Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transforming protein RhoA

Gene

Rhoa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436).By similarity1 Publication

Enzyme regulationi

GTP hydrolysis is stimulated by ARHGAP30.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: RGD
  2. GTPase activity Source: BHF-UCL
  3. GTP binding Source: RGD
  4. protein domain specific binding Source: RGD
  5. Rho GDP-dissociation inhibitor binding Source: RGD

GO - Biological processi

  1. actin cytoskeleton organization Source: RGD
  2. androgen receptor signaling pathway Source: Ensembl
  3. apical junction assembly Source: UniProtKB
  4. cell-matrix adhesion Source: Ensembl
  5. cellular response to progesterone stimulus Source: BHF-UCL
  6. cerebral cortex cell migration Source: Ensembl
  7. cleavage furrow formation Source: UniProtKB
  8. forebrain radial glial cell differentiation Source: Ensembl
  9. metabolic process Source: GOC
  10. negative regulation of cell death Source: RGD
  11. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: RGD
  12. negative regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
  13. negative regulation of neuron apoptotic process Source: Ensembl
  14. negative regulation of neuron differentiation Source: RGD
  15. neuron projection morphogenesis Source: RGD
  16. ossification involved in bone maturation Source: Ensembl
  17. positive regulation of actin filament polymerization Source: RGD
  18. positive regulation of cell adhesion Source: RGD
  19. positive regulation of cell growth Source: RGD
  20. positive regulation of cell migration Source: RGD
  21. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  22. positive regulation of cytokinesis Source: UniProtKB
  23. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  24. positive regulation of neuron apoptotic process Source: RGD
  25. positive regulation of podosome assembly Source: Ensembl
  26. positive regulation of smooth muscle contraction Source: RGD
  27. positive regulation of translation Source: RGD
  28. positive regulation of vasoconstriction Source: RGD
  29. regulation of actin polymerization or depolymerization Source: RGD
  30. regulation of calcium ion transport Source: RGD
  31. regulation of cell migration Source: UniProtKB
  32. regulation of dendrite development Source: RGD
  33. regulation of neural precursor cell proliferation Source: Ensembl
  34. regulation of osteoblast proliferation Source: Ensembl
  35. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  36. response to amino acid Source: RGD
  37. response to drug Source: RGD
  38. response to ethanol Source: RGD
  39. response to glucocorticoid Source: RGD
  40. response to glucose Source: RGD
  41. response to hypoxia Source: RGD
  42. response to mechanical stimulus Source: RGD
  43. skeletal muscle satellite cell migration Source: AgBase
  44. skeletal muscle tissue development Source: Ensembl
  45. small GTPase mediated signal transduction Source: InterPro
  46. stress-activated protein kinase signaling cascade Source: RGD
  47. stress fiber assembly Source: Ensembl
  48. trabecula morphogenesis Source: Ensembl
  49. wound healing, spreading of cells Source: AgBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_273778. PI3K/AKT activation.
REACT_277188. EPHB-mediated forward signaling.
REACT_296486. Axonal growth inhibition (RHOA activation).
REACT_297589. GPVI-mediated activation cascade.
REACT_298574. Rho GTPase cycle.
REACT_300978. G alpha (12/13) signalling events.
REACT_301330. VEGFA-VEGFR2 Pathway.
REACT_301547. G beta:gamma signalling through PI3Kgamma.
REACT_308893. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_330590. Sema4D mediated inhibition of cell attachment and migration.
REACT_330675. Axonal growth stimulation.
REACT_330939. Sema4D induced cell migration and growth-cone collapse.
REACT_335402. EPHA-mediated growth cone collapse.
REACT_345573. PCP/CE pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming protein RhoA
Gene namesi
Name:Rhoa
Synonyms:Arha, Arha2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi619921. Rhoa.

Subcellular locationi

Cell membrane By similarity; Lipid-anchor By similarity; 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).By similarity

GO - Cellular componenti

  1. apical junction complex Source: UniProtKB
  2. axon Source: RGD
  3. cell cortex Source: UniProtKB
  4. cleavage furrow Source: UniProtKB-SubCell
  5. cytoplasm Source: RGD
  6. cytoskeleton Source: UniProtKB-SubCell
  7. cytosol Source: BHF-UCL
  8. lamellipodium Source: UniProtKB
  9. membrane Source: BHF-UCL
  10. midbody Source: UniProtKB-SubCell
  11. mitochondrion Source: Ensembl
  12. nucleus Source: Ensembl
  13. ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Transforming protein RhoAPRO_0000030415Add
BLAST
Propeptidei191 – 1933Removed in mature formBy similarityPRO_0000030416

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine; by PKG/PRKG1By similarity
Modified residuei190 – 1901Cysteine methyl esterBy similarity
Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiP61589.
PRIDEiP61589.

2D gel databases

World-2DPAGE0004:P61589.

