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Identification
HMDB Protein ID HMDBP09122
Secondary Accession Numbers
  • 14868
Name Rho-related GTP-binding protein RhoU
Synonyms
  1. CDC42-like GTPase 1
  2. GTP-binding protein-like 1
  3. Rho GTPase-like protein ARHU
  4. Ryu GTPase
  5. WRCH-1
  6. Wnt-1 responsive Cdc42 homolog 1
Gene Name RHOU
Protein Type Enzyme
Biological Properties
General Function Involved in GTP binding
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
purine nucleotide binding
binding
nucleotide binding
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
intracellular signal transduction
small gtpase mediated signal transduction
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
  3. Lipid-anchor
  4. Golgi apparatus membrane
  5. Cytoplasmic side
  6. Cell junction
  7. Cell projection
  8. focal adhesion
  9. podosome
Gene Properties
Chromosome Location Chromosome:1
Locus 1q42.11-q42.3
SNPs RHOU
Gene Sequence
>777 bp
ATGCCCCCGCAGCAGGGGGACCCCGCGTTCCCCGACCGCTGCGAGGCGCCTCCGGTGCCG
CCGCGTCGGGAGCGCGGTGGACGCGGGGGACGCGGGCCTGGGGAGCCGGGGGGCCGGGGG
CGTGCGGGGGGTGCCGAGGGGCGCGGCGTCAAGTGCGTGCTGGTCGGCGACGGCGCGGTG
GGCAAGACGAGCCTGGTGGTGAGTTACACCACCAACGGCTACCCCACCGAGTACATCCCT
ACTGCCTTCGACAACTTCTCCGCGGTGGTGTCTGTGGATGGGCGGCCCGTGAGACTCCAA
CTCTGTGACACTGCCGGACAGGATGAATTTGACAAGCTGAGGCCTCTCTGCTACACCAAC
ACAGACATCTTCCTGCTCTGCTTCAGTGTCGTGAGCCCCTCATCCTTCCAGAACGTCAGT
GAGAAATGGGTGCCGGAGATTCGATGCCACTGTCCCAAAGCCCCCATCATCCTAGTTGGA
ACGCAGTCGGATCTCAGAGAAGATGTCAAAGTCCTCATTGAGTTGGACAAATGCAAAGAA
AAGCCAGTGCCTGAAGAGGCGGCTAAGCTGTGCGCCGAGGAAATCAAAGCCGCCTCCTAC
ATCGAGTGTTCAGCCTTGACTCAAAAAAACCTCAAAGAGGTCTTTGATGCAGCCATCGTC
GCTGGCATTCAATACTCGGACACTCAGCAACAGCCAAAGAAGTCTAAAAGCAGGACTCCA
GATAAAATGAAAAACCTCTCCAAGTCCTGGTGGAAGAAGTACTGCTGTTTCGTATGA
Protein Properties
Number of Residues 258
Molecular Weight 28218.0
Theoretical pI 8.14
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Rho-related GTP-binding protein RhoU
MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGAEGRGVKCVLVGDGAV
GKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVRLQLCDTAGQDEFDKLRPLCYTN
TDIFLLCFSVVSPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKE
KPVPEEAAKLCAEEIKAASYIECSALTQKNLKEVFDAAIVAGIQYSDTQQQPKKSKSRTP
DKMKNLSKSWWKKYCCFV
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q7L0Q8
UniProtKB/Swiss-Prot Entry Name RHOU_HUMAN
PDB IDs Not Available
GenBank Gene ID AF378087
GeneCard ID RHOU
GenAtlas ID RHOU
HGNC ID HGNC:17794
References
General References
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  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  4. Tao W, Pennica D, Xu L, Kalejta RF, Levine AJ: Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1. Genes Dev. 2001 Jul 15;15(14):1796-807. [PubMed:11459829 ]
  5. Kirikoshi H, Katoh M: Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta-estradiol in MCF-7 cells. Int J Oncol. 2002 Apr;20(4):777-83. [PubMed:11894124 ]
  6. Daigo Y, Takayama I, Ponder BA, Caldas C, Ward SM, Sanders KM, Fujino MA: 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. J Gastroenterol Hepatol. 2004 Feb;19(2):211-7. [PubMed:14731133 ]
  7. Bubb KL, Bovee D, Buckley D, Haugen E, Kibukawa M, Paddock M, Palmieri A, Subramanian S, Zhou Y, Kaul R, Green P, Olson MV: Scan of human genome reveals no new Loci under ancient balancing selection. Genetics. 2006 Aug;173(4):2165-77. Epub 2006 Jun 4. [PubMed:16751668 ]
  8. Berzat AC, Buss JE, Chenette EJ, Weinbaum CA, Shutes A, Der CJ, Minden A, Cox AD: Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif. J Biol Chem. 2005 Sep 23;280(38):33055-65. Epub 2005 Jul 26. [PubMed:16046391 ]
  9. Shutes A, Berzat AC, Chenette EJ, Cox AD, Der CJ: Biochemical analyses of the Wrch atypical Rho family GTPases. Methods Enzymol. 2006;406:11-26. [PubMed:16472646 ]
  10. Ory S, Brazier H, Blangy A: Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration. Biol Cell. 2007 Dec;99(12):701-16. [PubMed:17620058 ]