RRAD (gene)

Ras Related Glycolysis Inhibitor and Calcium Channel Regulator (RRAD) is a protein that in humans is encoded by the RRAD gene.^[5][6] RRAD is a Ras-related small GTPase that is regulated by p53 and plays a role in the regulation of aerobic glycolysis.^[7]

RRAD
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DPX, 2GJS, 3Q72, 3Q7P, 3Q7Q
Identifiers
Aliases	RRAD, RAD, RAD1, REM3, Ras related glycolysis inhibitor and calcium channel regulator
External IDs	OMIM: 179503; MGI: 1930943; HomoloGene: 3071; GeneCards: RRAD; OMA:RRAD - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q22.1 Start 66,921,679 bp[1] End 66,925,536 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 D3 Start 105,354,702 bp[2] End 105,357,959 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in olfactory zone of nasal mucosa Skeletal muscle tissue of rectus abdominis right ventricle apex of heart gastrocnemius muscle bronchial epithelial cell right auricle triceps brachii muscle muscle of thigh left ventricle Top expressed in right ventricle endocardial cushion interventricular septum cardiac muscle tissue of left ventricle atrioventricular valve ascending aorta atrium tunica media of zone of aorta aortic valve blastocyst More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GTP binding protein binding calmodulin binding GTPase activity calcium channel regulator activity Cellular component plasma membrane membrane intracellular anatomical structure Biological process signal transduction small GTPase mediated signal transduction regulation of high voltage-gated calcium channel activity negative regulation of high voltage-gated calcium channel activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6236 56437 Ensembl ENSG00000166592 ENSMUSG00000031880 UniProt P55042 O88667 RefSeq (mRNA) NM_004165 NM_001128850 NM_019662 RefSeq (protein) NP_001122322 NP_004156 n/a Location (UCSC) Chr 16: 66.92 – 66.93 Mb Chr 8: 105.35 – 105.36 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RRAD has been shown to interact with CAMK2G^[8] and TPM2.^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000166592 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031880 – 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.
5. Doria A, Caldwell JS, Ji L, Reynet C, Rich SS, Weremowicz S, Morton CC, Warram JH, Kahn CR, Krolewski AS (March 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.
6. "Entrez Gene: RRAD Ras-related associated with diabetes".
7. Zhang, Cen (2014). "Tumor suppressor p53 negatively regulates glycolysis stimulated by hypoxia through its target RRAD". Oncotarget. 4 (14): 5535–5546. doi:10.18632/oncotarget.2137. PMC 4170611. PMID 25114038.
8. Moyers JS, Bilan PJ, Zhu J, Kahn CR (May 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.
9. Zhu J, Bilan PJ, Moyers JS, Antonetti DA, Kahn CR (January 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.

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. Bibcode:1993Sci...262.1441R. doi:10.1126/science.8248782. PMID 8248782.
• Zhu J, Bilan PJ, Moyers JS, Antonetti DA, Kahn CR (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, Reynet C, Kahn RC (1996). "Molecular cloning of the human rad gene: gene structure and complete nucleotide sequence". Biochim. Biophys. Acta. 1316 (3): 145–8. doi:10.1016/0925-4439(96)00034-8. 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) (3): 609–14. doi:10.1042/bj3330609. PMC 1219623. PMID 9677319.
• 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, Rhodes CJ, Zetter BR, Moyers JS, Kahn CR (1999). "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. Bibcode:1999PNAS...9614911Z. doi:10.1073/pnas.96.26.14911. PMC 24747. PMID 10611312.
• Tseng YH, Vicent D, Zhu J, Niu Y, Adeyinka A, Moyers JS, Watson PH, Kahn CR (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.
• Yanuar A, Sakurai S, Kitano K, Hakoshima T (2005). "Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase". Acta Crystallographica Section F. 61 (Pt 11): 978–80. doi:10.1107/S1744309105031982. PMC 1978125. PMID 16511212.
• 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. S2CID 23729185.
• Suzuki M, Shigematsu H, Shames DS, Sunaga N, Takahashi T, Shivapurkar N, Iizasa T, Minna JD, Fujisawa T, Gazdar AF (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. S2CID 24884607.
• Yada H, Murata M, Shimoda K, Yuasa S, Kawaguchi H, Ieda M, Adachi T, Murata M, Ogawa S, Fukuda K (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, Hiller M, Huse K, Jahn N, Schreiber S, Backofen R, Platzer M (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biol. 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.

External links

• Overview of all the structural information available in the PDB for UniProt: P55042 (Human GTP-binding protein RAD (RRAD)) at the PDBe-KB.