Human Gene TRIM5 (ENST00000380034.8) Description and Page Index
Description: Homo sapiens tripartite motif containing 5 (TRIM5), transcript variant alpha, mRNA. (from RefSeq NM_033034) RefSeq Summary (NM_033034): 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]. Gencode Transcript: ENST00000380034.8 Gencode Gene: ENSG00000132256.19 Transcript (Including UTRs) Position: hg38 chr11:5,663,195-5,685,074 Size: 21,880 Total Exon Count: 8 Strand: - Coding Region Position: hg38 chr11:5,664,809-5,680,177 Size: 15,369 Coding Exon Count: 7
ID:TRIM5_HUMAN DESCRIPTION: RecName: Full=Tripartite motif-containing protein 5; EC=6.3.2.-; AltName: Full=RING finger protein 88; FUNCTION: Isoform Alpha is a retrovirus restriction factor, which mediates species-specific, early block to retrovirus infection. Targets retroviral capsid soon after entry into the cell, and prevents reverse transcription of the virus RNA genome. Isoform Alpha trimers may make multiple contacts with the hexameric lattice of CA proteins which constitute the surface of retrovirion core, and somehow inactivate the virus. Restricts efficiently infection by N-MLV, but not HIV-1. May have E3 ubiquitin-protein ligase activity. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Isoform Alpha forms homotrimers, and may interact with retroviral CA protein. Isoform Delta interacts with BTBD1 and BTBD2. INTERACTION: Self; NbExp=2; IntAct=EBI-924214, EBI-924214; Q2Y080:- (xeno); NbExp=3; IntAct=EBI-924230, EBI-924086; Q13049:TRIM32; NbExp=2; IntAct=EBI-924214, EBI-742790; SUBCELLULAR LOCATION: Cytoplasm, P-body. Note=Cytoplasmic bodies. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme (By similarity). PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation. SIMILARITY: Belongs to the TRIM/RBCC family. SIMILARITY: Contains 1 B box-type zinc finger. SIMILARITY: Contains 1 B30.2/SPRY domain. SIMILARITY: Contains 1 RING-type zinc finger. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/trim5/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9C035
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Mouse
Rat
Zebrafish
D. melanogaster
C. elegans
S. cerevisiae
No ortholog
No ortholog
No ortholog
No ortholog
No ortholog
No ortholog
Gene Ontology (GO) Annotations with Structured Vocabulary
US Server
