TRAF7_HUMAN - dbPTM
TRAF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRAF7_HUMAN
UniProt AC Q6Q0C0
Protein Name E3 ubiquitin-protein ligase TRAF7
Gene Name TRAF7
Organism Homo sapiens (Human).
Sequence Length 670
Subcellular Localization Cytoplasmic vesicle . Colocalizes with MAP3K3 to vesicle-like structures throughout the cytoplasm.
Protein Description E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed..
Protein Sequence MSSGKSARYNRFSGGPSNLPTPDVTTGTRMETTFGPAFSAVTTITKADGTSTYKQHCRTPSSSSTLAYSPRDEEDSMPPISTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNVKLTVVVNNIAVAEQIGELFIHCRHGCRVAGSGKPPIFEVDPRGCPFTIKLSARKDHEGSCDYRPVRCPNNPSCPPLLRMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLGKLSEKIDQLEKSLELKFDVLDENQSKLSEDLMEFRRDASMLNDELSHINARLNMGILGSYDPQQIFKCKGTFVGHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQKTLEGHDGIVLALCIQGCKLYSGSADCTIIVWDIQNLQKVNTIRAHDNPVCTLVSSHNVLFSGSLKAIKVWDIVGTELKLKKELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHVLQTSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRTLTGHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQTLLRHQGSVTALAVSRGRLFSGAVDSTVKVWTC
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
9PhosphorylationSSGKSARYNRFSGGP
CCCCCCCCCCCCCCC		15.4821712546
12 (in isoform 2)Phosphorylation-7.6827762562
13PhosphorylationSARYNRFSGGPSNLP
CCCCCCCCCCCCCCC		39.3325850435
15 (in isoform 2)Phosphorylation-22.6727762562
17PhosphorylationNRFSGGPSNLPTPDV
CCCCCCCCCCCCCCC		55.0329523821
21PhosphorylationGGPSNLPTPDVTTGT
CCCCCCCCCCCCCCC		34.9725159151
53PhosphorylationKADGTSTYKQHCRTP
ECCCCCCCCCCCCCC		14.39-
54UbiquitinationADGTSTYKQHCRTPS
CCCCCCCCCCCCCCC		33.38-
59PhosphorylationTYKQHCRTPSSSSTL
CCCCCCCCCCCCCCC		32.6827273156
61PhosphorylationKQHCRTPSSSSTLAY
CCCCCCCCCCCCCCC		42.0923401153
62PhosphorylationQHCRTPSSSSTLAYS
CCCCCCCCCCCCCCC		29.5230631047
63PhosphorylationHCRTPSSSSTLAYSP
CCCCCCCCCCCCCCC		31.5127794612
64PhosphorylationCRTPSSSSTLAYSPR
CCCCCCCCCCCCCCC		29.4127794612
65PhosphorylationRTPSSSSTLAYSPRD
CCCCCCCCCCCCCCC		19.8423663014
68PhosphorylationSSSSTLAYSPRDEED
CCCCCCCCCCCCCCC		23.4827732954
69PhosphorylationSSSTLAYSPRDEEDS
CCCCCCCCCCCCCCC		14.0925159151
76PhosphorylationSPRDEEDSMPPISTP
CCCCCCCCCCCCCCC		36.1530576142
81PhosphorylationEDSMPPISTPRRSDS
CCCCCCCCCCCCCCC		37.8326471730
82PhosphorylationDSMPPISTPRRSDSA
CCCCCCCCCCCCCCC		22.8721815630
86PhosphorylationPISTPRRSDSAISVR
CCCCCCCCCCCEEEE		36.8825159151
88PhosphorylationSTPRRSDSAISVRSL
CCCCCCCCCEEEEEE		28.8425159151
91PhosphorylationRRSDSAISVRSLHSE
CCCCCCEEEEEECCC		15.9325159151
94PhosphorylationDSAISVRSLHSESSM
CCCEEEEEECCCCCC		28.4225159151
97PhosphorylationISVRSLHSESSMSLR
EEEEEECCCCCCCCH		44.4626055452
99PhosphorylationVRSLHSESSMSLRST
EEEECCCCCCCCHHC		34.0623663014
100PhosphorylationRSLHSESSMSLRSTF
EEECCCCCCCCHHCC		14.3523663014
102PhosphorylationLHSESSMSLRSTFSL
ECCCCCCCCHHCCCC		23.6823663014
105PhosphorylationESSMSLRSTFSLPEE
CCCCCCHHCCCCCCC		38.8130278072
106PhosphorylationSSMSLRSTFSLPEEE
CCCCCHHCCCCCCCC		15.7130278072
108PhosphorylationMSLRSTFSLPEEEEE
