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Q9UL54

- TAOK2_HUMAN

UniProt

Q9UL54 - TAOK2_HUMAN

Protein

Serine/threonine-protein kinase TAO2

Gene

TAOK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Selectively inhibited by the enantiopure organoruthenium inhibitor 9E1. Activated following arsenic trioxide (As2O3) treatment.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571ATPPROSITE-ProRule annotation
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 429ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. mitogen-activated protein kinase kinase binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. activation of MAPKK activity Source: UniProtKB
    3. apoptotic process Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. cellular response to DNA damage stimulus Source: UniProtKB
    6. focal adhesion assembly Source: UniProtKB
    7. G2 DNA damage checkpoint Source: UniProtKB
    8. positive regulation of JNK cascade Source: UniProtKB
    9. positive regulation of stress-activated MAPK cascade Source: UniProtKB
    10. protein targeting to membrane Source: UniProtKB
    11. regulation of cell growth Source: UniProtKB
    12. regulation of cell shape Source: UniProtKB
    13. response to stress Source: UniProtKB
    14. stress-activated MAPK cascade Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9UL54.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase TAO2 (EC:2.7.11.1)
    Alternative name(s):
    Kinase from chicken homolog C
    Short name:
    hKFC-C
    Prostate-derived sterile 20-like kinase 1
    Short name:
    PSK-1
    Short name:
    PSK1
    Short name:
    Prostate-derived STE20-like kinase 1
    Thousand and one amino acid protein kinase 2
    Gene namesi
    Name:TAOK2
    Synonyms:KIAA0881, MAP3K17, PSK, PSK1
    ORF Names:UNQ2971/PRO7431
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16835. TAOK2.

    Subcellular locationi

    Cytoplasmic vesicle membrane Curated; Multi-pass membrane protein Curated. Cytoplasmcytoskeleton. Nucleus
    Note: Catalytically active full-length phosphorylated isoform 1 localizes to microtubules in the cytoplasm predominantly on microtubule cables positioned around the nucleus. A C-terminally truncated form of isoform 1 is present in the nucleus; isoform 2 and kinase-defective, as well as full-length isoform 1 are excluded from the nucleus.
    Isoform 2 : Cell projectiondendrite
    Note: In dendrites, colocalizes with PCDH8.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. dendrite Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW
    7. nucleolus Source: HPA
    8. nucleus Source: HPA
    9. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571K → A: Loss of kinase activity. In isoform 1, excluded from the nucleus. No effect on microtubule-binding. 4 Publications
    Mutagenesisi169 – 1691D → A: Loss of kinase activity; No effect on MAP3K7-mediated activation of NF-kappa-B. 1 Publication
    Mutagenesisi919 – 9191D → N: No effect on kinase activity, nor on JNK activation, but severe reduction in nuclear localization and apoptotic membrane blebbing. 1 Publication

    Organism-specific databases

    PharmGKBiPA134907964.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12351235Serine/threonine-protein kinase TAO2PRO_0000086733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine3 Publications
    Modified residuei181 – 1811Phosphoserine3 Publications
    Modified residuei486 – 4861Phosphoserine2 Publications
    Modified residuei777 – 7771Phosphoserine2 Publications
    Modified residuei825 – 8251Phosphoserine2 Publications
    Modified residuei827 – 8271Phosphoserine2 Publications

    Post-translational modificationi

    Isoforms 1 and 2 are autophosphorylated.
    C-terminal cleavage of isoform 1 and subsequent nuclear localization requires CASP9 activity.
    Autophosphorylated. Phosphorylated by ATM.
    Isoform 2: Phosphorylated on Ser-1031 by MAPK14. This phosphorylation is required PCDH8 for endocytosis By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UL54.
    PaxDbiQ9UL54.
    PRIDEiQ9UL54.

    PTM databases

    PhosphoSiteiQ9UL54.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with a higher level of expression in testis and brain.2 Publications

    Gene expression databases

    ArrayExpressiQ9UL54.
    BgeeiQ9UL54.
    CleanExiHS_TAOK2.
    GenevestigatoriQ9UL54.

    Organism-specific databases

    HPAiHPA010650.

    Interactioni

    Subunit structurei

    Interacts with MAP2K3 and MAP2K6 By similarity. Self-associates. Interacts with tubulins through the C-terminal domain. Interacts with MAP3K7 and interfers with MAP3K7-binding to CHUK and thus prevents NF-kappa-B activation. Isoform 2 interacts with PCDH8; this complex may also include CDH2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114750. 7 interactions.
    IntActiQ9UL54. 7 interactions.
    STRINGi9606.ENSP00000310094.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UL54.
    SMRiQ9UL54. Positions 12-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei965 – 98521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei987 – 100721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1012 – 103221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1043 – 106321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1166 – 118621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 281254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili486 – 54762Sequence AnalysisAdd
    BLAST
    Coiled coili574 – 60128Sequence AnalysisAdd
    BLAST
    Coiled coili681 – 71333Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi330 – 3367Poly-Glu
    Compositional biasi347 – 37024Ser-richAdd
    BLAST
    Compositional biasi378 – 40629Glu-richAdd
    BLAST
    Compositional biasi791 – 907117Glu-richAdd
    BLAST
    Compositional biasi943 – 1060118Leu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG094024.
    InParanoidiQ9UL54.
    KOiK04429.
    OMAiWGKEDES.
    OrthoDBiEOG74XS5S.
    PhylomeDBiQ9UL54.
    TreeFamiTF351444.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UL54-1) [UniParc]FASTAAdd to Basket

    Also known as: PSK1-alpha, TAO2

    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

    MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN     50
    SEVVAIKKMS YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT 100
    AWLVMEYCLG SASDLLEVHK KPLQEVEIAA VTHGALQGLA YLHSHNMIHR 150
    DVKAGNILLS EPGLVKLGDF GSASIMAPAN SFVGTPYWMA PEVILAMDEG 200
    QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPVLQSGHW 250
    SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA 300
    VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES 350
    SHSVPSMSIS ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEGPEAREMA 400
    MMQEGEHTVT SHSSIIHRLP GSDNLYDDPY QPEITPSPLQ PPAAPAPTST 450
    TSSARRRAYC RNRDHFATIR TASLVSRQIQ EHEQDSALRE QLSGYKRMRR 500
    QHQKQLLALE SRLRGEREEH SARLQRELEA QRAGFGAEAE KLARRHQAIG 550
    EKEARAAQAE ERKFQQHILG QQKKELAALL EAQKRTYKLR KEQLKEELQE 600
    NPSTPKREKA EWLLRQKEQL QQCQAEEEAG LLRRQRQYFE LQCRQYKRKM 650
    LLARHSLDQD LLREDLNKKQ TQKDLECALL LRQHEATREL ELRQLQAVQR 700
    TRAELTRLQH QTELGNQLEY NKRREQELRQ KHAAQVRQQP KSLKVRAGQR 750
    PPGLPLPIPG ALGPPNTGTP IEQQPCSPGQ EAVLDQRMLG EEEEAVGERR 800
    ILGKEGATLE PKQQRILGEE SGAPSPSPQK HGSLVDEEVW GLPEEIEELR 850
    VPSLVPQERS IVGQEEAGTW SLWGKEDESL LDEEFELGWV QGPALTPVPE 900
    EEEEEEEGAP IGTPRDPGDG CPSPDIPPEP PPTHLRPCPA SQLPGLLSHG 950
    LLAGLSFAVG SSSGLLPLLL LLLLPLLAAQ GGGGLQAALL ALEVGLVGLG 1000
    ASYLLLCTAL HLPSSLFLLL AQGTALGAVL GLSWRRGLMG VPLGLGAAWL 1050
    LAWPGLALPL VAMAAGGRWV RQQGPRVRRG ISRLWLRVLL RLSPMAFRAL 1100
    QGCGAVGDRG LFALYPKTNK DGFRSRLPVP GPRRRNPRTT QHPLALLARV 1150
    WVLCKGWNWR LARASQGLAS HLPPWAIHTL ASWGLLRGER PTRIPRLLPR 1200
    SQRQLGPPAS RQPLPGTLAG RRSRTRQSRA LPPWR 1235
    Length:1,235
    Mass (Da):138,251
    Last modified:October 17, 2006 - v2
    Checksum:i211852E690934307
    GO
    Isoform 2 (identifier: Q9UL54-2) [UniParc]FASTAAdd to Basket

