TRIM27
entrez
5987
canonical
uniprot
P14373
canonical
ensembl
ENSG00000204713
resolver
ensembl
ENSG00000215641
resolver
ensembl
ENSG00000229006
resolver
ensembl
ENSG00000234495
resolver
ensembl
ENSG00000237071
resolver
ensp
ENSP00000366404
resolver
genesymbol
TRIM27
resolver
genesymbol_syn
RFP
resolver
genesymbol_syn
RNF76
resolver
hgnc
HGNC:9975
resolver
uniprot
A2BE15
resolver
uniprot
Q5RJA8
resolver
uniprot
Q5ST26
resolver
uniprot
Q6LA73
resolver
uniprot
Q6NXR9
resolver
uniprot
Q9BZY6
resolver
uniprot
Q9UJL3
resolver
uniprot_entry
TRI27_HUMAN
resolver
uniprot_sec
A2BE15
resolver
uniprot_sec
Q5RJA8
resolver
uniprot_sec
Q5ST26
resolver
uniprot_sec
Q6LA73
resolver
uniprot_sec
Q6NXR9
resolver
uniprot_sec
Q9BZY6
resolver
uniprot_sec
Q9UJL3
resolver
amino_acid_sequence
MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving TRIM27/RFP is found in papillary thyroid carcinomas (PTCs). Translocation t(6;10)(p21.3;q11.2) with RET. The translocation generates TRIM27/RET and delta TRIM27/RET oncogenes. {ECO:0000269|PubMed:12787916, ECO:0000269|PubMed:3037315}.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of various substrates and thereby plays a role in diffent processes including proliferation, innate immunity, apoptosis, immune response or autophagy (PubMed:22829933, PubMed:24144979, PubMed:29688809, PubMed:36111389). Ubiquitinates PIK3C2B and inhibits its activity by mediating the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853). Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. Forms a complex with and ubiquitinates the ubiquitin-specific protease USP7, which in turn deubiquitinates RIPK1 resulting in the positive regulation of TNF-induced apoptosis (PubMed:24144979). In addition, acts with USP7 or PTPN11 as an inhibitor of the antiviral signaling pathway by promoting kinase TBK1 ubiquitination and degradation (PubMed:26358190, PubMed:29688809). Acts as a negative regulator of NOD2 signaling by mediating ubiquitination of NOD2, promoting its degradation by the proteasome (PubMed:22829933). Alternatively, facilitates mitophagy via stabilization of active TBK1 (PubMed:36111389). Negatively regulates autophagy flux under basal conditions by directly polyubiquitinating ULK1 (PubMed:35670107). During starvation-induced autophagy, catalyzes non-degradative ubiquitination of the kinase STK38L promoting its activation and phosphorylation of ULK1 leading to its ubiquitination and degradation to restrain the amplitude and duration of autophagy (PubMed:35670107). {ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:22829933, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:24144979, ECO:0000269|PubMed:26358190, ECO:0000269|PubMed:29688809, ECO:0000269|PubMed:35670107, ECO:0000269|PubMed:36111389}.; FUNCTION: (Microbial infection) Positively regulates hepatitis C virus replication by suppressing type I IFN response during infection. {ECO:0000269|PubMed:29688809}.
uniprot
proteins
mass_dalton
58490
uniprot
proteins
mutagenesis
MUTAGEN 16; /note="C->A: Abolished E3 ubiquitin-protein ligase activity; when associated with A-31."; /evidence="ECO:0000269|PubMed:22829933"; MUTAGEN 31; /note="C->A: Abolished E3 ubiquitin-protein ligase activity; when associated with A-16."; /evidence="ECO:0000269|PubMed:22829933
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:22829933, ECO:0000269|PubMed:26358190, ECO:0000269|PubMed:35670107}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
10504338
uniprot
proteins
pubmed
10976108
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
12445133
uniprot
proteins
pubmed
12787916
uniprot
proteins
pubmed
12807881
uniprot
proteins
pubmed
1437549
uniprot
proteins
pubmed
14530259
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15837424
uniprot
proteins
pubmed
17156811
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20864041
uniprot
proteins
pubmed
22128329
uniprot
proteins
pubmed
22829933
uniprot
proteins
pubmed
23452853
uniprot
proteins
pubmed
24144979
uniprot
proteins
pubmed
25320289
uniprot
proteins
pubmed
26358190
uniprot
proteins
pubmed
26365382
uniprot
proteins
pubmed
27698396
uniprot
proteins
pubmed
29688809
uniprot
proteins
pubmed
3037315
uniprot
proteins
pubmed
30847745
uniprot
proteins
pubmed
3380101
uniprot
proteins
pubmed
35670107
uniprot
proteins
pubmed
36111389
uniprot
proteins
pubmed
9247190
uniprot
proteins
pubmed
9570750
uniprot
proteins
sequence_length
513
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17156811}. Cytoplasm {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:36111389}. Nucleus, PML body {ECO:0000250}. Early endosome {ECO:0000269|PubMed:1437549, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:9247190}. Mitochondrion {ECO:0000269|PubMed:24144979}. Note=Nuclear or cytoplasmic depending on the cell type (By similarity). Colocalized with PML and EIF3S6 in nuclear bodies. Recruited to retromer-containing endosomes via interaction with MAGEL2 (PubMed:23452853). Co-localizes with p62/SQSTM1 and TBK1 in cytoplasmic structures that are closely associated with the mitochondria (PubMed:36111389). {ECO:0000250, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:36111389}.
uniprot
proteins