RAC1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000242 pericentriolar material	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Pericentriolar material localization transferred electronically from rodent. Reason: RAC1 is a prenylated membrane- and cytosol-associated GTPase; a pericentriolar pool is not established for the human protein and is not where its characterized activities occur.
GO:0001764 neuron migration	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 is required for neuronal migration in rodent brain. Reason: Neuronal migration is a tissue-level output of the general RAC1 actin/migration machinery rather than a separate core activity.
GO:0001764 neuron migration	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: RAC1 is required for neuronal migration in rodent brain. Reason: Neuronal migration is a tissue-level output of the general RAC1 actin/migration machinery rather than a separate core activity.
GO:0001891 phagocytic cup	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 acts at the phagocytic cup. Reason: RAC1 drives actin remodelling during engulfment, so a phagocytic-cup pool is expected; a specialized plasma-membrane subdomain, non-core relative to the general membrane location.
GO:0001934 positive regulation of protein phosphorylation	IMP PMID:23633677 β-arrestin-dependent activation of the cofilin pathway is re...	KEEP AS NON CORE	Summary: RAC1 activity leads to phosphorylation of downstream effectors. Reason: Increased phosphorylation (for example of PAK substrates and cofilin) is a downstream consequence of effector activation by GTP-RAC1, not a step RAC1 catalyses.
GO:0003376 sphingosine-1-phosphate receptor signaling pathway	IMP PMID:18558630 Overlapping and distinct roles for PI3Kbeta and gamma isofor...	KEEP AS NON CORE	Summary: RAC1 acts downstream of S1P receptors in endothelial cells. Reason: RAC1 transmits signals from S1P receptors to the actin machinery; a receptor-pathway context for its general effector function.
GO:0003924 GTPase activity	EXP PMID:21565175 ARHGAP30 is a Wrch-1-interacting protein involved in actin d...	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	IDA PMID:19787194 Role of Kenae/CCDC125 in cell motility through the deregulat...	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	IDA PMID:27917469 Association of dysfunctional synapse defective 1 (SYDE1) wit...	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	IEA GO_REF:0000120	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	TAS PMID:2674130 rac, a novel ras-related family of proteins that are botulin...	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003924 GTPase activity	TAS PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	ACCEPT	Summary: RAC1 hydrolyses GTP. Reason: Intrinsic and GAP-stimulated GTP hydrolysis is the defining catalytic activity of RAC1 and underlies its switch behaviour; UniProt records EC 3.6.5.2 with experimental evidence. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Reaction=GTP + H2O = GDP + phosphate + H(+) file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0003925 G protein activity	IEA GO_REF:0000120	ACCEPT	Summary: RAC1 is a nucleotide-dependent molecular switch. Reason: G protein activity covers monomeric small GTPases; RAC1 transduces signals by switching between GTP- and GDP-bound conformations and engaging effectors only in the GTP state. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In its active state, binds to a variety of effector proteins to regulate cellular responses
GO:0003925 G protein activity	ISS PMID:17448994 EphA-Ephrin-A-mediated beta cell communication regulates ins...	ACCEPT	Summary: RAC1 is a nucleotide-dependent molecular switch. Reason: G protein activity covers monomeric small GTPases; RAC1 transduces signals by switching between GTP- and GDP-bound conformations and engaging effectors only in the GTP state. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In its 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 very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11030651 Localized Rac activation dynamics visualized in living cells...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11084340 Synaptojanin 2, a novel Rac1 effector that regulates clathri...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11260256 Human homologues of the Caenorhabditis elegans cell polarity...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11260256 Human homologues of the Caenorhabditis elegans cell polarity...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11260256 Human homologues of the Caenorhabditis elegans cell polarity...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11260256 Human homologues of the Caenorhabditis elegans cell polarity...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11346801 The structural basis of Arfaptin-mediated cross-talk between...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11513578 Crystal structure of the Rac1-RhoGDI complex involved in nad...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11696321 Cdc42 induces filopodia by promoting the formation of an IRS...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:11807099 The integrin cytoplasmic domain-associated protein ICAP-1 bi...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12134158 Unconventional Rac-GEF activity is mediated through the Dock...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12134158 Unconventional Rac-GEF activity is mediated through the Dock...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12874273 The C-terminal domain of Rac1 contains two motifs that contr...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12879077 RhoG activates Rac1 by direct interaction with the Dock180-b...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12915445 Lowe syndrome protein OCRL1 interacts with Rac GTPase in the...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:12919680 The mammalian passenger protein TD-60 is an RCC1 family memb...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:15048733 CYFIP2 is highly abundant in CD4+ cells from multiple sclero...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:15247908 PH domain of ELMO functions in trans to regulate Rac activat...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:15723800 A Steric-inhibition model for regulation of nucleotide excha...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:15723800 A Steric-inhibition model for regulation of nucleotide excha...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:16492808 Targeting and activation of Rac1 are mediated by the exchang...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:16492808 Targeting and activation of Rac1 are mediated by the exchang...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:16628218 Phospholipase Cgamma/diacylglycerol-dependent activation of ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Ra...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:16968699 Role of RacC for the regulation of WASP and phosphatidylinos...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:17003044 The RAC binding domain/IRSp53-MIM homology domain of IRSp53 ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:17145773 Asef2 functions as a Cdc42 exchange factor and is stimulated...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:17245428 Rac1-induced cell migration requires membrane recruitment of...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:17245428 Rac1-induced cell migration requires membrane recruitment of...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:17245428 Rac1-induced cell migration requires membrane recruitment of...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:18511940 Crucial structural role for the PH and C1 domains of the Vav...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:18809683 Actin pedestal formation by enteropathogenic Escherichia col...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19171758 Kank attenuates actin remodeling by preventing interaction b...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19264842 PLC-gamma1 and Rac1 coregulate EGF-induced cytoskeleton remo...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19264842 PLC-gamma1 and Rac1 coregulate EGF-induced cytoskeleton remo...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19270716 ISG15 modification of filamin B negatively regulates the typ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19270716 ISG15 modification of filamin B negatively regulates the typ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19403692 BPAG1e maintains keratinocyte polarity through beta4 integri...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19596003 Adiponectin promotes migration activities of endothelial pro...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19732720 14-3-3zeta Cooperates with ErbB2 to promote ductal carcinoma...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:19843518 Structure and function of the intracellular region of the pl...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20148946 The SWI/SNF protein BAF60b is ubiquitinated through a signal...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20660631 Type I PIPK-alpha regulates directed cell migration by modul...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20679435 Ephexin4 and EphA2 mediate cell migration through a RhoG-dep...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20696164 POSH2 is a RING finger E3 ligase with Rac1 binding activity ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20696164 POSH2 is a RING finger E3 ligase with Rac1 binding activity ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20696164 POSH2 is a RING finger E3 ligase with Rac1 binding activity ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20810653 srGAP2 arginine methylation regulates cell migration and cel...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20875796 Abba promotes PDGF-mediated membrane ruffling through activa...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20936779 A human MAP kinase interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20936779 A human MAP kinase interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20936779 A human MAP kinase interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20936779 A human MAP kinase interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:20974804 The Rho target PRK2 regulates apical junction formation in h...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21029865 EphB-mediated degradation of the RhoA GEF Ephexin5 relieves ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21167153 Invasion of breast cancer cells into collagen matrix require...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21454543 Rac1 protein rescues neurite retraction caused by G2019S leu...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21454543 Rac1 protein rescues neurite retraction caused by G2019S leu...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21900206 A directed protein interaction network for investigating int...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:21988832 Toward an understanding of the protein interaction network o...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22036506 The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation o...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22117219 IAPs regulate the plasticity of cell migration by directly t...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22117219 IAPs regulate the plasticity of cell migration by directly t...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22117219 IAPs regulate the plasticity of cell migration by directly t...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22157745 A palmitoylation switch mechanism regulates Rac1 function an...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22581261 DOCK8 functions as an adaptor that links TLR-MyD88 signaling...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22614015 The tumour suppressor HACE1 controls cell migration by regul...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22614015 The tumour suppressor HACE1 controls cell migration by regul...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22705156 WNT-3a modulates platelet function by regulating small GTPas...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:22796473 Desmoglein 3 acting as an upstream regulator of Rho GTPases,...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:23109420 Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the d...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:23109420 Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the d...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:23195690 Cytoplasmic targeting of the proto-oncogene SET promotes cel...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:23209303 The novel synaptogenic protein Farp1 links postsynaptic cyto...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:23982733 IQGAP1 is a novel phosphatidylinositol 4,5 bisphosphate effe...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24086303 The human minor histocompatibility antigen 1 is a RhoGAP.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24172987 A small GTPase‑like protein fragment of Mycoplasma promotes ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24172987 A small GTPase‑like protein fragment of Mycoplasma promotes ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24274578 Human tumor necrosis factor (TNF)-alpha-induced protein 8-li...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24792722 Nox1 activation by βPix and the role of Ser-340 phosphorylat...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:24792722 Nox1 activation by βPix and the role of Ser-340 phosphorylat...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:25843002 Cancer cell-autonomous TRAIL-R signaling promotes KRAS-drive...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:26175416 DNA-PKcs-Mediated Transcriptional Regulation Drives Prostate...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:28007913 Vascular Endothelial Growth Factor (VEGF) Promotes Assembly ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:29734338 RIT1 controls actin dynamics via complex formation with RAC1...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:30250061 Fam49/CYRI interacts with Rac1 and locally suppresses protru...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31285585 CYRI/FAM49B negatively regulates RAC1-driven cytoskeletal re...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31871319 Mapping the proximity interaction network of the Rho-family ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:38833990 Incarvine C and its analogues inhibit the formation of cell ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:7673236 Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:8670882 Identification of a novel Rac1-interacting protein involved ...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005515 protein binding	IPI PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	REMOVE	Summary: Generic protein binding from a very large number of interaction studies. Reason: GO:0005515 is uninformative and is removed under the project protein-binding policy. Removal does not dispute the many documented RAC1 interactions; the informative ones are represented by GTP-dependent protein binding, protein kinase binding, RhoGDI binding and the process annotations they support.
GO:0005525 GTP binding	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IDA PMID:12551911 Novel mechanism of the co-regulation of nuclear transport of...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IDA PMID:15467718 Mammalian TOR complex 2 controls the actin cytoskeleton and ...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IDA PMID:15601624 TIM, a Dbl-related protein, regulates cell shape and cytoske...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IDA PMID:22036506 The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation o...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IDA PMID:23620790 CBAP functions as a novel component in chemokine-induced ZAP...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IEA GO_REF:0000120	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005525 GTP binding	IMP PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	ACCEPT	Summary: RAC1 binds GTP. Reason: Guanine nucleotide binding is directly demonstrated in multiple studies and is inseparable from the switch function of the protein. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt small GTPase which cycles between active GTP-bound and inactive GDP-bound states
GO:0005634 nucleus	IDA PMID:12551911 Novel mechanism of the co-regulation of nuclear transport of...	KEEP AS NON CORE	Summary: The RAC1 polybasic region has nuclear-localization activity. Reason: Rac1 accumulates in the nucleus with SmgGDS, driven by its C-terminal polybasic region; a genuine but minor pool compared with its membrane and cytosolic sites of action. Supporting Evidence: PMID:12551911 We show that the Rac1 PBR has significant NLS activity when it is fused to green fluorescent protein (GFP) or in the context of full-length Rac1.
GO:0005634 nucleus	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The RAC1 polybasic region has nuclear-localization activity. Reason: Rac1 accumulates in the nucleus with SmgGDS, driven by its C-terminal polybasic region; a genuine but minor pool compared with its membrane and cytosolic sites of action. Supporting Evidence: PMID:12551911 We show that the Rac1 PBR has significant NLS activity when it is fused to green fluorescent protein (GFP) or in the context of full-length Rac1.
GO:0005654 nucleoplasm	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: Nucleoplasmic signal in immunofluorescence screening. Reason: Consistent with the documented nuclear pool; peripheral to RAC1 function.
GO:0005730 nucleolus	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: Nucleolar signal in immunofluorescence screening. Reason: Reported by antibody-based imaging only; no functional role for RAC1 in the nucleolus is established, so this is retained as a peripheral localization.
GO:0005737 cytoplasm	EXP PMID:19948726 Activated Rac1 GTPase translocates protein phosphatase 5 to ...	TOO GENERAL	Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, plasma membrane (cytoplasmic side), lamellipodium and cell cortex locations asserted elsewhere in this review. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005737 cytoplasm	EXP PMID:29074776 N(ε)-Fatty acylation of Rho GTPases by a MARTX toxin effecto...	TOO GENERAL	Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, plasma membrane (cytoplasmic side), lamellipodium and cell cortex locations asserted elsewhere in this review. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005737 cytoplasm	IDA PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	TOO GENERAL	Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, plasma membrane (cytoplasmic side), lamellipodium and cell cortex locations asserted elsewhere in this review. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005737 cytoplasm	IEA GO_REF:0000120	TOO GENERAL	Summary: Cytoplasmic localization. Reason: True, but entailed by the more specific cytosol, plasma membrane (cytoplasmic side), lamellipodium and cell cortex locations asserted elsewhere in this review. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-5625959	KEEP AS NON CORE	Summary: Reactome places RAC1 reactions at the ER membrane. Reason: Pathway-derived compartment assignments for a prenylated GTPase that can associate with several cytoplasmic-face membranes; peripheral to its plasma-membrane site of action.
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-5672083	KEEP AS NON CORE	Summary: Reactome places RAC1 reactions at the ER membrane. Reason: Pathway-derived compartment assignments for a prenylated GTPase that can associate with several cytoplasmic-face membranes; peripheral to its plasma-membrane site of action.
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-9691168	KEEP AS NON CORE	Summary: Reactome places RAC1 reactions at the ER membrane. Reason: Pathway-derived compartment assignments for a prenylated GTPase that can associate with several cytoplasmic-face membranes; peripheral to its plasma-membrane site of action.
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-9691174	KEEP AS NON CORE	Summary: Reactome places RAC1 reactions at the ER membrane. Reason: Pathway-derived compartment assignments for a prenylated GTPase that can associate with several cytoplasmic-face membranes; peripheral to its plasma-membrane site of action.
GO:0005802 trans-Golgi network	IDA PMID:12915445 Lowe syndrome protein OCRL1 interacts with Rac GTPase in the...	KEEP AS NON CORE	Summary: RAC1 detected at the trans-Golgi network. Reason: A membrane-trafficking pool consistent with prenylated GTPase cycling; not the main site of RAC1 signalling.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	ISS GO_REF:0000024	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-1011598	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-1433415	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-200952	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-2424476	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-2730840	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-3858475	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-389348	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-3928628	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-3928642	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-4093336	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-418856	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-442273	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-442314	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-445064	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-5665809	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005829 cytosol	TAS Reactome:R-HSA-9013147	ACCEPT	Summary: RAC1 has a substantial cytosolic pool held by RhoGDI. Reason: Inactive, prenyl-shielded RAC1 resides in the cytosol in complex with RhoGDI and is delivered to the membrane on activation; the cytosolic pool is functionally important. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0005856 cytoskeleton	IBA GO_REF:0000033	MODIFY	Summary: Generic cytoskeleton localization inferred phylogenetically. Reason: The PAINT node correctly places Rac GTPases at actin structures, but cytoskeleton is less precise than the cortical and lamellipodial locations this gene carries with direct evidence, and RAC1 is a regulator of rather than a structural part of the cytoskeleton. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001530052 SUPPORTS TRANSFER The ancestral Rac node legitimately acts on the actin cytoskeleton, so the node assertion is sound; only the granularity of the location term is at issue. Proposed replacements: cell cortex lamellipodium
GO:0005884 actin filament	IDA PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	KEEP AS NON CORE	Summary: RAC1 associates with actin filament structures. Reason: Consistent with its cortical actin function; the informative locations are lamellipodium, ruffle membrane and cell cortex.
GO:0005886 plasma membrane	EXP PMID:1643658 The small GTP-binding protein rac regulates growth factor-in...	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	EXP PMID:22843693 Tetraspanin CD151 stimulates adhesion-dependent activation o...	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	EXP PMID:29074776 N(ε)-Fatty acylation of Rho GTPases by a MARTX toxin effecto...	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	IBA GO_REF:0000033	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	IDA PMID:10036235 ARF6 requirement for Rac ruffling suggests a role for membra...	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	IEA GO_REF:0000120	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	NAS PMID:27048830 CYBA encoding p22(phox), the cytochrome b558 alpha polypepti...	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-114542	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-1433415	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029451	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029454	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029456	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029465	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029466	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029467	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2029469	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-205039	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2130194	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2197690	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2316434	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2400009	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2424476	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2730840	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2730856	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-2730889	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-389348	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-389788	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928612	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928619	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928620	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928625	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928628	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928633	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928640	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928641	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-3928642	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-399930	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-399939	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-399952	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-400682	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-4093336	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-418856	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-445064	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-445072	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5218827	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5218839	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5218841	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5218850	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5357445	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5357472	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5357483	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5626469	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5626507	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5626549	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5627775	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5665802	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5665809	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5668714	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5668718	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5668731	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5668735	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5671970	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5671993	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5672329	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-6798743	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-6800426	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-8848618	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-8875591	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-8951586	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-8981926	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-8981931	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9013143	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9013144	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9013145	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9013147	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9032798	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9666428	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9666430	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9673284	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9673288	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9673794	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9673797	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9691168	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9751201	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9958873	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-HSA-9970163	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005886 plasma membrane	TAS Reactome:R-NUL-350365	MODIFY	Summary: RAC1 acts on the cytoplasmic face of the plasma membrane. Reason: C-terminal geranylgeranylation anchors RAC1 to the inner leaflet of the plasma membrane, where it is activated and engages effectors. This is its principal site of action; note that it is an intracellular, peripheral membrane protein and is not exposed on the cell surface. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- 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/RAC1/RAC1-uniprot.txt SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:1643658, ECO:0000269\|PubMed:22843693, ECO:0000269\|PubMed:29074776}; Lipid-anchor file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0005925 focal adhesion	HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome...	KEEP AS NON CORE	Summary: RAC1 detected in isolated focal adhesions. Reason: Consistent with its role in adhesion and spreading; a peripheral location relative to the plasma membrane and lamellipodium.
GO:0005938 cell cortex	IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri...	ACCEPT	Summary: RAC1 localizes to the actin-rich cortex during spreading and random migration. Reason: TIRF imaging of spreading and randomly migrating cells follows the cortical signalling and protrusion dynamics in which Rac1 activity is engaged. Supporting Evidence: PMID:19126672 3'-phosphoinositides are enriched in a localized and dynamic fashion during active spreading and random migration of mouse fibroblasts on adhesive surfaces
GO:0005938 cell cortex	ISS PMID:17448994 EphA-Ephrin-A-mediated beta cell communication regulates ins...	ACCEPT	Summary: RAC1 localizes to the cell cortex. Reason: Direct imaging places RAC1 at the actin-rich cortex, where it nucleates protrusive structures.
GO:0006911 phagocytosis, engulfment	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 drives actin remodelling during engulfment. Reason: Phagocytic engulfment is a cell-type-specific output of the core actin-regulatory function.
GO:0006954 inflammatory response	TAS PMID:9572733 Role of Rac1 and oxygen radicals in collagenase-1 expression...	KEEP AS NON CORE	Summary: RAC1 contributes to inflammatory responses. Reason: Inflammation is a high-level organismal process downstream of RAC1-dependent leukocyte migration and oxidase activation.
GO:0007015 actin filament organization	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 organizes actin filaments. Reason: Activation of the WAVE/Arp2/3 machinery by GTP-RAC1 produces branched actin networks; this is the central cellular process in which RAC1 participates, supported both by the PAINT node and by direct human experiments. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Required for DSG3 translocation to cell-cell junctions, DSG3-mediated organization of cortical F-actin bundles and anchoring of actin at cell junctions
GO:0007015 actin filament organization	IMP PMID:22796473 Desmoglein 3 acting as an upstream regulator of Rho GTPases,...	ACCEPT	Summary: RAC1 organizes actin filaments. Reason: Activation of the WAVE/Arp2/3 machinery by GTP-RAC1 produces branched actin networks; this is the central cellular process in which RAC1 participates, supported both by the PAINT node and by direct human experiments. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Required for DSG3 translocation to cell-cell junctions, DSG3-mediated organization of cortical F-actin bundles and anchoring of actin at cell junctions
GO:0007155 cell adhesion	TAS PMID:9572733 Role of Rac1 and oxygen radicals in collagenase-1 expression...	KEEP AS NON CORE	Summary: RAC1 participates in cell adhesion. Reason: Adhesion assembly and disassembly depend on RAC1-driven actin remodelling; a general, downstream process.
GO:0007160 cell-matrix adhesion	IGI PMID:20926685 The roles of two distinct regions of PINCH-1 in the regulati...	KEEP AS NON CORE	Summary: RAC1 regulates integrin-mediated adhesion to matrix. Reason: Supported by genetic interaction data; a downstream adhesion output of RAC1 actin signalling.
GO:0007160 cell-matrix adhesion	NAS PMID:18156211 Regulation of endothelial cell cytoskeletal reorganization b...	KEEP AS NON CORE	Summary: RAC1 regulates integrin-mediated adhesion to matrix. Reason: Supported by genetic interaction data; a downstream adhesion output of RAC1 actin signalling.
GO:0007163 establishment or maintenance of cell polarity	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: RAC1 establishes and maintains cell polarity. Reason: Polarity (for example epithelial polarization and front-rear polarity in migration) is a conserved output of RAC1 signalling. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt epithelial cell polarization
GO:0007167 enzyme-linked receptor protein signaling pathway	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 acts downstream of growth-factor receptors. Reason: Growth-factor-induced ruffling places RAC1 in receptor-initiated cascades; a context rather than a distinct activity. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt growth-factor induced formation of membrane ruffles
GO:0007264 small GTPase-mediated signal transduction	IMP PMID:26934001 MicroRNA-92b represses invasion-metastasis cascade of esopha...	ACCEPT	Summary: RAC1 activation transmits integrin signals to the motility machinery. Reason: Perturbation of upstream integrin signalling reduces Rac1 activation and motility, confirming RAC1 as the signal-transducing switch in this cascade. Supporting Evidence: PMID:26934001 reduced activation of Rac1, both of which were essential mediators of cellular motility in ESCC cells
GO:0008045 motor neuron axon guidance	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Motor neuron axon guidance inferred phylogenetically. Reason: Rac GTPases act in growth-cone actin dynamics across species; a neuronal-context output of the core actin function.
GO:0008360 regulation of cell shape	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: RAC1 regulates cell shape. Reason: Cell shape follows from cortical actin remodelling driven by RAC1; general and downstream.
GO:0009611 response to wounding	TAS PMID:9572733 Role of Rac1 and oxygen radicals in collagenase-1 expression...	KEEP AS NON CORE	Summary: RAC1 participates in wound responses. Reason: Wound healing depends on RAC1-driven migration; an organismal-level output.
GO:0009653 anatomical structure morphogenesis	TAS PMID:9572733 Role of Rac1 and oxygen radicals in collagenase-1 expression...	KEEP AS NON CORE	Summary: RAC1 contributes broadly to morphogenesis. Reason: Very general developmental term downstream of the actin and polarity functions.
GO:0010310 regulation of hydrogen peroxide metabolic process	TAS PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Ra...	KEEP AS NON CORE	Summary: RAC1 regulates production of reactive oxygen species by NADPH oxidases. Reason: By activating Nox1 and NOX2 complexes RAC1 sets cellular hydrogen peroxide levels; a downstream metabolic consequence of its oxidase subunit role. Supporting Evidence: PMID:16636067 Rac1 has been implicated in the generation of reactive oxygen species (ROS)
GO:0010591 regulation of lamellipodium assembly	IGI PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	ACCEPT	Summary: RAC1 regulates lamellipodium assembly. Reason: RAC1 is the canonical driver of lamellipodium formation through WAVE/Arp2/3-dependent branched actin polymerization.
GO:0010592 positive regulation of lamellipodium assembly	IDA PMID:15467718 Mammalian TOR complex 2 controls the actin cytoskeleton and ...	ACCEPT	Summary: RAC1 positively regulates lamellipodium assembly. Reason: Dominant-negative and loss-of-function experiments in human cells, including neutrophils, show that active RAC1 is required for lamellipodium formation. Supporting Evidence: PMID:19625648 Rac1 and Rac2, members of the small Rho GTPase family, play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants.
GO:0010592 positive regulation of lamellipodium assembly	IMP PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	ACCEPT	Summary: RAC1 positively regulates lamellipodium assembly. Reason: Dominant-negative and loss-of-function experiments in human cells, including neutrophils, show that active RAC1 is required for lamellipodium formation. Supporting Evidence: PMID:19625648 Rac1 and Rac2, members of the small Rho GTPase family, play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants.
GO:0010592 positive regulation of lamellipodium assembly	IMP PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	ACCEPT	Summary: RAC1 positively regulates lamellipodium assembly. Reason: Dominant-negative and loss-of-function experiments in human cells, including neutrophils, show that active RAC1 is required for lamellipodium formation. Supporting Evidence: PMID:19625648 Rac1 and Rac2, members of the small Rho GTPase family, play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants.
GO:0010595 positive regulation of endothelial cell migration	IMP PMID:18558630 Overlapping and distinct roles for PI3Kbeta and gamma isofor...	KEEP AS NON CORE	Summary: RAC1 promotes endothelial cell migration. Reason: Cell-type-specific migratory output of the core actin/migration function.
GO:0010762 regulation of fibroblast migration	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 regulates fibroblast migration. Reason: Cell-type-specific migratory output.
GO:0010764 negative regulation of fibroblast migration	IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri...	KEEP AS NON CORE	Summary: Context-dependent negative regulation of fibroblast migration. Reason: Direct experimental observation in a specific setting; a context-dependent sign of the general migration role, retained as non-core.
GO:0010810 regulation of cell-substrate adhesion	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: RAC1 regulates cell-substrate adhesion. Reason: Adhesion regulation follows from RAC1-driven actin and adhesion-complex dynamics.
GO:0016020 membrane	IEA GO_REF:0000107	MODIFY	Summary: Generic membrane localization. Reason: Correct but too general; RAC1 is specifically a prenylated peripheral protein on the cytoplasmic face of the plasma membrane. Proposed replacements: plasma membrane Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0016020 membrane	ISS GO_REF:0000024	MODIFY	Summary: Generic membrane localization. Reason: Correct but too general; RAC1 is specifically a prenylated peripheral protein on the cytoplasmic face of the plasma membrane. Proposed replacements: plasma membrane Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine
GO:0016477 cell migration	IDA PMID:23512198 SCF E3 ligase F-box protein complex SCF(FBXL19) regulates ce...	ACCEPT	Summary: RAC1 drives cell migration. Reason: RAC1 generates the protrusive actin structures that move cells; loss-of-function in human cells impairs migration. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt regulation of cell migration and adhesion assembly and disassembly
GO:0016477 cell migration	IMP PMID:26934001 MicroRNA-92b represses invasion-metastasis cascade of esopha...	ACCEPT	Summary: RAC1 drives cell migration. Reason: RAC1 generates the protrusive actin structures that move cells; loss-of-function in human cells impairs migration. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt regulation of cell migration and adhesion assembly and disassembly
GO:0016601 Rac protein signal transduction	IBA GO_REF:0000033	ACCEPT	Summary: Rac-family signal transduction. Reason: The term names precisely the signalling module RAC1 heads, supported by phylogenetic and curatorial inference.
GO:0016601 Rac protein signal transduction	IC PMID:12885773 Skeletal muscle signaling pathway through the dystrophin gly...	ACCEPT	Summary: Rac-family signal transduction. Reason: The term names precisely the signalling module RAC1 heads, supported by phylogenetic and curatorial inference.
GO:0016601 Rac protein signal transduction	IEA GO_REF:0000107	ACCEPT	Summary: Rac-family signal transduction. Reason: The term names precisely the signalling module RAC1 heads, supported by phylogenetic and curatorial inference.
GO:0019899 enzyme binding	IPI PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Ra...	KEEP AS NON CORE	Summary: RAC1 binds the Nox1 oxidase enzyme machinery. Reason: Enzyme binding is generic; the informative statement is that RAC1 is a subunit and activator of NADPH oxidase complexes. Supporting Evidence: PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Rac1.
GO:0019901 protein kinase binding	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 binds effector protein kinases. Reason: GTP-RAC1 binds and activates PAK-family kinases and PKN2 through their GTPase-binding domains; this is how much of its signalling output is delivered. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Stimulates PKN2 kinase activity (PubMed:9121475).
GO:0019901 protein kinase binding	IPI PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	ACCEPT	Summary: RAC1 binds effector protein kinases. Reason: GTP-RAC1 binds and activates PAK-family kinases and PKN2 through their GTPase-binding domains; this is how much of its signalling output is delivered. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Stimulates PKN2 kinase activity (PubMed:9121475).
GO:0030027 lamellipodium	IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri...	ACCEPT	Summary: RAC1 is found in protrusive lamellipodial structures. Reason: The dynamic protrusion phenotype imaged in this study is the lamellipodial structure that Rac1 signalling generates. Supporting Evidence: PMID:19126672 which induces a dynamic protrusion phenotype as seen by TIRF in our cells
GO:0030027 lamellipodium	IDA PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	ACCEPT	Summary: RAC1 localizes to the leading-edge lamellipodium of chemotaxing neutrophils. Reason: Rac1 is differentially activated at the leading edge during human neutrophil chemotaxis, where the lamellipodium forms. Supporting Evidence: PMID:19625648 play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants
GO:0030027 lamellipodium	IEA GO_REF:0000120	ACCEPT	Summary: RAC1 localizes to lamellipodia. Reason: Active RAC1 concentrates in the lamellipodium it generates; shown by direct imaging.
GO:0030032 lamellipodium assembly	IMP PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	ACCEPT	Summary: RAC1 is required for lamellipodium assembly. Reason: Dominant-negative Rac1 blocks peripheral actin polymerization and ruffling. Supporting Evidence: PMID:9312003 the dominant-negative mutant of Rac1, Rac1(S17N)
GO:0030036 actin cytoskeleton organization	IGI PMID:19890013 Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaff...	ACCEPT	Summary: RAC1 organizes the actin cytoskeleton. Reason: Core process, supported by genetic interaction experiments and by the whole body of Rho GTPase literature.
GO:0030041 actin filament polymerization	TAS PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	ACCEPT	Summary: RAC1 drives actin filament polymerization. Reason: Through WAVE/Arp2/3 activation, GTP-RAC1 initiates branched actin polymerization at the cell periphery. Supporting Evidence: PMID:9312003 remodels the actin cytoskeleton by inducing actin polymerization at the cell periphery
GO:0030334 regulation of cell migration	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 regulates cell migration. Reason: Supported by phylogenetic inference and by multiple human loss-of-function studies.
GO:0030334 regulation of cell migration	IMP PMID:19934221 The Rho-family GEF Asef2 activates Rac to modulate adhesion ...	ACCEPT	Summary: RAC1 regulates cell migration. Reason: Supported by phylogenetic inference and by multiple human loss-of-function studies.
GO:0030334 regulation of cell migration	IMP PMID:22036506 The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation o...	ACCEPT	Summary: RAC1 regulates cell migration. Reason: Supported by phylogenetic inference and by multiple human loss-of-function studies.
GO:0030425 dendrite	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: RAC1 is present in dendrites. Reason: Neuronal compartment consistent with its synaptic roles; peripheral to the general plasma-membrane localization. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Cell projection, dendrite {ECO:0000250\|UniProtKB:P63001}
GO:0030667 secretory granule membrane	TAS Reactome:R-HSA-6798743	KEEP AS NON CORE	Summary: Reactome places RAC1 on secretory granule membranes in neutrophils. Reason: Granule-membrane association accompanies oxidase assembly and degranulation; secondary location.
GO:0030672 synaptic vesicle membrane	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Synaptic vesicle membrane localization transferred from rodent. Reason: Consistent with presynaptic roles reported in rodents; peripheral and not directly shown for the human protein.
GO:0030742 GTP-dependent protein binding	IEA GO_REF:0000107	ACCEPT	Summary: RAC1 binds effectors in a GTP-dependent manner. Reason: Nucleotide-state-dependent effector binding is the mechanistic essence of RAC1 switch function and is far more informative than generic protein binding. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In its active state, binds to a variety of effector proteins to regulate cellular responses
GO:0030865 cortical cytoskeleton organization	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 organizes the cortical cytoskeleton. Reason: Cortical actin remodelling is the conserved core process of Rac GTPases.
GO:0030900 forebrain development	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 is required for forebrain development in rodents. Reason: Developmental output of neuronal migration and actin dynamics; pleiotropic and non-core.
GO:0031410 cytoplasmic vesicle	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: RAC1 associates with cytoplasmic vesicles. Reason: Prenylated RAC1 cycles among cytoplasmic-face membranes including endosomes; peripheral.
GO:0031410 cytoplasmic vesicle	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 associates with cytoplasmic vesicles. Reason: Prenylated RAC1 cycles among cytoplasmic-face membranes including endosomes; peripheral.
GO:0031529 ruffle organization	TAS PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	ACCEPT	Summary: RAC1 organizes membrane ruffles. Reason: Growth-factor-induced ruffling is the classical RAC1 phenotype. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt growth-factor induced formation of membrane ruffles
GO:0031901 early endosome membrane	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 associates with early endosome membranes. Reason: Endosomal pools participate in RAC1 trafficking and in ACKR2 recycling; peripheral.
GO:0031996 thioesterase binding	IPI PMID:12612085 The TRE17 oncogene encodes a component of a novel effector p...	KEEP AS NON CORE	Summary: Interaction with a thioesterase reported by co-purification. Reason: A specific binding partner class with no established functional consequence for RAC1; retained but peripheral.
GO:0032496 response to lipopolysaccharide	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 responds to LPS stimulation in immune cells. Reason: A stimulus-response context of RAC1 signalling, not an activity of the protein.
