Trim7
entrez
94089
canonical
uniprot
Q923T7
canonical
ensembl
ENSMUSG00000040350
resolver
ensp
ENSMUSP00000039011
resolver
ensp
ENSMUSP00000104836
resolver
ensp
ENSMUSP00000183086
resolver
ensp
ENSMUSP00000183087
resolver
enst
ENSMUST00000046903
resolver
genesymbol
Trim7
resolver
genesymbol_syn
Gnip
resolver
uniprot
Q5NCB6
resolver
uniprot
Q5NCB7
resolver
uniprot
Q99PQ5
resolver
uniprot_entry
Q5NCB7_MOUSE
resolver
uniprot_entry
TRIM7_MOUSE
resolver
uniprot_sec
Q5NCB6
resolver
uniprot_sec
Q99PQ5
resolver
amino_acid_sequence
MATVGPRTGPNAGAEALALAAELQGEATCSICLEFFREPVSVECGHSFCRACIMRCWERPGAGTGTATRTLPCPLPCPQCREPARPSQLRPNRQLAAVVSLLRRFSLPPTAPGERGTPAVPARAAAARCSQHGEQLKLYCQDDGRAICVVCDRAREHRSHAVLPLEEAVQEAKELLDSRLRALKKVLEDYEAFRSTEERESKELLKQMAAEKEKVGAEFQALRAFLVEQEGRLLSRLEVLSREVTQKQNENLAQLEGEITQLSKLSGQIQETAQKPDLDFLQEFKSTLSKCSSVPSSKPTTVSSEMKNKVWNVSLKSFVLKGLLKKFKEDLQGELEKEEKVELTLDPDTANPRLILSLDLKSVRLGQRAQDLPNHPRRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWAMQLNNGQYWAVTSPERTQLNCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP
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. Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein. Mechanistically, recognizes the C-terminal glutamine-containing motif generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation (PubMed:35972292). 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 (By similarity). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (PubMed:30928727). 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. Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1. Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation (PubMed:32126128). {ECO:0000250|UniProtKB:Q9C029, ECO:0000269|PubMed:30928727, ECO:0000269|PubMed:32126128, ECO:0000269|PubMed:35972292}.
uniprot
proteins
mass_dalton
57021
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9C029}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-106 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9C029}.; PTM: Auto-ubiquitinates via 'Lys-63'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q9C029}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
30928727
uniprot
proteins
pubmed
32126128
uniprot
proteins
pubmed
35972292
uniprot
proteins
sequence_length
510
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C029}. Cytoplasm {ECO:0000250|UniProtKB:Q9C029}. Golgi apparatus {ECO:0000250|UniProtKB:Q9C029}.
uniprot
proteins