RAP1B

RAP1B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3BRW, 3CF6, 4DXA, 4HDO, 4HDQ, 4M8N, 4MGI, 4MGK, 4MGY, 4MGZ, 4MH0
Identifiers
Aliases	RAP1B , K-REV, RAL1B, member of RAS oncogene family
External IDs	OMIM: 179530; MGI: 894315; HomoloGene: 68719; GeneCards: RAP1B; OMA:RAP1B - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q15 Start 68,610,855 bp [1] End 68,671,901 bp [1]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [2] Band 10|10 D2 Start 117,649,776 bp [2] End 117,681,940 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte Achilles tendon lymph node granulocyte appendix endometrium smooth muscle tissue gonad tibial arteries bone marrow Top expressed in left lung lobe blood decidua stroma of bone marrow right lung lobe endocardial cushion ureter dermis gastrula endothelial cell of lymphatic vessel More reference expression data BioGPS n/a
Gene ontology Molecular function nucleotide binding GDP binding protein-containing complex binding GTP binding protein binding GTPase activity Cellular component cytoplasm cytosol membrane cell-cell junction plasma membrane lipid droplet intracellular anatomical structure cell junction membrane raft extracellular exosome azurophil granule membrane Biological process establishment of endothelial barrier microvillus assembly regulation of cell junction assembly Rap protein signal transduction regulation of establishment of cell polarity cellular response to cAMP signal transduction neutrophil degranulation interleukin-12-mediated signaling pathway small GTPase mediated signal transduction cell population proliferation response to carbohydrate negative regulation of calcium ion-dependent exocytosis positive regulation of ERK1 and ERK2 cascade cellular response to organic cyclic compound cellular response to gonadotropin-releasing hormone negative regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5908 215449 Ensembl ENSG00000127314 ENSMUSG00000052681 UniProt P61224 Q99JI6 RefSeq (mRNA) NM_015646 NM_001010942 NM_001251917 NM_001251918 NM_001251921 NM_001251922 NM_024457 RefSeq (protein) NP_001010942 NP_001238846 NP_001238847 NP_001238850 NP_001238851 NP_056461 NP_001010942.1 NP_056461.1 NP_077777 Location (UCSC) Chr 12: 68.61 – 68.67 Mb Chr 10: 117.65 – 117.68 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ras-related protein Rap-1b, also known as GTP-binding protein smg p21B, is a protein that in humans is encoded by the RAP1B gene. ^{[5] [6] [7] [8]}

References

1. GRCh38: Ensembl release 89: ENSG00000127314 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052681 – 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: RAP1B".
6. Pizon V, Lerosey I, Chardin P, Tavitian A (August 1988). "Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B)". Nucleic Acids Res. 16 (15): 7719. doi:10.1093/nar/16.15.7719. PMC   338441 . PMID   3137530.
7. Matsui Y, Kikuchi A, Kawata M, Kondo J, Teranishi Y, Takai Y (January 1990). "Molecular cloning of smg p21B and identification of smg p21 purified from bovine brain and human platelets as smg p21B". Biochem. Biophys. Res. Commun. 166 (2): 1010–6. doi:10.1016/0006-291X(90)90911-6. PMID   2105724.
8. Rousseau-Merck MF, Pizon V, Tavitian A, Berger R (1990). "Chromosome mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to chromosomes 1p12----p13, 12q14, and 13q34, respectively". Cytogenet. Cell Genet. 53 (1): 2–4. doi:10.1159/000132883. PMID   2108841.

