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O96013

- PAK4_HUMAN

UniProt

O96013 - PAK4_HUMAN

Protein

Serine/threonine-protein kinase PAK 4

Gene

PAK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.7 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei350 – 3501ATPPROSITE-ProRule annotation
    Active sitei440 – 4401Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi327 – 3359ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein kinase activity Source: ProtInc
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cell growth Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. cell proliferation Source: UniProtKB
    6. cellular component movement Source: ProtInc
    7. cytoskeleton organization Source: UniProtKB
    8. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_19226. Activation of Rac.
    SignaLinkiO96013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PAK 4 (EC:2.7.11.1)
    Alternative name(s):
    p21-activated kinase 4
    Short name:
    PAK-4
    Gene namesi
    Name:PAK4
    Synonyms:KIAA1142
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:16059. PAK4.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways.

    GO - Cellular componenti

    1. Golgi apparatus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi445 – 4451S → N: Approximately 30-fold increased autophosphorylation (constitutively active mutant). 1 Publication
    Mutagenesisi474 – 4741S → E: Approximately 3-fold increased autophosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA32920.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591Serine/threonine-protein kinase PAK 4PRO_0000086474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411Phosphoserine2 Publications
    Modified residuei104 – 1041Phosphoserine2 Publications
    Modified residuei148 – 1481Phosphoserine2 Publications
    Modified residuei167 – 1671Phosphoserine2 Publications
    Modified residuei181 – 1811Phosphoserine5 Publications
    Modified residuei187 – 1871Phosphothreonine1 Publication
    Modified residuei195 – 1951Phosphoserine1 Publication
    Modified residuei258 – 2581Phosphoserine2 Publications
    Modified residuei267 – 2671Phosphoserine1 Publication
    Modified residuei291 – 2911Phosphoserine2 Publications
    Modified residuei474 – 4741Phosphoserine; by autocatalysis8 Publications

    Post-translational modificationi

    Autophosphorylated on serine residues when activated by CDC42/p21.8 Publications
    Phosphorylated on tyrosine residues upon stimulation of FGFR2.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO96013.
    PaxDbiO96013.
    PRIDEiO96013.

    PTM databases

    PhosphoSiteiO96013.

    Expressioni

    Tissue specificityi

    Highest expression in prostate, testis and colon.

    Gene expression databases

    ArrayExpressiO96013.
    BgeeiO96013.
    CleanExiHS_PAK4.
    GenevestigatoriO96013.

    Organism-specific databases

    HPAiCAB025747.

    Interactioni

    Subunit structurei

    Interacts with FGFR2 and GRB2 By similarity. Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC42P609532EBI-713738,EBI-81752

    Protein-protein interaction databases

    BioGridi115586. 23 interactions.
    DIPiDIP-39742N.
    IntActiO96013. 14 interactions.
    MINTiMINT-1387795.
    STRINGi9606.ENSP00000351049.

    Structurei

    Secondary structure

    1
    591
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 2612
    Turni27 – 304
    Beta strandi31 – 344
    Helixi37 – 393
    Turni40 – 423
    Turni46 – 483
    Helixi301 – 31111
    Beta strandi312 – 3154
    Helixi317 – 3193
    Beta strandi321 – 3299
    Beta strandi331 – 3333
    Beta strandi334 – 3407
    Turni341 – 3433
    Beta strandi346 – 3538
    Helixi354 – 3563
    Helixi360 – 3623
    Helixi363 – 3697
    Turni370 – 3723
    Beta strandi381 – 3877
    Beta strandi390 – 3956
    Helixi403 – 4097
    Helixi414 – 43320
    Helixi443 – 4453
    Beta strandi446 – 4483
    Beta strandi454 – 4563
    Helixi459 – 4613
    Beta strandi467 – 4693
    Beta strandi475 – 4773
    Helixi479 – 4813
    Helixi484 – 4874
    Helixi495 – 51016
    Turni514 – 5174
    Helixi520 – 52910
    Helixi538 – 5403
    Helixi543 – 55210
    Turni557 – 5593
    Helixi563 – 5664
    Helixi570 – 5745
    Helixi578 – 5814
    Helixi582 – 5843
    Turni586 – 5883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BVAX-ray2.30A/B300-591[»]
    2CDZX-ray2.30A291-591[»]
    2J0IX-ray1.60A291-591[»]
    2OV2X-ray2.10I/J/K/L/M/N/O/P10-44[»]
    2Q0NX-ray1.75A291-591[»]
    2X4ZX-ray2.10A297-591[»]
    4APPX-ray2.20A300-591[»]
    4FIEX-ray3.11A/B5-591[»]
    4FIFX-ray2.60A/B286-591[»]
    C/D49-56[»]
    4FIGX-ray3.01A/B286-591[»]
    4FIHX-ray1.97A286-591[»]
    4FIIX-ray2.00A286-591[»]
    B49-56[»]
    4FIJX-ray2.30A286-591[»]
    4JDHX-ray2.00A286-591[»]
    4JDIX-ray1.85A286-591[»]
    4JDJX-ray2.30A286-591[»]
    4JDKX-ray2.40A286-591[»]
    4L67X-ray2.80A300-591[»]
    B36-60[»]
    4NJDX-ray2.50A300-591[»]
    4O0VX-ray2.80A300-591[»]
    4O0XX-ray2.48A300-591[»]
    4O0YX-ray2.20A300-591[»]
    ProteinModelPortaliO96013.
    SMRiO96013. Positions 10-44, 300-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO96013.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 2414CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini321 – 572252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 320296LinkerAdd
    BLAST
    Regioni298 – 32326GEF-interaction domain (GID)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi105 – 1084Poly-Pro
    Compositional biasi242 – 2476Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108518.
    InParanoidiO96013.
    KOiK05734.
    OMAiIDPACIT.
    OrthoDBiEOG73804D.
    PhylomeDBiO96013.
    TreeFamiTF105352.

    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.
    [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.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O96013-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP    50
    KPLVDPACIT SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL 100
    RRDSPPPPAR ARQENGMPEE PATTARGGPG KAGSRGRFAG HSEAGGGSGD 150
    RRRAGPEKRP KSSREGSGGP QESSRDKRPL SGPDVGTPQP AGLASGAKLA 200
    AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP QSSSSSSRPP 250
    TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS 300
    HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK 350
    KMDLRKQQRR ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG 400
    GALTDIVTHT RMNEEQIAAV CLAVLQALSV LHAQGVIHRD IKSDSILLTH 450
    DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY WMAPELISRL PYGPEVDIWS 500
    LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK VSPSLKGFLD 550
    RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R 591
    Length:591
    Mass (Da):64,072
    Last modified:May 1, 1999 - v1
    Checksum:i04C2A5C0B06427D5
    GO
    Isoform 2 (identifier: O96013-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-120: E → K
         121-285: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:426
    Mass (Da):47,924
    Checksum:i505879690593E93A
    GO
    Isoform 3 (identifier: O96013-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-221: Missing.

    Show »
    Length:438
    Mass (Da):48,268
    Checksum:i4A596EBBCECE9883
    GO
    Isoform 4 (identifier: O96013-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         132-221: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:501
    Mass (Da):54,940
    Checksum:i6EE6240ECE65E79D
    GO

    Sequence cautioni

    The sequence BAA86456.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC11166.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351R → Q.1 Publication
    Corresponds to variant rs56099436 [ dbSNP | Ensembl ].
    VAR_040970
    Natural varianti139 – 1391A → T.1 Publication
    Corresponds to variant rs35655056 [ dbSNP | Ensembl ].
    VAR_040971

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 221153Missing in isoform 3. 3 PublicationsVSP_017572Add
    BLAST
    Alternative sequencei120 – 1201E → K in isoform 2. 1 PublicationVSP_004892
    Alternative sequencei121 – 285165Missing in isoform 2. 1 PublicationVSP_004893Add
    BLAST
    Alternative sequencei132 – 22190Missing in isoform 4. 1 PublicationVSP_017573Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011855 mRNA. Translation: CAA09820.1.
    AF005046 mRNA. Translation: AAD01210.1.
    AB032968 mRNA. Translation: BAA86456.1. Different initiation.
    AK074728 mRNA. Translation: BAC11166.1. Different initiation.
    AK294586 mRNA. Translation: BAG57777.1.
    AL834236 mRNA. Translation: CAD38914.2.
    CH471126 Genomic DNA. Translation: EAW56861.1.
    BC002921 mRNA. Translation: AAH02921.1.
    BC011368 mRNA. Translation: AAH11368.1.
    BC025282 mRNA. Translation: AAH25282.1.
    BC034511 mRNA. Translation: AAH34511.1.
    CCDSiCCDS12528.1. [O96013-1]
    CCDS33019.1. [O96013-3]
    RefSeqiNP_001014831.1. NM_001014831.2. [O96013-1]
    NP_001014832.1. NM_001014832.1. [O96013-1]
    NP_001014834.1. NM_001014834.2. [O96013-3]
    NP_001014835.1. NM_001014835.1. [O96013-3]
    NP_005875.1. NM_005884.3. [O96013-1]
    XP_006723034.1. XM_006722971.1. [O96013-1]
    XP_006723035.1. XM_006722972.1. [O96013-3]
    UniGeneiHs.20447.

    Genome annotation databases

    GeneIDi10298.
    KEGGihsa:10298.
    UCSCiuc002okj.1. human. [O96013-1]
    uc002okm.1. human. [O96013-3]
    uc002okp.1. human. [O96013-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011855 mRNA. Translation: CAA09820.1 .
    AF005046 mRNA. Translation: AAD01210.1 .
    AB032968 mRNA. Translation: BAA86456.1 . Different initiation.
    AK074728 mRNA. Translation: BAC11166.1 . Different initiation.
    AK294586 mRNA. Translation: BAG57777.1 .
    AL834236 mRNA. Translation: CAD38914.2 .
    CH471126 Genomic DNA. Translation: EAW56861.1 .
    BC002921 mRNA. Translation: AAH02921.1 .
    BC011368 mRNA. Translation: AAH11368.1 .
    BC025282 mRNA. Translation: AAH25282.1 .
    BC034511 mRNA. Translation: AAH34511.1 .
    CCDSi CCDS12528.1. [O96013-1 ]
    CCDS33019.1. [O96013-3 ]
    RefSeqi NP_001014831.1. NM_001014831.2. [O96013-1 ]
    NP_001014832.1. NM_001014832.1. [O96013-1 ]
    NP_001014834.1. NM_001014834.2. [O96013-3 ]
    NP_001014835.1. NM_001014835.1. [O96013-3 ]
    NP_005875.1. NM_005884.3. [O96013-1 ]
    XP_006723034.1. XM_006722971.1. [O96013-1 ]
    XP_006723035.1. XM_006722972.1. [O96013-3 ]
    UniGenei Hs.20447.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BVA X-ray 2.30 A/B 300-591 [» ]
    2CDZ X-ray 2.30 A 291-591 [» ]
    2J0I X-ray 1.60 A 291-591 [» ]
    2OV2 X-ray 2.10 I/J/K/L/M/N/O/P 10-44 [» ]
    2Q0N X-ray 1.75 A 291-591 [» ]
    2X4Z X-ray 2.10 A 297-591 [» ]
    4APP X-ray 2.20 A 300-591 [» ]
    4FIE X-ray 3.11 A/B 5-591 [» ]
    4FIF X-ray 2.60 A/B 286-591 [» ]
    C/D 49-56 [» ]
    4FIG X-ray 3.01 A/B 286-591 [» ]
    4FIH X-ray 1.97 A 286-591 [» ]
    4FII X-ray 2.00 A 286-591 [» ]
    B 49-56 [» ]
    4FIJ X-ray 2.30 A 286-591 [» ]
    4JDH X-ray 2.00 A 286-591 [» ]
    4JDI X-ray 1.85 A 286-591 [» ]
    4JDJ X-ray 2.30 A 286-591 [» ]
    4JDK X-ray 2.40 A 286-591 [» ]
    4L67 X-ray 2.80 A 300-591 [» ]
    B 36-60 [» ]
    4NJD X-ray 2.50 A 300-591 [» ]
    4O0V X-ray 2.80 A 300-591 [» ]
    4O0X X-ray 2.48 A 300-591 [» ]
    4O0Y X-ray 2.20 A 300-591 [» ]
    ProteinModelPortali O96013.
    SMRi O96013. Positions 10-44, 300-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115586. 23 interactions.
    DIPi DIP-39742N.
    IntActi O96013. 14 interactions.
    MINTi MINT-1387795.
    STRINGi 9606.ENSP00000351049.

