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P17081

- RHOQ_HUMAN

UniProt

P17081 - RHOQ_HUMAN

Protein

Rho-related GTP-binding protein RhoQ

Gene

RHOQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia.1 Publication

    Enzyme regulationi

    Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 238GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi121 – 1244GTPBy similarity

    GO - Molecular functioni

    1. GBD domain binding Source: BHF-UCL
    2. GTPase activity Source: BHF-UCL
    3. GTP binding Source: UniProtKB-KW
    4. profilin binding Source: BHF-UCL

    GO - Biological processi

    1. cellular response to insulin stimulus Source: BHF-UCL
    2. cortical actin cytoskeleton organization Source: BHF-UCL
    3. GTP catabolic process Source: BHF-UCL
    4. insulin receptor signaling pathway Source: BHF-UCL
    5. negative regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    6. positive regulation of filopodium assembly Source: BHF-UCL
    7. positive regulation of glucose import Source: BHF-UCL
    8. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    9. regulation of actin cytoskeleton organization Source: BHF-UCL
    10. regulation of cell shape Source: Ensembl
    11. regulation of small GTPase mediated signal transduction Source: Reactome
    12. small GTPase mediated signal transduction Source: Reactome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinkiP17081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoQ
    Alternative name(s):
    Ras-like protein TC10
    Ras-like protein family member 7A
    Gene namesi
    Name:RHOQ
    Synonyms:ARHQ, RASL7A, TC10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17736. RHOQ.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Lipid-anchor 1 Publication

    GO - Cellular componenti

    1. actin filament Source: BHF-UCL
    2. cytosol Source: Reactome
    3. membrane raft Source: Ensembl
    4. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231T → N: Loss of interaction with GOPC. 1 Publication
    Mutagenesisi44 – 441D → A: Loss of interaction with GOPC. 1 Publication
    Mutagenesisi67 – 671Q → L: Constitutively active. Interacts with PARD6 proteins and GOPC. 1 Publication

    Organism-specific databases

    PharmGKBiPA134904280.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 202202Rho-related GTP-binding protein RhoQPRO_0000198871Add
    BLAST
    Propeptidei203 – 2053Removed in mature formBy similarityPRO_0000281222

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021Cysteine methyl esterBy similarity
    Lipidationi202 – 2021S-farnesyl cysteineBy similarity

    Post-translational modificationi

    May be post-translationally modified by both palmitoylation and polyisoprenylation.

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP17081.
    PaxDbiP17081.
    PRIDEiP17081.

    PTM databases

    PhosphoSiteiP17081.

    Expressioni

    Gene expression databases

    ArrayExpressiP17081.
    BgeeiP17081.
    CleanExiHS_RHOQ.
    GenevestigatoriP17081.

    Interactioni

    Subunit structurei

    Interacts with CDC42EP4 in a GTP-dependent manner. Interacts with ARHGAP33/TCGAP By similarity. Interacts with CDC42EP1, CDC42EP2, CDC42EP3, PARD6A, PARD6G (and probably PARD6B) in a GTP-dependent manner. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ). Interacts with EXO70 in a GTP-dependent manner. Interacts with GOPC.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi117001. 13 interactions.
    IntActiP17081. 4 interactions.
    STRINGi9606.ENSP00000238738.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 1611
    Helixi22 – 3110
    Beta strandi46 – 549
    Beta strandi56 – 627
    Beta strandi67 – 704
    Turni71 – 733
    Helixi74 – 774
    Beta strandi82 – 898
    Helixi93 – 1019
    Helixi103 – 1108
    Beta strandi116 – 1216
    Helixi129 – 1357
    Turni136 – 1394
    Helixi145 – 15511
    Beta strandi160 – 1623
    Turni165 – 1673
    Helixi171 – 18313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ATXX-ray2.65A/B1-185[»]
    ProteinModelPortaliP17081.
    SMRiP17081. Positions 1-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17081.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi38 – 469Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiP17081.
    KOiK07194.
    OMAiLAPRCIN.
    OrthoDBiEOG764747.
    PhylomeDBiP17081.
    TreeFamiTF101109.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00174. RHO. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51420. RHO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17081-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV    50
    TVGGKQYLLG LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK 100
    EEWVPELKEY APNVPFLLIG TQIDLRDDPK TLARLNDMKE KPICVEQGQK 150
    LAKEIGACCY VECSALTQKG LKTVFDEAII AILTPKKHTV KKRIGSRCIN 200
    CCLIT 205
    Length:205
    Mass (Da):22,659
    Last modified:April 26, 2005 - v2
    Checksum:i82695B4F8FBF0B75
    GO

