HUMAN:RAC1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	RAC1 (synonyms: TC25)
Protein Name(s)	Ras-related C3 botulinum toxin substrate 1 Cell migration-inducing gene 5 protein Ras-like protein TC25 p21-Rac1
External Links
UniProt	P63000
EMBL	M29870 M31467 AJ132694 AJ132695 AJ132695 AF136373 AY279384 AF498964 BT007121 DQ165078 AC009412 AC009412 BC004247 BC050687 BC107748
CCDS	CCDS5348.1 CCDS5349.1
PIR	A34788
RefSeq	NP_008839.2 NP_061485.1
UniGene	Hs.413812
PDB	1E96 1FOE 1G4U 1HE1 1HH4 1I4D 1I4L 1I4T 1MH1 1RYF 1RYH 2FJU 2H7V 2NZ8 2P2L 2RMK 2VRW 2WKP 2WKQ 2WKR 2YIN 3B13 3BJI 3RYT 3SBD 3SBE 3SU8 3SUA 3TH5 4GZL 4GZM
PDBsum	1E96 1FOE 1G4U 1HE1 1HH4 1I4D 1I4L 1I4T 1MH1 1RYF 1RYH 2FJU 2H7V 2NZ8 2P2L 2RMK 2VRW 2WKP 2WKQ 2WKR 2YIN 3B13 3BJI 3RYT 3SBD 3SBE 3SU8 3SUA 3TH5 4GZL 4GZM
DisProt	DP00408
ProteinModelPortal	P63000
SMR	P63000
BioGrid	111817
DIP	DIP-29260N
IntAct	P63000
MINT	MINT-4999291
STRING	9606.ENSP00000348461
BindingDB	P63000
ChEMBL	CHEMBL6094
DrugBank	DB00514
PhosphoSite	P63000
DMDM	51702787
MaxQB	P63000
PaxDb	P63000
PRIDE	P63000
DNASU	5879
Ensembl	ENST00000348035 ENST00000356142
GeneID	5879
KEGG	hsa:5879
UCSC	uc003spx.3
CTD	5879
GeneCards	GC07P006380
H-InvDB	HIX0031500
HGNC	HGNC:9801
HPA	CAB035994
MIM	602048
neXtProt	NX_P63000
PharmGKB	PA34162
eggNOG	COG1100
GeneTree	ENSGT00760000118978
HOGENOM	HOG000233974
HOVERGEN	HBG009351
InParanoid	P63000
KO	K04392
OMA	PPRRMCK
OrthoDB	EOG764747
PhylomeDB	P63000
TreeFam	TF101109
Reactome	REACT_11068 REACT_111040 REACT_13638 REACT_147814 REACT_147867 REACT_160086 REACT_163701 REACT_1695 REACT_172581 REACT_18407 REACT_19226 REACT_19236 REACT_19238 REACT_19266 REACT_19277 REACT_19279 REACT_19342 REACT_22272 REACT_22351 REACT_228016 REACT_228085 REACT_228166 REACT_228189 REACT_228226 REACT_24970 REACT_25299
SignaLink	P63000
ChiTaRS	RAC1
EvolutionaryTrace	P63000
GeneWiki	RAC1
GenomeRNAi	5879
NextBio	22846
PMAP-CutDB	P63000
PRO	PR:P63000
Proteomes	UP000005640
Bgee	P63000
CleanEx	HS_RAC1
ExpressionAtlas	P63000
Genevestigator	P63000
GO	GO:0005737 GO:0036464 GO:0005829 GO:0070062 GO:0019897 GO:0005925 GO:0000139 GO:0030027 GO:0042470 GO:0016020 GO:0001891 GO:0005886 GO:0032587 GO:0005802 GO:0019899 GO:0005525 GO:0003924 GO:0051022 GO:0031996 GO:0030036 GO:0030041 GO:0048532 GO:0009653 GO:0097190 GO:0002093 GO:0007411 GO:0007596 GO:0045453 GO:0007155 GO:0048870 GO:0008283 GO:0045216 GO:0007160 GO:0006928 GO:0021799 GO:0090103 GO:0048813 GO:0071542 GO:0021831 GO:0043652 GO:0003382 GO:0038095 GO:0038096 GO:0007186 GO:0006184 GO:0006972 GO:0006954 GO:0045087 GO:0035556 GO:0030032 GO:0051668 GO:0002551 GO:0032707 GO:0048261 GO:0048011 GO:0030168 GO:0030838 GO:0043065 GO:0010811 GO:0045740 GO:0051894 GO:0010592 GO:0090023 GO:0043552 GO:0001934 GO:0035025 GO:0051496 GO:1900026 GO:0072659 GO:0030334 GO:0050690 GO:0010310 GO:0060263 GO:0009611 GO:0097178 GO:0031529 GO:0071526 GO:0007264 GO:0034446 GO:0031295 GO:0016032 GO:0060071
Gene3D	3.40.50.300
InterPro	IPR027417 IPR005225 IPR001806 IPR003578
Pfam	PF00071
PRINTS	PR00449
SMART	SM00174
SUPFAM	SSF52540
TIGRFAMs	TIGR00231
PROSITE	PS51420

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0060154	cellular process regulating host cell cycle in response to virus	PMID:19129452^[1]	ECO:0000315			P		Figure 5C. Figure 5 shows that in cells infected with dl1520 and under cell conditions in which Rac1 can work normally(lane1) that Akt and p70 S6K are phosphorylated which areknow to be involved in the control of the cell cycle. When invected but Rac1 in knocked down (lane 2 and 3)by using a mutant Rac1 that is negative dominant, those proteins are not phosphorylated.Figure 6B. middle graph-Cells that were infected with dl1520 and treated with NSC23766 which stops Rac1 from functioning in its normal manner resulted in a major drop of viable cells suggesting its important in response to a virus affecting cell prolifeation. It is IMP because of their use of a dominant negative Rac1 mutant phenotype.	complete
	GO:0006468	protein phosphorylation	PMID:19129452^[1]	ECO:0000315			P		Figure 5C. lane one shows dl1520 infection with normally working Rac1 in the cell and the phosphorylation of p70S6K and Akt. Lanes 2 and 3 show that when infected but dominant negative Rac1 is added that phosphorylation is not seen showing that in viral response Rac1 is involved in phosphorylation. It is IMP because the use dnRac1 phenotypically does not have normal function and in dominant not allowing the normal cellular Rac1 to function well.	complete
involved_in	GO:0045428	regulation of nitric oxide biosynthetic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6RUV5	P	occurs_in:(CL:0000235) regulates_o_occurs_in:(CL:0000235)	Seeded From UniProt	complete
involved_in	GO:0001764	neuron migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P63001	P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:21107423^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(GO:0031209)	Seeded From UniProt	complete
involved_in	GO:0097178	ruffle assembly	PMID:10036235^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0055038	recycling endosome membrane	PMID:10036235^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10036235^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	PMID:24352656^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	PMID:20875796^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:19787194^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051492	regulation of stress fiber assembly	PMID:8625410^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P42768	P		Seeded From UniProt	complete
involved_in	GO:0010591	regulation of lamellipodium assembly	PMID:8625410^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P42768	P		Seeded From UniProt	complete
involved_in	GO:0051496	positive regulation of stress fiber assembly	PMID:8625410^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010592	positive regulation of lamellipodium assembly	PMID:8625410^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:8625410^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13177	F		Seeded From UniProt	complete
involved_in	GO:0031116	positive regulation of microtubule polymerization	PMID:25198505^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000066)	Seeded From UniProt	complete
involved_in	GO:0048012	hepatocyte growth factor receptor signaling pathway	PMID:25198505^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000066)	Seeded From UniProt	complete
involved_in	GO:0008361	regulation of cell size	PMID:22467863^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008361	regulation of cell size	PMID:22467863^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P35241	P		Seeded From UniProt	complete
involved_in	GO:0060071	Wnt signaling pathway, planar cell polarity pathway	PMID:24431302^[10]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:15601624^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	PMID:19625648^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19625648^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000775)	Seeded From UniProt	complete
colocalizes_with	GO:0005884	actin filament	PMID:19625648^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000775) part_of:(GO:0071944)	Seeded From UniProt	complete
involved_in	GO:0010592	positive regulation of lamellipodium assembly	PMID:19625648^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0030593) occurs_at:(GO:0031252)	Seeded From UniProt	complete
involved_in	GO:0034446	substrate adhesion-dependent cell spreading	PMID:19625648^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0030593)	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:19625648^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090023	positive regulation of neutrophil chemotaxis	PMID:19625648^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010811	positive regulation of cell-substrate adhesion	PMID:20926685^[14]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q15404	P	has_input:(UniProtKB:P02751) occurs_in:(CL:0000066)	Seeded From UniProt	complete