Further reading

• Rehmann H, Arias-Palomo E, Hadders MA, et al. (2008). "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B". Nature. 455 (7209): 124–7. Bibcode:2008Natur.455..124R. doi:10.1038/nature07187. PMID   18660803. S2CID   4393652.
• Gyan E, Frew M, Bowen D, et al. (2005). "Mutation in RAP1 is a rare event in myelodysplastic syndromes". Leukemia. 19 (9): 1678–80. doi: 10.1038/sj.leu.2403882 . PMID   16118622.
• Carmona G, Göttig S, Orlandi A, et al. (2009). "Role of the small GTPase Rap1 for integrin activity regulation in endothelial cells and angiogenesis". Blood. 113 (2): 488–97. doi: 10.1182/blood-2008-02-138438 . PMID   18805968. S2CID   206868671.
• Shattil SJ (2005). "Integrins and Src: dynamic duo of adhesion signaling". Trends Cell Biol. 15 (8): 399–403. doi:10.1016/j.tcb.2005.06.005. PMID   16005629.
• Malchinkhuu E, Sato K, Maehama T, et al. (2009). "Role of Rap1B and tumor suppressor PTEN in the negative regulation of lysophosphatidic acid--induced migration by isoproterenol in glioma cells". Mol. Biol. Cell. 20 (24): 5156–65. doi:10.1091/mbc.E09-08-0692. PMC   2793292 . PMID   19864456.
• Daumke O, Weyand M, Chakrabarti PP, et al. (2004). "The GTPase-activating protein Rap1GAP uses a catalytic asparagine". Nature. 429 (6988): 197–201. Bibcode:2004Natur.429..197D. doi:10.1038/nature02505. PMID   15141215. S2CID   4426744.
• 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.
• Edreira MM, Li S, Hochbaum D, et al. (2009). "Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop". J. Biol. Chem. 284 (40): 27480–6. doi: 10.1074/jbc.M109.011312 . PMC   2785677 . PMID   19651783.
• Scrima A, Thomas C, Deaconescu D, Wittinghofer A (2008). "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues". EMBO J. 27 (7): 1145–53. doi:10.1038/emboj.2008.30. PMC   2265111 . PMID   18309292.
• Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC   1347501 . PMID   16381901.
• Canobbio I, Trionfini P, Guidetti GF, et al. (2008). "Targeting of the small GTPase Rap2b, but not Rap1b, to lipid rafts is promoted by palmitoylation at Cys176 and Cys177 and is required for efficient protein activation in human platelets". Cell. Signal. 20 (9): 1662–70. doi:10.1016/j.cellsig.2008.05.016. PMID   18582561.
• Bernardi B, Guidetti GF, Campus F, et al. (2006). "The small GTPase Rap1b regulates the cross talk between platelet integrin alpha2beta1 and integrin alphaIIbbeta3". Blood. 107 (7): 2728–35. doi:10.1182/blood-2005-07-3023. PMC   1895386 . PMID   16357324.
• Matsuse M, Mitsutake N, Rogounovitch T, et al. (2009). "Mutation analysis of RAP1 gene in papillary thyroid carcinomas". Endocr. J. 56 (1): 161–4. doi: 10.1507/endocrj.k08e-244 . PMID   18948674.
• Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC   528930 . PMID   15489336.
• Li YH, Werner H, Püschel AW (2008). "Rheb and mTOR regulate neuronal polarity through Rap1B". J. Biol. Chem. 283 (48): 33784–92. doi: 10.1074/jbc.M802431200 . PMC   2662285 . PMID   18842593.
• Lova P, Campus F, Lombardi R, et al. (2004). "Contribution of protease-activated receptors 1 and 4 and glycoprotein Ib-IX-V in the G(i)-independent activation of platelet Rap1B by thrombin". J. Biol. Chem. 279 (24): 25299–306. doi: 10.1074/jbc.M313199200 . PMID   15078882.
• Yan J, Li F, Ingram DA, Quilliam LA (2008). "Rap1a is a key regulator of fibroblast growth factor 2-induced angiogenesis and together with Rap1b controls human endothelial cell functions". Mol. Cell. Biol. 28 (18): 5803–10. doi:10.1128/MCB.00393-08. PMC   2546931 . PMID   18625726.
• Campus F, Lova P, Bertoni A, et al. (2005). "Thrombopoietin complements G(i)- but not G(q)-dependent pathways for integrin {alpha}(IIb){beta}(3) activation and platelet aggregation". J. Biol. Chem. 280 (26): 24386–95. doi: 10.1074/jbc.M501174200 . PMID   15863506.
• Defilippi P, Di Stefano P, Cabodi S (2006). "p130Cas: a versatile scaffold in signaling networks". Trends Cell Biol. 16 (5): 257–63. doi:10.1016/j.tcb.2006.03.003. PMID   16581250.