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Protein

GTP-binding protein Rhes

Gene

Rasd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.5 Publications

Regions

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

GO - Molecular functioni

  • GTP binding Source: MGI
  • phosphatidylinositol 3-kinase binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: UniProtKB

GO - Biological processi

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

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein Rhes
Alternative name(s):
Ras homolog enriched in striatum
SE6C
Gene namesi
Name:Rasd2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi628594. Rasd2.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi263 – 2631C → A: Loss of plasma membrane localization. 2 Publications
Mutagenesisi263 – 2631C → S: Rather found in granular structures translocated to the nucleus. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263GTP-binding protein RhesPRO_0000082722Add
BLAST
Propeptidei264 – 2663Removed in mature formBy similarityPRO_0000281377

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631Cysteine methyl esterBy similarity
Lipidationi263 – 2631S-farnesyl cysteine1 Publication

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting.

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP63033.

Expressioni

Tissue specificityi

Prominently expressed in the striatum, weakly in the cerebral cortex and the CA fields of the hippocampus. Highly expressed in the hippocampus and cerebellum, only during the postnatal period. Also expressed in pancreatic endocrine cells (islets of Langerhans), adrenal gland and stomach and in a thyroid cell line.5 Publications

Developmental stagei

Low levels detected at E16 through P10, and increased between P10 and P15 during the development of brain; the amount did decrease in the adult brain.

Inductioni

By thyroid hormone, efaroxan and glibenclamide.2 Publications

Gene expression databases

GenevisibleiP63033. RN.

Interactioni

Subunit structurei

Monomer (Potential). Interacts with GNB1, GNB2 and GNB3 (By similarity). Interacts with PIK3CA and UBE2I.By similarityCurated2 Publications

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020017.

Structurei

3D structure databases

ProteinModelPortaliP63033.
SMRiP63033. Positions 18-191.
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

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP63033.
KOiK07844.
OMAiDMDAYGM.
OrthoDBiEOG7M0NSN.
PhylomeDBiP63033.
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]
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.

P63033-1 [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 31, 2004 - v1
Checksum:i21B00C11CADD40B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134409 mRNA. Translation: AAD38928.1.
RefSeqiNP_598252.1. NM_133568.1.
UniGeneiRn.115571.

Genome annotation databases

EnsembliENSRNOT00000020017; ENSRNOP00000020017; ENSRNOG00000014761.
GeneIDi171099.
KEGGirno:171099.
UCSCiRGD:628594. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134409 mRNA. Translation: AAD38928.1.
RefSeqiNP_598252.1. NM_133568.1.
UniGeneiRn.115571.

3D structure databases

ProteinModelPortaliP63033.
SMRiP63033. Positions 18-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020017.

Proteomic databases

PaxDbiP63033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020017; ENSRNOP00000020017; ENSRNOG00000014761.
GeneIDi171099.
KEGGirno:171099.
UCSCiRGD:628594. rat.

Organism-specific databases

CTDi23551.
RGDi628594. Rasd2.

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP63033.
KOiK07844.
OMAiDMDAYGM.
OrthoDBiEOG7M0NSN.
PhylomeDBiP63033.
TreeFamiTF316238.

Miscellaneous databases

PROiP63033.

Gene expression databases

GenevisibleiP63033. RN.

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]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GTP-BINDING.
    Strain: Sprague-Dawley.
    Tissue: Corpus striatum.
  2. "Identification of the monomeric G-protein, Rhes, as an efaroxan-regulated protein in the pancreatic beta-cell."
    Chan S.L.F., Monks L.K., Gao H., Deaville P., Morgan N.G.
    Br. J. Pharmacol. 136:31-36(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  3. "Thyroid hormone regulation of rhes, a novel Ras homolog gene expressed in the striatum."
    Vargiu P., Morte B., Manzano J., Perez J., de Abajo R., Sutcliffe J.G., Bernal J.
    Brain Res. Mol. Brain Res. 94:1-8(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY THYROID HORMONE.
  4. Cited for: TISSUE SPECIFICITY.
  5. "The small GTP-binding protein, Rhes, regulates signal transduction from G protein-coupled receptors."
    Vargiu P., De Abajo R., Garcia-Ranea J.A., Valencia A., Santisteban P., Crespo P., Bernal J.
    Oncogene 23:559-568(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GTP-BINDING, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-263, MUTAGENESIS OF CYS-263, INTERACTION WITH PIK3CA.
  6. "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: TISSUE SPECIFICITY, INDUCTION BY EFAROXAN AND GLIBENCLAMIDE.
  7. "Ontogeny and dopaminergic regulation in brain of Ras homolog enriched in striatum (Rhes)."
    Harrison L.M., Lahoste G.J., Ruskin D.N.
    Brain Res. 1245:16-25(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity."
    Subramaniam S., Sixt K.M., Barrow R., Snyder S.H.
    Science 324:1327-1330(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBE2I, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-263.

Entry informationi

Entry nameiRHES_RAT
AccessioniPrimary (citable) accession number: P63033
Secondary accession number(s): Q9WVD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 6, 2016
This is version 100 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.