Reviewed, UniProtKB/Swiss-Prot Q13153 (PAK1_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase PAK 1
    EC=2.7.11.1
Alternative name(s):
    p21-activated kinase 1
      Short name=PAK-1
    p65-PAK
    Alpha-PAK

Gene names

Name:

PAK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The activated kinase acts on a variety of targets. Likely to be the GTPase effector that links the Rho-related GTPases to the JNK MAP kinase pathway. Activated by CDC42 and RAC1. Involved in dissolution of stress fibers and reorganization of focal complexes. Involved in regulation of microtubule biogenesis through phosphorylation of TBCB. Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Ref.7 Ref.10 Ref.11 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-423 and allows the kinase domain to adopt an active structure. Also activated by binding to GTP-bound CDC42, independent of the phosphorylation state of Thr-423. Phosphorylation of Thr-84 by OXSR1 inhibits this activation By similarity. Ref.5 Ref.9 Ref.23
Subunit structure	Homodimer in its autoinhibited state. Active as monomer. Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1. Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and GIT1. Interacts with ARHGEF7. Also interacts with CRIPAK. Interacts with NISCH By similarity. Interacts with SCRIB. Ref.10 Ref.13 Ref.9 Ref.16
Subcellular location	Cytoplasm. Cell junction › focal adhesion. Note: Recruited to focal adhesions upon activation. Ref.5
Post-translational modification	Autophosphorylated when activated by CDC42/p21 and RAC1. Ref.8 Ref.12 Ref.14 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 CRIB domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell junction Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	ER-nuclear signaling pathway Ref.13 Traceable author statement. Source: HGNC apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton organization Ref.13 Traceable author statement. Source: HGNC positive regulation of JUN kinase activity Ref.1 Inferred from mutant phenotype. Source: UniProtKB protein amino acid autophosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from Experiment. Source: Reactome focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW collagen binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Ref.13 Traceable author statement. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC2L1	P21127	2	EBI-1307,EBI-1298
CDC42	P60953	2	EBI-1307,EBI-81752
Cdc42	P60766	1	EBI-1307,EBI-81763	From a different organism.
CRIPAK	Q8N1N5	5	EBI-1307,EBI-1205846
RAC1	P63000	3	EBI-1307,EBI-413628
Rac1	P63001	1	EBI-1307,EBI-413646	From a different organism.
RHOU	Q7L0Q8	1	EBI-1019502,EBI-1638043
RHOU	Q7L0Q8	1	EBI-1307,EBI-1638043

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13153-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13153-2)

Also known as: PAK1B;

The sequence of this isoform differs from the canonical sequence as follows:
     518-545: HQFLKIAKPLSSLTPLIAAAKEATKNNH → VRKLRFQVFSNFSMIAASIPEDCQAPLQPHSTDCCS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 545

545

Serine/threonine-protein kinase PAK 1

PRO_0000086460

Regions

Domain

75 – 88

14

CRIB

Domain

270 – 521

252

Protein kinase

Nucleotide binding

276 – 284

9

ATP By similarity

Region

70 – 140

71

Autoregulatory region

Region

75 – 105

31

GTPase-binding By similarity

Region

132 – 270

139

Interaction with CRIPAK

Sites

Active site

389

1

Proton acceptor

Binding site

299

1

ATP By similarity

Amino acid modifications

Modified residue

21

1

Phosphoserine; by autocatalysis By similarity

Modified residue

57

1

Phosphoserine; by autocatalysis By similarity

Modified residue

84

1

Phosphothreonine; by OXSR1 By similarity

Modified residue

144

1

Phosphoserine; by autocatalysis By similarity

Modified residue

149

1

Phosphoserine; by autocatalysis By similarity

Modified residue

199

1

Phosphoserine; by autocatalysis By similarity

Modified residue

204

1

Phosphoserine; by autocatalysis By similarity

Modified residue

212

1

Phosphothreonine Ref.12 Ref.17 Ref.19

Modified residue

219

1

Phosphothreonine Ref.19

Modified residue

220

1

Phosphoserine Ref.19

Modified residue

223

1

Phosphoserine By similarity

Modified residue

225

1

Phosphothreonine Ref.17

Modified residue

229

1

Phosphothreonine Ref.17

Modified residue

230

1

Phosphothreonine Ref.14 Ref.17 Ref.19

Modified residue

256

1

N6-acetyllysine Ref.20

Modified residue

423

1

Phosphothreonine; by autocatalysis Probable

Modified residue

474

1

Phosphotyrosine Ref.18

Natural variations

Alternative sequence

518 – 545

28

HQFLK…TKNNH → VRKLRFQVFSNFSMIAASIP EDCQAPLQPHSTDCCS in isoform 2.

VSP_017507

Natural variant

515

1

L → V: dbSNP rs35345144.

VAR_051654

Experimental info

Mutagenesis

83

1

H → L: Decreases activity; when associated with L-86. Ref.6

Mutagenesis

86

1

H → L: Decreases activity; when associated with L-83. Ref.6

Mutagenesis

107

1

L → F: Constitutively active.

