TRAIP_HUMAN - dbPTM
TRAIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRAIP_HUMAN
UniProt AC Q9BWF2
Protein Name E3 ubiquitin-protein ligase TRAIP
Gene Name TRAIP
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Nucleus . Nucleus, nucleolus . In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci. After UV irradiation, rapidly localizes to sites of DNA damage, where it colocaliz
Protein Description E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity). [PubMed: 22945920 Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV-induced replication-blocking lesions during S phase]
Protein Sequence MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS
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
73UbiquitinationLAQEEENVLDAEFLK
HHHHHHCCCCHHHHH		6.0621963094
80SumoylationVLDAEFLKNELDNVR
CCCHHHHHHHHHHHH		54.41-
80SumoylationVLDAEFLKNELDNVR
CCCHHHHHHHHHHHH		54.41-
93UbiquitinationVRAQLSQKDKEKRDS
HHHHHHHHHHHHHHH		68.3529967540
97UbiquitinationLSQKDKEKRDSQVII
HHHHHHHHHHHHHHH		68.2129967540
117PhosphorylationTLEERNATVVSLQQA
HHHHCCCHHHHHHHH		25.6230622161
120PhosphorylationERNATVVSLQQALGK
HCCCHHHHHHHHHHH		19.0030622161
127SumoylationSLQQALGKAEMLCST
HHHHHHHHHHHHHHH		41.86-
127SumoylationSLQQALGKAEMLCST
HHHHHHHHHHHHHHH		41.86-
128UbiquitinationLQQALGKAEMLCSTL
HHHHHHHHHHHHHHH		12.9622817900
129UbiquitinationQQALGKAEMLCSTLK
HHHHHHHHHHHHHHH		35.8522817900
140UbiquitinationSTLKKQMKYLEQQQD
HHHHHHHHHHHHHHH		44.16-
149PhosphorylationLEQQQDETKQAQEEA
HHHHHHHHHHHHHHH		36.4230619164
150UbiquitinationEQQQDETKQAQEEAR
HHHHHHHHHHHHHHH		41.4021906983
165PhosphorylationRLRSKMKTMEQIELL
HHHHHHHHHHHHHHH		23.5722210691
175PhosphorylationQIELLLQSQRPEVEE
HHHHHHHCCCHHHHH		28.2922210691
200PhosphorylationAVEQLAVYCVSLKKE
HHHHHHHHHHHHHHH		4.9827251275
203PhosphorylationQLAVYCVSLKKEYEN
HHHHHHHHHHHHHHH		30.8027251275
205SumoylationAVYCVSLKKEYENLK
HHHHHHHHHHHHHHH		35.73-
205UbiquitinationAVYCVSLKKEYENLK
HHHHHHHHHHHHHHH		35.7322817900
205SumoylationAVYCVSLKKEYENLK
HHHHHHHHHHHHHHH		35.73-
206UbiquitinationVYCVSLKKEYENLKE
HHHHHHHHHHHHHHH		71.4722817900
208PhosphorylationCVSLKKEYENLKEAR
HHHHHHHHHHHHHHH		20.9927251275
231PhosphorylationKLRKDLFSSRSKLQT
HHHHHHHCCHHHHHH		31.9429083192
232PhosphorylationLRKDLFSSRSKLQTV
HHHHHHCCHHHHHHH		32.9929083192
234PhosphorylationKDLFSSRSKLQTVYS
HHHHCCHHHHHHHHH		39.4020860994
235UbiquitinationDLFSSRSKLQTVYSE
HHHCCHHHHHHHHHH		43.4329967540
238PhosphorylationSSRSKLQTVYSELDQ
CCHHHHHHHHHHHHH		31.6720860994
240PhosphorylationRSKLQTVYSELDQAK
HHHHHHHHHHHHHHH		10.3820860994
247SumoylationYSELDQAKLELKSAQ
HHHHHHHHHHHHHHH		36.54-
247SumoylationYSELDQAKLELKSAQ
HHHHHHHHHHHHHHH		36.54-
