RRAS

RRAS
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2FN4
Identifiers
Aliases	RRAS, related RAS viral (r-ras) oncogene homolog, R-Ras, RAS related
External IDs	OMIM: 165090 MGI: 98179 HomoloGene: 4565 GeneCards: RRAS
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	49,640,143 bp[1]
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)[2]
End	45,021,647 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • GDP binding; • GO:0032403 macromolecular complex binding; • GTP binding; • GO:0001948 protein binding; • GTPase activity;
Cellular component	• membrane; • focal adhesion; • cell membrane; • extracellular exosome; • intracellular;
Biological process	• positive regulation of angiogenesis; • negative regulation of cell migration; • regulation of protein kinase B signaling; • regulation of ERK1 and ERK2 cascade; • leukocyte differentiation; • Ras protein signal transduction; • face morphogenesis; • signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	6237
	20130
	ENSG00000126458
	ENSMUSG00000038387
	P10301
	P10833
	NM_006270
	NM_009101; NM_001360132; NM_001360133
	NP_006261
	NP_033127; NP_001347061; NP_001347062
	Wikidata
View/Edit Human	View/Edit Mouse

Ras-related protein R-Ras is a protein that in humans is encoded by the RRAS gene.[5][6]

Interactions

RRAS has been shown to interact with:

References

GRCh38: Ensembl release 89: ENSG00000126458 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000038387 - 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.
Lowe DG, Capon DJ, Delwart E, Sakaguchi AY, Naylor SL, Goeddel DV (February 1987). "Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes". Cell. 48 (1): 137–46. doi:10.1016/0092-8674(87)90364-3. PMID 3098437.
"Entrez Gene: RRAS related RAS viral (r-ras) oncogene homolog".
Yuryev A, Wennogle LP (February 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.
Yuryev A, Ono M, Goff SA, Macaluso F, Wennogle LP (July 2000). "Isoform-specific localization of A-RAF in mitochondria". Mol. Cell. Biol. 20 (13): 4870–8. doi:10.1128/mcb.20.13.4870-4878.2000. PMC 85938. PMID 10848612.
Fernandez-Sarabia MJ, Bischoff JR (November 1993). "Bcl-2 associates with the ras-related protein R-ras p23". Nature. 366 (6452): 274–5. doi:10.1038/366274a0. PMID 8232588.
Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (February 2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID 10671570.
Spaargaren M, Bischoff JR (December 1994). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (February 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.

Carboni JM, Yan N, Cox AD, Bustelo X, Graham SM, Lynch MJ, Weinmann R, Seizinger BR, Der CJ, Barbacid M (1995). "Farnesyltransferase inhibitors are inhibitors of Ras but not R-Ras2/TC21, transformation". Oncogene. 10 (10): 1905–13. PMID 7761092.
Spaargaren M, Bischoff JR (1994). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
Fernandez-Sarabia MJ, Bischoff JR (1993). "Bcl-2 associates with the ras-related protein R-ras p23". Nature. 366 (6452): 274–5. doi:10.1038/366274a0. PMID 8232588.
Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C (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.
Choy E, Chiu VK, Silletti J, Feoktistov M, Morimoto T, Michaelson D, Ivanov IE, Philips MR (1999). "Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi". Cell. 98 (1): 69–80. doi:10.1016/S0092-8674(00)80607-8. PMID 10412982.
Zou JX, Wang B, Kalo MS, Zisch AH, Pasquale EB, Ruoslahti E (1999). "An Eph receptor regulates integrin activity through R-Ras". Proc. Natl. Acad. Sci. U.S.A. 96 (24): 13813–8. doi:10.1073/pnas.96.24.13813. PMC 24147. PMID 10570155.
Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID 10671570.
Suzuki J, Kaziro Y, Koide H (2000). "Positive regulation of skeletal myogenesis by R-Ras". Oncogene. 19 (9): 1138–46. doi:10.1038/sj.onc.1203402. PMID 10713701.
Ohba Y, Mochizuki N, Yamashita S, Chan AM, Schrader JW, Hattori S, Nagashima K, Matsuda M (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.
Yuryev A, Ono M, Goff SA, Macaluso F, Wennogle LP (2000). "Isoform-specific localization of A-RAF in mitochondria". Mol. Cell. Biol. 20 (13): 4870–8. doi:10.1128/MCB.20.13.4870-4878.2000. PMC 85938. PMID 10848612.
Oertli B, Han J, Marte BM, Sethi T, Downward J, Ginsberg M, Hughes PE (2000). "The effector loop and prenylation site of R-Ras are involved in the regulation of integrin function". Oncogene. 19 (43): 4961–9. doi:10.1038/sj.onc.1203876. PMID 11042683.
Tian X, Feig LA (2001). "Basis for signaling specificity difference between Sos and Ras-GRF guanine nucleotide exchange factors". J. Biol. Chem. 276 (50): 47248–56. doi:10.1074/jbc.M107407200. PMID 11560935.
Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (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.
Yu Y, Feig LA (2002). "Involvement of R-Ras and Ral GTPases in estrogen-independent proliferation of breast cancer cells". Oncogene. 21 (49): 7557–68. doi:10.1038/sj.onc.1205961. PMID 12386818.
Kwong L, Wozniak MA, Collins AS, Wilson SD, Keely PJ (2003). "R-Ras promotes focal adhesion formation through focal adhesion kinase and p130(Cas) by a novel mechanism that differs from integrins". Mol. Cell. Biol. 23 (3): 933–49. doi:10.1128/MCB.23.3.933-949.2003. PMC 140691. PMID 12529399.
Rincón-Arano H, Rosales R, Mora N, Rodriguez-Castañeda A, Rosales C (2003). "R-Ras promotes tumor growth of cervical epithelial cells". Cancer. 97 (3): 575–85. doi:10.1002/cncr.11093. PMID 12548599.
Furuhjelm J, Peränen J (2003). "The C-terminal end of R-Ras contains a focal adhesion targeting signal". J. Cell Sci. 116 (Pt 18): 3729–38. doi:10.1242/jcs.00689. PMID 12890755.
Mitin NY, Ramocki MB, Zullo AJ, Der CJ, Konieczny SF, Taparowsky EJ (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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000126458 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000038387 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid3098437-5] Lowe DG, Capon DJ, Delwart E, Sakaguchi AY, Naylor SL, Goeddel DV (February 1987). "Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes". Cell. 48 (1): 137–46. doi:10.1016/0092-8674(87)90364-3. PMID 3098437.

[entrez-6] "Entrez Gene: RRAS related RAS viral (r-ras) oncogene homolog".

[pmid12620389-7] Yuryev A, Wennogle LP (February 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.

[pmid10848612-8] Yuryev A, Ono M, Goff SA, Macaluso F, Wennogle LP (July 2000). "Isoform-specific localization of A-RAF in mitochondria". Mol. Cell. Biol. 20 (13): 4870–8. doi:10.1128/mcb.20.13.4870-4878.2000. PMC 85938. PMID 10848612.

[pmid8232588-9] Fernandez-Sarabia MJ, Bischoff JR (November 1993). "Bcl-2 associates with the ras-related protein R-ras p23". Nature. 366 (6452): 274–5. doi:10.1038/366274a0. PMID 8232588.

[pmid10671570-10] Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (February 2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID 10671570.

[pmid7809086-11] Spaargaren M, Bischoff JR (December 1994). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.

[pmid11857081-12] Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J (February 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.

RRAS

Interactions

References

Further reading