Q13177 (PAK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PAK 2
EC=2.7.11.1

Alternative name(s):
Gamma-PAK
PAK65
S6/H4 kinase
p21-activated kinase 2
Short name=PAK-2
p58

Cleaved into the following 2 chains:

1. PAK-2p27
   Short name=p27
2. PAK-2p34
   Short name=p34
   Alternative name(s):
   C-t-PAK2

Gene names

Name:

PAK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation. Ref.6 Ref.9 Ref.10 Ref.14 Ref.21 Ref.25 Ref.26 Ref.27
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
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-402 and allows the kinase domain to adopt an active structure By similarity. Following caspase cleavage, autophosphorylated PAK-2p34 is constitutively active.
Subunit structure	Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with SH3MD4. Interacts with and activated by HIV-1 Nef. Interacts with SCRIB. Interacts with ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10. Ref.8 Ref.11 Ref.13 Ref.15 Ref.18
Subcellular location	Serine/threonine-protein kinase PAK 2: Cytoplasm. Note: MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. Ref.9 Ref.11 Ref.14 Ref.21 PAK-2p34: Nucleus. Cytoplasm › perinuclear region. Membrane; Lipid-anchor. Note: Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane. Ref.9 Ref.11 Ref.14 Ref.21
Tissue specificity	Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.
Post-translational modification	Full length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated, with PAK-2p27 being phosphorylated on serine and PAK-2p34 on threonine residues, respectively. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate. Ref.5 Ref.7 Ref.24 During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34. Ref.6 Ref.7 Ubiquitinated, leading to its proteasomal degradation. Ref.9 PAK-2p34 is myristoylated.
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 Growth regulation Host-virus interaction
Cellular component	Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome negative regulation of apoptotic process Inferred from mutant phenotype PubMed 21499899. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Inferred from direct assay PubMed 21499899. Source: UniProtKB negative regulation of protein kinase activity Traceable author statement PubMed 10748018. Source: ProtInc peptidyl-serine phosphorylation Inferred from direct assay PubMed 11121037. Source: BHF-UCL positive regulation of extrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 19240112. Source: UniProtKB protein autophosphorylation Inferred from direct assay PubMed 11805089. Source: MGI regulation of defense response to virus by virus Traceable author statement. Source: Reactome regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 11121037. Source: BHF-UCL protein tyrosine kinase activator activity Inferred from direct assay PubMed 11121037. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-1045887,EBI-1045887
CASP7	P55210	6	EBI-1045887,EBI-523958
HTT	P42858	2	EBI-1045887,EBI-466029
LIMK1	P53667	2	EBI-1045887,EBI-444403
RAF1	P04049	2	EBI-1045887,EBI-365996

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.22

Chain

2 – 524

523

Serine/threonine-protein kinase PAK 2

PRO_0000086465

Chain

2 – 212

211

PAK-2p27

PRO_0000304922

Chain

213 – 524

312

PAK-2p34

PRO_0000304923

Regions

Domain

74 – 87

14

CRIB

Domain

249 – 499

251

Protein kinase

Nucleotide binding

255 – 263

9

ATP By similarity

Region

69 – 137

69

Autoregulatory region By similarity

Region

69 – 112

44

GTPase-binding By similarity

Motif

245 – 251

7

Nuclear localization signal

Sites

Active site

367

1

Proton acceptor By similarity

Binding site

278

1

ATP By similarity

Site

212 – 213

2

Cleavage; by caspase-3 or caspase-3-like proteases

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.22 Ref.28

Modified residue

2

1

Phosphoserine Ref.12 Ref.22 Ref.28

Modified residue

58

1

Phosphoserine Ref.17

Modified residue

128

1

N6-acetyllysine Ref.20

Modified residue

139

1

Phosphotyrosine By similarity

Modified residue

141

1

Phosphoserine Ref.17 Ref.19 Ref.22 Ref.28

Modified residue

143

1

Phosphothreonine By similarity

Modified residue

169

1

Phosphothreonine Ref.17 Ref.28

Modified residue

197

1

Phosphoserine Ref.19

Modified residue

402

1

Phosphothreonine; by autocatalysis Probable

Lipidation

213

1

N-myristoyl glycine; in form PAK-2p34 Ref.14

Experimental info

Mutagenesis

212

1

D → N: Inhibits caspase-mediated cleavage. Ref.6

Mutagenesis

213

1

G → A: Abolishes myristoylation of PAK-2p34 and membrane location.

Mutagenesis

239 – 243

5

IVSIG → REGRS: Abolishes nuclear export. Ref.9

Mutagenesis

246 – 248

3

KKK → MHE: Greatly inhibits nuclear localization. Ref.9

Mutagenesis

278

1

K → R: Abolishes kinase activity and autophosphorylation. Ref.7

Mutagenesis

402

1

T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. Ref.7

Sequence conflict

90

1

A → T in AAA75468. Ref.3

Sequence conflict

150

1

F → L in AAA65442. Ref.1

Sequence conflict

225

1

T → P in AAA65442. Ref.1

Sequence conflict

258

1

G → R in AAH69613. Ref.2

Sequence conflict

329

1

G → R in AAA75468. Ref.3

Sequence conflict

338

1

T → TA in AAA65442. Ref.1

Secondary structure

1

.

.

.

524

Helix Strand Turn

Details...

Helix

123 – 126

4

Sequences

	Sequence		Length	Mass (Da)
	Q13177 [UniParc]. Last modified April 3, 2007. Version 3. Checksum: 00A7CD15F93D4180	FASTA	524	58,043
	10 20 30 40 50 60 MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR HKIISIFSGT 70 80 90 100 110 120 EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP 130 140 150 160 170 180 QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNAK GTEAPAVVTE EEDDDEETAP 190 200 210 220 230 240 PVIAPRPDHT KSIYTRSVID PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV 250 260 270 280 290 300 SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE 310 320 330 340 350 360 LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH 370 380 390 400 410 420 ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY 430 440 450 460 470 480 GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC 490 500 510 520 LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLIMAAKEAM KSNR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Sells M., Knause U.J., Bagrodia S., Ambrose D., Bokoch G.M., Chernoff J. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20." Martin G.A., Bollag G., McCormick F., Abo A. EMBO J. 14:1970-1978(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-524, PROTEIN SEQUENCE OF 401-417. Tissue: Placenta.
[4]	Erratum Martin G.A., Bollag G., McCormick F., Abo A. EMBO J. 14:4385-4385(1995) [PubMed] [Europe PMC] [Abstract]
[5]	"Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation." Benner G.E., Dennis P.B., Masaracchia R.A. J. Biol. Chem. 270:21121-21128(1995) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION.
[6]	"Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2." Rudel T., Bokoch G.M. Science 276:1571-1574(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CASPASE-3 CLEAVAGE AT ASP-512, FUNCTION, MUTAGENESIS OF ASP-212.
[7]	"Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity." Walter B.N., Huang Z., Jakobi R., Tuazon P.T., Alnemri E.S., Litwack G., Traugh J.A. J. Biol. Chem. 273:28733-28739(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CASPASE-3 CLEAVAGE AT ASP-512, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-278 AND THR-402.
[8]	"Lentivirus Nef specifically activates Pak2." Arora V.K., Molina R.P., Foster J.L., Blakemore J.L., Chernoff J., Fredericksen B.L., Garcia J.V. J. Virol. 74:11081-11087(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF.
[9]	"Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation." Jakobi R., McCarthy C.C., Koeppel M.A., Stringer D.K. J. Biol. Chem. 278:38675-38685(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (PAK-2P34), UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 239-ILE--GLY-243 AND 246-LYS--LYS-248.
[10]	"Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk." Orton K.C., Ling J., Waskiewicz A.J., Cooper J.A., Merrick W.C., Korneeva N.L., Rhoads R.E., Sonenberg N., Traugh J.A. J. Biol. Chem. 279:38649-38657(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MKNK1.
[11]	"Identification and characterization of PS-GAP as a novel regulator of caspase-activated PAK-2." Koeppel M.A., McCarthy C.C., Moertl E., Jakobi R. J. Biol. Chem. 279:53653-53664(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGAP10, SUBCELLULAR LOCATION.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome." Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K. EMBO Rep. 7:186-191(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SH3MD4.
[14]	"Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events." Vilas G.L., Corvi M.M., Plummer G.J., Seime A.M., Lambkin G.R., Berthiaume L.G. Proc. Natl. Acad. Sci. U.S.A. 103:6542-6547(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (PAK-2P34), MYRISTOYLATION AT GLY-213 (PAK-2P34), SUBCELLULAR LOCATION.
[15]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCRIB.
[16]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-141 AND THR-169, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Dual role of Cdc42 in spindle orientation control of adherent cells." Mitsushima M., Toyoshima F., Nishida E. Mol. Cell. Biol. 29:2816-2827(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF7 AND GIT1.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-197, MASS SPECTROMETRY. Tissue: Leukemic 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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, MASS SPECTROMETRY.
[21]	"Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration." Hsu R.M., Tsai M.H., Hsieh Y.J., Lyu P.C., Yu J.S. Mol. Biol. Cell 21:287-301(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[22]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-141, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"Mechanistic studies of the autoactivation of PAK2: a two-step model of cis initiation followed by trans amplification." Wang J., Wu J.W., Wang Z.X. J. Biol. Chem. 286:2689-2695(2011) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION.
[25]	"Identification of the atypical MAPK Erk3 as a novel substrate for p21-activated kinase (Pak) activity." De la Mota-Peynado A., Chernoff J., Beeser A. J. Biol. Chem. 286:13603-13611(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6.
[26]	"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 threonine sites promotes cell transformation." Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C., Ma W., Shi G., Dong Z., Bode A.M., Dong Z. Carcinogenesis 32:659-666(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF JUN.
[27]	"Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly." Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z. Genes Dev. 25:1359-1364(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H4.
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-141 AND THR-169, MASS SPECTROMETRY.
[29]	"The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold." Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C., Bresson S.M., Tomchick D.R., Alto N.M. Nature 469:107-111(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 121-136.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U24153 mRNA. Translation: AAA65442.1.
BC069613 mRNA. Translation: AAH69613.1.
U25975 mRNA. Translation: AAA75468.1.

