Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rho-related GTP-binding protein RhoU

Gene

RHOU

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+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

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. positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  5. Rac protein signal transduction Source: Ensembl
  6. regulation of cell shape Source: UniProtKB
  7. regulation of small GTPase mediated signal transduction Source: Reactome
  8. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17794. RHOU.

Subcellular locationi

  1. Cell membrane 3 Publications; Lipid-anchor 3 Publications; Cytoplasmic side 3 Publications
  2. Golgi apparatus membrane 3 Publications; Lipid-anchor 3 Publications
  3. Cell junctionfocal adhesion 3 Publications
  4. Cell projectionpodosome 3 Publications

  5. 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
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiRHOU.
DMDMi172046189.

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 cysteine1 Publication

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.
ExpressionAtlasiQ7L0Q8. baseline and differential.
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 – 556Combined sources
Helixi62 – 709Combined sources
Beta strandi82 – 9211Combined sources
Beta strandi95 – 1039Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 1185Combined sources
Beta strandi122 – 1298Combined sources
Helixi133 – 1419Combined sources
Helixi143 – 1508Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi156 – 1616Combined sources
Helixi163 – 1675Combined sources
Helixi169 – 1768Combined sources
Turni177 – 1793Combined sources
Helixi185 – 19511Combined sources
Beta strandi198 – 2025Combined sources
Turni205 – 2073Combined sources
Helixi211 – 22616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ7L0Q8.
KOiK07865.
OMAiTLSKSWW.
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. AlignAdd to basket

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

        10         20         30         40         50
MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV
60 70 80 90 100
KCVLVGDGAV GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ
110 120 130 140 150
LCDTAGQDEF DKLRPLCYTN TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH
160 170 180 190 200
CPKAPIILVG TQSDLREDVK VLIELDKCKE KPVPEEAAKL CAEEIKAASY
210 220 230 240 250
IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP DKMKNLSKSW

WKKYCCFV
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 (Ref. 7) CuratedAdd
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiRHOU.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ7L0Q8.

Polymorphism and mutation databases

BioMutaiRHOU.
DMDMi172046189.

Proteomic databases

PaxDbiQ7L0Q8.
PRIDEiQ7L0Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi58480.
GeneCardsiGC01P228785.
HGNCiHGNC:17794. RHOU.
HPAiHPA049592.
MIMi606366. gene.
neXtProtiNX_Q7L0Q8.
PharmGKBiPA38246.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ7L0Q8.
KOiK07865.
OMAiTLSKSWW.
OrthoDBiEOG7Z3F56.
PhylomeDBiQ7L0Q8.
TreeFamiTF321839.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiQ7L0Q8.

Miscellaneous databases

ChiTaRSiRHOU. human.
EvolutionaryTraceiQ7L0Q8.
GenomeRNAii58480.
NextBioi64926.
PROiQ7L0Q8.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L0Q8.
CleanExiHS_RHOU.
ExpressionAtlasiQ7L0Q8. baseline and differential.
GenevestigatoriQ7L0Q8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 79 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.