TRIM6

Tripartite motif containing 6
Identifiers
Symbols	TRIM6 ; RNF89
External IDs	OMIM: 607564 MGI: 2137352 HomoloGene: 14381 GeneCards: TRIM6 Gene
Gene ontology Molecular function • molecular_function • protein binding • zinc ion binding • ligase activity • protein kinase binding • protein binding, bridging • ubiquitin protein ligase activity • protein tyrosine kinase binding Cellular component • cytoplasm Biological process • positive regulation of defense response to virus by host • positive regulation of cytokine secretion involved in immune response • negative regulation of gene expression • positive regulation of peptidyl-threonine phosphorylation • free ubiquitin chain polymerization • protein ubiquitination • response to lipopolysaccharide • positive regulation of peptidyl-serine phosphorylation • cellular response to interferon-beta • negative regulation of viral genome replication • positive regulation of type I interferon-mediated signaling pathway • protein trimerization • regulation of NIK/NF-kappaB signaling • positive regulation of transcription regulatory region DNA binding Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	117854	94088
Ensembl	ENSG00000121236	ENSMUSG00000072244
UniProt	Q9C030	Q8BGE7
RefSeq (mRNA)	NM_001003818	NM_001013616
RefSeq (protein)	NP_001003818	NP_001013637
Location (UCSC)	Chr 11: 5.6 – 5.61 Mb	Chr 7: 104.22 – 104.24 Mb
PubMed search

Tripartite motif-containing protein 6 is a protein that in humans is encoded by the TRIM6 gene.^[1][2]

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 localizes to the nucleus, but its specific function has not been identified. This gene is mapped to chromosome 11p15, where it resides within a TRIM gene cluster. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. A read-through transcript transcribed from this gene and TRIM34 has been observed.^[2]

References

1. Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". EMBO J 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
2. "Entrez Gene: TRIM6 tripartite motif-containing 6".

Further reading

• Li X, Gold B, O'hUigin C, et al. (2007). "Unique features of TRIM5alpha among closely related human TRIM family members.". Virology 360 (2): 419–33. doi:10.1016/j.virol.2006.10.035. PMID 17156811.
• Zhang F, Hatziioannou T, Perez-Caballero D, et al. (2006). "Antiretroviral potential of human tripartite motif-5 and related proteins.". Virology 353 (2): 396–409. doi:10.1016/j.virol.2006.05.035. PMID 16828831.
• Li X, Li Y, Stremlau M, et al. (2006). "Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains.". J. Virol. 80 (13): 6198–206. doi:10.1128/JVI.00283-06. PMC 1488960. PMID 16775307.
• Woo JS, Imm JH, Min CK, et al. (2006). "Structural and functional insights into the B30.2/SPRY domain.". EMBO J. 25 (6): 1353–63. doi:10.1038/sj.emboj.7600994. PMC 1422157. PMID 16498413.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Orimo A, Tominaga N, Yoshimura K, et al. (2001). "Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem.". Genomics 69 (1): 143–9. doi:10.1006/geno.2000.6318. PMID 11013086.