MRAS

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Muscle RAS oncogene homolog

PDB rendering based on 1x1r.
Available structures
PDBOrtholog search: PDBe, RCSB
Identifiers
SymbolsMRAS; M-RAs; R-RAS3; RRAS3
External IDsOMIM608435 MGI1100856 HomoloGene7424 GeneCards: MRAS Gene
RNA expression pattern
PBB GE MRAS 206538 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez2280817532
EnsemblENSG00000158186ENSMUSG00000032470
UniProtO14807O08989
RefSeq (mRNA)NM_001085049NM_008624
RefSeq (protein)NP_001078518NP_032650
Location (UCSC)Chr 3:
138.07 – 138.12 Mb
Chr 9:
99.39 – 99.44 Mb
PubMed search[1][2]
 
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Muscle RAS oncogene homolog

PDB rendering based on 1x1r.
Available structures
PDBOrtholog search: PDBe, RCSB
Identifiers
SymbolsMRAS; M-RAs; R-RAS3; RRAS3
External IDsOMIM608435 MGI1100856 HomoloGene7424 GeneCards: MRAS Gene
RNA expression pattern
PBB GE MRAS 206538 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez2280817532
EnsemblENSG00000158186ENSMUSG00000032470
UniProtO14807O08989
RefSeq (mRNA)NM_001085049NM_008624
RefSeq (protein)NP_001078518NP_032650
Location (UCSC)Chr 3:
138.07 – 138.12 Mb
Chr 9:
99.39 – 99.44 Mb
PubMed search[1][2]

Ras-related protein M-Ras is a protein that in humans is encoded by the MRAS gene.[1][2][3]

Members of the RAS superfamily of GTP-binding proteins, which includes MRAS, are membrane-anchored, intracellular signal transducers responsible for a variety of normal cellular functions. They are oncogenically activated in a significant fraction of tumors.[supplied by OMIM][3]

Interactions[edit]

MRAS has been shown to interact with RASSF5[4] and RALGDS.[1][5]

References[edit]

  1. ^ a b Kimmelman A, Tolkacheva T, Lorenzi MV, Osada M, Chan AM (Jan 1998). "Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution". Oncogene 15 (22): 2675–85. doi:10.1038/sj.onc.1201674. PMID 9400994. 
  2. ^ Quilliam LA, Castro AF, Rogers-Graham KS, Martin CB, Der CJ, Bi C (Sep 1999). "M-Ras/R-Ras3, a transforming ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6". J Biol Chem 274 (34): 23850–7. doi:10.1074/jbc.274.34.23850. PMID 10446149. 
  3. ^ a b "Entrez Gene: MRAS muscle RAS oncogene homolog". 
  4. ^ Ortiz-Vega, Sara; Khokhlatchev Andrei, Nedwidek Maria, Zhang Xian-feng, Dammann Reinhard, Pfeifer Gerd P, Avruch Joseph (Feb. 2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene (England) 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. ISSN 0950-9232. PMID 11857081. 
  5. ^ Ehrhardt, G R; Leslie K B, Lee F, Wieler J S, Schrader J W (Oct. 1999). "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". Blood (UNITED STATES) 94 (7): 2433–44. ISSN 0006-4971. PMID 10498616. 

Further reading[edit]

  • Matsumoto K, Asano T, Endo T (1997). "Novel small GTPase M-Ras participates in reorganization of actin cytoskeleton". Oncogene 15 (20): 2409–17. doi:10.1038/sj.onc.1201416. PMID 9395237. 
  • Louahed J, Grasso L, De Smet C, et al. (1999). "Interleukin-9-induced expression of M-Ras/R-Ras3 oncogene in T-helper clones". Blood 94 (5): 1701–10. PMID 10477695. 
  • Ehrhardt GR, Leslie KB, Lee F, et al. (1999). "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". Blood 94 (7): 2433–44. PMID 10498616. 
  • Kimmelman AC, Osada M, Chan AM (2000). "R-Ras3, a brain-specific Ras-related protein, activates Akt and promotes cell survival in PC12 cells". Oncogene 19 (16): 2014–22. doi:10.1038/sj.onc.1203530. PMID 10803462. 
  • Rebhun JF, Castro AF, Quilliam LA (2001). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". J. Biol. Chem. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204. 
  • Gao X, Satoh T, Liao Y, et al. (2001). "Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras". J. Biol. Chem. 276 (45): 42219–25. doi:10.1074/jbc.M105760200. PMID 11524421. 
  • Ortiz-Vega S, Khokhlatchev A, Nedwidek M, et al. (2002). "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1". Oncogene 21 (9): 1381–90. doi:10.1038/sj.onc.1205192. PMID 11857081. 
  • Kimmelman AC, Nuñez Rodriguez N, Chan AM (2002). "R-Ras3/M-Ras induces neuronal differentiation of PC12 cells through cell-type-specific activation of the mitogen-activated protein kinase cascade". Mol. Cell. Biol. 22 (16): 5946–61. doi:10.1128/MCB.22.16.5946-5961.2002. PMC 133986. PMID 12138204. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Mitin NY, Ramocki MB, Zullo AJ, et al. (2004). "Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization". J. Biol. Chem. 279 (21): 22353–61. doi:10.1074/jbc.M312867200. PMID 15031288. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. 
  • Roberts AE, Araki T, Swanson KD, et al. (2007). "Germline gain-of-function mutations in SOS1 cause Noonan syndrome". Nat. Genet. 39 (1): 70–4. doi:10.1038/ng1926. PMID 17143285. 
  • Yoshikawa Y, Satoh T, Tamura T, et al. (2007). "The M-Ras-RA-GEF-2-Rap1 pathway mediates tumor necrosis factor-alpha dependent regulation of integrin activation in splenocytes". Mol. Biol. Cell 18 (8): 2949–59. doi:10.1091/mbc.E07-03-0250. PMC 1949361. PMID 17538012.