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Gene Review

RAP2A  -  RAP2A, member of RAS oncogene family

Homo sapiens

Synonyms: K-REV, KREV, RAP2, Ras-related protein Rap-2a, RbBP-30
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Disease relevance of RAP2A


Psychiatry related information on RAP2A


High impact information on RAP2A

  • The accelerated cell migration was suppressed by the expression of active Rap1, Rap2 and R-Ras [5].
  • RAP2B is 90% identical to RAP2 at the amino acid level with the most variability at the carboxyl terminus of the protein [6].
  • Nitric Oxide Produced in Response to Engagement of beta2 Integrins on Human Neutrophils Activates the Monomeric GTPases Rap1 and Rap2 and Promotes Adhesion [7].
  • Surprisingly, the beta2 integrin-induced activation of Rap2 was not regulated by any of the signaling pathways mentioned above [7].
  • Among our observations, TNIK interacted with Rap2 through its CNH domain but did not interact with Rap1 or Ras [8].

Biological context of RAP2A


Anatomical context of RAP2A

  • When co-expressed in cultured cells, TNIK colocalized with Rap2, while a mutant TNIK lacking the CNH domain did not [8].
  • To identify the specific isoprenoid attached to each protein, the cDNAs were transcribed in vitro and the rap2 specific RNA was translated in a rabbit reticulocyte lysate system in the presence of [3H]mevalonolactone [4].
  • Rap2, but not Rap1 GTPase is expressed in human red blood cells and is involved in vesiculation [12].
  • By immunoblot analysis, we observed that rap2p is predominantly located in specific granules, whereas rap1p is detected both in specific granules and a fraction enriched in plasma membranes [13].
  • Neither rap1p nor rap2p was found in the cytosol or in azurophil granules [13].

Associations of RAP2A with chemical compounds


Regulatory relationships of RAP2A


Other interactions of RAP2A

  • Rap2 potently enhanced the inhibitory function of TNIK against cell spreading, but this was not observed for the mutant TNIK lacking the CNH domain [8].
  • Little is known about the specific signaling roles of Rap2, a Ras family small GTP-binding protein [18].
  • The rap1 and rap2 genes encode proteins of 184 and 183 amino acid respectively with molecular weights of 20.9 kd and 20.7 kd [19].
  • The human rap2 gene encodes a 183 amino acid protein that shares 46% identity with the K-ras p21 [20].
  • These properties of the normal and mutant rap2 proteins are compared with those of ras p21 carrying similar substitutions and are discussed in relation to the structural models proposed for ras p21 [20].

Analytical, diagnostic and therapeutic context of RAP2A

  • The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site-directed mutagenesis [20].
  • Epac2 and Rap2 were detected in hamster spermatozoa using immunoblotting [21].
  • Western blot analysis indicated that the protein level of Ras and RalB in both the cytosolic and membranous fractions and that of Rap2 in the cytosolic fraction was significantly decreased, while that of Rab8 in the membranous fraction was significantly increased in AD brains compared with controls [22].


