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Protein

Transforming protein RhoA

Gene

RHOA

Organism
Homo sapiens (Human)
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. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. 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.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,PubMed:19403695).By similarity9 Publications

Cofactori

Enzyme regulationi

GTP hydrolysis is stimulated by ARHGAP30.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei189 – 1902Cleavage; by yopT

Regions

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

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • myosin binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • apical junction assembly Source: UniProtKB
  • apolipoprotein A-I-mediated signaling pathway Source: UniProtKB
  • axon guidance Source: Reactome
  • blood coagulation Source: Reactome
  • cleavage furrow formation Source: UniProtKB
  • ephrin receptor signaling pathway Source: Reactome
  • metabolic process Source: GOC
  • mitotic spindle assembly Source: BHF-UCL
  • negative chemotaxis Source: UniProtKB
  • negative regulation of axonogenesis Source: Reactome
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • ossification involved in bone maturation Source: BHF-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • platelet activation Source: Reactome
  • positive regulation of axonogenesis Source: Reactome
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of lipase activity Source: AgBase
  • positive regulation of neuron differentiation Source: MGI
  • positive regulation of NF-kappaB import into nucleus Source: UniProtKB
  • positive regulation of stress fiber assembly Source: MGI
  • regulation of axonogenesis Source: Reactome
  • regulation of cell migration Source: UniProtKB
  • regulation of osteoblast proliferation Source: BHF-UCL
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • Rho protein signal transduction Source: UniProtKB
  • skeletal muscle satellite cell migration Source: AgBase
  • small GTPase mediated signal transduction Source: Reactome
  • substantia nigra development Source: UniProtKB
  • trabecula morphogenesis Source: BHF-UCL
  • transforming growth factor beta receptor signaling pathway Source: Reactome
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral process Source: UniProtKB-KW
  • wound healing, spreading of cells Source: AgBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Host-virus interaction

Keywords - Ligandi

GTP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_12464. PI3K/AKT activation.
REACT_13779. Axonal growth stimulation.
REACT_13815. Axonal growth inhibition (RHOA activation).
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_263952. EPHB-mediated forward signaling.
REACT_264199. PCP/CE pathway.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355321. RHO GTPases activate KTN1.
REACT_355542. RHO GTPases activate PKNs.
SignaLinkiP61586.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming protein RhoA
Alternative name(s):
Rho cDNA clone 12
Short name:
h12
Gene namesi
Name:RHOA
Synonyms:ARH12, ARHA, RHO12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:667. RHOA.

Subcellular locationi

GO - Cellular componenti

  • apical junction complex Source: UniProtKB
  • cell cortex Source: UniProtKB
  • cell junction Source: Reactome
  • cleavage furrow Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • endosome Source: AgBase
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
  • vesicle Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141G → V: Causes constitutive activation. 1 Publication
Mutagenesisi34 – 341Y → A: Abolishes interaction with DGKQ. 2 Publications
Mutagenesisi34 – 341Y → F: Abolishes AMPylation by Haemophilus IbpA. 2 Publications
Mutagenesisi63 – 631Q → L: Causes constitutive activation.
Mutagenesisi193 – 1931L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA134865095.

Polymorphism and mutation databases

BioMutaiRHOA.
DMDMi47606458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Transforming protein RhoAPRO_0000030411Add
BLAST
Propeptidei191 – 1933Removed in mature formPRO_0000030412

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341O-AMP-tyrosine; by Haemophilus IbpA1 Publication
Modified residuei37 – 371O-AMP-threonine; by Vibrio VopS1 Publication
Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxin1 Publication
Modified residuei188 – 1881Phosphoserine; by PKG/PRKG11 Publication
Modified residuei190 – 1901Cysteine methyl esterBy similarity
Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Substrate for botulinum ADP-ribosyltransferase.
Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.2 Publications
AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.2 Publications
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling.1 Publication
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.1 Publication

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

MaxQBiP61586.
PaxDbiP61586.
PeptideAtlasiP61586.
PRIDEiP61586.

PTM databases

PhosphoSiteiP61586.

Miscellaneous databases

PMAP-CutDBP61586.

Expressioni

Gene expression databases

BgeeiP61586.
CleanExiHS_RHOA.
ExpressionAtlasiP61586. baseline and differential.
GenevisibleiP61586. HS.

Organism-specific databases

HPAiCAB005052.
HPA062346.

