Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GTP-binding protein Rhes

Gene

Rasd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi73 – 775GTPBy similarity
Nucleotide bindingi140 – 1434GTPBy similarity

GO - Molecular functioni

  1. G-protein beta-subunit binding Source: MGI
  2. GTP binding Source: MGI

GO - Biological processi

  1. locomotory behavior Source: UniProtKB
  2. negative regulation of protein ubiquitination Source: Ensembl
  3. positive regulation of protein kinase B signaling Source: UniProtKB
  4. positive regulation of protein sumoylation Source: Ensembl
  5. regulation of cAMP-mediated signaling Source: UniProtKB
  6. small GTPase mediated signal transduction Source: InterPro
  7. synaptic transmission, dopaminergic Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Behavior

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein Rhes
Alternative name(s):
Ras homolog enriched in striatum
Gene namesi
Name:Rasd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1922391. Rasd2.

Subcellular locationi

Cell membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263GTP-binding protein RhesPRO_0000082721Add
BLAST
Propeptidei264 – 2663Removed in mature formBy similarityPRO_0000281376

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631Cysteine methyl esterBy similarity
Lipidationi263 – 2631S-farnesyl cysteineBy similarity

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PRIDEiP63032.

PTM databases

PhosphoSiteiP63032.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed in the brain from E13.5.1 Publication

Inductioni

Down-regulated in hypothyroid conditions and up-regulated by glibenclamide.2 Publications

Gene expression databases

BgeeiP63032.
CleanExiMM_RASD2.
ExpressionAtlasiP63032. baseline and differential.
GenevestigatoriP63032.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi217250. 8 interactions.

Structurei

3D structure databases

ProteinModelPortaliP63032.
SMRiP63032. Positions 18-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 23547Interaction with GNB1, GNB2 and GNB3By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 569Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. RasD family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121857.
HOVERGENiHBG009351.
InParanoidiP63032.
KOiK07844.
OMAiDMDAYGM.
OrthoDBiEOG7M0NSN.
TreeFamiTF316238.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKTLSSGNC TLNVPAKNSY RMVVLGASRV GKSSIVSRFL NGRFEDQYTP
60 70 80 90 100
TIEDFHRKVY NIHGDMYQLD ILDTSGNHPF PAMRRLSILT GDVFILVFSL
110 120 130 140 150
DSRESFDEVK RLQKQILEVK SCLKNKTKEA AELPMVICGN KNDHSELCRQ
160 170 180 190 200
VPAMEAELLV SGDENCAYFE VSAKKNTNVN EMFYVLFSMA KLPHEMSPAL
210 220 230 240 250
HHKISVQYGD AFHPRPFCMR RTKVAGAYGM VSPFARRPSV NSDLKYIKAK
260
VLREGQARER DKCSIQ
Length:266
Mass (Da):30,197
Last modified:August 30, 2004 - v1
Checksum:i21B00C11CADD40B0
GO

Sequence cautioni

The sequence AAH26377.1 differs from that shown.Contaminating sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015898 mRNA. Translation: BAB30023.1.
BC026377 mRNA. Translation: AAH26377.1. Sequence problems.
CCDSiCCDS52602.1.
RefSeqiNP_083458.1. NM_029182.1.
UniGeneiMm.179267.

Genome annotation databases

EnsembliENSMUST00000132133; ENSMUSP00000120717; ENSMUSG00000034472.
ENSMUST00000139848; ENSMUSP00000118070; ENSMUSG00000034472.
GeneIDi75141.
KEGGimmu:75141.
UCSCiuc009mhg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015898 mRNA. Translation: BAB30023.1.
BC026377 mRNA. Translation: AAH26377.1. Sequence problems.
CCDSiCCDS52602.1.
RefSeqiNP_083458.1. NM_029182.1.
UniGeneiMm.179267.

3D structure databases

ProteinModelPortaliP63032.
SMRiP63032. Positions 18-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217250. 8 interactions.

PTM databases

PhosphoSiteiP63032.

Proteomic databases

PRIDEiP63032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000132133; ENSMUSP00000120717; ENSMUSG00000034472.
ENSMUST00000139848; ENSMUSP00000118070; ENSMUSG00000034472.
GeneIDi75141.
KEGGimmu:75141.
UCSCiuc009mhg.2. mouse.

Organism-specific databases

CTDi23551.
MGIiMGI:1922391. Rasd2.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121857.
HOVERGENiHBG009351.
InParanoidiP63032.
KOiK07844.
OMAiDMDAYGM.
OrthoDBiEOG7M0NSN.
TreeFamiTF316238.

Miscellaneous databases

NextBioi342319.
PROiP63032.
SOURCEiSearch...

Gene expression databases

BgeeiP63032.
CleanExiMM_RASD2.
ExpressionAtlasiP63032. baseline and differential.
GenevestigatoriP63032.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-266.
    Tissue: Salivary gland.
  3. 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY EFAROXAN AND GLIBENCLAMIDE, TISSUE SPECIFICITY.
  5. 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(2007) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRHES_MOUSE
AccessioniPrimary (citable) accession number: P63032
Secondary accession number(s): Q9WVD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2004
Last sequence update: August 30, 2004
Last modified: March 31, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.