EPN1_MOUSE - dbPTM
EPN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN1_MOUSE
UniProt AC Q80VP1
Protein Name Epsin-1
Gene Name Epn1
Organism Mus musculus (Mouse).
Sequence Length 575
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 MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
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		36.6823737553
3Phosphorylation-----MSTSSLRRQM
-----CCHHHHHHHH		22.4923737553
4Phosphorylation----MSTSSLRRQMK
----CCHHHHHHHHH		21.7723737553
5Phosphorylation---MSTSSLRRQMKN
---CCHHHHHHHHHH		26.4523737553
11UbiquitinationSSLRRQMKNIVHNYS
HHHHHHHHHHHHCCH		34.8722790023
11 (in isoform 2)Ubiquitination-34.8722790023
17PhosphorylationMKNIVHNYSEAEIKV
HHHHHHCCHHHEEEE		7.9429514104
23UbiquitinationNYSEAEIKVREATSN
CCHHHEEEEEECCCC		27.0922790023
23 (in isoform 2)Ubiquitination-27.0922790023
30UbiquitinationKVREATSNDPWGPSS
EEEECCCCCCCCCCH		55.8227667366
40UbiquitinationWGPSSSLMSEIADLT
CCCCHHHHHHHHHCH		3.5027667366
51UbiquitinationADLTYNVVAFSEIMS
HHCHHHHHHHHHHHH		3.8627667366
53UbiquitinationLTYNVVAFSEIMSMI
CHHHHHHHHHHHHHH		4.5627667366
69MalonylationKRLNDHGKNWRHVYK
HHHHHCCCCHHHHHH		50.3326320211
86 (in isoform 2)Ubiquitination-44.2122790023
86UbiquitinationTLMEYLIKTGSERVS
HHHHHHHHHCCHHHH		44.2122790023
97 (in isoform 2)Ubiquitination-48.0322790023
97UbiquitinationERVSQQCKENMYAVQ
HHHHHHHHHCCCHHE		48.0322790023
107 (in isoform 2)Ubiquitination-60.9422790023
107UbiquitinationMYAVQTLKDFQYVDR
CCHHEECCCCEEECC		60.9427667366
107SuccinylationMYAVQTLKDFQYVDR
CCHHEECCCCEEECC		60.9423954790
117 (in isoform 2)Ubiquitination-51.6822790023
117UbiquitinationQYVDRDGKDQGVNVR
EEECCCCCCCCCCHH		51.6822790023
128UbiquitinationVNVREKAKQLVALLR
CCHHHHHHHHHHHHC		56.0622790023
128 (in isoform 2)Ubiquitination-56.0622790023
169UbiquitinationSAAVGSGPPPEAEQA
HHHCCCCCCCHHHHH		42.8627667366
221UbiquitinationQLALSLSREEHDKEE
HHHHHHCHHHHCHHH		59.6327667366
246 (in isoform 2)Ubiquitination-58.4922790023
246UbiquitinationQMAIEESKRETGGKE
HHHHHHHHHHHCCCC		58.4922790023
382PhosphorylationFSDPWGGSPAKPSSN
CCCCCCCCCCCCCCC		20.11-
411PhosphorylationSDFDRLRTALPTSGS
CCHHHHHHCCCCCCC		36.8228833060
415PhosphorylationRLRTALPTSGSSTGE
HHHHCCCCCCCCCCC		46.7125521595
416O-linked_GlycosylationLRTALPTSGSSTGEL
HHHCCCCCCCCCCCE		34.4425477733
416PhosphorylationLRTALPTSGSSTGEL
HHHCCCCCCCCCCCE		34.4425521595
418PhosphorylationTALPTSGSSTGELEL
HCCCCCCCCCCCEEE		25.2125521595
419PhosphorylationALPTSGSSTGELELL
CCCCCCCCCCCEEEC		43.9125521595
420PhosphorylationLPTSGSSTGELELLA
CCCCCCCCCCEEECC		36.0525521595
434PhosphorylationAGEVPARSPGAFDMS
CCCCCCCCCCCCCCC		29.7724925903
441PhosphorylationSPGAFDMSGVGGSLA
CCCCCCCCCCCHHHH		31.9724925903
446PhosphorylationDMSGVGGSLAESVGS
CCCCCCHHHHHHHCC		20.6224925903
450PhosphorylationVGGSLAESVGSPPPA
CCHHHHHHHCCCCCC		26.6025521595
453PhosphorylationSLAESVGSPPPAATP
HHHHHHCCCCCCCCC		31.8825521595
459PhosphorylationGSPPPAATPTPTPPT
CCCCCCCCCCCCCCC		29.7825521595
461PhosphorylationPPPAATPTPTPPTRK
CCCCCCCCCCCCCCC		35.1324925903
463PhosphorylationPAATPTPTPPTRKTP
CCCCCCCCCCCCCCC		44.3624925903
466PhosphorylationTPTPTPPTRKTPESF
CCCCCCCCCCCCHHH		46.1024925903
468 (in isoform 2)Ubiquitination-71.5522790023
468UbiquitinationTPTPPTRKTPESFLG
CCCCCCCCCCHHHCC		71.5522790023
469PhosphorylationPTPPTRKTPESFLGP
CCCCCCCCCHHHCCC		29.0626824392
469 (in isoform 2)Ubiquitination-29.06-
470 (in isoform 2)Phosphorylation-37.9719144319
472PhosphorylationPTRKTPESFLGPNAA
CCCCCCHHHCCCCCE		27.2925177544
485PhosphorylationAALVDLDSLVSRPGP
CEEEEHHHHHCCCCC		37.6626643407
488PhosphorylationVDLDSLVSRPGPTPP
EEHHHHHCCCCCCCC		37.7426745281
493PhosphorylationLVSRPGPTPPGSKAS
HHCCCCCCCCCCCCC		48.2927818261
497PhosphorylationPGPTPPGSKASNPFL
CCCCCCCCCCCCCCC		30.7226745281
500PhosphorylationTPPGSKASNPFLPSG
CCCCCCCCCCCCCCC		49.0930352176
514PhosphorylationGAPPTGPSVTNPFQP
CCCCCCCCCCCCCCC		42.81-
533MethylationTLTLNQLRLSPVPPV
EEEECEEECCCCCCC		24.2924129315
535PhosphorylationTLNQLRLSPVPPVPG
EECEEECCCCCCCCC		19.8823649490
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 EPN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN1_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 EPN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VGFR3_MOUSEFlt4physical
25314967
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPN1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-419, AND MASSSPECTROMETRY.
"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 THR-469, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory