TRIM13
entrez
10206
canonical
uniprot
O60858
canonical
ensembl
ENSG00000204977
resolver
ensp
ENSP00000348299
resolver
ensp
ENSP00000367424
resolver
ensp
ENSP00000399206
resolver
ensp
ENSP00000412943
resolver
genesymbol
TRIM13
resolver
genesymbol_syn
LEU5
resolver
genesymbol_syn
RFP2
resolver
genesymbol_syn
RNF77
resolver
hgnc
HGNC:9976
resolver
uniprot
B2RB49
resolver
uniprot
Q5UBW0
resolver
uniprot
Q5W0U8
resolver
uniprot
Q5W0U9
resolver
uniprot
Q9BQ47
resolver
uniprot
Q9C021
resolver
uniprot_entry
TRI13_HUMAN
resolver
uniprot_sec
B2RB49
resolver
uniprot_sec
Q5UBW0
resolver
uniprot_sec
Q5W0U8
resolver
uniprot_sec
Q5W0U9
resolver
uniprot_sec
Q9BQ47
resolver
uniprot_sec
Q9C021
resolver
amino_acid_sequence
MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL
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 (PubMed:22178386). 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 (PubMed:28087809). Participates as well in T-cell receptor-mediated NF-kappa-B activation (PubMed:25088585). In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B (PubMed:25152375). {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25088585, ECO:0000269|PubMed:25152375, ECO:0000269|PubMed:28087809}.
uniprot
proteins
mass_dalton
46988
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="C->A: Absence of polyubiquitination. Stability of protein increased. No enhanced apoptosis on ionizing radiation induction. No ubiquitination of AKT1 or MDM2. Decreased p53/TP53 stability. No effect on induction of autophagy during ER stress."; /evidence="ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation. {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11264177
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
14499696
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17314412
uniprot
proteins
pubmed
21333377
uniprot
proteins
pubmed
22178386
uniprot
proteins
pubmed
25088585
uniprot
proteins
pubmed
25152375
uniprot
proteins
pubmed
28087809
uniprot
proteins
pubmed
9599022
uniprot
proteins
sequence_length
407
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25152375}; Single-pass membrane protein {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}. Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
uniprot
proteins
transmembrane_region
TRANSMEM 317..337; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins