RHOA is a ubiquitously expressed Rho-family small GTPase that cycles between an active GTP-bound and an inactive GDP-bound state and is anchored by C-terminal geranylgeranylation to the cytoplasmic face of the plasma membrane, with an inactive RhoGDI-bound cytosolic pool. In the GTP-bound state it engages effectors including ROCK1/2, the formins DIAPH1/mDia and PKN kinases to drive actomyosin contractility: it is the principal organizer of actin stress fibres and focal adhesions downstream of plasma-membrane receptors, and it is activated at the equatorial cortex by ECT2 during anaphase, where it specifies the cleavage furrow and the contractile ring for cytokinesis. RHOA also controls apical junction formation in epithelia, microtubule stabilization at the cell cortex through the MEMO1-RHOA-DIAPH1 axis, directed and chemokine-driven cell migration, and actin remodelling at postsynaptic sites. It is the target of bacterial toxins (C3 exoenzyme, YopT) and is recurrently mutated in diffuse gastric cancer and T-cell lymphoma.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000281 mitotic cytokinesis | IEA GO_REF:0000117 | ACCEPT | Summary: RHOA drives the actomyosin ring in mitotic cytokinesis. Reason: RHOA is activated at the equatorial cortex and is required for contractile ring assembly and furrow ingression; this is one of its best-established processes. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis |
| GO:0002363 alpha-beta T cell lineage commitment | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA is required for alpha-beta T cell lineage commitment in mouse. Reason: A lineage-specific developmental output of RHOA cytoskeletal signalling, transferred from rodent. |
| GO:0003189 aortic valve formation | IGI PMID:26188246 Cadherin-11 coordinates cellular migration and extracellular... | KEEP AS NON CORE | Summary: RHOA participates in aortic valve formation. Reason: Tissue-specific morphogenetic output of RHOA-dependent cytoskeletal and migratory control, supported by genetic interaction data. |
| GO:0003924 GTPase activity | EXP PMID:18829532 Breast tumor kinase phosphorylates p190RhoGAP to regulate rh... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | EXP PMID:21565175 ARHGAP30 is a Wrch-1-interacting protein involved in actin d... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | EXP PMID:23940119 The GEF Bcr activates RhoA/MAL signaling to promote keratino... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IDA PMID:19734146 Speckled-like pattern in the germinal center (SLIP-GC), a nu... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IDA PMID:19787194 Role of Kenae/CCDC125 in cell motility through the deregulat... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IDA PMID:26529257 Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppr... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IDA PMID:27917469 Association of dysfunctional synapse defective 1 (SYDE1) wit... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003924 GTPase activity | TAS PMID:10436159 Signaling from Rho to the actin cytoskeleton through protein... | ACCEPT | Summary: RHOA hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RHOA and the basis of its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0003925 G protein activity | IDA PMID:21565175 ARHGAP30 is a Wrch-1-interacting protein involved in actin d... | ACCEPT | Summary: RHOA is a nucleotide-dependent molecular switch. Reason: G protein activity covers monomeric small GTPases; RHOA signals by switching between GTP- and GDP-bound states and binding effectors only when GTP-loaded. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt in active state binds to a variety of effector proteins to regulate cellular responses |
| GO:0003925 G protein activity | IDA PMID:23940119 The GEF Bcr activates RhoA/MAL signaling to promote keratino... | ACCEPT | Summary: RHOA is a nucleotide-dependent molecular switch. Reason: G protein activity covers monomeric small GTPases; RHOA signals by switching between GTP- and GDP-bound states and binding effectors only when GTP-loaded. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt in active state binds to a variety of effector proteins to regulate cellular responses |
| GO:0003925 G protein activity | IEA GO_REF:0000003 | ACCEPT | Summary: RHOA is a nucleotide-dependent molecular switch. Reason: G protein activity covers monomeric small GTPases; RHOA signals by switching between GTP- and GDP-bound states and binding effectors only when GTP-loaded. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt in active state binds to a variety of effector proteins to regulate cellular responses |
| GO:0005515 protein binding | IPI PMID:10051605 The small GTPase RalA targets filamin to induce filopodia. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:10066731 Diacylglycerol kinase theta binds to and is negatively regul... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:10489445 How RhoGDI binds Rho. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:11067852 Identification, characterization, and functional analysis of... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:11335720 Prenylated Rab acceptor protein is a receptor for prenylated... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:11889037 A crystallographic view of interactions between Dbs and Cdc4... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:11927263 MgF(3)(-) as a transition state analog of phosphoryl transfe... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:12006984 Structural basis for the selective activation of Rho GTPases... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:12006984 Structural basis for the selective activation of Rho GTPases... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:12879077 RhoG activates Rac1 by direct interaction with the Dock180-b... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:14660612 Structural insights into the interaction of ROCKI with the s... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:15364580 Inter-domain motions of the N-domain of the KdpFABC complex,... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:15530360 The crystal structure of RhoA in complex with the DH/PH frag... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:15644318 BIG1 is a binding partner of myosin IXb and regulates its Rh... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:17115030 The armadillo protein p0071 regulates Rho signalling during ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:18218625 Biochemical characterization of the Rho GTPase-regulated act... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:18218625 Biochemical characterization of the Rho GTPase-regulated act... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:18256687 WGEF activates Rho in the Wnt-PCP pathway and controls conve... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:18256687 WGEF activates Rho in the Wnt-PCP pathway and controls conve... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:19470470 RSK1 drives p27Kip1 phosphorylation at T198 to promote RhoA ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:19887681 Activation of a bacterial virulence protein by the GTPase Rh... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:19944695 Advanced glycation end products increase endothelial permeab... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:19944695 Advanced glycation end products increase endothelial permeab... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20300064 A bacterial effector targets host DH-PH domain RhoGEFs and a... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20300064 A bacterial effector targets host DH-PH domain RhoGEFs and a... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20300064 A bacterial effector targets host DH-PH domain RhoGEFs and a... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20348415 Plk4 is required for cytokinesis and maintenance of chromoso... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20711218 The role of ezrin-associated protein network in human sperm ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:20974804 The Rho target PRK2 regulates apical junction formation in h... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21029865 EphB-mediated degradation of the RhoA GEF Ephexin5 relieves ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21281639 Arachidonic acid stimulates formation of a novel complex con... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21281639 Arachidonic acid stimulates formation of a novel complex con... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21708152 Binding of RhoA by the C2 domain of E3 ligase Smurf1 is esse... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:22404908 Effect of cancer-associated mutations in the PlexinB1 gene. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:22621765 Distinct biological activities of C3 and ADP-ribosyltransfer... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:22705156 WNT-3a modulates platelet function by regulating small GTPas... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:22740689 A Salmonella typhimurium-translocated glycerophospholipid:ch... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:22740689 A Salmonella typhimurium-translocated glycerophospholipid:ch... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:23241886 Fam65b is a new transcriptional target of FOXO1 that regulat... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:23241886 Fam65b is a new transcriptional target of FOXO1 that regulat... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:24259668 The RhoGAP ARHGAP19 controls cytokinesis and chromosome segr... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25150978 An extracellular-matrix-specific GEF-GAP interaction regulat... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25186459 The crystal structure of the RhoA-AKAP-Lbc DH-PH domain comp... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:25588844 Front-signal-dependent accumulation of the RHOA inhibitor FA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:26529257 Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppr... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:27807006 RHO binding to FAM65A regulates Golgi reorientation during c... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:28630045 Structure-based analysis of the guanine nucleotide exchange ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:30190425 GEF mechanism revealed by the structure of SmgGDS-558 and fa... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34237247 Global mapping of Salmonella enterica-host protein-protein i... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005515 protein binding | IPI PMID:9214622 p140mDia, a mammalian homolog of Drosophila diaphanous, is a... | REMOVE | Summary: Generic protein binding from a large number of interaction studies. Reason: GO:0005515 is uninformative and removed under the project protein-binding policy. The informative interactions are represented by myosin binding, protein kinase binding and the effector-driven process annotations; removal does not dispute the reported interactions. |
| GO:0005525 GTP binding | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA binds GTP. Reason: Guanine nucleotide binding is directly demonstrated and inseparable from the switch function. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0005525 GTP binding | IDA PMID:12777804 Structure of a constitutively activated RhoA mutant (Q63L) a... | ACCEPT | Summary: RHOA binds GTP. Reason: Guanine nucleotide binding is directly demonstrated and inseparable from the switch function. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0005525 GTP binding | IDA PMID:15601624 TIM, a Dbl-related protein, regulates cell shape and cytoske... | ACCEPT | Summary: RHOA binds GTP. Reason: Guanine nucleotide binding is directly demonstrated and inseparable from the switch function. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: RHOA binds GTP. Reason: Guanine nucleotide binding is directly demonstrated and inseparable from the switch function. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. |
| GO:0005634 nucleus | EXP PMID:12551911 Novel mechanism of the co-regulation of nuclear transport of... | KEEP AS NON CORE | Summary: A nuclear pool of RHOA is reported. Reason: RhoA accumulates in the nucleus in complex with SmgGDS, although the RhoA polybasic region itself has poor NLS activity; a minor pool relative to its membrane and cortical sites. Supporting Evidence: PMID:12551911 In contrast, the RhoA PBR has very poor NLS activity when it is fused to GFP or in the context of full-length RhoA. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: A nuclear pool of RHOA is reported. Reason: RhoA accumulates in the nucleus in complex with SmgGDS, although the RhoA polybasic region itself has poor NLS activity; a minor pool relative to its membrane and cortical sites. Supporting Evidence: PMID:12551911 In contrast, the RhoA PBR has very poor NLS activity when it is fused to GFP or in the context of full-length RhoA. |
| GO:0005737 cytoplasm | EXP PMID:23871831 A new mechanism of RhoA ubiquitination and degradation: role... | TOO GENERAL | Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, cytoplasmic side of plasma membrane, cell cortex and cleavage furrow locations asserted elsewhere in this review. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | TOO GENERAL | Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, cytoplasmic side of plasma membrane, cell cortex and cleavage furrow locations asserted elsewhere in this review. |
| GO:0005768 endosome | IMP PMID:19887681 Activation of a bacterial virulence protein by the GTPase Rh... | KEEP AS NON CORE | Summary: RHOA associates with endosomes. Reason: An endosomal pool is reported in the context of lipase regulation; peripheral to the plasma-membrane and cortical sites of action. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5625959 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at the ER membrane. Reason: Pathway-derived compartment assignment for a prenylated GTPase that can associate with cytoplasmic-face membranes; peripheral. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5672083 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at the ER membrane. Reason: Pathway-derived compartment assignment for a prenylated GTPase that can associate with cytoplasmic-face membranes; peripheral. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9013004 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at the ER membrane. Reason: Pathway-derived compartment assignment for a prenylated GTPase that can associate with cytoplasmic-face membranes; peripheral. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9013006 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at the ER membrane. Reason: Pathway-derived compartment assignment for a prenylated GTPase that can associate with cytoplasmic-face membranes; peripheral. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | IDA PMID:1328215 A rho gene product in human blood platelets. I. Identificati... | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3858495 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-442291 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-442314 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218826 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5228992 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5690843 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9012835 | ACCEPT | Summary: RHOA has a large RhoGDI-bound cytosolic pool. Reason: Prenylated RHOA is held soluble in the cytosol by RhoGDI and delivered to membranes on activation; the cytosolic pool is functionally significant. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | MODIFY | Summary: Generic cytoskeleton localization from the UniProt location mapping. Reason: RHOA is a regulator rather than a structural component of the cytoskeleton; its experimentally supported locations are the cell cortex and the cleavage furrow. Proposed replacements: cell cortex cleavage furrow Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436} |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Propagation Review Root cause: TERM SCOPING PROBLEM Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-114544 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-193646 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-193668 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-193696 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-194518 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202692 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928576 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928592 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928647 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928651 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416559 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416588 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-419049 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-419166 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5228992 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5623622 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5623632 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5623667 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5665982 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5665989 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5666197 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5666216 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5667008 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5671970 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5671993 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785648 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6798743 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6800426 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8849082 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8849085 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8980691 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8981637 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8985594 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9012761 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9012835 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9013006 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9013009 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-350485 | MODIFY | Summary: RHOA acts at the plasma membrane. Reason: Geranylgeranylation anchors RHOA to the plasma membrane, where it is activated by GEFs downstream of receptors. Note that it is on the cytoplasmic face and is not surface-exposed. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | KEEP AS NON CORE | Summary: RHOA detected in isolated focal adhesions. Reason: Consistent with its role in focal adhesion assembly; a peripheral location relative to the plasma membrane and cortex. |
| GO:0005938 cell cortex | IDA PMID:16103226 An ECT2-centralspindlin complex regulates the localization a... | ACCEPT | Summary: RHOA localizes to the cell cortex. Reason: Active RHOA concentrates at the cortex, including the equatorial cortex before furrow formation. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in an activated form |
| GO:0005938 cell cortex | IEA GO_REF:0000044 | ACCEPT | Summary: RHOA localizes to the cell cortex. Reason: Active RHOA concentrates at the cortex, including the equatorial cortex before furrow formation. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in an activated form |
| GO:0007266 Rho protein signal transduction | IBA GO_REF:0000033 | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | IDA PMID:21565175 ARHGAP30 is a Wrch-1-interacting protein involved in actin d... | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | IDA PMID:26529257 Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppr... | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | IEA GO_REF:0000107 | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | IMP PMID:23241886 Fam65b is a new transcriptional target of FOXO1 that regulat... | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | IMP PMID:31570889 Postzygotic inactivating mutations of RHOA cause a mosaic ne... | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | ISS GO_REF:0000024 | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0007266 Rho protein signal transduction | TAS PMID:10436159 Signaling from Rho to the actin cytoskeleton through protein... | ACCEPT | Summary: Rho-family signal transduction. Reason: The term names precisely the signalling module RHOA heads, supported by phylogenetic, experimental and curatorial evidence. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:1328215 A rho gene product in human blood platelets. I. Identificati... | ACCEPT | Summary: RHOA is on the cytoplasmic face of the plasma membrane. Reason: This is the precise location of the prenylated protein and the most informative membrane term for an intracellular GTPase. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. |
| GO:0010812 negative regulation of cell-substrate adhesion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA activity can reduce cell-substrate adhesion. Reason: Context-dependent adhesion outcome of actomyosin contractility; indirect. |
| GO:0010812 negative regulation of cell-substrate adhesion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA activity can reduce cell-substrate adhesion. Reason: Context-dependent adhesion outcome of actomyosin contractility; indirect. |
| GO:0016477 cell migration | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA is required for cell migration. Reason: RHOA-driven actomyosin contractility and adhesion turnover are required for cell movement; supported by several independent human loss-of-function studies. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt regulation of cell migration and adhesion assembly and disassembly |
| GO:0016477 cell migration | IDA PMID:26529257 Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppr... | ACCEPT | Summary: RHOA is required for cell migration. Reason: RHOA-driven actomyosin contractility and adhesion turnover are required for cell movement; supported by several independent human loss-of-function studies. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt regulation of cell migration and adhesion assembly and disassembly |
| GO:0016477 cell migration | IGI PMID:26188246 Cadherin-11 coordinates cellular migration and extracellular... | ACCEPT | Summary: RHOA is required for cell migration. Reason: RHOA-driven actomyosin contractility and adhesion turnover are required for cell movement; supported by several independent human loss-of-function studies. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt regulation of cell migration and adhesion assembly and disassembly |
| GO:0016477 cell migration | IMP PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: RHOA is required for cell migration. Reason: RHOA-driven actomyosin contractility and adhesion turnover are required for cell movement; supported by several independent human loss-of-function studies. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt regulation of cell migration and adhesion assembly and disassembly |
| GO:0017022 myosin binding | IPI PMID:15644318 BIG1 is a binding partner of myosin IXb and regulates its Rh... | ACCEPT | Summary: RHOA binds myosin and its regulatory machinery. Reason: Myosin binding reflects the direct coupling of RHOA to the contractile apparatus and is informative, unlike generic protein binding. |
| GO:0019901 protein kinase binding | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA binds effector protein kinases. Reason: GTP-RHOA binds ROCK1/2 and PKN kinases through their Rho-binding domains, the main route by which it delivers its signalling output. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt in active state binds to a variety of effector proteins to regulate cellular responses |
| GO:0021762 substantia nigra development | HEP PMID:22926577 Quantitative proteomic analysis of human substantia nigra in... | KEEP AS NON CORE | Summary: Expression-pattern-based association with substantia nigra development. Reason: HEP evidence reflects expression in the tissue, not a demonstrated role; retained as peripheral. |
| GO:0030027 lamellipodium | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: RHOA is present in lamellipodia. Reason: Transferred by similarity from rodent; RHOA activity is detected at protrusions although lamellipodium formation is primarily a RAC1 output. |
| GO:0030027 lamellipodium | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA is present in lamellipodia. Reason: Transferred by similarity from rodent; RHOA activity is detected at protrusions although lamellipodium formation is primarily a RAC1 output. |
| GO:0030036 actin cytoskeleton organization | IMP PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: RHOA organizes the actin cytoskeleton. Reason: The central cellular process of RHOA - stress fibre and contractile-ring assembly through ROCK and formin effectors. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Mainly associated with cytoskeleton organization |
| GO:0030036 actin cytoskeleton organization | TAS PMID:10436159 Signaling from Rho to the actin cytoskeleton through protein... | ACCEPT | Summary: RHOA organizes the actin cytoskeleton. Reason: The central cellular process of RHOA - stress fibre and contractile-ring assembly through ROCK and formin effectors. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Mainly associated with cytoskeleton organization |
| GO:0030054 cell junction | TAS Reactome:R-HSA-2160931 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030054 cell junction | TAS Reactome:R-HSA-2160932 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030054 cell junction | TAS Reactome:R-HSA-2160935 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030054 cell junction | TAS Reactome:R-NUL-2161147 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030054 cell junction | TAS Reactome:R-NUL-2161160 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030054 cell junction | TAS Reactome:R-NUL-2161165 | KEEP AS NON CORE | Summary: Reactome places RHOA reactions at cell junctions. Reason: Consistent with the directly supported apical junction complex localization; the generic cell junction term is less informative. |
| GO:0030334 regulation of cell migration | IMP PMID:19934221 The Rho-family GEF Asef2 activates Rac to modulate adhesion ... | ACCEPT | Summary: RHOA regulates cell migration. Reason: Loss-of-function experiments show RHOA sets migration rate and adhesion dynamics. |
| GO:0030335 positive regulation of cell migration | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Positive regulation of migration from automated rule-based annotation. Reason: RHOA can promote or inhibit migration depending on context; the signed term is context-specific and weakly evidenced here. |
| GO:0030425 dendrite | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: RHOA is present in dendrites. Reason: Neuronal compartment consistent with its postsynaptic actin role; transferred by similarity. |
| GO:0030496 midbody | IEA GO_REF:0000044 | ACCEPT | Summary: RHOA localizes to the midbody. Reason: Consistent with its role at the furrow and in abscission; recorded in UniProt as a location of the protein. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Midbody. |
| GO:0030667 secretory granule membrane | TAS Reactome:R-HSA-6798743 | KEEP AS NON CORE | Summary: Reactome places RHOA on secretory granule membranes. Reason: Granule-membrane association in leukocytes; secondary location. |
| GO:0031122 cytoplasmic microtubule organization | IMP PMID:31570889 Postzygotic inactivating mutations of RHOA cause a mosaic ne... | KEEP AS NON CORE | Summary: RHOA influences cytoplasmic microtubule organization. Reason: Through the MEMO1-RHOA-DIAPH1 axis RHOA stabilizes cortical microtubules; a real but effector-mediated, secondary process relative to actomyosin control. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt signaling pathway plays an important role in ERBB2 |
| GO:0031982 vesicle | IDA PMID:19887681 Activation of a bacterial virulence protein by the GTPase Rh... | KEEP AS NON CORE | Summary: RHOA detected on vesicles. Reason: Generic vesicular pool associated with its endosomal localization; peripheral. |
| GO:0032154 cleavage furrow | IDA PMID:16103226 An ECT2-centralspindlin complex regulates the localization a... | ACCEPT | Summary: RHOA localizes to the cleavage furrow. Reason: RHOA translocates to the equatorial region before furrow formation in an ECT2-dependent manner and is essential for furrow ingression. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. |
| GO:0032154 cleavage furrow | IEA GO_REF:0000044 | ACCEPT | Summary: RHOA localizes to the cleavage furrow. Reason: RHOA translocates to the equatorial region before furrow formation in an ECT2-dependent manner and is essential for furrow ingression. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. |
| GO:0032467 positive regulation of cytokinesis | IMP PMID:16103226 An ECT2-centralspindlin complex regulates the localization a... | ACCEPT | Summary: RHOA positively regulates cytokinesis. Reason: Loss-of-function experiments in human cells show RHOA is required for furrow formation and completion of cytokinesis. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Plays an essential role in cleavage furrow formation. |
| GO:0032467 positive regulation of cytokinesis | IMP PMID:17115030 The armadillo protein p0071 regulates Rho signalling during ... | ACCEPT | Summary: RHOA positively regulates cytokinesis. Reason: Loss-of-function experiments in human cells show RHOA is required for furrow formation and completion of cytokinesis. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Plays an essential role in cleavage furrow formation. |
| GO:0032587 ruffle membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ruffle membrane localization transferred electronically. Reason: Peripheral; ruffling is predominantly RAC1-driven, though RHOA activity is detected at protrusive membranes. |
| GO:0032956 regulation of actin cytoskeleton organization | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA regulates actin cytoskeleton organization. Reason: Conserved core process of the Rho clade, supported by phylogenetic inference and direct human experiments. |
| GO:0032956 regulation of actin cytoskeleton organization | IDA PMID:25911094 Odontogenic Ameloblast-associated Protein (ODAM) Mediates Ju... | ACCEPT | Summary: RHOA acts downstream of integrin-ODAM-ARHGEF5 to remodel actin. Reason: The pathway characterized here signals through ARHGEF5 to RhoA to control junctional epithelium attachment, a direct readout of RHOA-dependent actin regulation. Supporting Evidence: PMID:25911094 integrin-ODAM-ARHGEF5-RhoA signaling |
| GO:0032956 regulation of actin cytoskeleton organization | IEA GO_REF:0000107 | ACCEPT | Summary: RHOA regulates actin cytoskeleton organization. Reason: Conserved core process of the Rho clade, supported by phylogenetic inference and direct human experiments. |
| GO:0033688 regulation of osteoblast proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA regulates osteoblast proliferation in rodent. Reason: Cell-type-specific output transferred by sequence similarity. |
| GO:0033688 regulation of osteoblast proliferation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA regulates osteoblast proliferation in rodent. Reason: Cell-type-specific output transferred by sequence similarity. |
| GO:0034329 cell junction assembly | IMP PMID:22891260 Epithelial junction formation requires confinement of Cdc42 ... | ACCEPT | Summary: RHOA is required for cell junction assembly. Reason: RHOA is required for apical junction formation in keratinocytes and for epithelial junction assembly generally. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Required for the apical junction formation of keratinocyte cell-cell adhesion |
| GO:0034446 substrate adhesion-dependent cell spreading | IMP PMID:31570889 Postzygotic inactivating mutations of RHOA cause a mosaic ne... | ACCEPT | Summary: Inactivating RHOA mutations impair cell spreading. Reason: Postzygotic inactivating RHOA variants from patients were assayed in cells, where loss of RHOA function impairs spreading and stress-fibre formation. Supporting Evidence: PMID:31570889 Postzygotic inactivating mutations of RHOA cause a mosaic neuroectodermal syndrome |
| GO:0035385 Roundabout signaling pathway | IDA PMID:26529257 Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppr... | KEEP AS NON CORE | Summary: RHOA acts downstream of Robo receptors. Reason: A receptor-pathway context in which RHOA transduces guidance signals to the cytoskeleton. |
