MGP Database

MGP000197

UniProt Annotations

Entry Information
Gene Nameras homolog family member A
Protein EntryRHOA_HUMAN
UniProt IDP61586
SpeciesHuman
Comments
Comment typeDescription
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420;
DomainThe basic-rich region is essential for yopT recognition and cleavage.
Enzyme RegulationGTP hydrolysis is stimulated by ARHGAP30. {ECO:0000269|PubMed:21565175}.
FunctionRegulates 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). {ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.
InteractionQ15109:AGER; NbExp=2; IntAct=EBI-446668, EBI-1646426; Q07960:ARHGAP1; NbExp=2; IntAct=EBI-446668, EBI-602762; P52565:ARHGDIA; NbExp=2; IntAct=EBI-446668, EBI-712693; O15085:ARHGEF11; NbExp=6; IntAct=EBI-446668, EBI-311099; Q9NZN5:ARHGEF12; NbExp=2; IntAct=EBI-446668, EBI-821440; Q8IW93:ARHGEF19; NbExp=2; IntAct=EBI-446668, EBI-7799822; Q9Y4D1:DAAM1; NbExp=5; IntAct=EBI-446668, EBI-2817289; O60610:DIAPH1; NbExp=3; IntAct=EBI-446668, EBI-3959709; O08808:Diaph1 (xeno); NbExp=3; IntAct=EBI-446668, EBI-1026445; Q6PDM6:Mcf2l (xeno); NbExp=3; IntAct=EBI-446668, EBI-602149; P19338:NCL; NbExp=3; IntAct=EBI-446668, EBI-346967; Q9Z0S9:Rabac1 (xeno); NbExp=3; IntAct=EBI-446668, EBI-476965; Q13464:ROCK1; NbExp=4; IntAct=EBI-446668, EBI-876651; Q9BST9:RTKN; NbExp=5; IntAct=EBI-446668, EBI-446694; Q8C6B2:Rtkn (xeno); NbExp=3; IntAct=EBI-446668, EBI-1162441; Q15796:SMAD2; NbExp=2; IntAct=EBI-446668, EBI-1040141; Q9HCE7-2:SMURF1; NbExp=2; IntAct=EBI-446668, EBI-9845742;
PtmAMPylation 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. {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:19362538}.
PtmCleaved 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. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.
PtmPhosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling. {ECO:0000269|PubMed:11162591}.
PtmSubstrate for botulinum ADP-ribosyltransferase.
PtmUbiquitinated 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. {ECO:0000269|PubMed:19782033}.
SimilarityBelongs to the small GTPase superfamily. Rho family. {ECO:0000305}.
Subcellular LocationCell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium {ECO:0000250}. Note=Localized to cell-cell contacts in calcium-treated keratinocytes (By similarity). 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. {ECO:0000250}.
SubunitInteracts with ARHGEF28 (By similarity). Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. 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). {ECO:0000250, ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:10388627, ECO:0000269|PubMed:10438814, ECO:0000269|PubMed:10748207, ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:11696353, ECO:0000269|PubMed:12006984, ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:12538863, ECO:0000269|PubMed:12777804, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:17115030, ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:8641286, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9857026, ECO:0000305|PubMed:9635436}.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/RHOAID42107ch3p21.html";
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