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Q13177

- PAK2_HUMAN

UniProt

Q13177 - PAK2_HUMAN

Protein

Serine/threonine-protein kinase PAK 2

Gene

PAK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    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.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei212 – 2132Cleavage; by caspase-3 or caspase-3-like proteases
    Binding sitei278 – 2781ATPPROSITE-ProRule annotation
    Active sitei367 – 3671Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi255 – 2639ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: ProtInc
    5. protein kinase binding Source: BHF-UCL
    6. protein serine/threonine kinase activity Source: BHF-UCL
    7. protein tyrosine kinase activator activity Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. axon guidance Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. innate immune response Source: Reactome
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
    8. negative regulation of protein kinase activity Source: ProtInc
    9. peptidyl-serine phosphorylation Source: BHF-UCL
    10. phosphorylation Source: UniProtKB
    11. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    12. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    13. positive regulation of protein tyrosine kinase activity Source: GOC
    14. protein autophosphorylation Source: MGI
    15. protein phosphorylation Source: MGI
    16. regulation of apoptotic process Source: Reactome
    17. regulation of defense response to virus by virus Source: Reactome
    18. regulation of growth Source: UniProtKB-KW
    19. signal transduction Source: ProtInc
    20. T cell costimulation Source: Reactome
    21. T cell receptor signaling pathway Source: Reactome
    22. viral process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Growth regulation, Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_12623. Generation of second messenger molecules.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13528. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
    REACT_13532. Stimulation of the cell death response by PAK-2p34.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_19226. Activation of Rac.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19238. CD28 dependent Vav1 pathway.
    SignaLinkiQ13177.

    Names & Taxonomyi

    Protein namesi
    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:
    PAK-2p27
    Short name:
    p27
    PAK-2p34
    Short name:
    p34
    Alternative name(s):
    C-t-PAK2
    Gene namesi
    Name:PAK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8591. PAK2.

    Subcellular locationi

    Chain 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.
    Chain 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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleus Source: HPA
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi212 – 2121D → N: Inhibits caspase-mediated cleavage. 2 Publications
    Mutagenesisi213 – 2131G → A: Abolishes myristoylation of PAK-2p34 and membrane location. 1 Publication
    Mutagenesisi239 – 2435IVSIG → REGRS: Abolishes nuclear export. 1 Publication
    Mutagenesisi246 – 2483KKK → MHE: Greatly inhibits nuclear localization. 1 Publication
    Mutagenesisi278 – 2781K → R: Abolishes kinase activity and autophosphorylation. 2 Publications
    Mutagenesisi402 – 4021T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. 2 Publications

    Organism-specific databases

    PharmGKBiPA32918.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 524523Serine/threonine-protein kinase PAK 2PRO_0000086465Add
    BLAST
    Chaini2 – 212211PAK-2p27PRO_0000304922Add
    BLAST
    Chaini213 – 524312PAK-2p34PRO_0000304923Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei2 – 21Phosphoserine3 Publications
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei62 – 621N6-acetyllysineBy similarity
    Modified residuei128 – 1281N6-acetyllysine1 Publication
    Modified residuei141 – 1411Phosphoserine4 Publications
    Modified residuei169 – 1691Phosphothreonine2 Publications
    Modified residuei197 – 1971Phosphoserine1 Publication
    Lipidationi213 – 2131N-myristoyl glycine; in form PAK-2p341 Publication
    Modified residuei402 – 4021Phosphothreonine; by autocatalysisCurated

    Post-translational modificationi

    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.5 Publications
    During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34.
    Ubiquitinated, leading to its proteasomal degradation.1 Publication
    PAK-2p34 is myristoylated.1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13177.
    PaxDbiQ13177.
    PRIDEiQ13177.

    2D gel databases

    OGPiQ13177.

    PTM databases

    PhosphoSiteiQ13177.

    Miscellaneous databases

    PMAP-CutDBQ13177.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.

    Gene expression databases

    ArrayExpressiQ13177.
    BgeeiQ13177.
    CleanExiHS_PAK2.
    GenevestigatoriQ13177.

    Organism-specific databases

    HPAiCAB007794.
    HPA036205.

    Interactioni

    Subunit structurei

    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 ARHGAP10.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1045887,EBI-1045887
    ARHGEF6Q150522EBI-1045887,EBI-1642523
    ARHGEF7Q141554EBI-1045887,EBI-717515
    Arhgef7O550438EBI-1045887,EBI-3649585From a different organism.
    CASP7P552106EBI-1045887,EBI-523958
    GRB2P629932EBI-1045887,EBI-401755
    HCKP086312EBI-1045887,EBI-346340
    HTTP428582EBI-1045887,EBI-466029
    LIMK1P536672EBI-1045887,EBI-444403
    NCK1P163332EBI-1045887,EBI-389883
    RAC1P630004EBI-1045887,EBI-413628
    RAF1P040492EBI-1045887,EBI-365996
    SH3RF3Q8TEJ32EBI-1045887,EBI-7975674
    SORBS1Q9BX662EBI-1045887,EBI-433642
    SORBS2O948752EBI-1045887,EBI-311323
    SORBS3O605043EBI-1045887,EBI-741237
    SRCP129312EBI-1045887,EBI-621482

    Protein-protein interaction databases

    BioGridi111098. 53 interactions.
    DIPiDIP-38249N.
    IntActiQ13177. 34 interactions.
    MINTiMINT-235655.
    STRINGi9606.ENSP00000314067.

