Trim13
entrez
66597
canonical
uniprot
Q9CYB0
canonical
ensembl
ENSMUSG00000035235
resolver
ensp
ENSMUSP00000045009
resolver
ensp
ENSMUSP00000128509
resolver
ensp
ENSMUSP00000344460
resolver
enst
ENSMUST00000039562
resolver
enst
ENSMUST00000165015
resolver
genesymbol
Trim13
resolver
genesymbol_syn
Rfp2
resolver
uniprot
A6H6L2
resolver
uniprot
Q3TSD2
resolver
uniprot
Q8CEV0
resolver
uniprot
Q923J0
resolver
uniprot
Q925P1
resolver
uniprot
Q99PQ0
resolver
uniprot_entry
Q3TSD2_MOUSE
resolver
uniprot_entry
TRI13_MOUSE
resolver
uniprot_sec
A6H6L2
resolver
uniprot_sec
Q8CEV0
resolver
uniprot_sec
Q923J0
resolver
uniprot_sec
Q925P1
resolver
uniprot_sec
Q99PQ0
resolver
amino_acid_sequence
MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCVTDMQLICGICATRGEHTKHVFSSIEDAYAREKNAFESLFQSFETWRRGDALSRLDTLETNKRKALQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKINTILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPHSNLPTSPLMKNFDTSQWGDIKLVDVDKLSLPQDTGVFTSKIPWYPYLLLMMVVLLGLLIFFGPTVFLEWSPLDELATWKDYLSSFNSYLTKSADFIEQSVFYWEQMTDGFFIFGERVKNVSLVALNNVAEFICKYKLL
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B. {ECO:0000250|UniProtKB:O60858}.
uniprot
proteins
mass_dalton
46958
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:O60858}.
uniprot
proteins
post_translational_modification
PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation. {ECO:0000250|UniProtKB:O60858}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11161783
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
sequence_length
407
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60858}; Single-pass membrane protein {ECO:0000250|UniProtKB:O60858}. Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum. {ECO:0000250|UniProtKB:O60858}.
uniprot
proteins
transmembrane_region
TRANSMEM 316..336; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins