RAP2A

RAP2A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1KAO, 2RAP, 3RAP
Identifiers
Aliases	RAP2A, K-REV, KREV, RAP2, RbBP-30, member of RAS oncogene family
External IDs	OMIM: 179540; MGI: 97855; HomoloGene: 10875; GeneCards: RAP2A; OMA:RAP2A - orthologs
Gene location (Human)
Chr.	Chromosome 13 (human)
End	97,469,128 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	120,744,606 bp
RNA expression pattern
	Top expressed in
	pons; ; buccal mucosa cell; ; internal globus pallidus; ; superior vestibular nucleus; ; subthalamic nucleus; ; parietal lobe; ; middle temporal gyrus; ; Brodmann area 23; ; inferior ganglion of vagus nerve; ; postcentral gyrus;
	Top expressed in
	sciatic nerve; ; Region I of hippocampus proper; ; subiculum; ; left lung lobe; ; ventromedial nucleus; ; barrel cortex; ; anterior amygdaloid area; ; optic nerve; ; nucleus of stria terminalis; ; primary motor cortex;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; protein binding; magnesium ion binding; GTPase activity; GTP binding; GDP binding;
Cellular component	recycling endosome; cytosol; endosome; membrane; plasma membrane; recycling endosome membrane; midbody;
Biological process	actin cytoskeleton reorganization; microvillus assembly; positive regulation of protein phosphorylation; establishment of protein localization; Rap protein signal transduction; regulation of dendrite morphogenesis; regulation of JNK cascade; negative regulation of cell migration; establishment of epithelial cell apical/basal polarity; positive regulation of protein autophosphorylation; protein localization to plasma membrane; signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	5911
	76108
	ENSG00000125249
	ENSMUSG00000051615
	P10114
	Q80ZJ1
	NM_021033
	NM_029519
	NP_066361
	NP_083795
	Wikidata
View/Edit Human	View/Edit Mouse

Ras-related protein Rap-2a is a protein that in humans is encoded by the RAP2A gene.^[5] RAP2A is a member of the Ras-related protein family.

Interactions

RAP2A has been shown to interact with RUNDC3A,^[6] RASSF5^[7] and RALGDS.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000125249 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000051615 – 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: RAP2A RAP2A, member of RAS oncogene family".
^ Janoueix-Lerosey I, Pasheva E, de Tand MF, Tavitian A, de Gunzburg J (Mar 1998). "Identification of a specific effector of the small GTP-binding protein Rap2". European Journal of Biochemistry. 252 (2): 290–8. doi:10.1046/j.1432-1327.1998.2520290.x. PMID 9523700.
^ Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (Feb 2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene. 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID 11857081. S2CID 240243.
^ Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (Mar 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". The Journal of Biological Chemistry. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.

Lerosey I, Chardin P, de Gunzburg J, Tavitian A (Mar 1991). "The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site-directed mutagenesis". The Journal of Biological Chemistry. 266 (7): 4315–21. doi:10.1016/S0021-9258(20)64324-1. PMID 1900290.
Pizon V, Chardin P, Lerosey I, Olofsson B, Tavitian A (Aug 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.
Farrell FX, Yamamoto K, Lapetina EG (Jan 1993). "Prenyl group identification of rap2 proteins: a ras superfamily member other than ras that is farnesylated". The Biochemical Journal. 289 ( Pt 2) (Pt 2): 349–55. doi:10.1042/bj2890349. PMC 1132174. PMID 8424780.
Cherfils J, Ménétrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I (Sep 1997). "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS". The EMBO Journal. 16 (18): 5582–91. doi:10.1093/emboj/16.18.5582. PMC 1170190. PMID 9312017.
Janoueix-Lerosey I, Pasheva E, de Tand MF, Tavitian A, de Gunzburg J (Mar 1998). "Identification of a specific effector of the small GTP-binding protein Rap2". European Journal of Biochemistry. 252 (2): 290–8. doi:10.1046/j.1432-1327.1998.2520290.x. PMID 9523700.
Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (Mar 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". The Journal of Biological Chemistry. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.
Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C (May 1999). "Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily". The Journal of Biological Chemistry. 274 (19): 13556–62. doi:10.1074/jbc.274.19.13556. PMID 10224125.
Ménétrey J, Cherfils J (Nov 1999). "Structure of the small G protein Rap2 in a non-catalytic complex with GTP". Proteins. 37 (3): 465–73. doi:10.1002/(SICI)1097-0134(19991115)37:3<465::AID-PROT13>3.0.CO;2-O. PMID 10591105.
de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL (Jul 2000). "Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs". The Journal of Biological Chemistry. 275 (27): 20829–36. doi:10.1074/jbc.M001113200. PMID 10777494.
Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (Jul 2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nature Neuroscience. 3 (7): 661–9. doi:10.1038/76615. hdl:1842/742. PMID 10862698. S2CID 14392630.
Traver S, Bidot C, Spassky N, Baltauss T, De Tand MF, Thomas JL, Zalc B, Janoueix-Lerosey I, Gunzburg JD (Aug 2000). "RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao". The Biochemical Journal. 350 Pt 1 (Pt 1): 19–29. doi:10.1042/0264-6021:3500019. PMC 1221220. PMID 10926822.
Gao X, Satoh T, Liao Y, Song C, Hu CD, Kariya Ki K, Kataoka T (Nov 2001). "Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras". The Journal of Biological Chemistry. 276 (45): 42219–25. doi:10.1074/jbc.M105760200. PMID 11524421.
Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (Feb 2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene. 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID 11857081. S2CID 240243.
Song C, Satoh T, Edamatsu H, Wu D, Tadano M, Gao X, Kataoka T (Nov 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. S2CID 13499744.
Kuiperij HB, de Rooij J, Rehmann H, van Triest M, Wittinghofer A, Bos JL, Zwartkruis FJ (Feb 2003). "Characterisation of PDZ-GEFs, a family of guanine nucleotide exchange factors specific for Rap1 and Rap2". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1593 (2–3): 141–9. doi:10.1016/S0167-4889(02)00365-8. PMID 12581858.
Machida N, Umikawa M, Takei K, Sakima N, Myagmar BE, Taira K, Uezato H, Ogawa Y, Kariya K (Apr 2004). "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase". The Journal of Biological Chemistry. 279 (16): 15711–4. doi:10.1074/jbc.C300542200. PMID 14966141.
Mitin NY, Ramocki MB, Zullo AJ, Der CJ, Konieczny SF, Taparowsky EJ (May 2004). "Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization". The Journal of Biological Chemistry. 279 (21): 22353–61. doi:10.1074/jbc.M312867200. PMID 15031288.

This article on a gene on human chromosome 13 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000125249 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000051615 – 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.

[entrez-5] "Entrez Gene: RAP2A RAP2A, member of RAS oncogene family".

[pmid9523700-6] Janoueix-Lerosey I, Pasheva E, de Tand MF, Tavitian A, de Gunzburg J (Mar 1998). "Identification of a specific effector of the small GTP-binding protein Rap2". European Journal of Biochemistry. 252 (2): 290–8. doi:10.1046/j.1432-1327.1998.2520290.x. PMID 9523700.

[pmid11857081-7] Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (Feb 2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene. 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID 11857081. S2CID 240243.

[pmid10085114-8] Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (Mar 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". The Journal of Biological Chemistry. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

Interactions

References

Further reading