RAP1A

RAP1A, član RAS familije onkogena
RAP1A, član RAS familije onkogena
	PDB prikaz baziran na 1c1y.
Dostupne strukture
	1C1Y, 1GUA, 3KUC
Identifikatori
Simboli	RAP1A; KREV-1; KREV1; RAP1; SMGP21
Vanjski ID	OMIM: 179520 MGI: 97852 HomoloGene: 2162 GeneCards: RAP1A Gene
Ontologija gena
Molekularna funkcija	• vezivanje nukleotida; • aktivnost GTPaze; • proteinsko vezivanje; • GTP vezivanje; • vezivanje Ras GTPaze;
Celularna komponenta	• citozol; • ćelijska membrana; • kompleks faktora razmene guanil nukleotida;
Biološki proces	• aktivacija MAPKK aktivnosti; • metabolički proces energijske rezerve; • GTP katabolički proces; • prenos signala; • prenos signala posredovan malim GTPazama; • koagulacija krvi; • aktivacija trombocita; • metabolički proces malih molekula; • signalni put receptora faktora nervnog rasta; • regulacija sekrecije insulina;
Ortolozi
Vrsta	Čovek
Entrez	5906
Ensembl	ENSG00000116473
UniProt	P62834
RefSeq (mRNA)	NM_001010935.1
RefSeq (protein)	NP_001010935.1
Lokacija (UCSC)	Chr 1:; 112.08 - 112.26 Mb
PubMed pretraga	[1]

Ras srodni protein 1A je protein koji je kod ljudi kodiran RAP1A genom.^[1]

Interakcije[уреди | уреди извор]

RAP1A formira interakcije sa C-Raf,^[2]^[3]^[4]^[5] PDE6D,^[6]^[7] TSC2,^[8]^[9] RALGDS,^[10]^[11] RAPGEF2^[12] i MLLT4.^[10]

Reference[уреди | уреди извор]

^ Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (1989). „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”. J Biol Chem. 263 (35): 18965—71. PMID 3143720.
^ Han, L; Colicelli J (1995). „A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1”. Mol. Cell. Biol. UNITED STATES. 15 (3): 1318—23. ISSN 0270-7306. PMC 230355 . PMID 7862125.
^ Nassar, N; Horn G, Herrmann C; et al. (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. ENGLAND. 375 (6532): 554—60. ISSN 0028-0836. PMID 7791872. doi:10.1038/375554a0.
^ Hu, C D; Kariya K; et al. (1999). „Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation”. J. Biol. Chem. UNITED STATES. 274 (1): 48—51. ISSN 0021-9258. PMID 9867809. doi:10.1074/jbc.274.1.48.
^ Okada, T; Hu C D; et al. (1999). „The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases”. Mol. Cell. Biol. UNITED STATES. 19 (9): 6057—64. ISSN 0270-7306. PMC 84512 . PMID 10454553.
^ Nancy, Vanessa; Callebaut Isabelle; et al. (2002). „The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases”. J. Biol. Chem. United States. 277 (17): 15076—84. ISSN 0021-9258. PMID 11786539. doi:10.1074/jbc.M109983200.
^ Hanzal-Bayer, Michael; Renault Louis; et al. (2002). „The complex of Arl2-GTP and PDE delta: from structure to function”. EMBO J. England. 21 (9): 2095—106. ISSN 0261-4189. PMC 125981 . PMID 11980706. doi:10.1093/emboj/21.9.2095.
^ Castro, Ariel F; Rebhun John F; et al. (2003). „Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner”. J. Biol. Chem. United States. 278 (35): 32493—6. ISSN 0021-9258. PMID 12842888. doi:10.1074/jbc.C300226200.
^ Yamamoto, Yuji; Jones Kathryn A; et al. (2002). „Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin”. Arch. Biochem. Biophys. United States. 404 (2): 210—7. ISSN 0003-9861. PMID 12147258. doi:10.1016/S0003-9861(02)00300-4.
^ ^а ^б Boettner, B; Govek E E; et al. (2000). „The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 97 (16): 9064—9. ISSN 0027-8424. PMC 16822 . PMID 10922060. doi:10.1073/pnas.97.16.9064.
^ Nancy, V; Wolthuis R M; et al. (1999). „Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2”. J. Biol. Chem. UNITED STATES. 274 (13): 8737—45. ISSN 0021-9258. PMID 10085114. doi:10.1074/jbc.274.13.8737.
^ Rebhun, J F; Castro A F; Quilliam L A (2000). „Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction”. J. Biol. Chem. UNITED STATES. 275 (45): 34901—8. ISSN 0021-9258. PMID 10934204. doi:10.1074/jbc.M005327200.

[pmid3143720-1] Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (1989). „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”. J Biol Chem. 263 (35): 18965—71. PMID 3143720.

[pmid7862125-2] Han, L; Colicelli J (1995). „A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1”. Mol. Cell. Biol. UNITED STATES. 15 (3): 1318—23. ISSN 0270-7306. PMC 230355 . PMID 7862125.

[pmid7791872-3] Nassar, N; Horn G, Herrmann C; et al. (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. ENGLAND. 375 (6532): 554—60. ISSN 0028-0836. PMID 7791872. doi:10.1038/375554a0.

[pmid9867809-4] Hu, C D; Kariya K; et al. (1999). „Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation”. J. Biol. Chem. UNITED STATES. 274 (1): 48—51. ISSN 0021-9258. PMID 9867809. doi:10.1074/jbc.274.1.48.

[pmid10454553-5] Okada, T; Hu C D; et al. (1999). „The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases”. Mol. Cell. Biol. UNITED STATES. 19 (9): 6057—64. ISSN 0270-7306. PMC 84512 . PMID 10454553.

[pmid11786539-6] Nancy, Vanessa; Callebaut Isabelle; et al. (2002). „The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases”. J. Biol. Chem. United States. 277 (17): 15076—84. ISSN 0021-9258. PMID 11786539. doi:10.1074/jbc.M109983200.

[pmid11980706-7] Hanzal-Bayer, Michael; Renault Louis; et al. (2002). „The complex of Arl2-GTP and PDE delta: from structure to function”. EMBO J. England. 21 (9): 2095—106. ISSN 0261-4189. PMC 125981 . PMID 11980706. doi:10.1093/emboj/21.9.2095.

[pmid12842888-8] Castro, Ariel F; Rebhun John F; et al. (2003). „Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner”. J. Biol. Chem. United States. 278 (35): 32493—6. ISSN 0021-9258. PMID 12842888. doi:10.1074/jbc.C300226200.

[pmid12147258-9] Yamamoto, Yuji; Jones Kathryn A; et al. (2002). „Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin”. Arch. Biochem. Biophys. United States. 404 (2): 210—7. ISSN 0003-9861. PMID 12147258. doi:10.1016/S0003-9861(02)00300-4.

[pmid10922060-10] а ^б Boettner, B; Govek E E; et al. (2000). „The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 97 (16): 9064—9. ISSN 0027-8424. PMC 16822 . PMID 10922060. doi:10.1073/pnas.97.16.9064.

[pmid10085114-11] Nancy, V; Wolthuis R M; et al. (1999). „Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2”. J. Biol. Chem. UNITED STATES. 274 (13): 8737—45. ISSN 0021-9258. PMID 10085114. doi:10.1074/jbc.274.13.8737.

[pmid10934204-12] Rebhun, J F; Castro A F; Quilliam L A (2000). „Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction”. J. Biol. Chem. UNITED STATES. 275 (45): 34901—8. ISSN 0021-9258. PMID 10934204. doi:10.1074/jbc.M005327200.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]