RRAD: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (Bot: HTTP→HTTPS)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''GTP-binding protein RAD''' is a [[protein]] that in humans is encoded by the ''RRAD'' [[gene]].<ref name="pmid7859947">{{cite journal | vauthors = Doria A, Caldwell JS, Ji L, Reynet C, Rich SS, Weremowicz S, Morton CC, Warram JH, Kahn CR, Krolewski AS | title = Trinucleotide repeats at the rad locus. Allele distributions in NIDDM and mapping to a 3-cM region on chromosome 16q | journal = Diabetes | volume = 44 | issue = 2 | pages = 243–7  | date = March 1995 | pmid = 7859947 | pmc =  | doi = 10.2337/diabetes.44.2.243 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RRAD Ras-related associated with diabetes| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6236| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_RRAD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2dpx.
| PDB = {{PDB2|2dpx}}, {{PDB2|2gjs}}
| Name = Ras-related associated with diabetes
| HGNCid = 10446
| Symbol = RRAD
| AltSymbols =; RAD1; RAD; REM3
| OMIM = 179503
| ECnumber = 
| Homologene = 3071
| MGIid = 1930943
| GeneAtlas_image1 = PBB_GE_RRAD_204802_at_tn.png
| GeneAtlas_image2 = PBB_GE_RRAD_204803_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component =
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6236
    | Hs_Ensembl = ENSG00000166592
    | Hs_RefseqProtein = NP_004156
    | Hs_RefseqmRNA = NM_004165
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 65513092
    | Hs_GenLoc_end = 65516939
    | Hs_Uniprot = P55042
    | Mm_EntrezGene = 56437
    | Mm_Ensembl = ENSMUSG00000031880
    | Mm_RefseqmRNA = NM_019662
    | Mm_RefseqProtein = NP_062636
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 107517201
    | Mm_GenLoc_end = 107520445
    | Mm_Uniprot = Q6PGA2
  }}
}}
'''Ras-related associated with diabetes''', also known as '''RRAD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RRAD Ras-related associated with diabetes| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6236| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box BotSee Template:PBB_Controls to Stop updates. -->
RRAD has been shown to [[Protein-protein interaction|interact]] with [[CAMK2G]]<ref name=pmid9115241>{{cite journal | vauthors = Moyers JS, Bilan PJ, Zhu J, Kahn CR | title = Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11832–9 | date = May 1997 | pmid = 9115241 | doi = 10.1074/jbc.272.18.11832 }}</ref> and [[TPM2]].<ref name=pmid8557685>{{cite journal | vauthors = Zhu J, Bilan PJ, Moyers JS, Antonetti DA, Kahn CR | title = Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin | journal = J. Biol. Chem. | volume = 271 | issue = 2 | pages = 768–73  | date = January 1996 | pmid = 8557685 | doi = 10.1074/jbc.271.2.768 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Zhu J, Reynet C, Caldwell JS, Kahn CR | title = Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity | journal = J. Biol. Chem. | volume = 270 | issue = 9 | pages = 4805–12 | year = 1995 | pmid = 7876254 | doi = 10.1074/jbc.270.9.4805 }}
| citations =
* {{cite journal | vauthors = Reynet C, Kahn CR | title = Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans | journal = Science | volume = 262 | issue = 5138 | pages = 1441–4 | year = 1993 | pmid = 8248782 | doi = 10.1126/science.8248782 }}
*{{cite journal | author=Doria A, Caldwell JS, Ji L, ''et al.'' |title=Trinucleotide repeats at the rad locus. Allele distributions in NIDDM and mapping to a 3-cM region on chromosome 16q. |journal=Diabetes |volume=44 |issue= 2 |pages= 243-7 |year= 1995 |pmid= 7859947 |doi=  }}
* {{cite journal | vauthors = Zhu J, Bilan PJ, Moyers JS, Antonetti DA, Kahn CR | title = Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin | journal = J. Biol. Chem. | volume = 271 | issue = 2 | pages = 768–73 | year = 1996 | pmid = 8557685 | doi = 10.1074/jbc.271.2.768 }}
