Raf-like Ras-binding

Definition

Ras and heterotrimeric G proteins' alpha subunits are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. The activities of these GTPases are regulated in part by GTPase-activating protein (GAPs) that stimulate hydrolysis of GTP, and guanine nucleotide exchange factors (GEFs) that stimulate GDP release. Ras and G alpha GTPases are prolific signalling molecules interacting with a spectrum of effector molecules and acting through more than one signalling pathway. The Ras-binding domain (RBD) is an independent domain of about 75 residues, which is sufficient for GTP-dependent binding of Ras and other G alpha GTPases. The RBD domain can be present singly or in tandem and it can be found associated with many other domains, such as PDZ, RGS, PID, PH, C1, DH, or protein kinase PMID:10606204. Structurally, the RBD domain of Raf-1 consists of a five-stranded mixed beta- sheet with an interrupted α-helix and two additional small α-helices. The structure of the RBD domain belongs to the ubiquitin α/β roll superfold and is similar to that of the RA domain despite the lack of significant sequence identity. The major interaction between Ras and Raf-1 RBD domain occurs between two antiparallel β-strands: β2 of Ras and β2 of RBD PMID:7791872. This entry represents the entire RBD domain.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• ARAF
• BRAF
• RAF1
• RGS12
• RGS14
• TIAM1
• TIAM2