involved_in	GO:0010811	positive regulation of cell-substrate adhesion	PMID:20926685^[14]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P48059	P	has_input:(UniProtKB:P02751) occurs_in:(CL:0000066)	Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:15121898^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000031)	Seeded From UniProt	complete
involved_in	GO:0034446	substrate adhesion-dependent cell spreading	PMID:28886345^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0060263	regulation of respiratory burst	PMID:16636067^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051668	localization within membrane	PMID:16636067^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032707	negative regulation of interleukin-23 production	PMID:16982892^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:16636067^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y5S8	F		Seeded From UniProt	complete
involved_in	GO:0007160	cell-matrix adhesion	PMID:18156211^[21]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900026	positive regulation of substrate adhesion-dependent cell spreading	PMID:23129259^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051894	positive regulation of focal adhesion assembly	PMID:23129259^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051496	positive regulation of stress fiber assembly	PMID:23129259^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071526	semaphorin-plexin signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6RUV5	P		Seeded From UniProt	complete
enables	GO:0051022	Rho GDP-dissociation inhibitor binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6RUV5	F		Seeded From UniProt	complete
involved_in	GO:0048870	cell motility	PMID:19403692^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031996	thioesterase binding	PMID:12612085^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35125	F		Seeded From UniProt	complete
involved_in	GO:0030334	regulation of cell migration	PMID:22036506^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030334	regulation of cell migration	PMID:19934221^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030032	lamellipodium assembly	PMID:9312003^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6RUV5	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6RUV5	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:22036506^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:23633677^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:24352656^[4]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:15800193^[29]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:24352656^[4]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:15800193^[29]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	PMID:24352656^[4]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	PMID:15800193^[29]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	PMID:24352656^[4]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	PMID:15800193^[29]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:1902622	regulation of neutrophil migration	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:97845 MGI:MGI:97846 PANTHER:PTN002374567 UniProtKB:P15153 UniProtKB:P63000 ZFIN:ZDB-GENE-040625-27	P		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000633314 RGD:619755 UniProtKB:P63000	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 MGI:MGI:97845 PANTHER:PTN002784637 RGD:619755 UniProtKB:P15153 UniProtKB:P63000 WB:WBGene00004287	C		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:97845 PANTHER:PTN002784637 RGD:619755 UniProtKB:P63000 WB:WBGene00000424 dictyBase:DDB_G0293526	C		Seeded From UniProt	complete
involved_in	GO:0030036	actin cytoskeleton organization	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 FB:FBgn0014011 MGI:MGI:97845 MGI:MGI:97846 PANTHER:PTN002784637 RGD:1307568 RGD:619755 UniProtKB:P15153 UniProtKB:P63000 UniProtKB:Q6LC82 WB:WBGene00004287	P		Seeded From UniProt	complete
involved_in	GO:0030031	cell projection assembly	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:97846 PANTHER:PTN002374567	P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 FB:FBgn0014011 PANTHER:PTN002784637 RGD:619755 UniProtKB:P63000 dictyBase:DDB_G0293526	F		Seeded From UniProt	complete
involved_in	GO:0016601	Rac protein signal transduction	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002374567 RGD:619755	P		Seeded From UniProt	complete
involved_in	GO:0016477	cell migration	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 FB:FBgn0014011 MGI:MGI:97845 PANTHER:PTN002784637 RGD:619755 UniProtKB:Q6LC82 WB:WBGene00000424 WB:WBGene00004287 ZFIN:ZDB-GENE-030131-5415 ZFIN:ZDB-GENE-040625-27 dictyBase:DDB_G0293526	P		Seeded From UniProt	complete