*{{cite journal  | author=Zhu J, Reynet C, Caldwell JS, Kahn CR |title=Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4805-12 |year= 1995 |pmid= 7876254 |doi= }}
* {{cite journal | vauthors = Caldwell JS, Moyers JS, Doria A, Reynet C, Kahn RC | title = Molecular cloning of the human rad gene: gene structure and complete nucleotide sequence | journal = Biochim. Biophys. Acta | volume = 1316 | issue = 3 | pages = 145–8 | year = 1996 | pmid = 8781531 | doi = 10.1016/0925-4439(96)00034-8 }}
*{{cite journal | author=Reynet C, Kahn CR |title=Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans. |journal=Science |volume=262 |issue= 5138 |pages= 1441-4 |year= 1993 |pmid= 8248782 |doi= }}
* {{cite journal | vauthors = Moyers JS, Bilan PJ, Reynet C, Kahn CR | title = Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells | journal = J. Biol. Chem. | volume = 271 | issue = 38 | pages = 23111–6 | year = 1996 | pmid = 8798502 | doi = 10.1074/jbc.271.38.23111 }}
*{{cite journal | author=Zhu J, Bilan PJ, Moyers JS, ''et al.'' |title=Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin. |journal=J. Biol. Chem. |volume=271 |issue= 2 |pages= 768-73 |year= 1996 |pmid= 8557685 |doi= }}
* {{cite journal | vauthors = Moyers JS, Bilan PJ, Zhu J, Kahn CR | title = Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11832–9 | year = 1997 | pmid = 9115241 | doi = 10.1074/jbc.272.18.11832 }}
*{{cite journal | author=Caldwell JS, Moyers JS, Doria A, ''et al.'' |title=Molecular cloning of the human rad gene: gene structure and complete nucleotide sequence. |journal=Biochim. Biophys. Acta |volume=1316 |issue= 3 |pages= 145-8 |year= 1996 |pmid= 8781531 |doi= }}
* {{cite journal | vauthors = Moyers JS, Zhu J, Kahn CR | title = Effects of phosphorylation on function of the Rad GTPase | journal = Biochem. J. | volume = 333 ( Pt 3) | issue = 3 | pages = 609–14 | year = 1998 | pmid = 9677319 | pmc = 1219623 | doi =  }}
*{{cite journal | author=Moyers JS, Bilan PJ, Reynet C, Kahn CR |title=Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23111-6 |year= 1996 |pmid= 8798502 |doi= }}
* {{cite journal | vauthors = Finlin BS, Andres DA | title = Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins | journal = Arch. Biochem. Biophys. | volume = 368 | issue = 2 | pages = 401–12 | year = 1999 | pmid = 10441394 | doi = 10.1006/abbi.1999.1316 }}
*{{cite journal | author=Moyers JS, Bilan PJ, Zhu J, Kahn CR |title=Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11832-9 |year= 1997 |pmid= 9115241 |doi= }}
* {{cite journal | vauthors = Zhu J, Tseng YH, Kantor JD, Rhodes CJ, Zetter BR, Moyers JS, Kahn CR | title = Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 26 | pages = 14911–8 | year = 1999 | pmid = 10611312 | pmc = 24747 | doi = 10.1073/pnas.96.26.14911 }}
*{{cite journal | author=Moyers JS, Zhu J, Kahn CR |title=Effects of phosphorylation on function of the Rad GTPase. |journal=Biochem. J. |volume=333 ( Pt 3) |issue= |pages= 609-14 |year= 1998 |pmid= 9677319 |doi=  }}
* {{cite journal | vauthors = Tseng YH, Vicent D, Zhu J, Niu Y, Adeyinka A, Moyers JS, Watson PH, Kahn CR | title = Regulation of growth and tumorigenicity of breast cancer cells by the low molecular weight GTPase Rad and nm23 | journal = Cancer Res. | volume = 61 | issue = 5 | pages = 2071–9 | year = 2001 | pmid = 11280768 | doi =  }}
*{{cite journal | author=Finlin BS, Andres DA |title=Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins. |journal=Arch. Biochem. Biophys. |volume=368 |issue= 2 |pages= 401-12 |year= 1999 |pmid= 10441394 |doi= 10.1006/abbi.1999.1316 }}
* {{cite journal | vauthors = Yanuar A, Sakurai S, Kitano K, Hakoshima T | title = Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase | journal = Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. | volume = 61 | issue = Pt 11 | pages = 978–80 | year = 2005 | pmid = 16511212 | pmc = 1978125 | doi = 10.1107/S1744309105031982 }}
