This intronless gene belongs to a family of RAS-related genes. The proteins encoded by these genes share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between the RAP and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. Evidence suggests that this protein may be polyisoprenylated and palmitoylated.[6]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000181467 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000036894 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Ohmstede CA, Farrell FX, Reep BR, Clemetson KJ, Lapetina EG (Oct 1990). "RAP2B: a RAS-related GTP-binding protein from platelets". Proc Natl Acad Sci U S A. 87 (17): 6527–31. Bibcode:1990PNAS...87.6527O. doi:10.1073/pnas.87.17.6527. PMC54569. PMID 2118648.
^ ab"Entrez Gene: RAP2B RAP2B, member of RAS oncogene family".
Further readingedit
Farrell FX, Ohmstede CA, Reep BR, Lapetina EG (1990). "cDNA sequence of a new ras-related gene (rap2b) isolated from human platelets with sequence homology to rap2". Nucleic Acids Res. 18 (14): 4281. doi:10.1093/nar/18.14.4281. PMC331220. PMID 2115998.
Pizon V, Chardin P, Lerosey I, et al. (1988). "Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region". Oncogene. 3 (2): 201–4. PMID 3045729.
Torti M, Ramaschi G, Sinigaglia F, et al. (1993). "Association of the low molecular weight GTP-binding protein rap2B with the cytoskeleton during platelet aggregation". Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7553–7. Bibcode:1993PNAS...90.7553T. doi:10.1073/pnas.90.16.7553. PMC47180. PMID 8356055.
Mollinedo F, Perez-Sala D, Gajate C, et al. (1993). "Localization of rap1 and rap2 proteins in the gelatinase-containing granules of human neutrophils". FEBS Lett. 326 (1–3): 209–14. doi:10.1016/0014-5793(93)81792-X. PMID 8391995. S2CID 6867463.
Farrell FX, Yamamoto K, Lapetina EG (1993). "Prenyl group identification of rap2 proteins: a ras superfamily member other than ras that is farnesylated". Biochem. J. 289 ( Pt 2) (Pt 2): 349–55. doi:10.1042/bj2890349. PMC1132174. PMID 8424780.
Nancy V, Wolthuis RM, de Tand MF, et al. (1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.
Rebhun JF, Castro AF, Quilliam LA (2001). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". J. Biol. Chem. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204.
Nancy V, Callebaut I, El Marjou A, de Gunzburg J (2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". J. Biol. Chem. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
Evellin S, Nolte J, Tysack K, et al. (2002). "Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B". J. Biol. Chem. 277 (19): 16805–13. doi:10.1074/jbc.M112024200. PMID 11877431.
Song C, Satoh T, Edamatsu H, et al. (2002). "Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon". Oncogene. 21 (53): 8105–13. doi:10.1038/sj.onc.1206003. PMID 12444546.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. PMC139241. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Greco F, Sinigaglia F, Balduini C, Torti M (2005). "Activation of the small GTPase Rap2B in agonist-stimulated human platelets". J. Thromb. Haemost. 2 (12): 2223–30. doi:10.1111/j.1538-7836.2004.01018.x. PMID 15613030. S2CID 25336596.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Liu Y, Sun W, Zhang K, et al. (2007). "Identification of genes differentially expressed in human primary lung squamous cell carcinoma". Lung Cancer. 56 (3): 307–17. doi:10.1016/j.lungcan.2007.01.016. PMID 17316888.
This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.
rap2b, related, protein, protein, that, humans, encoded, gene, belongs, related, protein, family, available, structurespdbortholog, search, pdbe, rcsblist, codes1n4p, 1n4q, 1n4r, 1n4sidentifiersaliases, member, oncogene, familyexternal, idsomim, 179541, 192126. Ras related protein Rap 2b is a protein that in humans is encoded by the RAP2B gene 5 6 RAP2B belongs to the Ras related protein family RAP2BAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1N4P 1N4Q 1N4R 1N4SIdentifiersAliasesRAP2B member of RAS oncogene familyExternal IDsOMIM 179541 MGI 1921262 HomoloGene 55701 GeneCards RAP2BGene location Human Chr Chromosome 3 human 1 Band3q25 2Start153 162 226 bp 1 End153 170 627 bp 1 Gene location Mouse Chr Chromosome 3 mouse 2 Band3 3 E1Start61 269 059 bp 2 End61 275 851 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingerminal epitheliumamniotic fluidhair folliclehuman penispalpebral conjunctivasecondary oocyteoral cavitysynovial jointsynovial membraneparietal pleuraTop expressed inaortic valvecumulus cellascending aortacalvariaexternal carotid arterymolarbloodinternal carotid arteryRegion I of hippocampus propersubiculumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding protein domain specific binding GDP binding GTP binding protein binding GTPase activityCellular componentrecycling endosome cytosol endosome membrane cell cell contact zone bicellular tight junction