Interactioni

Subunit structurei

Interacts with ARHGEF28 (By similarity). Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts with DIAPH1 (PubMed:23325789). Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with human respiratory syncytial virus (HRSV) protein F; this interaction facilitates virus-induced syncytium formation. 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. Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB. Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436).By similarity1 Publication22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGERQ151092EBI-446668,EBI-1646426
ARHGAP1Q079602EBI-446668,EBI-602762
ARHGDIAP525655EBI-446668,EBI-712693
ARHGEF11O150856EBI-446668,EBI-311099
ARHGEF12Q9NZN52EBI-446668,EBI-821440
ARHGEF19Q8IW932EBI-446668,EBI-7799822
DAAM1Q9Y4D15EBI-446668,EBI-2817289
DIAPH1O606103EBI-446668,EBI-3959709
Diaph1O088083EBI-446668,EBI-1026445From a different organism.
FAM65BQ9Y4F94EBI-446668,EBI-2798942
IKZF3Q9UKT93EBI-446668,EBI-747204
Mcf2lQ6PDM63EBI-446668,EBI-602149From a different organism.
NCLP193383EBI-446668,EBI-346967
Rabac1Q9Z0S93EBI-446668,EBI-476965From a different organism.
ROCK1Q134644EBI-446668,EBI-876651
RTKNQ9BST95EBI-446668,EBI-446694
RtknQ8C6B23EBI-446668,EBI-1162441From a different organism.
SMAD2Q157962EBI-446668,EBI-1040141
SMURF1Q9HCE7-22EBI-446668,EBI-9845742
TRIP6Q156543EBI-446668,EBI-742327

Protein-protein interaction databases

BioGridi106880. 129 interactions.
DIPiDIP-29642N.
IntActiP61586. 53 interactions.
MINTiMINT-4999683.
STRINGi9606.ENSP00000400175.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi14 – 163Combined sources
Helixi18 – 2710Combined sources
Beta strandi38 – 4811Combined sources
Beta strandi51 – 6010Combined sources
Helixi64 – 663Combined sources
Turni67 – 693Combined sources
Helixi70 – 734Combined sources
Beta strandi78 – 858Combined sources
Helixi89 – 979Combined sources
Helixi99 – 1068Combined sources
Beta strandi112 – 1176Combined sources
Helixi119 – 1213Combined sources
Helixi125 – 1339Combined sources
Helixi141 – 15010Combined sources
Beta strandi154 – 1585Combined sources
Turni161 – 1633Combined sources
Helixi167 – 17913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2BX-ray2.40A1-181[»]
1CC0X-ray5.00A/C1-190[»]
1CXZX-ray2.20A1-181[»]
1DPFX-ray2.00A1-180[»]
1FTNX-ray2.10A1-193[»]
1KMQX-ray1.55A4-181[»]
1LB1X-ray2.81B/D/F/H1-190[»]
1OW3X-ray1.80B1-193[»]
1S1CX-ray2.60A/B1-181[»]
1TX4X-ray1.65B3-179[»]
1X86X-ray3.22B/D/F/H1-193[»]
1XCGX-ray2.50B/F3-180[»]
2RGNX-ray3.50C/F1-193[»]
3KZ1X-ray2.70E/F1-181[»]
3LW8X-ray1.85A/B/C/D2-181[»]
3LWNX-ray2.28A/B2-181[»]
3LXRX-ray1.68A2-181[»]
3MSXX-ray1.65A1-180[»]
3T06X-ray2.84B/F3-180[»]
4D0NX-ray2.10A1-184[»]
4XH9X-ray2.00B/E2-180[»]
ProteinModelPortaliP61586.
SMRiP61586. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61586.

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)

Domaini

The basic-rich region is essential for yopT recognition and cleavage.

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61586.
KOiK04513.
OMAiRNDPHTI.
OrthoDBiEOG73FQPD.
PhylomeDBiP61586.
TreeFamiTF300837.

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.

P61586-1 [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 LVL
Length:193
Mass (Da):21,768
Last modified:January 1, 1988 - v1
Checksum:iC4DA2DC31FF858BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231I → T in BAD96276 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05026 mRNA. Translation: CAA28690.1.
L25080 mRNA. Translation: AAC33178.1.
AF498970 mRNA. Translation: AAM21117.1.
BT019870 mRNA. Translation: AAV38673.1.
AK222556 mRNA. Translation: BAD96276.1.
BX647063 mRNA. Translation: CAE46190.1.
AC104452 Genomic DNA. No translation available.
AC121247 Genomic DNA. No translation available.
AC137114 Genomic DNA. No translation available.
BC001360 mRNA. Translation: AAH01360.1.
BC005976 mRNA. Translation: AAH05976.1.
L09159 mRNA. Translation: AAA50612.1.
M83094 Genomic DNA. Translation: AAA67539.1.
CCDSiCCDS2795.1.
PIRiA26675. TVHU12.
RefSeqiNP_001655.1. NM_001664.2.
XP_011531997.1. XM_011533695.1.
UniGeneiHs.247077.

