RASA1
RASA1 (RAS p21 protein activator 1, also known as p120GAP or p120RASGAP) is a cytoplasmic GTPase-activating protein that switches off Ras signalling by promoting hydrolysis of bound GTP. It is a member of the GAP1 family and is linked to vascular malformation disorders. Browse Assay Genie's current range of RASA1 research reagents below, or read on for the biology behind the target.
RASA1 is a GTPase-activating protein (GAP) that stimulates the intrinsic GTPase activity of Ras proteins, such as NRAS. By enhancing this weak activity, it helps convert Ras from the active GTP-bound state to the inactive GDP-bound state, thereby terminating Ras signalling. In this way RASA1 acts as a suppressor of Ras function and allows control of cellular proliferation and differentiation. According to the NCBI Gene summary, it stimulates the GTPase activity of normal RAS p21 but not its oncogenic counterpart.
The RASA1 gene encodes a cytoplasmic protein that belongs to the GAP1 family of GTPase-activating proteins. HGNC places it in several groups defined by its domain content: pleckstrin homology domain containing, SH2 domain containing, SH3 domain containing, and C2 and RasGAP domain containing. Alternative splicing produces two isoforms. The shorter isoform lacks the N-terminal hydrophobic region but retains the same activity, and appears to be abundantly expressed in placenta but not in adult tissues. A rat ortholog, Rasa1, is recorded.
The protein is also known as GAP, p120GAP, p120RASGAP, p120, RASA and CM-AVM, and was previously named RAS p21 protein activator (GTPase activating protein) 1. Mutations that change the binding sites of RASA1 or its partner are associated with basal cell carcinomas. Mutations are also associated with hereditary capillary malformations, with or without arteriovenous malformations, and with Parkes Weber syndrome, which makes the RASA1 gene a frequent subject in studies of Ras regulation and vascular disease.
RASA1 terminates Ras signalling by driving Ras proteins such as NRAS into the inactive GDP-bound state, making it a core regulator to study.
As a suppressor of Ras function, RASA1 contributes to control of cellular proliferation and differentiation.
Mutations in RASA1 are associated with hereditary capillary malformations, arteriovenous malformations and Parkes Weber syndrome.
Mutations affecting RASA1 binding sites are associated with basal cell carcinomas, linking this GAP to tumour research.
RASA1 is a GTPase-activating protein that stimulates the intrinsic GTPase activity of Ras proteins such as NRAS. This moves Ras from the active GTP-bound state to the inactive GDP-bound state, ending Ras signalling and helping control cell proliferation and differentiation.
RASA1 is also called GAP, p120GAP, p120RASGAP, p120, RASA and CM-AVM, and was formerly named RAS p21 protein activator (GTPase activating protein) 1. Alternative splicing gives two isoforms; the shorter one lacks the N-terminal hydrophobic region but keeps the same activity.
Yes. Mutations in RASA1 are associated with hereditary capillary malformations with or without arteriovenous malformations, and with Parkes Weber syndrome. Mutations altering binding sites are also associated with basal cell carcinomas. A rat ortholog, Rasa1, exists; check the datasheet of any product for its validated reactivity.
Other Ras GTPase-activating proteins and Ras pathway regulators with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P20936; product specifications from Assay Genie datasheets.