Ras association domain-containing protein 9 (RASSF9), also known as PAM COOH-terminal interactor protein 1 (PCIP1) or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor (PAMCI) is a protein that in humans is encoded by the RASSF9gene.[5]
Function
RASSF9 the N-terminal RASSF family member Ras association (RalGDS/AF-6) domain family (N-terminal) member 9 12q21.31,[6][7] is one of two new wild type RASSF9 and RASSF10[7] proteins. Three proteins that interact with a fragment of the PAM cytosolic domain containing signaling switch I and II the RA1 and RA2ras complex.[8]RASSF7, the first member of the N-terminal RASSF family is required for mitosis.[7] RASSF9 is recently found to be involved in regulation of epidermal homeostasis.[9]
Regulation
The mutant proregion encoding PAM COOH-terminal interactor protein-1 (P-CIP1) is comparable to that of human band 4.1-like TF (blood plasma protein) as a recycling endosomal pathway[6] in microtubule locations, does NOT bind RasGTP.[10] Specificity of interaction may all be related to microtubule locations of the endosomal-lysosomal system localized within the centrosome with Transferrin and different Ras proteins or with that one (N-Ras), but on the other hand, it interacts with three[11] (Ha-Ras, Ki-Ras,[12] and Rap[13]) residues function,[14] blocked by a mutation that affects Ras effector function[15] is the critical product of the t (6:11) abnormality associated with some human leukemias.[12]Phosphatidylinositol-3-kinase make contacts with both (6:11) switch I and II[12] regions of ras[8] and yeast adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro.[16] Ras-interacting residues, are appreciably different from that of RalGDS-RBD[17] through their C-terminal Ras-binding domains (RBD).[18] Such outliers as afadin/AF-6 and Rin1[16] were found to inhibit the binding of Raf to Ras.[14]Adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro with the Ras-associating domain-RA,[16] not all RA domains bind RasGTP it is a primary Ras-binding site.
^Wojcik J, Girault JA, Labesse G, Chomilier J, Mornon JP, Callebaut I (May 1999). "Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family". Biochem Biophys Res Commun. 259 (1): 113–20. doi:10.1006/bbrc.1999.0727. PMID10334925.
^Katagiri K, Imamura M, Kinashi T (September 2006). "Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion". Nat Immunol. 7 (9): 919–28. doi:10.1038/ni1374. PMID16892067. S2CID12337748.
