RAP2B

1N4P, 1N4Q, 1N4R, 1N4S

RAP2B

Identifiers

RAP2B, member of RAS oncogene family

External IDs

OMIM: 179541; MGI: 1921262; GeneCards: RAP2B

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1N4P, 1N4Q, 1N4R, 1N4S

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
3.6.5.2	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 3 (human)^[1]

Band	3q25.2	Start	153,162,226 bp^[1]
Band	3q25.2	End	153,170,627 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3\|3 E1	Start	61,269,059 bp^[2]
Band	3\|3 E1	End	61,275,851 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

gingival epithelium

germinal epithelium

buccal mucosa cell

amniotic fluid

tendon of biceps brachii

mucosa of pharynx

hair follicle

human penis

palpebral conjunctiva

secondary oocyte

Top expressed in

aortic valve

cumulus cell

ascending aorta

epithelium of lens

lumbar subsegment of spinal cord

Rostral migratory stream

tibiofemoral joint

calvaria

external carotid artery

dorsal striatum

More reference expression data


More reference expression data

Gene ontology
Molecular function	nucleotide binding protein domain specific binding GDP binding GTP binding protein binding GTPase activity
Cellular component	recycling 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 membrane
Biological process	regulation 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 degranulation
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


5912


74012


ENSG00000181467


ENSMUSG00000036894


P61225


P61226

RefSeq (mRNA)


NM_002886


NM_028712

RefSeq (protein)


NP_002877


NP_082988

Location (UCSC)

Chr 3: 153.16 – 153.17 Mb

Chr 3: 61.27 – 61.28 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

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.

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

^ ^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

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. 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.

v t e PDB gallery
1kao: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAP2A WITH GDP 2rap: THE SMALL G PROTEIN RAP2A IN COMPLEX WITH GTP 3rap: The small G protein Rap2 in a non catalytic complex with GTP

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