Mutagenesis

423

1

T → A: Decreases CDC42-stimulated activity and autophosphorylation. Ref.8

Sequence conflict

26

1

A → V in AAA65441. Ref.2

Sequence conflict

26

1

A → V in AAC24716. Ref.3

Sequence conflict

237

1

R → L in AAC50590. Ref.1

Sequence conflict

379

1

F → S in AAC50590. Ref.1

Sequence conflict

503

1

E → D in AAA65441. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

545

Helix Strand Turn

Details...

Beta strand

80 – 90

11

Turn

91 – 94

4

Beta strand

95 – 98

4

Helix

101 – 108

8

Helix

114 – 119

6

Helix

121 – 135

15

Beta strand

195 – 198

4

Helix

252 – 257

6

Turn

258 – 260

3

Helix

266 – 269

4

Beta strand

275 – 279

5

Beta strand

282 – 289

8

Turn

290 – 292

3

Beta strand

295 – 300

6

Helix

309 – 319

11

Beta strand

330 – 334

5

Beta strand

341 – 345

5

Beta strand

349 – 351

3

Helix

352 – 358

7

Helix

363 – 382

20

Helix

392 – 394

3

Beta strand

395 – 397

3

Beta strand

403 – 405

3

Beta strand

408 – 410

3

Helix

433 – 436

4

Helix

444 – 459

16

Turn

463 – 466

4

Helix

469 – 478

10

Helix

487 – 489

3

Helix

492 – 501

10

Turn

506 – 508

3

Helix

512 – 515

4

Helix

519 – 523

5

Helix

527 – 529

3

Helix

531 – 539

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 1A95CD5F2195CD7B	FASTA	545	60,647
	10 20 30 40 50 60 MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK KDRFYRSILP 70 80 90 100 110 120 GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP EQWARLLQTS NITKSEQKKN 130 140 150 160 170 180 PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA EDYNSSNALN VKAVSETPAV PPVSEDEDDD 190 200 210 220 230 240 DDDATPPPVI APRPEHTKSV YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE 250 260 270 280 290 300 KQKKKPKMSD EEILEKLRSI VSVGDPKKKY TRFEKIGQGA SGTVYTAMDV ATGQEVAIKQ 310 320 330 340 350 360 MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG SLTDVVTETC 370 380 390 400 410 420 MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD GSVKLTDFGF CAQITPEQSK 430 440 450 460 470 480 RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL GIMAIEMIEG EPPYLNENPL RALYLIATNG 490 500 510 520 530 540 TPELQNPEKL SAIFRDFLNR CLEMDVEKRG SAKELLQHQF LKIAKPLSSL TPLIAAAKEA TKNNH
	Isoform 2 (PAK1B). Checksum: 6A3BB134DD2A82A8	FASTA	553	61,632
	10 20 30 40 50 60 MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK KDRFYRSILP 70 80 90 100 110 120 GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP EQWARLLQTS NITKSEQKKN 130 140 150 160 170 180 PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA EDYNSSNALN VKAVSETPAV PPVSEDEDDD 190 200 210 220 230 240 DDDATPPPVI APRPEHTKSV YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE 250 260 270 280 290 300 KQKKKPKMSD EEILEKLRSI VSVGDPKKKY TRFEKIGQGA SGTVYTAMDV ATGQEVAIKQ 310 320 330 340 350 360 MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG SLTDVVTETC 370 380 390 400 410 420 MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD GSVKLTDFGF CAQITPEQSK 430 440 450 460 470 480 RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL GIMAIEMIEG EPPYLNENPL RALYLIATNG 490 500 510 520 530 540 TPELQNPEKL SAIFRDFLNR CLEMDVEKRG SAKELLQVRK LRFQVFSNFS MIAASIPEDC 550 QAPLQPHSTD CCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway." Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J. Curr. Biol. 6:598-605(1996) [PubMed: 8805275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells." Sells M.A., Knaus U.G., Bagrodia S., Ambrose D.M., Bokoch G.M., Chernoff J. Curr. Biol. 7:202-210(1997) [PubMed: 9395435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Human PAK1B." Reid T., Aspenstroem P., Bertoglio J. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes." Manser E., Huang H.Y., Loo T.H., Chen X.Q., Dong J.M., Leung T., Lim L. Mol. Cell. Biol. 17:1129-1143(1997) [PubMed: 9032240] [Abstract] Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
[6]	"Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation." Frost J.A., Khokhlatchev A., Stippec S., White M.A., Cobb M.H. J. Biol. Chem. 273:28191-28198(1998) [PubMed: 9774440] [Abstract] Cited for: MUTAGENESIS OF HIS-83 AND HIS-86.
[7]	"A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1." Zhao Z.S., Manser E., Chen X.Q., Chong C., Leung T., Lim L. Mol. Cell. Biol. 18:2153-2163(1998) [PubMed: 9528787] [Abstract] Cited for: FUNCTION, AUTOREGULATORY DOMAIN.
[8]	"Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity." Zenke F.T., King C.C., Bohl B.P., Bokoch G.M. J. Biol. Chem. 274:32565-32573(1999) [PubMed: 10551809] [Abstract] Cited for: PHOSPHORYLATION AT THR-423, MUTAGENESIS OF THR-423.
[9]	"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1." Parrini M.C., Lei M., Harrison S.C., Mayer B.J. Mol. Cell 9:73-83(2002) [PubMed: 11804587] [Abstract] Cited for: DIMERIZATION, ENZYME REGULATION.
[10]	"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis." Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H., Hu Y., Yuan Z., Shen Z., Gu J. J. Biol. Chem. 278:20029-20036(2003) [PubMed: 12624090] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDC2L1 AND CDC2L2.
[11]	"p21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor B." Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S., Marcus S., Goodson H.V., Sahin A.A., Kumar R. Mol. Cell. Biol. 25:3726-3736(2005) [PubMed: 15831477] [Abstract] Cited for: FUNCTION.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"CRIPak, a novel endogenous Pak1 inhibitor." Talukder A.H., Meng Q., Kumar R. Oncogene 25:1311-1319(2006) [PubMed: 16278681] [Abstract] Cited for: FUNCTION, INTERACTION WITH CRIPAK.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Scrib regulates PAK activity during the cell migration process." Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S., Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S., Borg J.-P., Santoni M.-J. Hum. Mol. Genet. 17:3552-3565(2008) [PubMed: 18716323] [Abstract] Cited for: INTERACTION WITH SCRIB.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-225; THR-229 AND THR-230, MASS SPECTROMETRY.
[18]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-474, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-204; THR-212; THR-219; SER-220 AND THR-230, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, MASS SPECTROMETRY.
[21]	"Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch." Lei M., Lu W., Meng W., Parrini M.C., Eck M.J., Mayer B.J., Harrison S.C. Cell 102:387-397(2000) [PubMed: 10975528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 70-545.
[22]	"Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)." Mott H.R., Nietlispach D., Evetts K.A., Owen D. Biochemistry 44:10977-10983(2005) [PubMed: 16101281] [Abstract] Cited for: STRUCTURE BY NMR OF 183-204 IN COMPLEX WITH ARHGEF7.
[23]	"The active conformation of the PAK1 kinase domain." Lei M., Robinson M.A., Harrison S.C. Structure 13:769-778(2005) [PubMed: 15893667] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-545, ENZYME REGULATION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U51120 mRNA. Translation: AAC50590.1.
U24152 mRNA. Translation: AAA65441.1.
AF071884 mRNA. Translation: AAC24716.1.
BC109299 mRNA. Translation: AAI09300.1.

IPI

IPI00289746.
IPI00656138.

PIR

G01773.

RefSeq

NP_001122092.1.
NP_002567.3.

UniGene

Hs.435714

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F3M	X-ray	2.30	A/B	70-149	[»]
			C/D	249-545	[»]
1YHV	X-ray	1.80	A	249-545	[»]
1YHW	X-ray	1.80	A	249-545	[»]
1ZSG	NMR	-	B	183-204	[»]
2HY8	X-ray	2.00	1	249-545	[»]
2QME	X-ray	1.75	I	74-109	[»]
3DVP	X-ray	2.50	C/D	212-221	[»]
3FXZ	X-ray	1.64	A	249-545	[»]
3FY0	X-ray	2.35	A	249-545	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13153. 11 interactions.

STRING

Q13153.

PTM databases

PhosphoSite

Q13153.

Proteomic databases

PRIDE

Q13153.

Genome annotation databases

Ensembl

ENST00000356341; ENSP00000348696; ENSG00000149269; Homo sapiens. [Genome view]

GeneID

5058.

KEGG

hsa:5058.

UCSC

uc001oyg.2. human.
uc001oyh.2. human.

Organism-specific databases

CTD

5058.

GeneCards

GC11M076710.

H-InvDB

HIX0009965.

HGNC

HGNC:8590. PAK1.

HPA

CAB005312.
HPA003565.

MIM

602590. gene.

PharmGKB

PA32917.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16871.

HOVERGEN

Q13153.

OMA

EATKNNH.

OrthoDB

EOG9N8TQ5.

PhylomeDB

Q13153.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
aurora_a_pathway. Aurora A signaling.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
s1p_s1p2_pathway. S1P2 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Reactome

REACT_18266. Axon guidance.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

Q13153.

Bgee

Q13153.

CleanEx

HS_PAK1.

Genevestigator

Q13153.

GermOnline

ENSG00000149269. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR015750. Ser/Thr_kinase_Pak-rel.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

PANTHER

PTHR22986:SF84. Pak_like. 1 hit.

Pfam

PF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

19488.

SOURCE

Search...

Entry information

Entry name

PAK1_HUMAN

Accession

Primary (citable) accession number: Q13153
Secondary accession number(s): O75561 , Q13567, Q32M53, Q32M54, Q86W79

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.