| GO:0036089 cleavage furrow formation | IDA PMID:16103226 An ECT2-centralspindlin complex regulates the localization a... | ACCEPT | Summary: RHOA drives cleavage furrow formation. Reason: Direct experimental evidence places activated RHOA at the equatorial cortex, where it specifies the furrow. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Plays an essential role in cleavage furrow formation. |
| GO:0038027 apolipoprotein A-I-mediated signaling pathway | IMP PMID:23726972 Apolipoprotein(a) acts as a chemorepellent to human vascular... | KEEP AS NON CORE | Summary: RHOA acts in apolipoprotein A-I-mediated signalling. Reason: A specific receptor-pathway context; downstream of the general signalling function. |
| GO:0042476 odontogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA contributes to tooth development in rodent. Reason: Tissue-specific developmental output transferred electronically. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IEP PMID:12761501 Large-scale identification and characterization of human gen... | KEEP AS NON CORE | Summary: RHOA activity promotes NF-kappaB signalling. Reason: Reported downstream regulatory effect in human cells; mediated by effector kinases rather than by RHOA acting in the cascade itself. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IMP PMID:25515214 Brain endothelial miR-146a negatively modulates T-cell adhes... | KEEP AS NON CORE | Summary: RHOA activity promotes NF-kappaB signalling. Reason: Reported downstream regulatory effect in human cells; mediated by effector kinases rather than by RHOA acting in the cascade itself. |
| GO:0043149 stress fiber assembly | IBA GO_REF:0000033 | ACCEPT | Summary: RHOA drives stress fibre assembly. Reason: The classical RHOA phenotype - ROCK- and formin-dependent assembly of contractile actin bundles, supported by phylogenetic inference and human experiments. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0043149 stress fiber assembly | IMP PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: RHOA drives stress fibre assembly. Reason: The classical RHOA phenotype - ROCK- and formin-dependent assembly of contractile actin bundles, supported by phylogenetic inference and human experiments. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0043149 stress fiber assembly | IMP PMID:31570889 Postzygotic inactivating mutations of RHOA cause a mosaic ne... | ACCEPT | Summary: RHOA drives stress fibre assembly. Reason: The classical RHOA phenotype - ROCK- and formin-dependent assembly of contractile actin bundles, supported by phylogenetic inference and human experiments. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0043197 dendritic spine | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: RHOA is present in dendritic spines. Reason: Consistent with its directly supported postsynaptic actin role; a neuronal compartment. |
| GO:0043296 apical junction complex | IDA PMID:20974804 The Rho target PRK2 regulates apical junction formation in h... | ACCEPT | Summary: RHOA localizes to the apical junction complex. Reason: Direct localization in epithelial cells, where RHOA is required for apical junction formation. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Required for the apical junction formation of keratinocyte cell-cell adhesion |
| GO:0043297 apical junction assembly | IEA GO_REF:0000107 | ACCEPT | Summary: RHOA is required for apical junction assembly. Reason: Loss-of-function in human keratinocytes prevents apical junction formation. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Required for the apical junction formation of keratinocyte cell-cell adhesion |
| GO:0043297 apical junction assembly | IMP PMID:20974804 The Rho target PRK2 regulates apical junction formation in h... | ACCEPT | Summary: RHOA is required for apical junction assembly. Reason: Loss-of-function in human keratinocytes prevents apical junction formation. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Required for the apical junction formation of keratinocyte cell-cell adhesion |
| GO:0043366 beta selection | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA is required for beta selection in thymocytes. Reason: Immune developmental output transferred from rodent. |
| GO:0043542 endothelial cell migration | IGI PMID:20208559 DLC2 modulates angiogenic responses in vascular endothelial ... | KEEP AS NON CORE | Summary: RHOA regulates endothelial cell migration. Reason: Cell-type-specific instance of the migration role, supported by genetic interaction data. |
| GO:0043931 ossification involved in bone maturation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA contributes to bone maturation in rodent. Reason: Tissue-level developmental output transferred by similarity. |
| GO:0043931 ossification involved in bone maturation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA contributes to bone maturation in rodent. Reason: Tissue-level developmental output transferred by similarity. |
| GO:0044319 wound healing, spreading of cells | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA contributes to cell spreading during wound healing. Reason: Organismal-level output of the spreading and migration functions. |
| GO:0044319 wound healing, spreading of cells | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA contributes to cell spreading during wound healing. Reason: Organismal-level output of the spreading and migration functions. |
| GO:0045198 establishment of epithelial cell apical/basal polarity | IMP PMID:22891260 Epithelial junction formation requires confinement of Cdc42 ... | KEEP AS NON CORE | Summary: RHOA establishes epithelial apical-basal polarity. Reason: Follows from junction assembly and cortical actin organization; supported by human loss-of-function but downstream of the core activity. |
| GO:0045666 positive regulation of neuron differentiation | IMP PMID:17488780 The Down syndrome critical region protein TTC3 inhibits neur... | KEEP AS NON CORE | Summary: RHOA promotes neuron differentiation. Reason: Cell-type-specific developmental output of cytoskeletal signalling. |
| GO:0045792 negative regulation of cell size | IMP PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G... | KEEP AS NON CORE | Summary: RHOA activity limits cell size. Reason: An indirect consequence of contractility; context-specific. |
| GO:0046638 positive regulation of alpha-beta T cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA promotes alpha-beta T cell differentiation in rodent. Reason: Immune developmental output transferred electronically. |
