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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ras-related protein Rap-1A''' is a [[protein]] that in humans is encoded by the ''RAP1A'' [[gene]].<ref name="pmid3143720">{{cite journal | vauthors = Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y | title = 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 | journal = The Journal of Biological Chemistry | volume = 263 | issue = 35 | pages = 18965–71 | date = Dec 1988 | pmid = 3143720 | pmc = | doi = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_RAP1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c1y.
| PDB = {{PDB2|1c1y}}, {{PDB2|1gua}}
| Name = RAP1A, member of RAS oncogene family
| HGNCid = 9855
| Symbol = RAP1A
| AltSymbols =; KREV-1; KREV1; RAP1; SMGP21
| OMIM = 179520
| ECnumber = 
| Homologene = 2162
| MGIid = 97852
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5906
    | Hs_Ensembl = ENSG00000116473
    | Hs_RefseqProtein = NP_001010935
    | Hs_RefseqmRNA = NM_001010935
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 111886363
    | Hs_GenLoc_end = 112060836
    | Hs_Uniprot = P62834
    | Mm_EntrezGene = 109905
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_145541
    | Mm_RefseqProtein = NP_663516
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =
  }}
}}
'''RAP1A, member of RAS oncogene family''', also known as '''RAP1A''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The product of this gene belongs to the family of [[Rap GTP-binding protein|Ras-related protein]]s. 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.<ref>{{cite web | title = Entrez Gene: RAP1A RAP1A, member of RAS oncogene family| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5906| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: RAP1A RAP1A, member of RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5906| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
{{refbegin | 2}}
RAP1A has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Further_reading
{{div col|colwidth=20em}}
| citations =  
* [[C-Raf]],<ref name = pmid7862125>{{cite journal | vauthors = Han L, Colicelli J | title = A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1 | journal = Molecular and Cellular Biology | volume = 15 | issue = 3 | pages = 1318–23 | date = Mar 1995 | pmid = 7862125 | pmc = 230355 | doi =  10.1128/mcb.15.3.1318}}</ref><ref name = pmid7791872>{{cite journal | vauthors = Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A | title = 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 | journal = Nature | volume = 375 | issue = 6532 | pages = 554–60 | date = Jun 1995 | pmid = 7791872 | doi = 10.1038/375554a0 }}</ref><ref name = pmid9867809>{{cite journal | vauthors = Hu CD, Kariya K, Okada T, Qi X, Song C, Kataoka T | title = Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation | journal = The Journal of Biological Chemistry | volume = 274 | issue = 1 | pages = 48–51 | date = Jan 1999 | pmid = 9867809 | doi =  10.1074/jbc.274.1.48}}</ref><ref name = pmid10454553>{{cite journal | vauthors = Okada T, Hu CD, Jin TG, Kariya K, Yamawaki-Kataoka Y, Kataoka T | title = The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases | journal = Molecular and Cellular Biology | volume = 19 | issue = 9 | pages = 6057–64 | date = Sep 1999 | pmid = 10454553 | pmc = 84512 | doi =  10.1128/mcb.19.9.6057}}</ref>
}}
* [[MLLT4]],<ref name = pmid10922060/>
{{refend}}
* [[PDE6D]],<ref name = pmid11786539>{{cite journal | vauthors = Nancy V, Callebaut I, El Marjou A, de Gunzburg J | title = The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases | journal = The Journal of Biological Chemistry | volume = 277 | issue = 17 | pages = 15076–84 | date = Apr 2002 | pmid = 11786539 | doi = 10.1074/jbc.M109983200 }}</ref><ref name = pmid11980706>{{cite journal | vauthors = Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC | title = The complex of Arl2-GTP and PDE delta: from structure to function | journal = The EMBO Journal | volume = 21 | issue = 9 | pages = 2095–106 | date = May 2002 | pmid = 11980706 | pmc = 125981 | doi = 10.1093/emboj/21.9.2095 }}</ref>
* [[RALGDS]],<ref name = pmid10922060>{{cite journal | vauthors = Boettner B, Govek EE, Cross J, Van Aelst L | title = The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 16 | pages = 9064–9 | date = Aug 2000 | pmid = 10922060 | pmc = 16822 | doi =  10.1073/pnas.97.16.9064}}</ref><ref name = pmid10085114>{{cite journal | vauthors = Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J | title = Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 13 | pages = 8737–45 | date = Mar 1999 | pmid = 10085114 | doi =  10.1074/jbc.274.13.8737}}</ref>
* [[RAPGEF2]],<ref name = pmid10934204>{{cite journal | vauthors = Rebhun JF, Castro AF, Quilliam LA | title = Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction | journal = The Journal of Biological Chemistry | volume = 275 | issue = 45 | pages = 34901–8 | date = Nov 2000 | pmid = 10934204 | doi = 10.1074/jbc.M005327200 }}</ref>  and
* [[TSC2]].<ref name = pmid12842888>{{cite journal | vauthors = Castro AF, Rebhun JF, Clark GJ, Quilliam LA | title = Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner | journal = The Journal of Biological Chemistry | volume = 278 | issue = 35 | pages = 32493–6 | date = Aug 2003 | pmid = 12842888 | doi = 10.1074/jbc.C300226200 }}</ref><ref name = pmid12147258>{{cite journal | vauthors = Yamamoto Y, Jones KA, Mak BC, Muehlenbachs A, Yeung RS | title = Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin | journal = Archives of Biochemistry and Biophysics | volume = 404 | issue = 2 | pages = 210–7 | date = Aug 2002 | pmid = 12147258 | doi =  10.1016/s0003-9861(02)00300-4}}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
{{PDB Gallery|geneid=5906}}


{{gene-1-stub}}
{{gene-1-stub}}
{{WikiDoc Sources}}

Latest revision as of 08:53, 10 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[2]

Interactions

RAP1A has been shown to interact with:

References

  1. ↑ 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. PMID 3143720.
  2. ↑ "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 7.0 7.1 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. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 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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