Aliases for TRIM5 Gene
- Tripartite Motif Containing 5 2 3 5
- RING-Type E3 Ubiquitin Transferase TRIM5 3 4
- Tripartite Motif Protein TRIM5 2 3
- RNF88 3 4
- Tripartite Motif Containing 5 Transcript Variant Kappa 3
- Tripartite Motif Containing 5 Transcript Variant Iota 3
- Tripartite Motif-Containing Protein 5 3
- Tripartite Motif Protein TRIM 2
External Ids for TRIM5 Gene
Previous GeneCards Identifiers for TRIM5 Gene
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Dec 2009]
GeneCards Summary for TRIM5 Gene
TRIM5 (Tripartite Motif Containing 5) is a Protein Coding gene. Diseases associated with TRIM5 include Rubella and Ipex Syndrome. Among its related pathways are Interferon gamma signaling and Mesodermal Commitment Pathway. GO annotations related to this gene include protein homodimerization activity and ligase activity. An important paralog of this gene is TRIM6-TRIM34.
UniProtKB/Swiss-Prot for TRIM5 Gene
Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates Lys-63-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057).