Revision as of 21:40, 24 November 2017 by en>JCW-CleanerBot(→Regulation: task, replaced: journal = Proc Natl Acad Sci U S A. → journal = Proc Natl Acad Sci U S A using AWB)
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.[1]
RASSF9 the N-terminal RASSF family member Ras association (RalGDS/AF-6) domain family (N-terminal) member 9 12q21.31,[2][3] is one of two new wild type RASSF9 and RASSF10[3] proteins. Three proteins that interact with a fragment of the PAM cytosolic domain containing signaling switch I and II the RA1 and RA2ras complex.[4]RASSF7, the first member of the N-terminal RASSF family is required for mitosis.[3] RASSF9 is recently found to be involved in regulation of epidermal homeostasis.[5]
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[2] in microtubule locations, does NOT bind RasGTP.[6] 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[7] (Ha-Ras, Ki-Ras,[8] and Rap[9]) residues function,[10] blocked by a mutation that affects Ras effector function[11] is the critical product of the t (6:11) abnormality associated with some human leukemias.[8]Phosphatidylinositol-3-kinase make contacts with both (6:11) switch I and II[8] regions of ras[4] and yeast adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro.[12] Ras-interacting residues, are appreciably different from that of RalGDS-RBD[13] through their C-terminal Ras-binding domains (RBD).[14] Such outliers as afadin/AF-6 and Rin1[12] were found to inhibit the binding of Raf to Ras.[10]Adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro with the Ras-associating domain-RA,[12] not all RA domains bind RasGTP it is a primary Ras-binding site.
↑ 2.02.1Chen L, Johnson RC, Milgram SL (December 1998). "P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes". J Biol Chem. 273 (50): 33524–32. doi:10.1074/jbc.273.50.33524. PMID9837933.
↑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.
↑Huang L, Weng X, Hofer F, Martin GS, Kim SH (August 1997). "Three-dimensional structure of the Ras-interacting domain of RalGDS". Nature Structural & Molecular Biology. 4 (8): 609–15. doi:10.1038/nsb0897-609. PMID9253406.
↑ 8.08.18.2Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K (January 1996). "Identification of AF-6 and canoe as putative targets for Ras". J Biol Chem. 271 (2): 607–10. doi:10.1074/jbc.271.2.607. PMID8557659.
↑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.
↑ 12.012.112.2Kido M, Shima F, Satoh T, Asato T, Kariya K, Kataoka T (February 2002). "Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase". J Biol Chem. 277 (5): 3117–23. doi:10.1074/jbc.M109526200. PMID11723130.
↑Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S (December 1998). "Solution structure of the Ras-binding domain of RGL". FEBS Lett. 441 (3): 413–8. doi:10.1016/S0014-5793(98)01596-8. PMID9891982.
↑Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P (September 1998). "Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf". Biochemistry. 37 (39): 13453–62. doi:10.1021/bi9811664. PMID9753431.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