PTM databases

PhosphoSiteiP61589.

Expressioni

Gene expression databases

ExpressionAtlasiP61589. baseline and differential.
GenevestigatoriP61589.

Interactioni

Subunit structurei

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). Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436).By similarity1 Publication

Protein-protein interaction databases

BioGridi250720. 1 interaction.
IntActiP61589. 4 interactions.
MINTiMINT-4542785.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Helixi18 – 2710Combined sources
Beta strandi43 – 486Combined sources
Beta strandi51 – 588Combined sources
Helixi65 – 695Combined sources
Helixi70 – 723Combined sources
Beta strandi78 – 858Combined sources
Helixi89 – 979Combined sources
Helixi99 – 1068Combined sources
Beta strandi112 – 1176Combined sources
Helixi119 – 1213Combined sources
Helixi125 – 1339Combined sources
Helixi141 – 15111Combined sources
Beta strandi154 – 1585Combined sources
Turni161 – 1644Combined sources
Helixi167 – 17913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TVDX-ray2.99A/B1-193[»]
ProteinModelPortaliP61589.
SMRiP61589. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi182 – 1876Arg/Lys-rich (basic)

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61589.
KOiK04513.
OMAiRNDPHTI.
OrthoDBiEOG73FQPD.
PhylomeDBiP61589.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRNDEHTRRE LAKMKQEPVK PEEGRDMANR
160 170 180 190
IGAFGYMECS AKTKDGVREV FEMATRAALQ ARRGKKKSGC LIL
Length:193
Mass (Da):21,782
Last modified:May 23, 2004 - v1
Checksum:iC4C8BDC31FF858BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026068 mRNA. Translation: AAK11717.1.
AY026069 mRNA. Translation: AAK11718.1.
BC061732 mRNA. Translation: AAH61732.1.
RefSeqiNP_476473.1. NM_057132.3.
XP_006243761.1. XM_006243699.1.
XP_006243762.1. XM_006243700.1.
XP_006243763.1. XM_006243701.1.
UniGeneiRn.107401.

Genome annotation databases

EnsembliENSRNOT00000071664; ENSRNOP00000066672; ENSRNOG00000050519.
GeneIDi117273.
KEGGirno:117273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026068 mRNA. Translation: AAK11717.1.
AY026069 mRNA. Translation: AAK11718.1.
BC061732 mRNA. Translation: AAH61732.1.
RefSeqiNP_476473.1. NM_057132.3.
XP_006243761.1. XM_006243699.1.
XP_006243762.1. XM_006243700.1.
XP_006243763.1. XM_006243701.1.
UniGeneiRn.107401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TVDX-ray2.99A/B1-193[»]
ProteinModelPortaliP61589.
SMRiP61589. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250720. 1 interaction.
IntActiP61589. 4 interactions.
MINTiMINT-4542785.

PTM databases

PhosphoSiteiP61589.

2D gel databases

World-2DPAGE0004:P61589.

Proteomic databases

PaxDbiP61589.
PRIDEiP61589.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071664; ENSRNOP00000066672; ENSRNOG00000050519.
GeneIDi117273.
KEGGirno:117273.

Organism-specific databases

CTDi387.
RGDi619921. Rhoa.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61589.
KOiK04513.
OMAiRNDPHTI.
OrthoDBiEOG73FQPD.
PhylomeDBiP61589.

Enzyme and pathway databases

ReactomeiREACT_273778. PI3K/AKT activation.
REACT_277188. EPHB-mediated forward signaling.
REACT_296486. Axonal growth inhibition (RHOA activation).
REACT_297589. GPVI-mediated activation cascade.
REACT_298574. Rho GTPase cycle.
REACT_300978. G alpha (12/13) signalling events.
REACT_301330. VEGFA-VEGFR2 Pathway.
REACT_301547. G beta:gamma signalling through PI3Kgamma.
REACT_308893. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_330590. Sema4D mediated inhibition of cell attachment and migration.
REACT_330675. Axonal growth stimulation.
REACT_330939. Sema4D induced cell migration and growth-cone collapse.
REACT_335402. EPHA-mediated growth cone collapse.
REACT_345573. PCP/CE pathway.

Miscellaneous databases

NextBioi620199.

Gene expression databases

ExpressionAtlasiP61589. baseline and differential.
GenevestigatoriP61589.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of Wistar-Kyoto (WKY) and spontaneously hypertensive rat (SHR) RhoA cDNA."
    Andresen B.T., Jackson E.K., Romero G.G.
    Submitted (DEC-2000) 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel."
    Cachero T.G., Morielli A.D., Peralta E.G.
    Cell 93:1077-1085(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA2.

Entry informationi

Entry nameiRHOA_RAT
AccessioniPrimary (citable) accession number: P61589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2004
Last sequence update: May 23, 2004
Last modified: March 31, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.