RRAS2: Difference between revisions

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{{Infobox_gene}}
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'''Ras-related protein R-Ras2''' is a [[protein]] that in humans is encoded by the ''RRAS2'' [[gene]].<ref name="pmid2108320">{{cite journal |vauthors=Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P | title = Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line | journal = Mol Cell Biol | volume = 10 | issue = 4 | pages = 1793–8 |date=May 1990 | pmid = 2108320 | pmc = 362288 | doi =  }}</ref><ref name="pmid8052619">{{cite journal |vauthors=Chan AM, Miki T, Meyers KA, Aaronson SA | title = A human oncogene of the RAS superfamily unmasked by expression cDNA cloning | journal = Proc Natl Acad Sci U S A | volume = 91 | issue = 16 | pages = 7558–62 |date=September 1994 | pmid = 8052619 | pmc = 44441 | doi =10.1073/pnas.91.16.7558 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RRAS2 related RAS viral (r-ras) oncogene homolog 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22800| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_RRAS2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ery.
| PDB = {{PDB2|2ery}}
| Name = Related RAS viral (r-ras) oncogene homolog 2
| HGNCid = 17271
| Symbol = RRAS2
| AltSymbols =; TC21
| OMIM = 600098
| ECnumber =
| Homologene = 6945
| MGIid = 1914172
| GeneAtlas_image1 = PBB_GE_RRAS2_212589_at_tn.png
| GeneAtlas_image2 = PBB_GE_RRAS2_208456_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RRAS2_212590_at_tn.png
  | 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:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
  | Process = {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 22800
    | Hs_Ensembl = ENSG00000133818
    | Hs_RefseqProtein = NP_036382
    | Hs_RefseqmRNA = NM_012250
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 14256889
    | Hs_GenLoc_end = 14337289
    | Hs_Uniprot = P62070
    | Mm_EntrezGene = 66922
    | Mm_Ensembl = ENSMUSG00000055723
    | Mm_RefseqmRNA = NM_025846
    | Mm_RefseqProtein = NP_080122
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 113837969
    | Mm_GenLoc_end = 113908962
    | Mm_Uniprot = Q9CTF6
  }}
}}
'''Related RAS viral (r-ras) oncogene homolog 2''', also known as '''RRAS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RRAS2 related RAS viral (r-ras) oncogene homolog 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22800| accessdate = }}</ref>


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==Interactions==
RRAS2 has been shown to [[Protein-protein interaction|interact]] with [[C-Raf]].<ref name=pmid10783161>{{cite journal |last=Li |first=W |authorlink= |author2=Han M |author3=Guan K L  |date=April 2000  |title=The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf |journal=Genes Dev. |volume=14 |issue=8 |pages=895–900 |publisher= |location = UNITED STATES| issn = 0890-9369| pmid = 10783161 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=316541 }}</ref><ref name=pmid10557073>{{cite journal |last=Movilla |first=N |authorlink= |author2=Crespo P |author3=Bustelo X R  |date=October 1999  |title=Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins |journal=Oncogene |volume=18 |issue=43 |pages=5860–9 |publisher= |location = ENGLAND| issn = 0950-9232| pmid = 10557073 |doi = 10.1038/sj.onc.1202968 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW |title=Ras and relatives--job sharing and networking keep an old family together. |journal=Exp. Hematol. |volume=30 |issue= 10 |pages= 1089-106 |year= 2002 |pmid= 12384139 |doi= }}
*{{cite journal  |vauthors=Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW |title=Ras and relatives--job sharing and networking keep an old family together. |journal=Exp. Hematol. |volume=30 |issue= 10 |pages= 1089–106 |year= 2002 |pmid= 12384139 |doi=10.1016/S0301-472X(02)00904-9 }}
*{{cite journal  | author=Drivas GT, Shih A, Coutavas E, ''et al.'' |title=Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. |journal=Mol. Cell. Biol. |volume=10 |issue= 4 |pages= 1793-8 |year= 1990 |pmid= 2108320 |doi=  }}
*{{cite journal  |vauthors=Rosário M, Paterson HF, Marshall CJ |title=Activation of the Raf/MAP kinase cascade by the Ras-related protein TC21 is required for the TC21-mediated transformation of NIH 3T3 cells. |journal=EMBO J. |volume=18 |issue= 5 |pages= 1270–9 |year= 1999 |pmid= 10064593 |doi= 10.1093/emboj/18.5.1270 | pmc=1171217 }}
*{{cite journal  | author=Chan AM, Miki T, Meyers KA, Aaronson SA |title=A human oncogene of the RAS superfamily unmasked by expression cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 16 |pages= 7558-62 |year= 1994 |pmid= 8052619 |doi= }}
*{{cite journal   |vauthors=Linnemann T, Geyer M, Jaitner BK, etal |title=Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13556–62 |year= 1999 |pmid= 10224125 |doi=10.1074/jbc.274.19.13556 }}
*{{cite journal  | author=Rosário M, Paterson HF, Marshall CJ |title=Activation of the Raf/MAP kinase cascade by the Ras-related protein TC21 is required for the TC21-mediated transformation of NIH 3T3 cells. |journal=EMBO J. |volume=18 |issue= 5 |pages= 1270-9 |year= 1999 |pmid= 10064593 |doi= 10.1093/emboj/18.5.1270 }}
*{{cite journal   |vauthors=Ehrhardt GR, Leslie KB, Lee F, etal |title=M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line. |journal=Blood |volume=94 |issue= 7 |pages= 2433–44 |year= 1999 |pmid= 10498616 |doi=  }}
*{{cite journal | author=Linnemann T, Geyer M, Jaitner BK, ''et al.'' |title=Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13556-62 |year= 1999 |pmid= 10224125 |doi=  }}
*{{cite journal  |vauthors=Movilla N, Crespo P, Bustelo XR |title=Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins. |journal=Oncogene |volume=18 |issue= 43 |pages= 5860–9 |year= 1999 |pmid= 10557073 |doi= 10.1038/sj.onc.1202968 }}
*{{cite journal | author=Ehrhardt GR, Leslie KB, Lee F, ''et al.'' |title=M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line. |journal=Blood |volume=94 |issue= 7 |pages= 2433-44 |year= 1999 |pmid= 10498616 |doi=  }}
*{{cite journal   |vauthors=Ohba Y, Mochizuki N, Yamashita S, etal |title=Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 20020–6 |year= 2000 |pmid= 10777492 |doi= 10.1074/jbc.M000981200 }}
*{{cite journal  | author=Movilla N, Crespo P, Bustelo XR |title=Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins. |journal=Oncogene |volume=18 |issue= 43 |pages= 5860-9 |year= 1999 |pmid= 10557073 |doi= 10.1038/sj.onc.1202968 }}
*{{cite journal  |vauthors=Figueroa C, Taylor J, Vojtek AB |title=Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28219–25 |year= 2001 |pmid= 11335720 |doi= 10.1074/jbc.M101763200 }}
*{{cite journal | author=Ohba Y, Mochizuki N, Yamashita S, ''et al.'' |title=Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 20020-6 |year= 2000 |pmid= 10777492 |doi= 10.1074/jbc.M000981200 }}
*{{cite journal   |vauthors=Murphy GA, Graham SM, Morita S, etal |title=Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9966–75 |year= 2002 |pmid= 11788587 |doi= 10.1074/jbc.M109059200 }}
*{{cite journal  | author=Figueroa C, Taylor J, Vojtek AB |title=Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28219-25 |year= 2001 |pmid= 11335720 |doi= 10.1074/jbc.M101763200 }}