*{{cite journal | author=Zhu J, Tseng YH, Kantor JD, ''et al.'' |title=Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 26 |pages= 14911-8 |year= 2000 |pmid= 10611312 |doi= }}
* {{cite journal | vauthors = Yanuar A, Sakurai S, Kitano K, Hakoshima T | title = Crystal structure of human Rad GTPase of the RGK-family | journal = Genes Cells | volume = 11 | issue = 8 | pages = 961–8 | year = 2006 | pmid = 16866878 | doi = 10.1111/j.1365-2443.2006.00994.x }}
*{{cite journal | author=Tseng YH, Vicent D, Zhu J, ''et al.'' |title=Regulation of growth and tumorigenicity of breast cancer cells by the low molecular weight GTPase Rad and nm23. |journal=Cancer Res. |volume=61 |issue= 5 |pages= 2071-9 |year= 2001 |pmid= 11280768 |doi=  }}
* {{cite journal | vauthors = Suzuki M, Shigematsu H, Shames DS, Sunaga N, Takahashi T, Shivapurkar N, Iizasa T, Minna JD, Fujisawa T, Gazdar AF | title = Methylation and gene silencing of the Ras-related GTPase gene in lung and breast cancers | journal = Ann. Surg. Oncol. | volume = 14 | issue = 4 | pages = 1397–404 | year = 2007 | pmid = 17195088 | doi = 10.1245/s10434-006-9089-6 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Yada H, Murata M, Shimoda K, Yuasa S, Kawaguchi H, Ieda M, Adachi T, Murata M, Ogawa S, Fukuda K | title = Dominant negative suppression of Rad leads to QT prolongation and causes ventricular arrhythmias via modulation of L-type Ca2+ channels in the heart | journal = Circ. Res. | volume = 101 | issue = 1 | pages = 69–77 | year = 2007 | pmid = 17525370 | doi = 10.1161/CIRCRESAHA.106.146399 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Szafranski K, Schindler S, Taudien S, Hiller M, Huse K, Jahn N, Schreiber S, Backofen R, Platzer M | title = Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns | journal = Genome Biol. | volume = 8 | issue = 8 | pages = R154 | year = 2007 | pmid = 17672918 | pmc = 2374985 | doi = 10.1186/gb-2007-8-8-r154 }}
*{{cite journal  | author=Yanuar A, Sakurai S, Kitano K, Hakoshima T |title=Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase. |journal=Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |volume=61 |issue= Pt 11 |pages= 978-80 |year= 2006 |pmid= 16511212 |doi= 10.1107/S1744309105031982 }}
*{{cite journal | author=Yanuar A, Sakurai S, Kitano K, Hakoshima T |title=Crystal structure of human Rad GTPase of the RGK-family. |journal=Genes Cells |volume=11 |issue= 8 |pages= 961-8 |year= 2006 |pmid= 16866878 |doi= 10.1111/j.1365-2443.2006.00994.x }}
*{{cite journal | author=Suzuki M, Shigematsu H, Shames DS, ''et al.'' |title=Methylation and gene silencing of the Ras-related GTPase gene in lung and breast cancers. |journal=Ann. Surg. Oncol. |volume=14 |issue= 4 |pages= 1397-404 |year= 2007 |pmid= 17195088 |doi= 10.1245/s10434-006-9089-6 }}
*{{cite journal | author=Yada H, Murata M, Shimoda K, ''et al.'' |title=Dominant negative suppression of Rad leads to QT prolongation and causes ventricular arrhythmias via modulation of L-type Ca2+ channels in the heart. |journal=Circ. Res. |volume=101 |issue= 1 |pages= 69-77 |year= 2007 |pmid= 17525370 |doi= 10.1161/CIRCRESAHA.106.146399 }}
*{{cite journal | author=Szafranski K, Schindler S, Taudien S, ''et al.'' |title=Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns. |journal= |volume=8 |issue= 8 |pages= R154 |year= |pmid= 17672918 |doi= 10.1186/gb-2007-8-8-r154 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=6236}}
{{WikiDoc Sources}}
 
 
{{gene-16-stub}}

Revision as of 09:29, 10 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. 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.
  2. "Entrez Gene: RRAD Ras-related associated with diabetes".
  3. 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.
  4. 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