    Also known as: PSK1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         745-1049: VRAGQRPPGL...GVPLGLGAAW → SKELQIKKQF...ILNGSSHFYS
         1050-1235: Missing.

    Note: Contains a phosphoserine at position 1011. Contains a phosphoserine at position 1031 (By similarity).By similarity

    Show »
    Length:1,049
    Mass (Da):119,281
    Checksum:iD6C5062F47794030
    GO
    Isoform 3 (identifier: Q9UL54-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-173: Missing.
         174-218: SIMAPANSFV...WSLGITCIEL → MMGTSQGHVA...SPSSLSPFSV

    Note: No experimental confirmation available.

    Show »
    Length:1,062
    Mass (Da):118,780
    Checksum:iA4B2B359EEC9CAAD
    GO
    Isoform 4 (identifier: Q9UL54-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         745-857: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,122
    Mass (Da):126,204
    Checksum:i3F00D8F3E84DF679
    GO

    Sequence cautioni

    The sequence AAQ89301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA74904.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1891M → T in AAI51222. 1 PublicationCurated
    Sequence conflicti189 – 1891M → T in AAI42664. 1 PublicationCurated
    Sequence conflicti1211 – 12111R → H in AAD45616. (PubMed:10660600)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 173173Missing in isoform 3. 1 PublicationVSP_015967Add
    BLAST
    Alternative sequencei174 – 21845SIMAP…TCIEL → MMGTSQGHVARKSRNWGLNP SRLSSIPLSSTPCHLSPSSL SPFSV in isoform 3. 1 PublicationVSP_015968Add
    BLAST
    Alternative sequencei745 – 1049305VRAGQ…LGAAW → SKELQIKKQFQETCKIQTRQ YKALRAHLLETTPKAQHKSL LKRLKEEQTRKLAILAEQYD QSISEMLSSQALRLDETQEA EFQALRQQLQQELELLNAYQ SKIKIRTESQHERELRELEQ RVALRRALLEQRVEEELLAL QTGRSERIRSLLERQAREIE AFDAESMRLGFSSMALGGIP AEAAAQGYPAPPPAPAWPSR PVPRSGAHWSHGPPPPGMPP PAWRQPSLLAPPGPPNWLGP PTQSGTPRGGALLLLRNSPQ PLRRAASGGSGSENVGPPAA AVPGPLSRSTSVASHILNGS SHFYS in isoform 2. 4 PublicationsVSP_015969Add
    BLAST
    Alternative sequencei745 – 857113Missing in isoform 4. 1 PublicationVSP_044894Add
    BLAST
    Alternative sequencei1050 – 1235186Missing in isoform 2. 4 PublicationsVSP_015970Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061943 mRNA. Translation: AAD45616.1.
    AF263313 mRNA. Translation: AAG38503.1.
    AB020688 mRNA. Translation: BAA74904.2. Different initiation.
    AK291473 mRNA. Translation: BAF84162.1.
    AL137701 mRNA. Translation: CAB70882.1.
    AC093512 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79963.1.
    CH471238 Genomic DNA. Translation: EAW79964.1.
    BC136653 mRNA. Translation: AAI36654.1.
    BC136655 mRNA. Translation: AAI36656.1.
    BC142663 mRNA. Translation: AAI42664.1.
    BC144344 mRNA. Translation: AAI44345.1.
    BC151221 mRNA. Translation: AAI51222.1.
    BC152413 mRNA. Translation: AAI52414.1.
    AY358942 mRNA. Translation: AAQ89301.1. Different initiation.
    CCDSiCCDS10662.1. [Q9UL54-2]
    CCDS10663.1. [Q9UL54-1]
    CCDS58448.1. [Q9UL54-4]
    PIRiT46444.
    RefSeqiNP_001238972.1. NM_001252043.1. [Q9UL54-4]
    NP_004774.1. NM_004783.3. [Q9UL54-2]
    NP_057235.2. NM_016151.3. [Q9UL54-1]
    UniGeneiHs.291623.