*{{cite journal   |vauthors=Rong R, He Q, Liu Y, etal |title=TC21 mediates transformation and cell survival via activation of phosphatidylinositol 3-kinase/Akt and NF-kappaB signaling pathway. |journal=Oncogene |volume=21 |issue= 7 |pages= 1062–70 |year= 2002 |pmid= 11850823 |doi= 10.1038/sj.onc.1205154 }}
*{{cite journal | author=Murphy GA, Graham SM, Morita S, ''et al.'' |title=Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9966-75 |year= 2002 |pmid= 11788587 |doi= 10.1074/jbc.M109059200 }}
*{{cite journal   |vauthors=Ortiz-Vega S, Khokhlatchev A, Nedwidek M, etal |title=The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1. |journal=Oncogene |volume=21 |issue= 9 |pages= 1381–90 |year= 2002 |pmid= 11857081 |doi= 10.1038/sj.onc.1205192 }}
*{{cite journal | author=Rong R, He Q, Liu Y, ''et al.'' |title=TC21 mediates transformation and cell survival via activation of phosphatidylinositol 3-kinase/Akt and NF-kappaB signaling pathway. |journal=Oncogene |volume=21 |issue= 7 |pages= 1062-70 |year= 2002 |pmid= 11850823 |doi= 10.1038/sj.onc.1205154 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Ortiz-Vega S, Khokhlatchev A, Nedwidek M, ''et al.'' |title=The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1. |journal=Oncogene |volume=21 |issue= 9 |pages= 1381-90 |year= 2002 |pmid= 11857081 |doi= 10.1038/sj.onc.1205192 }}
*{{cite journal  |vauthors=Yuryev A, Wennogle LP |title=Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis. |journal=Genomics |volume=81 |issue= 2 |pages= 112–25 |year= 2003 |pmid= 12620389 |doi=10.1016/S0888-7543(02)00008-3 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Mitin NY, Ramocki MB, Zullo AJ, etal |title=Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization. |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 22353–61 |year= 2004 |pmid= 15031288 |doi= 10.1074/jbc.M312867200 }}
*{{cite journal  | author=Yuryev A, Wennogle LP |title=Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis. |journal=Genomics |volume=81 |issue= 2 |pages= 112-25 |year= 2003 |pmid= 12620389 |doi=  }}
*{{cite journal   |vauthors=Kho Y, Kim SC, Jiang C, etal |title=A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 34 |pages= 12479–84 |year= 2004 |pmid= 15308774 |doi= 10.1073/pnas.0403413101 | pmc=515085 }}
*{{cite journal | author=Mitin NY, Ramocki MB, Zullo AJ, ''et al.'' |title=Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization. |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 22353-61 |year= 2004 |pmid= 15031288 |doi= 10.1074/jbc.M312867200 }}
*{{cite journal   |vauthors=Suzuki Y, Yamashita R, Shirota M, etal |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 | pmc=515316 }}
*{{cite journal | author=Kho Y, Kim SC, Jiang C, ''et al.'' |title=A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 34 |pages= 12479-84 |year= 2004 |pmid= 15308774 |doi= 10.1073/pnas.0403413101 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Suzuki Y, Yamashita R, Shirota M, ''et al.'' |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711-8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 }}
*{{cite journal   |vauthors=Barrios-Rodiles M, Brown KR, Ozdamar B, etal |title=High-throughput mapping of a dynamic signaling network in mammalian cells. |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Barrios-Rodiles M, Brown KR, Ozdamar B, ''et al.'' |title=High-throughput mapping of a dynamic signaling network in mammalian cells. |journal=Science |volume=307 |issue= 5715 |pages= 1621-5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=22800}}
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Revision as of 09:29, 10 September 2017

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

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Ras-related protein R-Ras2 is a protein that in humans is encoded by the RRAS2 gene.[1][2][3]


Interactions

RRAS2 has been shown to interact with C-Raf.[4][5]

References

  1. ↑ Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P (May 1990). "Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line". Mol Cell Biol. 10 (4): 1793–8. PMC 362288. PMID 2108320.
  2. ↑ Chan AM, Miki T, Meyers KA, Aaronson SA (September 1994). "A human oncogene of the RAS superfamily unmasked by expression cDNA cloning". Proc Natl Acad Sci U S A. 91 (16): 7558–62. doi:10.1073/pnas.91.16.7558. PMC 44441. PMID 8052619.
  3. ↑ "Entrez Gene: RRAS2 related RAS viral (r-ras) oncogene homolog 2".
  4. ↑ Li, W; Han M; Guan K L (April 2000). "The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf". Genes Dev. UNITED STATES. 14 (8): 895–900. ISSN 0890-9369. PMC 316541. PMID 10783161.
  5. ↑ Movilla, N; Crespo P; Bustelo X R (October 1999). "Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins". Oncogene. ENGLAND. 18 (43): 5860–9. doi:10.1038/sj.onc.1202968. ISSN 0950-9232. PMID 10557073.

Further reading



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