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Q9QUI0 (RHOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transforming protein RhoA
Gene names
Name:Rhoa
Synonyms:Arha, Arha2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization By similarity. Required for the apical junction formation of keratinocyte cell-cell adhesion. Ref.9 Ref.10

Enzyme regulation

GTP hydrolysis is stimulated by ARHGAP30 By similarity.

Subunit structure

Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2 and ARHGEF3. Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with GNB2L1/RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 By similarity. Interacts with DIAPH1, NET1, RGNEF and RTKN. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Cleavage furrow By similarity. Cytoplasmcell cortex By similarity. Midbody By similarity. Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in a activated form and in a myosin- and actin-independent manner By similarity. Localized to cell-cell contacts in calcium-treated keratinocytes. Ref.9

Induction

Up-regulated during keratinocyte differentiation. Ref.9

Post-translational modification

Substrate for botulinum ADP-ribosyltransferase By similarity.

Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling By similarity.

Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   DiseaseProto-oncogene
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processRho protein signal transduction

Traceable author statement. Source: MGI

androgen receptor signaling pathway

Inferred from direct assay. Source: MGI

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cell morphogenesis

Inferred from genetic interaction. Source: MGI

cell-matrix adhesion

Inferred from direct assay. Source: MGI

integrin-mediated signaling pathway

Traceable author statement. Source: MGI

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from direct assay. Source: MGI

negative regulation of neuron apoptosis

Inferred from mutant phenotype. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay. Source: MGI

skeletal muscle tissue development

Inferred from direct assay. Source: MGI

stress fiber assembly

Inferred from direct assay. Source: MGI

   Cellular componentcell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cleavage furrow

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay. Source: MGI

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay. Source: MGI

nucleus

Inferred from direct assay. Source: MGI

ruffle membrane

Inferred from direct assay Ref.6. Source: MGI

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Transforming protein RhoA
PRO_0000030413
Propeptide191 – 1933Removed in mature form By similarity
PRO_0000030414

Regions

Nucleotide binding12 – 198GTP By similarity
Nucleotide binding59 – 635GTP By similarity
Nucleotide binding117 – 1204GTP By similarity
Motif34 – 429Effector region Potential
Compositional bias182 – 1876Arg/Lys-rich (basic)

Amino acid modifications

Modified residue1561Phosphotyrosine By similarity
Modified residue1881Phosphoserine; by PKG/PRKG1 By similarity
Modified residue1901Cysteine methyl ester By similarity
Lipidation1901S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict681R → C in AAC23710. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QUI0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C4C8BDC31FF858BC

FASTA19321,782
        10         20         30         40         50         60 
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT 

        70         80         90        100        110        120 
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 

       130        140        150        160        170        180 
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ 

       190 
ARRGKKKSGC LIL 

« Hide

References

« Hide 'large scale' references
[1]"Transposition of RhoA to the murine Y chromosome."
Boettger-Tong H.L., Agulnik A.I., Ty T.I., Bishop C.E.
Genomics 49:180-187(1998) [PubMed: 9598304] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]Budge P.J., Graham B.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c, C57BL/6, CD-1 and FVB/N.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[4]"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].
Strain: C57BL/6.
Tissue: Brain.
[5]"Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
J. Biol. Chem. 271:13556-13560(1996) [PubMed: 8662891] [Abstract]
Cited for: INTERACTION WITH RTKN.
[6]"p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin."
Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.
EMBO J. 16:3044-3056(1997) [PubMed: 9214622] [Abstract]
Cited for: INTERACTION WITH DIAPH1.
[7]"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7."
Alberts A.S., Bouquin N., Johnston L.H., Treisman R.
J. Biol. Chem. 273:8616-8622(1998) [PubMed: 9535835] [Abstract]
Cited for: INTERACTION WITH NET1.
[8]"Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules."
van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O.
J. Biol. Chem. 276:4948-4956(2001) [PubMed: 11058585] [Abstract]
Cited for: INTERACTION WITH RGNEF.
[9]"Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion."
Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P.
J. Cell Biol. 156:137-148(2002) [PubMed: 11777936] [Abstract]
Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
[10]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed: 20974804] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PKN2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF014371 mRNA. Translation: AAC23710.1.
AF178958 mRNA. Translation: AAD52675.1.
AF178959 mRNA. Translation: AAD52676.1.
AF178960 mRNA. Translation: AAD52677.1.
AF178961 mRNA. Translation: AAD52678.1.
AK077606 mRNA. Translation: BAC36896.1.
AK083624 mRNA. Translation: BAC38971.1.
BC068115 mRNA. Translation: AAH68115.1.
IPIIPI00315100.
RefSeqNP_058082.2. NM_016802.4.
UniGeneMm.471622.
Mm.757.

3D structure databases

ProteinModelPortalQ9QUI0.
SMRQ9QUI0. Positions 2-181.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29984N.
IntActQ9QUI0. 6 interactions.
MINTMINT-118662.
STRINGQ9QUI0.

PTM databases

PhosphoSiteQ9QUI0.

Proteomic databases

PRIDEQ9QUI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007959; ENSMUSP00000007959; ENSMUSG00000007815.
GeneID11848.
KEGGmmu:11848.

Organism-specific databases

CTD387.
MGIMGI:1096342. Rhoa.

Phylogenomic databases

eggNOGroNOG08740.
GeneTreeENSGT00550000074256.
HOGENOMHBG745225.
HOVERGENHBG009351.
InParanoidQ9QUI0.
OMADSPDSLX.
OrthoDBEOG4G4GRD.
PhylomeDBQ9QUI0.

Gene expression databases

ArrayExpressQ9QUI0.
BgeeQ9QUI0.
CleanExMM_RHOA.
GenevestigatorQ9QUI0.
GermOnlineENSMUSG00000007815. Mus musculus.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
KOK04513.
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

NextBio279815.
SOURCESearch...

Entry information

Entry nameRHOA_MOUSE
AccessionPrimary (citable) accession number: Q9QUI0
Secondary accession number(s): O88336
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families