GO:0032587 ruffle membrane	IDA PMID:11084340 Synaptojanin 2, a novel Rac1 effector that regulates clathri...	ACCEPT	Summary: RAC1 localizes to ruffle membranes. Reason: Direct imaging places RAC1 in the ruffle membrane, the structure it generates. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Cell projection, ruffle membrane {ECO:0000269\|PubMed:11084340}
GO:0032587 ruffle membrane	IDA PMID:20875796 Abba promotes PDGF-mediated membrane ruffling through activa...	ACCEPT	Summary: RAC1 localizes to ruffle membranes. Reason: Direct imaging places RAC1 in the ruffle membrane, the structure it generates. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Cell projection, ruffle membrane {ECO:0000269\|PubMed:11084340}
GO:0032587 ruffle membrane	IEA GO_REF:0000120	ACCEPT	Summary: RAC1 localizes to ruffle membranes. Reason: Direct imaging places RAC1 in the ruffle membrane, the structure it generates. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Cell projection, ruffle membrane {ECO:0000269\|PubMed:11084340}
GO:0032707 negative regulation of interleukin-23 production	IDA PMID:16982892 Rac1 negatively regulates lipopolysaccharide-induced IL-23 p...	KEEP AS NON CORE	Summary: RAC1 activity limits IL-23 production in dendritic cells. Reason: A cytokine-regulation output in a specific immune cell type; downstream and non-core.
GO:0032956 regulation of actin cytoskeleton organization	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 regulates actin cytoskeleton organization. Reason: Phylogenetically conserved core process of the Rac clade.
GO:0034446 substrate adhesion-dependent cell spreading	IMP PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	ACCEPT	Summary: RAC1 inhibition impairs adhesion-dependent spreading of human leukocytes. Reason: Acute inhibition of Rac1 with a dominant-negative fusion protein blocks the protrusive behaviour that underlies spreading on substrate. Supporting Evidence: PMID:19625648 we used TAT dominant-negative Rac1-T17N and Rac2-T17N fusion proteins to acutely alter the activity of Rac1 and Rac2 individually in human neutrophils
GO:0034446 substrate adhesion-dependent cell spreading	IMP PMID:28886345 RAC1 Missense Mutations in Developmental Disorders with Dive...	ACCEPT	Summary: Disease-associated RAC1 variants change spreading and protrusion morphology. Reason: Human RAC1 missense variants alter the protrusive and spreading phenotype of transfected cells, confirming that adhesion-dependent spreading depends on RAC1. Supporting Evidence: PMID:28886345 Gln61Leu variant resulted in virtually all cells exhibiting large lamellipodia or membrane ruffles and a significantly increased circularity index.
GO:0035025 positive regulation of Rho protein signal transduction	TAS PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	KEEP AS NON CORE	Summary: Crosstalk in which RAC1 activity influences Rho signalling. Reason: Rac-Rho crosstalk is well described but indirect, mediated by GEFs, GAPs and effector kinases.
GO:0035556 intracellular signal transduction	TAS PMID:9572733 Role of Rac1 and oxygen radicals in collagenase-1 expression...	TOO GENERAL	Summary: Generic intracellular signal transduction. Reason: True but uninformative; the specific terms Rac protein signal transduction and small GTPase-mediated signal transduction asserted in this review already entail it.
GO:0035567 non-canonical Wnt signaling pathway	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 acts in non-canonical Wnt/planar cell polarity signalling. Reason: Rac GTPases operate downstream of Dishevelled in the PCP branch; a pathway context for the actin/polarity function.
GO:0035774 positive regulation of insulin secretion involved in cellular response to glucose stimulus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 promotes glucose-stimulated insulin secretion in beta cells. Reason: Cell-type-specific secretory output driven by cortical actin remodelling.
GO:0036464 cytoplasmic ribonucleoprotein granule	IDA PMID:15121898 The composition of Staufen-containing RNA granules from huma...	KEEP AS NON CORE	Summary: RAC1 detected in cytoplasmic ribonucleoprotein granules. Reason: A reported but mechanistically unexplained pool; peripheral.
GO:0042470 melanosome	EXP PMID:17081065 Proteomic and bioinformatic characterization of the biogenes...	KEEP AS NON CORE	Summary: RAC1 is recovered in melanosome fractions. Reason: Mass spectrometry of melanosome fractions detects RAC1 across maturation stages; UniProt records Melanosome. Likely reflects association of a prenylated GTPase with organelle membranes rather than a melanosome-specific function. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Identified by mass spectrometry in melanosome fractions from stage I to stage IV
GO:0042470 melanosome	EXP PMID:19948726 Activated Rac1 GTPase translocates protein phosphatase 5 to ...	KEEP AS NON CORE	Summary: RAC1 is recovered in melanosome fractions. Reason: Mass spectrometry of melanosome fractions detects RAC1 across maturation stages; UniProt records Melanosome. Likely reflects association of a prenylated GTPase with organelle membranes rather than a melanosome-specific function. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Identified by mass spectrometry in melanosome fractions from stage I to stage IV
GO:0042470 melanosome	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: RAC1 is recovered in melanosome fractions. Reason: Mass spectrometry of melanosome fractions detects RAC1 across maturation stages; UniProt records Melanosome. Likely reflects association of a prenylated GTPase with organelle membranes rather than a melanosome-specific function. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Identified by mass spectrometry in melanosome fractions from stage I to stage IV
GO:0042554 superoxide anion generation	IDA PMID:38355798 Structure of human phagocyte NADPH oxidase in the activated ...	ACCEPT	Summary: RAC1 is required for superoxide generation by the phagocyte NADPH oxidase. Reason: The cryo-EM structure of the activated human NOX2 complex includes RAC1, and UniProt records RAC1 as a subunit of the complex that transfers electrons from NADPH to O2. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion PMID:38355798 This process generates superoxide anions that are vital for killing pathogens
GO:0042734 presynaptic membrane	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Presynaptic membrane localization transferred from rodent. Reason: Consistent with neuronal roles; peripheral and not directly shown in human.
GO:0043020 NADPH oxidase complex	IDA PMID:38355798 Structure of human phagocyte NADPH oxidase in the activated ...	ACCEPT	Summary: RAC1 is a subunit of the NADPH oxidase complex. Reason: Structural and biochemical evidence places RAC1 in the activated phagocyte NADPH oxidase with NOX2, p22phox and the cytosolic factors. Supporting Evidence: PMID:38355798 The activation of phagocyte NADPH oxidase requires membrane translocation and the binding of several cytosolic factors file:human/RAC1/RAC1-uniprot.txt Subunit of the phagocyte NADPH oxidase complex
GO:0043020 NADPH oxidase complex	NAS PMID:24598074 Role of the Rho GTPase Rac in the activation of the phagocyt...	ACCEPT	Summary: RAC1 is a subunit of the NADPH oxidase complex. Reason: Structural and biochemical evidence places RAC1 in the activated phagocyte NADPH oxidase with NOX2, p22phox and the cytosolic factors. Supporting Evidence: PMID:38355798 The activation of phagocyte NADPH oxidase requires membrane translocation and the binding of several cytosolic factors file:human/RAC1/RAC1-uniprot.txt Subunit of the phagocyte NADPH oxidase complex
GO:0043652 engulfment of apoptotic cell	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 is required for engulfment of apoptotic cells. Reason: Efferocytosis is an actin-driven output of RAC1 signalling in phagocytes. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt phagocytosis of apoptotic cells
GO:0044877 protein-containing complex binding	IDA PMID:21107423 Structure and control of the actin regulatory WAVE complex.	KEEP AS NON CORE	Summary: RAC1 binds protein complexes such as the WAVE regulatory complex. Reason: True but generic; the informative statements are GTP-dependent effector binding and NADPH oxidase complex membership.
