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Q7L0Q8 (RHOU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RHOU
Synonyms:ARHU, CDC42L1, G28K, WRCH1
ORF Names:SB128
OrganismHomo sapiens (Human) [Reference 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. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. Ref.1 Ref.14 Ref.15 Ref.16 Ref.17

Cofactor

Magnesium. Ref.14

Subunit structure

Interacts with PAK3. Interacts with ARHGAP30 in a GTP-independent manner. In its GTP-loaded conformation, interacts with ARHGAP31. Interacts with PTK2B/PYK2. Ref.15 Ref.16 Ref.18

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.13 Ref.14 Ref.15 Ref.16

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

Post-translational modification

Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation. Ref.16

Sequence similarities

Belongs to the small GTPase superfamily. Rho family. Ref.14

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

cytoskeleton organization

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

podosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 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.13 Ref.14

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.
Corresponds to variant rs3820264 [ dbSNP | Ensembl ].
VAR_051975

Experimental info

Mutagenesis631T → N: Loss of GTP-binding and localization to focal adhesions. No effect on ARHGAP30-binding. Ref.1 Ref.15 Ref.18
Mutagenesis801P → G: No effect on ARHGAP30-binding. Ref.18
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 Ref.18
Mutagenesis831F → G: Loss of ARHGAP30-binding. Ref.15 Ref.18
Mutagenesis861F → C: Loss of PAK3-binding; when associated with S-81 and A-83. No effect on ARHGAP30-binding. Ref.15 Ref.18
Mutagenesis1071Q → L: Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. No effect on ARHGAP30-binding. Ref.1 Ref.15 Ref.18
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 [UniParc].

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] [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]"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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [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.
+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.
RefSeqNP_067028.1. NM_021205.5.
UniGeneHs.647774.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3HX-ray1.73A32-230[»]
ProteinModelPortalQ7L0Q8.
SMRQ7L0Q8. Positions 49-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ7L0Q8. 4 interactions.
MINTMINT-7136717.
STRING9606.ENSP00000355652.

PTM databases

PhosphoSiteQ7L0Q8.

Polymorphism databases

DMDM172046189.

Proteomic databases

PaxDbQ7L0Q8.
PRIDEQ7L0Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366691; ENSP00000355652; ENSG00000116574. [Q7L0Q8-1]
GeneID58480.
KEGGhsa:58480.
UCSCuc001htf.3. human. [Q7L0Q8-1]

Organism-specific databases

CTD58480.
GeneCardsGC01P228785.
HGNCHGNC:17794. RHOU.
HPAHPA049592.
MIM606366. gene.
neXtProtNX_Q7L0Q8.
PharmGKBPA38246.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidQ7L0Q8.
KOK07865.
OMAGIQYSDS.
OrthoDBEOG7Z3F56.
PhylomeDBQ7L0Q8.
TreeFamTF321839.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ7L0Q8.

Gene expression databases

BgeeQ7L0Q8.
CleanExHS_RHOU.
GenevestigatorQ7L0Q8.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHOU. human.
EvolutionaryTraceQ7L0Q8.
GenomeRNAi58480.
NextBio64926.
PROQ7L0Q8.
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: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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