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Q96D21 (RHES_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Tumor endothelial marker 2
Gene names
Name:RASD2
Synonyms:TEM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.5 Ref.6

Subunit structure

Monomer Potential. 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. Ref.6 Ref.7

Subcellular location

Cell membrane; Lipid-anchor By similarity.

Tissue specificity

Pancreatic endocrine cells (islets of Langerhans). Ref.5

Post-translational modification

Farnesylated. Farnesylation is required for membrane targeting By similarity.

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.

Sequence similarities

Belongs to the small GTPase superfamily. RasD family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263GTP-binding protein Rhes
PRO_0000082720
Propeptide264 – 2663Removed in mature form By similarity
PRO_0000281375

Regions

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

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q96D21 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2E23A76F346F9EDD

FASTA26630,366
        10         20         30         40         50         60 
MMKTLSSGNC TLSVPAKNSY RMVVLGASRV GKSSIVSRFL NGRFEDQYTP TIEDFHRKVY 

        70         80         90        100        110        120 
NIRGDMYQLD ILDTSGNHPF PAMRRLSILT GDVFILVFSL DNRESFDEVK RLQKQILEVK 

       130        140        150        160        170        180 
SCLKNKTKEA AELPMVICGN KNDHGELCRQ VPTTEAELLV SGDENCAYFE VSAKKNTNVD 

       190        200        210        220        230        240 
EMFYVLFSMA KLPHEMSPAL HRKISVQYGD AFHPRPFCMR RVKEMDAYGM VSPFARRPSV 

       250        260 
NSDLKYIKAK VLREGQARER DKCTIQ 

« Hide

References

« Hide 'large scale' references
[1]"Genes expressed in human tumor endothelium."
St Croix B., Rago C., Velculescu V.E., Traverso G., Romans K.E., Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B., Kinzler K.W.
Science 289:1197-1202(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF279143 mRNA. Translation: AAG00868.1. Different initiation.
CR456477 mRNA. Translation: CAG30363.1.
AL022334 Genomic DNA. Translation: CAI21838.1.
BC013419 mRNA. Translation: AAH13419.1.
RefSeqNP_055125.2. NM_014310.3.
XP_005261498.1. XM_005261441.2.
XP_005261499.1. XM_005261442.2.
XP_005261500.1. XM_005261443.1.
UniGeneHs.474711.

3D structure databases

ProteinModelPortalQ96D21.
SMRQ96D21. Positions 18-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117095. 6 interactions.
IntActQ96D21. 1 interaction.
STRING9606.ENSP00000216127.

PTM databases

PhosphoSiteQ96D21.

Polymorphism databases

DMDM21362868.

Proteomic databases

PaxDbQ96D21.
PRIDEQ96D21.

Protocols and materials databases

DNASU23551.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216127; ENSP00000216127; ENSG00000100302.
GeneID23551.
KEGGhsa:23551.
UCSCuc003anx.3. human.

Organism-specific databases

CTD23551.
GeneCardsGC22P035936.
HGNCHGNC:18229. RASD2.
HPAHPA005839.
MIM612842. gene.
neXtProtNX_Q96D21.
PharmGKBPA34237.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidQ96D21.
KOK07844.
OMADMDAYGM.
OrthoDBEOG7M0NSN.
PhylomeDBQ96D21.
TreeFamTF316238.

Gene expression databases

BgeeQ96D21.
CleanExHS_RASD2.
GenevestigatorQ96D21.

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

GeneWikiRASD2.
GenomeRNAi23551.
NextBio46100.
PROQ96D21.
SOURCESearch...

Entry information

Entry nameRHES_HUMAN
AccessionPrimary (citable) accession number: Q96D21
Secondary accession number(s): O95520, Q5THY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM