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Protein Page:
PAK1 (human)
rdtyret
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
PAK1 a protein kinase of the STE20 family that regulates cell motility and morphology. Critical RhoGTPase effector that regulates cytoskeleton reorganization, the JNK MAPK pathway, and nuclear signaling. Binding of Rac/cdc42 to the PBD of PAK1 causes autophosphorylation and conformational change. Phosphorylated and activated by PDK. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, STE; Protein kinase, Ser/Thr (non-receptor); Kinase, protein; EC 2.7.11.1; STE group; STE20 family; PAKA subfamily
Chromosomal Location of Human Ortholog: 11q13-q14
Cellular Component: axon; cytoplasm; cytosol; dendrite; filamentous actin; focal adhesion; Golgi apparatus; growth cone; intercellular junction; nuclear membrane; plasma membrane; protein complex; ruffle; Z disc
Molecular Function: ATP binding; collagen binding; protein binding; protein kinase activity; protein kinase binding; protein serine/threonine kinase activity; Rac GTPase binding
Biological Process: actin cytoskeleton reorganization; activation of protein kinase activity; amygdala development; apoptosis; axon guidance; branching morphogenesis of a tube; cell migration; cellular response to insulin stimulus; ephrin receptor signaling pathway; exocytosis; innate immune response; MAPKKK cascade; neurite morphogenesis; neuromuscular junction development; positive regulation of cell migration; positive regulation of estrogen receptor signaling pathway; positive regulation of JNK activity; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of stress fiber formation; protein amino acid autophosphorylation; protein amino acid phosphorylation; receptor clustering; regulation of apoptosis; regulation of gene expression; regulation of mitotic cell cycle; response to hypoxia; Rho protein signal transduction; small GTPase mediated signal transduction; stimulatory C-type lectin receptor signaling pathway; stress-activated protein kinase signaling pathway; T cell costimulation; T cell receptor signaling pathway; vascular endothelial growth factor receptor signaling pathway; wound healing
Reference #:  Q13153 (UniProtKB)
Alt. Names/Synonyms: Alpha-PAK; MGC130000; MGC130001; p21 protein (Cdc42/Rac)-activated kinase 1; p21-activated kinase 1; p21/Cdc42/Rac1-activated kinase 1 (STE20 homolog, yeast); p21/Cdc42/Rac1-activated kinase 1 (yeast Ste20-related); p65-PAK; PAK-1; PAK1; PAKalpha; Serine/threonine-protein kinase PAK 1; STE20 homolog, yeast
Gene Symbols: PAK1
Molecular weight: 60,647 Da
Basal Isoelectric point: 5.55  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  ErbB/HER Signaling  |  Growth And Differentiation Control by MAPKs  |  Microtubule Dynamics  |  TGF-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PAK1

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
apoptosis, altered: Y153‑p, Y201‑p, Y285‑p
cell adhesion, altered: S199‑p, S204‑p
cell cycle regulation: S174‑p
cell motility, altered: Y153‑p, S199‑p, Y201‑p, S204‑p, Y285‑p
cell motility, induced: Y153‑p, Y201‑p, S223‑p, Y285‑p
cytoskeletal reorganization: S21‑p, S144‑p
activity, induced: S223‑p
enzymatic activity, induced: S144‑p, Y153‑p, S174‑p, S199‑p, Y201‑p, S204‑p, Y285‑p, T423‑p
enzymatic activity, inhibited: T109‑p
intracellular localization: S21‑p, S144‑p, S199‑p, S204‑p, S223‑p
molecular association, regulation: S174‑p, T423‑p
protein conformation: S199‑p, S204‑p, T423‑p

Modification Sites and Domains  
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Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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

 
0 1 S2‑p ______MsNNGLDIQ
0 1 T20‑p PAPPMRNtsTMIGAG
3 10 S21‑p APPMRNtsTMIGAGS
0 2 K29‑ac TMIGAGSkDAGTLNH
0 1 K63‑ac RSILPGDkTNKKKEK
1 0 T84 LPSDFEHTIHVGFDA
1 1 T109‑p QWARLLQtsNITKsE
0 1 S110‑p WARLLQtsNITKsEQ
0 6 S115‑p QtsNITKsEQKKNPQ
0 8 Y131‑p VLDVLEFyNsKKtsN
0 2 S133‑p DVLEFyNsKKtsNsQ
0 5 T136‑p EFyNsKKtsNsQKyM
0 2 S137‑p FyNsKKtsNsQKyMs
0 8 S139‑p NsKKtsNsQKyMsFt
0 17 Y142‑p KtsNsQKyMsFtDKs
13 160 S144‑p sNsQKyMsFtDKsAE
0 15 T146‑p sQKyMsFtDKsAEDy
1 32 S149‑p yMsFtDKsAEDyNss
6 22 Y153‑p tDKsAEDyNssNALN
0 5 S155‑p KsAEDyNssNALNVK
0 1 S156‑p sAEDyNssNALNVKA
0 1 A158 EDyNssNALNVKAVS
1 23 S174‑p TPAVPPVsEDEDDDD
0 8 T185‑p DDDDDDAtPPPVIAP
0 1 T197‑p IAPRPEHtKsVyTRs
13 0 S199‑p PRPEHtKsVyTRsVI
6 0 Y201‑p PEHtKsVyTRsVIEP
11 10 S204‑p tKsVyTRsVIEPLPV
10 34 T212‑p VIEPLPVtPtRDVAt
0 6 T214‑p EPLPVtPtRDVAtsP
0 4 T219‑p tPtRDVAtsPIsPtE
0 13 S220‑p PtRDVAtsPIsPtEN
2 24 S223‑p DVAtsPIsPtENNtt
0 13 T225‑p AtsPIsPtENNttPP
0 11 T229‑p IsPtENNttPPDALt
0 38 T230‑p sPtENNttPPDALtR
0 2 T236‑p ttPPDALtRNTEKQK
0 1 S249 QKKKPKMSDEEILEk
0 1 K256‑ac SDEEILEkLRSIVsV
0 1 K256‑ub SDEEILEkLRSIVsV
0 1 S259 EILEkLRSIVsVGDP
0 2 S262‑p EkLRSIVsVGDPKKK
6 2 Y285‑p QGASGTVyTAMDVAT
0 1 T415‑p FGFCAQItPEQSkRs
0 1 K420‑ac QItPEQSkRstMVGt
0 11 K420‑ub QItPEQSkRstMVGt
0 4 S422‑p tPEQSkRstMVGtPY
28 11 T423‑p PEQSkRstMVGtPYW
0 4 T427‑p kRstMVGtPYWMAPE
0 9 Y474‑p ENPLRALyLIATNGT
0 1 S491‑p LQNPEKLsAIFRDFL
0 1 K513‑ac VEKRGSAkELLQHQF
0 1 S528‑p LKIAKPLssLtPLIA
0 1 S529‑p KIAKPLssLtPLIAA
0 1 T531‑p AKPLssLtPLIAAAK
2606 : Phospho-PAK1 (Ser144)/PAK2 (Ser141) Antibody
2605 : Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody
2605 : Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody
2601 : Phospho-PAK1 (Thr423)/PAK2 (Thr402) Antibody
  mouse

 
S2 ______MSNNGVDIQ
T20 PAPPMRNTsTMIGAG
S21‑p APPMRNTsTMIGAGS
K29 TMIGAGSKDTGTLNH
K63 RSILPGDKTNKKREK
T84 LPSDFEHTIHVGFDA
T109‑p QWARLLQtSNITKsE
S110 WARLLQtSNITKsEQ
S115‑p QtSNITKsEQKKNPQ
Y131 VLDVLEFYNSKKTSN
S133 DVLEFYNSKKTSNSK
T136 EFYNSKKTSNSKKYM
S137 FYNSKKTSNSKKYMs
S139 NSKKTSNSKKYMsFT
Y142 KTSNSKKYMsFTDKS
S144‑p SNSKKYMsFTDKSAE
T146 SKKYMsFTDKSAEDY
S149 YMsFTDKSAEDYNSS
Y153 TDKSAEDYNSSNtLN
S155 KSAEDYNSSNtLNVK
S156 SAEDYNSSNtLNVKT
T158‑p EDYNSSNtLNVKTVS
S174‑p TPAVPPVsEDDEDDD
T185‑p EDDDDDAtPPPVIAP
T197 IAPRPEHTKsVYTRs
S199‑p PRPEHTKsVYTRsVI
Y201 PEHTKsVYTRsVIEP
S204‑p TKsVYTRsVIEPLPV
T212‑p VIEPLPVtPtRDVAt
T214‑p EPLPVtPtRDVAtsP
T219‑p tPtRDVAtsPIsPtE
S220‑p PtRDVAtsPIsPtEN
S223‑p DVAtsPIsPtENNtt
T225‑p AtsPIsPtENNttPP
T229‑p IsPtENNttPPDALT
T230‑p sPtENNttPPDALTR
T236 ttPPDALTRNTEKQK
S249‑p QKKKPKMsDEEILEK
K256 sDEEILEKLRsIVsV
K256 sDEEILEKLRsIVsV
S259‑p EILEKLRsIVsVGDP
S262‑p EKLRsIVsVGDPKKK
Y285 QGASGTVYTAMDVAT
T415 FGFCAQITPEQSKRs
K420 QITPEQSKRstMVGt
K420 QITPEQSKRstMVGt
S422‑p TPEQSKRstMVGtPY
T423‑p PEQSKRstMVGtPYW
T427‑p KRstMVGtPYWMAPE
Y474 ENPLRALYLIATNGT
S491 LQNPEKLSAIFRDFL
K513 VEKRGSAKELLQHQF
S528 LKIAKPLSSLTPLMH
S529 KIAKPLSSLTPLMHA
T531 AKPLSSLTPLMHAAK
2606 : Phospho-PAK1 (Ser144)/PAK2 (Ser141) Antibody
2605 : Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody
2605 : Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody
2601 : Phospho-PAK1 (Thr423)/PAK2 (Thr402) Antibody
  rat

 
S2 ______MSNNGLDVQ
T20 PAPPMRNTsTMIGAG
S21‑p APPMRNTsTMIGAGS
K29 TMIGAGSKDPGTLNH
K63 RSILAGDKTNKKKEK
T84‑p LPSDFEHtIHVGFDA
T109 QWARLLQTSNITKSE
S110 WARLLQTSNITKSEQ
S115 QTSNITKSEQKKNPQ
Y131 VLDVLEFYNSKKTSN
S133 DVLEFYNSKKTSNSQ
T136 EFYNSKKTSNSQKYM
S137 FYNSKKTSNSQKYMs
S139 NSKKTSNSQKYMsFT
Y142 KTSNSQKYMsFTDKs
S144‑p SNSQKYMsFTDKsAE
T146 SQKYMsFTDKsAEDY
S149‑p YMsFTDKsAEDYNSS
Y153 TDKsAEDYNSSNTLN
S155 KsAEDYNSSNTLNVK
S156 sAEDYNSSNTLNVKT
T158 EDYNSSNTLNVKTVS
S174‑p TPAVPPVsEDEDDDD
T184 EDDDDDATPPPVIAP
T196 IAPRPEHTKsVYTRs
S198‑p PRPEHTKsVYTRsVI
Y200 PEHTKsVYTRsVIEP
S203‑p TKsVYTRsVIEPLPV
T211‑p VIEPLPVtPTRDVAT
T213 EPLPVtPTRDVATsP
T218 tPTRDVATsPIsPTE
S219‑p PTRDVATsPIsPTEN
S222‑p DVATsPIsPTENNTt
T224 ATsPIsPTENNTtPP
T228 IsPTENNTtPPDALT
T229‑p sPTENNTtPPDALTR
T235 TtPPDALTRNTEKQK
S248 QKKKPKMSDEEILEK
K255 SDEEILEKLRSIVSV
K255 SDEEILEKLRSIVSV
S258 EILEKLRSIVSVGDP
S261 EKLRSIVSVGDPKKK
Y284 QGASGTVYTAMDVAT
T414 FGFCAQITPEQSKRs
K419 QITPEQSKRstMVGT
K419 QITPEQSKRstMVGT
S421‑p TPEQSKRstMVGTPY
T422‑p PEQSKRstMVGTPYW
T426 KRstMVGTPYWMAPE
Y473 ENPLRALYLIATNGT
S490 LQNPEKLSAIFRDFL
K512 VEKRGSAKELLQHQF
S527 LKIAKPLSSLTPLIA
S528 KIAKPLSSLTPLIAA
T530 AKPLSSLTPLIAAAK
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