| GO:0050919 negative chemotaxis | IMP PMID:23726972 Apolipoprotein(a) acts as a chemorepellent to human vascular... | KEEP AS NON CORE | Summary: RHOA mediates repulsive (negative) chemotaxis. Reason: Directional responses to repellents are transduced through RHOA contractility; a context-specific output. |
| GO:0051496 positive regulation of stress fiber assembly | IDA PMID:15467718 Mammalian TOR complex 2 controls the actin cytoskeleton and ... | ACCEPT | Summary: RHOA positively regulates stress fibre assembly. Reason: Active RHOA is sufficient and necessary for stress fibre formation in human cells. |
| GO:0051496 positive regulation of stress fiber assembly | IMP PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G... | ACCEPT | Summary: RHOA positively regulates stress fibre assembly. Reason: Active RHOA is sufficient and necessary for stress fibre formation in human cells. |
| GO:0051893 regulation of focal adhesion assembly | TAS PMID:18981818 Interaction of microglia and amyloid-beta through beta2-inte... | ACCEPT | Summary: RHOA regulates focal adhesion assembly. Reason: RHOA couples receptor signals to focal adhesion assembly, as recorded in UniProt and reviewed in the cited reference. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers |
| GO:0060071 Wnt signaling pathway, planar cell polarity pathway | NAS PMID:24431302 Wnt signaling in midbrain dopaminergic neuron development an... | KEEP AS NON CORE | Summary: RHOA acts in the planar cell polarity branch of Wnt signalling. Reason: Rho GTPases operate downstream of Dishevelled in PCP; a pathway context for the core cytoskeletal function. |
| GO:0060193 positive regulation of lipase activity | IDA PMID:19887681 Activation of a bacterial virulence protein by the GTPase Rh... | KEEP AS NON CORE | Summary: RHOA activity increases lipase activity. Reason: A downstream regulatory effect on lipase-containing pathways, mediated by effectors. |
| GO:0060193 positive regulation of lipase activity | IMP PMID:22740689 A Salmonella typhimurium-translocated glycerophospholipid:ch... | KEEP AS NON CORE | Summary: RHOA activity increases lipase activity. Reason: A downstream regulatory effect on lipase-containing pathways, mediated by effectors. |
| GO:0061430 bone trabecula morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA contributes to bone trabecula morphogenesis. Reason: Tissue-level developmental output transferred by similarity. |
| GO:0061430 bone trabecula morphogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA contributes to bone trabecula morphogenesis. Reason: Tissue-level developmental output transferred by similarity. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: RHOA detected in exosome preparations. Reason: Common proteomic finding for abundant membrane-associated and cytosolic proteins; peripheral. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: RHOA detected in exosome preparations. Reason: Common proteomic finding for abundant membrane-associated and cytosolic proteins; peripheral. |
| GO:0070507 regulation of microtubule cytoskeleton organization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA regulates microtubule cytoskeleton organization. Reason: Through DIAPH1 and GSK3B-dependent control of APC and CLASP2, RHOA stabilizes cortical microtubules; an effector-mediated secondary process. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. |
| GO:0071222 cellular response to lipopolysaccharide | IDA PMID:19734146 Speckled-like pattern in the germinal center (SLIP-GC), a nu... | KEEP AS NON CORE | Summary: RHOA is activated in the cellular response to LPS. Reason: A stimulus context in which RHOA transduces signals, not a distinct activity. |
| GO:0071345 cellular response to cytokine stimulus | IMP PMID:25515214 Brain endothelial miR-146a negatively modulates T-cell adhes... | KEEP AS NON CORE | Summary: RHOA acts in cellular responses to cytokines. Reason: Receptor-pathway context for the cytoskeletal function. |
| GO:0071526 semaphorin-plexin signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RHOA acts downstream of plexins in semaphorin signalling. Reason: Plexins regulate Rho-family GTPases; a receptor-pathway context. |
| GO:0071526 semaphorin-plexin signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA acts downstream of plexins in semaphorin signalling. Reason: Plexins regulate Rho-family GTPases; a receptor-pathway context. |
| GO:0071902 positive regulation of protein serine/threonine kinase activity | IDA PMID:8617235 The small GTP-binding protein Rho binds to and activates a 1... | ACCEPT | Summary: RHOA activates effector serine/threonine kinases. Reason: GTP-RHOA binding activates ROCK and PKN kinases directly, which is the mechanism of its downstream signalling. |
| GO:0071944 cell periphery | IMP PMID:25911094 Odontogenic Ameloblast-associated Protein (ODAM) Mediates Ju... | TOO GENERAL | Summary: Cell periphery localization. Reason: True but entailed by the cytoplasmic side of plasma membrane and cell cortex locations asserted in this review. |
| GO:0090051 negative regulation of cell migration involved in sprouting angiogenesis | IGI PMID:20208559 DLC2 modulates angiogenic responses in vascular endothelial ... | KEEP AS NON CORE | Summary: RHOA restrains tip-cell migration during sprouting angiogenesis. Reason: Tissue-specific, context-dependent migratory output. |
| GO:0090307 mitotic spindle assembly | IMP PMID:19635168 Regulation of mitotic spindle formation by the RhoA guanine ... | KEEP AS NON CORE | Summary: RHOA contributes to mitotic spindle assembly. Reason: Reported requirement in human cells, probably through cortical and microtubule effects; secondary to its furrow role. |
| GO:0090324 negative regulation of oxidative phosphorylation | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Negative regulation of oxidative phosphorylation transferred electronically. Reason: No mechanism links RHOA to the respiratory chain; the annotation exceeds the evidence. |
| GO:0097498 endothelial tube lumen extension | IGI PMID:20208559 DLC2 modulates angiogenic responses in vascular endothelial ... | KEEP AS NON CORE | Summary: RHOA participates in endothelial tube lumen extension. Reason: Tissue-specific morphogenetic output of cytoskeletal control. |
| GO:0098794 postsynapse | IDA PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0098794 postsynapse | IDA PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera... | ACCEPT | Summary: RHOA activity is measured and manipulated at synapses in neurons. Reason: FRET-based RAICHU probes report RhoA activity in neurons, and its regulator Rich2 modulates that activity at postsynaptic sites; the curator assessed the full text. Supporting Evidence: PMID:24352656 The pRAICHU probes for Cdc42, RhoA, and Rac1 were generously provided by M. |
