RAP1A

RAP1A
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1C1Y, 1GUA, 3KUC, 4KVG
Identifikatori
Aliasi	RAP1A
Vanjski ID-jevi	OMIM: 179520 MGI: 97852 HomoloGene: 2162 GeneCards: RAP1A
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	111,716,691 bp
Lokacija gena (miš)
Hrom.	Hromosom 3 (miš)
Kraj	105,708,652 bp
Ontologija gena
Molekularna funkcija	• nucleotide binding; • GO:0032403 protein-containing complex binding; • GTP binding; • GO:0001948, GO:0016582 vezivanje za proteine; • GO:0006184 GTPase activity; • GDP binding;
Ćelijska komponenta	• citosol; • endozom; • membrana; • myelin sheath; • ćelijska membrana; • guanyl-nucleotide exchange factor complex; • neuron projection; • Egzosom; • early endosome; • late endosome; • citoplazma; • međućelijske veze; • perinuklearno područje citoplazme; • specific granule membrane; • phagocytic vesicle; • glutamatergic synapse;
Biološki proces	• 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; • GO:1904579 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; • GO:0072468 Transdukcija signala; • 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; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 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;
	Izvori:Amigo / QuickGO
Ortolozi
	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
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Ras-srodni protein Rap-1A jest protein koji je kod ljudi kodiran genom RAP1A sa hromosoma 1.^[5]

Aminokiselinska sekvenca[uredi | uredi izvor]

Dužina polipeptidnog lanca je 184 aminokiseline, a molekulska težina 20.987 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MREYKLVVLG	SGGVGKSALT	VQFVQGIFVE	KYDPTIEDSY	RKQVEVDCQQ
CMLEILDTAG	TEQFTAMRDL	YMKNGQGFAL	VYSITAQSTF	NDLQDLREQI
LRVKDTEDVP	MILVGNKCDL	EDERVVGKEQ	GQNLARQWCN	CAFLESSAKS
KINVNEIFYD	LVRQINRKTP	VEKKKPKKKS	CLLL

Funkcija[uredi | uredi izvor]

Proizvod ovog gena pripada porodici Ras-srodnih proteina. Ovi proteini dijele približno 50% aminokiselinskog identiteta s klasičnim RAS proteinima i imaju brojne zajedničke strukturne karakteristike. Najupečatljivija razlika između RAP proteina i RAS proteina je u njihovoj 61. aminokiselini: glutamin u RAS je zamijenjen treoninom u RAP proteinima. Proizvod ovog gena suprotstavlja se mitogenoj funkciji RAS-a jer može komunicirati sa RAS GAP-ovima i RAF-om na kompetitivni način. Za ovaj gen su identificirane dvije varijante transkripta koje kodiraju isti protein.^[7]

Interakcije[uredi | uredi izvor]

Pokazalo se da je RAP1A u interakciji sa:

Reference[uredi | uredi izvor]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116473 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000068798 - Ensembl, maj 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.
^ "UniProt, P62834" (jezik: eng.). Pristupljeno 4. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ "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. 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 (maj 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.

Vanjski linkovi[uredi | uredi izvor]

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

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

[UniProt-6] "UniProt, P62834" (jezik: eng.). Pristupljeno 4. 12. 2021.CS1 održavanje: nepoznati jezik (link)

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

[pmid7862125-8] 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.

[pmid7791872-9] 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. doi:10.1038/375554a0. PMID 7791872. S2CID 4347807.

[pmid9867809-10] 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.

[pmid10454553-11] 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.

[pmid10922060-12] 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.

[pmid11786539-13] 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.

[pmid11980706-14] Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (maj 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.

[pmid10085114-15] 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.

[pmid10934204-16] 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.

[pmid12842888-17] 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.

[pmid12147258-18] 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.

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