RASA3

RASA3
Identifiers
Aliases	RASA3, GAP1IP4BP, GAPIII, RAS p21 protein activator 3
External IDs	OMIM: 605182 MGI: 1197013 HomoloGene: 7217 GeneCards: RASA3
Gene location (Human) Chr. Chromosome 13 (human) Band 13q34 Start 113,977,783 bp End 114,132,623 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 A1.1|8 6.29 cM Start 13,616,948 bp End 13,727,603 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium sural nerve monocyte blood subcutaneous adipose tissue lymph node right uterine tube canal of the cervix appendix gastric mucosa Top expressed in blood spleen calvaria subcutaneous adipose tissue white adipose tissue cerebellum femur body of femur superior surface of tongue cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium-release channel activity metal ion binding GTPase activator activity Cellular component cytoplasm cytosol membrane intrinsic component of the cytoplasmic side of the plasma membrane plasma membrane Biological process intracellular signal transduction regulation of GTPase activity MAPK cascade signal transduction positive regulation of GTPase activity release of sequestered calcium ion into cytosol negative regulation of Ras protein signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 22821 19414 Ensembl ENSG00000280477 ENSG00000185989 ENSMUSG00000031453 UniProt Q14644 Q60790 RefSeq (mRNA) NM_007368 NM_001320821 NM_001320822 NM_009025 RefSeq (protein) NP_001307750 NP_001307751 NP_031394 NP_033051 Location (UCSC) Chr 13: 113.98 – 114.13 Mb Chr 8: 13.62 – 13.73 Mb PubMed search
Wikidata
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Ras GTPase-activating protein 3 is an enzyme that in humans is encoded by the RASA3 gene.

The protein encoded by this gene is member of the GAP1 family of GTPase-activating proteins. The gene product stimulates the GTPase activity of normal RAS p21 but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, thereby allowing control of cellular proliferation and differentiation. This family member is an inositol 1,3,4,5-tetrakisphosphate-binding protein, like the closely related RAS p21 protein activator 2. The two family members have distinct pleckstrin-homology domains, with this particular member having a domain consistent with its localization to the plasma membrane.

Interactions

RASA3 has been shown to interact with HCK.

Further reading

• Hata Y, Kikuchi A, Sasaki T, et al. (1990). "Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s". J. Biol. Chem. 265 (13): 7104–7. doi:10.1016/S0021-9258(19)39083-0. PMID 2158984.
• Hjermstad SJ, Briggs SD, Smithgall TE (1993). "Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanism". Biochemistry. 32 (39): 10519–25. doi:10.1021/bi00090a031. PMID 7691175.
• Briggs SD, Bryant SS, Jove R, et al. (1995). "The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck". J. Biol. Chem. 270 (24): 14718–24. doi:10.1074/jbc.270.24.14718. PMID 7782336.
• Lockyer PJ, Vanlingen S, Reynolds JS, et al. (1999). "Tissue-specific expression and endogenous subcellular distribution of the inositol 1,3,4,5-tetrakisphosphate-binding proteins GAP1(IP4BP) and GAP1(m)". Biochem. Biophys. Res. Commun. 255 (2): 421–6. doi:10.1006/bbrc.1999.0217. PMID 10049724.
• El-Daher SS, Patel Y, Siddiqua A, et al. (2000). "Distinct localization and function of (1,4,5)IP(3) receptor subtypes and the (1,3,4,5)IP(4) receptor GAP1(IP4BP) in highly purified human platelet membranes". Blood. 95 (11): 3412–22. doi:10.1182/blood.V95.11.3412. PMID 10828023.
• Cozier GE, Lockyer PJ, Reynolds JS, et al. (2000). "GAP1IP4BP contains a novel group I pleckstrin homology domain that directs constitutive plasma membrane association". J. Biol. Chem. 275 (36): 28261–8. doi:10.1074/jbc.M000469200. PMID 10869341.
• Koehler JA, Moran MF (2001). "RACK1, a protein kinase C scaffolding protein, interacts with the PH domain of p120GAP". Biochem. Biophys. Res. Commun. 283 (4): 888–95. doi:10.1006/bbrc.2001.4889. PMID 11350068.
• Walker SA, Kupzig S, Lockyer PJ, et al. (2003). "Analyzing the role of the putative inositol 1,3,4,5-tetrakisphosphate receptor GAP1IP4BP in intracellular Ca2+ homeostasis". J. Biol. Chem. 277 (50): 48779–85. doi:10.1074/jbc.M204839200. PMID 12356770.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
• Battram AM, Durrant TN, Agbani EO, et al. (2016). "The Phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-binder Rasa3 Regulates Phosphoinositide 3-kinase (PI 3-kinase)-dependent Integrin αIIbβ3 Outside-in Signaling". J. Biol. Chem. 292 (5): 1691–1704. doi:10.1074/jbc.M116.746867. PMC 5290945. PMID 27903653.