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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. 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
(Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders.2 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

GTP hydrolysis is stimulated by ARHGAP30.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 19GTP2 Publications8
Nucleotide bindingi59 – 63GTPBy similarity5
Nucleotide bindingi117 – 120GTP2 Publications4

GO - Molecular functioni

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

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin cytoskeleton reorganization Source: UniProtKB
  • apical junction assembly Source: UniProtKB
  • apolipoprotein A-I-mediated signaling pathway Source: UniProtKB
  • cell migration Source: UniProtKB
  • cleavage furrow formation Source: UniProtKB
  • endothelial cell migration Source: MGI
  • endothelial tube lumen extension Source: MGI
  • ephrin receptor signaling pathway Source: Reactome
  • mitotic cleavage furrow formation Source: UniProtKB
  • mitotic spindle assembly Source: BHF-UCL
  • negative chemotaxis Source: UniProtKB
  • negative regulation of axonogenesis Source: Reactome
  • negative regulation of cell migration involved in sprouting angiogenesis Source: MGI
  • 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 protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of stress fiber assembly Source: MGI
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell migration Source: UniProtKB
  • regulation of cell motility Source: Reactome
  • regulation of osteoblast proliferation Source: BHF-UCL
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • Rho protein signal transduction Source: UniProtKB
  • Roundabout signaling pathway Source: UniProtKB
  • skeletal muscle satellite cell migration Source: AgBase
  • stress fiber assembly Source: UniProtKB
  • 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
  • Wnt signaling pathway, planar cell polarity pathway Source: ParkinsonsUK-UCL
  • 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

BioCyciZFISH:ENSG00000067560-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-193634. Axonal growth inhibition (RHOA activation).
R-HSA-194840. Rho GTPase cycle.
R-HSA-198203. PI3K/AKT activation.
R-HSA-209563. Axonal growth stimulation.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-6785631. ERBB2 Regulates Cell Motility.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP61586.
SIGNORiP61586.

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
Proteomesi
  • UP000005640 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
  • cell periphery Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • endosome Source: AgBase
  • extracellular exosome Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane 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)DescriptionActionsGraphical viewLength
Mutagenesisi14G → V: Causes constitutive activation. 1 Publication1
Mutagenesisi34Y → A: Abolishes interaction with DGKQ. 2 Publications1
Mutagenesisi34Y → F: Abolishes AMPylation by Haemophilus IbpA. 2 Publications1
Mutagenesisi63Q → L: Causes constitutive activation. 1
Mutagenesisi193L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi387.
OpenTargetsiENSG00000067560.
PharmGKBiPA134865095.

Chemistry databases

ChEMBLiCHEMBL6052.

Polymorphism and mutation databases

BioMutaiRHOA.
DMDMi47606458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000304111 – 190Transforming protein RhoAAdd BLAST190
PropeptideiPRO_0000030412191 – 193Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34O-AMP-tyrosine; by Haemophilus IbpA; alternate1 Publication1
Glycosylationi34O-linked (GlcNAc); by Photorhabdus PAU_02230; alternate1 Publication1
Modified residuei37O-AMP-threonine; by Vibrio VopS1 Publication1
Modified residuei41ADP-ribosylasparagine; by botulinum toxin1 Publication1
Modified residuei188Phosphoserine; by PKG/PRKG1By similarity1 Publication1
Modified residuei190Cysteine methyl esterBy similarity1
Lipidationi190S-geranylgeranyl cysteineBy similarity1

Post-translational modificationi

(Microbial infection) Substrate for botulinum ADP-ribosyltransferase.1 Publication
(Microbial infection) 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
(Microbial infection) 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
(Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly.1 Publication
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).By similarity1 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei189 – 190Cleavage; by yopT2

Keywords - PTMi

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

Proteomic databases

EPDiP61586.
MaxQBiP61586.
PaxDbiP61586.
PeptideAtlasiP61586.
PRIDEiP61586.
TopDownProteomicsiP61586.

PTM databases

iPTMnetiP61586.
PhosphoSitePlusiP61586.
SwissPalmiP61586.

Miscellaneous databases

PMAP-CutDBP61586.

Expressioni

Gene expression databases

BgeeiENSG00000067560.
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 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.
FAM65BQ9Y4F96EBI-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
sseJA0A0F6B1Q87EBI-446668,EBI-10760263From a different organism.
TRIP6Q156543EBI-446668,EBI-742327

GO - Molecular functioni

  • myosin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106880. 160 interactors.
DIPiDIP-29642N.
IntActiP61586. 69 interactors.
MINTiMINT-4999683.
STRINGi9606.ENSP00000400175.

Chemistry databases

BindingDBiP61586.

