RAC3 (gene)

From Wikipedia, the free encyclopedia

Ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3)

PDB rendering based on 1e96.

Available structures: 1e96, 1foe, 1g4u, 1he1, 1hh4, 1i4d, 1i4l, 1i4t, 1mh1, 2c2h, 2fju, 2g0n, 2h7v, 2ic5, 2nz8, 2ov2, 2p2l

Identifiers

Symbol(s)

RAC3;

External IDs

OMIM: 602050 MGI: 2180784 HomoloGene: 68433

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • protein binding • GTP binding
Cellular Component:	• intracellular • endomembrane system
Biological Process:	• small GTPase mediated signal transduction • cell projection biogenesis • actin cytoskeleton organization and biogenesis • regulation of balance • neuromuscular process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005052 (mRNA)
NP_005043 (protein)

NM_133223 (mRNA)
NP_573486 (protein)

Location

Chr 17: 77.58 - 77.59 Mb

Chr 11: 120.54 - 120.54 Mb

Pubmed search

[1]

[2]

Ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3), also known as RAC3, is a human gene.^[1]

The protein encoded by this gene is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.^[1]

[edit] References

^ ^a ^b Entrez Gene: RAC3 ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3).

[edit] Further reading

Didsbury J, Weber RF, Bokoch GM, et al. (1989). "rac, a novel ras-related family of proteins that are botulinum toxin substrates.". J. Biol. Chem. 264 (28): 16378–82. PMID 2674130.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Haataja L, Groffen J, Heisterkamp N (1997). "Characterization of RAC3, a novel member of the Rho family.". J. Biol. Chem. 272 (33): 20384–8. PMID 9252344.
Courjal F, Chuchana P, Theillet C, Fort P (1997). "Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes.". Genomics 44 (2): 242–6. doi:10.1006/geno.1997.4871. PMID 9299243.
Mira JP, Benard V, Groffen J, et al. (2000). "Endogenous, hyperactive Rac3 controls proliferation of breast cancer cells by a p21-activated kinase-dependent pathway.". Proc. Natl. Acad. Sci. U.S.A. 97 (1): 185–9. PMID 10618392.
Soutoglou E, Papafotiou G, Katrakili N, Talianidis I (2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins.". J. Biol. Chem. 275 (17): 12515–20. PMID 10777539.
Morris CM, Haataja L, McDonald M, et al. (2000). "The small GTPase RAC3 gene is located within chromosome band 17q25.3 outside and telomeric of a region commonly deleted in breast and ovarian tumours.". Cytogenet. Cell Genet. 89 (1-2): 18–23. PMID 10894930.
Gnanapragasam VJ, Leung HY, Pulimood AS, et al. (2002). "Expression of RAC 3, a steroid hormone receptor co-activator in prostate cancer.". Br. J. Cancer 85 (12): 1928–36. doi:10.1054/bjoc.2001.2179. PMID 11747336.
Haataja L, Kaartinen V, Groffen J, Heisterkamp N (2002). "The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading.". J. Biol. Chem. 277 (10): 8321–8. doi:10.1074/jbc.M105363200. PMID 11756406.
De Langhe S, Haataja L, Senadheera D, et al. (2002). "Interaction of the small GTPase Rac3 with NRBP, a protein with a kinase-homology domain.". Int. J. Mol. Med. 9 (5): 451–9. PMID 11956649.
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.
Zhang A, Yeung PL, Li CW, et al. (2004). "Identification of a novel family of ankyrin repeats containing cofactors for p160 nuclear receptor coactivators.". J. Biol. Chem. 279 (32): 33799–805. doi:10.1074/jbc.M403997200. PMID 15184363.
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.
Hwang SL, Chang JH, Cheng TS, et al. (2006). "Expression of Rac3 in human brain tumors.". Journal of clinical neuroscience : official journal of the Neurosurgical Society of Australasia 12 (5): 571–4. doi:10.1016/j.jocn.2004.08.013. PMID 15993075.
Chan AY, Coniglio SJ, Chuang YY, et al. (2005). "Roles of the Rac1 and Rac3 GTPases in human tumor cell invasion.". Oncogene 24 (53): 7821–9. doi:10.1038/sj.onc.1208909. PMID 16027728.
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.
Baugher PJ, Krishnamoorthy L, Price JE, Dharmawardhane SF (2006). "Rac1 and Rac3 isoform activation is involved in the invasive and metastatic phenotype of human breast cancer cells.". Breast Cancer Res. 7 (6): R965–74. doi:10.1186/bcr1329. PMID 16280046.
Watabe-Uchida M, John KA, Janas JA, et al. (2006). "The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18.". Neuron 51 (6): 727–39. doi:10.1016/j.neuron.2006.07.020. PMID 16982419.
Hajdo-Milasinović A, Ellenbroek SI, van Es S, et al. (2007). "Rac1 and Rac3 have opposing functions in cell adhesion and differentiation of neuronal cells.". J. Cell. Sci. 120 (Pt 4): 555–66. doi:10.1242/jcs.03364. PMID 17244648.