247UbiquitinationYSELDQAKLELKSAQ
HHHHHHHHHHHHHHH		36.5429967540
259PhosphorylationSAQKDLQSADKEIMS
HHHHHHHHHHHHHHH		45.8122817900
266O-linked_GlycosylationSADKEIMSLKKKLTM
HHHHHHHHHHHHHHH		42.5730379171
269UbiquitinationKEIMSLKKKLTMLQE
HHHHHHHHHHHHHHH		59.31-
272PhosphorylationMSLKKKLTMLQETLN
HHHHHHHHHHHHHHC		25.3922210691
277PhosphorylationKLTMLQETLNLPPVA
HHHHHHHHHCCCCCC		14.1622210691
295PhosphorylationVDRLVLESPAPVEVN
HCEEEECCCCCEEEE		23.3830266825
304SumoylationAPVEVNLKLRRPSFR
CCEEEEEEECCCCCC		34.4428112733
345PhosphorylationEKLCLEKSHSPIQDV
HHHHCCCCCCCCCCC		21.5930266825
347PhosphorylationLCLEKSHSPIQDVPK
HHCCCCCCCCCCCCH		30.6830266825
362UbiquitinationKICKGPRKESQLSLG
HHCCCCCCHHCEECC		65.92-
364PhosphorylationCKGPRKESQLSLGGQ
CCCCCCHHCEECCCC		39.18-
397UbiquitinationRNAILGQKQPKRPRS
HHHHHCCCCCCCCCC		67.7629967540
410UbiquitinationRSESSCSKDVVRTGF
CCCCCCCCHHHHHCC		59.89-
430PhosphorylationRTKFIQPTDTVMIRP
CCEEECCCCEEEEEE		28.1129449344
432PhosphorylationKFIQPTDTVMIRPLP
EEECCCCEEEEEECC		17.9129449344
453SumoylationVKQRVRVKTVPSLFQ
CCCCEEEECCCHHHH		32.99-
453SumoylationVKQRVRVKTVPSLFQ
CCCCEEEECCCHHHH		32.99-
454PhosphorylationKQRVRVKTVPSLFQA
CCCEEEECCCHHHHH		34.4928555341
454O-linked_GlycosylationKQRVRVKTVPSLFQA
CCCEEEECCCHHHHH		34.4930379171
462SumoylationVPSLFQAKLDTFLWS
CCHHHHHHHHHHCCC		35.79-
462SumoylationVPSLFQAKLDTFLWS
CCHHHHHHHHHHCCC		35.79-
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 TRAIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRAIP_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 TRAIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLII_HUMANFLIIphysical
9671805
TRAF1_HUMANTRAF1physical
9104814
TRAF2_HUMANTRAF2physical
9104814
TRAIP_HUMANTRAIPphysical
17544371
TRAF1_HUMANTRAF1physical
17544371
TRAF2_HUMANTRAF2physical
17544371
TRAF3_HUMANTRAF3physical
17544371
TRAF5_HUMANTRAF5physical
17544371
TRAF6_HUMANTRAF6physical
17544371
TBK1_HUMANTBK1physical
22945920
TRAF3_HUMANTRAF3physical
22945920
KSYK_HUMANSYKphysical
19151749
UB2D1_HUMANUBE2D1physical
17544371
UB2D2_HUMANUBE2D2physical
17544371
UB2D3_HUMANUBE2D3physical
17544371
A4_HUMANAPPphysical
21832049
RN114_HUMANRNF114physical
22493164
TRI41_HUMANTRIM41physical
22493164
RNF37_HUMANUBOX5physical
22493164
POLH_HUMANPOLHphysical
24553286
POLK_HUMANPOLKphysical
24553286
MARE2_HUMANMAPRE2physical
25416956
TRAIP_HUMANTRAIPphysical
26093298
M3K7_HUMANMAP3K7physical
27847407
UIMC1_HUMANUIMC1physical
26781088
BRE1A_HUMANRNF20physical
26781088
BRE1B_HUMANRNF40physical
26781088
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 TRAIP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.

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