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AliasesRASSF9, P-CIP1, PAMCI, PCIP1, Ras association domain family member 9
External IDsMGI: 2384307 HomoloGene: 3976 GeneCards: RASSF9
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for RASSF9
Genomic location for RASSF9
Band12q21.31Start85,800,697 bp[1]
End85,836,570 bp[1]
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 12: 85.8 – 85.84 MbChr 10: 102.51 – 102.55 Mb
PubMed search[3][4]
View/Edit HumanView/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.[5]


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]


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.


  • 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[19]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198774 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000044921 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ "Entrez Gene: Ras association (RalGDS/AF-6) domain family (N-terminal) member 9".
  6. ^ a b 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. ^ a b c 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. ^ a b 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. 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.
  12. ^ a b c 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.
  14. ^ a b 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. 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.
  16. ^ a b c 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. 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.
  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: D433–D437. doi:10.1093/nar/gki005. PMC 539959. PMID 15608232.

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