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Q96D21

- RHES_HUMAN

UniProt

Q96D21 - RHES_HUMAN

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Protein
GTP-binding protein Rhes
Gene
RASD2, TEM2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Regions

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

GO - Molecular functioni

  1. G-protein beta-subunit binding Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. GTPase activity Source: UniProtKB
Complete GO annotation...

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: UniProtKB
  5. regulation of cAMP-mediated signaling Source: UniProtKB
  6. small GTPase mediated signal transduction Source: UniProtKB
  7. 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
Tumor endothelial marker 2
Gene namesi
Name:RASD2
Synonyms:TEM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18229. RASD2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263GTP-binding protein Rhes
PRO_0000082720Add
BLAST
Propeptidei264 – 2663Removed in mature form By similarity
PRO_0000281375

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631Cysteine methyl ester By similarity
Lipidationi263 – 2631S-farnesyl cysteine By similarity

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting By similarity.

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ96D21.
PRIDEiQ96D21.

PTM databases

PhosphoSiteiQ96D21.

Expressioni

Tissue specificityi

Pancreatic endocrine cells (islets of Langerhans).1 Publication

Gene expression databases

BgeeiQ96D21.
CleanExiHS_RASD2.
GenevestigatoriQ96D21.

Organism-specific databases

HPAiHPA005839.

Interactioni

Subunit structurei

Monomer Reviewed prediction. Interacts with PIK3CA and UBE2I By similarity. Interacts with GNB1, GNB2 and GNB3. Interacts with HTT; interacts with mutant HTT (mHTT) with a much higher affinity than wild type HTT.2 Publications

Protein-protein interaction databases

BioGridi117095. 6 interactions.
IntActiQ96D21. 1 interaction.
STRINGi9606.ENSP00000216127.

Structurei

3D structure databases

ProteinModelPortaliQ96D21.
SMRiQ96D21. Positions 18-191.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 23547Interaction with GNB1, GNB2 and GNB3
Add
BLAST

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ96D21.
KOiK07844.
OMAiDMDAYGM.
OrthoDBiEOG7M0NSN.
PhylomeDBiQ96D21.
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.

Q96D21-1 [UniParc]FASTAAdd to Basket

« Hide

MMKTLSSGNC TLSVPAKNSY RMVVLGASRV GKSSIVSRFL NGRFEDQYTP    50
TIEDFHRKVY NIRGDMYQLD ILDTSGNHPF PAMRRLSILT GDVFILVFSL 100
DNRESFDEVK RLQKQILEVK SCLKNKTKEA AELPMVICGN KNDHGELCRQ 150
VPTTEAELLV SGDENCAYFE VSAKKNTNVD EMFYVLFSMA KLPHEMSPAL 200
HRKISVQYGD AFHPRPFCMR RVKEMDAYGM VSPFARRPSV NSDLKYIKAK 250
VLREGQARER DKCTIQ 266
Length:266
Mass (Da):30,366
Last modified:December 1, 2001 - v1
Checksum:i2E23A76F346F9EDD
GO

Sequence cautioni

The sequence AAG00868.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF279143 mRNA. Translation: AAG00868.1. Different initiation.
CR456477 mRNA. Translation: CAG30363.1.
AL022334 Genomic DNA. Translation: CAI21838.1.
BC013419 mRNA. Translation: AAH13419.1.
CCDSiCCDS13916.1.
RefSeqiNP_055125.2. NM_014310.3.
XP_005261498.1. XM_005261441.2.
XP_005261499.1. XM_005261442.2.
XP_005261500.1. XM_005261443.1.
UniGeneiHs.474711.

Genome annotation databases

EnsembliENST00000216127; ENSP00000216127; ENSG00000100302.
GeneIDi23551.
KEGGihsa:23551.
UCSCiuc003anx.3. human.

Polymorphism databases

DMDMi21362868.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF279143 mRNA. Translation: AAG00868.1 . Different initiation.
CR456477 mRNA. Translation: CAG30363.1 .
AL022334 Genomic DNA. Translation: CAI21838.1 .
BC013419 mRNA. Translation: AAH13419.1 .
CCDSi CCDS13916.1.
RefSeqi NP_055125.2. NM_014310.3.
XP_005261498.1. XM_005261441.2.
XP_005261499.1. XM_005261442.2.
XP_005261500.1. XM_005261443.1.
UniGenei Hs.474711.

3D structure databases

ProteinModelPortali Q96D21.
SMRi Q96D21. Positions 18-191.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117095. 6 interactions.
IntActi Q96D21. 1 interaction.
STRINGi 9606.ENSP00000216127.

PTM databases

PhosphoSitei Q96D21.

Polymorphism databases

DMDMi 21362868.

Proteomic databases

PaxDbi Q96D21.
PRIDEi Q96D21.

Protocols and materials databases

DNASUi 23551.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216127 ; ENSP00000216127 ; ENSG00000100302 .
GeneIDi 23551.
KEGGi hsa:23551.
UCSCi uc003anx.3. human.

Organism-specific databases

CTDi 23551.
GeneCardsi GC22P035936.
HGNCi HGNC:18229. RASD2.
HPAi HPA005839.
MIMi 612842. gene.
neXtProti NX_Q96D21.
PharmGKBi PA34237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233973.
HOVERGENi HBG009351.
InParanoidi Q96D21.
KOi K07844.
OMAi DMDAYGM.
OrthoDBi EOG7M0NSN.
PhylomeDBi Q96D21.
TreeFami TF316238.

Miscellaneous databases

GeneWikii RASD2.
GenomeRNAii 23551.
NextBioi 46100.
PROi Q96D21.
SOURCEi Search...

Gene expression databases

Bgeei Q96D21.
CleanExi HS_RASD2.
Genevestigatori Q96D21.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view ]
PANTHERi PTHR24070. PTHR24070. 1 hit.
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00173. RAS. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51421. RAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Endothelial cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Uterus.
  5. "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: FUNCTION, TISSUE SPECIFICITY.
  6. "The cationic region of Rhes mediates its interactions with specific Gbeta subunits."
    Hill C., Goddard A., Ladds G., Davey J.
    Cell. Physiol. Biochem. 23:1-8(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GNB1; GNB2 AND GNB3.
  7. "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: INTERACTION WITH HTT, INVOLVEMENT IN CELL SURVIVAL.

Entry informationi

Entry nameiRHES_HUMAN
AccessioniPrimary (citable) accession number: Q96D21
Secondary accession number(s): O95520, Q5THY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Reduces cell survival in striatal cells with Huntington disease by binding to mutant Huntington disease protein (mHTT; poly-Gln region with 82 repeats) and inducing sumoylation of mHTT.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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