    Sequence cautioni

    The sequence AAA36547.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAM21123.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31470 mRNA. Translation: AAA36547.1. Different initiation.
    AF498976 mRNA. Translation: AAM21123.1. Different initiation.
    AC018682 Genomic DNA. Translation: AAY14834.1.
    CH471053 Genomic DNA. Translation: EAX00251.1.
    BC056154 mRNA. Translation: AAH56154.3.
    BC065291 mRNA. Translation: AAH65291.2.
    BC070485 mRNA. Translation: AAH70485.2.
    BC093805 mRNA. Translation: AAH93805.2.
    BC101806 mRNA. Translation: AAI01807.1.
    CCDSiCCDS33191.1.
    PIRiD34788. TVHUC4.
    RefSeqiNP_036381.2. NM_012249.3.
    UniGeneiHs.709193.

    Genome annotation databases

    EnsembliENST00000238738; ENSP00000238738; ENSG00000119729.
    GeneIDi23433.
    KEGGihsa:23433.
    UCSCiuc002rva.3. human.

    Polymorphism databases

    DMDMi62906861.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31470 mRNA. Translation: AAA36547.1 . Different initiation.
    AF498976 mRNA. Translation: AAM21123.1 . Different initiation.
    AC018682 Genomic DNA. Translation: AAY14834.1 .
    CH471053 Genomic DNA. Translation: EAX00251.1 .
    BC056154 mRNA. Translation: AAH56154.3 .
    BC065291 mRNA. Translation: AAH65291.2 .
    BC070485 mRNA. Translation: AAH70485.2 .
    BC093805 mRNA. Translation: AAH93805.2 .
    BC101806 mRNA. Translation: AAI01807.1 .
    CCDSi CCDS33191.1.
    PIRi D34788. TVHUC4.
    RefSeqi NP_036381.2. NM_012249.3.
    UniGenei Hs.709193.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ATX X-ray 2.65 A/B 1-185 [» ]
    ProteinModelPortali P17081.
    SMRi P17081. Positions 1-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117001. 13 interactions.
    IntActi P17081. 4 interactions.
    STRINGi 9606.ENSP00000238738.

    PTM databases

    PhosphoSitei P17081.

    Polymorphism databases

    DMDMi 62906861.

    Proteomic databases

    MaxQBi P17081.
    PaxDbi P17081.
    PRIDEi P17081.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238738 ; ENSP00000238738 ; ENSG00000119729 .
    GeneIDi 23433.
    KEGGi hsa:23433.
    UCSCi uc002rva.3. human.

    Organism-specific databases

    CTDi 23433.
    GeneCardsi GC02P046768.
    HGNCi HGNC:17736. RHOQ.
    MIMi 605857. gene.
    neXtProti NX_P17081.
    PharmGKBi PA134904280.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi P17081.
    KOi K07194.
    OMAi LAPRCIN.
    OrthoDBi EOG764747.
    PhylomeDBi P17081.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinki P17081.

    Miscellaneous databases

    ChiTaRSi RHOQ. human.
    EvolutionaryTracei P17081.
    GeneWikii RHOQ.
    GenomeRNAii 23433.
    NextBioi 45687.
    PROi P17081.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17081.
    Bgeei P17081.
    CleanExi HS_RHOQ.
    Genevestigatori P17081.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
      Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
      Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Lung and Skin.
    6. "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins."
      Joberty G., Perlungher R.R., Macara I.G.
      Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3.
      Tissue: Embryo.
    7. "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
      Joberty G., Petersen C., Gao L., Macara I.G.
      Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6A AND PARD6G, MUTAGENESIS OF GLN-67.
    8. "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10."
      Neudauer C.L., Joberty G., Macara I.G.
      Biochem. Biophys. Res. Commun. 280:541-547(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GOPC, MUTAGENESIS OF THR-23 AND ASP-44.
    9. "Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10."
      Cheng J., Wang H., Guggino W.B.
      J. Biol. Chem. 280:3731-3739(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GOPC, SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiRHOQ_HUMAN
    AccessioniPrimary (citable) accession number: P17081
    Secondary accession number(s): D6W5A6
    , Q0VGN1, Q52LS8, Q53SJ1, Q6NS39, Q6P146, Q7Z480
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3