TRIM25
entrez
7706
canonical
uniprot
Q14258
canonical
ensembl
ENSG00000121060
resolver
ensp
ENSP00000323889
resolver
ensp
ENSP00000445961
resolver
enst
ENST00000316881
resolver
enst
ENST00000537230
resolver
genesymbol
TRIM25
resolver
genesymbol_syn
EFP
resolver
genesymbol_syn
RNF147
resolver
genesymbol_syn
ZNF147
resolver
hgnc
HGNC:12932
resolver
uniprot_entry
TRI25_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: RING domain dimerization is required for catalysis, TRIM25-mediated RIG-I ubiquitination, interferon induction, and antiviral activity. {ECO:0000269|PubMed:27425606}.
uniprot
proteins
amino_acid_sequence
MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
ec_number
6.3.2.n3
uniprot
proteins
function
FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase (PubMed:16352599). Involved in innate immune defense against viruses by mediating ubiquitination of RIGI and IFIH1 (PubMed:17392790, PubMed:29357390, PubMed:30193849, PubMed:31710640, PubMed:33849980, PubMed:36045682, PubMed:40719442). Mediates 'Lys-63'-linked polyubiquitination of the RIGI N-terminal CARD-like region and may play a role in signal transduction that leads to the production of interferons in response to viral infection (PubMed:17392790, PubMed:23950712). Mediates 'Lys-63'-linked polyubiquitination of IFIH1 (PubMed:30193849). Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway (PubMed:16352599, PubMed:17069755). Mediates estrogen action in various target organs (PubMed:22452784). Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3 (PubMed:22452784). Plays a role in promoting the restart of stalled replication forks via interaction with the KHDC3L-OOEP scaffold and subsequent ubiquitination of BLM, resulting in the recruitment and retainment of BLM at DNA replication forks (By similarity). Plays an essential role in the antiviral activity of ZAP/ZC3HAV1; an antiviral protein which inhibits the replication of certain viruses. Mechanistically, mediates 'Lys-63'-linked polyubiquitination of ZAP/ZC3HAV1 that is required for its optimal binding to target mRNA (PubMed:28060952, PubMed:28202764). Also mediates the ubiquitination of various substrates implicated in stress granule formation, nonsense-mediated mRNA decay, nucleoside synthesis and mRNA translation and stability (PubMed:36067236). Participates in autophagy suppression by ubiquitinating and degrading p62/SQSTM1 (PubMed:40542578). {ECO:0000250|UniProtKB:Q61510, ECO:0000269|PubMed:16352599, ECO:0000269|PubMed:17069755, ECO:0000269|PubMed:17392790, ECO:0000269|PubMed:22452784, ECO:0000269|PubMed:23950712, ECO:0000269|PubMed:29357390, ECO:0000269|PubMed:30193849, ECO:0000269|PubMed:31710640, ECO:0000269|PubMed:33849980, ECO:0000269|PubMed:36045682, ECO:0000269|PubMed:36067236, ECO:0000269|PubMed:40542578}.
uniprot
proteins
mass_dalton
70973
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="E->A: E3 ubiquitin ligase dead mutant; when associated with A-10."; /evidence="ECO:0000269|PubMed:40542578"; MUTAGEN 10; /note="E->A: E3 ubiquitin ligase dead mutant; when associated with A-9."; /evidence="ECO:0000269|PubMed:40542578"; MUTAGEN 21; /note="K->R: No effect on ISGylation."; /evidence="ECO:0000269|PubMed:17222803"; MUTAGEN 50; /note="C->S: Almost complete loss of ZAP/ZC3HAV1 ubiquitination; when associated with S-53."; /evidence="ECO:0000269|PubMed:28202764"; MUTAGEN 53; /note="C->S: Almost complete loss of ZAP/ZC3HAV1 ubiquitination; when associated with S-50."; /evidence="ECO:0000269|PubMed:28202764"; MUTAGEN 54; /note="R->P: Complete loss of viral inhibition independently of the host interferon response."; /evidence="ECO:0000269|PubMed:36067236"; MUTAGEN 65; /note="K->A: Almost complete loss of ubiquitination activity."; /evidence="ECO:0000269|PubMed:27425606"; MUTAGEN 65; /note="K->R: No effect on ISGylation."; /evidence="ECO:0000269|PubMed:17222803"; MUTAGEN 71; /note="N->D: Almost complete loss of ubiquitination activity."; /evidence="ECO:0000269|PubMed:27425606"; MUTAGEN 112; /note="K->R: No effect on ISGylation."; /evidence="ECO:0000269|PubMed:17222803"; MUTAGEN 117; /note="K->R: No ISGylation."; /evidence="ECO:0000269|PubMed:17222803
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Auto-ISGylated. {ECO:0000269|PubMed:17222803}.; PTM: (Microbial infection) Autoubiquitinated; promoted by Epstein-Barr virus protein BPLF1. {ECO:0000269|PubMed:29357390, ECO:0000269|PubMed:31710640}.
uniprot
proteins
pubmed
15130519
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16352599
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17069755
uniprot
proteins
pubmed
17222803
uniprot
proteins
pubmed
17392790
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19454348
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22452784
uniprot
proteins
pubmed
22607805
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23950712
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24478431
uniprot
proteins
pubmed
27154206
uniprot
proteins
pubmed
27425606
uniprot
proteins
pubmed
28060952
uniprot
proteins
pubmed
28202764
uniprot
proteins
pubmed
29321315
uniprot
proteins
pubmed
29357390
uniprot
proteins
pubmed
30193849
uniprot
proteins
pubmed
30558248
uniprot
proteins
pubmed
30902577
uniprot
proteins
pubmed
31710640
uniprot
proteins
pubmed
33849980
uniprot
proteins
pubmed
34313226
uniprot
proteins
pubmed
36045682
uniprot
proteins
pubmed
36067236
uniprot
proteins
pubmed
40542578
uniprot
proteins
pubmed
40719442
uniprot
proteins
pubmed
8248217
uniprot
proteins
sequence_length
630
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17392790, ECO:0000269|PubMed:40542578, ECO:0000269|PubMed:40719442}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23950712}. Nucleus {ECO:0000250|UniProtKB:Q61510}.
uniprot
proteins