ras GTPase activator protein (Ras p21 protein activator, p120, rasGAP, RASA1)
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Introduction
Facilitates p21ras GTPase activity.
Function
- inhibitory regulator of the Ras-cyclic AMP pathway
- stimulates the GTPase of normal but not oncogenic Ras p21
- interacts with SQTSM1
- negatively regulated by Tyr phosphorylation
- associates with rap1A-protein ras-GAP-associated-p190 ras-GAP-associated-p62
Structure
- N-terminus is blocked
- contains 1 C2 domain
- contains 1 PH domain
- contains 1 Ras-GAP domain
- contains 2 SH2 domains
- contains 1 SH3 domain
- SH2/SH3 domains of ras GAP are hypothesized to convey signal of ras[6]
Compartment
- cytoplasm
- may undergo Ca+2-mediated translocation to cellular membranes {via CaLB-motif}[6]
Alternative splicing
named isoforms=2
Pathology
- mutations in the SH2 domain of RASA seem to be oncogenic & cause basal cell carcinomas
- defects in RASA1 are the cause of
More general terms
More specific terms
- disabled homolog 2-interacting protein (DAB2-interacting protein, DAB2 interaction protein, ASK-interacting protein 1, DAB2IP, AF9Q34, AIP1, KIAA1743)
- neurofibromatosis type 1 [NF1] protein or neurofibromin
- Ras GTPase-activating protein 2; GAP1m (RASA2, GAP1M, RASGAP)
- Ras GTPase-activating protein 3; GAP1(IP4BP); ins P4-binding protein (RASA3)
- Ras GTPase-activating protein 4; Ras p21 protein activator 4; RasGAP-activating-like protein 2; Ca+2-promoted Ras inactivator (RASA4, CAPRI, GAPL, KIAA0538)
- Ras GTPase-activating protein FLJ00412 (RASAL3)
- Ras GTPase-activating protein nGAP; RAS protein activator-like 2 (RASAL2, NGAP)
- Ras GTPase-activating protein synGAP; neuronal RasGAP; synaptic Ras GTPase-activating protein 1; synaptic Ras-GAP 1 (SYNGAP1, KIAA1938)
- Ras GTPase-activating-like protein IQGAP
- RasGAP-activating-like protein 1 (RASAL1 RASAL)
Additional terms
References
- ↑ Kazlauskas A, Ellis C, Pawson T, Cooper JA. Binding of GAP to activated PDGF receptors. Science. 1990 Mar 30;247(4950):1578-81. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2157284
- ↑ Ellis C, Moran M, McCormick F, Pawson T. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature. 1990 Jan 25;343(6256):377-81. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1689011
- ↑ Matsuda M, Mayer BJ, Fukui Y, Hanafusa H. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science. 1990 Jun 22;248(4962):1537-9. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1694307
- ↑ Wigler MH. Oncoproteins. GAPs in understanding Ras. Nature. 1990 Aug 23;346(6286):696-7. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2201920
- ↑ Liscovitch M. Crosstalk among multiple signal-activated phospholipases. Trends Biochem Sci. 1992 Oct;17(10):393-9. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1455508
- ↑ 6.0 6.1 6.2 Boguski MS & McCormick F Proteins regulating Ras and its relative. Nature 366:643 1993 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8259209
- ↑ GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=RASA1
- ↑ UniProt http://www.uniprot.org/uniprot/P20936.html