT SER-382, MUTAGENESIS OF SER-382, AND INTERACTIONWITH REPS2; EPS15 AND AP-2 ALPHA SUBUNIT.
"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-494, 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 THR-494, AND MASSSPECTROMETRY.

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