RAP1A

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RAP1A, member of RAS oncogene family
Protein RAP1A PDB 1c1y.png
PDB rendering based on 1c1y.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RAP1A ; C21KG; G-22K; KREV-1; KREV1; RAP1; SMGP21
External IDs OMIM179520 MGI97852 HomoloGene2162 ChEMBL: 1255139 GeneCards: RAP1A Gene
Orthologs
Species Human Mouse
Entrez 5906 109905
Ensembl ENSG00000116473 ENSMUSG00000068798
UniProt P62834 P62835
RefSeq (mRNA) NM_001010935 NM_145541
RefSeq (protein) NP_001010935 NP_663516
Location (UCSC) Chr 1:
112.08 – 112.26 Mb
Chr 3:
105.73 – 105.8 Mb
PubMed search [1] [2]

Ras-related protein Rap-1A is a protein that in humans is encoded by the RAP1A gene.[1]

Function[edit]

The product of this gene belongs to the family of Ras-related proteins. These proteins share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between RAP proteins and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. The product of this gene counteracts the mitogenic function of RAS because it can interact with RAS GAPs and RAF in a competitive manner. Two transcript variants encoding the same protein have been identified for this gene.[2]

Role in Lymphocytes[edit]

RAP1A is an important player in adhesion and migration of lymphocytes.

Interactions[edit]

RAP1A has been shown to interact with C-Raf,[3][4][5][6] PDE6D,[7][8] TSC2,[9][10] RALGDS,[11][12] RAPGEF2[13] and MLLT4.[11]

References[edit]

  1. ^ Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (January 1989). "A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization". J Biol Chem 263 (35): 18965–71. PMID 3143720. 
  2. ^ "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family". 
  3. ^ Han, L; Colicelli J (March 1995). "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1". Mol. Cell. Biol. (UNITED STATES) 15 (3): 1318–23. ISSN 0270-7306. PMC 230355. PMID 7862125. 
  4. ^ Nassar, N; Horn G; Herrmann C; Scherer A; McCormick F; Wittinghofer A (June 1995). "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue". Nature (ENGLAND) 375 (6532): 554–60. doi:10.1038/375554a0. ISSN 0028-0836. PMID 7791872. 
  5. ^ Hu, C D; Kariya K; Okada T; Qi X; Song C; Kataoka T (January 1999). "Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation". J. Biol. Chem. (UNITED STATES) 274 (1): 48–51. doi:10.1074/jbc.274.1.48. ISSN 0021-9258. PMID 9867809. 
  6. ^ Okada, T; Hu C D; Jin T G; Kariya K; Yamawaki-Kataoka Y; Kataoka T (September 1999). "The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases". Mol. Cell. Biol. (UNITED STATES) 19 (9): 6057–64. ISSN 0270-7306. PMC 84512. PMID 10454553. 
  7. ^ Nancy, Vanessa; Callebaut Isabelle; El Marjou Ahmed; de Gunzburg Jean (April 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". J. Biol. Chem. (United States) 277 (17): 15076–84. doi:10.1074/jbc.M109983200. ISSN 0021-9258. PMID 11786539. 
  8. ^ Hanzal-Bayer, Michael; Renault Louis; Roversi Pietro; Wittinghofer Alfred; Hillig Roman C (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. (England) 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. ISSN 0261-4189. PMC 125981. PMID 11980706. 
  9. ^ Castro, Ariel F; Rebhun John F; Clark Geoffrey J; Quilliam Lawrence A (August 2003). "Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner". J. Biol. Chem. (United States) 278 (35): 32493–6. doi:10.1074/jbc.C300226200. ISSN 0021-9258. PMID 12842888. 
  10. ^ Yamamoto, Yuji; Jones Kathryn A; Mak Baldwin C; Muehlenbachs Atis; Yeung Raymond S (August 2002). "Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin". Arch. Biochem. Biophys. (United States) 404 (2): 210–7. doi:10.1016/S0003-9861(02)00300-4. ISSN 0003-9861. PMID 12147258. 
  11. ^ a b Boettner, B; Govek E E; Cross J; Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. ISSN 0027-8424. PMC 16822. PMID 10922060. 
  12. ^ Nancy, V; Wolthuis R M, de Tand M F, Janoueix-Lerosey I, Bos J L, de Gunzburg J (March 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. (UNITED STATES) 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. ISSN 0021-9258. PMID 10085114. 
  13. ^ Rebhun, J F; Castro A F; Quilliam L A (November 2000). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". J. Biol. Chem. (UNITED STATES) 275 (45): 34901–8. doi:10.1074/jbc.M005327200. ISSN 0021-9258. PMID 10934204.