IPI

IPI00419979.

PIR

S58682.

RefSeq

NP_002568.2. NM_002577.4.

UniGene

Hs.518530.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PCS	X-ray	2.86	E/F/G/H	121-136	[»]

ProteinModelPortal

Q13177.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38249N.

IntAct

Q13177. 11 interactions.

MINT

MINT-235655.

STRING

9606.ENSP00000314067.

PTM databases

PhosphoSite

Q13177.

Polymorphism databases

DMDM

143811432.

2D gel databases

OGP

Q13177.

Proteomic databases

PaxDb

Q13177.

PRIDE

Q13177.

Protocols and materials databases

DNASU

5062.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327134; ENSP00000314067; ENSG00000180370.

GeneID

5062.

KEGG

hsa:5062.

UCSC

uc003fwy.4. human.

Organism-specific databases

CTD

5062.

GeneCards

GC03P196466.

H-InvDB

HIX0030815.

HGNC

HGNC:8591. PAK2.

HPA

CAB007794.

MIM

605022. gene.

neXtProt

NX_Q13177.

PharmGKB

PA32918.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000234202.

HOVERGEN

HBG108518.

InParanoid

Q13177.

KO

K04410.

OMA

APALNTK.

OrthoDB

EOG4M3988.

PhylomeDB

Q13177.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

faspathway. FAS signaling pathway (CD95).
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.

Reactome

REACT_111045. Developmental Biology.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.

SignaLink

Q13177.

Gene expression databases

ArrayExpress

Q13177.

Bgee

Q13177.

CleanEx

HS_PAK2.

Genevestigator

Q13177.

GermOnline

ENSG00000180370. Homo sapiens.

Family and domain databases

Gene3D

3.90.810.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

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

SMART

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

SUPFAM

SSF56112. Kinase_like. 1 hit.

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

BindingDB

Q13177.

ChEMBL

CHEMBL4487.

ChiTaRS

PAK2. human.

EvolutionaryTrace

Q13177.

GenomeRNAi

5062.

NextBio

19496.

PMAP-CutDB

Q13177.

SOURCE

Search...

Entry information

Entry name

PAK2_HUMAN

Accession

Primary (citable) accession number: Q13177
Secondary accession number(s): Q13154, Q6ISC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 3, 2007
Last modified:	May 29, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.