Search by BoMiProt ID - Bomi5385


Primary Information

BoMiProt ID Bomi5385
Protein Name E3 ubiquitin-protein ligase TRIM11/RING-type E3 ubiquitin transferase TRIM11/Tripartite motif-containing protein 11
Organism Bos taurus
Uniprot IdA0JN74
Milk FractionWhey,MFGM
Ref Sequence Id NP_001071388.1
Aminoacid Length 468
Molecular Weight 52947
Fasta Sequence https://www.uniprot.org/uniprot/A0JN74.fasta
Gene Name TRIM11
Gene Id 514580
Protein Existence Status reviewed

Secondary Information

Protein Function TRIM11 binds to both the proteasome and USP14, a deubiquitinase that prematurely removes ubiquitins from proteasome-bound substrates and also noncatalytically inhibits the proteasome, and precludes their association, thereby increasing proteasome activity.enhances degradation of aberrant and normal regulatory proteins, and augments overall rate of proteolysis. 
Biochemical Properties characterized by an N-terminal TRIM/RBCC motif comprising a RING domain, one or two B-Boxes, and a predicted coiled-coil region, which is followed by a more diverse C-terminal region. RING domain is required for interaction with USP14.composed of a C-terminal PRY-SPRY (PS) motif.
PTMs phosphorylation on Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A0JN74|TRI11_BOVIN E3 ubiquitin-protein ligase TRIM11 OS=Bos taurus OX=9913 GN=TRIM11 PE=2 SV=1 MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELF PQRNLRPNRPLAKMAEMARRLHPPS*85PVPQGVCAAHREPLAAFCGDELRLLCAACERSGEH WAHRVRPLQDAAEDLKSKLEKSLEHLRKQMEDALLFQAQAEETCSLWQKMVETQRQNVLT EFERLRRLLVEEEQLLLQRLEEEELEVLPPLRESAARLGQQSAQLAELITELEGRCQLPA LGLLQDIRDTLRRVQDVKLQPPEVVPMEMRTVCRVPGLVEALRRFRGDMTLDPDTANPEL VLSEDRRSVRRGDLRQALPDSPERFDPGPCVLGREPLTSGRHYWEVEVGERASWALGVCR ENANRKEKGELFAGNGFWILVFLGSYYNSSERAFAPLRDPPRRVGIFLDYEAGHLSFYSA NDGSLLYTFPETPFSGTLRALFSPLSSSPTPMTICRLKGGPGDGLAPQ
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction no TM helices
Additional Comments promotes cell survival and is upregulated upon heat shock.upregulation of TRIM11 and other TRIMs may contribute to an enhanced cellular capacity to remove misfolded proteins in tumor cell.
Bibliography Chen L, Zhu G, Johns EM, Yang X. TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14. Nat Commun. 2018 Mar 26;9(1):1223. doi: 10.1038/s41467-018-03499-z. PMID: 29581427; PMCID: PMC5964324.