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Protein Page:
RAC1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RAC1 a plasma membrane-associated member of the Rho-GTPase family. Plays a key role in cytoskeletal reorganization, membrane trafficking, transcriptional regulation and cell growth and development. GTP binding stimulates its activity. Phosphorylation by Akt may inhibit GTP binding of Rac1, therefore attenuating the downstream signal transduction pathway. Found in a trimeric complex composed of DOCK1 and ELMO1, which plays a central role in phagocytosis of apoptotic cells. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric, Rho; Motility/polarity/chemotaxis; G protein, monomeric; G protein
Chromosomal Location of Human Ortholog: 7p22
Cellular Component: actin filament; cytoplasm; cytosol; endoplasmic reticulum membrane; focal adhesion; lamellipodium; membrane; plasma membrane; trans-Golgi network
Molecular Function: enzyme binding; GTP binding; GTPase activity; protein binding; Rho GDP-dissociation inhibitor binding; thioesterase binding
Biological Process: actin cytoskeleton organization and biogenesis; actin filament polymerization; anatomical structure morphogenesis; blood coagulation; cell adhesion; cell motility; cell motility involved in cell locomotion; ephrin receptor signaling pathway; inflammatory response; lamellipodium biogenesis; localization within membrane; negative regulation of interleukin-23 production; negative regulation of receptor-mediated endocytosis; platelet activation; positive regulation of apoptosis; positive regulation of focal adhesion formation; positive regulation of protein amino acid phosphorylation; positive regulation of Rho protein signal transduction; positive regulation of stress fiber formation; regulation of cell migration; regulation of cell size; regulation of defense response to virus by virus; regulation of hydrogen peroxide metabolic process; regulation of small GTPase mediated signal transduction; response to wounding; ruffle organization and biogenesis; T cell costimulation; vascular endothelial growth factor receptor signaling pathway; Wnt receptor signaling pathway, planar cell polarity pathway
Reference #:  P63000 (UniProtKB)
Alt. Names/Synonyms: Cell migration-inducing gene 5 protein; MGC111543; MIG5; migration-inducing gene 5; p21-Rac1; RAC1; Ras-like protein TC25; Ras-related C3 botulinum toxin substrate 1; ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1); rho family, small GTP binding protein Rac1; TC-25; TC25
Gene Symbols: RAC1
Molecular weight: 21,450 Da
Basal Isoelectric point: 8.77  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  Growth And Differentiation Control by MAPKs  |  Microtubule Dynamics  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-ß Signaling  |  Wnt/ß-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RAC1