Genome annotation databases

EnsembliENST00000418115; ENSP00000400175; ENSG00000067560.
GeneIDi387.
KEGGihsa:387.
UCSCiuc003cwu.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05026 mRNA. Translation: CAA28690.1.
L25080 mRNA. Translation: AAC33178.1.
AF498970 mRNA. Translation: AAM21117.1.
BT019870 mRNA. Translation: AAV38673.1.
AK222556 mRNA. Translation: BAD96276.1.
BX647063 mRNA. Translation: CAE46190.1.
AC104452 Genomic DNA. No translation available.
AC121247 Genomic DNA. No translation available.
AC137114 Genomic DNA. No translation available.
BC001360 mRNA. Translation: AAH01360.1.
BC005976 mRNA. Translation: AAH05976.1.
L09159 mRNA. Translation: AAA50612.1.
M83094 Genomic DNA. Translation: AAA67539.1.
CCDSiCCDS2795.1.
PIRiA26675. TVHU12.
RefSeqiNP_001655.1. NM_001664.2.
XP_011531997.1. XM_011533695.1.
UniGeneiHs.247077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2BX-ray2.40A1-181[»]
1CC0X-ray5.00A/C1-190[»]
1CXZX-ray2.20A1-181[»]
1DPFX-ray2.00A1-180[»]
1FTNX-ray2.10A1-193[»]
1KMQX-ray1.55A4-181[»]
1LB1X-ray2.81B/D/F/H1-190[»]
1OW3X-ray1.80B1-193[»]
1S1CX-ray2.60A/B1-181[»]
1TX4X-ray1.65B3-179[»]
1X86X-ray3.22B/D/F/H1-193[»]
1XCGX-ray2.50B/F3-180[»]
2RGNX-ray3.50C/F1-193[»]
3KZ1X-ray2.70E/F1-181[»]
3LW8X-ray1.85A/B/C/D2-181[»]
3LWNX-ray2.28A/B2-181[»]
3LXRX-ray1.68A2-181[»]
3MSXX-ray1.65A1-180[»]
3T06X-ray2.84B/F3-180[»]
4D0NX-ray2.10A1-184[»]
4XH9X-ray2.00B/E2-180[»]
ProteinModelPortaliP61586.
SMRiP61586. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106880. 129 interactions.
DIPiDIP-29642N.
IntActiP61586. 53 interactions.
MINTiMINT-4999683.
STRINGi9606.ENSP00000400175.

Chemistry

BindingDBiP61586.
ChEMBLiCHEMBL6052.

PTM databases

PhosphoSiteiP61586.

Polymorphism and mutation databases

BioMutaiRHOA.
DMDMi47606458.

Proteomic databases

MaxQBiP61586.
PaxDbiP61586.
PeptideAtlasiP61586.
PRIDEiP61586.

Protocols and materials databases

DNASUi387.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418115; ENSP00000400175; ENSG00000067560.
GeneIDi387.
KEGGihsa:387.
UCSCiuc003cwu.3. human.

Organism-specific databases

CTDi387.
GeneCardsiGC03M049397.
HGNCiHGNC:667. RHOA.
HPAiCAB005052.
HPA062346.
MIMi165390. gene.
neXtProtiNX_P61586.
PharmGKBiPA134865095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61586.
KOiK04513.
OMAiRNDPHTI.
OrthoDBiEOG73FQPD.
PhylomeDBiP61586.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_12464. PI3K/AKT activation.
REACT_13779. Axonal growth stimulation.
REACT_13815. Axonal growth inhibition (RHOA activation).
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_263952. EPHB-mediated forward signaling.
REACT_264199. PCP/CE pathway.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355321. RHO GTPases activate KTN1.
REACT_355542. RHO GTPases activate PKNs.
SignaLinkiP61586.

Miscellaneous databases

ChiTaRSiRHOA. human.
EvolutionaryTraceiP61586.
GeneWikiiRHOA.
GenomeRNAii387.
NextBioi1611.
PMAP-CutDBP61586.
PROiP61586.
SOURCEiSearch...

