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RRAS - Wikipedia

From Wikipedia, the free encyclopedia

RRAS

Available structures

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; OMA:RRAS - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19q13.33	Start	49,635,292 bp^[1]
End	49,640,143 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7 B3\|7 29.08 cM	Start	44,667,385 bp^[2]
End	44,671,071 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right coronary artery

popliteal artery

tibial arteries

thoracic aorta

ascending aorta

Descending thoracic aorta

left coronary artery

gastric mucosa

left uterine tube

muscle layer of sigmoid colon

Top expressed in

tunica media of zone of aorta

carotid body

external carotid artery

ascending aorta

right lung

white adipose tissue

right lung lobe

left lung

aortic valve

tunica adventitia of aorta

More reference expression data

BioGPS

More reference expression data

Gene ontology
Molecular function	nucleotide binding GDP binding protein-containing complex binding GTP binding protein binding GTPase activity
Cellular component	membrane focal adhesion plasma membrane extracellular exosome intracellular anatomical structure
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

Species

Human

Mouse

Entrez


6237


20130

Ensembl


ENSG00000126458


ENSMUSG00000038387

UniProt


P10301


P10833

RefSeq (mRNA)


NM_006270


NM_009101 NM_001360132 NM_001360133

RefSeq (protein)


NP_006261


NP_033127 NP_001347061 NP_001347062

Location (UCSC)

Chr 19: 49.64 – 49.64 Mb

Chr 7: 44.67 – 44.67 Mb

PubMed search

^[3]

^[4]

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]

RRAS has been shown to interact with:

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000126458 – Ensembl, May 2017
^ ^a ^b ^c 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. S2CID 22622027.
^ "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. Bibcode:1993Natur.366..274F. doi:10.1038/366274a0. PMID 8232588. S2CID 4312803.
^ 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. Bibcode:1994PNAS...9112609S. 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. Bibcode:1994PNAS...9112609S. 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. Bibcode:1993Natur.366..274F. doi:10.1038/366274a0. PMID 8232588. S2CID 4312803.
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. S2CID 1018802.
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. Bibcode:1999PNAS...9613813Z. 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. S2CID 22504390.
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.