TRIM32
Tripartite motif-containing 32 | |||||||||||
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Identifiers | |||||||||||
Symbols | TRIM32 ; BBS11; HT2A; LGMD2H; TATIP | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 36327 | ||||||||||
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RNA expression pattern | |||||||||||
File:PBB GE TRIM32 203846 at tn.png | |||||||||||
More reference expression data | |||||||||||
Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
Tripartite motif-containing 32, also known as TRIM32, is a human gene.[1]
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 cytoplasmic bodies. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes.[1]
See also
References
Further reading
- Albor A, El-Hizawi S, Horn EJ; et al. (2006). "The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB". J. Biol. Chem. 281 (35): 25850–66. doi:10.1074/jbc.M601655200. PMID 16816390.
- Lim J, Hao T, Shaw C; et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
- Chiang AP, Beck JS, Yen HJ; et al. (2006). "Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11)". Proc. Natl. Acad. Sci. U.S.A. 103 (16): 6287–92. doi:10.1073/pnas.0600158103. PMID 16606853.
- Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Schoser BG, Frosk P, Engel AG; et al. (2005). "Commonality of TRIM32 mutation in causing sarcotubular myopathy and LGMD2H". Ann. Neurol. 57 (4): 591–5. doi:10.1002/ana.20441. PMID 15786463.
- Benzinger A, Muster N, Koch HB; et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
- 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. PMID 15489334.
- Humphray SJ, Oliver K, Hunt AR; et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMID 15164053.
- 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. PMID 12477932.
- Frosk P, Weiler T, Nylen E; et al. (2002). "Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene". Am. J. Hum. Genet. 70 (3): 663–72. PMID 11822024.
- Reymond A, Meroni G, Fantozzi A; et al. (2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMID 11331580.
- Weiler T, Greenberg CR, Zelinski T; et al. (1998). "A gene for autosomal recessive limb-girdle muscular dystrophy in Manitoba Hutterites maps to chromosome region 9q31-q33: evidence for another limb-girdle muscular dystrophy locus". Am. J. Hum. Genet. 63 (1): 140–7. PMID 9634523.
- Fridell RA, Harding LS, Bogerd HP, Cullen BR (1995). "Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins". Virology. 209 (2): 347–57. doi:10.1006/viro.1995.1266. PMID 7778269.
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