GO:0045202 synapse	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: RAC1 is present at synapses. Reason: General synaptic compartment; the postsynapse and glutamatergic synapse annotations with direct evidence are more informative.
GO:0045202 synapse	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: RAC1 is present at synapses. Reason: General synaptic compartment; the postsynapse and glutamatergic synapse annotations with direct evidence are more informative.
GO:0045211 postsynaptic membrane	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Postsynaptic membrane localization transferred from rodent. Reason: Consistent with directly supported postsynaptic localization; retained as non-core.
GO:0045428 regulation of nitric oxide biosynthetic process	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: RAC1 influences nitric oxide synthesis. Reason: Indirect regulatory effect reported by similarity; not an activity of RAC1.
GO:0045730 respiratory burst	NAS PMID:27048830 CYBA encoding p22(phox), the cytochrome b558 alpha polypepti...	ACCEPT	Summary: RAC1 is required for the respiratory burst. Reason: As an NADPH oxidase subunit, RAC1 is necessary for the oxidative burst of phagocytes and performs part of the work by completing the activated complex. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt which is involved in stimulation of the NADPH oxidase activity in macrophages
GO:0046425 regulation of receptor signaling pathway via JAK-STAT	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Regulation of JAK-STAT signalling transferred electronically. Reason: Effects on JAK-STAT output are indirect and poorly defined for RAC1; the annotation exceeds the evidence.
GO:0048012 hepatocyte growth factor receptor signaling pathway	IMP PMID:25198505 Microtubule dynamics control HGF-induced lung endothelial ba...	KEEP AS NON CORE	Summary: RAC1 acts downstream of MET in hepatocyte growth factor signalling. Reason: Receptor-pathway context for RAC1-driven motility (scatter response).
GO:0048261 negative regulation of receptor-mediated endocytosis	TAS PMID:9312003 A role for POR1, a Rac1-interacting protein, in ARF6-mediate...	KEEP AS NON CORE	Summary: RAC1 activity inhibits receptor-mediated endocytosis. Reason: Reported regulatory effect on endocytic uptake, downstream of cortical actin changes.
GO:0048812 neuron projection morphogenesis	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 shapes neuron projections. Reason: Neurite and growth-cone morphogenesis is an actin-dependent neuronal output.
GO:0048870 cell motility	IDA PMID:19403692 BPAG1e maintains keratinocyte polarity through beta4 integri...	ACCEPT	Summary: RAC1 activity is required for keratinocyte motility. Reason: Loss of the BPAG1e scaffold lowers Rac1 activity and abolishes front-to-rear polarity and directed motility in human keratinocytes. Supporting Evidence: PMID:19403692 the amount of Rac1 associating with beta4 integrin and the activity of both Rac1 and cofilin are significantly lower in BPAG1e-deficient cells compared with wild-type keratinocytes
GO:0051022 Rho GDP-dissociation inhibitor binding	ISS GO_REF:0000024	ACCEPT	Summary: RAC1 binds RhoGDI. Reason: The RAC1-RhoGDI heterodimer is a defined biochemical entity that holds prenylated RAC1 soluble in the cytosol and controls its membrane delivery. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1
GO:0051492 regulation of stress fiber assembly	IGI PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	KEEP AS NON CORE	Summary: RAC1 influences stress fibre assembly. Reason: Stress fibres are primarily RhoA-driven; RAC1 modulates them through crosstalk, so this is an indirect regulatory role.
GO:0051496 positive regulation of stress fiber assembly	IDA PMID:23129259 S100A10 is required for the organization of actin stress fib...	KEEP AS NON CORE	Summary: RAC1 can promote stress fibre assembly. Reason: Context-dependent and mediated by Rac-Rho crosstalk rather than direct action on contractile bundles.
GO:0051496 positive regulation of stress fiber assembly	IMP PMID:8625410 Wiskott-Aldrich syndrome protein, a novel effector for the G...	KEEP AS NON CORE	Summary: RAC1 can promote stress fibre assembly. Reason: Context-dependent and mediated by Rac-Rho crosstalk rather than direct action on contractile bundles.
GO:0051668 localization within membrane	IMP PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Ra...	KEEP AS NON CORE	Summary: Membrane localization of RAC1 is required for Nox1 activation. Reason: Describes the regulated targeting of RAC1 itself; informative mechanistically but not a separate core process. Supporting Evidence: PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Rac1.
GO:0051894 positive regulation of focal adhesion assembly	IDA PMID:23129259 S100A10 is required for the organization of actin stress fib...	KEEP AS NON CORE	Summary: RAC1 promotes focal adhesion assembly. Reason: Adhesion assembly follows protrusion driven by RAC1; downstream output.
GO:0055038 recycling endosome membrane	IDA PMID:10036235 ARF6 requirement for Rac ruffling suggests a role for membra...	KEEP AS NON CORE	Summary: RAC1 is present on recycling endosome membranes. Reason: Consistent with RAC1 trafficking to and from the plasma membrane; peripheral location.
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: RAC1 acts in the planar cell polarity branch of Wnt signalling. Reason: Review-based assertion consistent with the established role of Rac GTPases downstream of Dishevelled; a pathway context.
GO:0060091 kinocilium	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Kinocilium localization transferred electronically. Reason: A highly specialized hair-cell structure; the evidence does not support assigning this location to human RAC1.
GO:0060263 regulation of respiratory burst	IDA PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Ra...	ACCEPT	Summary: RAC1 regulates the respiratory burst. Reason: RAC1 membrane targeting and GTP loading control Nox1 and NOX2 activity, setting the rate of superoxide production. Supporting Evidence: PMID:16636067 Nox1-dependent reactive oxygen generation is regulated by Rac1.
GO:0060326 cell chemotaxis	IBA GO_REF:0000033	ACCEPT	Summary: RAC1 is required for chemotaxis. Reason: Directional migration toward chemoattractants requires RAC1-driven leading-edge protrusion, shown directly in human neutrophils. Supporting Evidence: PMID:19625648 play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants
GO:0061344 regulation of cell adhesion involved in heart morphogenesis	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 regulates adhesion during heart morphogenesis. Reason: Tissue-specific developmental output of the adhesion/actin function.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	KEEP AS NON CORE	Summary: RAC1 detected in exosome preparations. Reason: Common proteomic finding for abundant cytosolic and membrane-associated proteins; peripheral.
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	KEEP AS NON CORE	Summary: RAC1 detected in exosome preparations. Reason: Common proteomic finding for abundant cytosolic and membrane-associated proteins; peripheral.
GO:0071526 semaphorin-plexin signaling pathway	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: RAC1 acts downstream of plexin receptors in semaphorin signalling. Reason: Plexins bind and regulate Rho-family GTPases; a receptor-pathway context for the core actin function.
