MRAS
From Wikipedia, the free encyclopedia
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Muscle RAS oncogene homolog
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| PDB rendering based on 1x1r. | ||||||||||||||
| Available structures: 1x1r, 1x1s | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | MRAS; FLJ42964; M-RAs; R-RAS3; RRAS3 | |||||||||||||
| External IDs | OMIM: 608435 MGI: 1100856 HomoloGene: 7424 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 22808 | 17532 | ||||||||||||
| Ensembl | ENSG00000158186 | ENSMUSG00000032470 | ||||||||||||
| Uniprot | O14807 | Q3TPX5 | ||||||||||||
| Refseq | NM_012219 (mRNA) NP_036351 (protein) |
NM_008624 (mRNA) NP_032650 (protein) |
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| Location | Chr 3: 139.55 - 139.6 Mb | Chr 9: 99.2 - 99.24 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Muscle RAS oncogene homolog, also known as MRAS, is a human gene.[1]
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][1]
[edit] References
[edit] Further reading
- Matsumoto K, Asano T, Endo T (1997). "Novel small GTPase M-Ras participates in reorganization of actin cytoskeleton.". Oncogene 15 (20): 2409–17. doi:. PMID 9395237.
- Kimmelman A, Tolkacheva T, Lorenzi MV, et al. (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:. PMID 9400994.
- Quilliam LA, Castro AF, Rogers-Graham KS, et al. (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. PMID 10446149.
- 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:. 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:. 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:. 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:. 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. 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:. 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:. 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:. 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:. 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:. 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:. PMID 17538012.