Protein Structure Not Found.
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Sites Implicated In
cell adhesion, inhibited: Y64‑p
activity, inhibited: S71‑p
molecular association, regulation: Y64‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 Y32‑p TNAFPGEyIPTVFDN
1 0 Y32‑ad TNAFPGEyIPTVFDN
1 33 Y64‑p DTAGQEDyDRLRPLs
4 8 S71‑p yDRLRPLsYPQTDVF
0 1 T75 RPLsYPQTDVFLICF
0 1 - gap
0 4 K96‑ub SFENVRAkWYPEVRH
2 0 T108‑p VRHHCPNtPIILVGT
0 33 K116‑ub PIILVGTkLDLRDDk
0 2 K123‑ac kLDLRDDkDTIEKLK
0 7 K123‑ub kLDLRDDkDTIEKLK
0 1 K132 TIEKLKEKkLTPITY
0 1 K133 IEKLKEKKLTPITYP
0 13 K133‑ub IEKLKEKkLTPITYP
0 1 T135 KLKEKkLTPITYPQG
0 2 K147 PQGLAMAKEIGAVkY
2 31 K147‑ub PQGLAMAkEIGAVkY
0 1 K147‑sc PQGLAMAkEIGAVkY
0 1 K153 AkEIGAVKYLECSAL
0 3 K153‑ub AkEIGAVkYLECSAL
0 6 T161‑p YLECSALtQRGLktV
0 7 K166‑ub ALtQRGLktVFDEAI
0 17 T167‑p LtQRGLktVFDEAIR
0 30 K183‑ub VLCPPPVkkRKRKCL
0 23 K184‑ub LCPPPVkkRKRKCLL
2461 : Phospho-Rac1/cdc42 (Ser71) Antibody
  RAC1 iso2  
Y32 TNAFPGEYIPTVFDN
Y32 TNAFPGEYIPTVFDN
Y64‑p DTAGQEDyDRLRPLs
S71‑p yDRLRPLsYPQtVGE
T75‑p RPLsYPQtVGETyGK
Y80‑p PQtVGETyGKDITSR
K115 SFENVRAKWYPEVRH
T127 VRHHCPNTPIILVGT
K135 PIILVGTKLDLRDDK
K142 KLDLRDDKDTIEKLK
K142 KLDLRDDKDTIEKLK
K151 TIEKLKEKKLTPITY
K152 IEKLKEKKLTPITYP
K152 IEKLKEKKLTPITYP
T154 KLKEKKLTPITYPQG
K166 PQGLAMAKEIGAVKY
K166 PQGLAMAKEIGAVKY
K166 PQGLAMAKEIGAVKY
K172 AKEIGAVKYLECSAL
K172 AKEIGAVKYLECSAL
T180 YLECSALTQRGLKTV
K185 ALTQRGLKTVFDEAI
T186 LTQRGLKTVFDEAIR
K202 VLCPPPVKKRKRKCL
K203 LCPPPVKKRKRKCLL
  mouse

 
Y32 TNAFPGEYIPTVFDN
Y32 TNAFPGEYIPTVFDN
Y64 DTAGQEDYDRLRPLS
S71 YDRLRPLSYPQTDVF
T75 RPLSYPQTDVFLICF
- gap
K96‑ub SFENVRAkWYPEVRH
T108 VRHHCPNTPIILVGT
K116‑ub PIILVGTkLDLRDDk
K123 kLDLRDDKDTIEKLK
K123‑ub kLDLRDDkDTIEKLK
K132‑ac TIEKLKEkkLtPITY
K133‑ac IEKLKEkkLtPITYP
K133‑ub IEKLKEkkLtPITYP
T135‑p KLKEkkLtPITYPQG
K147 PQGLAMAKEIGAVkY
K147‑ub PQGLAMAkEIGAVkY
K147 PQGLAMAKEIGAVkY
K153 AkEIGAVKYLECSAL
K153‑ub AkEIGAVkYLECSAL
T161‑p YLECSALtQRGLktV
K166‑ub ALtQRGLktVFDEAI
T167‑p LtQRGLktVFDEAIR
K183‑ub VLCPPPVkkRKRKCL
K184‑ub LCPPPVkkRKRKCLL
2461 : Phospho-Rac1/cdc42 (Ser71) Antibody
  rat

 
Y32 TNAFPGEYIPTVFDN
Y32 TNAFPGEYIPTVFDN
Y64 DTAGQEDYDRLRPLS
S71 YDRLRPLSYPQTDVF
T75 RPLSYPQTDVFLICF
- gap
K96 SFENVRAKWYPEVRH
T108 VRHHCPNTPIILVGT
K116‑ub PIILVGTkLDLRDDk
K123‑ac kLDLRDDkDTIEKLK
K123‑ub kLDLRDDkDTIEKLK
K132 TIEKLKEKKLTPITY
K133 IEKLKEKKLTPITYP
K133 IEKLKEKKLTPITYP
T135 KLKEKKLTPITYPQG
K147‑ac PQGLAMAkEIGAVkY
K147‑ub PQGLAMAkEIGAVkY
K147 PQGLAMAKEIGAVkY
K153‑ac AkEIGAVkYLECSAL
K153 AkEIGAVKYLECSAL
T161 YLECSALTQRGLKtV
K166 ALTQRGLKtVFDEAI
T167‑p LTQRGLKtVFDEAIR
K183‑ub VLCPPPVkkRKRKCL
K184‑ub LCPPPVkkRKRKCLL
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