GO:0090023 positive regulation of neutrophil chemotaxis	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 promotes neutrophil chemotaxis. Reason: Cell-type-specific instance of the chemotaxis role, supported by human neutrophil experiments. Supporting Evidence: PMID:19625648 play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants
GO:0090023 positive regulation of neutrophil chemotaxis	IMP PMID:19625648 Human neutrophils coordinate chemotaxis by differential acti...	KEEP AS NON CORE	Summary: RAC1 promotes neutrophil chemotaxis. Reason: Cell-type-specific instance of the chemotaxis role, supported by human neutrophil experiments. Supporting Evidence: PMID:19625648 play essential roles in coordinating directional migration and superoxide production during neutrophil responses to chemoattractants
GO:0097178 ruffle assembly	IEA GO_REF:0000107	ACCEPT	Summary: RAC1 is required for ruffle assembly. Reason: Membrane ruffling is the defining RAC1-dependent actin structure, shown by direct perturbation in human cells.
GO:0097178 ruffle assembly	IMP PMID:10036235 ARF6 requirement for Rac ruffling suggests a role for membra...	ACCEPT	Summary: RAC1 is required for ruffle assembly. Reason: Membrane ruffling is the defining RAC1-dependent actin structure, shown by direct perturbation in human cells.
GO:0098794 postsynapse	IDA PMID:15800193 A GIT1/PIX/Rac/PAK signaling module regulates spine morphoge...	ACCEPT	Summary: RAC1 acts at the postsynapse. Reason: Direct localization and loss-of-function experiments place RAC1 at postsynaptic sites, where it controls spine actin and synapse assembly. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In neurons, is involved in dendritic spine formation and synaptic plasticity
GO:0098794 postsynapse	IDA PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera...	ACCEPT	Summary: RAC1 acts at the postsynapse. Reason: Direct localization and loss-of-function experiments place RAC1 at postsynaptic sites, where it controls spine actin and synapse assembly. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In neurons, is involved in dendritic spine formation and synaptic plasticity
GO:0098794 postsynapse	IMP PMID:15800193 A GIT1/PIX/Rac/PAK signaling module regulates spine morphoge...	ACCEPT	Summary: RAC1 acts at the postsynapse. Reason: Direct localization and loss-of-function experiments place RAC1 at postsynaptic sites, where it controls spine actin and synapse assembly. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In neurons, is involved in dendritic spine formation and synaptic plasticity
GO:0098794 postsynapse	IMP PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera...	ACCEPT	Summary: RAC1 acts at the postsynapse. Reason: Direct localization and loss-of-function experiments place RAC1 at postsynaptic sites, where it controls spine actin and synapse assembly. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In neurons, is involved in dendritic spine formation and synaptic plasticity
GO:0098978 glutamatergic synapse	IDA PMID:15800193 A GIT1/PIX/Rac/PAK signaling module regulates spine morphoge...	ACCEPT	Summary: RAC1 acts at glutamatergic synapses. Reason: Direct and mutant-based evidence from hippocampal neurons supports RAC1 function in spine morphogenesis and synapse formation at excitatory synapses. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs)
GO:0098978 glutamatergic synapse	IDA PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera...	ACCEPT	Summary: RAC1 acts at glutamatergic synapses. Reason: Direct and mutant-based evidence from hippocampal neurons supports RAC1 function in spine morphogenesis and synapse formation at excitatory synapses. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs)
GO:0098978 glutamatergic synapse	IEA GO_REF:0000107	ACCEPT	Summary: RAC1 acts at glutamatergic synapses. Reason: Direct and mutant-based evidence from hippocampal neurons supports RAC1 function in spine morphogenesis and synapse formation at excitatory synapses. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs)
GO:0098978 glutamatergic synapse	IMP PMID:15800193 A GIT1/PIX/Rac/PAK signaling module regulates spine morphoge...	ACCEPT	Summary: RAC1 acts at glutamatergic synapses. Reason: Direct and mutant-based evidence from hippocampal neurons supports RAC1 function in spine morphogenesis and synapse formation at excitatory synapses. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs)
GO:0098978 glutamatergic synapse	IMP PMID:24352656 Rho-GTPase-activating protein interacting with Cdc-42-intera...	ACCEPT	Summary: RAC1 acts at glutamatergic synapses. Reason: Direct and mutant-based evidence from hippocampal neurons supports RAC1 function in spine morphogenesis and synapse formation at excitatory synapses. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs)
GO:0101003 ficolin-1-rich granule membrane	TAS Reactome:R-HSA-6800426	KEEP AS NON CORE	Summary: Reactome places RAC1 on ficolin-1-rich granule membranes. Reason: Neutrophil granule membranes are a site of oxidase assembly; secondary location.
GO:0150052 regulation of postsynapse assembly	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 regulates postsynapse assembly. Reason: Consistent with the directly supported postsynaptic role; retained as non-core because the evidence here is electronic transfer.
GO:1900026 positive regulation of substrate adhesion-dependent cell spreading	IDA PMID:23129259 S100A10 is required for the organization of actin stress fib...	KEEP AS NON CORE	Summary: RAC1 promotes cell spreading on substrate. Reason: Specific positive-regulation form of the spreading role already accepted.
GO:1900029 positive regulation of ruffle assembly	IDA PMID:15467718 Mammalian TOR complex 2 controls the actin cytoskeleton and ...	ACCEPT	Summary: RAC1 positively regulates ruffle assembly. Reason: Active RAC1 is sufficient to induce ruffles; directly demonstrated.
GO:1900242 regulation of synaptic vesicle endocytosis	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 regulates synaptic vesicle endocytosis. Reason: Presynaptic regulatory role reported in rodents; non-core for the human protein.
GO:1903348 positive regulation of bicellular tight junction assembly	IMP PMID:22796473 Desmoglein 3 acting as an upstream regulator of Rho GTPases,...	KEEP AS NON CORE	Summary: RAC1 promotes tight junction assembly. Reason: Junction assembly depends on RAC1-dependent cortical actin organization, shown by loss-of-function in human keratinocytes. Supporting Evidence: file:human/RAC1/RAC1-uniprot.txt Required for DSG3 translocation to cell-cell junctions
GO:1904948 midbrain dopaminergic neuron differentiation	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 contributes to midbrain dopaminergic neuron differentiation. Reason: Developmental, cell-type-specific output.
GO:2000386 positive regulation of ovarian follicle development	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: RAC1 promotes ovarian follicle development. Reason: Tissue-specific developmental output transferred electronically.

Gene Description

Existing Annotations Review

Core Functions

Serves as the GTPase subunit of NADPH oxidase complexes - with NOX2/p22phox in phagocytes and with Nox1 in other cells - translocating to the membrane and completing the activated complex that transfers electrons from NADPH to oxygen to generate superoxide.

At postsynaptic sites of glutamatergic synapses, is locally activated by synaptic GEFs such as ARHGEF6/ARHGEF7 and remodels spine actin, controlling dendritic spine morphogenesis and synapse assembly.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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