| GO:0098794 postsynapse | IMP PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0098794 postsynapse | IMP PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera... | ACCEPT | Summary: RHOA activity is measured and manipulated at synapses in neurons. Reason: FRET-based RAICHU probes report RhoA activity in neurons, and its regulator Rich2 modulates that activity at postsynaptic sites; the curator assessed the full text. Supporting Evidence: PMID:24352656 The pRAICHU probes for Cdc42, RhoA, and Rac1 were generously provided by M. |
| GO:0098978 glutamatergic synapse | IDA PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0098978 glutamatergic synapse | IDA PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera... | ACCEPT | Summary: RHOA activity is measured and manipulated at synapses in neurons. Reason: FRET-based RAICHU probes report RhoA activity in neurons, and its regulator Rich2 modulates that activity at postsynaptic sites; the curator assessed the full text. Supporting Evidence: PMID:24352656 The pRAICHU probes for Cdc42, RhoA, and Rac1 were generously provided by M. |
| GO:0098978 glutamatergic synapse | IMP PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0098978 glutamatergic synapse | IMP PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera... | ACCEPT | Summary: RHOA activity is measured and manipulated at synapses in neurons. Reason: FRET-based RAICHU probes report RhoA activity in neurons, and its regulator Rich2 modulates that activity at postsynaptic sites; the curator assessed the full text. Supporting Evidence: PMID:24352656 The pRAICHU probes for Cdc42, RhoA, and Rac1 were generously provided by M. |
| GO:0099159 regulation of modification of postsynaptic structure | IDA PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0099159 regulation of modification of postsynaptic structure | IMP PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:0101003 ficolin-1-rich granule membrane | TAS Reactome:R-HSA-6800426 | KEEP AS NON CORE | Summary: Reactome places RHOA on ficolin-1-rich granule membranes. Reason: Neutrophil granule membrane association; secondary location. |
| GO:1901224 positive regulation of non-canonical NF-kappaB signal transduction | NAS PMID:12761501 Large-scale identification and characterization of human gen... | KEEP AS NON CORE | Summary: RHOA promotes non-canonical NF-kappaB signalling. Reason: Author-stated downstream regulatory effect; indirect. |
| GO:1902766 skeletal muscle satellite cell migration | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA is required for satellite cell migration. Reason: Cell-type-specific migratory output transferred by similarity. |
| GO:1902766 skeletal muscle satellite cell migration | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: RHOA is required for satellite cell migration. Reason: Cell-type-specific migratory output transferred by similarity. |
| GO:1903427 negative regulation of reactive oxygen species biosynthetic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Negative regulation of ROS biosynthesis transferred electronically. Reason: Indirect at best and not mechanistically linked to RHOA activity in human cells. |
| GO:1903673 mitotic cleavage furrow formation | IMP PMID:16103226 An ECT2-centralspindlin complex regulates the localization a... | ACCEPT | Summary: RHOA is required for mitotic cleavage furrow formation. Reason: Direct loss-of-function evidence in human cells; the most specific form of the furrow role. Supporting Evidence: file:human/RHOA/RHOA-uniprot.txt Plays an essential role in cleavage furrow formation. |
| GO:1904996 positive regulation of leukocyte adhesion to vascular endothelial cell | IMP PMID:25515214 Brain endothelial miR-146a negatively modulates T-cell adhes... | KEEP AS NON CORE | Summary: RHOA promotes leukocyte adhesion to endothelium. Reason: Adhesion output in a specific immune context; downstream of contractility and integrin regulation. |
| GO:1905274 regulation of modification of postsynaptic actin cytoskeleton | IDA PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:1905274 regulation of modification of postsynaptic actin cytoskeleton | IMP PMID:21423166 Local, persistent activation of Rho GTPases during plasticit... | ACCEPT | Summary: RHOA is locally activated in single dendritic spines during plasticity. Reason: FRET sensor imaging shows persistent, spine-local RhoA activation accompanying structural plasticity of individual spines on glutamatergic neurons, placing RHOA activity at the postsynapse and linking it to remodelling of postsynaptic structure. Supporting Evidence: PMID:21423166 Local, persistent activation of Rho GTPases during plasticity of single dendritic spines |
| GO:1990869 cellular response to chemokine | IMP PMID:23241886 Fam65b is a new transcriptional target of FOXO1 that regulat... | KEEP AS NON CORE | Summary: RHOA mediates cellular responses to chemokines. Reason: Receptor-pathway context for migration control. |
| GO:2000406 positive regulation of T cell migration | IMP PMID:23241886 Fam65b is a new transcriptional target of FOXO1 that regulat... | KEEP AS NON CORE | Summary: RHOA promotes T cell migration. Reason: Cell-type-specific migratory output supported by human loss-of-function data. |
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Download this section (compressed HTML)Q: What determines whether RHOA activation produces stress fibres, a cleavage furrow or a junctional actin belt - the GEF that loads it, the effector available, or the membrane microdomain in which it is activated?
Q: How do the recurrent RHOA mutations in diffuse gastric cancer (Y42C, G17V in lymphoma) change effector selection rather than simply switching the protein on or off?
Q: How are the RHOA and RAC1 activity zones kept spatially separate in a migrating cell, and which GAPs and GEFs enforce that separation?
Experiment: Biosensor imaging of RHOA activity combined with acute, localized optogenetic activation in human epithelial cells, to test whether the same activity level produces junctional versus stress-fibre outputs depending on where it is generated.
Experiment: Effector-selective RHOA mutants (separating ROCK, DIAPH1 and PKN binding) expressed in RHOA-null human cells, scored for stress fibres, furrow formation, junction assembly and postsynaptic spine morphology.
Experiment: Comparative analysis of cancer-derived RHOA variants in isogenic cells, measuring nucleotide cycling, GEF/GAP responsiveness and effector binding, to connect genotype to the cytoskeletal phenotype.
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