recycling endosome membrane membrane raft extracellular exosome plasma membrane specific granule membrane tertiary granule membraneBiological processregulation of protein tyrosine kinase activity microvillus assembly establishment of endothelial intestinal barrier Rap protein signal transduction platelet activation negative regulation of cell migration positive regulation of protein autophosphorylation platelet aggregation signal transduction neutrophil degranulationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez591274012EnsemblENSG00000181467ENSMUSG00000036894UniProtP61225P61226RefSeq mRNA NM 002886NM 028712RefSeq protein NP 002877NP 082988Location UCSC Chr 3 153 16 153 17 MbChr 3 61 27 61 28 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse This intronless gene belongs to a family of RAS related genes The proteins encoded by these genes share approximately 50 amino acid identity with the classical RAS proteins and have numerous structural features in common The most striking difference between the RAP and RAS proteins resides in their 61st amino acid glutamine in RAS is replaced by threonine in RAP proteins Evidence suggests that this protein may be polyisoprenylated and palmitoylated 6 References edit a b c GRCh38 Ensembl release 89 ENSG00000181467 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000036894 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Ohmstede CA Farrell FX Reep BR Clemetson KJ Lapetina EG Oct 1990 RAP2B a RAS related GTP binding protein from platelets Proc Natl Acad Sci U S A 87 17 6527 31 Bibcode 1990PNAS 87 6527O doi 10 1073 pnas 87 17 6527 PMC 54569 PMID 2118648 a b Entrez Gene RAP2B RAP2B member of RAS oncogene family Further reading editFarrell FX Ohmstede CA Reep BR Lapetina EG 1990 cDNA sequence of a new ras related gene rap2b isolated from human platelets with sequence homology to rap2 Nucleic Acids Res 18 14 4281 doi 10 1093 nar 18 14 4281 PMC 331220 PMID 2115998 Pizon V Chardin P Lerosey I et al 1988 Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the effector region Oncogene 3 2 201 4 PMID 3045729 Torti M Ramaschi G Sinigaglia F et al 1993 Association of the low molecular weight GTP binding protein rap2B with the cytoskeleton during platelet aggregation Proc Natl Acad Sci U S A 90 16 7553 7 Bibcode 1993PNAS 90 7553T doi 10 1073 pnas 90 16 7553 PMC 47180 PMID 8356055 Mollinedo F Perez Sala D Gajate C et al 1993 Localization of rap1 and rap2 proteins in the gelatinase containing granules of human neutrophils FEBS Lett 326 1 3 209 14 doi 10 1016 0014 5793 93 81792 X PMID 8391995 S2CID 6867463 Farrell FX Yamamoto K Lapetina EG 1993 Prenyl group identification of rap2 proteins a ras superfamily member other than ras that is farnesylated Biochem J 289 Pt 2 Pt 2 349 55 doi 10 1042 bj2890349 PMC 1132174 PMID 8424780 Nancy V Wolthuis RM de Tand MF et al 1999 Identification and characterization of potential effector molecules of the Ras related GTPase Rap2 J Biol Chem 274 13 8737 45 doi 10 1074 jbc 274 13 8737 PMID 10085114 Rebhun JF Castro AF Quilliam LA 2001 Identification of guanine nucleotide exchange factors GEFs for the Rap1 GTPase Regulation of MR GEF by M Ras GTP interaction J Biol Chem 275 45 34901 8 doi 10 1074 jbc M005327200 PMID 10934204 Nancy V Callebaut I El Marjou A de Gunzburg J 2002 The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases J Biol Chem 277 17 15076 84 doi 10 1074 jbc M109983200 PMID 11786539 Evellin S Nolte J Tysack K et al 2002 Stimulation of phospholipase C epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B J Biol Chem 277 19 16805 13 doi 10 1074 jbc M112024200 PMID 11877431 Song C Satoh T Edamatsu H et al 2002 Differential roles of Ras and Rap1 in growth factor dependent activation of phospholipase C epsilon Oncogene 21 53 8105 13 doi 10 1038 sj onc 1206003 PMID 12444546 Strausberg RL Feingold EA Grouse LH et al 2003 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 Gerhard DS Wagner L Feingold EA et al 2004 The Status Quality and Expansion of the NIH Full Length cDNA Project The Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Greco F Sinigaglia F Balduini C Torti M 2005 Activation of the small GTPase Rap2B in agonist stimulated human platelets J Thromb Haemost 2 12 2223 30 doi 10 1111 j 1538 7836 2004 01018 x PMID 15613030 S2CID 25336596 Rual JF Venkatesan K Hao T et al 2005 Towards a proteome scale map of the human protein protein interaction network Nature 437 7062 1173 8 Bibcode 2005Natur 437 1173R doi 10 1038 nature04209 PMID 16189514 S2CID 4427026 Liu Y Sun W Zhang K et al 2007 Identification of genes differentially expressed in human primary lung squamous cell carcinoma Lung Cancer 56 3 307 17 doi 10 1016 j lungcan 2007 01 016 PMID 17316888 nbsp This article on a gene on human chromosome 3 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title RAP2B amp oldid 1142698670, wikipedia, wiki, book, books, library,
