TRI26_HUMAN - dbPTM
TRI26_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI26_HUMAN
UniProt AC Q12899
Protein Name Tripartite motif-containing protein 26
Gene Name TRIM26
Organism Homo sapiens (Human).
Sequence Length 539
Subcellular Localization Cytoplasm . Nucleus . Viral infection mediates TRIM26 nuclear translocation.
Protein Description E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs). Promotes nuclear IRF3 ubiquitination and proteasomal degradation. Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1..
Protein Sequence MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDVRPISGSRPVCPLCKKPFKKENIRPVWQLASLVENIERLKVDKGRQPGEVTREQQDAKLCERHREKLHYYCEDDGKLLCVMCRESREHRPHTAVLMEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAALKKLQDQRQYIVAEFEQGHQFLREREEHLLEQLAKLEQELTEGREKFKSRGVGELARLALVISELEGKAQQPAAELMQDTRDFLNRYPRKKFWVGKPIARVVKKKTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYTSLYKSAYLHPQQFDCEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGDGYDDWETDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTSPEAELFPALRPRRVGIALDYEGGTVTFTNAESQELIYTFTATFTRRLVPFLWLKWPGTRLLLRP
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
9PhosphorylationATSAPLRSLEEEVTC
CCCCCCCCCCHHHHH
48.0627251275
47PhosphorylationTTDVRPISGSRPVCP
CCCCEECCCCCCCCC
33.1425159151
49PhosphorylationDVRPISGSRPVCPLC
CCEECCCCCCCCCCC
26.9825159151
73PhosphorylationRPVWQLASLVENIER
CHHHHHHHHHHHHHH
41.3527251275
85UbiquitinationIERLKVDKGRQPGEV
HHHHCCCCCCCCCCC
60.01-
140UbiquitinationHTAVLMEKAAQPHRE
CHHHHHHHCCHHHHH
34.75-
148AcetylationAAQPHREKILNHLST
CCHHHHHHHHHHHHH
53.0725953088
148UbiquitinationAAQPHREKILNHLST
CCHHHHHHHHHHHHH
53.07-
154PhosphorylationEKILNHLSTLRRDRD
HHHHHHHHHHHHCHH
20.1827174698
155PhosphorylationKILNHLSTLRRDRDK
HHHHHHHHHHHCHHH
30.5527174698
162UbiquitinationTLRRDRDKIQGFQAK
HHHHCHHHHHCCHHH
37.51-
169UbiquitinationKIQGFQAKGEADILA
HHHCCHHHCHHHHHH
46.64-
179UbiquitinationADILAALKKLQDQRQ
HHHHHHHHHHHHHHH
46.8721890473
179UbiquitinationADILAALKKLQDQRQ
HHHHHHHHHHHHHHH
46.8721890473
180UbiquitinationDILAALKKLQDQRQY
HHHHHHHHHHHHHHH
52.83-
223UbiquitinationELTEGREKFKSRGVG
HHHHHHHHHHHCCHH
57.65-
245UbiquitinationVISELEGKAQQPAAE
HHHHHCCCCCCHHHH
33.3821890473
273UbiquitinationRKKFWVGKPIARVVK
HHHCCCCCCHHHHHH
24.51-
289UbiquitinationKTGEFSDKLLSLQRG
HHCCCHHHHHHHHHH
50.56-
289AcetylationKTGEFSDKLLSLQRG
HHCCCHHHHHHHHHH
50.5625953088
292PhosphorylationEFSDKLLSLQRGLRE
CCHHHHHHHHHHHHH
32.6524719451
303AcetylationGLREFQGKLLRDLEY
HHHHHHHHHHHCCEE
33.3020167786
310PhosphorylationKLLRDLEYKTVSVTL
HHHHCCEEEEEEEEE
21.1826270265
312PhosphorylationLRDLEYKTVSVTLDP
HHCCEEEEEEEEECC
19.6726270265
314PhosphorylationDLEYKTVSVTLDPQS
CCEEEEEEEEECCCC
18.0226270265
316PhosphorylationEYKTVSVTLDPQSAS
EEEEEEEEECCCCCC
20.2426270265
337PhosphorylationEDWKCVTYTSLYKSA
CCCEEEEHHHHHHHH
3.6429116813
341PhosphorylationCVTYTSLYKSAYLHP
EEEHHHHHHHHCCCH
11.5829116813
342UbiquitinationVTYTSLYKSAYLHPQ
EEHHHHHHHHCCCHH
33.62-
345PhosphorylationTSLYKSAYLHPQQFD
HHHHHHHCCCHHHCC
16.7827642862
361UbiquitinationEPGVLGSKGFTWGKV
CCCCCCCCCCCCEEE
57.13-
367UbiquitinationSKGFTWGKVYWEVEV
CCCCCCEEEEEEEEE
24.58-
369PhosphorylationGFTWGKVYWEVEVER
CCCCEEEEEEEEEEE
10.1919835603
449UbiquitinationARDSVKRKGDLSLRP
CHHHHHHCCCCCCCC
51.57-
453PhosphorylationVKRKGDLSLRPEDGV
HHHCCCCCCCCCCCE
27.3724719451
466PhosphorylationGVWALRLSSSGIWAN
CEEEEEEECCCCCCC
18.9428348404
467PhosphorylationVWALRLSSSGIWANT
EEEEEEECCCCCCCC
36.8628348404
468PhosphorylationWALRLSSSGIWANTS
EEEEEECCCCCCCCC
30.8128348404
474PhosphorylationSSGIWANTSPEAELF
CCCCCCCCCCHHHHC
37.6027251275
475PhosphorylationSGIWANTSPEAELFP
CCCCCCCCCHHHHCC
22.1327251275
499PhosphorylationALDYEGGTVTFTNAE
EEEECCCEEEEECCC
27.5130576142
503PhosphorylationEGGTVTFTNAESQEL
CCCEEEEECCCCCCE
24.9330576142
515PhosphorylationQELIYTFTATFTRRL
CCEEEEEEECCHHHC
19.5830576142
529UbiquitinationLVPFLWLKWPGTRLL
CCCCCEEECCCCEEE
39.50-

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 TRI26_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI26_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 TRI26_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI26_HUMANTRIM26physical
11331580
TRI26_HUMANTRIM26physical
22493164
TRI41_HUMANTRIM41physical
22493164
RN126_HUMANRNF126physical
22493164
PHF7_HUMANPHF7physical
22493164
RNF10_HUMANRNF10physical
22493164
THAP1_HUMANTHAP1physical
25416956
TOP1_HUMANTOP1physical
26496610
CSKP_HUMANCASKphysical
26496610
CHERP_HUMANCHERPphysical
26496610
CE162_HUMANCEP162physical
26496610
MTCH1_HUMANMTCH1physical
26496610
ARFG3_HUMANARFGAP3physical
26496610
PHF10_HUMANPHF10physical
26496610
EMSY_HUMANC11orf30physical
26496610
IRF3_HUMANIRF3physical
25763818
TBK1_HUMANTBK1physical
26611359
TRI26_HUMANTRIM26physical
26611359

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 TRI26_HUMAN

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Related Literatures of Post-Translational Modification

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