CCCHHCCCCCCCCCC		43.0030278072
123 (in isoform 2)Ubiquitination-52.1121890473
126PhosphorylationLVFAEQPSVKLCCQL
CEECCCCCHHHHHHH		31.4226074081
144PhosphorylationVFKDPVITTCGHTFC
HHCCCEEEECCCCHH		19.10-
149PhosphorylationVITTCGHTFCRRCAL
EEEECCCCHHHHHHH		15.09-
160UbiquitinationRCALKSEKCPVDNVK
HHHHCCCCCCCCCEE		51.43-
197PhosphorylationHGCRVAGSGKPPIFE
CCCEECCCCCCCEEE		33.6328555341
199UbiquitinationCRVAGSGKPPIFEVD
CEECCCCCCCEEEEC		49.6821890473
199 (in isoform 1)Ubiquitination-49.6821890473
212 (in isoform 2)Ubiquitination-14.8721890473
220UbiquitinationTIKLSARKDHEGSCD
EEEEECCCCCCCCCC		64.25-
225PhosphorylationARKDHEGSCDYRPVR
CCCCCCCCCCCCCCC		10.7920873877
252UbiquitinationMNLEAHLKECEHIKC
HHHHHHHHHCCCCCC		50.91-
255 (in isoform 2)Ubiquitination-50.1421890473
264PhosphorylationIKCPHSKYGCTFIGN
CCCCCCCCCEEEECC		22.0524043423
267PhosphorylationPHSKYGCTFIGNQDT
CCCCCCEEEECCCCC		17.5824043423
270 (in isoform 2)Ubiquitination-22.8921890473
274PhosphorylationTFIGNQDTYETHLET
EEECCCCCCHHHHHH		17.3124043423
275PhosphorylationFIGNQDTYETHLETC
EECCCCCCHHHHHHH		27.4124043423
277PhosphorylationGNQDTYETHLETCRF
CCCCCCHHHHHHHCH		22.7324043423
281PhosphorylationTYETHLETCRFEGLK
CCHHHHHHHCHHHHH		18.4924043423
288 (in isoform 1)Ubiquitination-58.2221890473
288UbiquitinationTCRFEGLKEFLQQTD
HHCHHHHHHHHHHHC		58.2221906983
308UbiquitinationMHVALAQKDQEIAFL
HHHHHHHHHHHHHHH		56.63-
317PhosphorylationQEIAFLRSMLGKLSE
HHHHHHHHHHHHHHH		22.1027174698
321UbiquitinationFLRSMLGKLSEKIDQ
HHHHHHHHHHHHHHH		44.90-
323PhosphorylationRSMLGKLSEKIDQLE
HHHHHHHHHHHHHHH		40.0927174698
325UbiquitinationMLGKLSEKIDQLEKS
HHHHHHHHHHHHHHH		48.48-
331UbiquitinationEKIDQLEKSLELKFD
HHHHHHHHHHHHCEE		69.7721890473
331 (in isoform 1)Ubiquitination-69.7721890473
332PhosphorylationKIDQLEKSLELKFDV
HHHHHHHHHHHCEEC		20.0825690035
346UbiquitinationVLDENQSKLSEDLME
CCCCCHHHHCHHHHH		46.392190698
346 (in isoform 1)Ubiquitination-46.3921890473
359PhosphorylationMEFRRDASMLNDELS
HHHHHHHHHHHHHHH		28.2628555341
387MethylationYDPQQIFKCKGTFVG
CCHHHHEEEECEECC		36.3482994029
387UbiquitinationYDPQQIFKCKGTFVG
CCHHHHEEEECEECC		36.34-
430UbiquitinationWDTCTTYKCQKTLEG
EEECCCCCCCHHHCC		28.26-
484PhosphorylationAHDNPVCTLVSSHNV
CCCCCCEEEECCCCE		30.3522210691
511UbiquitinationDIVGTELKLKKELTG
EEECCEEECCHHHHC		52.61-
517PhosphorylationLKLKKELTGLNHWVR
EECCHHHHCCHHHHH		40.49-
629PhosphorylationDRSLRVWSMDNMICT
CCCCCEEEECCCCHH		17.2524043423
636PhosphorylationSMDNMICTQTLLRHQ
EECCCCHHHHHHHCC		17.4224043423
658PhosphorylationVSRGRLFSGAVDSTV
EECCCCCCCCCCCEE		30.3623312004
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 TRAF7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRAF7_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 TRAF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K3_HUMANMAP3K3physical
15001576
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 TRAF7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-105, 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-88 AND SER-91, AND MASSSPECTROMETRY.

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