involved_in	GO:0008045	motor neuron axon guidance	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 PANTHER:PTN002784640 WB:WBGene00000424 WB:WBGene00004287	P		Seeded From UniProt	complete
involved_in	GO:0007266	Rho protein signal transduction	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010341 FB:FBgn0014011 MGI:MGI:1931551 PANTHER:PTN000632671 RGD:619921 UniProtKB:I3LVS7 UniProtKB:P61586 UniProtKB:P84095	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 MGI:MGI:97845 PANTHER:PTN002784637 UniProtKB:P63000 WB:WBGene00000424 WB:WBGene00004287	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 MGI:MGI:97845 MGI:MGI:97846 PANTHER:PTN002784637 RGD:619755 UniProtKB:P15153 UniProtKB:P63000 WB:WBGene00000424 ZFIN:ZDB-GENE-040625-27 dictyBase:DDB_G0280975 dictyBase:DDB_G0293526	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0039140 MGI:MGI:108446 MGI:MGI:97845 PANTHER:PTN000632671 RGD:619755 RGD:619921 RGD:71043 SGD:S000001380 TAIR:locus:2131606 TAIR:locus:2204380 UniProtKB:A0A1D8PDV5 UniProtKB:P15153 UniProtKB:P60953 UniProtKB:P61586 UniProtKB:P63000 UniProtKB:Q15669 UniProtKB:Q9SSX0 WB:WBGene00000390 WB:WBGene00000424 WB:WBGene00004287 WB:WBGene00004357	F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21873635^[30]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010333 FB:FBgn0010341 FB:FBgn0014011 FB:FBgn0014020 MGI:MGI:106211 MGI:MGI:1096342 MGI:MGI:1916831 MGI:MGI:97845 MGI:MGI:97846 PANTHER:PTN000632671 PomBase:SPAC110.03 PomBase:SPAC16.01 PomBase:SPAC16A10.04 PomBase:SPAC1F7.04 PomBase:SPAC23C4.08 RGD:619755 RGD:619921 SGD:S000000046 SGD:S000001380 SGD:S000001763 SGD:S000004219 SGD:S000005034 SGD:S000005124 SGD:S000006369 TAIR:locus:2099232 TAIR:locus:2131606 UniProtKB:A0A1D8PCX9 UniProtKB:A0A1D8PH96 UniProtKB:P17081 UniProtKB:P60763 UniProtKB:P60953 UniProtKB:P61586 UniProtKB:P63000 UniProtKB:P84095 UniProtKB:Q5A904 WB:WBGene00000390 WB:WBGene00000424 WB:WBGene00003239 WB:WBGene00004287 WB:WBGene00004357	F		Seeded From UniProt	complete
involved_in	GO:0031529	ruffle organization	PMID:15467718^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030036	actin cytoskeleton organization	PMID:19890013^[32]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P17105	P		Seeded From UniProt	complete
involved_in	GO:0010592	positive regulation of lamellipodium assembly	PMID:15467718^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:23620790^[33]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:15467718^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005802	trans-Golgi network	PMID:12915445^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071526	semaphorin-plexin signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0071260	cellular response to mechanical stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
enables	GO:0051117	ATPase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
enables	GO:0051022	Rho GDP-dissociation inhibitor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
involved_in	GO:0045740	positive regulation of DNA replication	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0045453	bone resorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0045428	regulation of nitric oxide biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
involved_in	GO:0035774	positive regulation of insulin secretion involved in cellular response to glucose stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
involved_in	GO:0030036	actin cytoskeleton organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
enables	GO:0017137	Rab GTPase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
involved_in	GO:0016601	Rac protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
involved_in	GO:0010592	positive regulation of lamellipodium assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0007015	actin filament organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
involved_in	GO:0006935	chemotaxis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	F		Seeded From UniProt	complete
involved_in	GO:0002551	mast cell chemotaxis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	P		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6RUV5 ensembl:ENSRNOP00000001417	C		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806 InterPro:IPR003578 InterPro:IPR005225	F		Seeded From UniProt	complete
