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Q96D21

- RHES_HUMAN

UniProt

Q96D21 - RHES_HUMAN

Protein

GTP-binding protein Rhes

Gene

RASD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB-KW

    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

    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

    Cell membrane By similarity; Lipid-anchor By similarity

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB

    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 RhesPRO_0000082720Add
    BLAST
    Propeptidei264 – 2663Removed in mature formBy similarityPRO_0000281375

    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

    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 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.By similarity2 PublicationsCurated

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ96D21.
    SMRiQ96D21. Positions 18-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni189 – 23547Interaction with GNB1, GNB2 and GNB3Add
    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 118 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