    Chemistry

    BindingDBi O96013.
    ChEMBLi CHEMBL4482.
    GuidetoPHARMACOLOGYi 2136.

    PTM databases

    PhosphoSitei O96013.

    Proteomic databases

    MaxQBi O96013.
    PaxDbi O96013.
    PRIDEi O96013.

    Protocols and materials databases

    DNASUi 10298.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10298.
    KEGGi hsa:10298.
    UCSCi uc002okj.1. human. [O96013-1 ]
    uc002okm.1. human. [O96013-3 ]
    uc002okp.1. human. [O96013-4 ]

    Organism-specific databases

    CTDi 10298.
    GeneCardsi GC19P039616.
    HGNCi HGNC:16059. PAK4.
    HPAi CAB025747.
    MIMi 605451. gene.
    neXtProti NX_O96013.
    PharmGKBi PA32920.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108518.
    InParanoidi O96013.
    KOi K05734.
    OMAi IDPACIT.
    OrthoDBi EOG73804D.
    PhylomeDBi O96013.
    TreeFami TF105352.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_19226. Activation of Rac.
    SignaLinki O96013.

    Miscellaneous databases

    ChiTaRSi PAK4. human.
    EvolutionaryTracei O96013.
    GeneWikii PAK4.
    GenomeRNAii 10298.
    NextBioi 39028.
    PROi O96013.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O96013.
    Bgeei O96013.
    CleanExi HS_PAK4.
    Genevestigatori O96013.

    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.
    [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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia."
      Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A.
      EMBO J. 17:6527-6540(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymphoma.
    2. Melnick M.B.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Neuroblastoma.
    3. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
      Tissue: Brain and Teratocarcinoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1; 2 AND 4).
      Tissue: Eye, Pancreas and Placenta.
    8. "The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis."
      Gnesutta N., Qu J., Minden A.
      J. Biol. Chem. 276:14414-14419(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
    9. "Activated PAK4 regulates cell adhesion and anchorage-independent growth."
      Qu J., Cammarano M.S., Shi Q., Ha K.C., de Lanerolle P., Minden A.
      Mol. Cell. Biol. 21:3523-3533(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-445 AND SER-474.
    10. "P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration."
      Zhang H., Li Z., Viklund E.K., Stromblad S.
      J. Cell Biol. 158:1287-1297(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Death receptor-induced activation of initiator caspase 8 is antagonized by serine/threonine kinase PAK4."
      Gnesutta N., Minden A.
      Mol. Cell. Biol. 23:7838-7848(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
      Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
      EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "PAK4 mediates morphological changes through the regulation of GEF-H1."
      Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.
      J. Cell Sci. 118:1861-1872(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF2.
    14. "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-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; SER-258; SER-267; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; THR-187; SER-195; SER-258; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "p21-activated kinase 4 phosphorylation of integrin beta5 Ser-759 and Ser-762 regulates cell migration."
      Li Z., Zhang H., Lundin L., Thullberg M., Liu Y., Wang Y., Claesson-Welsh L., Stromblad S.
      J. Biol. Chem. 285:23699-23710(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ITGB5.
    20. "Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis."
      Bompard G., Rabeharivelo G., Frank M., Cau J., Delsert C., Morin N.
      J. Cell Biol. 190:807-822(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RAN.
    21. "Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B."
      Wallace S.W., Durgan J., Jin D., Hall A.
      Mol. Biol. Cell 21:2996-3006(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "p21-activated kinases: three more join the Pak."
      Jaffer Z.M., Chernoff J.
      Int. J. Biochem. Cell Biol. 34:713-717(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    23. "The emerging importance of group II PAKs."
      Wells C.M., Jones G.E.
      Biochem. J. 425:465-473(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Crystal structure of the human p21-activated kinase 4."
      Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S.
      Submitted (JUL-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, PHOSPHORYLATION AT SER-474.
    28. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.

    Entry informationi

    Entry nameiPAK4_HUMAN
    AccessioniPrimary (citable) accession number: O96013
    Secondary accession number(s): B4DGG6
    , Q8N4E1, Q8NCH5, Q8NDE3, Q9BU33, Q9ULS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 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, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3