involved_in	GO:0007264	small GTPase mediated signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003578	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	PMID:9572733^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009653	anatomical structure morphogenesis	PMID:9572733^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009611	response to wounding	PMID:9572733^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	PMID:9572733^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006954	inflammatory response	PMID:9572733^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:2674130^[36] PMID:9312003^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010310	regulation of hydrogen peroxide metabolic process	PMID:16636067^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048261	negative regulation of receptor-mediated endocytosis	PMID:9312003^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035025	positive regulation of Rho protein signal transduction	PMID:9312003^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031529	ruffle organization	PMID:9312003^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030041	actin filament polymerization	PMID:9312003^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0101003	ficolin-1-rich granule membrane	Reactome:R-HSA-6800426	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0060071	Wnt signaling pathway, planar cell polarity pathway	Reactome:R-HSA-4086400	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	Reactome:R-HSA-2316434	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051056	regulation of small GTPase mediated signal transduction	Reactome:R-HSA-194840	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050690	regulation of defense response to virus by virus	Reactome:R-HSA-164944	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048013	ephrin receptor signaling pathway	Reactome:R-HSA-2682334	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048010	vascular endothelial growth factor receptor signaling pathway	Reactome:R-HSA-194138	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038096	Fc-gamma receptor signaling pathway involved in phagocytosis	Reactome:R-HSA-2029480	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038095	Fc-epsilon receptor signaling pathway	Reactome:R-HSA-2454202	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031295	T cell costimulation	Reactome:R-HSA-389356	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030667	secretory granule membrane	Reactome:R-HSA-6798743	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007596	blood coagulation	Reactome:R-HSA-109582	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-NUL-350365 Reactome:R-HSA-9032798 Reactome:R-HSA-8981931 Reactome:R-HSA-8981926 Reactome:R-HSA-8951586 Reactome:R-HSA-8875591 Reactome:R-HSA-8848618 Reactome:R-HSA-6800426 Reactome:R-HSA-6798743 Reactome:R-HSA-5672329 Reactome:R-HSA-5671993 Reactome:R-HSA-5671970 Reactome:R-HSA-5668735 Reactome:R-HSA-5668731 Reactome:R-HSA-5668718 Reactome:R-HSA-5668714 Reactome:R-HSA-5665809 Reactome:R-HSA-5665802 Reactome:R-HSA-5627775 Reactome:R-HSA-5626549 Reactome:R-HSA-5626507 Reactome:R-HSA-5626469 Reactome:R-HSA-5357483 Reactome:R-HSA-5357472 Reactome:R-HSA-5357445 Reactome:R-HSA-5218850 Reactome:R-HSA-5218841 Reactome:R-HSA-5218839 Reactome:R-HSA-5218827 Reactome:R-HSA-451366 Reactome:R-HSA-451347 Reactome:R-HSA-445072 Reactome:R-HSA-445064 Reactome:R-HSA-418856 Reactome:R-HSA-4093336 Reactome:R-HSA-400682 Reactome:R-HSA-399952 Reactome:R-HSA-399939 Reactome:R-HSA-399930 Reactome:R-HSA-3928642 Reactome:R-HSA-3928641 Reactome:R-HSA-3928640 Reactome:R-HSA-3928633 Reactome:R-HSA-3928628 Reactome:R-HSA-3928625 Reactome:R-HSA-3928620 Reactome:R-HSA-3928619 Reactome:R-HSA-3928612 Reactome:R-HSA-389788 Reactome:R-HSA-389348 Reactome:R-HSA-376123 Reactome:R-HSA-2730889 Reactome:R-HSA-2730856 Reactome:R-HSA-2730840 Reactome:R-HSA-2424476 Reactome:R-HSA-2400009 Reactome:R-HSA-2316434 Reactome:R-HSA-2197690 Reactome:R-HSA-2130194 Reactome:R-HSA-205039 Reactome:R-HSA-2029469 Reactome:R-HSA-2029467 Reactome:R-HSA-2029466 Reactome:R-HSA-2029465 Reactome:R-HSA-2029456 Reactome:R-HSA-2029454 Reactome:R-HSA-2029451 Reactome:R-HSA-194922 Reactome:R-HSA-194913 Reactome:R-HSA-194894 Reactome:R-HSA-194854 Reactome:R-HSA-1433415 Reactome:R-HSA-114542	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-5665809 Reactome:R-HSA-445064 Reactome:R-HSA-442314 Reactome:R-HSA-442273 Reactome:R-HSA-418856 Reactome:R-HSA-4093336 Reactome:R-HSA-3928642 Reactome:R-HSA-3928628 Reactome:R-HSA-389348 Reactome:R-HSA-3858475 Reactome:R-HSA-2730840 Reactome:R-HSA-2424476 Reactome:R-HSA-200952 Reactome:R-HSA-195146 Reactome:R-HSA-194854 Reactome:R-HSA-1433415 Reactome:R-HSA-1011598	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-5672083 Reactome:R-HSA-5625959	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0291	C		Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Thomas, MA et al. (2009) E4orf1 limits the oncolytic potential of the E1B-55K deletion mutant adenovirus. J. Virol. 83 2406-16 PubMed GONUTS page
↑ Chen, Z et al. (2010) Structure and control of the actin regulatory WAVE complex. Nature 468 533-8 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Radhakrishna, H et al. (1999) ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell. Sci. 112 ( Pt 6) 855-66 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Raynaud, F et al. (2014) Rho-GTPase-activating protein interacting with Cdc-42-interacting protein 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1 (Rac1) GTPase-activating protein that controls dendritic spine morphogenesis. J. Biol. Chem. 289 2600-9 PubMed GONUTS page
↑ Zheng, D et al. (2010) Abba promotes PDGF-mediated membrane ruffling through activation of the small GTPase Rac1. Biochem. Biophys. Res. Commun. 401 527-32 PubMed GONUTS page
↑ Araya, N et al. (2009) Role of Kenae/CCDC125 in cell motility through the deregulation of RhoGTPase. Int. J. Mol. Med. 24 605-11 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Symons, M et al. (1996) Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84 723-34 PubMed GONUTS page
↑ ^8.0 ^8.1 Tian, X et al. (2014) Microtubule dynamics control HGF-induced lung endothelial barrier enhancement. PLoS ONE 9 e105912 PubMed GONUTS page
↑ ^9.0 ^9.1 Valderrama, F et al. (2012) Radixin regulates cell migration and cell-cell adhesion through Rac1. J. Cell. Sci. 125 3310-9 PubMed GONUTS page
↑ Arenas, E (2014) Wnt signaling in midbrain dopaminergic neuron development and regenerative medicine for Parkinson's disease. J Mol Cell Biol 6 42-53 PubMed GONUTS page
↑ Xie, X et al. (2005) TIM, a Dbl-related protein, regulates cell shape and cytoskeletal organization in a Rho-dependent manner. Cell. Signal. 17 461-71 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 Zhang, H et al. (2009) Human neutrophils coordinate chemotaxis by differential activation of Rac1 and Rac2. J. Immunol. 183 2718-28 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ ^14.0 ^14.1 Ito, S et al. (2010) The roles of two distinct regions of PINCH-1 in the regulation of cell attachment and spreading. Mol. Biol. Cell 21 4120-9 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page
↑ Reijnders, MRF et al. (2017) RAC1 Missense Mutations in Developmental Disorders with Diverse Phenotypes. Am. J. Hum. Genet. 101 466-477 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Cheng, G et al. (2006) Nox1-dependent reactive oxygen generation is regulated by Rac1. J. Biol. Chem. 281 17718-26 PubMed GONUTS page
↑ Utsugi, M et al. (2006) Rac1 negatively regulates lipopolysaccharide-induced IL-23 p19 expression in human macrophages and dendritic cells and NF-kappaB p65 trans activation plays a novel role. J. Immunol. 177 4550-7 PubMed GONUTS page
↑ Dufourcq, P et al. (2008) Regulation of endothelial cell cytoskeletal reorganization by a secreted frizzled-related protein-1 and frizzled 4- and frizzled 7-dependent pathway: role in neovessel formation. Am. J. Pathol. 172 37-49 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Sayeed, S et al. (2013) S100A10 is required for the organization of actin stress fibers and promotion of cell spreading. Mol. Cell. Biochem. 374 105-11 PubMed GONUTS page
↑ Hamill, KJ et al. (2009) BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities. Mol. Biol. Cell 20 2954-62 PubMed GONUTS page
↑ Masuda-Robens, JM et al. (2003) The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol. Cell. Biol. 23 2151-61 PubMed GONUTS page
↑ ^25.0 ^25.1 Torrino, S et al. (2011) The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1. Dev. Cell 21 959-65 PubMed GONUTS page
↑ Bristow, JM et al. (2009) The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration. J. Cell. Sci. 122 4535-46 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 ^27.3 ^27.4 ^27.5 D'Souza-Schorey, C et al. (1997) A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. EMBO J. 16 5445-54 PubMed GONUTS page
↑ Borroni, EM et al. (2013) β-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6. Sci Signal 6 ra30.1-11, S1-3 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 Zhang, H et al. (2005) A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC. J. Neurosci. 25 3379-88 PubMed GONUTS page
↑ ^30.00 ^30.01 ^30.02 ^30.03 ^30.04 ^30.05 ^30.06 ^30.07 ^30.08 ^30.09 ^30.10 ^30.11 ^30.12 ^30.13 ^30.14 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^31.0 ^31.1 ^31.2 Jacinto, E et al. (2004) Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6 1122-8 PubMed GONUTS page
↑ Kim, IH et al. (2009) Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaffold for synaptic Rac signaling. J. Neurosci. 29 14039-49 PubMed GONUTS page
↑ Chiang, YJ et al. (2013) CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration. PLoS ONE 8 e61761 PubMed GONUTS page
↑ Faucherre, A et al. (2003) Lowe syndrome protein OCRL1 interacts with Rac GTPase in the trans-Golgi network. Hum. Mol. Genet. 12 2449-56 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 ^35.4 Kheradmand, F et al. (1998) Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280 898-902 PubMed GONUTS page
↑ Didsbury, J et al. (1989) rac, a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264 16378-82 PubMed GONUTS page

[PMID:19129452-1] 1.0 ^1.1 Thomas, MA et al. (2009) E4orf1 limits the oncolytic potential of the E1B-55K deletion mutant adenovirus. J. Virol. 83 2406-16 PubMed GONUTS page

[PMID:21107423-2] Chen, Z et al. (2010) Structure and control of the actin regulatory WAVE complex. Nature 468 533-8 PubMed GONUTS page

[PMID:10036235-3] 3.0 ^3.1 ^3.2 Radhakrishna, H et al. (1999) ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell. Sci. 112 ( Pt 6) 855-66 PubMed GONUTS page

[PMID:24352656-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Raynaud, F et al. (2014) Rho-GTPase-activating protein interacting with Cdc-42-interacting protein 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1 (Rac1) GTPase-activating protein that controls dendritic spine morphogenesis. J. Biol. Chem. 289 2600-9 PubMed GONUTS page

[PMID:20875796-5] Zheng, D et al. (2010) Abba promotes PDGF-mediated membrane ruffling through activation of the small GTPase Rac1. Biochem. Biophys. Res. Commun. 401 527-32 PubMed GONUTS page

[PMID:19787194-6] Araya, N et al. (2009) Role of Kenae/CCDC125 in cell motility through the deregulation of RhoGTPase. Int. J. Mol. Med. 24 605-11 PubMed GONUTS page

[PMID:8625410-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Symons, M et al. (1996) Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84 723-34 PubMed GONUTS page

[PMID:25198505-8] 8.0 ^8.1 Tian, X et al. (2014) Microtubule dynamics control HGF-induced lung endothelial barrier enhancement. PLoS ONE 9 e105912 PubMed GONUTS page

[PMID:22467863-9] 9.0 ^9.1 Valderrama, F et al. (2012) Radixin regulates cell migration and cell-cell adhesion through Rac1. J. Cell. Sci. 125 3310-9 PubMed GONUTS page

[PMID:24431302-10] Arenas, E (2014) Wnt signaling in midbrain dopaminergic neuron development and regenerative medicine for Parkinson's disease. J Mol Cell Biol 6 42-53 PubMed GONUTS page

[PMID:15601624-11] Xie, X et al. (2005) TIM, a Dbl-related protein, regulates cell shape and cytoskeletal organization in a Rho-dependent manner. Cell. Signal. 17 461-71 PubMed GONUTS page

[PMID:19625648-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 Zhang, H et al. (2009) Human neutrophils coordinate chemotaxis by differential activation of Rac1 and Rac2. J. Immunol. 183 2718-28 PubMed GONUTS page

