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.[7] It has been shown that RASA3 promotes a shift from noncanonical to canonical TGF-β signaling through SMAD3 in B cells.[8]
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Cullen PJ, Hsuan JJ, Truong O, Letcher AJ, Jackson TR, Dawson AP, Irvine RF (Sep 1995). "Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family". Nature. 376 (6540): 527–30. Bibcode:1995Natur.376..527C. doi:10.1038/376527a0. PMID7637787. S2CID4283160.
↑ Mamand S, Liu H, Kashem M, Martin A (25 October 2024). "Suppression of Class Switch Recombination to IgA by RASA2 and RASA3 through Inhibition of TGF-β Signaling". The Journal of Immunology. 213 (9): 1739–1745. doi:10.4049/jimmunol.2400353. PMID39451029.
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. PMID7691175.
Lockyer PJ, Vanlingen S, Reynolds JS, etal. (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. PMID10049724.
El-Daher SS, Patel Y, Siddiqua A, etal. (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. PMID10828023.
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. PMID11350068.
Rush J, Moritz A, Lee KA, etal. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID15592455. S2CID7200157.
Mamand S, etal. (2024). "Suppression of Class Switch Recombination to IgA by RASA2 and RASA3 through Inhibition of TGF-β Signaling". The Journal of Immunology. 213 (9): 1739–1745. doi:10.4049/jimmunol.2400353. PMID39451029.
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