RIAM Polyclonal Antibody

Domain:The two Pro-rich regions are required for the suppression of AP1 transcription activity., function:Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion., induction:Induced by all-trans-retinoic acid., similarity:Belongs to the MRL family., similarity:Contains 1 PH domain., similarity:Contains 1 Ras-associating domain., subcellular location:Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns (5) P and PtdIns (3) P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases., subunit:Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, VASP and ENAH., tissue specificity:Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes.

APBB1IP; PREL1; RARP1; RIAM; Amyloid beta A4 precursor protein-binding family B member 1-interacting protein; APBB1-interacting protein 1; Proline-rich EVH1 ligand 1; PREL-1; Proline-rich protein 73; Rap1-GTP-interacting adapter molecule; R