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Q13177 (PAK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Cytoplasmperinuclear 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 processApoptosis
Growth regulation
Host-virus interaction
   Cellular componentCytoplasm
Membrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Lipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

actin cytoskeleton organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

axon guidance

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 21555521. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis

Inferred from direct assay PubMed 21555521. 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 process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activator activity

Inferred from direct assay PubMed 11121037. Source: BHF-UCL

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 524523Serine/threonine-protein kinase PAK 2
PRO_0000086465
Chain2 – 212211PAK-2p27
PRO_0000304922
Chain213 – 524312PAK-2p34
PRO_0000304923

Regions

Domain74 – 8714CRIB
Domain249 – 499251Protein kinase
Nucleotide binding255 – 2639ATP By similarity
Region69 – 13769Autoregulatory region By similarity
Region69 – 11244GTPase-binding By similarity
Motif245 – 2517Nuclear localization signal

Sites

Active site3671Proton acceptor By similarity
Binding site2781ATP By similarity
Site212 – 2132Cleavage; by caspase-3 or caspase-3-like proteases

Amino acid modifications

Modified residue21N-acetylserine Ref.22 Ref.28 Ref.30
Modified residue21Phosphoserine Ref.12 Ref.22 Ref.28
Modified residue581Phosphoserine Ref.17
Modified residue621N6-acetyllysine By similarity
Modified residue1281N6-acetyllysine Ref.20
Modified residue1411Phosphoserine Ref.17 Ref.19 Ref.22 Ref.28
Modified residue1691Phosphothreonine Ref.17 Ref.28
Modified residue1971Phosphoserine Ref.19
Modified residue4021Phosphothreonine; by autocatalysis Probable
Lipidation2131N-myristoyl glycine; in form PAK-2p34 Ref.14

Experimental info

Mutagenesis2121D → N: Inhibits caspase-mediated cleavage. Ref.6
Mutagenesis2131G → A: Abolishes myristoylation of PAK-2p34 and membrane location.
Mutagenesis239 – 2435IVSIG → REGRS: Abolishes nuclear export. Ref.9
Mutagenesis246 – 2483KKK → MHE: Greatly inhibits nuclear localization. Ref.9
Mutagenesis2781K → R: Abolishes kinase activity and autophosphorylation. Ref.7
Mutagenesis4021T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. Ref.7
Sequence conflict901A → T in AAA75468. Ref.3
Sequence conflict1501F → L in AAA65442. Ref.1
Sequence conflict2251T → P in AAA65442. Ref.1
Sequence conflict2581G → R in AAH69613. Ref.2
Sequence conflict3291G → R in AAA75468. Ref.3
Sequence conflict3381T → TA in AAA65442. Ref.1

Secondary structure

... 524
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13177 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 00A7CD15F93D4180

FASTA52458,043
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24153 mRNA. Translation: AAA65442.1.
BC069613 mRNA. Translation: AAH69613.1.
U25975 mRNA. Translation: AAA75468.1.
PIRS58682.
RefSeqNP_002568.2. NM_002577.4.
UniGeneHs.518530.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCSX-ray2.86E/F/G/H121-136[»]
ProteinModelPortalQ13177.
SMRQ13177. Positions 69-143, 228-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111098. 55 interactions.
DIPDIP-38249N.
IntActQ13177. 31 interactions.
MINTMINT-235655.
STRING9606.ENSP00000314067.

Chemistry

BindingDBQ13177.
ChEMBLCHEMBL4487.
GuidetoPHARMACOLOGY2134.

PTM databases

PhosphoSiteQ13177.

Polymorphism databases

DMDM143811432.

2D gel databases

OGPQ13177.

Proteomic databases

PaxDbQ13177.
PRIDEQ13177.

Protocols and materials databases

DNASU5062.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327134; ENSP00000314067; ENSG00000180370.
GeneID5062.
KEGGhsa:5062.
UCSCuc003fwy.4. human.

Organism-specific databases

CTD5062.
GeneCardsGC03P196466.
H-InvDBHIX0030815.
HGNCHGNC:8591. PAK2.
HPACAB007794.
HPA036205.
MIM605022. gene.
neXtProtNX_Q13177.
PharmGKBPA32918.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234202.
HOVERGENHBG108518.
InParanoidQ13177.
KOK04410.
OMAFSGAEKG.
PhylomeDBQ13177.
TreeFamTF105351.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ13177.

Gene expression databases

ArrayExpressQ13177.
BgeeQ13177.
CleanExHS_PAK2.
GenevestigatorQ13177.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAK2. human.
EvolutionaryTraceQ13177.
GeneWikiPAK2.
GenomeRNAi5062.
NextBio19496.
PMAP-CutDBQ13177.
PROQ13177.
SOURCESearch...

Entry information

Entry namePAK2_HUMAN
AccessionPrimary (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: March 19, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM