RAC3

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

PDB rendering based on 1e96.

Available structures
PDB	2C2H, 2G0N, 2IC5, 2OV2, 2QME

Identifiers

Symbols

RAC3;

External IDs

OMIM: 602050 MGI: 2180784 HomoloGene: 68433 GeneCards: RAC3 Gene

Gene Ontology
Molecular function	• nucleotide binding • GTPase activity • protein binding • GTP binding
Cellular component	• cytoplasm • cytosol • plasma membrane • endomembrane system • lamellipodium • growth cone • filamentous actin • neuron projection • neuronal cell body
Biological process	• GTP catabolic process • small GTPase mediated signal transduction • cell projection assembly • actin cytoskeleton organization • neuron projection development • intracellular signal transduction • neuromuscular process controlling balance • regulation of small GTPase mediated signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
79.99 – 79.99 Mb

Chr 11:
120.58 – 120.59 Mb

PubMed search

[1]

[2]

Ras-related C3 botulinum toxin substrate 3 is a protein that in humans is encoded by the RAC3 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]

1 Interactions
2 References
3 Further reading
4 External links

Interactions

RAC3 has been shown to interact with CIB1^[2] and HNF1A.^[3]

References

^ ^a ^b "Entrez Gene: RAC3 ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5881.
^ Haataja, Leena; Kaartinen Vesa, Groffen John, Heisterkamp Nora (March 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. (United States) 277 (10): 8321–8. doi:10.1074/jbc.M105363200. ISSN 0021-9258. PMID 11756406. "yes"
^ Soutoglou, E; Papafotiou G, Katrakili N, Talianidis I (April 2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins". J. Biol. Chem. (UNITED STATES) 275 (17): 12515–20. doi:10.1074/jbc.275.17.12515. ISSN 0021-9258. PMID 10777539. "yes"

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. doi:10.1101/gr.6.9.791. 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. doi:10.1074/jbc.272.33.20384. 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. doi:10.1073/pnas.97.1.185. PMC 26637. PMID 10618392. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26637.
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. doi:10.1074/jbc.275.17.12515. 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. doi:10.1159/000015583. 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. PMC 2364015. PMID 11747336. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2364015.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Hwang SL, Chang JH, Cheng TS, et al. (2006). "Expression of Rac3 in human brain tumors". Journal of Clinical Neuroscience 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. PMC 1410764. PMID 16280046. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1410764.
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.

External links

RAC3 Info with links in the Cell Migration Gateway

PDB gallery

1e96: STRUCTURE OF THE RAC/P67PHOX COMPLEX

1foe: CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH THE GUANINE NUCLEOTIDE EXCHANGE REGION OF TIAM1

1g4u: CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1

1he1: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN AND HUMAN RAC

1hh4: RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION

1i4d: CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)

1i4l: CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN COMPLEX WITH ARFAPTIN (P41)

1i4t: CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTIN

1mh1: SMALL G-PROTEIN

2c2h: CRYSTAL STRUCTURE OF THE HUMAN RAC3 IN COMPLEX WITH GDP

2fju: Activated Rac1 bound to its effector phospholipase C beta 2

2g0n: The Crystal Structure of the Human RAC3 in complex with GDP and Chloride

2h7v: Co-crystal structure of YpkA-Rac1

2ic5: Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.

2nz8: N-terminal DHPH cassette of Trio in complex with nucleotide-free Rac1

2ov2: The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4)

2p2l: Rac1-GDP-Zinc Complex

RAC3

Contents

Interactions

References

Further reading

External links