    Structurei

    Secondary structure

    1
    524
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi123 – 1264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PCSX-ray2.86E/F/G/H121-136[»]
    ProteinModelPortaliQ13177.
    SMRiQ13177. Positions 69-143, 228-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13177.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 8714CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini249 – 499251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni69 – 13769Autoregulatory regionBy similarityAdd
    BLAST
    Regioni69 – 11244GTPase-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi245 – 2517Nuclear localization signal

    Sequence similaritiesi

    Contains 1 CRIB domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234202.
    HOVERGENiHBG108518.
    InParanoidiQ13177.
    KOiK04410.
    OMAiFSGAEKG.
    PhylomeDBiQ13177.
    TreeFamiTF105351.

    Family and domain databases

    Gene3Di3.90.810.10. 1 hit.
    InterProiIPR000095. 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]
    PfamiPF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50108. CRIB. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13177-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR    50
    HKIISIFSGT EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE 100
    QWARLLQTSN ITKLEQKKNP QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF 150
    PSGTPALNAK GTEAPAVVTE EEDDDEETAP PVIAPRPDHT KSIYTRSVID 200
    PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV SIGDPKKKYT 250
    RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE 300
    LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR 350
    ECLQALEFLH ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR 400
    STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE PPYLNENPLR 450
    ALYLIATNGT PELQNPEKLS PIFRDFLNRC LEMDVEKRGS AKELLQHPFL 500
    KLAKPLSSLT PLIMAAKEAM KSNR 524
    Length:524
    Mass (Da):58,043
    Last modified:April 3, 2007 - v3
    Checksum:i00A7CD15F93D4180
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901A → T in AAA75468. (PubMed:7744004)Curated
    Sequence conflicti150 – 1501F → L in AAA65442. 1 PublicationCurated
    Sequence conflicti225 – 2251T → P in AAA65442. 1 PublicationCurated
    Sequence conflicti258 – 2581G → R in AAH69613. (PubMed:15489334)Curated
    Sequence conflicti329 – 3291G → R in AAA75468. (PubMed:7744004)Curated
    Sequence conflicti338 – 3381T → TA in AAA65442. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24153 mRNA. Translation: AAA65442.1.
    BC069613 mRNA. Translation: AAH69613.1.
    U25975 mRNA. Translation: AAA75468.1.
    CCDSiCCDS3321.1.
    PIRiS58682.
    RefSeqiNP_002568.2. NM_002577.4.
    UniGeneiHs.518530.

    Genome annotation databases

    EnsembliENST00000327134; ENSP00000314067; ENSG00000180370.
    GeneIDi5062.
    KEGGihsa:5062.
    UCSCiuc003fwy.4. human.

    Polymorphism databases

    DMDMi143811432.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24153 mRNA. Translation: AAA65442.1 .
    BC069613 mRNA. Translation: AAH69613.1 .
    U25975 mRNA. Translation: AAA75468.1 .
    CCDSi CCDS3321.1.
    PIRi S58682.
    RefSeqi NP_002568.2. NM_002577.4.
    UniGenei Hs.518530.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PCS X-ray 2.86 E/F/G/H 121-136 [» ]
    ProteinModelPortali Q13177.
    SMRi Q13177. Positions 69-143, 228-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111098. 53 interactions.
    DIPi DIP-38249N.
    IntActi Q13177. 34 interactions.
    MINTi MINT-235655.
    STRINGi 9606.ENSP00000314067.

    Chemistry

    BindingDBi Q13177.
    ChEMBLi CHEMBL4487.
    GuidetoPHARMACOLOGYi 2134.

    PTM databases

    PhosphoSitei Q13177.

    Polymorphism databases

    DMDMi 143811432.

    2D gel databases

    OGPi Q13177.

    Proteomic databases

    MaxQBi Q13177.
    PaxDbi Q13177.
    PRIDEi Q13177.

    Protocols and materials databases

    DNASUi 5062.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327134 ; ENSP00000314067 ; ENSG00000180370 .
    GeneIDi 5062.
    KEGGi hsa:5062.
    UCSCi uc003fwy.4. human.

    Organism-specific databases

    CTDi 5062.
    GeneCardsi GC03P196466.
    H-InvDB HIX0030815.
    HGNCi HGNC:8591. PAK2.
    HPAi CAB007794.
    HPA036205.
    MIMi 605022. gene.
    neXtProti NX_Q13177.
    PharmGKBi PA32918.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234202.
    HOVERGENi HBG108518.
    InParanoidi Q13177.
    KOi K04410.
    OMAi FSGAEKG.
    PhylomeDBi Q13177.
    TreeFami TF105351.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_11068. Nef and signal transduction.
    REACT_12623. Generation of second messenger molecules.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13528. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
    REACT_13532. Stimulation of the cell death response by PAK-2p34.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_19226. Activation of Rac.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19238. CD28 dependent Vav1 pathway.
    SignaLinki Q13177.

    Miscellaneous databases

    ChiTaRSi PAK2. human.
    EvolutionaryTracei Q13177.
    GeneWikii PAK2.
    GenomeRNAii 5062.
    NextBioi 19496.
    PMAP-CutDB Q13177.
    PROi Q13177.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13177.
    Bgeei Q13177.
    CleanExi HS_PAK2.
    Genevestigatori Q13177.

    Family and domain databases

    Gene3Di 3.90.810.10. 1 hit.
    InterProi IPR000095. 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 ]
    Pfami PF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50108. CRIB. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: INTERACTION WITH SCRIB.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    17. 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. 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. 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.

    Entry informationi

    Entry nameiPAK2_HUMAN
    AccessioniPrimary (citable) accession number: Q13177
    Secondary accession number(s): Q13154, Q6ISC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3