RRAD
GTP-binding protein RAD is a protein that in humans is encoded by the RRAD gene.[1][2]
Interactions
RRAD has been shown to interact with CAMK2G[3] and TPM2.[4]
References
- ^ Doria A, Caldwell JS, Ji L, Reynet C, Rich SS, Weremowicz S, Morton CC, Warram JH, Kahn CR, Krolewski AS (Mar 1995). "Trinucleotide repeats at the rad locus. Allele distributions in NIDDM and mapping to a 3-cM region on chromosome 16q". Diabetes 44 (2): 243–7. doi:10.2337/diabetes.44.2.243. PMID 7859947.
- ^ "Entrez Gene: RRAD Ras-related associated with diabetes". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6236.
- ^ Moyers, J S; Bilan P J, Zhu J, Kahn C R (May. 1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II". J. Biol. Chem. (UNITED STATES) 272 (18): 11832–9. doi:10.1074/jbc.272.18.11832. ISSN 0021-9258. PMID 9115241.
- ^ Zhu, J; Bilan P J, Moyers J S, Antonetti D A, Kahn C R (Jan. 1996). "Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin". J. Biol. Chem. (UNITED STATES) 271 (2): 768–73. doi:10.1074/jbc.271.2.768. ISSN 0021-9258. PMID 8557685.
Further reading
- Zhu J, Reynet C, Caldwell JS, Kahn CR (1995). "Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity.". J. Biol. Chem. 270 (9): 4805–12. doi:10.1074/jbc.270.9.4805. PMID 7876254.
- Reynet C, Kahn CR (1993). "Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans.". Science 262 (5138): 1441–4. doi:10.1126/science.8248782. PMID 8248782.
- Zhu J, Bilan PJ, Moyers JS, et al. (1996). "Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin.". J. Biol. Chem. 271 (2): 768–73. doi:10.1074/jbc.271.2.768. PMID 8557685.
- Caldwell JS, Moyers JS, Doria A, et al. (1996). "Molecular cloning of the human rad gene: gene structure and complete nucleotide sequence.". Biochim. Biophys. Acta 1316 (3): 145–8. PMID 8781531.
- Moyers JS, Bilan PJ, Reynet C, Kahn CR (1996). "Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells.". J. Biol. Chem. 271 (38): 23111–6. doi:10.1074/jbc.271.38.23111. PMID 8798502.
- Moyers JS, Bilan PJ, Zhu J, Kahn CR (1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II.". J. Biol. Chem. 272 (18): 11832–9. doi:10.1074/jbc.272.18.11832. PMID 9115241.
- Moyers JS, Zhu J, Kahn CR (1998). "Effects of phosphorylation on function of the Rad GTPase.". Biochem. J. 333 ( Pt 3): 609–14. PMC 1219623. PMID 9677319. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219623.
- Finlin BS, Andres DA (1999). "Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins.". Arch. Biochem. Biophys. 368 (2): 401–12. doi:10.1006/abbi.1999.1316. PMID 10441394.
- Zhu J, Tseng YH, Kantor JD, et al. (2000). "Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation.". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14911–8. doi:10.1073/pnas.96.26.14911. PMC 24747. PMID 10611312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24747.
- Tseng YH, Vicent D, Zhu J, et al. (2001). "Regulation of growth and tumorigenicity of breast cancer cells by the low molecular weight GTPase Rad and nm23.". Cancer Res. 61 (5): 2071–9. PMID 11280768.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Yanuar A, Sakurai S, Kitano K, Hakoshima T (2006). "Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase.". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 11): 978–80. doi:10.1107/S1744309105031982. PMC 1978125. PMID 16511212. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1978125.
- Yanuar A, Sakurai S, Kitano K, Hakoshima T (2006). "Crystal structure of human Rad GTPase of the RGK-family.". Genes Cells 11 (8): 961–8. doi:10.1111/j.1365-2443.2006.00994.x. PMID 16866878.
- Suzuki M, Shigematsu H, Shames DS, et al. (2007). "Methylation and gene silencing of the Ras-related GTPase gene in lung and breast cancers.". Ann. Surg. Oncol. 14 (4): 1397–404. doi:10.1245/s10434-006-9089-6. PMID 17195088.
- Yada H, Murata M, Shimoda K, et al. (2007). "Dominant negative suppression of Rad leads to QT prolongation and causes ventricular arrhythmias via modulation of L-type Ca2+ channels in the heart.". Circ. Res. 101 (1): 69–77. doi:10.1161/CIRCRESAHA.106.146399. PMID 17525370.
- Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.". Genome Biology 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2374985.
PDB gallery
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2dpx: Crystal Structure of human Rad GTPase
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2gjs: The crystal structure of human RRAD in complex with GDP
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