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Q7L0Q8

- RHOU_HUMAN

UniProt

Q7L0Q8 - RHOU_HUMAN

Protein

Rho-related GTP-binding protein RhoU

Gene

RHOU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape.5 Publications

    Cofactori

    Magnesium.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi56 – 638GTP1 Publication
    Nucleotide bindingi103 – 1075GTPBy similarity
    Nucleotide bindingi161 – 1644GTP

    GO - Molecular functioni

    1. GTPase activity Source: Ensembl
    2. GTP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. cytoskeleton organization Source: UniProtKB
    3. G1/S transition of mitotic cell cycle Source: Ensembl
    4. Rac protein signal transduction Source: Ensembl
    5. regulation of cell shape Source: UniProtKB
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. small GTPase mediated signal transduction Source: Reactome

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    SignaLinkiQ7L0Q8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoU
    Alternative name(s):
    CDC42-like GTPase 1
    GTP-binding protein-like 1
    Rho GTPase-like protein ARHU
    Ryu GTPase
    Wnt-1 responsive Cdc42 homolog 1
    Short name:
    WRCH-1
    Gene namesi
    Name:RHOUImported
    Synonyms:ARHUImported, CDC42L1Imported, G28KImported, WRCH1Imported
    ORF Names:SB128
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17794. RHOU.

    Subcellular locationi

    Cell membrane 3 Publications; Lipid-anchor 3 Publications; Cytoplasmic side 3 Publications. Golgi apparatus membrane 3 Publications; Lipid-anchor 3 Publications. Cell junctionfocal adhesion 3 Publications. Cell projectionpodosome 3 Publications
    Note: Localizes to podosomes in SRC-transformed cells.3 Publications

    GO - Cellular componenti

    1. cell projection Source: UniProtKB-KW
    2. cytosol Source: Reactome
    3. focal adhesion Source: UniProtKB-SubCell
    4. Golgi membrane Source: UniProtKB-SubCell
    5. plasma membrane Source: Reactome
    6. podosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631T → N: Loss of GTP-binding and localization to focal adhesions. No effect on ARHGAP30-binding. 3 Publications
    Mutagenesisi80 – 801P → G: No effect on ARHGAP30-binding. 1 Publication
    Mutagenesisi81 – 811T → S: Loss of binding to PAK3; when associated with A-83 and C-86. 1 Publication
    Mutagenesisi83 – 831F → A: Loss of binding to PAK3; when associated with S-81 and C-86. 2 Publications
    Mutagenesisi83 – 831F → G: Loss of ARHGAP30-binding. 2 Publications
    Mutagenesisi86 – 861F → C: Loss of PAK3-binding; when associated with S-81 and A-83. No effect on ARHGAP30-binding. 2 Publications
    Mutagenesisi107 – 1071Q → L: Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. No effect on ARHGAP30-binding. 3 Publications
    Mutagenesisi255 – 2551C → S: No effect on subcellular location. 1 Publication
    Mutagenesisi256 – 2561C → S: Loss of subcellular location to plasma and intracellular membranes. 1 Publication

    Organism-specific databases

    PharmGKBiPA38246.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 258258Rho-related GTP-binding protein RhoUPRO_0000326435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi256 – 2561S-palmitoyl cysteine2 Publications

    Post-translational modificationi

    Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiQ7L0Q8.
    PRIDEiQ7L0Q8.

    PTM databases

    PhosphoSiteiQ7L0Q8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissues examined. Expressed at high levels in the stomach, small intestine, brain, skeletal muscle and placenta.2 Publications

    Gene expression databases

    BgeeiQ7L0Q8.
    CleanExiHS_RHOU.
    GenevestigatoriQ7L0Q8.

    Organism-specific databases

    HPAiHPA049592.

    Interactioni

    Subunit structurei

    Interacts with PAK3. Interacts with ARHGAP30 in a GTP-independent manner. In its GTP-loaded conformation, interacts with ARHGAP31. Interacts with PTK2B/PYK2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK2O436396EBI-1638043,EBI-713635
    PAK1Q13153-22EBI-1638043,EBI-1019502
    PTK2BQ142894EBI-1638043,EBI-298640

    Protein-protein interaction databases

    IntActiQ7L0Q8. 4 interactions.
    MINTiMINT-7136717.
    STRINGi9606.ENSP00000355652.

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 556
    Helixi62 – 709
    Beta strandi82 – 9211
    Beta strandi95 – 1039
    Beta strandi111 – 1133
    Helixi114 – 1185
    Beta strandi122 – 1298
    Helixi133 – 1419
    Helixi143 – 1508
    Beta strandi152 – 1543
    Beta strandi156 – 1616
    Helixi163 – 1675
    Helixi169 – 1768
    Turni177 – 1793
    Helixi185 – 19511
    Beta strandi198 – 2025
    Turni205 – 2073
    Helixi211 – 22616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q3HX-ray1.73A32-230[»]
    ProteinModelPortaliQ7L0Q8.
    SMRiQ7L0Q8. Positions 49-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7L0Q8.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi26 – 6136Gly-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.1 Publication

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiQ7L0Q8.
    KOiK07865.
    OMAiKKSKCRT.
    OrthoDBiEOG7Z3F56.
    PhylomeDBiQ7L0Q8.
    TreeFamiTF321839.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 17 Publications (identifier: Q7L0Q8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV    50
    KCVLVGDGAV GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ 100
    LCDTAGQDEF DKLRPLCYTN TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH 150
    CPKAPIILVG TQSDLREDVK VLIELDKCKE KPVPEEAAKL CAEEIKAASY 200
    IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP DKMKNLSKSW 250
    WKKYCCFV 258
    Length:258
    Mass (Da):28,218
    Last modified:February 5, 2008 - v1
    Checksum:iD90059DE82288B97
    GO
    Isoform 2 (identifier: Q7L0Q8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: Missing.
         62-66: KTSLV → MTNIG

    Note: No experimental confirmation available.Curated

    Show »
    Length:197
    Mass (Da):22,164
    Checksum:iCAE1A9715F8B7D0B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 1313MPPQQ…AFPDR → QLLPTATLRGGGAVGPGPAS PRPQA in BAD92748. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti71 – 711T → P in AAL99390. (PubMed:11894124)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211T → A.
    Corresponds to variant rs3820264 [ dbSNP | Ensembl ].
    VAR_051975

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161Missing in isoform 2. 1 PublicationVSP_052732Add
    BLAST
    Alternative sequencei62 – 665KTSLV → MTNIG in isoform 2. 1 PublicationVSP_052733

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF378087 mRNA. Translation: AAK83340.1.
    AB074878 mRNA. Translation: BAB86361.1.
    AB051826 mRNA. Translation: BAB18638.1.
    DQ384420 Genomic DNA. Translation: ABD48870.1.
    DQ384421 Genomic DNA. Translation: ABD48871.1.
    DQ384422 Genomic DNA. Translation: ABD48872.1.
    DQ384423 Genomic DNA. Translation: ABD48873.1.
    DQ384424 Genomic DNA. Translation: ABD48874.1.
    DQ384425 Genomic DNA. Translation: ABD48875.1.
    AF211836 mRNA. Translation: AAL54874.1.
    AF282258 mRNA. Translation: AAG46058.1.
    AF251701 mRNA. Translation: AAL99390.1.
    AK289971 mRNA. Translation: BAF82660.1.
    AB209511 mRNA. Translation: BAD92748.1.
    AL096776 Genomic DNA. Translation: CAC00584.1.
    CH471098 Genomic DNA. Translation: EAW69885.1.
    BC040076 mRNA. Translation: AAH40076.1.
    CCDSiCCDS1575.1. [Q7L0Q8-1]
    RefSeqiNP_067028.1. NM_021205.5. [Q7L0Q8-1]
    UniGeneiHs.647774.

    Genome annotation databases

    EnsembliENST00000366691; ENSP00000355652; ENSG00000116574. [Q7L0Q8-1]
    GeneIDi58480.
    KEGGihsa:58480.
    UCSCiuc001htf.3. human. [Q7L0Q8-1]

    Polymorphism databases

    DMDMi172046189.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF378087 mRNA. Translation: AAK83340.1 .
    AB074878 mRNA. Translation: BAB86361.1 .
    AB051826 mRNA. Translation: BAB18638.1 .
    DQ384420 Genomic DNA. Translation: ABD48870.1 .
    DQ384421 Genomic DNA. Translation: ABD48871.1 .
    DQ384422 Genomic DNA. Translation: ABD48872.1 .
    DQ384423 Genomic DNA. Translation: ABD48873.1 .
    DQ384424 Genomic DNA. Translation: ABD48874.1 .
    DQ384425 Genomic DNA. Translation: ABD48875.1 .
    AF211836 mRNA. Translation: AAL54874.1 .
    AF282258 mRNA. Translation: AAG46058.1 .
    AF251701 mRNA. Translation: AAL99390.1 .
    AK289971 mRNA. Translation: BAF82660.1 .
    AB209511 mRNA. Translation: BAD92748.1 .
    AL096776 Genomic DNA. Translation: CAC00584.1 .
    CH471098 Genomic DNA. Translation: EAW69885.1 .
    BC040076 mRNA. Translation: AAH40076.1 .
    CCDSi CCDS1575.1. [Q7L0Q8-1 ]
    RefSeqi NP_067028.1. NM_021205.5. [Q7L0Q8-1 ]
    UniGenei Hs.647774.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q3H X-ray 1.73 A 32-230 [» ]
    ProteinModelPortali Q7L0Q8.
    SMRi Q7L0Q8. Positions 49-227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q7L0Q8. 4 interactions.
    MINTi MINT-7136717.
    STRINGi 9606.ENSP00000355652.

