RRAD

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
Gene location (Human)
Chr.	Chromosome 16 (human)[1]
End	66,925,536 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	104,631,327 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • GTP binding; • GO:0001948 protein binding; • calmodulin binding; • GTPase activity; • calcium channel regulator activity;
Cellular component	• cell membrane; • membrane; • intracellular;
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
	6236
	56437
	ENSG00000166592
	ENSMUSG00000031880
	P55042
	O88667
	NM_004165; NM_001128850
	NM_019662
	NP_001122322; NP_004156
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

GTP-binding protein RAD is a protein that in humans is encoded by the RRAD gene.[5][6]

Interactions

RRAD has been shown to interact with CAMK2G[7] and TPM2.[8]

References

GRCh38: Ensembl release 89: ENSG00000166592 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031880 - 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.
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.
"Entrez Gene: RRAD Ras-related associated with diabetes".
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.
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.

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, 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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000166592 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid7859947-5] 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.

[entrez-6] "Entrez Gene: RRAD Ras-related associated with diabetes".

[pmid9115241-7] 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.

[pmid8557685-8] 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.

RRAD

Interactions

References

Further reading

External links