TRI38_HUMAN - dbPTM
TRI38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI38_HUMAN
UniProt AC O00635
Protein Name E3 ubiquitin-protein ligase TRIM38
Gene Name TRIM38
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase. Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling..
Protein Sequence MASTTSTKKMMEEATCSICLSLMTNPVSINCGHSYCHLCITDFFKNPSQKQLRQETFCCPQCRAPFHMDSLRPNKQLGSLIEALKETDQEMSCEEHGEQFHLFCEDEGQLICWRCERAPQHKGHTTALVEDVCQGYKEKLQKAVTKLKQLEDRCTEQKLSTAMRITKWKEKVQIQRQKIRSDFKNLQCFLHEEEKSYLWRLEKEEQQTLSRLRDYEAGLGLKSNELKSHILELEEKCQGSAQKLLQNVNDTLSRSWAVKLETSEAVSLELHTMCNVSKLYFDVKKMLRSHQVSVTLDPDTAHHELILSEDRRQVTRGYTQENQDTSSRRFTAFPCVLGCEGFTSGRRYFEVDVGEGTGWDLGVCMENVQRGTGMKQEPQSGFWTLRLCKKKGYVALTSPPTSLHLHEQPLLVGIFLDYEAGVVSFYNGNTGCHIFTFPKASFSDTLRPYFQVYQYSPLFLPPPGD
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
3Phosphorylation-----MASTTSTKKM
-----CCCCHHHHHH
30.8029759185
50UbiquitinationFFKNPSQKQLRQETF
HHHCHHHHHHHHHEE
56.49-
70PhosphorylationRAPFHMDSLRPNKQL
CCCCCHHHCCCCHHH
20.7830108239
75UbiquitinationMDSLRPNKQLGSLIE
HHHCCCCHHHHHHHH
49.97-
122UbiquitinationCERAPQHKGHTTALV
EECCCCCCCCCHHHH
47.33-
125PhosphorylationAPQHKGHTTALVEDV
CCCCCCCCHHHHHHH
23.5625072903
126PhosphorylationPQHKGHTTALVEDVC
CCCCCCCHHHHHHHH
16.6025072903
136PhosphorylationVEDVCQGYKEKLQKA
HHHHHHHHHHHHHHH
7.0625072903
137UbiquitinationEDVCQGYKEKLQKAV
HHHHHHHHHHHHHHH
56.02-
139UbiquitinationVCQGYKEKLQKAVTK
HHHHHHHHHHHHHHH
52.66-
142UbiquitinationGYKEKLQKAVTKLKQ
HHHHHHHHHHHHHHH
56.09-
142AcetylationGYKEKLQKAVTKLKQ
HHHHHHHHHHHHHHH
56.0925953088
148UbiquitinationQKAVTKLKQLEDRCT
HHHHHHHHHHHHHHH
55.16-
155O-linked_GlycosylationKQLEDRCTEQKLSTA
HHHHHHHHHHHHHHH
42.2030379171
158UbiquitinationEDRCTEQKLSTAMRI
HHHHHHHHHHHHHHH
37.87-
158AcetylationEDRCTEQKLSTAMRI
HHHHHHHHHHHHHHH
37.8726051181
160PhosphorylationRCTEQKLSTAMRITK
HHHHHHHHHHHHHHH
22.5822210691
161PhosphorylationCTEQKLSTAMRITKW
HHHHHHHHHHHHHHH
34.6022210691
167AcetylationSTAMRITKWKEKVQI
HHHHHHHHHHHHHHH
54.6320167786
171UbiquitinationRITKWKEKVQIQRQK
HHHHHHHHHHHHHHH
35.39-
184MalonylationQKIRSDFKNLQCFLH
HHHHHHHHHCEEEEC
62.8326320211
184AcetylationQKIRSDFKNLQCFLH
HHHHHHHHHCEEEEC
62.8325953088
184UbiquitinationQKIRSDFKNLQCFLH
HHHHHHHHHCEEEEC
62.83-
195UbiquitinationCFLHEEEKSYLWRLE
EEECHHHHHHHHHCC
47.91-
203UbiquitinationSYLWRLEKEEQQTLS
HHHHHCCHHHHHHHH
71.75-
215PhosphorylationTLSRLRDYEAGLGLK
HHHHHHHHHHCCCCC
10.9727642862
222UbiquitinationYEAGLGLKSNELKSH
HHHCCCCCHHHHHHH
49.81-
227UbiquitinationGLKSNELKSHILELE
CCCHHHHHHHHHHHH
33.53-
236UbiquitinationHILELEEKCQGSAQK
HHHHHHHHHCHHHHH
23.60-
243UbiquitinationKCQGSAQKLLQNVND
HHCHHHHHHHHHHHH
51.38-
251PhosphorylationLLQNVNDTLSRSWAV
HHHHHHHHCHHHHEE
22.7928857561
280PhosphorylationMCNVSKLYFDVKKML
HHCHHHHHHHHHHHH
11.0626307563
284UbiquitinationSKLYFDVKKMLRSHQ
HHHHHHHHHHHHHCC
34.02-
285UbiquitinationKLYFDVKKMLRSHQV
HHHHHHHHHHHHCCC
42.91-
319PhosphorylationRQVTRGYTQENQDTS
CHHHCCCCCCCCCCC
32.03-
343PhosphorylationVLGCEGFTSGRRYFE
EEECCCCCCCCEEEE
40.9222210691
344PhosphorylationLGCEGFTSGRRYFEV
EECCCCCCCCEEEEE
28.2122210691
375UbiquitinationVQRGTGMKQEPQSGF
CCCCCCCCCCCCCCC
53.51-

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
-KUbiquitinationE3 ubiquitin ligaseTRIM38O00635
PMID:21306652

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI38_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 TRI38_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
UB2D4_HUMANUBE2D4physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UB2E2_HUMANUBE2E2physical
21143188
UB2E3_HUMANUBE2E3physical
21143188
TRAF6_HUMANTRAF6physical
22323536
TAB2_HUMANTAB2physical
24434549
TAB3_HUMANTAB3physical
24434549
TRI38_HUMANTRIM38physical
25416956
TSYL4_HUMANTSPYL4physical
25416956
GORS2_HUMANGORASP2physical
25416956
GMCL1_HUMANGMCL1physical
25416956
AZI2_HUMANAZI2physical
22539786

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 TRI38_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP