EPN3_HUMAN - dbPTM
EPN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN3_HUMAN
UniProt AC Q9H201
Protein Name Epsin-3
Gene Name EPN3
Organism Homo sapiens (Human).
Sequence Length 632
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cytoplasmic vesicle, clathrin-coated vesicle . Nucleus . Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus.
Protein Description
Protein Sequence MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIGIGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQLQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQSSILDLADIFVPALAPPSTHCSADPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILGEALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQVAKTRNPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPFL
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------MTTSALRRQ
------CCHHHHHHH		29.4729116813
3Phosphorylation-----MTTSALRRQV
-----CCHHHHHHHH		15.6523836654
4Phosphorylation----MTTSALRRQVK
----CCHHHHHHHHH		19.0129116813
17PhosphorylationVKNIVHNYSEAEIKV
HHHHHHCCCHHEEEE		7.9428152594
18PhosphorylationKNIVHNYSEAEIKVR
HHHHHCCCHHEEEEE		35.3328152594
23 (in isoform 1)Ubiquitination-27.0921890473
23UbiquitinationNYSEAEIKVREATSN
CCCHHEEEEEECCCC		27.0921890473
23 (in isoform 2)Ubiquitination-27.0921890473
47PhosphorylationMSEIADLTFNTVAFT
HHHHHHCCHHHHHHH		18.5230257219
75PhosphorylationGKNWRHVYKALTLLD
CCCHHHHHHHHHHHH		5.6118083107
83PhosphorylationKALTLLDYLLKTGSE
HHHHHHHHHHHHCCH		17.5722817900
101PhosphorylationHQCRENLYTIQTLKD
HHHHHCCEEEEECCC		17.24-
102PhosphorylationQCRENLYTIQTLKDF
HHHHCCEEEEECCCC		15.13-
111PhosphorylationQTLKDFQYIDRDGKD
EECCCCCEECCCCCC		12.5529978859
117UbiquitinationQYIDRDGKDQGVNVR
CEECCCCCCCCCCHH		51.6829901268
117 (in isoform 1)Ubiquitination-51.6821890473
117 (in isoform 2)Ubiquitination-51.6821890473
149UbiquitinationQERTHALKTKERMAL
HHHHHHHHHHHHHHH		59.33-
163PhosphorylationLEGIGIGSGQLGFSR
HCCCCCCCCCCCCCC		22.8024719451
169PhosphorylationGSGQLGFSRRYGEDY
CCCCCCCCCHHCCCC		17.6624719451
172PhosphorylationQLGFSRRYGEDYSRS
CCCCCCHHCCCCCCC		24.6124927040
176PhosphorylationSRRYGEDYSRSRGSP
CCHHCCCCCCCCCCC		11.1528152594
177PhosphorylationRRYGEDYSRSRGSPS
CHHCCCCCCCCCCCC		35.7828152594
179PhosphorylationYGEDYSRSRGSPSSY
HCCCCCCCCCCCCCC		34.7423090842
182PhosphorylationDYSRSRGSPSSYNSS
CCCCCCCCCCCCCCC		22.0925849741
184PhosphorylationSRSRGSPSSYNSSSS
CCCCCCCCCCCCCCC		47.3433259812
185PhosphorylationRSRGSPSSYNSSSSS
CCCCCCCCCCCCCCC		31.5523090842
186PhosphorylationSRGSPSSYNSSSSSP
CCCCCCCCCCCCCCC		24.3319534553
188PhosphorylationGSPSSYNSSSSSPRY
CCCCCCCCCCCCCCC		24.3023090842
189PhosphorylationSPSSYNSSSSSPRYT
CCCCCCCCCCCCCCC		30.5123090842
190PhosphorylationPSSYNSSSSSPRYTS
CCCCCCCCCCCCCCC		34.3623090842
191PhosphorylationSSYNSSSSSPRYTSD
CCCCCCCCCCCCCCC		46.4325849741
192PhosphorylationSYNSSSSSPRYTSDL
CCCCCCCCCCCCCCH		18.4928985074
195PhosphorylationSSSSSPRYTSDLEQA
CCCCCCCCCCCHHHH		17.6122817900
206PhosphorylationLEQARPQTSGEEELQ
HHHHCCCCCCHHHHH		41.19-
207PhosphorylationEQARPQTSGEEELQL
HHHCCCCCCHHHHHH		38.67-
258PhosphorylationEHEKEVRSWQGDGSP
HHHHHHHHCCCCCCC		29.0027794612
264PhosphorylationRSWQGDGSPMANGAG
HHCCCCCCCCCCCCC		19.0825849741
358PhosphorylationSGTVLSRSQPWDLTP
CCCEEECCCCCCCCC		36.9028102081
364PhosphorylationRSQPWDLTPMLSSSE
CCCCCCCCCCCCCCC		12.2728102081
368PhosphorylationWDLTPMLSSSEPWGR
CCCCCCCCCCCCCCC		26.0928348404
