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PAK1 (human)

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; Kinase, protein; EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); STE group; STE20 family; PAKA subfamily Cellular Component: Golgi apparatus; nuclear membrane; focal adhesion; protein complex; dendrite; intercellular junction; cytosol; Z disc; filamentous actin; ruffle; growth cone; axon; cytoplasm; plasma membrane Molecular Function: collagen binding; identical protein binding; protein serine/threonine kinase activity; protein binding; protein kinase binding; ATP binding; protein kinase activity Biological Process: axon guidance; positive regulation of JNK activity; wound healing; apoptosis; protein amino acid autophosphorylation; cellular response to stress; positive regulation of estrogen receptor signaling pathway; MAPKKK cascade; receptor clustering; protein amino acid phosphorylation; T cell receptor signaling pathway; positive regulation of peptidyl-serine phosphorylation; branching morphogenesis of a tube; cellular response to insulin stimulus; positive regulation of stress fiber formation; T cell costimulation; actin cytoskeleton reorganization; dendrite development; response to hypoxia; neurite morphogenesis; neuromuscular junction development 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:  ErbB/HER Signaling  |  MAPK/Erk in Growth and Differentiation  |  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics  |  TGF-ß Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PAK1 1F3M - A/B=70-149, C/D=249-545 (human) 1YHV - A=249-545 (human) 1YHW - A=249-545 (human) 1ZSG - B=183-204 (human) 2HY8 - 1=249-545 (human) 2QME - I=74-109 (human) 3DVP - D/C=212-221 (human) 3FXZ - A=249-545 (human) 3FY0 - A=249-545 (human) 3Q4Z - A/B=248-545 (human) 3Q52 - A=248-545 (human) 3Q53 - A=248-545 (human) 4DAW - A=249-545 (human) 1E0A - B=75-118 (rat) Substrate Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1F3M 1YHV 1YHW 1ZSG 2HY8 2QME 3DVP 3FXZ 3FY0 3Q4Z 3Q52 3Q53 4DAW  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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, Y285‑p cytoskeletal reorganization: S21‑p, S144‑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 molecular association, regulation: S174‑p, T423‑p protein conformation: S199‑p, S204‑p, T423‑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

SS  SS: 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.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		T20-p	PAPPMRNtsTMIGAG
3	10		S21-p	APPMRNtsTMIGAGS
0	1		K29-a	TMIGAGSkDAGTLNH
1	0		T84	LPSDFEHTIHVGFDA
1	1		T109-p	QWARLLQtSNITKsE
0	3		S115-p	QtSNITKsEQKKNPQ
0	7		Y131-p	VLDVLEFyNsKKtsN
0	2		S133-p	DVLEFyNsKKtsNsQ
0	2		T136-p	EFyNsKKtsNsQKyM
0	2		S137-p	FyNsKKtsNsQKyMs
0	4		S139-p	NsKKtsNsQKyMsFt
0	13		Y142-p	KtsNsQKyMsFtDKs
7	137		S144-p	sNsQKyMsFtDKsAE
0	15		T146-p	sQKyMsFtDKsAEDy
1	25		S149-p	yMsFtDKsAEDyNss
4	23		Y153-p	tDKsAEDyNssNALN
0	4		S155-p	KsAEDyNssNALNVK
0	1		S156-p	sAEDyNssNALNVKA
0	1		A158	EDyNssNALNVKAVS
1	8		S174-p	TPAVPPVsEDEDDDD
0	6		T185-p	DDDDDDAtPPPVIAP
12	0		S199-p	PRPEHTKsVyTRsVI
4	0		Y201-p	PEHTKsVyTRsVIEP
10	6		S204-p	TKsVyTRsVIEPLPV
8	28		T212-p	VIEPLPVtPtRDVAt
0	4		T214-p	EPLPVtPtRDVAtsP
0	2		T219-p	tPtRDVAtsPIsPtE
0	9		S220-p	PtRDVAtsPIsPtEN
0	18		S223-p	DVAtsPIsPtENNtt
0	10		T225-p	AtsPIsPtENNttPP
0	8		T229-p	IsPtENNttPPDALt
0	30		T230-p	sPtENNttPPDALtR
0	2		T236-p	ttPPDALtRNTEKQK
0	1		K256-a	SDEEILEkLRSIVSV
0	1		K256-u	SDEEILEkLRSIVSV
4	2		Y285-p	QGASGTVyTAMDVAT
0	1		K420-a	QITPEQSkRstMVGt
0	10		K420-u	QITPEQSkRstMVGt
0	3		S422-p	TPEQSkRstMVGtPY
22	10		T423-p	PEQSkRstMVGtPYW
0	3		T427-p	kRstMVGtPYWMAPE
0	9		Y474-p	ENPLRALyLIATNGT
0	1		S491-p	LQNPEKLsAIFRDFL
0	1		K513-a	VEKRGSAkELLQHQF
0	1		S528-p	LKIAKPLssLtPLIA
0	1		S529-p	KIAKPLssLtPLIAA
0	1		T531-p	AKPLssLtPLIAAAK

	mouse
T20	PAPPMRNTsTMIGAG
S21-p	APPMRNTsTMIGAGS
K29	TMIGAGSKDTGTLNH
T84	LPSDFEHTIHVGFDA
T109-p	QWARLLQtSNITKsE
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
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
K256	SDEEILEKLRSIVSV
K256	SDEEILEKLRSIVSV
Y285	QGASGTVYTAMDVAT
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

	rat
T20	PAPPMRNTsTMIGAG
S21-p	APPMRNTsTMIGAGS
K29	TMIGAGSKDPGTLNH
T84-p	LPSDFEHtIHVGFDA
T109	QWARLLQTSNITKSE
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	TPAVPPVSEDEDDDD
T184	EDDDDDATPPPVIAP
S198-p	PRPEHTKsVYTRsVI
Y200	PEHTKsVYTRsVIEP
S203-p	TKsVYTRsVIEPLPV
T211-p	VIEPLPVtPTRDVAT
T213	EPLPVtPTRDVATSP
T218	tPTRDVATSPISPTE
S219	PTRDVATSPISPTEN
S222	DVATSPISPTENNTT
T224	ATSPISPTENNTTPP
T228	ISPTENNTTPPDALT
T229	SPTENNTTPPDALTR
T235	TTPPDALTRNTEKQK
K255	SDEEILEKLRSIVSV
K255	SDEEILEKLRSIVSV
Y284	QGASGTVYTAMDVAT
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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