    Genome annotation databases

    EnsembliENST00000279394; ENSP00000279394; ENSG00000149930. [Q9UL54-2]
    ENST00000308893; ENSP00000310094; ENSG00000149930. [Q9UL54-1]
    ENST00000416441; ENSP00000393048; ENSG00000149930. [Q9UL54-3]
    ENST00000543033; ENSP00000440336; ENSG00000149930. [Q9UL54-4]
    GeneIDi9344.
    KEGGihsa:9344.
    UCSCiuc002dva.2. human. [Q9UL54-1]
    uc002dvc.2. human. [Q9UL54-2]
    uc002dvd.2. human. [Q9UL54-3]
    uc021tgf.1. human.

    Polymorphism databases

    DMDMi116242813.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061943 mRNA. Translation: AAD45616.1 .
    AF263313 mRNA. Translation: AAG38503.1 .
    AB020688 mRNA. Translation: BAA74904.2 . Different initiation.
    AK291473 mRNA. Translation: BAF84162.1 .
    AL137701 mRNA. Translation: CAB70882.1 .
    AC093512 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79963.1 .
    CH471238 Genomic DNA. Translation: EAW79964.1 .
    BC136653 mRNA. Translation: AAI36654.1 .
    BC136655 mRNA. Translation: AAI36656.1 .
    BC142663 mRNA. Translation: AAI42664.1 .
    BC144344 mRNA. Translation: AAI44345.1 .
    BC151221 mRNA. Translation: AAI51222.1 .
    BC152413 mRNA. Translation: AAI52414.1 .
    AY358942 mRNA. Translation: AAQ89301.1 . Different initiation.
    CCDSi CCDS10662.1. [Q9UL54-2 ]
    CCDS10663.1. [Q9UL54-1 ]
    CCDS58448.1. [Q9UL54-4 ]
    PIRi T46444.
    RefSeqi NP_001238972.1. NM_001252043.1. [Q9UL54-4 ]
    NP_004774.1. NM_004783.3. [Q9UL54-2 ]
    NP_057235.2. NM_016151.3. [Q9UL54-1 ]
    UniGenei Hs.291623.

    3D structure databases

    ProteinModelPortali Q9UL54.
    SMRi Q9UL54. Positions 12-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114750. 7 interactions.
    IntActi Q9UL54. 7 interactions.
    STRINGi 9606.ENSP00000310094.

    Chemistry

    BindingDBi Q9UL54.
    ChEMBLi CHEMBL1075195.
    GuidetoPHARMACOLOGYi 2234.

    PTM databases

    PhosphoSitei Q9UL54.

    Polymorphism databases

    DMDMi 116242813.

    Proteomic databases

    MaxQBi Q9UL54.
    PaxDbi Q9UL54.
    PRIDEi Q9UL54.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000279394 ; ENSP00000279394 ; ENSG00000149930 . [Q9UL54-2 ]
    ENST00000308893 ; ENSP00000310094 ; ENSG00000149930 . [Q9UL54-1 ]
    ENST00000416441 ; ENSP00000393048 ; ENSG00000149930 . [Q9UL54-3 ]
    ENST00000543033 ; ENSP00000440336 ; ENSG00000149930 . [Q9UL54-4 ]
    GeneIDi 9344.
    KEGGi hsa:9344.
    UCSCi uc002dva.2. human. [Q9UL54-1 ]
    uc002dvc.2. human. [Q9UL54-2 ]
    uc002dvd.2. human. [Q9UL54-3 ]
    uc021tgf.1. human.

