RAP1B

RAP1B, member of RAS oncogene family

PDB rendering based on 1c1y.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3BRW, 3CF6, 4DXA, 4HDO, 4HDQ, 4M8N, 4MGI, 4MGK, 4MGY, 4MGZ, 4MH0

Identifiers

Symbols

RAP1B ; K-REV; RAL1B

External IDs

OMIM: 179530 MGI: 894315 HomoloGene: 68719 GeneCards: RAP1B Gene

Gene ontology
Molecular function	• GTPase activity • protein binding • GTP binding • GDP binding • protein complex binding
Cellular component	• intracellular • lipid particle • cytosol • plasma membrane • cell-cell junction • membrane • membrane raft • extracellular exosome
Biological process	• blood coagulation • cell proliferation • microvillus assembly • platelet activation • Rap protein signal transduction • negative regulation of calcium ion-dependent exocytosis • establishment of endothelial barrier • positive regulation of ERK1 and ERK2 cascade • cellular response to cAMP • regulation of cell junction assembly • regulation of establishment of cell polarity • negative regulation of synaptic vesicle exocytosis
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
68.61 – 68.67 Mb

Chr 10:
117.81 – 117.85 Mb

PubMed search

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.^[1]^[2]^[3]^[4]

References

↑ "Entrez Gene: RAP1B".
↑ 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.
↑ 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.
↑ 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.

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. doi:10.1038/nature07187. PMID 18660803.
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.
Schwamborn JC, Müller M, Becker AH, Püschel AW (2007). "Ubiquitination of the GTPase Rap1B by the ubiquitin ligase Smurf2 is required for the establishment of neuronal polarity.". EMBO J. 26 (5): 1410–22. doi:10.1038/sj.emboj.7601580. PMC 1817628. PMID 17318188.
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.
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. doi:10.1038/nature02505. PMID 15141215.
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.

PDB gallery

1c1y: CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).

1gua: HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131

3brw: Structure of the Rap-RapGAP complex

3cf6: Structure of Epac2 in complex with cyclic-AMP and Rap

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RAP1B

References

Further reading