  1. Isoprenylation of rap2 proteins in platelets and human erythroleukemia cells. Winegar, D.A., Molina y Vedia, L., Lapetina, E.G. J. Biol. Chem. (1991) [Pubmed]
  2. Expression of RPIP9 (Rap2 interacting protein 9) is activated in breast carcinoma and correlates with a poor prognosis. Raguz, S., De Bella, M.T., Slade, M.J., Higgins, C.F., Coombes, R.C., Yagüe, E. Int. J. Cancer (2005) [Pubmed]
  3. Expression of the ras-related rap genes in human tumors. Culine, S., Olofsson, B., Gosselin, S., Honore, N., Tavitian, A. Int. J. Cancer (1989) [Pubmed]
  4. Prenyl group identification of rap2 proteins: a ras superfamily member other than ras that is farnesylated. Farrell, F.X., Yamamoto, K., Lapetina, E.G. Biochem. J. (1993) [Pubmed]
  5. Requirement for C3G-dependent Rap1 activation for cell adhesion and embryogenesis. Ohba, Y., Ikuta, K., Ogura, A., Matsuda, J., Mochizuki, N., Nagashima, K., Kurokawa, K., Mayer, B.J., Maki, K., Miyazaki , J., Matsuda, M. EMBO J. (2001) [Pubmed]
  6. RAP2B: a RAS-related GTP-binding protein from platelets. Ohmstede, C.A., Farrell, F.X., Reep, B.R., Clemetson, K.J., Lapetina, E.G. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  7. Nitric Oxide Produced in Response to Engagement of beta2 Integrins on Human Neutrophils Activates the Monomeric GTPases Rap1 and Rap2 and Promotes Adhesion. Jenei, V., Deevi, R.K., Adams, C.A., Axelsson, L., Hirst, D.G., Andersson, T., Dib, K. J. Biol. Chem. (2006) [Pubmed]
  8. The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton. Taira, K., Umikawa, M., Takei, K., Myagmar, B.E., Shinzato, M., Machida, N., Uezato, H., Nonaka, S., Kariya, K. J. Biol. Chem. (2004) [Pubmed]
  9. Identification of a specific effector of the small GTP-binding protein Rap2. Janoueix-Lerosey, I., Pasheva, E., de Tand, M.F., Tavitian, A., de Gunzburg, J. Eur. J. Biochem. (1998) [Pubmed]
  10. Identification and disruption of the gene encoding the third member of the low-molecular-mass rhoptry complex in Plasmodium falciparum. Baldi, D.L., Good, R., Duraisingh, M.T., Crabb, B.S., Cowman, A.F. Infect. Immun. (2002) [Pubmed]
  11. Assessment of the humoral immune response against Plasmodium falciparum rhoptry-associated proteins 1 and 2. Stowers, A., Taylor, D., Prescott, N., Cheng, Q., Cooper, J., Saul, A. Infect. Immun. (1997) [Pubmed]
  12. Rap2, but not Rap1 GTPase is expressed in human red blood cells and is involved in vesiculation. Greco, F., Ciana, A., Pietra, D., Balduini, C., Minetti, G., Torti, M. Biochim. Biophys. Acta (2006) [Pubmed]
  13. Association of rap1 and rap2 proteins with the specific granules of human neutrophils. Translocation to the plasma membrane during cell activation. Maridonneau-Parini, I., de Gunzburg, J. J. Biol. Chem. (1992) [Pubmed]
  14. Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras. Gao, X., Satoh, T., Liao, Y., Song, C., Hu, C.D., Kariya Ki, K., Kataoka, T. J. Biol. Chem. (2001) [Pubmed]
  15. Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity. Wienecke, R., König, A., DeClue, J.E. J. Biol. Chem. (1995) [Pubmed]
  16. Post-translational processing and subcellular localization of the Ras-related Rap2 protein. Béranger, F., Tavitian, A., de Gunzburg, J. Oncogene (1991) [Pubmed]
  17. PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector. Myagmar, B.E., Umikawa, M., Asato, T., Taira, K., Oshiro, M., Hino, A., Takei, K., Uezato, H., Kariya, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  18. Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase. Machida, N., Umikawa, M., Takei, K., Sakima, N., Myagmar, B.E., Taira, K., Uezato, H., Ogawa, Y., Kariya, K. J. Biol. Chem. (2004) [Pubmed]
  19. Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Pizon, V., Chardin, P., Lerosey, I., Olofsson, B., Tavitian, A. Oncogene (1988) [Pubmed]
  20. The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site-directed mutagenesis. Lerosey, I., Chardin, P., de Gunzburg, J., Tavitian, A. J. Biol. Chem. (1991) [Pubmed]
  21. Roles of cAMP in regulating microtubule sliding and flagellar bending in demembranated hamster spermatozoa. Kinukawa, M., Oda, S., Shirakura, Y., Okabe, M., Ohmuro, J., Baba, S.A., Nagata, M., Aoki, F. FEBS Lett. (2006) [Pubmed]
  22. Differential involvement of small G proteins in Alzheimer's disease. Shimohama, S., Kamiya, S., Taniguchi, T., Sumida, Y., Fujimoto, S. Int. J. Mol. Med. (1999) [Pubmed]
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