TRI11_HUMAN - dbPTM
TRI11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI11_HUMAN
UniProt AC Q96F44
Protein Name E3 ubiquitin-protein ligase TRIM11
Gene Name TRIM11
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Cytoplasm. Nucleus.
Protein Description E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle..
Protein Sequence MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
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
7Phosphorylation-MAAPDLSTNLQEEA
-CCCCCCCHHHHHHH
23.7224043423
8PhosphorylationMAAPDLSTNLQEEAT
CCCCCCCHHHHHHHH
47.4424043423
15PhosphorylationTNLQEEATCAICLDY
HHHHHHHHHHHHHHH
13.0224043423
22PhosphorylationTCAICLDYFTDPVMT
HHHHHHHHHCCCCCC
8.7424043423
24PhosphorylationAICLDYFTDPVMTDC
HHHHHHHCCCCCCCC
32.9124043423
29PhosphorylationYFTDPVMTDCGHNFC
HHCCCCCCCCCCCHH
28.5024043423
60PhosphorylationCPECRELSPQRNLRP
CHHHHHHCCCCCCCC
17.7726074081
73UbiquitinationRPNRPLAKMAEMARR
CCCCHHHHHHHHHHH
46.4532015554
85PhosphorylationARRLHPPSPVPQGVC
HHHHCCCCCCCCCCC
42.8723401153
136 (in isoform 2)Ubiquitination-56.6621906983
136 (in isoform 1)Ubiquitination-56.6621906983
136UbiquitinationQDAAEDLKAKLEKSL
HHHHHHHHHHHHHHH
56.6621906983
138UbiquitinationAAEDLKAKLEKSLEH
HHHHHHHHHHHHHHH
56.4422817900
141 (in isoform 2)Ubiquitination-71.43-
141UbiquitinationDLKAKLEKSLEHLRK
HHHHHHHHHHHHHHH
71.4329901268
142PhosphorylationLKAKLEKSLEHLRKQ
HHHHHHHHHHHHHHH
29.6121406692
163PhosphorylationFQAQADETCVLWQKM
HHHHCHHHHHHHHHH
14.4129978859
181UbiquitinationQRQNVLGEFERLRRL
HHHHHHHHHHHHHHH
39.9327667366
248 (in isoform 2)Ubiquitination-45.28-
248UbiquitinationLGLLQDIKDALRRVQ
HHHHHHHHHHHHHHH
45.28-
257UbiquitinationALRRVQDVKLQPPEV
HHHHHHCCCCCCCCC
3.5927667366
258 (in isoform 2)Ubiquitination-50.0921906983
258UbiquitinationLRRVQDVKLQPPEVV
HHHHHCCCCCCCCCC
50.0927667366
258 (in isoform 1)Ubiquitination-50.0921906983
281PhosphorylationRVPGLVETLRRFRGD
CCCCHHHHHHHHCCC
20.3421406692
286MethylationVETLRRFRGDVTLDP
HHHHHHHCCCCCCCC
38.29115918949
304 (in isoform 2)Ubiquitination-52.68-
308PhosphorylationILSEDRRSVQRGDLR
EECCCCCCCCCCCHH
24.40-
321PhosphorylationLRQALPDSPERFDPG
HHHHCCCCCCCCCCC
27.0721815630
458UbiquitinationPMTICRPKGGSGDTL
CEEEEECCCCCCCCC
57.4633845483

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 TRI11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI11_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 TRI11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI11_HUMANTRIM11physical
11331580
MED15_HUMANMED15physical
16904669
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UBE2N_HUMANUBE2Nphysical
21143188
HMN1_HUMANMTRNR2L1physical
12670303
TRI35_HUMANTRIM35physical
22493164
KKCC1_HUMANCAMKK1physical
28514442
RLF_HUMANRLFphysical
28514442
USF1_HUMANUSF1physical
28514442
RBG10_HUMANRABGAP1Lphysical
28514442
RBG1L_HUMANRABGAP1Lphysical
28514442
KS6A3_HUMANRPS6KA3physical
28514442
KDM3B_HUMANKDM3Bphysical
28514442
RBGP1_HUMANRABGAP1physical
28514442
LYPA1_HUMANLYPLA1physical
28514442
POGK_HUMANPOGKphysical
28514442
KS6A2_HUMANRPS6KA2physical
28514442
TBCE_HUMANTBCEphysical
28514442
RBPS2_HUMANRBPMS2physical
28514442
PUM1_HUMANPUM1physical
28514442
BT3A3_HUMANBTN3A3physical
28514442
BANP_HUMANBANPphysical
28514442
AAKB1_HUMANPRKAB1physical
28514442
SELO_HUMANSELOphysical
28514442
UBB_HUMANUBBphysical
28514442
AAKB2_HUMANPRKAB2physical
28514442
SEP10_HUMANSEPT10physical
28514442
VATF_HUMANATP6V1Fphysical
28514442
COIA1_HUMANCOL18A1physical
28514442
QKI_HUMANQKIphysical
28514442
AAKG1_HUMANPRKAG1physical
28514442
EHD4_HUMANEHD4physical
28514442
CREB1_HUMANCREB1physical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
UBE2N_HUMANUBE2Nphysical
27173435
GAG_HV1H2gagphysical
27737691

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 TRI11_HUMAN

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Related Literatures of Post-Translational Modification

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