    PTM databases

    PhosphoSitei Q7L0Q8.

    Polymorphism databases

    DMDMi 172046189.

    Proteomic databases

    PaxDbi Q7L0Q8.
    PRIDEi Q7L0Q8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366691 ; ENSP00000355652 ; ENSG00000116574 . [Q7L0Q8-1 ]
    GeneIDi 58480.
    KEGGi hsa:58480.
    UCSCi uc001htf.3. human. [Q7L0Q8-1 ]

    Organism-specific databases

    CTDi 58480.
    GeneCardsi GC01P228785.
    HGNCi HGNC:17794. RHOU.
    HPAi HPA049592.
    MIMi 606366. gene.
    neXtProti NX_Q7L0Q8.
    PharmGKBi PA38246.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi Q7L0Q8.
    KOi K07865.
    OMAi KKSKCRT.
    OrthoDBi EOG7Z3F56.
    PhylomeDBi Q7L0Q8.
    TreeFami TF321839.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    SignaLinki Q7L0Q8.

    Miscellaneous databases

    ChiTaRSi RHOU. human.
    EvolutionaryTracei Q7L0Q8.
    GenomeRNAii 58480.
    NextBioi 64926.
    PROi Q7L0Q8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7L0Q8.
    CleanExi HS_RHOU.
    Genevestigatori Q7L0Q8.

    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. "Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1."
      Tao W., Pennica D., Xu L., Kalejta R.F., Levine A.J.
      Genes Dev. 15:1796-1807(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-63 AND GLN-107.
    2. "Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta-estradiol in MCF-7 cells."
      Kirikoshi H., Katoh M.
      Int. J. Oncol. 20:777-783(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Novel human, mouse and Xenopus genes encoding a member of the RAS superfamily of low-molecular-weight GTP-binding proteins and its downregulation in W/WV mouse jejunum."
      Daigo Y., Takayama I., Ponder B.A.J., Caldas C., Ward S.M., Sanders K.M., Fujino M.A.
      J. Gastroenterol. Hepatol. 19:211-217(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "A novel GTPase homologous to CDC42."
      Zhang J.S., Smith D.I., Urrutia R.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "Ryu: a new member of Rho family."
      Ikeda W., Nakanishi H., Takai Y.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. Zhang W., Wan T., Li N., He L., Chen T., Cao X.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: HippocampusImported.
    9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    10. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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] (ISOFORM 1).
      Tissue: BrainImported.
    13. "Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif."
      Berzat A.C., Buss J.E., Chenette E.J., Weinbaum C.A., Shutes A., Der C.J., Minden A., Cox A.D.
      J. Biol. Chem. 280:33055-33065(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-255 AND CYS-256, PALMITOYLATION AT CYS-256.
    14. "Biochemical analyses of the Wrch atypical Rho family GTPases."
      Shutes A., Berzat A.C., Chenette E.J., Cox A.D., Der C.J.
      Methods Enzymol. 406:11-26(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION, GTP-BINDING, PALMITOYLATION.
    15. "Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration."
      Ory S., Brazier H., Blangy A.
      Biol. Cell 99:701-716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAK3, MUTAGENESIS OF THR-63; THR-81; PHE-83; PHE-86 AND GLN-107.
    16. "The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics."
      Ruusala A., Aspenstrom P.
      Mol. Cell. Biol. 28:1802-1814(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    17. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
      Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
      BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion."
      Naji L., Pacholsky D., Aspenstrom P.
      Biochem. Biophys. Res. Commun. 409:96-102(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP30 AND ARHGAP31, MUTAGENESIS OF THR-63; PRO-80; PHE-83; PHE-86 AND GLN-107.
    19. "The crystal structure of RHOUA in the GDP-bound state."
      Structural genomics consortium (SGC)
      Submitted (JUN-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 32-230 IN COMPLEX WITH GDP AND MAGNESIUM IONS.

    Entry informationi

    Entry nameiRHOU_HUMAN
    AccessioniPrimary (citable) accession number: Q7L0Q8
    Secondary accession number(s): B1AKN1, Q59FE9, Q8TDQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 73 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3