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P61589 (RHOA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Required for the apical junction formation of keratinocyte cell-cell adhesion. 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.

Enzyme regulation

GTP hydrolysis is stimulated by ARHGAP30 By similarity.

Subunit structure

Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts with ARHGEF28. 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 ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Cleavage furrow By similarity. Cytoplasmcell cortex By similarity. Midbody By similarity. Cell projectionlamellipodium 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. Localized to cell-cell contacts in calcium-treated keratinocytes By similarity.

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
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DiseaseProto-oncogene
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 21440892. Source: BHF-UCL

actin cytoskeleton organization

Traceable author statement PubMed 12782387. Source: RGD

androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

apical junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to progesterone stimulus

Non-traceable author statement PubMed 21440892. Source: BHF-UCL

cerebral cortex cell migration

Inferred from electronic annotation. Source: Ensembl

cleavage furrow formation

Inferred from sequence or structural similarity. Source: UniProtKB

forebrain radial glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 17615156. Source: RGD

negative regulation of cell death

Inferred from mutant phenotype PubMed 20858895. Source: RGD

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from mutant phenotype PubMed 14517206. Source: RGD

neuron projection morphogenesis

Inferred from expression pattern PubMed 17109064. Source: RGD

ossification involved in bone maturation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 17369454. Source: RGD

positive regulation of cell adhesion

Inferred from expression pattern PubMed 17488779. Source: RGD

positive regulation of cell growth

Inferred from mutant phenotype PubMed 17537920. Source: RGD

positive regulation of cell migration

Inferred from expression pattern PubMed 17488779. Source: RGD

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 17425560. Source: RGD

positive regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17425560. Source: RGD

positive regulation of podosome assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 17379756. Source: RGD

positive regulation of translation

Inferred from expression pattern PubMed 17562852. Source: RGD

positive regulation of vasoconstriction

Inferred from expression pattern PubMed 17468135. Source: RGD

regulation of actin polymerization or depolymerization

Inferred from expression pattern PubMed 17562852. Source: RGD

regulation of calcium ion transport

Inferred from mutant phenotype PubMed 17558400. Source: RGD

regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dendrite development

Inferred from mutant phenotype PubMed 17670984. Source: RGD

regulation of neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of osteoblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from expression pattern PubMed 17515837. Source: RGD

response to drug

Inferred from direct assay PubMed 17492663. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 17109064PubMed 17442046. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 18391481. Source: RGD

response to glucose

Inferred from expression pattern PubMed 18356410. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16205723. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 17456553. Source: RGD

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

stress-activated protein kinase signaling cascade

Inferred from mutant phenotype PubMed 17369826. Source: RGD

trabecula morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical junction complex

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from direct assay PubMed 18554585. Source: RGD

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 18554585. Source: RGD

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 21440892. Source: BHF-UCL

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 21440892. Source: BHF-UCL

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP binding

Inferred from direct assay PubMed 20472934. Source: RGD

GTP binding

Inferred from direct assay PubMed 20472934. Source: RGD

GTPase activity

Inferred from direct assay PubMed 21440892. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 17620967PubMed 20472934. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 11696353. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Transforming protein RhoA
PRO_0000030415
Propeptide191 – 1933Removed in mature form By similarity
PRO_0000030416

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

Secondary structure

................................ 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61589 [UniParc].

Last modified May 24, 2004. 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]"Sequence of Wistar-Kyoto (WKY) and spontaneously hypertensive rat (SHR) RhoA cDNA."
Andresen B.T., Jackson E.K., Romero G.G.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SHR and Wistar Kyoto.
[2]"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].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY026068 mRNA. Translation: AAK11717.1.
AY026069 mRNA. Translation: AAK11718.1.
BC061732 mRNA. Translation: AAH61732.1.
RefSeqNP_476473.1. NM_057132.3.
XP_006243761.1. XM_006243699.1.
XP_006243762.1. XM_006243700.1.
XP_006243763.1. XM_006243701.1.
UniGeneRn.107401.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TVDX-ray2.99A/B1-193[»]
ProteinModelPortalP61589.
SMRP61589. Positions 2-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250720. 1 interaction.
IntActP61589. 4 interactions.
MINTMINT-4542785.

PTM databases

PhosphoSiteP61589.

2D gel databases

World-2DPAGE0004:P61589.

Proteomic databases

PaxDbP61589.
PRIDEP61589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000071664; ENSRNOP00000066672; ENSRNOG00000050519.
GeneID117273.
KEGGrno:117273.

Organism-specific databases

CTD387.
RGD619921. Rhoa.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00700000104143.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP61589.
KOK04513.
OMARNDPHTI.
OrthoDBEOG73FQPD.
PhylomeDBP61589.

Gene expression databases

ArrayExpressP61589.
GenevestigatorP61589.

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

NextBio620199.

Entry information

Entry nameRHOA_RAT
AccessionPrimary (citable) accession number: P61589
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references