RAP1B

Protein-coding gene in the species Homo sapiens

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]
Band	12q15	End	68,671,901 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 D2	Start	117,649,776 bp^[2]
Band	10\|10 D2	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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000127314 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000052681 – 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.
^ "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. 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.

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