    Organism-specific databases

    CTDi 9344.
    GeneCardsi GC16P029985.
    HGNCi HGNC:16835. TAOK2.
    HPAi HPA010650.
    MIMi 613199. gene.
    neXtProti NX_Q9UL54.
    PharmGKBi PA134907964.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG094024.
    InParanoidi Q9UL54.
    KOi K04429.
    OMAi WGKEDES.
    OrthoDBi EOG74XS5S.
    PhylomeDBi Q9UL54.
    TreeFami TF351444.

    Enzyme and pathway databases

    SignaLinki Q9UL54.

    Miscellaneous databases

    GeneWikii TAOK2.
    GenomeRNAii 9344.
    NextBioi 34999.
    PROi Q9UL54.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UL54.
    Bgeei Q9UL54.
    CleanExi HS_TAOK2.
    Genevestigatori Q9UL54.

    Family and domain databases

    InterProi 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 PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PSK, a novel STE20-like kinase derived from prostatic carcinoma that activates the JNK MAPK pathway and regulates actin cytoskeletal organisation."
      Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J., Morris J.D.H.
      J. Biol. Chem. 275:4311-4322(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-57.
      Tissue: Mammary carcinoma.
    2. "Comparative studies of a new subfamily of human Ste20-like kinases: homodimerization, subcellular localization, and selective activation of MKK3 and p38."
      Yustein J.T., Xia L., Kahlenburg J.M., Robinson D., Templeton D., Kung H.-J.
      Oncogene 22:6129-6141(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SELF-ASSOCIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      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 2).
      Tissue: Fetal brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 957-1235 (ISOFORMS 1/3).
    10. "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2."
      Chen Z., Cobb M.H.
      J. Biol. Chem. 276:16070-16075(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2K3 AND MAP2K6, INTERACTION WITH MAP2K3 AND MAP2K6.
    11. "The prostate-derived sterile 20-like kinase (PSK) regulates microtubule organization and stability."
      Mitsopoulos C., Zihni C., Garg R., Ridley A.J., Morris J.D.
      J. Biol. Chem. 278:18085-18091(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULINS, MUTAGENESIS OF LYS-57.
    12. "TAO (thousand-and-one amino acid) protein kinases mediate signaling from carbachol to p38 mitogen-activated protein kinase and ternary complex factors."
      Chen Z., Raman M., Chen L., Lee S.F., Gilman A.G., Cobb M.H.
      J. Biol. Chem. 278:22278-22283(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-mediated NF-kappaB activation: TAO2 regulates TAK1 pathways."
      Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J.
      J. Biol. Chem. 281:28802-28810(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K7, MUTAGENESIS OF LYS-57 AND ASP-169.
    14. "TAO kinases mediate activation of p38 in response to DNA damage."
      Raman M., Earnest S., Zhang K., Zhao Y., Cobb M.H.
      EMBO J. 26:2005-2014(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY ATM, INDUCTION.
    15. "Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing."
      Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.
      J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-181, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-57 AND ASP-919.
    16. "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-9 AND SER-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Toward the development of a potent and selective organoruthenium mammalian sterile 20 kinase inhibitor."
      Anand R., Maksimoska J., Pagano N., Wong E.Y., Gimotty P.A., Diamond S.L., Meggers E., Marmorstein R.
      J. Med. Chem. 52:1602-1611(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-181 AND SER-486, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Arsenic trioxide-dependent activation of thousand-and-one amino acid kinase 2 and transforming growth factor-beta-activated kinase 1."
      McNeer J.L., Goussetis D.J., Sassano A., Dolniak B., Kroczynska B., Glaser H., Altman J.K., Platanias L.C.
      Mol. Pharmacol. 77:828-835(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    20. "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-825 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTAOK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UL54
    Secondary accession number(s): A5PKY1
    , A7MCZ2, B2RN35, B7ZM88, O94957, Q6UW73, Q7LC09, Q9NSW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3