[PMID:23533145-13] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:20926685-14] 14.0 ^14.1 Ito, S et al. (2010) The roles of two distinct regions of PINCH-1 in the regulation of cell attachment and spreading. Mol. Biol. Cell 21 4120-9 PubMed GONUTS page

[PMID:21423176-15] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:15121898-16] Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page

[PMID:28886345-17] Reijnders, MRF et al. (2017) RAC1 Missense Mutations in Developmental Disorders with Diverse Phenotypes. Am. J. Hum. Genet. 101 466-477 PubMed GONUTS page

[PMID:20458337-18] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:16636067-19] 19.0 ^19.1 ^19.2 ^19.3 Cheng, G et al. (2006) Nox1-dependent reactive oxygen generation is regulated by Rac1. J. Biol. Chem. 281 17718-26 PubMed GONUTS page

[PMID:16982892-20] Utsugi, M et al. (2006) Rac1 negatively regulates lipopolysaccharide-induced IL-23 p19 expression in human macrophages and dendritic cells and NF-kappaB p65 trans activation plays a novel role. J. Immunol. 177 4550-7 PubMed GONUTS page

[PMID:18156211-21] Dufourcq, P et al. (2008) Regulation of endothelial cell cytoskeletal reorganization by a secreted frizzled-related protein-1 and frizzled 4- and frizzled 7-dependent pathway: role in neovessel formation. Am. J. Pathol. 172 37-49 PubMed GONUTS page

[PMID:23129259-22] 22.0 ^22.1 ^22.2 Sayeed, S et al. (2013) S100A10 is required for the organization of actin stress fibers and promotion of cell spreading. Mol. Cell. Biochem. 374 105-11 PubMed GONUTS page

[PMID:19403692-23] Hamill, KJ et al. (2009) BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities. Mol. Biol. Cell 20 2954-62 PubMed GONUTS page

[PMID:12612085-24] Masuda-Robens, JM et al. (2003) The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol. Cell. Biol. 23 2151-61 PubMed GONUTS page

[PMID:22036506-25] 25.0 ^25.1 Torrino, S et al. (2011) The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1. Dev. Cell 21 959-65 PubMed GONUTS page

[PMID:19934221-26] Bristow, JM et al. (2009) The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration. J. Cell. Sci. 122 4535-46 PubMed GONUTS page

[PMID:9312003-27] 27.0 ^27.1 ^27.2 ^27.3 ^27.4 ^27.5 D'Souza-Schorey, C et al. (1997) A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. EMBO J. 16 5445-54 PubMed GONUTS page

[PMID:23633677-28] Borroni, EM et al. (2013) β-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6. Sci Signal 6 ra30.1-11, S1-3 PubMed GONUTS page

[PMID:15800193-29] 29.0 ^29.1 ^29.2 ^29.3 Zhang, H et al. (2005) A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC. J. Neurosci. 25 3379-88 PubMed GONUTS page

[PMID:21873635-30] 30.00 ^30.01 ^30.02 ^30.03 ^30.04 ^30.05 ^30.06 ^30.07 ^30.08 ^30.09 ^30.10 ^30.11 ^30.12 ^30.13 ^30.14 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:15467718-31] 31.0 ^31.1 ^31.2 Jacinto, E et al. (2004) Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6 1122-8 PubMed GONUTS page

[PMID:19890013-32] Kim, IH et al. (2009) Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaffold for synaptic Rac signaling. J. Neurosci. 29 14039-49 PubMed GONUTS page

[PMID:23620790-33] Chiang, YJ et al. (2013) CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration. PLoS ONE 8 e61761 PubMed GONUTS page

[PMID:12915445-34] Faucherre, A et al. (2003) Lowe syndrome protein OCRL1 interacts with Rac GTPase in the trans-Golgi network. Hum. Mol. Genet. 12 2449-56 PubMed GONUTS page

[PMID:9572733-35] 35.0 ^35.1 ^35.2 ^35.3 ^35.4 Kheradmand, F et al. (1998) Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280 898-902 PubMed GONUTS page

[PMID:2674130-36] Didsbury, J et al. (1989) rac, a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264 16378-82 PubMed GONUTS page

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