Misplaced Pages

RASSF9
Identifiers
Aliases	RASSF9, P-CIP1, PAMCI, PCIP1, Ras association domain family member 9
External IDs	OMIM: 610383; MGI: 2384307; HomoloGene: 3976; GeneCards: RASSF9; OMA:RASSF9 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q21.31 Start 85,800,703 bp End 85,836,409 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 D1 Start 102,348,083 bp End 102,385,597 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of paranasal sinus bronchial epithelial cell germinal epithelium olfactory zone of nasal mucosa visceral pleura parietal pleura palpebral conjunctiva epithelium of nasopharynx gonad testicle Top expressed in lumbar spinal ganglion spermatid endothelium of vein tooth molar urethra endothelium of artery vasa recta ascending aorta aortic valve More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding transporter activity Cellular component cytosol endosome trans-Golgi network transport vesicle membrane extracellular exosome recycling endosome Biological process protein targeting signal transduction endosomal transport intracellular transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9182 237504 Ensembl ENSG00000198774 ENSMUSG00000044921 UniProt O75901 Q8K342 RefSeq (mRNA) NM_005447 NM_146240 RefSeq (protein) NP_005438 NP_666352 Location (UCSC) Chr 12: 85.8 – 85.84 Mb Chr 10: 102.35 – 102.39 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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 RASSF9 gene.

Function

RASSF9 the N-terminal RASSF family member Ras association (RalGDS/AF-6) domain family (N-terminal) member 9 12q21.31, is one of two new wild type RASSF9 and RASSF10 proteins. Three proteins that interact with a fragment of the PAM cytosolic domain containing signaling switch I and II the RA1 and RA2ras complex. RASSF7, the first member of the N-terminal RASSF family is required for mitosis. RASSF9 is recently found to be involved in regulation of epidermal homeostasis.

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 in microtubule locations, does NOT bind RasGTP. 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 (Ha-Ras, Ki-Ras, and Rap) residues function, blocked by a mutation that affects Ras effector function is the critical product of the t (6:11) abnormality associated with some human leukemias. Phosphatidylinositol-3-kinase make contacts with both (6:11) switch I and II regions of ras and yeast adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro. Ras-interacting residues, are appreciably different from that of RalGDS-RBD through their C-terminal Ras-binding domains (RBD). Such outliers as afadin/AF-6 and Rin1 were found to inhibit the binding of Raf to Ras. Adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro with the Ras-associating domain-RA, not all RA domains bind RasGTP it is a primary Ras-binding site.

Interactions

• PAM Peptidyl-glycine alpha-amidating monooxygenase precursor (PAM)
• RASSF7 Ras association domain-containing protein 7 (HRAS1-related cluster protein 1)
• BLOC1S2 Biogenesis of lysosome-related organelles complex-1 subunit 2 (BLOC subunit 2)
• TF Serotransferrin precursor (Transferrin) (Beta-1-metal- binding globulin)
• RAB11A Ras-related protein Rab-11A

References

1. ^ GRCh38: Ensembl release 89: ENSG00000198774 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000044921 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Ras association (RalGDS/AF-6) domain family (N-terminal) member 9".
6. ^ Chen 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. PMID 9837933.
7. ^ Sherwood V, Manbodh R, Sheppard C, Chalmers AD (April 2008). "RASSF7 is a member of a new family of RAS association domain-containing proteins and is required for completing mitosis". Mol Biol Cell. 19 (4): 1772–82. doi:10.1091/mbc.E07-07-0652. PMC 2291435. PMID 18272789.
8. ^ Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M (February 2006). "Structural and mechanistic insights into ras association domains of phospholipase C epsilon". Mol Cell. 21 (4): 495–507. doi:10.1016/j.molcel.2006.01.008. PMID 16483931.
9. Lee CM, Yang P, Chen LC, Chen CC, Wu SC, Cheng HY, Chang YS (21 March 2011). "A Novel Role of RASSF9 in Maintaining Epidermal Homeostasis". PLOS ONE. 6 (3): e17867. Bibcode:2011PLoSO...617867L. doi:10.1371/journal.pone.0017867. PMC 3061870. PMID 21445300.
10. 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. PMID 10334925.
11. 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. PMID 9253406. S2CID 1328881.
12. ^ Kuriyama 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. PMID 8557659.
13. 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. PMID 16892067. S2CID 12337748.
14. ^ Hofer F, Fields S, Schneider C, Martin GS (November 1994). "Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator". Proc Natl Acad Sci U S A. 91 (23): 11089–93. Bibcode:1994PNAS...9111089H. doi:10.1073/pnas.91.23.11089. PMC 45172. PMID 7972015.
15. Wang J, Williams RW, Manly KF (2003). " BioGPS: NM_005447,. WebQTL: web-based complex trait analysis". Neuroinformatics. 1 (4): 299–08. doi:10.1385/NI:1:4:299. PMID 15043217. S2CID 195348266. Archived from the original on 2017-08-10. Retrieved 2010-12-06.
16. ^ Kido 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. hdl:20.500.14094/D1002436. PMID 11723130.
17. 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. PMID 9891982. S2CID 23727331.
18. 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. PMID 9753431.
19. von Mering C, Jensen LJ, Snel B, Hooper SD, Krupp M, Foglierini M, Jouffre N, Huynen MA, Bork P (December 2004). "STRING: known and predicted protein-protein associations, integrated and transferred across organisms". Nucleic Acids Res. 33 (Database issue): D433 – D437. doi:10.1093/nar/gki005. PMC 539959. PMID 15608232.

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. PMID 14702039.

• Genes on human chromosome 12