TRIM7
entrez
81786
canonical
uniprot
Q9C029
canonical
ensembl
ENSG00000146054
resolver
ensp
ENSP00000274773
resolver
ensp
ENSP00000334666
resolver
ensp
ENSP00000376991
resolver
ensp
ENSP00000376994
resolver
ensp
ENSP00000391458
resolver
genesymbol
TRIM7
resolver
genesymbol_syn
GNIP
resolver
genesymbol_syn
RNF90
resolver
hgnc
HGNC:16278
resolver
uniprot
A2RUE4
resolver
uniprot
D3DWR7
resolver
uniprot
Q969F5
resolver
uniprot
Q96F67
resolver
uniprot
Q96J89
resolver
uniprot
Q96J90
resolver
uniprot_entry
TRIM7_HUMAN
resolver
uniprot_sec
A2RUE4
resolver
uniprot_sec
D3DWR7
resolver
uniprot_sec
Q969F5
resolver
uniprot_sec
Q96F67
resolver
uniprot_sec
Q96J89
resolver
uniprot_sec
Q96J90
resolver
amino_acid_sequence
MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration (PubMed:25851810, PubMed:32853985, PubMed:34062120). Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and NSP8 proteins (PubMed:34062120, PubMed:35982226). Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation (PubMed:35867826, PubMed:35893676, PubMed:35982226). Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (PubMed:25851810). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (By similarity). Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation (PubMed:32126128). Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1 (PubMed:32853985). Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation (PubMed:36067704). {ECO:0000250|UniProtKB:Q923T7, ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:32126128, ECO:0000269|PubMed:32853985, ECO:0000269|PubMed:34062120, ECO:0000269|PubMed:35867826, ECO:0000269|PubMed:35893676, ECO:0000269|PubMed:35982226, ECO:0000269|PubMed:36067704}.; FUNCTION: (Microbial infection) Promotes Zika virus replication by mediating envelope protein E ubiquitination. {ECO:0000269|PubMed:32641828}.
uniprot
proteins
mass_dalton
56631
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="C->A: Abolishes ubiquitination and stabilization of RNF187; when associated with A-32."; /evidence="ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:36067704"; MUTAGEN 32; /note="C->A: Abolishes ubiquitination and stabilization of RNF187; when associated with A-29."; /evidence="ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:36067704"; MUTAGEN 57; /note="W->A: Abolishes ubiquitination and stabilization of RNF187."; /evidence="ECO:0000269|PubMed:25851810"; MUTAGEN 107; /note="S->A: Abolishes phosphorylation by RPS6KA5/MSK1. Reduced ubiquitination activity towards RNF187."; /evidence="ECO:0000269|PubMed:25851810"; MUTAGEN 383; /note="N->A: Complete loss of substrate binding."; /evidence="ECO:0000269|PubMed:35893676"; MUTAGEN 385; /note="R->A: Complete loss of substrate binding."; /evidence="ECO:0000269|PubMed:35893676"; MUTAGEN 423; /note="L->A: Complete loss of interaction with GYG1."; /evidence="ECO:0000269|PubMed:33989636"; MUTAGEN 426; /note="F->A: Complete loss of substrate binding."; /evidence="ECO:0000269|PubMed:35893676"; MUTAGEN 436; /note="Q->A: Complete loss of substrate binding."; /evidence="ECO:0000269|PubMed:35893676"; MUTAGEN 499; /note="S->A: Complete loss of interaction with GYG1."; /evidence="ECO:0000269|PubMed:33989636"; MUTAGEN 501; /note="C->A: Complete loss of interaction with GYG1."; /evidence="ECO:0000269|PubMed:33989636
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:25851810}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-107 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity. {ECO:0000269|PubMed:25851810}.; PTM: Auto-ubiquitinates via 'Lys-63'-linked polyubiquitination. {ECO:0000269|PubMed:35893676}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
11916970
uniprot
proteins
pubmed
14984203
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
25851810
uniprot
proteins
pubmed
32126128
uniprot
proteins
pubmed
32641828
uniprot
proteins
pubmed
32853985
uniprot
proteins
pubmed
33989636
uniprot
proteins
pubmed
34062120
uniprot
proteins
pubmed
35867826
uniprot
proteins
pubmed
35893676
uniprot
proteins
pubmed
35982226
uniprot
proteins
pubmed
36067704
uniprot
proteins
sequence_length
511
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32853985}. Cytoplasm {ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32853985, ECO:0000269|PubMed:34062120}. Golgi apparatus {ECO:0000269|PubMed:32641828}.
uniprot
proteins