TRIM7 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of TRIM7 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of TRIM7 at tissue level.

III. Associated gene sets

GO_0016567Biological processprotein ubiquitination
GO_0140374Biological processantiviral innate immune response
GO_0005794Cellular componentGolgi apparatus
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0005515Molecular functionprotein binding
GO_0008270Molecular functionzinc ion binding

IV. Literature review

[source]
Gene nameTRIM7
Protein nameE3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27) (Glycogenin-interacting protein) (RING finger protein 90) (Tripartite motif-containing protein 7)
SynonymsGNIP
RNF90
DescriptionFUNCTION: 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 or SARS-CoV-2 NSP5 and NSP8 proteins . Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation . 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 . 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 . 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 . .; FUNCTION: (Microbial infection) Promotes Zika virus replication by mediating envelope protein E ubiquitination. .

AccessionsENST00000274773.12 [Q9C029-2]
ENST00000422067.2 [Q9C029-3]
Q9C029
ENST00000393315.5 [Q9C029-3]
ENST00000393319.7 [Q9C029-4]
ENST00000334421.5 [Q9C029-1]