TRIM32

From Wikipedia, the free encyclopedia

Tripartite motif-containing 32

Identifiers

TRIM32; BBS11; HT2A; LGMD2H; TATIP

External IDs

OMIM: 602290 MGI: 1917057 HomoloGene: 36327

Gene ontology
Molecular Function:	• transcription coactivator activity • protein binding • zinc ion binding • ligase activity • metal ion binding
Cellular Component:	• intracellular • nucleus
Biological Process:	• ubiquitin cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012210 (mRNA)
NP_036342 (protein)

NM_053084 (mRNA)
NP_444314 (protein)

Location

Chr 9: 118.49 - 118.5 Mb

Chr 4: 65.09 - 65.1 Mb

Pubmed search

[1]

[2]

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]

[edit] See also

tripartite motif family

[edit] References

^ ^a ^b Entrez Gene: TRIM32 tripartite motif-containing 32.

[edit] 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.