Gene expression databases

BgeeiP61586.
CleanExiHS_RHOA.
ExpressionAtlasiP61586. baseline and differential.
GenevisibleiP61586. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts."
    Fagan K.P., Oliveira L., Pittler S.J.
    Exp. Eye Res. 59:235-237(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Esophageal carcinoma.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain and Colon.
  9. "Utilization of multiple polyadenylation signals in the human RHOA protooncogene."
    Moscow J.A., He R., Gudas J.M., Cowan K.H.
    Gene 144:229-236(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
    Tissue: Mammary cancer.
  10. "A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein."
    Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.
    J. Biol. Chem. 267:20916-20920(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184, ADP-RIBOSYLATION AT ASN-41.
    Tissue: Platelet.
  11. "Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)."
    Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.
    J. Biol. Chem. 267:5949-5958(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
  12. "The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase."
    Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.
    EMBO J. 15:1885-1893(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK1.
  13. "Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho."
    Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.
    EMBO J. 15:2208-2216(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK2.
  14. "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
    Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
    J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
    Vincent S., Settleman J.
    Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN2.
  16. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA2, SUBCELLULAR LOCATION.
  17. "Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases."
    Ren Y., Li R., Zheng Y., Busch H.
    J. Biol. Chem. 273:34954-34960(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF2.
  18. "Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA."
    Houssa B., de Widt J., Kranenburg O., Moolenaar W.H., van Blitterswijk W.J.
    J. Biol. Chem. 274:6820-6822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DGKQ, MUTAGENESIS OF TYR-34.
  19. "RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation."
    Pastey M.K., Crowe J.E. Jr., Graham B.S.
    J. Virol. 73:7262-7270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV PROTEIN F.
  20. "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
    Reynaud C., Fabre S., Jalinot P.
    J. Biol. Chem. 275:33962-33968(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTKN.
  21. Cited for: PHOSPHORYLATION AT SER-188 BY PRKG1.
  22. "Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling."
    Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.
    FEBS Lett. 507:264-268(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP13.
  23. "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC."
    Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.
    J. Biol. Chem. 277:42964-42972(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF3.
  24. "A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis."
    Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.
    Cell 109:575-588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE.
  25. "Direct activation of phospholipase C-epsilon by Rho."
    Wing M.R., Snyder J.T., Sondek J., Harden T.K.
    J. Biol. Chem. 278:41253-41258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLCE1.
  26. "Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases."
    Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.
    Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE, MUTAGENESIS OF LEU-193.
  27. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
    Yuce O., Piekny A., Glotzer M.
    J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  28. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
    Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
    Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  29. "The armadillo protein p0071 regulates Rho signalling during cytokinesis."
    Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
    Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKP4, SUBCELLULAR LOCATION.
  30. "The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration."
    Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.
    J. Cell Sci. 122:4535-4546(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "Dual roles for RHOA/RHO-kinase in the regulated trafficking of a voltage-sensitive potassium channel."
    Stirling L., Williams M.R., Morielli A.D.
    Mol. Biol. Cell 20:2991-3002(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. Cited for: AMPYLATION AT TYR-34, MUTAGENESIS OF TYR-34.
  33. "Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement."
    Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H.B., Shao F.
    Mol. Cell 35:841-855(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  34. "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
    Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
    Science 323:269-272(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: AMPYLATION AT THR-37.
  35. "Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro."
    Chatterjee A., Wang L., Armstrong D.L., Rossie S.
    J. Biol. Chem. 285:3872-3882(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-14.
  36. "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
    Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
    Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGDIA.
  37. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
    Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
    Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "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: ENZYME REGULATION.
  40. "RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway."
    Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., Liu X.P.
    Breast Cancer Res. Treat. 126:555-563(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  41. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN2.
  42. "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells."
    Li D., Dammer E.B., Lucki N.C., Sewer M.B.
    Mol. Biol. Cell 24:848-857(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIAPH1, IDENTIFICATION BY MASS SPECTROMETRY.
  43. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  44. "Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue."
    Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S., Kaibuchi K., Hakoshima T.
    J. Biol. Chem. 273:9656-9666(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
  45. "Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
    Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
    J. Struct. Biol. 126:166-170(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
  46. "An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism."
    Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K., Hakoshima T.
    J. Biol. Chem. 275:18311-18317(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  48. "Structural basis for the selective activation of Rho GTPases by Dbl exchange factors."
    Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.
    Nat. Struct. Biol. 9:468-475(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
  49. "Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution."
    Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K., Derewenda Z.S.
    Acta Crystallogr. D 59:876-880(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH A GTP ANALOG AND MG(2+).

Entry informationi

Entry nameiRHOA_HUMAN
AccessioniPrimary (citable) accession number: P61586
Secondary accession number(s): P06749
, Q53HM4, Q5U024, Q9UDJ0, Q9UEJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 22, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.