RRAS2

RRAS2

Identifiers

RRAS2, TC21, related RAS viral (r-ras) oncogene homolog 2, RAS related 2, NS12

External IDs

OMIM: 600098; MGI: 1914172; GeneCards: RRAS2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2ERY

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
3.6.5.2	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 11 (human)

Band	11p15.2	Start	14,277,922 bp
Band	11p15.2	End	14,364,506 bp

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)

Band	7\|7 F1	Start	113,646,017 bp
Band	7\|7 F1	End	113,717,016 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

secondary oocyte

Skeletal muscle tissue of rectus abdominis

epithelium of colon

kidney tubule

biceps brachii

Skeletal muscle tissue of biceps brachii

thoracic diaphragm

glutes

mucosa of paranasal sinus

germinal epithelium

Top expressed in

interventricular septum

endothelial cell of lymphatic vessel

decidua

endocardial cushion

medullary collecting duct

gastrula

renal corpuscle

left lung lobe

atrioventricular valve

stroma of bone marrow

More reference expression data


More reference expression data

Gene ontology
Molecular function	nucleotide binding GTP binding protein binding GTPase activity GDP binding
Cellular component	plasma membrane extracellular exosome intracellular anatomical structure endoplasmic reticulum membrane focal adhesion
Biological process	cellular process or phenomenon Ras protein signal transduction osteoblast differentiation regulation of neuron death signal transduction positive regulation of cell migration
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


22800


66922


ENSG00000133818


ENSMUSG00000055723


P62070


P62071

RefSeq (mRNA)


NM_012250 NM_001102669 NM_001177314 NM_001177315


NM_025846

RefSeq (protein)


NP_001096139 NP_001170785 NP_001170786 NP_036382


NP_080122

Location (UCSC)

Chr 11: 14.28 – 14.36 Mb

Chr 7: 113.65 – 113.72 Mb

PubMed search

View/Edit Human

View/Edit Mouse

Ras-related protein R-Ras2 is a protein that in humans is encoded by the RRAS2 gene.

Interactions

RRAS2 has been shown to interact with C-Raf.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000133818 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055723 – Ensembl, May 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.
↑ 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. doi:10.1128/mcb.10.4.1793. PMC 362288. PMID 2108320.
↑ 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. Bibcode:1994PNAS...91.7558C. doi:10.1073/pnas.91.16.7558. PMC 44441. PMID 8052619.
↑ "Entrez Gene: RRAS2 related RAS viral (r-ras) oncogene homolog 2".
↑ 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. 14 (8). UNITED STATES: 895–900. doi:10.1101/gad.14.8.895. ISSN 0890-9369. PMC 316541. PMID 10783161.
↑ 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. 18 (43). ENGLAND: 5860–9. doi:10.1038/sj.onc.1202968. ISSN 0950-9232. PMID 10557073. S2CID 31576945.

Further reading

Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW (2002). "Ras and relatives--job sharing and networking keep an old family together". Exp. Hematol. 30 (10): 1089–106. doi:10.1016/S0301-472X(02)00904-9. PMID 12384139.
Rosário M, Paterson HF, Marshall CJ (1999). "Activation of the Raf/MAP kinase cascade by the Ras-related protein TC21 is required for the TC21-mediated transformation of NIH 3T3 cells". EMBO J. 18 (5): 1270–9. doi:10.1093/emboj/18.5.1270. PMC 1171217. PMID 10064593.
Linnemann T, Geyer M, Jaitner BK, et al. (1999). "Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily". J. Biol. Chem. 274 (19): 13556–62. doi:10.1074/jbc.274.19.13556. PMID 10224125.
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. doi:10.1182/blood.V94.7.2433.419k31_2433_2444. PMID 10498616. S2CID 40024826.
Movilla N, Crespo P, Bustelo XR (1999). "Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins". Oncogene. 18 (43): 5860–9. doi:10.1038/sj.onc.1202968. PMID 10557073. S2CID 31576945.
Ohba Y, Mochizuki N, Yamashita S, et al. (2000). "Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3". J. Biol. Chem. 275 (26): 20020–6. doi:10.1074/jbc.M000981200. PMID 10777492.
Figueroa C, Taylor J, Vojtek AB (2001). "Prenylated Rab acceptor protein is a receptor for prenylated small GTPases". J. Biol. Chem. 276 (30): 28219–25. doi:10.1074/jbc.M101763200. PMID 11335720.
Murphy GA, Graham SM, Morita S, et al. (2002). "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation". J. Biol. Chem. 277 (12): 9966–75. doi:10.1074/jbc.M109059200. PMID 11788587.
Rong R, He Q, Liu Y, et al. (2002). "TC21 mediates transformation and cell survival via activation of phosphatidylinositol 3-kinase/Akt and NF-kappaB signaling pathway". Oncogene. 21 (7): 1062–70. doi:10.1038/sj.onc.1205154. PMID 11850823. S2CID 21196767.
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. S2CID 240243.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Yuryev A, Wennogle LP (2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis". Genomics. 81 (2): 112–25. doi:10.1016/S0888-7543(02)00008-3. PMID 12620389.
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.
Kho Y, Kim SC, Jiang C, et al. (2004). "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (34): 12479–84. Bibcode:2004PNAS..10112479K. doi:10.1073/pnas.0403413101. PMC 515085. PMID 15308774.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
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.
Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.

v t e PDB gallery
2ery: The crystal structure of the Ras related protein RRas2 (RRAS2) in the GDP bound state

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