RASA3

RASA3

RAS p21 protein activator 3, also known as RASA3, is a human gene.cite web | title = Entrez Gene: RASA3 RAS p21 protein activator 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22821| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: RASA3 RAS p21 protein activator 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22821| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hata Y, Kikuchi A, Sasaki T, "et al." |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 13 |pages= 7104–7 |year= 1990 |pmid= 2158984 |doi=
*cite journal | author=Cullen PJ, Hsuan JJ, Truong O, "et al." |title=Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family. |journal=Nature |volume=376 |issue= 6540 |pages= 527–30 |year= 1995 |pmid= 7637787 |doi= 10.1038/376527a0
*cite journal | author=Hjermstad SJ, Briggs SD, Smithgall TE |title=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. |journal=Biochemistry |volume=32 |issue= 39 |pages= 10519–25 |year= 1993 |pmid= 7691175 |doi=
*cite journal | author=Briggs SD, Bryant SS, Jove R, "et al." |title=The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14718–24 |year= 1995 |pmid= 7782336 |doi=
*cite journal | author=Lockyer PJ, Bottomley JR, Reynolds JS, "et al." |title=Distinct subcellular localisations of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m result from the GAP1IP4BP PH domain directing plasma membrane targeting. |journal=Curr. Biol. |volume=7 |issue= 12 |pages= 1007–10 |year= 1998 |pmid= 9382842 |doi=
*cite journal | author=Lockyer PJ, Vanlingen S, Reynolds JS, "et al." |title=Tissue-specific expression and endogenous subcellular distribution of the inositol 1,3,4,5-tetrakisphosphate-binding proteins GAP1(IP4BP) and GAP1(m). |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 2 |pages= 421–6 |year= 1999 |pmid= 10049724 |doi= 10.1006/bbrc.1999.0217
*cite journal | author=El-Daher SS, Patel Y, Siddiqua A, "et al." |title=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. |journal=Blood |volume=95 |issue= 11 |pages= 3412–22 |year= 2000 |pmid= 10828023 |doi=
*cite journal | author=Cozier GE, Lockyer PJ, Reynolds JS, "et al." |title=GAP1IP4BP contains a novel group I pleckstrin homology domain that directs constitutive plasma membrane association. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28261–8 |year= 2000 |pmid= 10869341 |doi= 10.1074/jbc.M000469200
*cite journal | author=Koehler JA, Moran MF |title=RACK1, a protein kinase C scaffolding protein, interacts with the PH domain of p120GAP. |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue= 4 |pages= 888–95 |year= 2001 |pmid= 11350068 |doi= 10.1006/bbrc.2001.4889
*cite journal | author=Walker SA, Kupzig S, Lockyer PJ, "et al." |title=Analyzing the role of the putative inositol 1,3,4,5-tetrakisphosphate receptor GAP1IP4BP in intracellular Ca2+ homeostasis. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48779–85 |year= 2003 |pmid= 12356770 |doi= 10.1074/jbc.M204839200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Rush J, Moritz A, Lee KA, "et al." |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046

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  • C2 domain — Pfam box Symbol = C2 Name = C2 domain width =200 caption = The C2 domain of C.absonum α toxin (PDB 1OLP). β strands are shown in yellow. Co ordinated Calcium ions are in cyan Pfam= PF00168 InterPro= IPR000008 SMART= C2 PROSITE = PDOC00380 SCOP =… …   Wikipedia

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