RAP1A

RAP1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1C1Y, 1GUA, 3KUC, 4KVG
Identifiers
Aliases	RAP1A, C21KG, G-22K, KREV-1, KREV1, RAP1, SMGP21, member of RAS oncogene family
External IDs	OMIM: 179520; MGI: 97852; HomoloGene: 2162; GeneCards: RAP1A; OMA:RAP1A - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	111,716,691 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	105,708,652 bp
RNA expression pattern
	Top expressed in
	monocyte; ; tail of epididymis; ; superficial temporal artery; ; popliteal artery; ; tibial arteries; ; jejunal mucosa; ; muscle layer of sigmoid colon; ; gastric mucosa; ; saphenous vein; ; right ventricle;
	Top expressed in
	tail of embryo; ; genital tubercle; ; jejunum; ; granulocyte; ; esophagus; ; stomach; ; thymus; ; placenta; ; dentate gyrus of hippocampal formation granule cell; ; duodenum;
	More reference expression data
	n/a
Gene ontology
Molecular function	nucleotide binding; protein-containing complex binding; GTP binding; protein binding; GTPase activity; GDP binding;
Cellular component	cytosol; endosome; membrane; myelin sheath; plasma membrane; guanyl-nucleotide exchange factor complex; neuron projection; extracellular exosome; early endosome; late endosome; cytoplasm; cell junction; perinuclear region of cytoplasm; specific granule membrane; phagocytic vesicle; glutamatergic synapse;
Biological process	establishment of endothelial barrier; positive regulation of glucose import; microvillus assembly; regulation of cell junction assembly; regulation of insulin secretion; small GTPase mediated signal transduction; Rap protein signal transduction; cellular response to organic cyclic compound; nervous system development; negative regulation of synaptic vesicle exocytosis; liver regeneration; protein transport; response to antineoplastic agent; response to carbohydrate; negative regulation of collagen biosynthetic process; cellular response to glucose stimulus; signal transduction; cellular response to nerve growth factor stimulus; nerve growth factor signaling pathway; positive regulation of ERK1 and ERK2 cascade; positive regulation of protein kinase activity; positive regulation of vasculogenesis; positive regulation of GTPase activity; cellular response to cAMP; positive regulation of neuron projection development; neutrophil degranulation; positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; protein localization to plasma membrane;
	Sources:Amigo / QuickGO
Orthologs
	5906
	109905
	ENSG00000116473
	ENSMUSG00000068798
	P62834
	P62835
NM_001010935; NM_001291896; NM_002884; NM_001370216; NM_001370217;
	NM_001394066
	NM_145541
	NP_001010935; NP_001278825; NP_002875; NP_001357145; NP_001357146
	NP_663516
	Wikidata
View/Edit Human	View/Edit Mouse

Ras-related protein Rap-1A is a protein that in humans is encoded by the RAP1A gene.^[5]

Function

The product of this gene belongs to the family of Ras-related proteins. These proteins share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between RAP proteins and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. The product of this gene counteracts the mitogenic function of RAS because it can interact with RAS GAPs and RAF in a competitive manner. Two transcript variants encoding the same protein have been identified for this gene.^[6]

Interactions

RAP1A has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116473 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000068798 – 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.
^ Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (Dec 1988). "A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization". The Journal of Biological Chemistry. 263 (35): 18965–71. doi:10.1016/S0021-9258(18)37376-9. PMID 3143720.
^ "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family".
^ Han L, Colicelli J (Mar 1995). "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1". Molecular and Cellular Biology. 15 (3): 1318–23. doi:10.1128/mcb.15.3.1318. PMC 230355. PMID 7862125.
^ Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A (Jun 1995). "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue". Nature. 375 (6532): 554–60. Bibcode:1995Natur.375..554N. doi:10.1038/375554a0. PMID 7791872. S2CID 4347807.
^ Hu CD, Kariya K, Okada T, Qi X, Song C, Kataoka T (Jan 1999). "Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation". The Journal of Biological Chemistry. 274 (1): 48–51. doi:10.1074/jbc.274.1.48. PMID 9867809.
^ Okada T, Hu CD, Jin TG, Kariya K, Yamawaki-Kataoka Y, Kataoka T (Sep 1999). "The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases". Molecular and Cellular Biology. 19 (9): 6057–64. doi:10.1128/mcb.19.9.6057. PMC 84512. PMID 10454553.
^ ^a ^b Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
^ Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
^ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
^ 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.
^ Rebhun JF, Castro AF, Quilliam LA (Nov 2000). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". The Journal of Biological Chemistry. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204.
^ Castro AF, Rebhun JF, Clark GJ, Quilliam LA (Aug 2003). "Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner". The Journal of Biological Chemistry. 278 (35): 32493–6. doi:10.1074/jbc.C300226200. PMID 12842888.
^ Yamamoto Y, Jones KA, Mak BC, Muehlenbachs A, Yeung RS (Aug 2002). "Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin". Archives of Biochemistry and Biophysics. 404 (2): 210–7. doi:10.1016/s0003-9861(02)00300-4. PMID 12147258.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000116473 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000068798 – 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.

[pmid3143720-5] Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (Dec 1988). "A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization". The Journal of Biological Chemistry. 263 (35): 18965–71. doi:10.1016/S0021-9258(18)37376-9. PMID 3143720.

[6] "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family".

[pmid7862125-7] Han L, Colicelli J (Mar 1995). "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1". Molecular and Cellular Biology. 15 (3): 1318–23. doi:10.1128/mcb.15.3.1318. PMC 230355. PMID 7862125.

[pmid7791872-8] Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A (Jun 1995). "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue". Nature. 375 (6532): 554–60. Bibcode:1995Natur.375..554N. doi:10.1038/375554a0. PMID 7791872. S2CID 4347807.

[pmid9867809-9] Hu CD, Kariya K, Okada T, Qi X, Song C, Kataoka T (Jan 1999). "Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation". The Journal of Biological Chemistry. 274 (1): 48–51. doi:10.1074/jbc.274.1.48. PMID 9867809.

[pmid10454553-10] Okada T, Hu CD, Jin TG, Kariya K, Yamawaki-Kataoka Y, Kataoka T (Sep 1999). "The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases". Molecular and Cellular Biology. 19 (9): 6057–64. doi:10.1128/mcb.19.9.6057. PMC 84512. PMID 10454553.

[pmid10922060-11] Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.

[pmid11786539-12] Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.

[pmid11980706-13] Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.

[pmid10085114-14] 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.

[pmid10934204-15] Rebhun JF, Castro AF, Quilliam LA (Nov 2000). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". The Journal of Biological Chemistry. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204.

[pmid12842888-16] Castro AF, Rebhun JF, Clark GJ, Quilliam LA (Aug 2003). "Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner". The Journal of Biological Chemistry. 278 (35): 32493–6. doi:10.1074/jbc.C300226200. PMID 12842888.

[pmid12147258-17] Yamamoto Y, Jones KA, Mak BC, Muehlenbachs A, Yeung RS (Aug 2002). "Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin". Archives of Biochemistry and Biophysics. 404 (2): 210–7. doi:10.1016/s0003-9861(02)00300-4. PMID 12147258.

[5]

[1]

[2]

[3]

[4]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]