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P63032 (RHES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding protein Rhes
Alternative name(s):
Ras homolog enriched in striatum
Gene names
Name:Rasd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.3 Ref.5

Subunit structure

Monomer Potential. Interacts with PIK3CA and UBE2I. Interacts with GNB1, GNB2 and GNB3 By similarity.

Subcellular location

Cell membrane; Lipid-anchor By similarity.

Tissue specificity

Highly expressed in brain; prominently in the striatum and weakly in kidney, thyroid, lung, heart and testis. Not expressed in liver. Expressed in pancreatic cell lines and in a embryonic stem cell line. Ref.3 Ref.4

Developmental stage

Expressed in the brain from E13.5. Ref.3

Induction

Down-regulated in hypothyroid conditions and up-regulated by glibenclamide. Ref.4 Ref.6

Post-translational modification

Farnesylated. Farnesylation is required for membrane targeting By similarity.

Disruption phenotype

Shows behavioral abnormalities, displaying a gender-dependent increase in anxiety levels and a clear motor coordination deficit and a mild hyperactive phenotype. Mice are more sensitive to D2 receptor stimulation and have decreased body weight. Ref.3 Ref.5 Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. RasD family.

Sequence caution

The sequence AAH26377.1 differs from that shown. Reason: Contaminating sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263GTP-binding protein Rhes
PRO_0000082721
Propeptide264 – 2663Removed in mature form By similarity
PRO_0000281376

Regions

Nucleotide binding26 – 338GTP By similarity
Nucleotide binding73 – 775GTP By similarity
Nucleotide binding140 – 1434GTP By similarity
Region189 – 23547Interaction with GNB1, GNB2 and GNB3 By similarity
Motif48 – 569Effector region

Amino acid modifications

Modified residue2631Cysteine methyl ester By similarity
Lipidation2631S-farnesyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63032 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 21B00C11CADD40B0

FASTA26630,197
        10         20         30         40         50         60 
MMKTLSSGNC TLNVPAKNSY RMVVLGASRV GKSSIVSRFL NGRFEDQYTP TIEDFHRKVY 

        70         80         90        100        110        120 
NIHGDMYQLD ILDTSGNHPF PAMRRLSILT GDVFILVFSL DSRESFDEVK RLQKQILEVK 

       130        140        150        160        170        180 
SCLKNKTKEA AELPMVICGN KNDHSELCRQ VPAMEAELLV SGDENCAYFE VSAKKNTNVN 

       190        200        210        220        230        240 
EMFYVLFSMA KLPHEMSPAL HHKISVQYGD AFHPRPFCMR RTKVAGAYGM VSPFARRPSV 

       250        260 
NSDLKYIKAK VLREGQARER DKCSIQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-266.
Tissue: Salivary gland.
[3]"Rhes is involved in striatal function."
Spano D., Branchi I., Rosica A., Pirro M.T., Riccio A., Mithbaokar P., Affuso A., Arra C., Campolongo P., Terracciano D., Macchia V., Bernal J., Alleva E., Di Lauro R.
Mol. Cell. Biol. 24:5788-5796(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"Rhes expression in pancreatic beta-cells is regulated by efaroxan in a calcium-dependent process."
Taylor J.P., Jackson D.A., Morgan N.G., Chan S.L.
Biochem. Biophys. Res. Commun. 349:809-815(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY EFAROXAN AND GLIBENCLAMIDE, TISSUE SPECIFICITY.
[5]"The GTP-binding protein Rhes modulates dopamine signalling in striatal medium spiny neurons."
Errico F., Santini E., Migliarini S., Borgkvist A., Centonze D., Nasti V., Carta M., De Chiara V., Prosperetti C., Spano D., Herve D., Pasqualetti M., Di Lauro R., Fisone G., Usiello A.
Mol. Cell. Neurosci. 37:335-345(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"T3 administration in adult hypothyroid mice modulates expression of proteins involved in striatal synaptic plasticity and improves motor behavior."
Vallortigara J., Alfos S., Micheau J., Higueret P., Enderlin V.
Neurobiol. Dis. 31:378-385(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HYPOTHYROIDISM.
[7]"The Ras homolog Rhes affects dopamine D1 and D2 receptor-mediated behavior in mice."
Quintero G.C., Spano D., Lahoste G.J., Harrison L.M.
NeuroReport 19:1563-1566(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK015898 mRNA. Translation: BAB30023.1.
BC026377 mRNA. Translation: AAH26377.1. Sequence problems.
RefSeqNP_083458.1. NM_029182.1.
UniGeneMm.179267.

3D structure databases

ProteinModelPortalP63032.
SMRP63032. Positions 18-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid217250. 8 interactions.

PTM databases

PhosphoSiteP63032.

Proteomic databases

PRIDEP63032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000132133; ENSMUSP00000120717; ENSMUSG00000034472.
ENSMUST00000139848; ENSMUSP00000118070; ENSMUSG00000034472.
GeneID75141.
KEGGmmu:75141.
UCSCuc009mhg.2. mouse.

Organism-specific databases

CTD23551.
MGIMGI:1922391. Rasd2.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117225.
HOVERGENHBG009351.
InParanoidP63032.
KOK07844.
OMADMDAYGM.
OrthoDBEOG7M0NSN.
TreeFamTF316238.

Gene expression databases

ArrayExpressP63032.
BgeeP63032.
CleanExMM_RASD2.
GenevestigatorP63032.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio342319.
PROP63032.
SOURCESearch...

Entry information

Entry nameRHES_MOUSE
AccessionPrimary (citable) accession number: P63032
Secondary accession number(s): Q9WVD3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot