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Reviewed, UniProtKB/Swiss-Prot Q7L0Q8 (RHOU_HUMAN)

Last modified February 9, 2010. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rho-related GTP-binding protein RhoU
Alternative name(s):
    Wnt-1 responsive Cdc42 homolog 1
      Short name=WRCH-1
    Ryu GTPase
    CDC42-like GTPase 1
    Rho GTPase-like protein ARHU
    GTP-binding protein-like 1
Gene names
Name: RHOU
Synonyms: ARHU, CDC42L1, G28K, WRCH1
ORF Names: SB128
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.1 Ref.14 Ref.15

Cofactor

Magnesium. Ref.14

Subunit structure

Interacts with PAK3. Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor. Cell junctionfocal adhesion. Cell projectionpodosome. Note: Localizes to podosomes in SRC-transformed cells. Ref.14 Ref.15 Ref.13

Tissue specificity

Ubiquitously expressed in all tissues examined. Expressed at high levels in the stomach, small intestine, brain, skeletal muscle and placenta. Ref.1 Ref.3

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.3 Ref.5 Ref.6 Ref.2 Ref.7 Ref.8 Ref.12 (identifier: Q7L0Q8-1)

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.
Isoform 2 Ref.9 (identifier: Q7L0Q8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     62-66: KTSLV → MTNIG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Rho-related GTP-binding protein RhoU
PRO_0000326435

Regions

Nucleotide binding56 – 638GTP Ref.1
Nucleotide binding103 – 1075GTP By similarity Ref.1
Nucleotide binding161 – 1644GTP UniProtKB P61586
Compositional bias26 – 6136Gly-rich

Amino acid modifications

Lipidation2561S-palmitoyl cysteine Ref.14 Ref.13

Natural variations

Alternative sequence1 – 6161Missing in isoform 2. Ref.9
VSP_052732
Alternative sequence62 – 665KTSLV → MTNIG in isoform 2. Ref.9
VSP_052733
Natural variant1211T → A: dbSNP rs3820264.
VAR_051975

Experimental info

Mutagenesis631T → N: Loss of GTP binding and localization to focal adhesions. Ref.1 Ref.15
Mutagenesis811T → S: Loss of binding to PAK3; when associated with A-83 and C-86. Ref.15
Mutagenesis831F → A: Loss of binding to PAK3; when associated with S-81 and C-86. Ref.15
Mutagenesis861F → C: Loss of binding to PAK3; when associated with S-81 and A-83. Ref.15
Mutagenesis1071Q → L: Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. Ref.1 Ref.15
Mutagenesis2551C → S: No effect on subcellular location. Ref.13
Mutagenesis2561C → S: Loss of subcellular location to plasma and intracellular membranes. Ref.13
Sequence conflict1 – 1313MPPQQ…AFPDR → QLLPTATLRGGGAVGPGPAS PRPQA in BAD92748. Ref.7
Sequence conflict711T → P in AAL99390. Ref.2

Secondary structure

................................... 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D90059DE82288B97

FASTA25828,218
        10         20         30         40         50         60 
MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV KCVLVGDGAV 

        70         80         90        100        110        120 
GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ LCDTAGQDEF DKLRPLCYTN 

       130        140        150        160        170        180 
TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH CPKAPIILVG TQSDLREDVK VLIELDKCKE 

       190        200        210        220        230        240 
KPVPEEAAKL CAEEIKAASY IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP 

       250 
DKMKNLSKSW WKKYCCFV 

« Hide

Isoform 2.

Checksum: CAE1A9715F8B7D0B
Show »

FASTA19722,164

References

« Hide 'large scale' references
[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: 11459829] [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: 11894124] [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: 14731133] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]"Scan of human genome reveals no new loci under ancient balancing selection."
Bubb K.L., Bovee D., Buckley D., Haugen E., Kibukawa M., Paddock M., Palmieri A., Subramanian S., Zhou Y., Kaul R., Green P., Olson M.V.
Genetics 173:2165-2177(2006) [PubMed: 16751668] [Abstract]
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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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: 16046391] [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: 16472646] [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: 17620058] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAK3, MUTAGENESIS OF THR-63; THR-81; PHE-83; PHE-86 AND GLN-107.
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00009644.
IPI00889079.
RefSeqNP_067028.1.
UniGeneHs.647774

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3HX-ray1.73A32-230[»]
SMRQ7L0Q8. Positions 23-219.
ModBaseSearch...

Protein-protein interaction databases

IntActQ7L0Q8. 6 interactions.
STRINGQ7L0Q8.

Proteomic databases

PRIDEQ7L0Q8.

Genome annotation databases

EnsemblENST00000366691; ENSP00000355652; ENSG00000116574; Homo sapiens. [Genome view]
GeneID58480.
KEGGhsa:58480.
UCSCuc001htf.1. human.

Organism-specific databases

CTD58480.
GeneCardsGC01P226937.
HGNCHGNC:17794. RHOU.
MIM606366. gene.
PharmGKBPA38246.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13152.
HOGENOMHBG745225.
InParanoidQ7L0Q8.
OMAEIRRHCP.
OrthoDBEOG9JHG1V.
PhylomeDBQ7L0Q8.

Enzyme and pathway databases

ReactomeREACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpressQ7L0Q8.
BgeeQ7L0Q8.
CleanExHS_RHOU.
GenevestigatorQ7L0Q8.

Family and domain databases

InterProIPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio64926.
SOURCESearch...

Entry information

Entry nameRHOU_HUMAN
AccessionPrimary (citable) accession number: Q7L0Q8
Secondary accession number(s): B1AKN1, Q59FE9, Q8TDQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 5, 2008
Last modified: February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents