TRA2A

From Wikipedia, the free encyclopedia

Transformer-2 alpha

Identifiers

TRA2A; HSU53209

External IDs

OMIM: 602718 MGI: 1933972 HomoloGene: 40866

Gene ontology
Molecular Function:	• nucleotide binding • RNA binding • identical protein binding
Cellular Component:	• nucleus
Biological Process:	• nuclear mRNA splicing, via spliceosome • RNA splicing

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_013293 (mRNA)
NP_037425 (protein)

NM_198102 (mRNA)
NP_932770 (protein)

Location

Chr 7: 23.51 - 23.54 Mb

Chr 6: 49.17 - 49.19 Mb

Pubmed search

[1]

[2]

Transformer-2 alpha, also known as TRA2A, is a human gene.^[1]

This gene is a member of the transformer 2 homolog family and encodes a protein with two RS domains and an RRM (RNA recognition motif) domain. This phosphorylated nuclear protein binds to specific RNA sequences and plays a role in the regulation of pre-mRNA splicing. Several alternatively spliced transcript variants of this gene have been described; however, the full-length nature of some of these variants has not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: TRA2A transformer-2 alpha.

[edit] Further reading

Dauwalder B, Amaya-Manzanares F, Mattox W (1996). "A human homologue of the Drosophila sex determination factor transformer-2 has conserved splicing regulatory functions.". Proc. Natl. Acad. Sci. U.S.A. 93 (17): 9004–9. PMID 8799144.
Tacke R, Tohyama M, Ogawa S, Manley JL (1998). "Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing.". Cell 93 (1): 139–48. PMID 9546399.
"Toward a complete human genome sequence." (1999). Genome Res. 8 (11): 1097–108. PMID 9847074.
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.
Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.". Oncogene 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.
Shin C, Feng Y, Manley JL (2004). "Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock.". Nature 427 (6974): 553–8. doi:10.1038/nature02288. PMID 14765198.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
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.
Gevaert K, Staes A, Van Damme J, et al. (2006). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.". Proteomics 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034.
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.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.