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Helixi14 – 16Combined sources3
Helixi18 – 27Combined sources10
Beta strandi43 – 47Combined sources5
Beta strandi52 – 58Combined sources7
Helixi63 – 69Combined sources7
Helixi70 – 73Combined sources4
Beta strandi78 – 85Combined sources8
Helixi89 – 97Combined sources9
Helixi99 – 106Combined sources8
Beta strandi107 – 109Combined sources3
Beta strandi112 – 117Combined sources6
Helixi119 – 121Combined sources3
Helixi125 – 132Combined sources8
Turni133 – 135Combined sources3
Helixi141 – 151Combined sources11
Beta strandi154 – 158Combined sources5
Turni161 – 163Combined sources3
Helixi167 – 179Combined sources13
Beta strandi190 – 193Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XOIX-ray2.09A/C1-180[»]
4XSGX-ray1.80A1-179[»]
4XSHX-ray2.50A1-179[»]
5A0FX-ray2.00A1-181[»]
5BWMX-ray2.50A1-179[»]
5C2KX-ray1.42A1-193[»]
5C4MX-ray1.30A1-193[»]
5FR1X-ray2.75A1-193[»]
5FR2X-ray3.35A1-193[»]
5HPYX-ray2.40B/F3-181[»]
5IRCX-ray1.72D/F2-181[»]
5JCPX-ray2.10A/B1-181[»]
ProteinModelPortaliP61586.
SMRiP61586.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61586.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi34 – 42Effector regionSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi182 – 187Arg/Lys-rich (basic)6

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

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61586.
KOiK04513.
OMAiGKKHHCV.
OrthoDBiEOG091G0QVS.
PhylomeDBiP61586.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 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)DescriptionActionsGraphical viewLength
Sequence conflicti23I → T in BAD96276 (Ref. 5) Curated1

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_001300870.1. NM_001313941.1.
NP_001655.1. NM_001664.3.
UniGeneiHs.247077.

Genome annotation databases

EnsembliENST00000418115; ENSP00000400175; ENSG00000067560.
GeneIDi387.
KEGGihsa:387.
UCSCiuc003cwu.4. 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_001300870.1. NM_001313941.1.
NP_001655.1. NM_001664.3.
UniGeneiHs.247077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XOIX-ray2.09A/C1-180[»]
4XSGX-ray1.80A1-179[»]
4XSHX-ray2.50A1-179[»]
5A0FX-ray2.00A1-181[»]
5BWMX-ray2.50A1-179[»]
5C2KX-ray1.42A1-193[»]
5C4MX-ray1.30A1-193[»]
5FR1X-ray2.75A1-193[»]
5FR2X-ray3.35A1-193[»]
5HPYX-ray2.40B/F3-181[»]
5IRCX-ray1.72D/F2-181[»]
5JCPX-ray2.10A/B1-181[»]
ProteinModelPortaliP61586.
SMRiP61586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106880. 160 interactors.
DIPiDIP-29642N.
IntActiP61586. 69 interactors.
MINTiMINT-4999683.
STRINGi9606.ENSP00000400175.

Chemistry databases

BindingDBiP61586.
ChEMBLiCHEMBL6052.

PTM databases

iPTMnetiP61586.
PhosphoSitePlusiP61586.
SwissPalmiP61586.

Polymorphism and mutation databases

BioMutaiRHOA.
DMDMi47606458.

Proteomic databases

EPDiP61586.
MaxQBiP61586.
PaxDbiP61586.
PeptideAtlasiP61586.
PRIDEiP61586.
TopDownProteomicsiP61586.

Protocols and materials databases

DNASUi387.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418115; ENSP00000400175; ENSG00000067560.
GeneIDi387.
KEGGihsa:387.
UCSCiuc003cwu.4. human.

Organism-specific databases

CTDi387.
DisGeNETi387.
GeneCardsiRHOA.
HGNCiHGNC:667. RHOA.
HPAiCAB005052.
HPA062346.
MIMi165390. gene.
neXtProtiNX_P61586.
OpenTargetsiENSG00000067560.
PharmGKBiPA134865095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61586.
KOiK04513.
OMAiGKKHHCV.
OrthoDBiEOG091G0QVS.
PhylomeDBiP61586.
TreeFamiTF300837.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000067560-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-193634. Axonal growth inhibition (RHOA activation).
R-HSA-194840. Rho GTPase cycle.
R-HSA-198203. PI3K/AKT activation.
R-HSA-209563. Axonal growth stimulation.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-6785631. ERBB2 Regulates Cell Motility.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP61586.
SIGNORiP61586.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000067560.
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.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 158 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

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 one 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.