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Showing Protein GTP-binding protein Rhes (HMDBP08548)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP08548
Secondary Accession Numbers
  • 14261
Name GTP-binding protein Rhes
Synonyms
  1. Ras homolog enriched in striatum
  2. Tumor endothelial marker 2
Gene Name RASD2
Protein Type Unknown
Biological Properties
General Function Involved in GTP binding
Specific Function GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
intracellular
Function
purine nucleotide binding
binding
nucleotide binding
catalytic activity
hydrolase activity
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
gtpase activity
nucleoside-triphosphatase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
intracellular signal transduction
small gtpase mediated signal transduction
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
Gene Properties
Chromosome Location Chromosome:2
Locus 22q13.1
SNPs RASD2
Gene Sequence 
>801 bp
ATGATGAAGACTTTGTCCAGCGGGAACTGCACGCTCAGTGTGCCCGCCAAAAACTCATAC
CGCATGGTGGTGCTGGGTGCCTCTCGGGTGGGCAAGAGCTCCATCGTGTCTCGCTTCCTC
AATGGCCGCTTTGAGGACCAGTACACACCCACCATCGAGGACTTCCACCGTAAGGTATAC
AACATCCGCGGCGACATGTACCAGCTCGACATCCTGGATACCTCTGGCAACCACCCCTTC
CCCGCCATGCGCAGGCTGTCCATCCTCACAGGGGATGTCTTCATCCTGGTGTTCAGCCTG
GATAACCGGGAGTCCTTCGATGAGGTCAAGCGCCTTCAGAAGCAGATCCTGGAGGTCAAG
TCCTGCCTGAAGAACAAGACCAAGGAGGCGGCGGAGCTGCCCATGGTCATCTGTGGCAAC
AAGAACGACCACGGCGAGCTGTGCCGCCAGGTGCCCACCACCGAGGCCGAGCTGCTGGTG
TCGGGCGACGAGAACTGCGCCTACTTCGAGGTGTCGGCCAAGAAGAACACCAACGTGGAC
GAGATGTTCTACGTGCTCTTCAGCATGGCCAAGCTGCCACACGAGATGAGCCCCGCCCTG
CATCGCAAGATCTCCGTGCAGTACGGTGACGCCTTCCACCCCAGGCCCTTCTGCATGCGC
CGCGTCAAGGAGATGGACGCCTATGGCATGGTCTCGCCCTTCGCCCGCCGCCCCAGCGTC
AACAGTGACCTCAAGTACATCAAGGCCAAGGTCCTTCGGGAAGGCCAGGCCCGTGAGAGG
GACAAGTGCACCATCCAGTGA
Protein Properties
Number of Residues 266
Molecular Weight 30365.8
Theoretical pI 9.18
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>GTP-binding protein Rhes
MMKTLSSGNCTLSVPAKNSYRMVVLGASRVGKSSIVSRFLNGRFEDQYTPTIEDFHRKVY
NIRGDMYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRESFDEVKRLQKQILEVK
SCLKNKTKEAAELPMVICGNKNDHGELCRQVPTTEAELLVSGDENCAYFEVSAKKNTNVD
EMFYVLFSMAKLPHEMSPALHRKISVQYGDAFHPRPFCMRRVKEMDAYGMVSPFARRPSV
NSDLKYIKAKVLREGQARERDKCTIQ
GenBank ID Protein 22027486
UniProtKB/Swiss-Prot ID Q96D21
UniProtKB/Swiss-Prot Entry Name RHES_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_014310.3
GeneCard ID RASD2
GenAtlas ID RASD2
HGNC ID HGNC:18229
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed:10591208 ]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed:15461802 ]
  4. St Croix B, Rago C, Velculescu V, Traverso G, Romans KE, Montgomery E, Lal A, Riggins GJ, Lengauer C, Vogelstein B, Kinzler KW: Genes expressed in human tumor endothelium. Science. 2000 Aug 18;289(5482):1197-202. [PubMed:10947988 ]
  5. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. doi: 10.1159/000204075. Epub 2009 Feb 18. [PubMed:19255495 ]
  6. Chan SL, Monks LK, Gao H, Deaville P, Morgan NG: Identification of the monomeric G-protein, Rhes, as an efaroxan-regulated protein in the pancreatic beta-cell. Br J Pharmacol. 2002 May;136(1):31-6. [PubMed:11976265 ]
  7. Subramaniam S, Sixt KM, Barrow R, Snyder SH: Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science. 2009 Jun 5;324(5932):1327-30. doi: 10.1126/science.1172871. [PubMed:19498170 ]