385PhosphorylationVLPAGPPTTDPWALN
CCCCCCCCCCCCHHC		47.1423312004
386PhosphorylationLPAGPPTTDPWALNS
CCCCCCCCCCCHHCC		45.9323312004
393PhosphorylationTDPWALNSPHHKLPS
CCCCHHCCCCCCCCC		26.8525849741
409PhosphorylationGADPWGASLETSDTP
CCCCCCCCCCCCCCC		23.8527251275
412PhosphorylationPWGASLETSDTPGGA
CCCCCCCCCCCCCCC		36.8827251275
413PhosphorylationWGASLETSDTPGGAS
CCCCCCCCCCCCCCC		30.0627251275
444PhosphorylationGLEQALPSGKPSSPV
HHHHHCCCCCCCCCE		61.3728857561
448PhosphorylationALPSGKPSSPVELDL
HCCCCCCCCCEEEEC		51.2425849741
449PhosphorylationLPSGKPSSPVELDLF
CCCCCCCCCEEEECC		41.3030278072
460PhosphorylationLDLFGDPSPSSKQNG
EECCCCCCCCCCCCC		42.0025849741
462PhosphorylationLFGDPSPSSKQNGTK
CCCCCCCCCCCCCCC		55.2830278072
463PhosphorylationFGDPSPSSKQNGTKE
CCCCCCCCCCCCCCC		41.4630278072
495PhosphorylationKEARACRTPESFLGP
HHHHHCCCCHHHHCC		31.1530278072
498PhosphorylationRACRTPESFLGPSAS
HHCCCCHHHHCCCHH		27.2930278072
503PhosphorylationPESFLGPSASSLVNL
CHHHHCCCHHHHCCH		38.7026657352
505PhosphorylationSFLGPSASSLVNLDS
HHHCCCHHHHCCHHH		28.6626657352
506PhosphorylationFLGPSASSLVNLDSL
HHCCCHHHHCCHHHH		35.7327542207
522PhosphorylationKAPQVAKTRNPFLTG
CCCHHHCCCCCCCCC		26.4128102081
528PhosphorylationKTRNPFLTGLSAPSP
CCCCCCCCCCCCCCC		36.1328348404
531PhosphorylationNPFLTGLSAPSPTNP
CCCCCCCCCCCCCCC		39.2128348404
534PhosphorylationLTGLSAPSPTNPFGA
CCCCCCCCCCCCCCC		44.0328102081
536PhosphorylationGLSAPSPTNPFGAGE
CCCCCCCCCCCCCCC		60.9228102081
613PhosphorylationAPQPLLPTPSSAGPR
CCCCCCCCCCCCCCC		35.4526853621
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 EPN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN3_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 EPN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBB_HUMANUBBphysical
26186194
VPS39_HUMANVPS39physical
26186194
HS71L_HUMANHSPA1Lphysical
26186194
EPN2_HUMANEPN2physical
26186194
EPN1_HUMANEPN1physical
26186194
TNKS2_HUMANTNKS2physical
26186194
TNKS1_HUMANTNKSphysical
26186194
SERA_HUMANPHGDHphysical
26186194
TRIM1_HUMANMID2physical
26186194
TRI18_HUMANMID1physical
26186194
TRI32_HUMANTRIM32physical
26186194
SMUF1_HUMANSMURF1physical
26186194
BACD3_HUMANKCTD10physical
26186194
CDC27_HUMANCDC27physical
26186194
ARI1_HUMANARIH1physical
26186194
BTBD9_HUMANBTBD9physical
26186194
FEM1B_HUMANFEM1Bphysical
26186194
CASP2_HUMANCASP2physical
26186194
KCTD3_HUMANKCTD3physical
26186194
SHKB1_HUMANSHKBP1physical
26186194
CYHR1_HUMANCYHR1physical
26186194
BTBD1_HUMANBTBD1physical
26186194
EPN2_HUMANEPN2physical
28514442
EPN1_HUMANEPN1physical
28514442
UBB_HUMANUBBphysical
28514442
TNKS2_HUMANTNKS2physical
28514442
TRI18_HUMANMID1physical
28514442
CASP2_HUMANCASP2physical
28514442
TRIM1_HUMANMID2physical
28514442
TNKS1_HUMANTNKSphysical
28514442
ARI1_HUMANARIH1physical
28514442
CYHR1_HUMANCYHR1physical
28514442
SMUF1_HUMANSMURF1physical
28514442
VPS39_HUMANVPS39physical
28514442
SERA_HUMANPHGDHphysical
28514442
BACD3_HUMANKCTD10physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
UBR1_HUMANUBR1physical
28514442
BTBD1_HUMANBTBD1physical
28514442
KCTD3_HUMANKCTD3physical
28514442
SHKB1_HUMANSHKBP1physical
28514442
MIB1_HUMANMIB1physical
28514442
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 EPN3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17; TYR-176 AND TYR-186,AND MASS SPECTROMETRY.

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