RASSF9

Last updated

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
Orthologs
SpeciesHumanMouse
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 [3] [4]
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. [5]

Contents

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.

Interactions

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000198774 – Ensembl, May 2017
  2. 1 2 3 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. 1 2 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. 1 2 3 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. 1 2 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. 1 2 3 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. 1 2 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. 1 2 3 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.[ permanent dead link ]

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